EIF3D_NASVI
ID EIF3D_NASVI Reviewed; 558 AA.
AC K7IM66;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 1.
DT 25-MAY-2022, entry version 42.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit D {ECO:0000255|HAMAP-Rule:MF_03003};
DE Short=eIF3d {ECO:0000255|HAMAP-Rule:MF_03003};
DE AltName: Full=Eukaryotic translation initiation factor 3 subunit 7 {ECO:0000255|HAMAP-Rule:MF_03003};
OS Nasonia vitripennis (Parasitic wasp).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Parasitoida; Chalcidoidea;
OC Pteromalidae; Pteromalinae; Nasonia.
OX NCBI_TaxID=7425;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AsymCX;
RX PubMed=20075255; DOI=10.1126/science.1178028;
RG Nasonia Genome Working Group;
RA Werren J.H., Richards S., Desjardins C.A., Niehuis O., Gadau J.,
RA Colbourne J.K., Werren J.H., Richards S., Desjardins C.A., Niehuis O.,
RA Gadau J., Colbourne J.K., Beukeboom L.W., Desplan C., Elsik C.G.,
RA Grimmelikhuijzen C.J., Kitts P., Lynch J.A., Murphy T., Oliveira D.C.,
RA Smith C.D., van de Zande L., Worley K.C., Zdobnov E.M., Aerts M.,
RA Albert S., Anaya V.H., Anzola J.M., Barchuk A.R., Behura S.K., Bera A.N.,
RA Berenbaum M.R., Bertossa R.C., Bitondi M.M., Bordenstein S.R., Bork P.,
RA Bornberg-Bauer E., Brunain M., Cazzamali G., Chaboub L., Chacko J.,
RA Chavez D., Childers C.P., Choi J.H., Clark M.E., Claudianos C.,
RA Clinton R.A., Cree A.G., Cristino A.S., Dang P.M., Darby A.C.,
RA de Graaf D.C., Devreese B., Dinh H.H., Edwards R., Elango N., Elhaik E.,
RA Ermolaeva O., Evans J.D., Foret S., Fowler G.R., Gerlach D., Gibson J.D.,
RA Gilbert D.G., Graur D., Grunder S., Hagen D.E., Han Y., Hauser F.,
RA Hultmark D., Hunter H.C. IV, Hurst G.D., Jhangian S.N., Jiang H.,
RA Johnson R.M., Jones A.K., Junier T., Kadowaki T., Kamping A., Kapustin Y.,
RA Kechavarzi B., Kim J., Kim J., Kiryutin B., Koevoets T., Kovar C.L.,
RA Kriventseva E.V., Kucharski R., Lee H., Lee S.L., Lees K., Lewis L.R.,
RA Loehlin D.W., Logsdon J.M. Jr., Lopez J.A., Lozado R.J., Maglott D.,
RA Maleszka R., Mayampurath A., Mazur D.J., McClure M.A., Moore A.D.,
RA Morgan M.B., Muller J., Munoz-Torres M.C., Muzny D.M., Nazareth L.V.,
RA Neupert S., Nguyen N.B., Nunes F.M., Oakeshott J.G., Okwuonu G.O.,
RA Pannebakker B.A., Pejaver V.R., Peng Z., Pratt S.C., Predel R., Pu L.L.,
RA Ranson H., Raychoudhury R., Rechtsteiner A., Reese J.T., Reid J.G.,
RA Riddle M., Robertson H.M., Romero-Severson J., Rosenberg M., Sackton T.B.,
RA Sattelle D.B., Schluns H., Schmitt T., Schneider M., Schuler A.,
RA Schurko A.M., Shuker D.M., Simoes Z.L., Sinha S., Smith Z., Solovyev V.,
RA Souvorov A., Springauf A., Stafflinger E., Stage D.E., Stanke M.,
RA Tanaka Y., Telschow A., Trent C., Vattathil S., Verhulst E.C.,
RA Viljakainen L., Wanner K.W., Waterhouse R.M., Whitfield J.B., Wilkes T.E.,
RA Williamson M., Willis J.H., Wolschin F., Wyder S., Yamada T., Yi S.V.,
RA Zecher C.N., Zhang L., Gibbs R.A.;
RT "Functional and evolutionary insights from the genomes of three parasitoid
RT Nasonia species.";
RL Science 327:343-348(2010).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 172-537, AND DOMAIN.
RX PubMed=27462815; DOI=10.1038/nature18954;
RA Lee A.S., Kranzusch P.J., Doudna J.A., Cate J.H.;
RT "eIF3d is an mRNA cap-binding protein that is required for specialized
RT translation initiation.";
RL Nature 536:96-99(2016).
CC -!- FUNCTION: mRNA cap-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. In the
CC eIF-3 complex, eif3d specifically recognizes and binds the 7-
CC methylguanosine cap of a subset of mRNAs. {ECO:0000255|HAMAP-
CC Rule:MF_03003}.
CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex. {ECO:0000255, ECO:0000255|HAMAP-Rule:MF_03003}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255, ECO:0000255|HAMAP-
CC Rule:MF_03003}.
CC -!- DOMAIN: The RNA gate region regulates mRNA cap recognition to prevent
CC promiscuous mRNA-binding before assembly of eif3d into the full
CC eukaryotic translation initiation factor 3 (eIF-3) complex.
CC {ECO:0000305|PubMed:27462815}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit D family. {ECO:0000255,
CC ECO:0000255|HAMAP-Rule:MF_03003}.
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 RefSeq; XP_001605972.1; XM_001605922.4.
DR PDB; 5K4B; X-ray; 1.40 A; A/B=172-537.
DR PDB; 5K4C; X-ray; 1.70 A; A=172-537.
DR PDB; 5K4D; X-ray; 2.00 A; A/B=172-537.
DR PDB; 6W2T; EM; 3.36 A; 9=1-558.
DR PDBsum; 5K4B; -.
DR PDBsum; 5K4C; -.
DR PDBsum; 5K4D; -.
DR PDBsum; 6W2T; -.
DR AlphaFoldDB; K7IM66; -.
DR SMR; K7IM66; -.
DR STRING; 7425.NV10150-PA; -.
DR EnsemblMetazoa; XM_001605922; XP_001605972; LOC100122367.
DR GeneID; 100122367; -.
DR KEGG; nvi:100122367; -.
DR eggNOG; KOG2479; Eukaryota.
DR HOGENOM; CLU_024521_2_0_1; -.
DR InParanoid; K7IM66; -.
DR OMA; PDGWGPC; -.
DR OrthoDB; 1030308at2759; -.
DR PhylomeDB; K7IM66; -.
DR Proteomes; UP000002358; Unplaced.
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:0098808; F:mRNA cap binding; IDA:UniProtKB.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0002191; P:cap-dependent translational initiation; IEA:UniProtKB-UniRule.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR HAMAP; MF_03003; eIF3d; 1.
DR InterPro; IPR007783; eIF3d.
DR PANTHER; PTHR12399; PTHR12399; 1.
DR Pfam; PF05091; eIF-3_zeta; 1.
DR PIRSF; PIRSF016281; EIF-3_zeta; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Initiation factor; Protein biosynthesis;
KW Reference proteome; RNA-binding.
FT CHAIN 1..558
FT /note="Eukaryotic translation initiation factor 3 subunit
FT D"
FT /id="PRO_0000438132"
FT REGION 296..310
FT /note="RNA gate"
FT /evidence="ECO:0000269|PubMed:27462815"
FT REGION 534..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..550
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 180..186
FT /evidence="ECO:0007829|PDB:5K4B"
FT HELIX 187..192
FT /evidence="ECO:0007829|PDB:5K4B"
FT STRAND 202..210
FT /evidence="ECO:0007829|PDB:5K4B"
FT HELIX 215..219
FT /evidence="ECO:0007829|PDB:5K4B"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:5K4B"
FT HELIX 244..249
FT /evidence="ECO:0007829|PDB:5K4B"
FT TURN 250..252
FT /evidence="ECO:0007829|PDB:5K4B"
FT STRAND 255..259
FT /evidence="ECO:0007829|PDB:5K4B"
FT HELIX 260..267
FT /evidence="ECO:0007829|PDB:5K4B"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:5K4B"
FT STRAND 276..283
FT /evidence="ECO:0007829|PDB:5K4B"
FT STRAND 286..290
FT /evidence="ECO:0007829|PDB:5K4B"
FT STRAND 293..296
FT /evidence="ECO:0007829|PDB:5K4B"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:5K4B"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:5K4B"
FT HELIX 320..337
FT /evidence="ECO:0007829|PDB:5K4B"
FT HELIX 357..362
FT /evidence="ECO:0007829|PDB:5K4B"
FT STRAND 365..374
FT /evidence="ECO:0007829|PDB:5K4B"
FT STRAND 380..391
FT /evidence="ECO:0007829|PDB:5K4B"
FT STRAND 399..409
FT /evidence="ECO:0007829|PDB:5K4B"
FT TURN 411..415
FT /evidence="ECO:0007829|PDB:5K4B"
FT HELIX 419..437
FT /evidence="ECO:0007829|PDB:5K4B"
FT HELIX 439..452
FT /evidence="ECO:0007829|PDB:5K4B"
FT STRAND 455..466
FT /evidence="ECO:0007829|PDB:5K4B"
FT STRAND 469..481
FT /evidence="ECO:0007829|PDB:5K4B"
FT HELIX 483..489
FT /evidence="ECO:0007829|PDB:5K4B"
FT HELIX 494..509
FT /evidence="ECO:0007829|PDB:5K4B"
FT STRAND 513..520
FT /evidence="ECO:0007829|PDB:5K4B"
FT STRAND 524..531
FT /evidence="ECO:0007829|PDB:5K4B"
SQ SEQUENCE 558 AA; 64430 MW; 19407BBDA6605ED3 CRC64;
MANDENTDGV NKSEKMEKMC EFIRPMVQNN PDGWGPCELP DQFKDIPYQP FSKSDRLGKI
SDWTGTAYQD KKFQNKYNSQ FGGSGMKAYA YEHDEDETTF HLVDTTRVQK PPYQRGRFGQ
RNQRMRGRGG QRGGMSQMQA LGKLKIHERD RRGQNKRWTR RNQAPIKMRD ASVTVRPDWV
TIEEMDFPRL SKLTLPGVKE GEDVLCCGAV EYYDKSYDRV NVKNEKPLQR IDRIFHTVTT
TDDPVIRKLS KTEGNVYATD AILATIMCCT RSNYSWDIVI EKIGNKLFFD KRDNTEFDLL
TVNETSVEPP QDDGNSLNSP RNLALEATFI NHNFSQQVLK SNEPRYKFDE PNPFISEEEE
GEVASVAYRY RKWDLNNGIT LIARCEHDAV MQGPNNETQF LTIKALNEWD SKLANGVEWR
RKLDTQRGAV LANELRNNAC KLAKWTVQAL LAGSDQLKFG YVSRASVRDS SKHVILETQQ
YKPNEFATQI NLNMDNAWGI LRCIIDICMN QKDGKYLIMK DPNKPMIRLY DIPDNTFESE
GEEEDSDEEE QVKDAFQR
