ID A0A0V1CJC1_TRIBR Unreviewed; 1086 AA.
AC A0A0V1CJC1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN Name=EIF4A3 {ECO:0000313|EMBL:KRY49329.1};
GN ORFNames=T03_14171 {ECO:0000313|EMBL:KRY49329.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY49329.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY49329.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY49329.1};
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 -!- SIMILARITY: Belongs to the NPL4 family.
CC {ECO:0000256|ARBA:ARBA00011025}.
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:KRY49329.1}.
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DR EMBL; JYDI01000179; KRY49329.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1CJC1; -.
DR Proteomes; UP000054653; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0043186; C:P granule; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd18045; DEADc_EIF4AIII_DDX48; 1.
DR CDD; cd08061; MPN_NPL4; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR037518; MPN.
DR InterPro; IPR016563; Npl4.
DR InterPro; IPR007717; NPL4_C.
DR InterPro; IPR024682; Npl4_Ub-like_dom.
DR InterPro; IPR007716; NPL4_Zn-bd_put.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR PANTHER; PTHR12710; NUCLEAR PROTEIN LOCALIZATION 4; 1.
DR PANTHER; PTHR12710:SF0; NUCLEAR PROTEIN LOCALIZATION PROTEIN 4 HOMOLOG; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF05021; NPL4; 1.
DR Pfam; PF11543; UN_NPL4; 1.
DR Pfam; PF05020; zf-NPL4; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF90209; Ran binding protein zinc finger-like; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50249; MPN; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Initiation factor {ECO:0000313|EMBL:KRY49329.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000313|EMBL:KRY49329.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054653};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1045..1065
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 40..68
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 71..250
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 261..422
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 430..501
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 656..793
FT /note="MPN"
FT /evidence="ECO:0000259|PROSITE:PS50249"
FT MOTIF 40..68
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
SQ SEQUENCE 1086 AA; 124391 MW; 79287A04AC58426F CRC64;
MARVFTSKEF RRKRRLQDDF EEEDMSRVDF ETSENVVVIP TFEEMNLKRE LLRGIYAYGF
NKPSMIQKRA IRPIVSGRDV IAQSQSGTGK TATFSIGLLQ VIDTQLRETQ ALVLAPTREL
AQQIQKVVLA LGDRMNVQAH ACIGGTNVGE DIRKLDYGQH VVVGTPGRVF DMITRQNLRT
DSLKVFVMDE ADEMLTKGNE LLYLILGFKD QIYDIYRFLP PGIQVVVISA TLPHEILEMT
GKFMTEPIRI LVKRDELTLE GIRQYFVHVE REDWKFETLC DLYDSITISQ AVVFCNTRHK
VEWLDEKMKE SNFTVGAIHG EMDQKDRNEV VRKFRDGIYR VLISTDVWSR GLDIPGVSLV
INYDVPTNRE AYLHRIGRSG RYGRKGCAIN FATTEDIPTM LEIESYYGTQ IDEMPMNGLF
WQQRKMVSEM VIRVQSRDGQ HRIRLKPSDT VETLLQKISD LIDLKDYPVK VYRDRAKSRV
LVESDVTIEE YGIQNGDMLY LENHIQPKSV SVQENISYIN IDRPFSAMKL KKDVEEDLVD
QILEKQSGVI ERKHQSNMCK HGDSKKCSNC LPIHVYDDEF LKEKEVNYLS FHAYLRKNGF
DDNIRSAASI PSLEKVSCEI IPNCRNHLPW PQGICSKCQP NPVTLNHQRY RHVDNVEIEN
KEIMSNFLSY WYKSHGQRMG FLFGRYEPMT DVPLGIRAVV TVIYEPPQIT YTDGIDILED
PHDEIVDSLA ECLGLKRIGW IFTDFLRDPD DPTLLVNTRN ANTYMLSAAE CLIAAKYQNK
YPNACKYSLD GTFGSKFVTL VLSGGENKMV DFAAYQVSNQ GSALVAAECL LPSRSSPNMA
CVRRSTPTHY VPDVYYMCHD EYNNKIRKTA GLLPVEYLFV TIPVGLAKEM RYTLTSQENP
FPIENRSSIG IAQNIRVVGE YVKQFEESEF LKMISNFHFL VYLLTNTEVT FELDDLAELL
DAVAKQDSDL AKQWAENMPS GGESVEESEP WACGHCTYLN DHPNADCEMC SLPQKFNLIF
NFRLFIMVDL DGSQSPHSHK ISNTVFIIPA VIVLIIVGIV VYKLINTLQS KHKKKEEKKK
AKGKQK
//
