ID   A6VVA5_MARMS            Unreviewed;       651 AA.
AC   A6VVA5;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 99.
DE   SubName: Full=ATP-dependent DNA helicase, RecQ family {ECO:0000313|EMBL:ABR70384.1};
GN   OrderedLocusNames=Mmwyl1_1455 {ECO:0000313|EMBL:ABR70384.1};
OS   Marinomonas sp. (strain MWYL1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinomonas.
OX   NCBI_TaxID=400668 {ECO:0000313|EMBL:ABR70384.1};
RN   [1] {ECO:0000313|EMBL:ABR70384.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MWYL1 {ECO:0000313|EMBL:ABR70384.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Johnston A.W.B., Todd J.D., Rogers R., Wexler M., Bond P.L., Li Y.,
RA   Richardson P.;
RT   "Complete sequence of Marinomonas sp. MWYL1.";
RL   Submitted (JUN-2007) 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=3.6.4.12;
CC         Evidence={ECO:0000256|ARBA:ARBA00001665};
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DR   EMBL; CP000749; ABR70384.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6VVA5; -.
DR   STRING; 400668.Mmwyl1_1455; -.
DR   KEGG; mmw:Mmwyl1_1455; -.
DR   eggNOG; COG0514; Bacteria.
DR   HOGENOM; CLU_001103_9_2_6; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR   CDD; cd18018; DEXHc_RecQ4-like; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR032284; RecQ_Zn-bd.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   NCBIfam; TIGR00614; recQ_fam; 1.
DR   PANTHER; PTHR13710:SF105; BLOOM SYNDROME PROTEIN; 1.
DR   PANTHER; PTHR13710; DNA HELICASE RECQ FAMILY MEMBER; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF16124; RecQ_Zn_bind; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:ABR70384.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          30..198
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          224..367
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   651 AA;  73364 MW;  89BAF714C4CDDA1E CRC64;
     MMPSNTAHLE HSLHSLFGFD QFREGQQQTI EQLLTGHSSL AVFPTGSGKS LCYQFTATQL
     PNLTLVISPL IALMHDQLAF LTAKGIPAAC LDSSQSKDES QAVMSGVQSG AIKILMISVE
     RFKNERFRRF IKRVPISMLV VDEAHCISEW GHNFRPDYLK LPSYQQELAI PLVLLLTATA
     TRRVQRDMAQ KFAIYPEHIV QTGFYRHNLD IDLIPIQRHE KLSTLKNVLN DTQGASIVYV
     TQQKTAEDVA RALQADGYSA VAYHAGLNSD IRSAIQADFM NSKTRIIVAT IAFGMGIDKS
     DIRLVVHFDL PKSIENYSQE IGRAGRDNQP SRCVMLASLE GLSTLENFVY GDTPEPQDID
     TLLRCITEQT VEYEWETQLY GLSNLTNIRS LPLKTLLVQL ELFGALTPKY SFYADIKIKW
     EGDRIAFANQ IPTEWQAAYQ AILKGIQYKK IWGTPDFDKL FNEAGLSRGD VLQVLEFAAD
     HNVLTLESKG LTEVYQVHSE HFHHQTLANQ LHQYVEEKQS AEVARIATMI RFFQLDRCLN
     NNLARYFGDQ NSPEHCGHCS VCRGKILVFS QQADLDSDVS WQDNLAEYAR EFAQHVGNKS
     PATQVTAILI TRFLTGLTQP IFTKIKARQL SGFGAYEEKS YLSVLKAIQD L
//