3N4S

Structure of Csm1 C-terminal domain, P21212 form

External Resource: Annotation

Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
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)
A	SCOP2B Superfamily	RWD domain-like	8103665	3000774	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	RWD domain-like	8103665	3000774	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	RWD domain-like	8103665	3000774	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	RWD domain-like	8103665	3000774	SCOP2B (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	PF12539	e3n4sA1	A: a+b two layers	X: Kinetochore globular domain-like (From Topology)	H: Kinetochore globular domain-like (From Topology)	T: Kinetochore globular domain-like	F: PF12539	ECOD (1.6)
B	PF12539	e3n4sB1	A: a+b two layers	X: Kinetochore globular domain-like (From Topology)	H: Kinetochore globular domain-like (From Topology)	T: Kinetochore globular domain-like	F: PF12539	ECOD (1.6)
C	PF12539	e3n4sC1	A: a+b two layers	X: Kinetochore globular domain-like (From Topology)	H: Kinetochore globular domain-like (From Topology)	T: Kinetochore globular domain-like	F: PF12539	ECOD (1.6)
D	PF12539	e3n4sD1	A: a+b two layers	X: Kinetochore globular domain-like (From Topology)	H: Kinetochore globular domain-like (From Topology)	T: Kinetochore globular domain-like	F: PF12539	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.90.1150.80	Alpha Beta	Alpha-Beta Complex	Aspartate Aminotransferase, domain 1		CATH (4.3.0)
B	3.90.1150.80	Alpha Beta	Alpha-Beta Complex	Aspartate Aminotransferase, domain 1		CATH (4.3.0)
C	3.90.1150.80	Alpha Beta	Alpha-Beta Complex	Aspartate Aminotransferase, domain 1		CATH (4.3.0)
D	3.90.1150.80	Alpha Beta	Alpha-Beta Complex	Aspartate Aminotransferase, domain 1		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF12539	Chromosome segregation protein Csm1/Pcs1 (Csm1)	Chromosome segregation protein Csm1/Pcs1	-	Family
A, B, C, D	PF18504	Csm1 N-terminal domain (Csm1_N)	Csm1 N-terminal domain	-	Coiled-coil

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	Monopolin complex subunit CSM1	identical protein binding protein binding binding	chromosome organization sister chromatid cohesion meiotic sister chromatid cohesion, centromeric cellular component organization centromeric sister chromatid cohesion organelle organization cellular process cellular component organization or biogenesis cell cycle meiotic sister chromatid cohesion cell cycle process protein localization cellular localization protein localization to nucleolar rDNA repeats chromosome organization sister chromatid cohesion meiotic sister chromatid cohesion, centromeric cellular component organization centromeric sister chromatid cohesion organelle organization cellular process cellular component organization or biogenesis cell cycle meiotic sister chromatid cohesion cell cycle process protein localization cellular localization protein localization to nucleolar rDNA repeats localization nucleus organization protein localization to chromosome nucleolus organization protein localization to organelle cellular macromolecule localization macromolecule localization meiotic chromosome segregation sexual reproduction reproductive process meiotic cell cycle organelle fission meiotic cell cycle process nuclear division meiosis I meiosis I cell cycle process nuclear chromosome segregation meiotic nuclear division homologous chromosome segregation chromosome segregation rDNA chromatin condensation protein-containing complex organization nucleolar chromatin organization protein-DNA complex organization chromatin organization chromosome condensation establishment of organelle localization attachment of meiotic spindle microtubules to kinetochore metaphase chromosome alignment meiotic metaphase I homologous chromosome alignment chromosome localization organelle localization establishment of localization in cell attachment of spindle microtubules to kinetochore spindle attachment to meiosis I kinetochore establishment of localization meiotic metaphase chromosome alignment establishment of chromosome localization	membrane-bounded organelle intracellular anatomical structure nucleus membrane-enclosed lumen intracellular membrane-bounded organelle cellular anatomical entity nucleolus intracellular organelle lumen intracellular organelle organelle lumen organelle intracellular non-membrane-bounded organelle nuclear lumen non-membrane-bounded organelle membrane-bounded organelle intracellular anatomical structure nucleus membrane-enclosed lumen intracellular membrane-bounded organelle cellular anatomical entity nucleolus intracellular organelle lumen intracellular organelle organelle lumen organelle intracellular non-membrane-bounded organelle nuclear lumen non-membrane-bounded organelle organelle envelope nuclear envelope endomembrane system monopolin complex protein-containing complex chromosome chromosomal region kinetochore chromosome, centromeric region condensed chromosome, centromeric region supramolecular complex condensed chromosome

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR038608	Csm1/Pcs1, C-terminal domain superfamily	Homologous Superfamily
A, B, C, D	IPR041671	Csm1 N-terminal domain	Domain
A, B, C, D	IPR020981	Monopolin complex subunit Csm1/Pcs1, C-terminal	Domain
A, B, C, D	IPR040349	Monopolin complex subunit Csm1/Pcs1	Family

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.