ID A0A0V0WW51_9BILA Unreviewed; 1538 AA.
AC A0A0V0WW51;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 22-FEB-2023, entry version 31.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN Name=Supv3l1 {ECO:0000313|EMBL:KRX79925.1};
GN ORFNames=T06_6367 {ECO:0000313|EMBL:KRX79925.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX79925.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX79925.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX79925.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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=3.6.4.13;
CC Evidence={ECO:0000256|ARBA:ARBA00001556};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the CRELD family.
CC {ECO:0000256|ARBA:ARBA00005897}.
CC -!- SIMILARITY: Belongs to the helicase family.
CC {ECO:0000256|ARBA:ARBA00008708}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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:KRX79925.1}.
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DR EMBL; JYDK01000047; KRX79925.1; -; Genomic_DNA.
DR Proteomes; UP000054673; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0016817; F:hydrolase activity, acting on acid anhydrides; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0032367; P:intracellular cholesterol transport; IEA:InterPro.
DR CDD; cd17913; DEXQc_Suv3; 1.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00064; FU; 1.
DR CDD; cd00916; Npc2_like; 2.
DR CDD; cd18805; SF2_C_suv3; 1.
DR Gene3D; 1.10.1740.140; -; 1.
DR Gene3D; 1.20.272.40; -; 1.
DR Gene3D; 1.20.58.1080; -; 1.
DR Gene3D; 2.60.40.770; -; 2.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR021852; DUF3456.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR006212; Furin_repeat.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002049; LE_dom.
DR InterPro; IPR003172; ML_dom.
DR InterPro; IPR033916; ML_Npc2-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR022192; SUV3_C.
DR InterPro; IPR041082; Suv3_C_1.
DR InterPro; IPR044774; Suv3_DEXQc.
DR InterPro; IPR041453; Suv3_N.
DR PANTHER; PTHR12131; ATP-DEPENDENT RNA AND DNA HELICASE; 1.
DR PANTHER; PTHR12131:SF1; ATP-DEPENDENT RNA HELICASE SUPV3L1, MITOCHONDRIAL; 1.
DR Pfam; PF11938; DUF3456; 2.
DR Pfam; PF02221; E1_DerP2_DerF2; 2.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF12513; SUV3_C; 1.
DR Pfam; PF18147; Suv3_C_1; 1.
DR Pfam; PF18114; Suv3_N; 1.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00179; EGF_CA; 1.
DR SMART; SM00261; FU; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00737; ML; 2.
DR SUPFAM; SSF81296; E set domains; 2.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS01248; EGF_LAM_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:KRX79925.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000054673};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1481..1499
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1506..1525
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 702..892
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1323..1368
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1422..1461
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 1358..1367
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1538 AA; 171469 MW; 66DA812DB2BD97F4 CRC64;
MVKNAALCRR RPEEHFPTSM TMLAATRTKF TLIVCFAFGF FYFAQPKSVE FNNCSTCLLL
CSAKSGFNFL VSYIRITEQL FVALDAKFDV PRRKNSLFQR DEIVIVNIGK VTTLFCNLES
IFTVNDVAVD PCDAEGSTCP LIRGSKASIT IRFVPDREVK QLKARVHGIL MKLGKVPFLL
PNSDACKNSN LTCPLVAGEE YTYQQSIHVL RSYPKMNLLI KWELIEPGDE PKNGSVPIIA
VMYKLLSYAC LLAAAVAINI NFRDCGSVAG SVQNVTLDPC DNPNYCSLKR GTSPKVGILF
TPSQETTAVH VVVHGIIKGL PVPFPVPNPD GCKDSGLQCP LSSNNTVHYE DVFDVKSEYP
TIGLLVRWEL VDQNKKDLFT VARRTVKNEN FDEIGQLYLT QVVRDMTSVK AVLLGLRNTG
RLLQLRHLSG SKKSFEDLVV PLTVKSASTA NDVDVGVEFG GILAKDALAS VLSQFARRPA
VRKLGAEHGL TGKFFLQALA SFRRCCQESA VLPVDLHIML ADILQNSRHV DDLFPLFLRH
ARQVFPHLEC IEELKNISDL RLPQNWYPEA RSIQRRVIFH AGPTNSGKTY QALQRYLAAK
SGVYCGPLKL LASEVFHKSN AAGVPCDLIT GEERCLANGQ TCSEHISCTV EMLDTRVHYE
VAVIDEIQMM RDLQRGWAWT RALLGVCADE IHVCGESAAV DFVKELLVSL GDEFEVHTYE
RKTPLKVLDS PLGSLDSIQP YDCIVAFNRN DLFKVTRQVE ASGRSVAMIY GSLPPGTKLA
QARKFNDPDD PCDVLVATDA IGMGLNLSIR RVIFYSLVKV TLNESGEKEL EPISTSQALQ
IAGRAGRFGT FHESGEVTTL RMEDLPALKA ILTKPTEPIS AAGLFPTLEQ IEMFSYYLPK
ATLSNLLDIF VSLSAVDESR FFMCNVDDLK FLADMIEHVP LTLKVRYIFC MAPISRKKPF
VCGMFLRYAR KFSRGEPLTS DWLARTVGWP FSAPTKIVDL IHLEDVFDVL DTYLWLGYRF
TDMFPETEQV RAMQRELDVL IRESLQNVKQ LLKTVQVAGL FDQQGLNGFD SKSPTTANAA
AVAKDSPAKM KQATTTAATA VRKGGVIQSL IKQGLLTPGM VEQIRKEIQA DQEELFIPTR
YFLITVCHVI PYDVGMNVGS VMLFNCSTDL MLFSYLFECS CGMEVNTFAF TISAPDVPHG
DRCDTCRFLV RSFEKGFNDT NKSHFEGGNT AWENENLGKY STSETRFIEI MELICSKKSK
DVKEESKIKN LESKCHAMAE EHEETLETWY YHNQKKYPDL FDWFCIRTVK VCCPDNTFGA
SCAPCPGDPK RPCFGNGICE VMNNIGSGSR FGSGKCKCHR GYQGKLCRHC DSNFFKVHSN
ETYILCQPCH ESCKGGCSGE GPKECNSCRV GWIMDKDTGC KDIDECESSP CTDQFEKCEN
TPGSYKCVCA EAFRREDGVC IPDPDVPRPK PVFFGLLAQQ VLRYASYFGL LLSFLLILLR
PKTPLIVLFT CSLVIIALIE AGHAVRMLNA IFLGDQAL
//
