ID F7V5S4_CLOSS Unreviewed; 1211 AA.
AC F7V5S4;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN OrderedLocusNames=CXIVA_21360 {ECO:0000313|EMBL:BAK48103.1};
OS Clostridium sp. (strain SY8519).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1042156 {ECO:0000313|EMBL:BAK48103.1, ECO:0000313|Proteomes:UP000008937};
RN [1] {ECO:0000313|Proteomes:UP000008937}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SY8519 {ECO:0000313|Proteomes:UP000008937};
RX PubMed=21914882; DOI=10.1128/JB.05637-11;
RA Yokoyama S., Oshima K., Nomura I., Hattori M., Suzuki T.;
RT "Complete genomic sequence of the O-desmethylangolensin-producing bacterium
RT Clostridium rRNA cluster XIVa strain SY8519, isolated from adult human
RT intestine.";
RL J. Bacteriol. 193:5568-5569(2011).
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; AP012212; BAK48103.1; -; Genomic_DNA.
DR RefSeq; WP_013978060.1; NC_015737.1.
DR AlphaFoldDB; F7V5S4; -.
DR STRING; 1042156.CXIVA_21360; -.
DR KEGG; cls:CXIVA_21360; -.
DR eggNOG; COG1074; Bacteria.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000008937; Chromosome.
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:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0006302; P:double-strand break repair; IEA:InterPro.
DR Gene3D; 1.10.274.50; -; 1.
DR Gene3D; 3.90.320.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR InterPro; IPR014152; AddA.
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; IPR038726; PDDEXK_AddAB-type.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR NCBIfam; TIGR02785; addA_Gpos; 1.
DR PANTHER; PTHR11070:SF48; ATP-DEPENDENT HELICASE_NUCLEASE SUBUNIT A; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF12705; PDDEXK_1; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
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 4: Predicted;
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}; Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000008937}.
FT DOMAIN 3..469
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 470..788
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 24..31
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1211 AA; 140577 MW; 8EC55226FB9EBBC4 CRC64;
MGTEWTEEQR KVIDLRNRSM LVSAAAGSGK TAVLVERILS RVLDPEHPVD IDRILVVTFT
NAAAAQMRER ILRSMEQKLE EHPEDQRLRR QTTLIHNAHI ETIDSFCLQV VRSHFHRIDL
EPGFRIADQG EIKLIKGEVC DRVMEWFYAE KDPEFLTFAD NYSSAGKDEG IQNMILSLYE
YANSYPWPEE WLESCLQSGR ADTLEEMDEK PWMRQYIGFF RQMTEEYLQT IEQLLRICRE
PGGPDKYEAA LESDRTQLSE LLERSGYSAW QQGLKELTFA KLGRCGKETD PEWKDYVKNQ
RDAYKEDIRS HWKKYFAADP EEQKNILQDT AEMLQVLVRM TRSFAEEFTA VKRKKNILDF
SDMEHFALQI LLTEEEHQPT EIAREYQELF EEIMIDEYQD SNYVQEALLQ AVSRESDGEQ
NVFMVGDVKQ SIYRFRMARS ELFMEKYHTY QTANSPHQRI DLHKNFRSRP EVLDFANRIF
ARVMREDIGN ITYDREAALY PGGNFADDPA GNYDPEVILL EKQKGMDAAE SEARAAALKI
RQMVEEQVIE GLTYGDIVIL MRSPKKWAPI YQSVFADAGI PFLVTADSGY FSAREVQVLL
AYLKILDNPM QDIPLTVCMT GFFGKFSSDD LARIKAAYPY LTFAESVFAY GGRISDTLTS
RIPEELFLPA EEPDPELAAR IGIFLDTLEI YRSRVPDTPI HRLMEEIMRE TGYYQYQAAL
PAGRRRKANL DMLLEKAVAY EQTSYQGLMH FNRYIEELHK YEVDFGEAET AETHENAVHL
YSIHKSKGLE FPVVLLGQTG KKFNTNDQKG DLILHPEYGA ALRYRNRAEH RRRDTILKNA
LTLEEKRDSL GEELRILYVA LTRAEKKVIV MGTLEKLPDG ENEPDREEMG IFSGESQPLP
FAQRFSAVCY MEWVLGAIRG DASCHREIWK PEDLDQMEAR YRSAVSRESA RILEESYEGD
RTMMQELEHR FAWKYPWADR MLRRQKVSVS DLKHRAMAEQ MRAFSDVDEP ELLPQKEPEP
HIPAFIQASE ENGGALYGTA MHRLLECIDY TELPETGDLY AVLEAVEKQM ENLYEAGRID
AQIRARIDRK RAAAFFCTDL ARRMRRAQQK GCLHREQPFV MSIEAFRVWE EAETEETVLT
QGIIDAFWEE EDGIVLLDYK TDRVSDPEEL RQRYSTQLKL YQEAISRRYH GSAGVKETLI
YSFALQTVIP L
//
