ID A1IGB7_PHOPO Unreviewed; 675 AA. AC A1IGB7; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 06-MAR-2013, entry version 38. DE RecName: Full=UvrABC system protein B; DE Short=Protein UvrB; DE AltName: Full=Excinuclease ABC subunit B; GN Name=uvrB; OS Photobacterium phosphoreum. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Photobacterium. OX NCBI_TaxID=659; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=IFO 13896; RA Kasai S.; RT "Identification of luxO in Photobacterium phosphoreum IFO 13896."; RL Submitted (JAN-2003) 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB101000; BAF43690.1; -; Genomic_DNA. DR ProteinModelPortal; A1IGB7; -. DR SMR; A1IGB7; 5-597. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:HAMAP. DR GO; GO:0009381; F:excinuclease ABC activity; IEA:HAMAP. DR GO; GO:0004386; F:helicase activity; IEA:HAMAP. DR GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC. DR GO; GO:0006289; P:nucleotide-excision repair; IEA:HAMAP. DR GO; GO:0009432; P:SOS response; IEA:HAMAP. 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; 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; UvrB_C; 1. 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; Cytoplasm; DNA damage; DNA excision; DNA repair; KW Excision nuclease; Helicase; Hydrolase; Nucleotide-binding; KW SOS response. FT DOMAIN 26 181 Helicase ATP-binding (By similarity). FT DOMAIN 432 598 Helicase C-terminal (By similarity). FT DOMAIN 635 670 UVR (By similarity). FT NP_BIND 39 46 ATP (By similarity). FT MOTIF 92 115 Beta-hairpin (By similarity). SQ SEQUENCE 675 AA; 76639 MW; 4F58FAA7DD96A344 CRC64; MSKLFNLVSD YSPAGDQPTA IEQLMDGLDS GLAQQTLLGV TGSGKTFTIA NVIAQANRPT LIMAPNKTLA AQLYGEMRDF FPDNAVEYFV SYYDYYQPEA YVPTTDTFIE KDASVNAHIE QMRLSATKAL MERRDVIIIA SVSAIYGLGD PESYLKMMLH VRRGDVLDQR DILRRLAELQ YKRNDAVFER GTFRVRGEVI DIFPAESEKE AIRLELFDGE VEVISSFDPL TGAIIQRNLA RTTIYPKTHY VTPREKILDA IEGIKLELTQ RKQQLLDNNK LVEEQRISQR TQFDIEMMNE LGFCSGIENY SRYLSGRTEG EPPPTLFDYL PADGLLIIDE SHVTVSQIGA MFRGDRSRKE NLVEYGFRLP SALDNRPMKF EEFESLAPQT IYVSATPGNY EIEKSGGDIA EQVVRPTGLL DPEIEVRPVA TQVDDLLSEI HIRSAKQERV LVTTLTKRMS EDLTEYLTEH GVKVRYLHSD IDTVERVEII RDLRLGKFDV LVGINLLREG LDIPEVSLVA ILDADKEGFL RSERSLIQTM GRAARNIEGK AILYGDRITG SMERAINETQ RRREKQIIYN LEHNIIPQKL NKKIGDLLEL GAPSGRSKSR NKAADLHKVA ESKGTYSVLT PQQLELEIQR LEKQMYDFAQ NLEFEQAADT RDKIHQLRQQ FIANS //