ID   A0A1K1P172_9FLAO        Unreviewed;      1127 AA.
AC   A0A1K1P172;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   ORFNames=SAMN02927921_01539 {ECO:0000313|EMBL:SFW41316.1};
OS   Sinomicrobium oceani.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Sinomicrobium.
OX   NCBI_TaxID=1150368 {ECO:0000313|EMBL:SFW41316.1, ECO:0000313|Proteomes:UP000182248};
RN   [1] {ECO:0000313|EMBL:SFW41316.1, ECO:0000313|Proteomes:UP000182248}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.12145 {ECO:0000313|EMBL:SFW41316.1,
RC   ECO:0000313|Proteomes:UP000182248};
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; FPJE01000007; SFW41316.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1K1P172; -.
DR   STRING; 1150368.SAMN02927921_01539; -.
DR   Proteomes; UP000182248; 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   GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
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; 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; 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}; Exonuclease {ECO:0000313|EMBL:SFW41316.1};
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:0000313|EMBL:SFW41316.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000182248}.
FT   DOMAIN          68..553
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          554..810
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   REGION          935..960
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        943..960
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         89..96
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   1127 AA;  130527 MW;  E41B2B456F7CFCDB CRC64;
     MRNKFRYKLK QSIIINSKEL IKFVYFGIKF PYRKNPGFPD GFKRQKAARS TSLPKDPATL
     LSFVSCSGSE NYNYNYYILS DTTFQIYNAS AGSGKTFTLV REYLKLLLRS DYPDTYKQIL
     AITFTNKAVN EMKERVIRSL REMASEDILS SPTDMFLQLG KDLNTDSITL HNRSSNVLKR
     ILHNYAFFDI ATIDKFNHRL LRAFAHDLHL PVNFEVAIDT VSLLNEAVDR LVYQAGEDQL
     LTRVLVDFAL EKADDDKSWD ISLDLKKIAR LLLEENHYEH IRDIENKSLS DLRELANILQ
     KQISEDEDKM SETAATFFSI ITSNDLAPED FTRSSIPNFF QKARENILKS IDFQKKKWQD
     EIHSAALYTK TTEKKSPEKT VIIDEMQPRI ATLFEQCKRL FFHIQFLRNF RSKLIPLSLL
     SAINRELNHI KEAENLMPIS EFNRILAGVI TDQPAPFIYE RLGEKYRHYF IDEFQDTSEM
     QWKNLQPLIG NALEGETITG KRGSLMLVGD AKQAIYRWRG GKAEQFISLY NREDVPFQID
     PRVEQLPVNY RSYDEIIAFN NRFFKHAAAH LSHPEYRDLY ENKSYQETNP KKGGVVSITF
     LEKDSQDIRQ DYCDTTLQKI EALRDQGYTL SAICILTRKR DQGALLAEHL QENGIPVISS
     ESLLLKSHPK IVFLIHLMSY FLQTDNREIC LKLLEFLAES ENTEDKHLFF TSGLADMATV
     WETHNFSPDI FLERPLFDAV QYAISCFSLN DPSDAYLQSF LDEILEQVNR NHTGPAEFLS
     YWEKKKDTLG IAAPEGINAV QIMTIHKSKG LQFPIVLFPF ADTNIYEDRE PLIWFPVDRQ
     TFGIPYALIS KNKDLEYLSE YGAEMVQAYD AKLELDSFNI LYVALTRAVE QLHIIGKKDT
     DRNGNENTRS FSGLFINFLK AEGYWIEDQA TYQLPRGEHP DSIPGKSTTT KRSDNPKIPY
     TSNVSANRKF RIITRAGSLW SAGLDKAIET GNIYHMLLAR IRYATDVDHV VREAILQGHI
     THTEEDRFIE RLRTLTTHTE IGRYYTPDYT IYNERDIFTE KGEILRPDRI ATDNTGNAFL
     LDYKTGSYDT KYESQVRQYM QVLTDMGYKA TRGYLVFIDN DIRIYPV
//