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Database: UniProt
Entry: Q7V9M1
LinkDB: Q7V9M1
Original site: Q7V9M1 
ID   UVRB_PROMA              Reviewed;         677 AA.
AC   Q7V9M1;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   16-APR-2014, entry version 70.
DE   RecName: Full=UvrABC system protein B;
DE            Short=Protein UvrB;
DE   AltName: Full=Excinuclease ABC subunit B;
GN   Name=uvrB; OrderedLocusNames=Pro_1809;
OS   Prochlorococcus marinus (strain SARG / CCMP1375 / SS120).
OC   Bacteria; Cyanobacteria; Prochlorales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167539;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SARG / CCMP1375 / SS120;
RX   PubMed=12917486; DOI=10.1073/pnas.1733211100;
RA   Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M.,
RA   Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F.,
RA   Makarova K.S., Ostrowski M., Oztas S., Robert C., Rogozin I.B.,
RA   Scanlan D.J., Tandeau de Marsac N., Weissenbach J., Wincker P.,
RA   Wolf Y.I., Hess W.R.;
RT   "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120,
RT   a nearly minimal oxyphototrophic genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(2003).
CC   -!- FUNCTION: The UvrABC repair system catalyzes the recognition and
CC       processing of DNA lesions. A damage recognition complex composed
CC       of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon
CC       binding of the UvrA(2)B(2) complex to a putative damaged site, the
CC       DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP
CC       binding by UvrB and probably causes local melting of the DNA
CC       helix, facilitating insertion of UvrB beta-hairpin between the DNA
CC       strands. Then UvrB probes one DNA strand for the presence of a
CC       lesion. If a lesion is found the UvrA subunits dissociate and the
CC       UvrB-DNA preincision complex is formed. This complex is
CC       subsequently bound by UvrC and the second UvrB is released. If no
CC       lesion is found, the DNA wraps around the other UvrB subunit that
CC       will check the other stand for damage (By similarity).
CC   -!- SUBUNIT: Forms a heterotetramer with UvrA during the search for
CC       lesions. Interacts with UvrC in an incision complex (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- DOMAIN: The beta-hairpin motif is involved in DNA binding (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the UvrB family.
CC   -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC   -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC   -!- SIMILARITY: Contains 1 UVR domain.
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DR   EMBL; AE017126; AAQ00853.1; -; Genomic_DNA.
DR   RefSeq; NP_876200.1; NC_005042.1.
DR   ProteinModelPortal; Q7V9M1; -.
DR   SMR; Q7V9M1; 3-590.
DR   STRING; 167539.Pro1809; -.
DR   EnsemblBacteria; AAQ00853; AAQ00853; Pro_1809.
DR   GeneID; 1463192; -.
DR   KEGG; pma:Pro_1809; -.
DR   PATRIC; 23030471; VBIProMar8617_1911.
DR   eggNOG; COG0556; -.
DR   KO; K03702; -.
DR   OMA; MQYERND; -.
DR   OrthoDB; EOG6B360R; -.
DR   ProtClustDB; PRK05298; -.
DR   BioCyc; PMAR167539:GJN2-1853-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009381; F:excinuclease ABC activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006289; P:nucleotide-excision repair; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009432; P:SOS response; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.50.300; -; 4.
DR   Gene3D; 4.10.860.10; -; 1.
DR   HAMAP; MF_00204; UvrB; 1.
DR   InterPro; IPR006935; Helicase/UvrB_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001943; UVR_dom.
DR   InterPro; IPR004807; UvrB.
DR   InterPro; IPR024759; UvrB_YAD/RRR_dom.
DR   PANTHER; PTHR24029; PTHR24029; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF04851; ResIII; 1.
DR   Pfam; PF02151; UVR; 1.
DR   Pfam; PF12344; UvrB; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF46600; SSF46600; 1.
DR   SUPFAM; SSF52540; SSF52540; 3.
DR   TIGRFAMs; TIGR00631; uvrb; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS50151; UVR; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Cytoplasm; DNA damage; DNA excision;
KW   DNA repair; Excision nuclease; Nucleotide-binding; Reference proteome;
KW   SOS response.
FT   CHAIN         1    677       UvrABC system protein B.
FT                                /FTId=PRO_0000227341.
FT   DOMAIN       25    412       Helicase ATP-binding.
FT   DOMAIN      429    591       Helicase C-terminal.
FT   DOMAIN      639    674       UVR.
FT   NP_BIND      38     45       ATP (Potential).
FT   MOTIF        91    114       Beta-hairpin.
SQ   SEQUENCE   677 AA;  77240 MW;  3AF1E0DA4996F5F8 CRC64;
     MSKYYLKAPY QPKGDQPKAI TKLVDGVNSG REYQTLLGAT GTGKTFTIAN VIAKTGRPAL
     VLAHNKTLAA QLCNELREFF PNNAVEYFIS YYDYYQPEAY VPVSDTYIAK TSSINEEIDM
     LRHSATRSLF ERDDVIVVAS ISCIYGLGIP SEYLKASVKF KVGNEINLRK SLRELVANQY
     FRNDFDIGRG KFRVKGDVLE IGPAYDDRLV RIELFGDEIE AIRYVDPITG EILDSLNCIS
     IYPAKHFVTP KERLVTAIDD IQKELKEQLD FFNKEGKLLE AQRLEQRTKY DLEMLREVGY
     CNGVENYARH LSGREAGSPP ECLIDYFPKD WLLVIDESHV TCSQLLAMYN GDQSRKKVLI
     EHGFRLPSAA DNRPLKSQEF WNKANQTVFI SATPGNWELE ISSGAIIEQV IRPTGVLDPL
     VEVRPTKGQV EDLLDEIRER SRKKQRVLIT TLTKRMAEDL TDYLSENDVR VRYLHSEIHS
     IERIEIIQDL RMGEYDVLVG VNLLREGLDL PEVSLVVILD ADKEGFLRAE RSLIQTIGRA
     ARHIEGKALL YADNFTDSMK KAIEETERRR AIQESYNQQN NIVPMPAGKK ANNSILSFLE
     LSRRVQKDGI DNDLVEIAGN VVDEFKFNNN SELAIENLPQ LIDELETKMK KSAKDLDFEN
     AAKLRDKIHQ LRKKLIR
//
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