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Database: UniProt/TrEMBL
Entry: F4GYZ1_CELFA
LinkDB: F4GYZ1_CELFA
Original site: F4GYZ1_CELFA 
ID   F4GYZ1_CELFA            Unreviewed;       701 AA.
AC   F4GYZ1;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   11-JUN-2014, entry version 23.
DE   RecName: Full=UvrABC system protein B;
DE            Short=Protein UvrB;
DE   AltName: Full=Excinuclease ABC subunit B;
GN   Name=uvrB; OrderedLocusNames=Celf_1851;
OS   Cellulomonas fimi (strain ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513
OS   / NCIMB 8980 / NCTC 7547).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Micrococcineae; Cellulomonadaceae; Cellulomonas.
OX   NCBI_TaxID=590998;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 / NCIMB 8980 /
RC   NCTC 7547;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Chertkov O., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I.,
RA   Mead D., Brumm P., Woyke T.;
RT   "Complete sequence of Cellulomonas fimi ATCC 484.";
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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 UVR domain.
CC   -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC   -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC   -!- SIMILARITY: Contains UVR domain.
CC   -!- SIMILARITY: Contains helicase ATP-binding domain.
CC   -!- SIMILARITY: Contains helicase C-terminal domain.
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DR   EMBL; CP002666; AEE45981.1; -; Genomic_DNA.
DR   RefSeq; YP_004453368.1; NC_015514.1.
DR   EnsemblBacteria; AEE45981; AEE45981; Celf_1851.
DR   GeneID; 10592633; -.
DR   KEGG; cfi:Celf_1851; -.
DR   PATRIC; 54614630; VBICelFim18861_1853.
DR   KO; K03702; -.
DR   OMA; GIAGWHE; -.
DR   BioCyc; CFIM590998:GJFK-1873-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; Helicase; Hydrolase;
KW   Nucleotide-binding; SOS response.
FT   DOMAIN       35    192       Helicase ATP-binding (By similarity).
FT   DOMAIN      438    604       Helicase C-terminal (By similarity).
FT   DOMAIN      657    692       UVR (By similarity).
FT   NP_BIND      48     55       ATP (By similarity){EA2}.
FT   MOTIF       101    124       Beta-hairpin (By similarity).
SQ   SEQUENCE   701 AA;  78433 MW;  F11FEE83DAC60F48 CRC64;
     MRPVTELQRT VAPFQVVSEF TPSGDQPAAI AELASRINAG EKDVVLLGAT GTGKSATTAW
     LIEQVQRPTL VMAPNKTLAA QLATEFRELL PNNAVEYFVS YYDYYQPEAY IVQTDTYIEK
     DSSINDEVER LRHSATSSLL TRRDVVVVAS VSCIYGLGTP QEYVDRMVTL DVGQQIDRDQ
     LLRRFVQMQY TRNDLAFTRG TFRVRGDTVE IIPMYEELAI RIEFFGDEIE AIATLHPLTG
     DVVRSEDQMM IFPATHYVAG PERMERAIAG IELELEDRLA ELESQNKLLE AQRLRMRTTY
     DIEMMRQIGS CSGIENYSRH IDGRTAGSAP NTLLDFFPED FLLVIDESHV TVPQIGAMFE
     GDMSRKRALV EHGFRLPSAT DNRPLRWEEF VERIGQTVYL SATPGDYELS MADGVVEQII
     RPTGLVDPEV VVKPTKGQID DLLGEIHDRV ERDERVLVTT LTKKMAEDLT DYFLEKGVRV
     RYLHSEVDTL RRVELLRELR LGEYDVLVGI NLLREGLDLP EVSLVAILDA DKEGFLRSGK
     SLIQTIGRAA RNVSGQVHMY ADKITPAMQL AIEETSRRRE KQIAYNTERG IDPQPLRKKI
     GDITDLLARE DADTAELLGG AGRQASRGKA PVPGFGSKGA PRDERTRLTG AAAGELAGLI
     QELTDQMHAA AGELQFELAA RLRDEISGLK KELRQMQAAT A
//
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