ID J5GX88_9FIRM Unreviewed; 1147 AA.
AC J5GX88;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=HMPREF1140_1332 {ECO:0000313|EMBL:EJP23965.1};
OS Lachnoanaerobaculum sp. ICM7.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Lachnoanaerobaculum.
OX NCBI_TaxID=936594 {ECO:0000313|EMBL:EJP23965.1, ECO:0000313|Proteomes:UP000006599};
RN [1] {ECO:0000313|EMBL:EJP23965.1, ECO:0000313|Proteomes:UP000006599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICM7 {ECO:0000313|EMBL:EJP23965.1,
RC ECO:0000313|Proteomes:UP000006599};
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJP23965.1}.
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DR EMBL; ALJL01000015; EJP23965.1; -; Genomic_DNA.
DR RefSeq; WP_009662346.1; NZ_ALJL01000015.1.
DR AlphaFoldDB; J5GX88; -.
DR PATRIC; fig|936594.3.peg.443; -.
DR Proteomes; UP000006599; Unassembled WGS sequence.
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; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW 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, ECO:0000313|EMBL:EJP23965.1};
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}.
FT DOMAIN 1..458
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 481..771
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT COILED 62..89
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 21..28
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1147 AA; 131866 MW; A9DF7F97F0ACBDED CRC64;
MWTEAQQAAI DIKKGSILVS AAAGSGKTAV LVERIIKKIT DSKNPIDVDS LLVMTFTRAA
AASMKEKIYN ALLKEMEKHE NNSKEFKRLK EQSILLSSAK IMTTDSFCLS ILKENIDKLD
IDPAFSVADE SEISLLRADT MEELLESEYE LGSEDFIELS DAFANTKGDK SISEFIEKLY
RFAISKPWPE EWLNSLNEKG DEWQQYIFKE IIRSIDSILS DIEEIIEICN EDEGPVQYLD
NVLEEQSSIG NIKNAKDIFE LSEKLNNVSF GRLKSVKGGN EELKEKAKGL RDSYKKAISK
LSEEYCFDKK RLLEEEEKEK PKIRAIVDLT KKYIALFNEK KRDKNIVDFS DIEHMALRIL
LDENKNPTEI AKRYRKEFSE IYIDEYQDSN YLQEAIVEAI EKNNVFMVGD VKQSIYGFRQ
ASPGLFMDKY KRFTHFEKAD FDDETQKKVI LSKNFRSRSN VLSCANVIFK KIMKENTGGI
EYDDDAALYL GADFKEGKEY ISEIMLTQTS DIEDDTNAIE LEARAIAKRI KELKVELKVG
DGRDLRYSDI VILVRNNIGE SIAKVLNDEN IPAYAENNKG YFKTFEVRKI LAILAAIDNP
YSDVDLTAFL NSNLVGITDL ELANIVSAYR KSKNIEKSEK IRMMDAILYE GSESNIELET
REKIKNALEF LNRYRKKSAY MNIAALLQDI YNETDFLNLI AAMPGGQVRR ANLMLLINKA
KTFSNSGYSG LYNFIRYIAK LKDFDNDFGE ASILSENDDI VRIMTIHKSK GLEFPVCFLA
CAHKKFNKTD LRQGMVIDTD FGLGVQYVDS KNNIKDSSIK QNVIKHKLNV DLMGEELRVL
YVALTRAMEK MIISGSCNDA EKELEKMKES PSFLDIRTCN SYLDMILLGR DNVHFDIKTY
DYNMLLKEEV ETQKEVRDLN KVFEEPSTNE YDDLKNRLEY SYPYAENIDL KTKFSVSEIK
RMSQSEEFEV KENKKPTINA GNASERGNAY HKLMQKIHYE NIDKFSSRED FVREEISLLN
NHVYRELINP LDIVKFLDSK LGADFIKYND SLKRENQFIM GIPAKEAGMG ESDETILIQG
IIDAYIEKDD NIILVDYKTD NVRDAESLIK RYKTQLMLYK KSLEMSTGKT VNDIFIYSFA
LGKEIKI
//
