ID A0A2H1E9J2_9FLAO Unreviewed; 698 AA.
AC A0A2H1E9J2;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=ATP-dependent DNA helicase RecG {ECO:0000256|ARBA:ARBA00017846, ECO:0000256|RuleBase:RU363016};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551, ECO:0000256|RuleBase:RU363016};
GN Name=recG {ECO:0000256|RuleBase:RU363016,
GN ECO:0000313|EMBL:SFZ82530.1};
GN ORFNames=MARIT_1633 {ECO:0000313|EMBL:SFZ82530.1};
OS Tenacibaculum maritimum NCIMB 2154.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Tenacibaculum.
OX NCBI_TaxID=1349785 {ECO:0000313|EMBL:SFZ82530.1, ECO:0000313|Proteomes:UP000231564};
RN [1] {ECO:0000313|EMBL:SFZ82530.1, ECO:0000313|Proteomes:UP000231564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCIMB 2154T {ECO:0000313|EMBL:SFZ82530.1};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Critical role in recombination and DNA repair. Helps process
CC Holliday junction intermediates to mature products by catalyzing branch
CC migration. Has a DNA unwinding activity characteristic of a DNA
CC helicase with a 3'- to 5'- polarity. Unwinds branched duplex DNA (Y-
CC DNA). {ECO:0000256|RuleBase:RU363016}.
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=3.6.4.12;
CC Evidence={ECO:0000256|RuleBase:RU363016};
CC -!- SIMILARITY: Belongs to the helicase family. RecG subfamily.
CC {ECO:0000256|ARBA:ARBA00007504, ECO:0000256|RuleBase:RU363016}.
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DR EMBL; LT634361; SFZ82530.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H1E9J2; -.
DR STRING; 1349785.GCA_000509405_00615; -.
DR KEGG; tmar:MARIT_1633; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000231564; Chromosome MARIT.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR CDD; cd17992; DEXHc_RecG; 1.
DR CDD; cd04488; RecG_wedge_OBF; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR004609; ATP-dep_DNA_helicase_RecG.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR047112; RecG/Mfd.
DR InterPro; IPR045562; RecG_dom3_C.
DR InterPro; IPR033454; RecG_wedge.
DR NCBIfam; TIGR00643; recG; 1.
DR PANTHER; PTHR47964; ATP-DEPENDENT DNA HELICASE HOMOLOG RECG, CHLOROPLASTIC; 1.
DR PANTHER; PTHR47964:SF1; ATP-DEPENDENT DNA HELICASE HOMOLOG RECG, CHLOROPLASTIC; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF19833; RecG_dom3_C; 1.
DR Pfam; PF17191; RecG_wedge; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363016};
KW DNA damage {ECO:0000256|RuleBase:RU363016};
KW DNA recombination {ECO:0000256|RuleBase:RU363016};
KW DNA repair {ECO:0000256|RuleBase:RU363016};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU363016};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363016};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363016};
KW Reference proteome {ECO:0000313|Proteomes:UP000231564}.
FT DOMAIN 282..444
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 463..630
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 698 AA; 79132 MW; 7A68434B0540170C CRC64;
MNLQKPITYI KGVTINRAEL LYTELGIKTA DDLLNFFPFR YIDKTKFYTI KELENNNSEV
QIVGKITGIK TVKQKKGSRL VATFSDATGT IDLVWFKGVK WIKDSLKINT LYVIYGKLNL
FGSRYSMPHP EMELVAEYKK KLQMAMQPVY PSTEKLTNKG VTNKVIRSLM QNLFQQTYAG
IAENLPAYLL EKEKLIDKKE ALLNIHFPKS QELLAKAQYR LKFEELFFIQ LQLLQKKLIR
KSKIKGYSFS EVGEKFNSFY KNYLPFDLTN AQKRVLKEIR KDVGSNAHMN RLLQGDVGSG
KTIVALLTML LALDNGFQAT IMAPTEILAI QHYNGIKELL EGMDISIELL TGSTRAKKRR
EIHGNLETGG LDILVGTHAL LEDKVRFHNL GIAIIDEQHR FGVAQRSKMW QKNELPPHIL
VMTATPIPRT LAMSVYGDLD ISVIDELPPG RKEIKTVHRY DSNRLAVFKF LKDEIAKGRQ
VYIVYPLIEE SEAMDYKDLM DGYESVAREF PPPHYQISIV HGKMKPADKE YEMNRFINGE
TQIMVATTVI EVGVNVPNAS VMVIESSERF GLSQLHQLRG RVGRGAKQSF CILLSSYKLS
SDGKTRLQTM VDTTDGFKIA EVDLKLRGPG NIMGTQQSGI LNLKIADVVK DTPILQSARK
VAIEILQKDP DLSDPENIPI AKTYTQLQKK SGLWSKIS
//
