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RFA1_CAEBR
ID   RFA1_CAEBR              Reviewed;         658 AA.
AC   O97472;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Probable replication factor A 73 kDa subunit {ECO:0000250|UniProtKB:Q19537};
DE   AltName: Full=RP-A p73;
DE   AltName: Full=Replication factor A protein 1;
DE            Short=RF-A protein 1;
GN   Name=rpa-1 {ECO:0000312|EMBL:CAP31894.1}; ORFNames=CBG13026;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1] {ECO:0000312|EMBL:CAA10310.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10224256; DOI=10.1093/genetics/152.1.221;
RA   Dufourcq P., Chanal P., Vicaire S., Camut E., Quintin S., den Boer B.B.W.,
RA   Bosher J.M., Labouesse M.;
RT   "lir-2, lir-1 and lin-26 encode a new class of zinc-finger proteins and are
RT   organized in two overlapping operons both in Caenorhabditis elegans and in
RT   Caenorhabditis briggsae.";
RL   Genetics 152:221-235(1999).
RN   [2] {ECO:0000312|EMBL:CAP31894.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16 {ECO:0000312|EMBL:CAP31894.1};
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- FUNCTION: As part of the heterotrimeric replication protein A complex
CC       (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates,
CC       that form during DNA replication or upon DNA stress. It prevents their
CC       reannealing and in parallel, recruits and activates different proteins
CC       and complexes involved in DNA metabolism. Thereby, it plays an
CC       essential role both in DNA replication and the cellular response to DNA
CC       damage. {ECO:0000250|UniProtKB:P27694}.
CC   -!- SUBUNIT: Component of the heterotrimeric canonical replication protein
CC       A complex (RPA). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q19537}.
CC   -!- SIMILARITY: Belongs to the replication factor A protein 1 family.
CC       {ECO:0000255}.
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DR   EMBL; AJ131134; CAA10310.1; -; Genomic_DNA.
DR   EMBL; AJ131634; CAA10466.1; -; Genomic_DNA.
DR   EMBL; HE600938; CAP31894.1; -; Genomic_DNA.
DR   RefSeq; XP_002630573.1; XM_002630527.1.
DR   AlphaFoldDB; O97472; -.
DR   SMR; O97472; -.
DR   STRING; 6238.CBG13026; -.
DR   EnsemblMetazoa; CBG13026.1; CBG13026.1; WBGene00033864.
DR   GeneID; 8572089; -.
DR   KEGG; cbr:CBG_13026; -.
DR   CTD; 8572089; -.
DR   WormBase; CBG13026; CBP03074; WBGene00033864; Cbr-rpa-1.
DR   eggNOG; KOG0851; Eukaryota.
DR   HOGENOM; CLU_012393_2_1_1; -.
DR   InParanoid; O97472; -.
DR   OMA; YRLLINM; -.
DR   OrthoDB; 1189265at2759; -.
DR   Proteomes; UP000008549; Chromosome II.
DR   GO; GO:0005662; C:DNA replication factor A complex; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IEA:EnsemblMetazoa.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central.
DR   GO; GO:0019899; F:enzyme binding; IEA:EnsemblMetazoa.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
DR   GO; GO:0043047; F:single-stranded telomeric DNA binding; IBA:GO_Central.
DR   GO; GO:0006260; P:DNA replication; ISS:UniProtKB.
DR   GO; GO:0006268; P:DNA unwinding involved in DNA replication; IBA:GO_Central.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR   GO; GO:0051321; P:meiotic cell cycle; IBA:GO_Central.
DR   GO; GO:0006289; P:nucleotide-excision repair; IBA:GO_Central.
DR   GO; GO:0051096; P:positive regulation of helicase activity; IEA:EnsemblMetazoa.
DR   GO; GO:0110039; P:positive regulation of nematode male tail tip morphogenesis; IEA:EnsemblMetazoa.
DR   GO; GO:0007004; P:telomere maintenance via telomerase; IBA:GO_Central.
DR   CDD; cd04476; RPA1_DBD_C; 1.
DR   Gene3D; 2.40.50.140; -; 3.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004365; NA-bd_OB_tRNA.
DR   InterPro; IPR013955; Rep_factor-A_C.
DR   InterPro; IPR031657; REPA_OB_2.
DR   InterPro; IPR004591; Rfa1.
DR   PANTHER; PTHR23273; PTHR23273; 1.
DR   Pfam; PF08646; Rep_fac-A_C; 1.
DR   Pfam; PF16900; REPA_OB_2; 1.
DR   Pfam; PF01336; tRNA_anti-codon; 1.
DR   SUPFAM; SSF50249; SSF50249; 3.
DR   TIGRFAMs; TIGR00617; rpa1; 1.
PE   3: Inferred from homology;
KW   DNA replication; DNA-binding; Metal-binding; Nucleus; Reference proteome;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..658
FT                   /note="Probable replication factor A 73 kDa subunit"
FT                   /id="PRO_0000361044"
FT   DNA_BIND        236..326
FT                   /note="OB"
FT                   /evidence="ECO:0000255"
FT   ZN_FING         518..539
FT                   /note="C4-type"
FT                   /evidence="ECO:0000250|UniProtKB:Q19537, ECO:0000255"
FT   REGION          134..155
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          169..222
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        187..201
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   658 AA;  73427 MW;  A919B58C8061A6E4 CRC64;
     MTSIKISSDV FNKYHTNGKL RLSTGYVQEA LEKQGYPGHD GVVQILKGKE DIGEQMGHGF
     TYRIRICDGI FQYNTLVSAD IDDQIKREAE HLVEGAIIAI TNLSTFSQGA GIKTSFLITG
     YTLLSRYHQT LSAPEVKPRS HSGNPAEHHG YRPNIVVEDV WPEAESITSE FQENMSNPPA
     AKMPKRESGG EASHNRVPAP EPHRSRAPPP PARRGPSNTE RGVIPIAMVT PYVNNFRIHG
     MVSRKEDIKN IPAKNMKIFN FEITDSNGDT IRCTAFNETA ESFHSTITEN LSYYLSGGSV
     RQANKKFNNT GHDYEITLRN DSVVEAGGEL LAAPKLNLKR VSLAEIAGHC GEMIDVLVIV
     EKMDAEATEF TSKAGKTLTK REMELIDESQ ALVRLTLWGD EAIKANVDDY HGKVIAFKGV
     IPREFNGGYS LGTGSGTRII PVPEISGVSE LYDWYTTEKP HSELKLISQT SGGMSEAPRT
     IAGLQEMQFG KDSDKGDYAS VKAMITRINP NSALYKGCAS EGCQKKVIES DGEYRCEKCN
     KSMNKFKWLY MMQFELSDET GQVYVTAFGD SAAKVVGKTA QEVGDLKDEN LNEYNATFER
     LQFVPKMWRL RCKMETYNEE VRQKMTVFSV EEVNQDKYIE NLKELIEQMK GIEDEGSY
 
 
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