ID A0A0Q5V2G1_9FLAO Unreviewed; 1051 AA.
AC A0A0Q5V2G1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=ASG38_03035 {ECO:0000313|EMBL:KQS49970.1};
OS Flavobacterium sp. Leaf359.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1736351 {ECO:0000313|EMBL:KQS49970.1, ECO:0000313|Proteomes:UP000051024};
RN [1] {ECO:0000313|Proteomes:UP000051024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf359 {ECO:0000313|Proteomes:UP000051024};
RA Garrido-Oter R., Mueller D.B.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000051024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf359 {ECO:0000313|Proteomes:UP000051024};
RA Vorholt J.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQS49970.1}.
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DR EMBL; LMPW01000010; KQS49970.1; -; Genomic_DNA.
DR RefSeq; WP_056067601.1; NZ_LMPW01000010.1.
DR AlphaFoldDB; A0A0Q5V2G1; -.
DR STRING; 1736351.ASG38_03035; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000051024; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
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; 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; IPR011335; Restrct_endonuc-II-like.
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; 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:UP000051024}.
FT DOMAIN 1..465
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 496..739
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 11..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1051 AA; 120457 MW; A7C550364D82EE96 CRC64;
MQKTAFTLYD ASAGSGKTFT LVKEYLKILL TSPKNDAYRN ILAITFTNKA VGEMKSRIVS
SLSEFAKDEP GPKAVELMEV IQQETALNAI DIKIKARQII KNIIHNYASF DISTIDKFTH
KVIRAFAHDL GLPITFDVSL ETDNLLTEAV DAIIAQAGED ETLTRLLVDF TMEKTDDDKS
WDVTREILDT GKLLLNENNR NEIVHFQDKT ISEFVEIKKK IQQVVTDLDA ECAVLAQEAI
AVITAAGVDE KSFSGGYFPK HLQSIKEGRF NAKNKTYHQA EDIKINKTAK DKEIIEGIIP
ELLSLLKRVY KNQEKMAFYM AFLKNITPLS LLNTVSQELS KIQKEQNILS ISEFNAIIYK
EIQNQPAPFI YERLGEKYKH FFIDEFQDTS EMQWQNLIPL IDNALSSEDL QGERGSLMIV
GDPKQSIYRW RGGKAEQFIE LSKEHNPFNN PDKKIEHLDR NFRSYSEIIQ FNNGFFRMIS
EQFTNPDYKN LYENHSHQEH NSKIGGYINI SFLPKIEKTE GDDEETPDKT RQYVQATLVA
IKKSLAQGFE YKDIAILTRR RDQGIAVAGY LTEQGIPILS SETLMIENAT EVIFILNVLR
YLNNSSNLEA KAYLLQYIGE YVQKQLPVHD FIFQGMENRN EKEFENWLMS FDISLSFQEL
RRKSLYEAVE SIISKFINLK QNNAYIQYFL DLVLERDIKN QAGITDFLSY WEKNGHKFSI
PSPEGKNAVR ILTIHKSKGL EFPVVIFPFA EEDYSRRPKD KLWLDSEDNI SELPRVLIDN
SSAVEGFGEE ASLVYQQKKQ EDLLDNVNVL YVALTRAEEQ LYIISSMNLS AKGELPKNNM
ALFFINYLEK FVGFDIQKHE YEIGSPERIS HKSPIGEEAR KIPFVREVLD PKNIKIAQRE
SLMWGTHQQK AIEYGNIVHE ILSYIGTASD VGLALTKAIE NGLIVESQQD EVAKTISLIL
GHPELMDYFA EGNNVMNEQT IIRKEGTPIK PDRMVMAQDN KVYLLDYKTG SHNQKYLQQL
EAYEQAIEKM GYQVAKKALV YIGEEVNVVN L
//
