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UVRA_VIBVU
ID   UVRA_VIBVU              Reviewed;         940 AA.
AC   Q8DCJ3;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=UvrABC system protein A {ECO:0000255|HAMAP-Rule:MF_00205};
DE            Short=UvrA protein {ECO:0000255|HAMAP-Rule:MF_00205};
DE   AltName: Full=Excinuclease ABC subunit A {ECO:0000255|HAMAP-Rule:MF_00205};
GN   Name=uvrA {ECO:0000255|HAMAP-Rule:MF_00205}; OrderedLocusNames=VV1_1427;
OS   Vibrio vulnificus (strain CMCP6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=216895;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CMCP6;
RA   Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT   "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL   Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The UvrABC repair system catalyzes the recognition and
CC       processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein.
CC       A damage recognition complex composed of 2 UvrA and 2 UvrB subunits
CC       scans DNA for abnormalities. When the presence of a lesion has been
CC       verified by UvrB, the UvrA molecules dissociate. {ECO:0000255|HAMAP-
CC       Rule:MF_00205}.
CC   -!- SUBUNIT: Forms a heterotetramer with UvrB during the search for
CC       lesions. {ECO:0000255|HAMAP-Rule:MF_00205}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00205}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. UvrA family.
CC       {ECO:0000255|HAMAP-Rule:MF_00205}.
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DR   EMBL; AE016795; AAO09867.1; -; Genomic_DNA.
DR   RefSeq; WP_011079386.1; NC_004459.3.
DR   AlphaFoldDB; Q8DCJ3; -.
DR   SMR; Q8DCJ3; -.
DR   EnsemblBacteria; AAO09867; AAO09867; VV1_1427.
DR   KEGG; vvu:VV1_1427; -.
DR   HOGENOM; CLU_001370_0_2_6; -.
DR   OMA; PFEGIIP; -.
DR   Proteomes; UP000002275; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0009380; C:excinuclease repair complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009381; F:excinuclease ABC activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006289; P:nucleotide-excision repair; IEA:UniProtKB-UniRule.
DR   GO; GO:0009432; P:SOS response; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   HAMAP; MF_00205; UvrA; 1.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR004602; UvrA.
DR   InterPro; IPR041552; UvrA_DNA-bd.
DR   InterPro; IPR041102; UvrA_inter.
DR   Pfam; PF00005; ABC_tran; 1.
DR   Pfam; PF17755; UvrA_DNA-bind; 1.
DR   Pfam; PF17760; UvrA_inter; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   TIGRFAMs; TIGR00630; uvra; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; DNA damage; DNA excision; DNA repair; DNA-binding;
KW   Excision nuclease; Metal-binding; Nucleotide-binding; Repeat; SOS response;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..940
FT                   /note="UvrABC system protein A"
FT                   /id="PRO_0000093113"
FT   DOMAIN          309..586
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT   DOMAIN          606..936
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT   ZN_FING         252..279
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT   ZN_FING         739..765
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT   BINDING         31..38
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
FT   BINDING         639..646
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00205"
SQ   SEQUENCE   940 AA;  103960 MW;  8DB4C3150866C40A CRC64;
     MDKIEVRGAR THNLKNINLT IPRDKLIVIT GLSGSGKSSL AFDTLYAEGQ RRYVESLSAY
     ARQFLSLMEK PDVDHIEGLS PAISIEQKST SHNPRSTVGT ITEVYDYLRL LYARVGEPRC
     PEHQVPLAAQ TISQMVDKVL ELPEGAKMML LAPIVKERKG EHVKTLENLA AQGFIRARID
     GETCDLTDPP TLELHKKHTI EVVVDRVKVR GDLQQRLAES FETALELSGG IAVIAPMEGD
     GEEIVFSANF ACPHCGYSMQ ELEPRLFSFN NPAGACGTCD GLGVQQYFDP ERVIQDANLS
     LAQGAIRGWD QKNYYYFQML TSLAEHYDFD LHAPFNSLSK RIQEVILKGS GRTEIEFKYI
     NDRGDIRLKR HPFEGILNTL ERRYRDTESN SVREELVKYI STKPCTSCGG TRLRLEARNV
     FINDTTLPQI VELSIADALT FFATLKLEGQ RAQIAEKVMK EINDRLQFLV NVGLNYLNLS
     RSAETLSGGE AQRIRLASQI GAGLVGVMYV LDEPSIGLHQ RDNERLLKTL THLRDLGNTV
     LVVEHDEDAI RCADHVIDIG PGAGVHGGQV VAEGTMAEIL ANPDSLTGQY LSGAKQIIVP
     TQRTPRDKNK TVELIGASGN NLKEVNLSVP VGLFSCITGV SGSGKSTLIN DTFFKIAHTQ
     LNGATTAQPA PYKSIKGLEH FDKVIDIDQS PIGRTPRSNP ATYTGIFTPI RELFSGTQES
     RSRGYKPGRF SFNVRGGRCE ACQGDGVIKV EMHFLPDVYV PCDVCKGKRY NRETLEVHYK
     GKSIDEVLEM TVEDAHEFFA PVPVIARKLQ TLMDVGLSYI RLGQAATTLS GGEAQRVKLA
     RELSKRDTGK TLYILDEPTT GLHFHDIQQL LTVLHRLRDH GNTVVVIEHN LDVIKTADWI
     IDLGPEGGQG GGEIIAQGTP EDVAQIEGSH TARFLKPMLK
 
 
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