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Database: UniProt
Entry: A0A3M9MQP4_9BACT
LinkDB: A0A3M9MQP4_9BACT
Original site: A0A3M9MQP4_9BACT 
ID   A0A3M9MQP4_9BACT        Unreviewed;      1121 AA.
AC   A0A3M9MQP4;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   ORFNames=EFA69_15435 {ECO:0000313|EMBL:RNI27517.1};
OS   Rufibacter immobilis.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Rufibacter.
OX   NCBI_TaxID=1348778 {ECO:0000313|EMBL:RNI27517.1, ECO:0000313|Proteomes:UP000271010};
RN   [1] {ECO:0000313|EMBL:RNI27517.1, ECO:0000313|Proteomes:UP000271010}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCC P1 {ECO:0000313|EMBL:RNI27517.1,
RC   ECO:0000313|Proteomes:UP000271010};
RA   Yang Y.;
RT   "Rufibacter latericius sp. nov., isolated from water in Baiyang Lake.";
RL   Submitted (NOV-2018) 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:RNI27517.1}.
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DR   EMBL; RJJE01000017; RNI27517.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M9MQP4; -.
DR   OrthoDB; 9810135at2; -.
DR   Proteomes; UP000271010; 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   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; IPR014016; UvrD-like_ATP-bd.
DR   PANTHER; PTHR11070:SF67; DNA HELICASE; 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   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   Helicase {ECO:0000256|PROSITE-ProRule:PRU00560};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00560};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}.
FT   DOMAIN          1..501
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          543..800
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   COILED          232..259
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         10..17
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   1121 AA;  129125 MW;  BB24CC38C493EBED CRC64;
     MPASFKIYSS SAGSGKTYHL TKEYLKLALQ SEEPSYYKNI LAITFTNDAA QEMKTRILGA
     LRGFNDTALP EKEKRNSDQL LFYILQEIRT EYGQSDLTEE GLRARASKVF DHLLFHYSEF
     AVSTIDSFVN KVVSAFTTEL KLPHNFEVDM DAQTLLSTAV SLLLNKVNTQ AENRLLAETL
     QQYALDKAEE GKSWNVLPDE LADFARNLLN EQTYEHLLDI GKLTLQDFKK IRSELYSQKV
     NVEKQIQTLA QEASDLIDRH GIMPEEMSYG KNGIYSYFRK WNSGFDITIA NSNAAKTVND
     DKWASAKAST GAKVALDQIK PRLAEIYRGI EDLKERETQN HILISAMLPH LYKLSVLSEL
     DRCIQEIKLD KNLVHISEFN KRITEIVLQE PIPFIYERLG ERYQHILIDE FQDTSVLQWN
     NLLPLVENAL AGDNFNMVVG DAKQAIYGWR GGEMEQILHL HRNQTHHLYQ NSRFEENVAP
     RYDTLRWTLS PDNLNTNYRS APEIIQFNNE LFGFISQSNP QFPLLQAIYD DKFQQESPAG
     KESGKAHLQV LFTQDEVPPF KVDLDACRQT EEIYEGYAEE DLLSYQESTL QLVLQMVQQA
     QADGYAPRDI AILSRTNRNS KLVANFLKQK KYDIISQDSL SLQFAEVINL IIAFFRILNQ
     PTNSLARSQA LYLVYKVVHQ ELPDSATTGK IAALAVEPSI DPFFQFLQQQ GFDLAYRDAG
     NLSIYELTEK LIRVFDLLDK NNECEYLFRF LDLVLEYTLK YSNNLNNFLQ YWDLHKENLS
     INTPKDRDAI TITSIHKSKG LDYPVVIVPF CDWSLEPQTS SLLWGTLPES VAAGGKLRTA
     VVNLNKKLEQ TALADQYAQK LEKTFIESLN MLYVALTRPV DRLYLIGKAQ DFRKGGAQKN
     VSFWLHKYLE SKALWQEGQF CYQLAKGAPQ AVSHKAVSED VYVLDKFTSA DWAQNLKLKQ
     HANNVFDFET QQEHRRWNRK LHYALARITY ADDAPKALRQ LVHQGIISQR ELPTLTQMVD
     HVLTHPQMQR YFSRAVTVEN EREVLDVRTN RYKPDRIVFG ETGEVTLIDY KLPPAKEEYV
     ENLNSYAALF RELMMSRITC VVYYFEEERV EEWEFVGEVA G
//
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