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Database: UniProt
Entry: A0A2T7PNS4_POMCA
LinkDB: A0A2T7PNS4_POMCA
Original site: A0A2T7PNS4_POMCA 
ID   A0A2T7PNS4_POMCA        Unreviewed;       871 AA.
AC   A0A2T7PNS4;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Helicase ATP-binding domain-containing protein {ECO:0000259|PROSITE:PS51193};
GN   ORFNames=C0Q70_06354 {ECO:0000313|EMBL:PVD35073.1};
OS   Pomacea canaliculata (Golden apple snail).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Architaenioglossa; Ampullarioidea; Ampullariidae; Pomacea.
OX   NCBI_TaxID=400727 {ECO:0000313|EMBL:PVD35073.1, ECO:0000313|Proteomes:UP000245119};
RN   [1] {ECO:0000313|EMBL:PVD35073.1, ECO:0000313|Proteomes:UP000245119}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SZHN2017 {ECO:0000313|EMBL:PVD35073.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:PVD35073.1};
RA   Liu C., Liu B., Ren Y., Zhang Y., Wang H., Li S., Jiang F., Yin L.,
RA   Zhang G., Qian W., Fan W.;
RT   "The genome of golden apple snail Pomacea canaliculata provides insight
RT   into stress tolerance and invasive adaptation.";
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC       DDX11/CHL1 sub-subfamily. {ECO:0000256|ARBA:ARBA00008435}.
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:PVD35073.1}.
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DR   EMBL; PZQS01000003; PVD35073.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T7PNS4; -.
DR   STRING; 400727.A0A2T7PNS4; -.
DR   Proteomes; UP000245119; Miscellaneous, Linkage group lg3.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR   GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR   GO; GO:0006139; P:nucleobase-containing compound metabolic process; IEA:InterPro.
DR   CDD; cd18788; SF2_C_XPD; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR006555; ATP-dep_Helicase_C.
DR   InterPro; IPR045028; DinG/Rad3-like.
DR   InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR   InterPro; IPR006554; Helicase-like_DEXD_c2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010614; RAD3-like_helicase_DEAD.
DR   InterPro; IPR013020; Rad3/Chl1-like.
DR   NCBIfam; TIGR00604; rad3; 1.
DR   PANTHER; PTHR11472:SF41; ATP-DEPENDENT DNA HELICASE DDX11-RELATED; 1.
DR   PANTHER; PTHR11472; DNA REPAIR DEAD HELICASE RAD3/XP-D SUBFAMILY MEMBER; 1.
DR   Pfam; PF06733; DEAD_2; 1.
DR   Pfam; PF13307; Helicase_C_2; 1.
DR   SMART; SM00488; DEXDc2; 1.
DR   SMART; SM00491; HELICc2; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245119}.
FT   DOMAIN          41..388
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51193"
FT   REGION          195..215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          134..164
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        196..215
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   871 AA;  97950 MW;  FA4BBEF5F91FCFEB CRC64;
     MADNFEDDDD ELFSVIVDEE CGKETTTQKV AEKENFGDCS VPTTFPFPFE PYQIQTDFMR
     QLYICLQEGK VGIFESPTGT GKSLSLICGA LTWLKDFQDN QRKELDAFLS ESTKTNGYSQ
     GGGGFDWVTE FSKRKEQEDR LSRAKQEQEL IEQREKRLKN VQSSSKVTRG KRKFAQLEDD
     FSDLLKGSSI ETQKAFNEDY ESDEEKSAEW KENENDEDAH VTKNLCINEA VRKLKSVSFI
     NDRCLELQQK KSKKNPGCPY RKQEILEDFR DRALLGLCDI EQLTTLGRET KTCPYYGSRL
     AIPSAEVVVL PYNTLLHKST REASGVKLAG NVVIVDEAHN LLETVNSVHS VEVTGAQILR
     AHSQLSQYEV KYRSRLKAKN LMYVKQILFV LSNLVKCMGG KTGVPADKQN TGKSDVNLMT
     INNFLFEAKI DNLNLFKIRG ILSPQSDQQE EKYQVAEVIP AMPVAVKETA TFGVSMFLKN
     IGKAKTSDPI KEDITVDVVN RNKSTPVLNS PLMHIESFLQ ALTTANDDGR VVLSKQMLLS
     QSGIKFLLLN PAVHFADVLQ EARAVVVAGG TMQPISEFKD QLFFAAGLQP DKLLEFSCGH
     VIPPDHLLSL TLATGPTGRQ LDFTFQTRDD PHLLEELGRL VVNLCSVVPG GIVLFFPSYD
     YEQLVSVSWE KSGILGRIEA KKKIFREPKS AIQVEHVLTQ YGDCIKKCQC RTTGGPTGAI
     LMCVVGGKMS EGINFSDDLG RCVLMVGMPY PNLRSPELKE KIDYLNSNFP KDEAGRPAGQ
     VHYENLCMKA INQSIGRAIR HREDYAVIIL ADQRYSRTSV SSKLPGWIAK HLYKMDAFPP
     ALARVSKKEE NDFQWWMLLL MFATDDFRDH L
//
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