ID A0A0V0R7G9_PSEPJ Unreviewed; 1074 AA.
AC A0A0V0R7G9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=PPERSA_10524 {ECO:0000313|EMBL:KRX10425.1};
OS Pseudocohnilembus persalinus (Ciliate).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Scuticociliatia; Philasterida; Pseudocohnilembidae;
OC Pseudocohnilembus.
OX NCBI_TaxID=266149 {ECO:0000313|EMBL:KRX10425.1, ECO:0000313|Proteomes:UP000054937};
RN [1] {ECO:0000313|EMBL:KRX10425.1, ECO:0000313|Proteomes:UP000054937}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=36N120E {ECO:0000313|EMBL:KRX10425.1};
RX PubMed=26486372; DOI=10.1038/srep15470;
RA Xiong J., Wang G., Cheng J., Tian M., Pan X., Warren A., Jiang C., Yuan D.,
RA Miao W.;
RT "Genome of the facultative scuticociliatosis pathogen Pseudocohnilembus
RT persalinus provides insight into its virulence through horizontal gene
RT transfer.";
RL Sci. Rep. 5:15470-15470(2015).
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:KRX10425.1}.
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DR EMBL; LDAU01000028; KRX10425.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0R7G9; -.
DR EnsemblProtists; KRX10425; KRX10425; PPERSA_10524.
DR InParanoid; A0A0V0R7G9; -.
DR OMA; DENMENY; -.
DR OrthoDB; 5475708at2759; -.
DR Proteomes; UP000054937; Unassembled WGS sequence.
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 CDD; cd18807; SF1_C_UvrD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
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; PF13245; AAA_19; 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.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Coiled coil {ECO:0000256|SAM:Coils};
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:UP000054937}.
FT DOMAIN 8..236
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT REGION 352..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 925..992
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 359..380
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 29..36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1074 AA; 127318 MW; FDEA659555629110 CRC64;
MFGSSAVYLN DQQLSIVNSN IDENQKILAC AGSGKTTTII CRIKFLVEKG VDPSKIWMTA
FNIDAARQIK EKLSLVMGKE LSEKVKVNNI DKISKGLLCK FDTNFQKKIS LQSKEMEKMK
EKFDEEGLTE SEFNRKGYYK IKDFTPMLLK YFQQNQQVVP QMFDYFFFDE FQDVNPDEYE
FLKYLAHQGV KVSVIGDDAQ NIYSFRDSVV DIIQSQINKD IPNIKSYYLT TNYRSSPEIV
HFANEVVKAS DVLIKKQMLA DKFSCEQKPL LKKMNSVEEQ NQYVIEYIQQ QIYQKQKNPE
QIAVLCRNNR PLQIFEDQLL NYNKKQEFKD KQINISPKPI NYVANFTSEN LNQNKESDEN
NNQESENNKK NVKGRKNLKN EGKKTQRSLL NFMGSNQNPH FQKPITLSTI HKAKGLEWDV
VIIIHCNDEF FPGSSQVEEE RRVFYVAVTR AKIQLLITYI NNEQVFKLSR FVNQINAKYF
EGDFQSQQEI YIENQLRMLK EKNENQQEIK MFEQQQKDEE DFITKDQIQS AKKLFNLEEI
LNYLDIQGQI KQKYYNKLNL LLEKELNLEF LENVNNFYKK QGGLKIESCN LPGNLGNWIV
ANNMHNVYYN FLRHFLIRAI IFQVYVNKND DYELIKKLKL MLINQEAETV LYNGEKEKNF
TYIKDQKKYQ QFSKSYEIFQ CIDKEPLDII EDIYRVSVMK YILQDKQMFI QREDILKNFM
VQSNLLKNCY KKFVCKYIIE NSLSSENNLQ EFKFGEQLEF QIDENMENYK NVYANLNKEK
LQKFKNENNF LKLHTSMDLI IGNTLVIFQF INYQGLQFND IVRLYFQIAI LKIKNINKIQ
FVKIYNPLKG NVFTINVLKF YDNHMEQFLN LIFEVQTTLI GQIIPQILSK QAQQQIKSKK
NITNNPINVR FEGIHDFEDS QSDNYQNENN DIQFKQNEIN NKIEQNQNLQ RNLNKTVFQG
FQSATQILQS QNQEKQQKLE EKNCQFKQTK NNKQGFIQNK INTNNIFNFG FQNAKTYQEQ
QLKSQDQKFQ ADNKNNSLKI KVKMIVENET KICQQNKQFQ VQKLQQKLNF IQKK
//
