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SSB_RICPR
ID   SSB_RICPR               Reviewed;         152 AA.
AC   Q9ZCC2;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 106.
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=RP836;
OS   Rickettsia prowazekii (strain Madrid E).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=272947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA   Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA   Kurland C.G.;
RT   "The genome sequence of Rickettsia prowazekii and the origin of
RT   mitochondria.";
RL   Nature 396:133-140(1998).
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; AJ235273; CAA15261.1; -; Genomic_DNA.
DR   PIR; E71645; E71645.
DR   RefSeq; NP_221185.1; NC_000963.1.
DR   RefSeq; WP_004596816.1; NC_000963.1.
DR   AlphaFoldDB; Q9ZCC2; -.
DR   SMR; Q9ZCC2; -.
DR   STRING; 272947.RP836; -.
DR   EnsemblBacteria; CAA15261; CAA15261; CAA15261.
DR   GeneID; 57569959; -.
DR   KEGG; rpr:RP836; -.
DR   PATRIC; fig|272947.5.peg.873; -.
DR   eggNOG; COG0629; Bacteria.
DR   HOGENOM; CLU_078758_0_2_5; -.
DR   OMA; GNCIGRF; -.
DR   Proteomes; UP000002480; Chromosome.
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..152
FT                   /note="Single-stranded DNA-binding protein"
FT                   /id="PRO_0000096089"
FT   DOMAIN          5..111
FT                   /note="SSB"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00984"
FT   DNA_BIND        54..60
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00984"
FT   REGION          118..152
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           147..152
FT                   /note="Important for interaction with partner proteins"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00984"
FT   COMPBIAS        130..152
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   152 AA;  17477 MW;  57B5C86F73707493 CRC64;
     MAGSLNKVIL IGNVGRDPEI RTTGEGKKII NLSLATTETW KDRITSERKE RTEWHRVVIF
     SEGLVSIVER YVTKGSKLYI EGSLQTRKWN DNSGQEKYTT EVVLQNFNSQ LILLDHKNSN
     QNTQGSGHHE YKYPETKNHS FDHSDLDDEI PF
 
 
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