UniProt: A0A1M5DBG6

Database: UniProt
Entry: A0A1M5DBG6_9FLAO

LinkDB:  A0A1M5DBG6_9FLAO 
Original site:  A0A1M5DBG6_9FLAO

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Ontology (4)   
   GO (4)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (11)   
   InterPro (6)   
   Pfam (3)   
   PROSITE (2)   
All databases (18)   

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ID   A0A1M5DBG6_9FLAO        Unreviewed;      1042 AA.
AC   A0A1M5DBG6;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   ORFNames=SAMN05444344_0951 {ECO:0000313|EMBL:SHF64280.1};
OS   Tenacibaculum mesophilum.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Tenacibaculum.
OX   NCBI_TaxID=104268 {ECO:0000313|EMBL:SHF64280.1, ECO:0000313|Proteomes:UP000183998};
RN   [1] {ECO:0000313|EMBL:SHF64280.1, ECO:0000313|Proteomes:UP000183998}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13764 {ECO:0000313|EMBL:SHF64280.1,
RC   ECO:0000313|Proteomes:UP000183998};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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};
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DR   EMBL; FQVV01000001; SHF64280.1; -; Genomic_DNA.
DR   RefSeq; WP_073182201.1; NZ_FQVV01000001.1.
DR   AlphaFoldDB; A0A1M5DBG6; -.
DR   STRING; 104268.SAMN05444344_0951; -.
DR   OrthoDB; 9810135at2; -.
DR   Proteomes; UP000183998; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR   GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
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; IPR038726; PDDEXK_AddAB-type.
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; PF12705; PDDEXK_1; 1.
DR   Pfam; PF00580; UvrD-helicase; 1.
DR   Pfam; PF13361; UvrD_C; 2.
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}; DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000313|EMBL:SHF64280.1};
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..465
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          478..729
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   BINDING         13..20
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   1042 AA;  120888 MW;  5652CA638ACC6CFA CRC64;
     MLENPSTFQV YNASAGSGKT FTLVKEYLKV LLQSEDIFRF QKILAITFTN KAAGEMKERV
     LNNLQAFAEG EANDLLEIII EETSLDRSVV KDRSKKILNE ILRNYSAFSI TTIDSFTHKI
     IKSFAYDLGL PLNFEVEMDA VSLLNEAVDV LISKIGSDEA LTKLLIDFSL DKADDDKSWD
     ISRELNEFAK ILLNEDDTKH FKNLADNELA DFTNLKTKLS KHQTQIKKRW KEIGEEALQA
     IQSVQLDHKD FYRSMLPNHF VALSKNPEKA KFFDQSKLRE RIEEGNFYSK SKSEDIKSAI
     EGVLPKLLSL YTESEKLYQQ FSMNKLALKS IIPLAVLNNI NQELTHLKEE NNLRLNAEFN
     HLISENIKDQ PAPFIYERIG QRFMHYFIDE MQDTSTLQWQ NLIPLIDNAL AQESSNLLLV
     GDGKQAIYRW RGGKSEQFIG LGSEKDNPFQ ISKEVRTLET NFRSYAEVIN FNNQFFQHTA
     NFLQNESYKQ LFIEGNKQLT TAKKGGYVSL SFLRKEENKE EEGIKYPKKV LELVKNLEAD
     FTLNEICILV RKKKDGIAVA NYLSENGIDI VSSETLLLEN SSKVNFIVNV LQVIQHPNDK
     ETCLEMLYFL QEHLKVAKDK HLFIDSLIQQ PNEKLFLELK EYGTSFDLST FHQLPFYEKI
     EEIIRSFQLI ASSDAYVQFF LDVVLEQQRK GTSIQEFLDY WSEKKDKLSI VAPESGNAVQ
     VMTIHKSKGL EFPVVIFPYD LDIYRQVNPK VWLNELPENY DKFKELLVPF NKELNYVNDR
     GFEIYEQQRE ELELDNFNLL YVALTRAVEQ LYIVTENKIS SKGEENTNFY SGVFINYLKK
     VGEWNDEVLE YSFGNKERVS ILKEKASGVQ IQECFISTPW KEHNIHMLAS ASKLWDTEQG
     KAIEFGNLVH EMMAEIKTKE DVEKVVYRYE QQGVLPREKS SEVIKNIQQI ANHSELKEYF
     SEEVVVFNER EIVDIDGQIV IPDRLVFYSK DEVVIIDYKT GKPSKAYHQQ LLRYGRVLQA
     LNFKVLKKLL VYIDEEILVE EV
//

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