7ELL

In situ structure of capping enzyme lambda2, penetration protein mu1 of mammalian reovirus capsid asymmetric unit.

External Resource: Annotation

Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
R [auth i]	SCOP2 Family	Reovirus mu1 protein-like	8105400	4007739	SCOP2 (2022-06-29)
R [auth i]	SCOP2 Superfamily	Reovirus mu1 protein-like	8105401	3002506	SCOP2 (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF05993	e7ellA1	A: a+b complex topology	X: a+b domain in membrane penetration protein mu1 (From Topology)	H: a+b domain in membrane penetration protein mu1 (From Topology)	T: a+b domain in membrane penetration protein mu1	F: PF05993	ECOD (1.6)
C [auth B]	PF05993	e7ellB1	A: a+b complex topology	X: a+b domain in membrane penetration protein mu1 (From Topology)	H: a+b domain in membrane penetration protein mu1 (From Topology)	T: a+b domain in membrane penetration protein mu1	F: PF05993	ECOD (1.6)
E [auth C]	PF05993	e7ellC1	A: a+b complex topology	X: a+b domain in membrane penetration protein mu1 (From Topology)	H: a+b domain in membrane penetration protein mu1 (From Topology)	T: a+b domain in membrane penetration protein mu1	F: PF05993	ECOD (1.6)
G [auth D]	PF05993	e7ellD1	A: a+b complex topology	X: a+b domain in membrane penetration protein mu1 (From Topology)	H: a+b domain in membrane penetration protein mu1 (From Topology)	T: a+b domain in membrane penetration protein mu1	F: PF05993	ECOD (1.6)
I [auth E]	PF05993	e7ellE1	A: a+b complex topology	X: a+b domain in membrane penetration protein mu1 (From Topology)	H: a+b domain in membrane penetration protein mu1 (From Topology)	T: a+b domain in membrane penetration protein mu1	F: PF05993	ECOD (1.6)
K [auth F]	PF05993	e7ellF1	A: a+b complex topology	X: a+b domain in membrane penetration protein mu1 (From Topology)	H: a+b domain in membrane penetration protein mu1 (From Topology)	T: a+b domain in membrane penetration protein mu1	F: PF05993	ECOD (1.6)
M [auth G]	PF05993	e7ellG1	A: a+b complex topology	X: a+b domain in membrane penetration protein mu1 (From Topology)	H: a+b domain in membrane penetration protein mu1 (From Topology)	T: a+b domain in membrane penetration protein mu1	F: PF05993	ECOD (1.6)
O [auth H]	PF05993	e7ellH1	A: a+b complex topology	X: a+b domain in membrane penetration protein mu1 (From Topology)	H: a+b domain in membrane penetration protein mu1 (From Topology)	T: a+b domain in membrane penetration protein mu1	F: PF05993	ECOD (1.6)
Q [auth I]	PF05993	e7ellI1	A: a+b complex topology	X: a+b domain in membrane penetration protein mu1 (From Topology)	H: a+b domain in membrane penetration protein mu1 (From Topology)	T: a+b domain in membrane penetration protein mu1	F: PF05993	ECOD (1.6)
S [auth J]	PF05993	e7ellJ1	A: a+b complex topology	X: a+b domain in membrane penetration protein mu1 (From Topology)	H: a+b domain in membrane penetration protein mu1 (From Topology)	T: a+b domain in membrane penetration protein mu1	F: PF05993	ECOD (1.6)
B [auth a]	PF05993	e7ella3	A: beta sandwiches	X: jelly-roll	H: Jelly-roll domain in membrane penetration protein mu1 (From Topology)	T: Jelly-roll domain in membrane penetration protein mu1	F: PF05993	ECOD (1.6)
B [auth a]	PF05993	e7ella2	A: alpha arrays	X: Alpha-helical domain in membrane penetration protein mu1 (From Topology)	H: Alpha-helical domain in membrane penetration protein mu1 (From Topology)	T: Alpha-helical domain in membrane penetration protein mu1	F: PF05993	ECOD (1.6)
B [auth a]	PF05993	e7ella1	A: a+b complex topology	X: a+b domain in membrane penetration protein mu1 (From Topology)	H: a+b domain in membrane penetration protein mu1 (From Topology)	T: a+b domain in membrane penetration protein mu1	F: PF05993	ECOD (1.6)
D [auth b]	PF05993	e7ellb3	A: beta sandwiches	X: jelly-roll	H: Jelly-roll domain in membrane penetration protein mu1 (From Topology)	T: Jelly-roll domain in membrane penetration protein mu1	F: PF05993	ECOD (1.6)
D [auth b]	PF05993	e7ellb2	A: alpha arrays	X: Alpha-helical domain in membrane penetration protein mu1 (From Topology)	H: Alpha-helical domain in membrane penetration protein mu1 (From Topology)	T: Alpha-helical domain in membrane penetration protein mu1	F: PF05993	ECOD (1.6)
D [auth b]	PF05993	e7ellb1	A: a+b complex topology	X: a+b domain in membrane penetration protein mu1 (From Topology)	H: a+b domain in membrane penetration protein mu1 (From Topology)	T: a+b domain in membrane penetration protein mu1	F: PF05993	ECOD (1.6)
F [auth c]	PF05993	e7ellc3	A: beta sandwiches	X: jelly-roll	H: Jelly-roll domain in membrane penetration protein mu1 (From Topology)	T: Jelly-roll domain in membrane penetration protein mu1	F: PF05993	ECOD (1.6)
F [auth c]	PF05993	e7ellc2	A: alpha arrays	X: Alpha-helical domain in membrane penetration protein mu1 (From Topology)	H: Alpha-helical domain in membrane penetration protein mu1 (From Topology)	T: Alpha-helical domain in membrane penetration protein mu1	F: PF05993	ECOD (1.6)
F [auth c]	PF05993	e7ellc1	A: a+b complex topology	X: a+b domain in membrane penetration protein mu1 (From Topology)	H: a+b domain in membrane penetration protein mu1 (From Topology)	T: a+b domain in membrane penetration protein mu1	F: PF05993	ECOD (1.6)
H [auth d]	PF05993	e7elld3	A: beta sandwiches	X: jelly-roll	H: Jelly-roll domain in membrane penetration protein mu1 (From Topology)	T: Jelly-roll domain in membrane penetration protein mu1	F: PF05993	ECOD (1.6)
H [auth d]	PF05993	e7elld2	A: alpha arrays	X: Alpha-helical domain in membrane penetration protein mu1 (From Topology)	H: Alpha-helical domain in membrane penetration protein mu1 (From Topology)	T: Alpha-helical domain in membrane penetration protein mu1	F: PF05993	ECOD (1.6)
H [auth d]	PF05993	e7elld1	A: a+b complex topology	X: a+b domain in membrane penetration protein mu1 (From Topology)	H: a+b domain in membrane penetration protein mu1 (From Topology)	T: a+b domain in membrane penetration protein mu1	F: PF05993	ECOD (1.6)
J [auth e]	PF05993	e7elle3	A: beta sandwiches	X: jelly-roll	H: Jelly-roll domain in membrane penetration protein mu1 (From Topology)	T: Jelly-roll domain in membrane penetration protein mu1	F: PF05993	ECOD (1.6)
J [auth e]	PF05993	e7elle2	A: alpha arrays	X: Alpha-helical domain in membrane penetration protein mu1 (From Topology)	H: Alpha-helical domain in membrane penetration protein mu1 (From Topology)	T: Alpha-helical domain in membrane penetration protein mu1	F: PF05993	ECOD (1.6)
J [auth e]	PF05993	e7elle1	A: a+b complex topology	X: a+b domain in membrane penetration protein mu1 (From Topology)	H: a+b domain in membrane penetration protein mu1 (From Topology)	T: a+b domain in membrane penetration protein mu1	F: PF05993	ECOD (1.6)
L [auth f]	PF05993	e7ellf3	A: beta sandwiches	X: jelly-roll	H: Jelly-roll domain in membrane penetration protein mu1 (From Topology)	T: Jelly-roll domain in membrane penetration protein mu1	F: PF05993	ECOD (1.6)
L [auth f]	PF05993	e7ellf2	A: alpha arrays	X: Alpha-helical domain in membrane penetration protein mu1 (From Topology)	H: Alpha-helical domain in membrane penetration protein mu1 (From Topology)	T: Alpha-helical domain in membrane penetration protein mu1	F: PF05993	ECOD (1.6)
L [auth f]	PF05993	e7ellf1	A: a+b complex topology	X: a+b domain in membrane penetration protein mu1 (From Topology)	H: a+b domain in membrane penetration protein mu1 (From Topology)	T: a+b domain in membrane penetration protein mu1	F: PF05993	ECOD (1.6)
N [auth g]	PF05993	e7ellg3	A: beta sandwiches	X: jelly-roll	H: Jelly-roll domain in membrane penetration protein mu1 (From Topology)	T: Jelly-roll domain in membrane penetration protein mu1	F: PF05993	ECOD (1.6)
N [auth g]	PF05993	e7ellg2	A: alpha arrays	X: Alpha-helical domain in membrane penetration protein mu1 (From Topology)	H: Alpha-helical domain in membrane penetration protein mu1 (From Topology)	T: Alpha-helical domain in membrane penetration protein mu1	F: PF05993	ECOD (1.6)
N [auth g]	PF05993	e7ellg1	A: a+b complex topology	X: a+b domain in membrane penetration protein mu1 (From Topology)	H: a+b domain in membrane penetration protein mu1 (From Topology)	T: a+b domain in membrane penetration protein mu1	F: PF05993	ECOD (1.6)
P [auth h]	PF05993	e7ellh3	A: beta sandwiches	X: jelly-roll	H: Jelly-roll domain in membrane penetration protein mu1 (From Topology)	T: Jelly-roll domain in membrane penetration protein mu1	F: PF05993	ECOD (1.6)
P [auth h]	PF05993	e7ellh2	A: alpha arrays	X: Alpha-helical domain in membrane penetration protein mu1 (From Topology)	H: Alpha-helical domain in membrane penetration protein mu1 (From Topology)	T: Alpha-helical domain in membrane penetration protein mu1	F: PF05993	ECOD (1.6)
P [auth h]	PF05993	e7ellh1	A: a+b complex topology	X: a+b domain in membrane penetration protein mu1 (From Topology)	H: a+b domain in membrane penetration protein mu1 (From Topology)	T: a+b domain in membrane penetration protein mu1	F: PF05993	ECOD (1.6)
R [auth i]	PF05993	e7elli3	A: beta sandwiches	X: jelly-roll	H: Jelly-roll domain in membrane penetration protein mu1 (From Topology)	T: Jelly-roll domain in membrane penetration protein mu1	F: PF05993	ECOD (1.6)
R [auth i]	PF05993	e7elli2	A: alpha arrays	X: Alpha-helical domain in membrane penetration protein mu1 (From Topology)	H: Alpha-helical domain in membrane penetration protein mu1 (From Topology)	T: Alpha-helical domain in membrane penetration protein mu1	F: PF05993	ECOD (1.6)
R [auth i]	PF05993	e7elli1	A: a+b complex topology	X: a+b domain in membrane penetration protein mu1 (From Topology)	H: a+b domain in membrane penetration protein mu1 (From Topology)	T: a+b domain in membrane penetration protein mu1	F: PF05993	ECOD (1.6)
T [auth j]	PF05993	e7ellj3	A: beta sandwiches	X: jelly-roll	H: Jelly-roll domain in membrane penetration protein mu1 (From Topology)	T: Jelly-roll domain in membrane penetration protein mu1	F: PF05993	ECOD (1.6)
T [auth j]	PF05993	e7ellj2	A: alpha arrays	X: Alpha-helical domain in membrane penetration protein mu1 (From Topology)	H: Alpha-helical domain in membrane penetration protein mu1 (From Topology)	T: Alpha-helical domain in membrane penetration protein mu1	F: PF05993	ECOD (1.6)
T [auth j]	PF05993	e7ellj1	A: a+b complex topology	X: a+b domain in membrane penetration protein mu1 (From Topology)	H: a+b domain in membrane penetration protein mu1 (From Topology)	T: a+b domain in membrane penetration protein mu1	F: PF05993	ECOD (1.6)
U [auth K]	PF06016	e7ellK8	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: PF06016	ECOD (1.6)
U [auth K]	PF21060	e7ellK7	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: PF21060	ECOD (1.6)
U [auth K]	PF21061	e7ellK5	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: PF21061	ECOD (1.6)
U [auth K]	PF21062	e7ellK6	A: a+b two layers	X: ferredoxin-like domain in VP1 (From Topology)	H: ferredoxin-like domain in VP1 (From Topology)	T: ferredoxin-like domain in VP1	F: PF21062	ECOD (1.6)
U [auth K]	PF21063	e7ellK2	A: a+b three layers	X: HIT-like	H: HIT-related (From Topology)	T: HIT-related	F: PF21063	ECOD (1.6)
U [auth K]	PF21064	e7ellK4	A: a+b complex topology	X: Rotavirus NSP2 fragment, N-terminal domain (From Topology)	H: Rotavirus NSP2 fragment, N-terminal domain (From Topology)	T: Rotavirus NSP2 fragment, N-terminal domain	F: PF21064	ECOD (1.6)
U [auth K]	PF21065	e7ellK1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: S-adenosyl-L-methionine-dependent methyltransferases	F: PF21065	ECOD (1.6)
U [auth K]	PF21066	e7ellK3	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: S-adenosyl-L-methionine-dependent methyltransferases	F: PF21066	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, C [auth B], E [auth C], G [auth D], I [auth E], A, C [auth B], E [auth C], G [auth D], I [auth E], K [auth F], M [auth G], O [auth H], Q [auth I], S [auth J]	PF05993	Reovirus major virion structural protein Mu-1/Mu-1C (M2) (Reovirus_M2)	Reovirus major virion structural protein Mu-1/Mu-1C (M2)	-	Family
B [auth a], D [auth b], F [auth c], H [auth d], J [auth e], B [auth a], D [auth b], F [auth c], H [auth d], J [auth e], L [auth f], N [auth g], P [auth h], R [auth i], T [auth j]	PF05993	Reovirus major virion structural protein Mu-1/Mu-1C (M2) (Reovirus_M2)	Reovirus major virion structural protein Mu-1/Mu-1C (M2)	-	Family
U [auth K]	PF21064	Reovirus core-spike protein lambda-2 (L2), N-terminal (Reovirus_L2_N)	Reovirus core-spike protein lambda-2 (L2), N-terminal	Reovirus core-spike protein VP1/lambda-2 (VP1/L2) forms a pentamer that mediates enzymatic reactions in 5' capping of the viral plus-strand transcripts [1]. It forms a hollow cylinder with projecting turrets. Each VP1/L2 monomer consists of eight dom ...	Reovirus core-spike protein VP1/lambda-2 (VP1/L2) forms a pentamer that mediates enzymatic reactions in 5' capping of the viral plus-strand transcripts [1]. It forms a hollow cylinder with projecting turrets. Each VP1/L2 monomer consists of eight domains with the most N-terminal domain at the base of the turret and the most C-terminal domain at the top [2]. This entry represents the N-terminal domain which adopts an alpha/beta topology.	Domain
U [auth K]	PF21063	Reovirus core-spike protein lambda-2 (L2), GTase domain (Reovirus_L2_GTase)	Reovirus core-spike protein lambda-2 (L2), GTase domain	Reovirus core-spike protein VP1/lambda-2 (VP1/L2) forms a pentamer that mediates enzymatic reactions in 5' capping of the viral plus-strand transcripts [1]. It forms a hollow cylinder with projecting turrets. Each VP1/L2 monomer consists of eight dom ...	Reovirus core-spike protein VP1/lambda-2 (VP1/L2) forms a pentamer that mediates enzymatic reactions in 5' capping of the viral plus-strand transcripts [1]. It forms a hollow cylinder with projecting turrets. Each VP1/L2 monomer consists of eight domains with the most N-terminal domain at the base of the turret and the most C-terminal domain at the top. This entry represents the second one, which contains the nucleotide-binding histidine triad (HIT)-like motif from the GTase (guanylyltransferase) domain [2].	Domain
U [auth K]	PF21066	Reovirus core-spike protein lambda-2 (L2), methyltransferase-2 (Reovirus_L2_MT2)	Reovirus core-spike protein lambda-2 (L2), methyltransferase-2	Reovirus core-spike protein VP1/lambda-2 (VP1/L2) forms a pentamer that mediates enzymatic reactions in 5' capping of the viral plus-strand transcripts [1]. It forms a hollow cylinder with projecting turrets. Each VP1/L2 monomer consists of eight dom ...	Reovirus core-spike protein VP1/lambda-2 (VP1/L2) forms a pentamer that mediates enzymatic reactions in 5' capping of the viral plus-strand transcripts [1]. It forms a hollow cylinder with projecting turrets. Each VP1/L2 monomer consists of eight domains with the most N-terminal domain at the base of the turret and the most C-terminal domain at the top. This entry represents the second methyltransferase domain (MT2), which catalyses the last reaction, 2'O-methylation [2].	Domain
U [auth K]	PF21065	Reovirus core-spike protein lambda-2 (L2), methyltransferase-1 (Reovirus_L2_MT1)	Reovirus core-spike protein lambda-2 (L2), methyltransferase-1	Reovirus core-spike protein VP1/lambda-2 (VP1/L2) forms a pentamer that mediates enzymatic reactions in 5' capping of the viral plus-strand transcripts [1]. It forms a hollow cylinder with projecting turrets. Each VP1/L2 monomer consists of eight dom ...	Reovirus core-spike protein VP1/lambda-2 (VP1/L2) forms a pentamer that mediates enzymatic reactions in 5' capping of the viral plus-strand transcripts [1]. It forms a hollow cylinder with projecting turrets. Each VP1/L2 monomer consists of eight domains with the most N-terminal domain at the base of the turret and the most C-terminal domain at the top. This entry represents the methyltransferase-1 domain [2] which adds a methyl group to the N7 of the guanosine added by the GTase [2].	Domain
U [auth K]	PF21060	Reovirus core-spike protein lambda-2 (L2), 6th domain (Reovirus_L2_6th)	Reovirus core-spike protein lambda-2 (L2), 6th domain	Reovirus core-spike protein VP1/lambda-2 (VP1/L2) forms a pentamer that mediates enzymatic reactions in 5' capping of the viral plus-strand transcripts [1]. It forms a hollow cylinder with projecting turrets. Each VP1/L2 monomer consists of eight dom ...	Reovirus core-spike protein VP1/lambda-2 (VP1/L2) forms a pentamer that mediates enzymatic reactions in 5' capping of the viral plus-strand transcripts [1]. It forms a hollow cylinder with projecting turrets. Each VP1/L2 monomer consists of eight domains with the most N-terminal domain at the base of the turret and the most C-terminal domain at the top. This entry represents the sixth domain which, together with the seventh and eighth (Pfam:PF06016) domains forms a three-domain flap at the top of the turret, that may serve as a gate to retard exit of the 5' terminus of the mRNA [2]. This domain has a Ig-like fold, resembling the V of an antibody light chain [2].	Domain
U [auth K]	PF21062	Reovirus core-spike protein lambda-2 (L2), ferredoxin-like domain (Reovirus_L2_4th)	Reovirus core-spike protein lambda-2 (L2), ferredoxin-like domain	Reovirus core-spike protein VP1/lambda-2 (VP1/L2) forms a pentamer that mediates enzymatic reactions in 5' capping of the viral plus-strand transcripts [1]. It forms a hollow cylinder with projecting turrets. Each VP1/L2 monomer consists of eight dom ...	Reovirus core-spike protein VP1/lambda-2 (VP1/L2) forms a pentamer that mediates enzymatic reactions in 5' capping of the viral plus-strand transcripts [1]. It forms a hollow cylinder with projecting turrets. Each VP1/L2 monomer consists of eight domains with the most N-terminal domain at the base of the turret and the most C-terminal domain at the top. This entry represents the fourth domain, which adopts a ferredoxin-like fold consisting of four beta-strands protected by alpha-helices that probably functions as a structural support for the three enzyme domains (two methyltransferase and GTase domains) [2].	Domain
U [auth K]	PF06016	Reovirus core-spike protein lambda-2 (L2), C-terminal (Reovirus_L2_8th)	Reovirus core-spike protein lambda-2 (L2), C-terminal	Reovirus core-spike protein VP1/lambda-2 (VP1/L2) forms a pentamer that mediates enzymatic reactions in 5' capping of the viral plus-strand transcripts [1]. It forms a hollow cylinder with projecting turrets. Each VP1/L2 monomer consists of eight dom ...	Reovirus core-spike protein VP1/lambda-2 (VP1/L2) forms a pentamer that mediates enzymatic reactions in 5' capping of the viral plus-strand transcripts [1]. It forms a hollow cylinder with projecting turrets. Each VP1/L2 monomer consists of eight domains with the most N-terminal domain at the base of the turret and the most C-terminal domain at the top. This entry represents the C-terminal (eighth) domain which, together with the sixth and seventh domains, forms a three-domain flap at the top of the turret, that may serve as a gate to retard exit of the 5' terminus of the mRNA [2]. This domain has a Ig-like, resembling a truncated V region of an antibody light chain.	Domain
U [auth K]	PF21061	Reovirus core-spike protein lambda-2 (L2), 7th domain (Reovirus_L2_7th)	Reovirus core-spike protein lambda-2 (L2), 7th domain	Reovirus core-spike protein VP1/lambda-2 (VP1/L2) forms a pentamer that mediates enzymatic reactions in 5' capping of the viral plus-strand transcripts [1]. It forms a hollow cylinder with projecting turrets. Each VP1/L2 monomer consists of eight dom ...	Reovirus core-spike protein VP1/lambda-2 (VP1/L2) forms a pentamer that mediates enzymatic reactions in 5' capping of the viral plus-strand transcripts [1]. It forms a hollow cylinder with projecting turrets. Each VP1/L2 monomer consists of eight domains with the most N-terminal domain at the base of the turret and the most C-terminal domain at the top. This entry represents the seventh domain which, together with the sixth (Pfam:PF21060) and eighth (Pfam:PF06016) domains forms a three-domain flap at the top of the turret, that may serve as a gate to retard exit of the 5' terminus of the mRNA [2]. This domain has a Ig-like fold, resembling the C region of an antibody light chain [2].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, C [auth B], E [auth C], G [auth D], I [auth E], A, C [auth B], E [auth C], G [auth D], I [auth E], K [auth F], M [auth G], O [auth H], Q [auth I], S [auth J]	Mu1	host cell surface binding binding	symbiont-mediated disruption of host anatomical structure symbiont entry into host cell via permeabilization of inner membrane biological process involved in interspecies interaction between organisms symbiont entry into host cell via permeabilization of host membrane viral life cycle biological process involved in interaction with host biological process involved in symbiotic interaction symbiont-mediated perturbation of host membrane symbiont-mediated disruption of host cellular anatomical entity symbiont entry into host cell viral process symbiont entry into host disruption of anatomical structure in another organism permeabilization of host organelle membrane involved in viral entry into host cell	membrane cellular anatomical entity host intracellular membrane-bounded organelle host cellular component host intracellular part host cell cytoplasm host cell part host cell endoplasmic reticulum host intracellular region host cell cytoplasm part host intracellular organelle host cell mitochondrion host cell plasma membrane host cell membrane membrane cellular anatomical entity host intracellular membrane-bounded organelle host cellular component host intracellular part host cell cytoplasm host cell part host cell endoplasmic reticulum host intracellular region host cell cytoplasm part host intracellular organelle host cell mitochondrion host cell plasma membrane host cell membrane viral capsid icosahedral viral capsid virion component viral outer capsid
B [auth a], D [auth b], F [auth c], H [auth d], J [auth e], B [auth a], D [auth b], F [auth c], H [auth d], J [auth e], L [auth f], N [auth g], P [auth h], R [auth i], T [auth j]	Mu1	host cell surface binding binding	symbiont-mediated disruption of host anatomical structure symbiont entry into host cell via permeabilization of inner membrane biological process involved in interspecies interaction between organisms symbiont entry into host cell via permeabilization of host membrane viral life cycle biological process involved in interaction with host biological process involved in symbiotic interaction symbiont-mediated perturbation of host membrane symbiont-mediated disruption of host cellular anatomical entity symbiont entry into host cell viral process symbiont entry into host disruption of anatomical structure in another organism permeabilization of host organelle membrane involved in viral entry into host cell	membrane cellular anatomical entity host intracellular membrane-bounded organelle host cellular component host intracellular part host cell cytoplasm host cell part host cell endoplasmic reticulum host intracellular region host cell cytoplasm part host intracellular organelle host cell mitochondrion host cell plasma membrane host cell membrane membrane cellular anatomical entity host intracellular membrane-bounded organelle host cellular component host intracellular part host cell cytoplasm host cell part host cell endoplasmic reticulum host intracellular region host cell cytoplasm part host intracellular organelle host cell mitochondrion host cell plasma membrane host cell membrane viral capsid icosahedral viral capsid virion component viral outer capsid
U [auth K]	mRNA (guanine-N(7)-)-methyltransferase	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding guanylyltransferase activity mRNA guanylyltransferase activity RNA guanylyltransferase activity catalytic activity, acting on RNA catalytic activity, acting on a nucleic acid transferase activity catalytic activity nucleotidyltransferase activity transferase activity, transferring phosphorus-containing groups RNA methyltransferase activity transferase activity, transferring one-carbon groups S-adenosylmethionine-dependent methyltransferase activity mRNA 5'-cap (guanine-N7-)-methyltransferase activity N-methyltransferase activity methyltransferase activity mRNA methyltransferase activity guanyl nucleotide binding GTP binding guanyl ribonucleotide binding	-	viral capsid icosahedral viral capsid virion component viral outer capsid

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, C [auth B], E [auth C], G [auth D], I [auth E], A, C [auth B], E [auth C], G [auth D], I [auth E], K [auth F], M [auth G], O [auth H], Q [auth I], S [auth J]	IPR015961	Mu1 membrane penetration protein, domain I	Homologous Superfamily
A, C [auth B], E [auth C], G [auth D], I [auth E], A, C [auth B], E [auth C], G [auth D], I [auth E], K [auth F], M [auth G], O [auth H], Q [auth I], S [auth J]	IPR015960	Mu1 membrane penetration protein, domain IV	Homologous Superfamily
A, C [auth B], E [auth C], G [auth D], I [auth E], A, C [auth B], E [auth C], G [auth D], I [auth E], K [auth F], M [auth G], O [auth H], Q [auth I], S [auth J]	IPR036256	Mu1/VP4 superfamily	Homologous Superfamily
A, C [auth B], E [auth C], G [auth D], I [auth E], A, C [auth B], E [auth C], G [auth D], I [auth E], K [auth F], M [auth G], O [auth H], Q [auth I], S [auth J]	IPR009113	Outer capsid protein Mu1/VP4	Family
A, C [auth B], E [auth C], G [auth D], I [auth E], A, C [auth B], E [auth C], G [auth D], I [auth E], K [auth F], M [auth G], O [auth H], Q [auth I], S [auth J]	IPR015962	Mu1 membrane penetration protein, domain II	Homologous Superfamily
A, C [auth B], E [auth C], G [auth D], I [auth E], A, C [auth B], E [auth C], G [auth D], I [auth E], K [auth F], M [auth G], O [auth H], Q [auth I], S [auth J]	IPR044937	Mu1 membrane penetration protein, domain III	Homologous Superfamily
B [auth a], D [auth b], F [auth c], H [auth d], J [auth e], B [auth a], D [auth b], F [auth c], H [auth d], J [auth e], L [auth f], N [auth g], P [auth h], R [auth i], T [auth j]	IPR015961	Mu1 membrane penetration protein, domain I	Homologous Superfamily
B [auth a], D [auth b], F [auth c], H [auth d], J [auth e], B [auth a], D [auth b], F [auth c], H [auth d], J [auth e], L [auth f], N [auth g], P [auth h], R [auth i], T [auth j]	IPR015960	Mu1 membrane penetration protein, domain IV	Homologous Superfamily
B [auth a], D [auth b], F [auth c], H [auth d], J [auth e], B [auth a], D [auth b], F [auth c], H [auth d], J [auth e], L [auth f], N [auth g], P [auth h], R [auth i], T [auth j]	IPR036256	Mu1/VP4 superfamily	Homologous Superfamily
B [auth a], D [auth b], F [auth c], H [auth d], J [auth e], B [auth a], D [auth b], F [auth c], H [auth d], J [auth e], L [auth f], N [auth g], P [auth h], R [auth i], T [auth j]	IPR009113	Outer capsid protein Mu1/VP4	Family
B [auth a], D [auth b], F [auth c], H [auth d], J [auth e], B [auth a], D [auth b], F [auth c], H [auth d], J [auth e], L [auth f], N [auth g], P [auth h], R [auth i], T [auth j]	IPR015962	Mu1 membrane penetration protein, domain II	Homologous Superfamily
B [auth a], D [auth b], F [auth c], H [auth d], J [auth e], B [auth a], D [auth b], F [auth c], H [auth d], J [auth e], L [auth f], N [auth g], P [auth h], R [auth i], T [auth j]	IPR044937	Mu1 membrane penetration protein, domain III	Homologous Superfamily
U [auth K]	IPR048601	Reovirus core-spike protein lambda-2-like, GTase domain	Domain
U [auth K]	IPR048602	Reovirus core-spike protein lambda-2-like, 7th domain	Domain
U [auth K]	IPR048604	Reovirus core-spike protein lambda-2-like, ferredoxin-like domain	Domain
U [auth K]	IPR029063	S-adenosyl-L-methionine-dependent methyltransferase superfamily	Homologous Superfamily
U [auth K]	IPR048598	Reovirus core-spike protein lambda-2-like, first methyltransferase domain	Domain
U [auth K]	IPR048596	Reovirus core-spike protein lambda-2-like, N-terminal domain	Domain
U [auth K]	IPR013783	Immunoglobulin-like fold	Homologous Superfamily
U [auth K]	IPR048603	Reovirus core-spike protein lambda-2-like, 6th domain	Domain
U [auth K]	IPR010311	Reovirus core-spike lambda-2	Family
U [auth K]	IPR048597	Reovirus core-spike protein lambda-2-like, second methyltransferase domain	Domain
U [auth K]	IPR048294	Reovirus core-spike protein lambda-2-like, C-terminal domain	Domain