UniProt: Q74CY7

Database: UniProt
Entry: Q74CY7_GEOSL

LinkDB:  Q74CY7_GEOSL 
Original site:  Q74CY7_GEOSL

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Ontology (9)   
   GO (9)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (2)   
   RefSeq(pep) (2)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (11)   
   InterPro (7)   
   Pfam (2)   
   PROSITE (2)   
Literature (1)   
   PubMed (1)   
All databases (26)   

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ID   Q74CY7_GEOSL            Unreviewed;      1204 AA.
AC   Q74CY7;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 134.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   Name=recB {ECO:0000313|EMBL:AAR34908.1};
GN   OrderedLocusNames=GSU1534 {ECO:0000313|EMBL:AAR34908.1};
OS   Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA).
OC   Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC   Geobacteraceae; Geobacter.
OX   NCBI_TaxID=243231 {ECO:0000313|EMBL:AAR34908.1, ECO:0000313|Proteomes:UP000000577};
RN   [1] {ECO:0000313|EMBL:AAR34908.1, ECO:0000313|Proteomes:UP000000577}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51573 / DSM 12127 / PCA
RC   {ECO:0000313|Proteomes:UP000000577};
RX   PubMed=14671304; DOI=10.1126/science.1088727;
RA   Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.,
RA   Heidelberg J.F., Wu D., Wu M., Ward N., Beanan M.J., Dodson R.J.,
RA   Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., Gwinn M.,
RA   Kolonay J.F., Sullivan S.A., Haft D.H., Selengut J., Davidsen T.M.,
RA   Zafar N., White O., Tran B., Romero C., Forberger H.A., Weidman J.,
RA   Khouri H., Feldblyum T.V., Utterback T.R., Van Aken S.E., Lovley D.R.,
RA   Fraser C.M.;
RT   "Genome of Geobacter sulfurreducens: metal reduction in subsurface
RT   environments.";
RL   Science 302:1967-1969(2003).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=5.6.2.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00034618};
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DR   EMBL; AE017180; AAR34908.1; -; Genomic_DNA.
DR   RefSeq; NP_952585.1; NC_002939.5.
DR   RefSeq; WP_010942181.1; NC_002939.5.
DR   AlphaFoldDB; Q74CY7; -.
DR   SMR; Q74CY7; -.
DR   STRING; 243231.GSU1534; -.
DR   EnsemblBacteria; AAR34908; AAR34908; GSU1534.
DR   KEGG; gsu:GSU1534; -.
DR   PATRIC; fig|243231.5.peg.1577; -.
DR   eggNOG; COG1074; Bacteria.
DR   HOGENOM; CLU_001114_6_1_7; -.
DR   InParanoid; Q74CY7; -.
DR   OrthoDB; 9810135at2; -.
DR   Proteomes; UP000000577; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0009338; C:exodeoxyribonuclease V complex; IBA:GO_Central.
DR   GO; GO:0043138; F:3'-5' DNA helicase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008854; F:exodeoxyribonuclease V activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000725; P:recombinational repair; IBA:GO_Central.
DR   CDD; cd22352; RecB_C-like; 1.
DR   Gene3D; 3.90.320.10; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 1.10.3170.10; Recbcd, chain B, domain 2; 1.
DR   HAMAP; MF_01485; RecB; 1.
DR   InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR   InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011604; PDDEXK-like_dom_sf.
DR   InterPro; IPR004586; RecB.
DR   InterPro; IPR011335; Restrct_endonuc-II-like.
DR   InterPro; IPR014016; UvrD-like_ATP-bd.
DR   NCBIfam; TIGR00609; recB; 1.
DR   PANTHER; PTHR11070:SF23; RECBCD ENZYME SUBUNIT RECB; 1.
DR   PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR   Pfam; PF00580; UvrD-helicase; 2.
DR   Pfam; PF13361; UvrD_C; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF52980; Restriction endonuclease-like; 1.
DR   PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR   PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}; DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}; Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000000577}.
FT   DOMAIN          1..446
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          473..745
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   REGION          923..956
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         22..29
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   1204 AA;  133252 MW;  64BDEC3DB00C585E CRC64;
     MTSLRPHDNL TVELSGHNLV EASAGTGKTF AIACLYLRLV VEGEGLLPDN ILVVTFTEAA
     TKELRARIRQ RLRQARDRFA GGGAPDEFLD RLALGERWPG HATALARIDS ALQTFDCAAI
     STIHGFCLRA LQENAFESGS LFDTELAADQ EPLLRQVADD FWRHHFFGAD APLLPLALGR
     RWSPEELAAF LRNIAGKPHL AVEPVWHSGE ADRVAGEIRD AFAALSSLWR TQRAEIAAIL
     AADPGLSRSR SNYHPDLVPG LLVAMDGYAA GADPYALFAG FDKFTTGFLA GQRLKKADPP
     RHDCFDLCDR LARLTSQRLL LLKAEFAARG RERLAALKAQ RNVRGYDDLL TDLHAALGGP
     GGAALADRLR ERYRAALIDE FQDTDQVQYR IFRAVFSGGA VPLFLIGDPK QAIYSFRGAD
     VFAYLEARQE IPAERRFTMD RNWRSTPEMV EAVSSLFRLG GEHPFLAGDI AFPPVTAARR
     QGCSFGDRDP APLQLWFFRR GESDRDCINL GTGRQRIVTA VADEISGLLA DGRAGTACLE
     DEDGRMQPLT PGDVAVIVRS HFEAGLVQQA LRERGIPSVV QSADSLFETR EAGEVWTVMG
     AVAEPGNEGR VRAALVTALF GLNGNDLALL MEQEAAWEAR IAAFRDYRDL WREQGFMTMF
     RALLDREGVR ERCLPLPDGE RRLTNLRHCA EVLHQAAVER RLGPDALTAW FGERVSVPPP
     GEDYQIRLES DDRAVRIVTV HVSKGLEYPV VFAPFMWGGL RDDGDLTLCH EEGYRLVADF
     GTDRRDERQR RARTEALAEN LRLLYVALTR ARCRAYLVWG KFRGAETSAP GWLLHGSRPD
     GGGDPVALLE GTLKKATDQT LLERLDHLAT ASGGGIAVTE DPCPDRLPRF RPAMGEAPLV
     CRDFRGDIDA GWRVASFTSF ASGHREPAEL PDRDQTPPEL PPDAASDTAA PPEGSMFAFP
     RGPRAGIFLH GLFEQLDFAV AGDDTVRDLV RRELERNGHG AQWLDPVSRM VGNVLNVPLG
     GEGNSFRLAD LAPGSWLAEL EFYFPLRFVR DAQVATILAG AGVLPQGADL GAVARRIAFG
     EARGMVRGFV DLVFRHSGRY YLIDWKSNHL GNRAEDYGPE RLCREMERSL YPLQYLLYTV
     ALNRFLERRL PGYRYEEHFG GVFYLFLRGI DPERPALGVY HDLPRPDLVR ALTDCLAGRE
     GGAP
//

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