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SSB_VIBPA
ID   SSB_VIBPA               Reviewed;         176 AA.
AC   Q87LA3;
DT   24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=Single-stranded DNA-binding protein {ECO:0000255|HAMAP-Rule:MF_00984};
DE            Short=SSB {ECO:0000255|HAMAP-Rule:MF_00984};
GN   Name=ssb; OrderedLocusNames=VP2709;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(2003).
CC   -!- FUNCTION: Plays an important role in DNA replication, recombination and
CC       repair. Binds to ssDNA and to an array of partner proteins to recruit
CC       them to their sites of action during DNA metabolism.
CC       {ECO:0000255|HAMAP-Rule:MF_00984}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00984}.
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DR   EMBL; BA000031; BAC60972.1; -; Genomic_DNA.
DR   RefSeq; NP_799088.1; NC_004603.1.
DR   RefSeq; WP_005466625.1; NC_004603.1.
DR   AlphaFoldDB; Q87LA3; -.
DR   SMR; Q87LA3; -.
DR   STRING; 223926.28807719; -.
DR   EnsemblBacteria; BAC60972; BAC60972; BAC60972.
DR   GeneID; 1190254; -.
DR   KEGG; vpa:VP2709; -.
DR   PATRIC; fig|223926.6.peg.2605; -.
DR   eggNOG; COG0629; Bacteria.
DR   HOGENOM; CLU_078758_0_2_6; -.
DR   OMA; GQMQERT; -.
DR   Proteomes; UP000002493; Chromosome 1.
DR   GO; GO:0003697; F:single-stranded DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR   CDD; cd04496; SSB_OBF; 1.
DR   Gene3D; 2.40.50.140; -; 1.
DR   HAMAP; MF_00984; SSB; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR000424; Primosome_PriB/ssb.
DR   InterPro; IPR011344; ssDNA-bd.
DR   PANTHER; PTHR10302; PTHR10302; 1.
DR   Pfam; PF00436; SSB; 1.
DR   PIRSF; PIRSF002070; SSB; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR00621; ssb; 1.
DR   PROSITE; PS50935; SSB; 1.
PE   3: Inferred from homology;
KW   DNA damage; DNA recombination; DNA repair; DNA replication; DNA-binding;
KW   Reference proteome.
FT   CHAIN           1..176
FT                   /note="Single-stranded DNA-binding protein"
FT                   /id="PRO_0000096137"
FT   DOMAIN          6..111
FT                   /note="SSB"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00984"
FT   DNA_BIND        55..61
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00984"
FT   REGION          114..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           171..176
FT                   /note="Important for interaction with partner proteins"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00984"
FT   COMPBIAS        124..165
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   176 AA;  19564 MW;  BC3FB8C181951EB7 CRC64;
     MASRGINKVI LVGNLGNDPE IRYMPNGGAV ANITIATSES WRDKATGEQR EKTEWHRVVL
     FGKLAEVAGE YLRKGSQVYV EGQLQTRKWQ DQSGQDRYST EVVVQGFNGV MQMLGGRAQG
     GAPAMGGQQQ QQGGWGQPQQ PAQQQYNAPQ QQQQAPQQPQ QQYNEPPMDF DDDIPF
 
 
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