SUPERFAMILY 1.75 HMM library and genome assignments server


N-terminal domains of the minor coat protein g3p superfamily

SCOP classification
Root:   SCOP hierarchy in SUPERFAMILY [ 0] (11)
Class:   All beta proteins [ 48724] (174)
Fold:   N-terminal domains of the minor coat protein g3p [ 50175]
Superfamily:   N-terminal domains of the minor coat protein g3p [ 50176]
Families:   N-terminal domains of the minor coat protein g3p [ 50177]


Superfamily statistics
Genomes (3) Uniprot 2013_05 PDB chains (SCOP 1.75)
Domains 4 51 6
Proteins 4 36 4


Functional annotation
General category Other
Detailed category Viral proteins

Document:
Function annotation of SCOP domain superfamilies

UniProtKB KeyWords (KW)

(show details)
KW termFDR (all)SDKW levelAnnotation (direct or inherited)
Biological processHost-virus interaction0Moderately InformativeDirect
Biological processVirus entry into host cell0InformativeDirect
Biological processVirus exit from host cell0Highly InformativeDirect
Cellular componentMembrane0Least InformativeDirect
Cellular componentHost membrane0InformativeDirect
DomainTransmembrane0Least InformativeDirect
DomainSignal0Least InformativeDirect

Document: KW annotation of SCOP domains

InterPro annotation
Cross references IPR008021 SSF50176 Protein matches
Abstract

The g3p protein (also known as attachment protein or coat protein A) of filamentous phage such as M13, phage fd and phage f1, is an essential coat protein for the infection of Escherichia coli. The g3p protein consists of three domains: two N-terminal domains (N1 and N2) with a similar beta-barrel fold, and a C-terminal domain [PubMed9461080]. The N-terminal domains protrude from the phage surface, while the C-terminal domain acts as an anchor embedded in the phage coat, together forming a horseshoe-like structure [PubMed12767837]. The g3p protein exists as 3-5 copies at the tip of the phage particle.

Infection by filamentous phage occurs in two steps, both of which are mediated by the g3p protein: phage attachment to the F-pilus of the host cell as the primary receptor, followed by attachment to the C-terminal domain of the periplasmic protein TolA as a co-receptor.

This entry represents the two N-terminal domains, N1 and N2, of the filamentous phage coat protein g3p.


InterPro database


PDBeMotif information about ligands, sequence and structure motifs
Cross references PDB entries
Ligand binding statistics
Nucleic-acid binding statistics
Occurrence of secondary structure elements
Occurrence of small 3D structural motifs

PDBeMotif resource

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Internal database links

Browse genome assignments for this superfamily. The SUPERFAMILY hidden Markov model library has been used to carry out SCOP domain assignments to all genomes at the superfamily level.


Alignments of sequences to 2 models in this superfamily are available by clicking on the 'Alignments' icon above. PDB sequences less than 40% identical are shown by default, but any other sequence(s) may be aligned. Select PDB sequences, genome sequences, or paste in or upload your own sequences.


Browse and view proteins in genomes which have different domain combinations including a N-terminal domains of the minor coat protein g3p domain.


Examine the distribution of domain superfamilies, or families, across the major taxonomic kingdoms or genomes within a kingdom. This gives an immediate impression of how superfamilies, or families, are restricted to certain kingdoms of life.


Explore domain occurrence network where nodes represent genomes and edges are domain architectures (shared between genomes) containing the superfamily of interest.

There are 2 hidden Markov models representing the N-terminal domains of the minor coat protein g3p superfamily. Information on how the models are built, and plots showing hydrophobicity, match emmission probabilities and insertion/deletion probabilities can be inspected.


Jump to [ Top of page · SCOP classification · InterPro annotation · PDBeMotif links · Functional annotation · UniProtKB KeyWords (KW) · Internal database links ]