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Database: UniProt
Entry: A0A2W1MYW8_9FLAO
LinkDB: A0A2W1MYW8_9FLAO
Original site: A0A2W1MYW8_9FLAO 
ID   A0A2W1MYW8_9FLAO        Unreviewed;      1037 AA.
AC   A0A2W1MYW8;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   ORFNames=DNU06_12835 {ECO:0000313|EMBL:PZE16430.1};
OS   Putridiphycobacter roseus.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Crocinitomicaceae; Putridiphycobacter.
OX   NCBI_TaxID=2219161 {ECO:0000313|EMBL:PZE16430.1, ECO:0000313|Proteomes:UP000249248};
RN   [1] {ECO:0000313|EMBL:PZE16430.1, ECO:0000313|Proteomes:UP000249248}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM1701 {ECO:0000313|EMBL:PZE16430.1,
RC   ECO:0000313|Proteomes:UP000249248};
RA   Zhang X.;
RT   "The draft genome sequence of Crocinitomix sp. SM1701.";
RL   Submitted (JUN-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:PZE16430.1}.
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DR   EMBL; QKSB01000008; PZE16430.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2W1MYW8; -.
DR   OrthoDB; 9810135at2; -.
DR   Proteomes; UP000249248; 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:InterPro.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
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:SF64; ATP-DEPENDENT DNA HELICASE REP; 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};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000249248}.
FT   DOMAIN          1..488
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          489..743
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   1037 AA;  119070 MW;  262226DC439E7BB9 CRC64;
     MQTQVQPLKI YNASAGSGKT YTLVQDYLKI VLHHKDPLKF RSILAMTFTN KAANEMKERV
     LSALIDLSKT NHLKTPEQLD FLENTAKNIK LAPDIIEIRA KAILNKILHN YSSFSVMTID
     KFTHKIIRTF AKDLDISIDF NVEMDTTGFL QSITDLLMDE IGRNQKLTGL LLRYTNHNLD
     NERSWNIKRD IYEFTTLLLK EDALEAIEHL KDLNEEDFIS IGENLKKENA IILQELTSTA
     EAAIHLIKSY HLEDEDFASK SNGVYGFFKR TLSRVDALSK MTPPSKTILK YTESNEFSHK
     KSPHKATIDS ISDLLGKYVL QLNQIITVSV PQLKLNKEIN KNLNNLAILK YILALIEKVK
     ADENILLLSD FYKEIAAIIT RERVPFIYER LGIRYQHFLL DEFQDTSQMQ WVNLIPLVHN
     SLAQQHENLI VGDGKQAIYR WRNGEVEQFT KLPGEIHNPK GIPSLKEAEN LFSVMGRKEN
     LESNYRSSAE IVNFNNTFFT ELSQQISAPL AYIYDGLNQA VTKKFKGYVE ATFFTDNDED
     AQLENVLNTV KKAVNAGFSF SDICIITRNN RNGANIANYL TDHDYPVISP DSLFIGKDKY
     VQFLHYLMQS LTNFNDKNAQ VKTIEHYCEI TAAVVPDFII DKSLPFPSLE NYFEAFGIHV
     LAPEHFQNIY EYVEFLLETF DIDATDNVYL QFFMESIHQF EVNKNVNIRA FLDWFKDKGK
     EKSIISPEGS NAISIMTIHK SKGLQFPVVI CPLFNWSPKL DRQQIWVIAP GERLPAYFVK
     TTKYLAETPL KDLYEIEKAK FELDTINMLY VAFTRPEIAL FITGDMSSTV VKNQIEPLVK
     NMPDFSLIGD TYRYGELINY KPAKKVSKEK FEIQFLKQKM NKPSLSYKSA LEWDIESLDE
     KRNFGTMVHH VLSILKTPQE LPSKLKELAI KQGLTNKEVI ALEQYISPLF KNERFAAYFT
     PEAMNETALI DNHGMKFIPD KIIQTATEVL VVDFKTGQNS PAHLKQVGQY IKLLKDMGHD
     NVNGELCYTE GMTFITV
//
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