ID A0A2N4S8U2_9BACT Unreviewed; 1083 AA.
AC A0A2N4S8U2;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=C0T31_05065 {ECO:0000313|EMBL:PLB86504.1};
OS Dysgonamonadaceae bacterium.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Dysgonomonadaceae.
OX NCBI_TaxID=2065189 {ECO:0000313|EMBL:PLB86504.1, ECO:0000313|Proteomes:UP000234415};
RN [1] {ECO:0000313|EMBL:PLB86504.1, ECO:0000313|Proteomes:UP000234415}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XHS2771 {ECO:0000313|EMBL:PLB86504.1,
RC ECO:0000313|Proteomes:UP000234415};
RA Vasudevan G., Joshi A.J., Hivarkar S., Lanjekar V.B., Engineer A.S.,
RA Dhakephalkar P.K., Dagar S.;
RT "Anaerobic cellulose degrading bacterium isolated from hot springs that can
RT be used for biotechnological applications.";
RL Submitted (DEC-2017) 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:PLB86504.1}.
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DR EMBL; PKMK01000010; PLB86504.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N4S8U2; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000234415; 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:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR Gene3D; 3.90.320.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR Gene3D; 1.10.3170.10; Recbcd, chain B, domain 2; 1.
DR InterPro; IPR022765; Dna2/Cas4_DUF83.
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; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070:SF64; ATP-DEPENDENT DNA HELICASE REP; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF01930; Cas_Cas4; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 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:UP000234415}.
FT DOMAIN 1..470
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 502..761
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT COILED 211..238
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 17..24
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1083 AA; 124984 MW; 4A51629D7860D93E CRC64;
MPNHALSENE VLHIYKASAG SGKTHRLTGE YLRLLYRGEN NYKHILAVTF TNKATDEMKS
RIVKELYHLA TNRKSGYLDD LMKEFEMDET SIRLKAKNLL ETILHDYSAF SVSTIDRFFQ
QTIRAFTREI GLAGNYNIEL DQTAMLNEAI DLLISELDKA ENKPVADWLL SMMKSQIGDN
KSWNIRKILQ DFGKQMFKEN VRVLAKEGFS TIQDKEKLES YRKKLERIKN EYLNSLKTIG
KEALVIMQRH GVAYDDMKYG KNSGFLIFSK LANGELSKPS SRLENAANNV DNWTKDDNPK
ASQIRAAYAD GLNDCLNRII ALSKDDLFYN TANSILENYY ALGILSDIEK RLRSLQQETD
TLFLSDTTEL LNHLISESDS PFIYEKTGTR LLHFMIDEFQ DTSPLQWNNF LPLVRESLAS
NHFNLIVGDV KQSIYRFRNG DWRLLEDQIN QDFQPSQINH HALDINWRSE QCIVEFNNSL
FIQVPRLLQD VYNGPLATDD ESQFAKYARS KIIDIYAQAY QCIPDKKKTA QGYVKMTFLR
NEKGDDWKSE SLKRLPLDLE SLQDRGFSLS QIAILVRSNK DAVLVAESLL NYKREHSESK
YRYDIISNEA LLVANAQSVK AAIAILKHFQ NPADATRRMM AIYELLRFHR AMAPGEALAF
CTDPANAEAL AEMEVQLTHI SQLPLYESVE AFFAMSSQFM NENENAFVQA FLDVVLKFSA
DSSSDLNSFL EWWEEQSQSL TLFSPDGQDA IRLITIHKSK GLEFDVVLMP FVDWEVDHSA
GHAEFVWCKP DREPFNELAI VPVKYKKDMA NTIFRDDYLR EKLLSYIDNL NLLYVAFTRP
KQQLICYSPK GKDNITRISD LIYRAVSEPL ALSDSIKSDI DLKKYYFEND DESVFEYGIP
SKIESGNQSN SIDTCKMNEW RSIPFEGRLK LRLNSIGYFN DDGSRARGTL MHEIVSSIKT
VDDLSVALQR RVMEGELSET ERSEIFDEIT EMLSLPEVVD WYSGKYIVLN EVQTLDPERG
FSRPDRIMID GDKAIVVDYK FGETEDPKYR RQVQHYVRLL QKMDFSDVKG YIYYVKLKKI
EQI
//
