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Database: UniProt
Entry: A0A0V1NU15_9BILA
LinkDB: A0A0V1NU15_9BILA
Original site: A0A0V1NU15_9BILA 
ID   A0A0V1NU15_9BILA        Unreviewed;      1542 AA.
AC   A0A0V1NU15;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   Name=mog-1 {ECO:0000313|EMBL:KRZ87452.1};
GN   ORFNames=T08_6435 {ECO:0000313|EMBL:KRZ87452.1};
OS   Trichinella sp. T8.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ87452.1, ECO:0000313|Proteomes:UP000054924};
RN   [1] {ECO:0000313|EMBL:KRZ87452.1, ECO:0000313|Proteomes:UP000054924}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS272 {ECO:0000313|EMBL:KRZ87452.1};
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   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC       PRP16 sub-subfamily. {ECO:0000256|ARBA:ARBA00038040}.
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:KRZ87452.1}.
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DR   EMBL; JYDM01000100; KRZ87452.1; -; Genomic_DNA.
DR   Proteomes; UP000054924; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0022414; P:reproductive process; IEA:UniProt.
DR   CDD; cd18791; SF2_C_RHA; 1.
DR   Gene3D; 1.20.120.1080; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR048333; HA2_WH.
DR   InterPro; IPR007502; Helicase-assoc_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR   PANTHER; PTHR18934:SF91; PRE-MRNA-SPLICING FACTOR ATP-DEPENDENT RNA HELICASE PRP16; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF21010; HA2_C; 1.
DR   Pfam; PF04408; HA2_N; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF07717; OB_NTP_bind; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Helicase {ECO:0000313|EMBL:KRZ87452.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054924}.
FT   DOMAIN          521..685
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          699..883
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          33..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          73..182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          199..260
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1282..1321
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1143..1177
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        73..102
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        115..133
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        144..163
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        215..234
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        236..260
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1297..1311
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1542 AA;  175011 MW;  4C82954AC0162D05 CRC64;
     MTFYLYEEEE ICTVAMEEED SKAVIGDDDR SLHRLEGSKQ TGGGLVIKKR KEDNKSLDPK
     VSLLGLDKLA EAKRAERRKE VEEREKVRRI MDKRHYRSTD EDLGSGVTDS VRGRISNWVE
     KRNHDEGRGL AASSKKATKR GHRRDVKREQ DVDDDDDNCG WSSKRKSRPQ QPATPVFKVP
     FTPSRCRWDD EEVYRAQSGG RFRSRDLPWN SPAPGLVRPT SSSEVSQTAR WRRQHPGSCS
     YRDDREDEEE GRIIFNSEQE REEWEDEQRR LDRDWYAMEE AQECLDEEHN PFYWVSDEYR
     KRREEHFEEQ QQNKMKKNKK PLTARQLQIK KDNEKWENNR LFRSGIIDKL ELEEDELLLE
     EDAESRVNLL VQNLVPPFLD GRIVFTKQPE PVVPVRDPTS DMAIIARKGS AAIRAWREKE
     ERRRDQEKHW QLGGTQLGNL LGITKQQQSD SNSQQVGGGT EEDFADDYKA RNRFAEHMDN
     DGAGSAGDGT AGGGASEFTQ KKSLKEQREF LPVFAVRQRL LNVIRENSVV VVVGETGSGK
     TTQLSQYLFE DGYADRGLMI GCTQPRRVAA MSVARRVADE MGVALGEQVG YAIRFEDATS
     PATVLKYMTD GILLRECLRE PDLDHYSVVI MDEAHERSLN TDVLFGLLKE VLARRRDLKL
     IVTSATMDAA KFADFFGNVP VFNIPGRTFP VQVSHSKLVV DDHVQAAVKQ AVSVHLGAPL
     PGDILIFMPG QEEVEATCAL IAQRLDQLDD APPLSVLPIY SQLPADLQAR IFHRAVDNSR
     KCVVATNIAE TSLTLDGILF VIDPGYCKLK VFNPRIGMDA LQVFPISQAS ANQRSGRAGR
     TGPGQCYRLY TERQYEEELL PNTVPEIQRT NLSNVVLLLK SLGVDDLLKF HFMDAPPQDN
     LLNSMYQLWT LGALDNTGQL TKLGRRMIEL PLDPTLSKML IVACEMGCSE EVLTVVSMLS
     VPSVFYRPKG REEDGDAKRE KFQVPESDHL TLLNVYQQWR VHRYGASWCA DHFVHVKAMR
     KVREIRAQLK DIMDQQKMPI QSCGTDWDIV RKCICSAYFH NAARLKGIGE YVNLRTGIPC
     FLHPTSALFG MGYTPDYVVY HELVMTAKEY MQCVTAVDGY WLAELGPMFY TVKESGSSRK
     ENRIRALKDM ETMEREMRDA QQQIDEQKAK QEAALRAQWK TPKIATPGRV DPTKSTPHRT
     GLKKQRFLGR SASAHVTSRM TSAHRCFGHC DEVFVEVRLC RVGSVVIVLR RATHPISQRM
     DVQTDAGHVD VDYIMLLGDQ SSEQLDNSGG SDARTAGEVE SAQQGTVIAQ SKQGRIADKA
     RTPDGQFAQS VVLDHQKQKS IVEHMHGMTV DQTQNLEPFQ FTNAEQSQLA VDGHGQIVHV
     QRIQMGASVE EHSKNHRIQS VFGFREDVVV DENRPQILTR DSEHHVQQLP ASETVRPAGA
     QAHRQAHRTE VHGRAEAELC VAFVAHEHQF QASQRTQLPT QQIEPTTTDQ TARESVENFQ
     LVENIQQNFT RKLETVPPAE SPNTIITVTR KQITEHRPTW NM
//
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