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Database: UniProt
Entry: A0A2G1XYC4_9GAMM
LinkDB: A0A2G1XYC4_9GAMM
Original site: A0A2G1XYC4_9GAMM 
ID   A0A2G1XYC4_9GAMM        Unreviewed;       722 AA.
AC   A0A2G1XYC4;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
DE   AltName: Full=DNA 3'-5' helicase II {ECO:0000256|ARBA:ARBA00034923};
GN   ORFNames=COA29_04330 {ECO:0000313|EMBL:PHQ56304.1};
OS   Porticoccus sp.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Porticoccaceae; Porticoccus.
OX   NCBI_TaxID=2024853 {ECO:0000313|EMBL:PHQ56304.1, ECO:0000313|Proteomes:UP000226842};
RN   [1] {ECO:0000313|Proteomes:UP000226842}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Tully B.J., Wheat C.G., Glazer B.T., Huber J.A.;
RT   "A dynamic microbial community with high functional redundancy inhabits the
RT   cold, oxic subseafloor aquifer.";
RL   Submitted (AUG-2017) 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   -!- CATALYTIC ACTIVITY:
CC       Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by
CC         translocating in the 3'-5' direction.; EC=5.6.2.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00034617};
CC   -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC       {ECO:0000256|ARBA:ARBA00009922}.
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:PHQ56304.1}.
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DR   EMBL; NVQM01000046; PHQ56304.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G1XYC4; -.
DR   Proteomes; UP000226842; 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   CDD; cd17932; DEXQc_UvrD; 1.
DR   CDD; cd18807; SF1_C_UvrD; 1.
DR   Gene3D; 1.10.10.160; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
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:SF2; ATP-DEPENDENT DNA HELICASE SRS2; 1.
DR   PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR   Pfam; PF21196; PcrA_UvrD_tudor; 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   3: Inferred from homology;
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}.
FT   DOMAIN          8..286
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          287..562
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   BINDING         29..36
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   722 AA;  82169 MW;  BF69B569BB42FB05 CRC64;
     MDVTTILDPL NPAQREAVSS NASHLLVLAG AGSGKTRVLV HRIAWLIQVE QVSPYSIIAV
     TFTNKAAREM RGRIEELLGF SARGMWVGTF HGLAHRLLKM HWQDAGLPEN FQILDSDDQL
     RLVKRLYQSL GIDDSRWPHR QAQSFINNQK DEGLRSRDLQ PAHDPYQRTM QQVYAAYEEA
     CERGGMVDFG ELLLRAHELW LKNPELLQHY QHRFQHLLAD EFQDTNAIQY AWLRVLAGDQ
     VPVTAVGDDD QSIYGWRGAK VENIRYFSRD YPATQTVRLE QNYRSSKNIL EAANAVISRN
     TNRLGKNLWT DDNEGEAISL YAAFNEQDEA RFIAERLREW VNQGNLREES AILYRSNAQS
     RVLEEALLRA AIPYRIYGGQ KFYERQEIRN ALAYLRLLVN CHDDAAFERV VNTPTRGIGD
     KTIQELRELA REEGMSLWRT AEHAIAAGRF SGRASNALEA FLKLLAKLGE ESAELPLHEL
     VDHIIEGSGL IDFHRREKGD RGESRVENLQ ELVIACRSFE PEEKELPSLP QFLDRAALDA
     GDRQADVGED AVQLMTLHSA KGLEFPLVFL AGMEENLFPH RMSAEDPNRL EEERRLAYVG
     ITRAMQKLYL TFAESRQQYG IENYNRVSRF VRDIPANLVE EVRLRAQIKR PTSYARQPAM
     NLSDSGEDTG LSLGQRVLHP IFGEGVVINF EGNGAHARVQ VNFDKEGTKW LVLAYAKLSP
     VA
//
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