(data stored in SCRATCH zone)

SWISSPROT: C1AT20_RHOOB

ID   C1AT20_RHOOB            Unreviewed;       720 AA.
AC   C1AT20;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   07-JUN-2017, entry version 70.
DE   RecName: Full=UvrABC system protein B {ECO:0000256|HAMAP-Rule:MF_00204, ECO:0000256|RuleBase:RU003587, ECO:0000256|SAAS:SAAS00632035};
DE            Short=Protein UvrB {ECO:0000256|HAMAP-Rule:MF_00204};
DE   AltName: Full=Excinuclease ABC subunit B {ECO:0000256|HAMAP-Rule:MF_00204};
GN   Name=uvrB {ECO:0000256|HAMAP-Rule:MF_00204,
GN   ECO:0000313|EMBL:BAH48952.1};
GN   OrderedLocusNames=ROP_07050 {ECO:0000313|EMBL:BAH48952.1};
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH48952.1, ECO:0000313|Proteomes:UP000002212};
RN   [1] {ECO:0000313|EMBL:BAH48952.1, ECO:0000313|Proteomes:UP000002212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:BAH48952.1,
RC   ECO:0000313|Proteomes:UP000002212};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus
RT   erythropolis PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) 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. {ECO:0000256|HAMAP-
CC       Rule:MF_00204, ECO:0000256|SAAS:SAAS00632042}.
CC   -!- SUBUNIT: Forms a heterotetramer with UvrA during the search for
CC       lesions. Interacts with UvrC in an incision complex.
CC       {ECO:0000256|HAMAP-Rule:MF_00204, ECO:0000256|RuleBase:RU003587,
CC       ECO:0000256|SAAS:SAAS00632049}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00204,
CC       ECO:0000256|RuleBase:RU003587, ECO:0000256|SAAS:SAAS00632032}.
CC   -!- DOMAIN: The beta-hairpin motif is involved in DNA binding.
CC       {ECO:0000256|HAMAP-Rule:MF_00204}.
CC   -!- SIMILARITY: Belongs to the UvrB family. {ECO:0000256|HAMAP-
CC       Rule:MF_00204, ECO:0000256|RuleBase:RU003587,
CC       ECO:0000256|SAAS:SAAS00632074}.
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DR   EMBL; AP011115; BAH48952.1; -; Genomic_DNA.
DR   RefSeq; WP_012687952.1; NC_012522.1.
DR   STRING; 632772.ROP_07050; -.
DR   EnsemblBacteria; BAH48952; BAH48952; ROP_07050.
DR   KEGG; rop:ROP_07050; -.
DR   PATRIC; fig|632772.20.peg.766; -.
DR   eggNOG; ENOG4105CCW; Bacteria.
DR   eggNOG; COG0556; LUCA.
DR   HOGENOM; HOG000073580; -.
DR   KO; K03702; -.
DR   OMA; RYMHSEI; -.
DR   OrthoDB; POG091H02LK; -.
DR   Proteomes; UP000002212; Chromosome.
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:0006289; P:nucleotide-excision repair; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009432; P:SOS response; IEA:UniProtKB-HAMAP.
DR   Gene3D; 4.10.860.10; -; 1.
DR   HAMAP; MF_00204; UvrB; 1.
DR   InterPro; IPR006935; Helicase/UvrB_N.
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;
DR   PRODOM; C1AT20.
DR   SWISS-2DPAGE; C1AT20.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00204,
KW   ECO:0000256|SAAS:SAAS00632044}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002212};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00204,
KW   ECO:0000256|SAAS:SAAS00632071};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_00204,
KW   ECO:0000256|RuleBase:RU003587, ECO:0000256|SAAS:SAAS00632043};
KW   DNA excision {ECO:0000256|HAMAP-Rule:MF_00204,
KW   ECO:0000256|RuleBase:RU003587, ECO:0000256|SAAS:SAAS00632054};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_00204,
KW   ECO:0000256|RuleBase:RU003587, ECO:0000256|SAAS:SAAS00632038};
KW   Excision nuclease {ECO:0000256|HAMAP-Rule:MF_00204,
KW   ECO:0000256|RuleBase:RU003587, ECO:0000256|SAAS:SAAS00632031};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00204,
KW   ECO:0000256|SAAS:SAAS00632060};
KW   SOS response {ECO:0000256|HAMAP-Rule:MF_00204,
KW   ECO:0000256|RuleBase:RU003587, ECO:0000256|SAAS:SAAS00632076}.
FT   DOMAIN       49    184       Helicase ATP-binding.
FT                                {ECO:0000259|PROSITE:PS51192}.
FT   DOMAIN      453    619       Helicase C-terminal.
FT                                {ECO:0000259|PROSITE:PS51194}.
FT   DOMAIN      675    710       UVR. {ECO:0000259|PROSITE:PS50151}.
FT   NP_BIND      62     69       ATP. {ECO:0000256|HAMAP-Rule:MF_00204}.
FT   COILED      279    313       {ECO:0000256|SAM:Coils}.
FT   MOTIF       115    138       Beta-hairpin. {ECO:0000256|HAMAP-Rule:
FT                                MF_00204}.
SQ   SEQUENCE   720 AA;  80860 MW;  63BC1981D9B09178 CRC64;
     MAFASEHPVV AHSEFRPIGE IERSEARFEV VSDHKPAGDQ PTAIADLERR INAGEKDVVL
     LGATGTGKSA TTAWLIEKVQ RPTLVMAPNK TLAAQLANEL RDMLPNNSVE YFVSYYDYYQ
     PEAYIAQTDT YIEKDSSIND DVERLRHSAT SSLLSRRDVV VVASVSCIYG LGTPQSYLDR
     SVQLEVGVEV PRDALLRLLV DVQYTRNDLA FTRGSFRVRG DTVEIIPSYE ELAVRIEFFG
     DEIEALYYLH PLTGDVVRKV DSVRIFPATH YVAGPERMER AVKDIEAELE ERLADLENKG
     KLLEAQRLRM RTQYDLEMIK QVGFCSGIEN YSRHIDGRGP GTAPATLIDY FPEDFLLVID
     ESHVTVPQIG AMYEGDMSRK RNLVEFGFRL PSATDNRPLT WEEFTQRIGQ TVYLSATPGK
     YELGQAGGEF VEQVIRPTGL VDPEVVVKPT KGQIDDLVHE IRERADRDER VLVTTLTKKM
     AEDLTDYLLE LGIRVRYLHS DIDTLRRVEL LRQLRLGEYD VLVGINLLRE GLDLPEVSLV
     AILDADKEGF LRSSTSLIQT IGRAARNVSG QVHMYADKIT DSMQHAIEET ERRREKQIAY
     NEKMGVDPQP LRKKIADILD QVYEEAEDTA SGVDVGGSGR NATRGRRAQG EAGRSVSAGV
     YEGRDTKSMP RAELADLVKE LTDQMMNAAR DLQFELAGRL RDEIADLKKE LRGMDAAGLK
//

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