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Database: UniProt
Entry: A0A0V0YD32_TRIPS
LinkDB: A0A0V0YD32_TRIPS
Original site: A0A0V0YD32_TRIPS 
ID   A0A0V0YD32_TRIPS        Unreviewed;      1025 AA.
AC   A0A0V0YD32;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Putative pre-mRNA-splicing factor ATP-dependent RNA helicase mog-5 {ECO:0000313|EMBL:KRX98310.1};
GN   Name=mog-5 {ECO:0000313|EMBL:KRX98310.1};
GN   ORFNames=T4E_10348 {ECO:0000313|EMBL:KRX98310.1};
OS   Trichinella pseudospiralis (Parasitic roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6337 {ECO:0000313|EMBL:KRX98310.1, ECO:0000313|Proteomes:UP000054815};
RN   [1] {ECO:0000313|EMBL:KRX98310.1, ECO:0000313|Proteomes:UP000054815}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS141 {ECO:0000313|EMBL:KRX98310.1};
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   -!- 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:KRX98310.1}.
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DR   EMBL; JYDU01000022; KRX98310.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0YD32; -.
DR   STRING; 6337.A0A0V0YD32; -.
DR   Proteomes; UP000054815; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   CDD; cd21691; GH2-like_DHX8; 1.
DR   CDD; cd05684; S1_DHX8_helicase; 1.
DR   CDD; cd18791; SF2_C_RHA; 1.
DR   Gene3D; 1.20.120.1080; -; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR   InterPro; IPR049588; DHX8_GH2-like.
DR   InterPro; IPR048333; HA2_WH.
DR   InterPro; IPR007502; Helicase-assoc_dom.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR049621; S1_DHX8_helicase.
DR   InterPro; IPR003029; S1_domain.
DR   PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR   PANTHER; PTHR18934:SF85; ATP-DEPENDENT RNA HELICASE DHX8; 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   Pfam; PF00575; S1; 1.
DR   SMART; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00316; S1; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS50126; S1; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000313|EMBL:KRX98310.1};
KW   Helicase {ECO:0000313|EMBL:KRX98310.1};
KW   Hydrolase {ECO:0000313|EMBL:KRX98310.1};
KW   mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW   mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW   Nucleotide-binding {ECO:0000313|EMBL:KRX98310.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054815}.
FT   DOMAIN          237..307
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          547..736
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          129..221
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          307..329
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          458..489
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        129..174
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        193..221
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        315..329
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        459..473
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1025 AA;  117034 MW;  C2415E20040ABCA2 CRC64;
     MEEMERLQYI SLVSKICTEL ENHLGLSDKD LAEFIIHLGQ KNPTFESFKS ALESNGAEFD
     NSLISNLLRR IQLMSKPTGK SENADENASH MLSMSSKSDR EVMKQCLPAL AMPNKPVSET
     LSELENLIPQ WRRENETEQK ENAGDGSRDE RKKRERRRSR DRSRSCDSSE RRTERHRARR
     RRSSSFSGES SRKHASRRRR SRSGSELRTK LKSRRRSRSG ERISRIRIKL DDTPIVGKIY
     DGRVNSIRDF GCFVELFGLR RHVEGLVHIS QIKNERVNAV TDVVTRGQKV KVKVLACSGN
     RTSLSMREVD QETGEDLNPT EDVDQEEQPF DETLQLRNPD LPSAAQQKLM QLQAEEFKAS
     TSKRIKRLSS PERWELKQMM AASCISTADL PDFDEETGVL LQEDMLDDHE EDVEVELVEE
     EPQFLQGYGR VRQDLEPIKV VKNPDGSLAQ AAMMQGALAK ERREQKIQQQ RERGNEQLGR
     GSGAASKSFL DPLADADNKY SKVLQNVERK HMDLPEWKRH IAAGKSFGKP QGSMTILEQR
     QSLPIYKLRG ELVKAVSENQ ILIVIGETGS GKTTQITQYL AEEGFTFSGK IACTQPRRSL
     GPDVPELIIL PVYSALPSEM QTRIFESAPP GSRKVVIATN IAETSLTIDG IYYVVDPGFV
     KQKIYNPKTG MDSLVVTPIS QAQAKQRSGR AGRTGPGKCY RLYTERAYRD EMLPTPVPEI
     QRTNLASTLL QLKAMGINNL IDFDFMDPPP VEAMVMALEQ LHSLSALDDE GLLTRVGRRM
     AEFPLEPSLS KLLIMSVHLG CSEEVLTIVS MISVQNVFYR PKDKQDVADQ KKSKFHQPEG
     DHLTLLAVYN SWKNHRYSHS WCYENFVQIR TLKRAQDIRK QLLGIMDRHR LDMISCGKNM
     QKVQKAICSG FFRNAAKKDP QEGYRTLVDS QTVYIHPSSS LFHNQPEWVV YHELVMTTKE
     YMREVCAIEP KWLVEFAPAF FRFGDPTKLS KFKKGQKIEP LFNKYEDVNA WRISKVKKKI
     YNPNR
//
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