(data stored in SCRATCH zone)

SWISSPROT: D5E9Y2_METMS

ID   D5E9Y2_METMS            Unreviewed;       658 AA.
AC   D5E9Y2;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   11-DEC-2019, entry version 63.
DE   RecName: Full=UvrABC system protein B {ECO:0000256|HAMAP-Rule:MF_00204, ECO:0000256|RuleBase:RU003587};
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   OrderedLocusNames=Mmah_0453 {ECO:0000313|EMBL:ADE35983.1};
OS   Methanohalophilus mahii (strain ATCC 35705 / DSM 5219 / SLP).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanohalophilus.
OX   NCBI_TaxID=547558 {ECO:0000313|EMBL:ADE35983.1, ECO:0000313|Proteomes:UP000001059};
RN   [1] {ECO:0000313|EMBL:ADE35983.1, ECO:0000313|Proteomes:UP000001059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35705 / DSM 5219 / SLP
RC   {ECO:0000313|Proteomes:UP000001059};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Lykidis A., Saunders E., Brettin T., Detter J.C., Han C., Land M.,
RA   Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA   Spring S., Schneider S., Schroeder M., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Methanohalophilus mahii DSM 5219.";
RL   Submitted (MAR-2010) 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 of 2
CC       UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of
CC       the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps
CC       around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB
CC       and probably causes local melting of the DNA helix, facilitating
CC       insertion of UvrB beta-hairpin between the DNA strands. Then UvrB
CC       probes one DNA strand for the presence of a lesion. If a lesion is
CC       found the UvrA subunits dissociate and the UvrB-DNA preincision complex
CC       is formed. This complex is subsequently bound by UvrC and the second
CC       UvrB is released. If no lesion is found, the DNA wraps around the other
CC       UvrB subunit that will check the other stand for damage.
CC       {ECO:0000256|HAMAP-Rule:MF_00204}.
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00204,
CC       ECO:0000256|RuleBase:RU003587}.
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   ---------------------------------------------------------------------------
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; CP001994; ADE35983.1; -; Genomic_DNA.
DR   RefSeq; WP_013036926.1; NC_014002.1.
DR   EnsemblBacteria; ADE35983; ADE35983; Mmah_0453.
DR   GeneID; 8982592; -.
DR   KEGG; mmh:Mmah_0453; -.
DR   eggNOG; arCOG04748; Archaea.
DR   eggNOG; COG0556; LUCA.
DR   HOGENOM; HOG000073580; -.
DR   KO; K03702; -.
DR   OMA; RYMHSEI; -.
DR   OrthoDB; 4923at2157; -.
DR   BioCyc; MMAH547558:G1GHT-452-MONOMER; -.
DR   Proteomes; UP000001059; Chromosome.
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:ATPase 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:0006289; P:nucleotide-excision repair; IEA:UniProtKB-UniRule.
DR   GO; GO:0009432; P:SOS response; IEA:UniProtKB-UniRule.
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; IPR036876; UVR_dom_sf.
DR   InterPro; IPR004807; UvrB.
DR   InterPro; IPR041471; UvrB_inter.
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   Pfam; PF17757; UvrB_inter; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF46600; SSF46600; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
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; D5E9Y2.
DR   SWISS-2DPAGE; D5E9Y2.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00204};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00204};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_00204,
KW   ECO:0000256|RuleBase:RU003587};
KW   DNA excision {ECO:0000256|HAMAP-Rule:MF_00204,
KW   ECO:0000256|RuleBase:RU003587};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_00204,
KW   ECO:0000256|RuleBase:RU003587};
KW   Excision nuclease {ECO:0000256|HAMAP-Rule:MF_00204,
KW   ECO:0000256|RuleBase:RU003587};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00204};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001059};
KW   SOS response {ECO:0000256|HAMAP-Rule:MF_00204,
KW   ECO:0000256|RuleBase:RU003587}.
FT   DOMAIN          25..181
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          431..593
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          620..655
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   NP_BIND         38..45
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00204"
FT   COILED          265..285
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          616..643
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOTIF           91..114
FT                   /note="Beta-hairpin"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00204"
SQ   SEQUENCE   658 AA;  75431 MW;  648347FBB05B7868 CRC64;
     MPEFELVSNY SPRGDQPQAI DNLSNGINGG FRHQTLLGVT GSGKTFTMAN VIQNVQRPTL
     VIAHNKTLAA QLFSEFRDFF PDNAVEYFVS YYDYYQPEAY LPTTDTYIEK DSSINEEIDR
     LRLSATKSLM ERRDVIVVSS VSCIYNLGSP KEWQEMSLFL KPGDEVDRSW IFGKLVDIQY
     ERNDVEFTQG TFRARGDTVE IFPAQDNVAV RVEMFGDEID RISYFEPLTG KVVREVEDDM
     QVVIYPAKHF VMPQSQIDRA LVSIEEELKD TVAEFEKQGQ LLEAQRIMQR TRFDIEMIEE
     LGYCSGIENY SRHFDGRKPG EAPSSLLDFF PDDYLLIIDE SHVTIPQIGG MHNGDRARKK
     SLIEYGFRLP SAFDNRPLNY REFEERINQA VYVSATPADY ELGLSDQVVE QIIRPTGLVD
     PPVQVRPVAN QIDDLMEEVR KVSERGYRTL VTTLTKKMAE DLTDYLLEMG IRVRYMHSDI
     DTLERAEIVR ELRKGTFDVL VGINLLREGL DIPEVALVAI LDADKEGFLR SERSLIQTIG
     RASRNVDAYA IMYADRITGS MSRAMSEMER RRNIQLEFNR KHNITPTSIM KEIQREIVEV
     EEVSTPAAGV DMGLSKMEAN SMLIDLEAEM HEAARNLEFE EAARLRDAIR EMRETYSL
//

If you have problems or comments...

PBIL Back to PBIL home page