ID   EIF3H_NEMVE             Reviewed;         332 AA.
AC   A7SA47;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Eukaryotic translation initiation factor 3 subunit H {ECO:0000255|HAMAP-Rule:MF_03007};
DE            Short=eIF3h {ECO:0000255|HAMAP-Rule:MF_03007};
GN   ORFNames=v1g168210;
OS   Nematostella vectensis (Starlet sea anemone).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC   Edwardsiidae; Nematostella.
OX   NCBI_TaxID=45351;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CH2 X CH6;
RX   PubMed=17615350; DOI=10.1126/science.1139158;
RA   Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA   Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA   Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA   Technau U., Martindale M.Q., Rokhsar D.S.;
RT   "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT   genomic organization.";
RL   Science 317:86-94(2007).
CC   -!- FUNCTION: Component of the eukaryotic translation initiation factor 3
CC       (eIF-3) complex, which is involved in protein synthesis of a
CC       specialized repertoire of mRNAs and, together with other initiation
CC       factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S
CC       ribosome. The eIF-3 complex specifically targets and initiates
CC       translation of a subset of mRNAs involved in cell proliferation.
CC       {ECO:0000255|HAMAP-Rule:MF_03007}.
CC   -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC       (eIF-3) complex. {ECO:0000255|HAMAP-Rule:MF_03007}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03007}.
CC   -!- SIMILARITY: Belongs to the eIF-3 subunit H family. {ECO:0000255|HAMAP-
CC       Rule:MF_03007}.
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DR   EMBL; DS469607; EDO39430.1; -; Genomic_DNA.
DR   RefSeq; XP_001631493.1; XM_001631443.1.
DR   AlphaFoldDB; A7SA47; -.
DR   SMR; A7SA47; -.
DR   STRING; 45351.EDO39430; -.
DR   MEROPS; M67.971; -.
DR   PRIDE; A7SA47; -.
DR   EnsemblMetazoa; EDO39430; EDO39430; NEMVEDRAFT_v1g168210.
DR   GeneID; 5511049; -.
DR   KEGG; nve:5511049; -.
DR   eggNOG; KOG1560; Eukaryota.
DR   HOGENOM; CLU_044094_0_0_1; -.
DR   InParanoid; A7SA47; -.
DR   OMA; KFNRYQQ; -.
DR   OrthoDB; 976469at2759; -.
DR   PhylomeDB; A7SA47; -.
DR   Proteomes; UP000001593; Unassembled WGS sequence.
DR   GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IBA:GO_Central.
DR   GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; IBA:GO_Central.
DR   GO; GO:0042788; C:polysomal ribosome; IBA:GO_Central.
DR   GO; GO:0070122; F:isopeptidase activity; IEA:InterPro.
DR   GO; GO:0140492; F:metal-dependent deubiquitinase activity; IEA:InterPro.
DR   GO; GO:0008237; F:metallopeptidase activity; IBA:GO_Central.
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; cd08065; MPN_eIF3h; 1.
DR   HAMAP; MF_03007; eIF3h; 1.
DR   InterPro; IPR027524; eIF3h.
DR   InterPro; IPR045810; eIF3h_C.
DR   InterPro; IPR000555; JAMM/MPN+_dom.
DR   InterPro; IPR037518; MPN.
DR   PANTHER; PTHR10410:SF3; PTHR10410:SF3; 1.
DR   Pfam; PF19445; eIF3h_C; 1.
DR   Pfam; PF01398; JAB; 1.
DR   SMART; SM00232; JAB_MPN; 1.
DR   PROSITE; PS50249; MPN; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Initiation factor; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..332
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   H"
FT                   /id="PRO_0000365195"
FT   DOMAIN          18..153
FT                   /note="MPN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   REGION          251..285
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        251..265
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        266..281
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   332 AA;  38086 MW;  C873FAD422071762 CRC64;
     MAEGRSSKNS PSGQIDIVQV DGLTVLKIIK HCEEEGSSGD LVQGVLLGLI QDNRLEITNC
     FPFPSNKAGD DEDDDDVNYQ MEVMRRLRAV NIDHLHVGWY QSTYLGSYIN RTLLDSQYSY
     QKSIEESVVL IYDPLRTSQG MLTLKAFRLS DEMMKLYKDG EFSADKLSKA GISFHSMFQE
     IPLVIKNSSL MNVLLCELDE NTPTPSADQF LTLSTGSYLE KNVRVLMESV DELCQDSNKY
     HNYQRSVIRQ QQQKENYLQR RQQENQSRIQ RGEDPLPDED LSKMFKPLPV PSRLDNLLLS
     EQVNTYCQHV HQFSTQSFGK FFLAQALQDK KE