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Database: UniProt
Entry: J9J6L2_9SPIT
LinkDB: J9J6L2_9SPIT
Original site: J9J6L2_9SPIT 
ID   J9J6L2_9SPIT            Unreviewed;       845 AA.
AC   J9J6L2;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   ORFNames=OXYTRI_16720 {ECO:0000313|EMBL:EJY85418.1};
OS   Oxytricha trifallax.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC   Stichotrichia; Sporadotrichida; Oxytrichidae; Oxytrichinae; Oxytricha.
OX   NCBI_TaxID=1172189 {ECO:0000313|EMBL:EJY85418.1};
RN   [1] {ECO:0000313|EMBL:EJY85418.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JRB310 {ECO:0000313|EMBL:EJY85418.1};
RX   PubMed=23382650; DOI=10.1371/journal.pbio.1001473;
RA   Swart E.C., Bracht J.R., Magrini V., Minx P., Chen X., Zhou Y.,
RA   Khurana J.S., Goldman A.D., Nowacki M., Schotanus K., Jung S., Fulton R.S.,
RA   Ly A., McGrath S., Haub K., Wiggins J.L., Storton D., Matese J.C.,
RA   Parsons L., Chang W.J., Bowen M.S., Stover N.A., Jones T.A., Eddy S.R.,
RA   Herrick G.A., Doak T.G., Wilson R.K., Mardis E.R., Landweber L.F.;
RT   "The Oxytricha trifallax Macronuclear Genome: A Complex Eukaryotic Genome
RT   with 16,000 Tiny Chromosomes.";
RL   PLoS Biol. 11:E1001473-E1001473(2013).
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:EJY85418.1}.
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DR   EMBL; AMCR01003122; EJY85418.1; -; Genomic_DNA.
DR   AlphaFoldDB; J9J6L2; -.
DR   EnsemblProtists; EJY85418; EJY85418; OXYTRI_16720.
DR   OrthoDB; 5475708at2759; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd17932; DEXQc_UvrD; 1.
DR   Gene3D; 1.10.10.160; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
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; 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          45..362
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          363..765
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          582..609
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          621..653
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         66..73
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   845 AA;  98508 MW;  22B2E65CD763A8CA CRC64;
     MKKVSKDKTI EINPQKRSNS KSDSKKSKKS KEEQKHILDK YPQFQELNDD QKEAVVYNDS
     PLLILAGVGT GKTQTLMSKY AYLVMEGQQK FDINQTNILA VTFTNKAAKT MQVRASQITQ
     RDLRQNWIGT FHSLSARMLL QDDHYKLVQL KEDYHLLSQE KQRKQVRKVL KDQNAIRDLI
     LNHEQRQLDK QQQKGQMSQY SQYYRQQKPS MPYSKILRAI DTFKNRLLKP DDQIPDDLKE
     FEQIVFYNVY ELYQESMRKE NLIDFGDLLM YVVDILKRFP EILQKFRAQF KYILVDEVQD
     LNYIQQEWLK LIVGDNLHLT CVGDDDQMVY GFRGASGDFI LNFEHHFDTS HTIKLEQNYR
     STKKILEGAN NLISKNFNRK GKTLWTDNQT GEDISFLEYK SKDQEIQSIV EYIKQMIGGG
     EDFGFSPEQI AILTRTNADG REIEKCLIKE SVNYELAANK KAFLDLKEVN LALMFLVILH
     KPFDNYAWKE ILGNLEGFGK DTVKKITTYA EKNDIAIHDI CEYLVEPCRY NLGKRIEAPT
     NVRTLESRIK SSVLGNNFSN AQSKVGNIQN LKQNSLSSYY SIQKQKQKEE KKTRYSKGPA
     KNKKGNIKNL NCDDSDSWEC INDQPIDKND QSIMSDKSDQ SVQTPPQPQS KPLYTTIDID
     HKLTKKQREK LEALISARDK YKKGKTNNFA SYLEDSLFYD CLSKISKTKE GKSNKVQENV
     RDLLEIALTF EDIDEFFNHI TLFSGDASKQ DQKAIKVMTI HASKGLEFNQ VFLPFWVKGK
     FPVELSRENE KVEVEEERRT AFVGLTRARE HLFISHHEEC EEFVKQQQVS QFVQEIQTKT
     YKIKK
//
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