Annotations: 3UXF

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Gram-positive pilin BB domain-like	8092042	4004692	SCOP2 (2022-06-29)
A	SCOP2 Family	Gram-positive pilin N-terminal domain-like	8048171	4004671	SCOP2 (2022-06-29)
A	SCOP2 Family	Gram-positive pilin backbone D3 domain-like	8092044	4004691	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Bacterial adhesin-like	8092043	3000723	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Cna B-type domain-like	8092041	3000862	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Cna B-type domain-like	8092045	3000862	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	PF16555	e3uxfA5	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Prealbumin-like	F: PF16555	ECOD (1.6)
A	PF17802	e3uxfA4	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Prealbumin-like	F: PF17802	ECOD (1.6)
A	F_UNCLASSIFIED	e3uxfA3	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Common fold of diphtheria toxin/transcription factors/cytochrome f	F: F_UNCLASSIFIED	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.60.40.10	Mainly Beta	Sandwich	Immunoglobulin-like	Immunoglobulins	CATH (4.3.0)
A	2.60.40.740	Mainly Beta	Sandwich	Immunoglobulin-like		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00746	LPXTG cell wall anchor motif (Gram_pos_anchor)	LPXTG cell wall anchor motif	-	Motif
A	PF16555	Gram-positive pilin subunit D1, N-terminal domain (GramPos_pilinD1)	Gram-positive pilin subunit D1, N-terminal domain	GramPos_pilinD1 is the first subunit domain of Gram-positive pilins from Strep.pneumoniae. There are three major pilin subunits that form the polymeric backbone of the pilin from S. pneumoniae, constructed of three Ig-like, CnaB, domains along with a ...	GramPos_pilinD1 is the first subunit domain of Gram-positive pilins from Strep.pneumoniae. There are three major pilin subunits that form the polymeric backbone of the pilin from S. pneumoniae, constructed of three Ig-like, CnaB, domains along with a crucial N-terminal domain, D1. The three IG-like domains are stabilised by internal Lys-Asn isopeptide bonds, but this N-terminal domain makes few contact with the rest of the molecule due to the different orientation of its G beta-strand. Strand G of D1 also carries the YPKN motif that provides the essential Lys residue for the sortase-mediated intermolecular linkages along the pilus shaft. Gram-positive pili are formed from a single chain of covalently linked subunit proteins (pilins), usually comprising an adhesin at the distal tip, a major pilin that forms the polymer shaft and a minor pilin that mediates cell wall anchoring at the base [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Fimbrial subunit type 1	-	carbohydrate metabolic process organic substance metabolic process primary metabolic process metabolic process	extracellular region cellular anatomical entity pilus cell projection

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR013783	Immunoglobulin-like fold	Homologous Superfamily
A	IPR006311	Twin-arginine translocation pathway, signal sequence	Conserved Site
A	IPR026466	Fimbrial isopeptide formation D2 domain	Domain
A	IPR048052	Fimbrial subunit type 1-like	Family
A	IPR032364	Gram-positive pilin subunit D1, N-terminal	Domain
A	IPR019931	LPXTG cell wall anchor domain	Domain

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), 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.