ID A0A0V0UQK1_9BILA Unreviewed; 1015 AA.
AC A0A0V0UQK1;
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=Eukaryotic translation initiation factor 3 subunit G {ECO:0000256|HAMAP-Rule:MF_03006};
DE Short=eIF3g {ECO:0000256|HAMAP-Rule:MF_03006};
DE AltName: Full=Eukaryotic translation initiation factor 3 RNA-binding subunit {ECO:0000256|HAMAP-Rule:MF_03006};
DE Short=eIF-3 RNA-binding subunit {ECO:0000256|HAMAP-Rule:MF_03006};
DE AltName: Full=Eukaryotic translation initiation factor 3 subunit 4 {ECO:0000256|HAMAP-Rule:MF_03006};
GN Name=eif3g {ECO:0000313|EMBL:KRX53579.1};
GN ORFNames=T09_11452 {ECO:0000313|EMBL:KRX53579.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX53579.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX53579.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX53579.1};
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 -!- FUNCTION: RNA-binding component of the eukaryotic translation
CC initiation factor 3 (eIF-3) complex, which is involved in protein
CC synthesis of a specialized repertoire of mRNAs and, together with other
CC initiation factors, stimulates binding of mRNA and methionyl-tRNAi to
CC the 40S ribosome. The eIF-3 complex specifically targets and initiates
CC translation of a subset of mRNAs involved in cell proliferation. This
CC subunit can bind 18S rRNA. {ECO:0000256|HAMAP-Rule:MF_03006}.
CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex. {ECO:0000256|HAMAP-Rule:MF_03006}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03006}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit G family. {ECO:0000256|HAMAP-
CC Rule:MF_03006}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00124}.
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:KRX53579.1}.
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DR EMBL; JYDN01000197; KRX53579.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0UQK1; -.
DR STRING; 181606.A0A0V0UQK1; -.
DR Proteomes; UP000054681; Unassembled WGS sequence.
DR GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; IEA:UniProtKB-UniRule.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR CDD; cd12933; eIF3G; 1.
DR CDD; cd00112; LDLa; 5.
DR CDD; cd12408; RRM_eIF3G_like; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 4.10.1220.10; EGF-type module; 1.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 5.
DR HAMAP; MF_03006; eIF3g; 1.
DR InterPro; IPR017334; eIF3_g.
DR InterPro; IPR024675; eIF3g_N.
DR InterPro; IPR034240; eIF3G_RRM.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR24270; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED; 1.
DR PANTHER; PTHR24270:SF55; VERY LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED; 1.
DR Pfam; PF12353; eIF3g; 1.
DR Pfam; PF00057; Ldl_recept_a; 4.
DR Pfam; PF00076; RRM_1; 1.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00192; LDLa; 7.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 5.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS01209; LDLRA_1; 3.
DR PROSITE; PS50068; LDLRA_2; 7.
DR PROSITE; PS50102; RRM; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03006};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540, ECO:0000256|HAMAP-
KW Rule:MF_03006}; Membrane {ECO:0000256|SAM:Phobius};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_03006}; Reference proteome {ECO:0000313|Proteomes:UP000054681};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 370..392
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 205..283
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DISULFID 625..640
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 748..763
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 836..854
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 893..908
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 933..948
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 1015 AA; 115165 MW; BB9FA9718834DC4E CRC64;
MFAGFDLGDA KTNWAEQIEE ELALPERSEE IVGDVKTVTE YHLNDENRRV KTVSRFKVSK
KRIPKSVLER RKWARFGQDA DMSLEDLMSK TTYYDDEITM QFLRSRTGEL LEFANSEFSG
LDTQRSTMQF RMCRFCKSMD HWSTQCPYRD VFEEEKAKEA AADAGAQSGG DLQSSRSGVY
IAPALRGLGA GSKLSMDPLQ RRDDNTVRVT NLPEDISDVV LKELFSQVGK VVRLYLARDK
VTQRCKGYAF VSYMSRADAQ KAIDELSGYK YEHLIFKVEW AKYEHKITQT AKYNTAYGMQ
RISMNSAVDT EPMVIPKEEE SFGRKASYTP AMKQAQTNRN KIHYDQNANI NSSIDSSRIA
SSHRSSKKKC IIFALYIILV LLLIILAIVL PLNLTSEDNP YAQLLFENDI TLNGSAMIHL
ANQSKPVNAS LIEKIELFCY EQFNSSNPCF ANFSTVEYAT DYFIPMLTNS VVNTKFCEQF
DCHLDTVEHV AIDEENVNFD FSVHLKLNGT KFSDFLSMST SEFMKNVISN FEKILDNRFR
DYHKNITIVL ELKQICQIFN IDCAKLFWEN IYSSASLKKE DDKSATFIMD WMSQFRPPVA
YKVCEEASGF VCRSDGKRIR QSKVCDGIKH CQDGSDEQAC EKCQTAYSCI NKDGSLTCIR
GKQVCDGQHK CYRALEFSKV CNTPKNDCKS PLYFPCADSS TCIPKEWVCD GEEHCPNGDD
ESPICEKDEC NNNAHWCNGR CIAQWKLCDG INDCHDKSDE MNCTCEQCSG DGILLCSGPV
GQCILENRVC DGRADCPNEE DERCLIEEEE PAKITCSSNS DHVSCKSCNI ENQFQCGNGL
CINRTEMCDN KKDCDDGSDE DDQLCSCDDS DGFFCKSNNE TKFSNCKPNS FRCDGFADCE
GETDETDCDS CFNNPKAFYC NVTRTCLPES SRCDGAVDCP DYSDEDFCSC SVCKSQKHST
YMCRERNRCL RAEYACNPSS KYHCPGEPSE DMILCPPAWK PLGVEDKKRE NFQNF
//
