ID A0A0V1M4G1_9BILA Unreviewed; 1249 AA.
AC A0A0V1M4G1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Putative pre-mRNA-splicing factor ATP-dependent RNA helicase mog-1 {ECO:0000313|EMBL:KRZ66733.1};
DE Flags: Fragment;
GN Name=mog-1 {ECO:0000313|EMBL:KRZ66733.1};
GN ORFNames=T10_3240 {ECO:0000313|EMBL:KRZ66733.1};
OS Trichinella papuae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ66733.1, ECO:0000313|Proteomes:UP000054843};
RN [1] {ECO:0000313|EMBL:KRZ66733.1, ECO:0000313|Proteomes:UP000054843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ66733.1};
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:KRZ66733.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JYDO01000227; KRZ66733.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1M4G1; -.
DR STRING; 268474.A0A0V1M4G1; -.
DR Proteomes; UP000054843; 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 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 Helicase {ECO:0000313|EMBL:KRZ66733.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000054843}.
FT DOMAIN 565..729
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 751..927
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 161..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1208..1249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRZ66733.1"
SQ SEQUENCE 1249 AA; 142483 MW; 9FFFE81EEB07DA4A CRC64;
LCGLFNFIWF SIENTLDEIT QDISVLLNIV IFIIMRENVE LFEASLLRSI MEEEEESKAM
NVDDEDRSLH RLEGSKQTGG GLVIKKRKED KSLDSGVVPK ASLLGLDKLA EAKRAEKKEL
EEREKVRKIM DKRHYRSTDE DIESGVTDSV RGRILNLVEK RNHDEGRGLA ASSKKTTTKR
GHRRDLKREQ EDNDDCGWSS KRKSRTADQQ QPATPVFKVP FTPSRCRWDD EELCRAQQST
GAGGRFRSRD LPWNSPAPGL GRPSGSSEMS SERWRRQHPS SSYREEEEDD DGGGRIIFNN
DQEREDWEDE QRRLDRDWYA MEEAQECLDE EHNPFYWVSD EYRKRREEHF EEQQQQKKAK
SKSKKPLTAR QLQIKKDNEK WENNRLFRSG IIDKLELEDE LLLEEDAESR VNLLVQNLVP
PFLDGRIVFT KQPEPVVPVR DPTSDMAIIA RKGSAAIRAW REKEERRRDQ EKHWQLGGTQ
LGNLLGISKQ QEQQSDADSQ RQKGAVEEDF ADDYKARNRF AEHMDNSGRD AVGAGGLCAS
EFTQKKSLKE QRQFLPVFAV RQRLLNVIRE NSVVVVVGET GSGKTTQLSQ YLFEDGYADR
GLMIGCTQPR RVAAMSVAKR VADEMGVALG EQVGYAIRFE DCTTPTTVLK YMTDGILLRE
CLRDKDLDHY SVVIMDEAHE RSLNTDVLFG LLKEVLARRR DLKLIVTSAT MDAAKFADFF
GNVPVFNIPG RTFPVQVTHS RLVVEDHVQA AVKQAVSVHL GAPLPGDILI FMPGQEEVEA
TCALIGQRLE QLDDAPALSV LPIYSQLPAD LQARIFHRAA DNSRKCVVAT NIAETSLTLD
GILFVIDPGY CKLKVFNPRI GMDALQVFPI SQASANQRSG RAGRTGPGQC YRLYTERQYE
EELLANTVPE IQRTNLSNVV LLLKSLGVDD LLKFQFMDAP PQDNLLNSMY QLWTLGALDN
TGQLTKLGRR MIELPLDPTL SKMLIVACDM RCSEEVLTVV SMLSVPSVFY RPKGREEDGD
AKREKFQVPE SDHLTLLNVY QQWRVHRYSA SWCAEHFVHV KAMRKVREIR AQLKDIMDQQ
KMRIQSCGTD WDIVRKCICS AYFHNAARLK GIGEYVNLRT GIPCFLHPTS ALFGMGYTPD
YVVYHELVMT AKEYMQCVTA VDGYWLAELG PMFYTVKESG SSRKENRIRA LKDMETMERE
MRDAQQQMDQ QKAKEEAALR AQWKTPKIAT PGRVDPTKST PHRTGRFGL
//