ID   A2TX70_9FLAO            Unreviewed;      1041 AA.
AC   A2TX70;
DT   20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 2.
DT   27-MAR-2024, entry version 93.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   ORFNames=MED152_10775 {ECO:0000313|EMBL:EAQ43203.2};
OS   Polaribacter sp. MED152.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae.
OX   NCBI_TaxID=313598 {ECO:0000313|EMBL:EAQ43203.2, ECO:0000313|Proteomes:UP000006470};
RN   [1] {ECO:0000313|EMBL:EAQ43203.2, ECO:0000313|Proteomes:UP000006470}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MED152 {ECO:0000313|EMBL:EAQ43203.2};
RX   PubMed=17215843; DOI=10.1038/nature05381;
RA   Gomez-Consarnau L., Gonzalez J.M., Coll-Llado M., Gourdon P., Pascher T.,
RA   Neutze R., Pedros-Alio C., Pinhassi J.;
RT   "Light stimulates growth of proteorhodopsin-containing marine
RT   Flavobacteria.";
RL   Nature 445:210-213(2007).
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; CP004349; EAQ43203.2; -; Genomic_DNA.
DR   RefSeq; WP_015481893.1; NC_020830.1.
DR   AlphaFoldDB; A2TX70; -.
DR   STRING; 313598.MED152_10775; -.
DR   KEGG; pom:MED152_10775; -.
DR   eggNOG; COG1074; Bacteria.
DR   HOGENOM; CLU_010638_0_0_10; -.
DR   OrthoDB; 9810135at2; -.
DR   Proteomes; UP000006470; Chromosome.
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: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; 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};
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:UP000006470}.
FT   DOMAIN          1..465
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          466..729
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   BINDING         12..19
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   1041 AA;  120411 MW;  CCF3FFF4033C275F CRC64;
     MQKPEIFEVY NASAGSGKTF TLVKEYLKVL LSADDIFTFQ KILAITFTNK AAGEMKERVL
     SNLESFAEGE ENDLFTIISN EIAVDKETIQ VRSKKIIDVI LQNYSAFSIT TIDSFTHKII
     KSFAYDLGLS LNFEVEMDAV SLLNEAVDVL ISKIGTDKKL TKLLIDYSLD KIDDDKSWDI
     SRDLNEFAKV LLNEDDIHHF RELSKRKLED FTDLKSKLYA HQQELKTSFT KIGEACLELI
     HAKGLEQKDF MRGTIPKFFA DIKEKSVNFS FLTRSETIAK AIDNHQYYSK STTDAIAQDI
     ESIVPQIIAF YEQAKEIYSQ FLLNKLALKN LIPLAVLNNI NQELESIKDE SNIRLNSEFN
     QLISDNIKEQ PAPFIYERIG QRFQHYFIDE MQDTSVLQWQ NLIPLIDNAL AQENSNLLLV
     GDGKQAIYRW RGGKAEQFIS LGASEENPFS ISKEVKHLET NYRSFSEVIN FNNSFFQHTA
     NFLQNESYKS LFLEGNTQLE NKKKGGYVSL DFLEKEEEKE DEEIKYPKKV LAHILALKNE
     FALGEICVLT RTKKDGIAVA NYLSENEVPI VSSETLLLNT STKVNFIVDV LKVIQNPSDQ
     ETRFEMLYFL HQHLNISADK TSFLKKYVAL ENHEIFKELE QYNVVFDIGR FNQFPFYEKI
     EEIVRGFQLL ETSDAYVQFF LDIVLEQQRK STDINAFLDF WENKKDKLSI VAPESANAVQ
     VMTIHKSKGL EFPVVIFPCD VEIYREIKPK AWLNDLPESF GEFKELLLPF NKELGQVNAR
     GLQIYEQRRE ELELDNFNLL YVALTRAVEQ LYVITEKRIS AKGVENTNYY SGVFINYLIQ
     QNLWKDDCLH YSFGDKNRVS QLIESESVAE THQKFISTSW QEHNVVLLAS ASKLWNTAQG
     EAIDYGNLFH EILSKIFTKS DVAPILNQYH QQGFIDDEQK KYMFQKIIEI VAHPELRSFY
     AKDVIIYNER EIVDVDNQIV IPDRLIFKDD KVTIIDYKTG VASNNHKQQL LKYAQVLQSM
     NFSVHYKLLV YINENIEVVK V
//