ID W0T8B2_KLUMD Unreviewed; 926 AA.
AC W0T8B2;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit A {ECO:0000256|HAMAP-Rule:MF_03000};
DE Short=eIF3a {ECO:0000256|HAMAP-Rule:MF_03000};
DE AltName: Full=Eukaryotic translation initiation factor 3 110 kDa subunit homolog {ECO:0000256|HAMAP-Rule:MF_03000};
DE Short=eIF3 p110 {ECO:0000256|HAMAP-Rule:MF_03000};
DE AltName: Full=Translation initiation factor eIF3, p110 subunit homolog {ECO:0000256|HAMAP-Rule:MF_03000};
GN Name=TIF32 {ECO:0000256|HAMAP-Rule:MF_03000,
GN ECO:0000313|EMBL:BAO39847.1};
GN ORFNames=KLMA_30552 {ECO:0000313|EMBL:BAO39847.1};
OS Kluyveromyces marxianus (strain DMKU3-1042 / BCC 29191 / NBRC 104275)
OS (Yeast) (Candida kefyr).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=1003335 {ECO:0000313|EMBL:BAO39847.1, ECO:0000313|Proteomes:UP000065495};
RN [1] {ECO:0000313|EMBL:BAO39847.1, ECO:0000313|Proteomes:UP000065495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DMKU3-1042 / BCC 29191 / NBRC 104275
RC {ECO:0000313|Proteomes:UP000065495};
RX PubMed=25834639; DOI=10.1186/s13068-015-0227-x;
RA Lertwattanasakul N., Kosaka T., Hosoyama A., Suzuki Y., Rodrussamee N.,
RA Matsutani M., Murata M., Fujimoto N., Suprayogi, Tsuchikane K., Limtong S.,
RA Fujita N., Yamada M.;
RT "Genetic basis of the highly efficient yeast Kluyveromyces marxianus:
RT complete genome sequence and transcriptome analyses.";
RL Biotechnol. Biofuels 8:47-47(2015).
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.
CC {ECO:0000256|HAMAP-Rule:MF_03000}.
CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex. {ECO:0000256|HAMAP-Rule:MF_03000}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03000}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit A family. {ECO:0000256|HAMAP-
CC Rule:MF_03000}.
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DR EMBL; AP012215; BAO39847.1; -; Genomic_DNA.
DR AlphaFoldDB; W0T8B2; -.
DR VEuPathDB; FungiDB:KLMA_30552; -.
DR OrthoDB; 10990at2759; -.
DR Proteomes; UP000065495; Chromosome 3.
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: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 Gene3D; 1.25.40.860; -; 1.
DR Gene3D; 4.10.860.10; UVR domain; 1.
DR HAMAP; MF_03000; eIF3a; 1.
DR InterPro; IPR027512; EIF3A.
DR InterPro; IPR000717; PCI_dom.
DR PANTHER; PTHR14005:SF0; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT A; 1.
DR PANTHER; PTHR14005; EUKARYOTIC TRANSLATION INITIATION FACTOR 3, THETA SUBUNIT; 1.
DR Pfam; PF01399; PCI; 1.
DR SMART; SM00088; PINT; 1.
DR PROSITE; PS50250; PCI; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|HAMAP-
KW Rule:MF_03000}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03000};
KW Initiation factor {ECO:0000256|HAMAP-Rule:MF_03000,
KW ECO:0000313|EMBL:BAO39847.1};
KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_03000};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_03000}.
FT DOMAIN 322..496
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT REGION 506..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 792..812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 833..926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 588..660
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03000"
FT COMPBIAS 511..531
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 833..876
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 877..895
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 911..926
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 926 AA; 107741 MW; 0466B63A4D89B6B2 CRC64;
MAPPALRPEN AIRRADELVS VGEPMAGLQS LFDLLSSRRS RFADAATLEP IIFKFLELGV
ELRKGKMIKE GLYQYKKHMQ HTTEGLHSVG AVARKFIDLI EKKMTTVQAQ ADAKDQANEA
DDDLEGGVTP ENLLVSVYEQ EQTVGGFNND DVSAWLRFTW ESYRTTLDFL RNNSQLEITY
AGVVNRTMQF CYKYNRKNEF KRLAEMLRQH LDAANYQQQR YGHHTVDLSD ADTLQRYSDQ
RFQQVNVSVK LELWHEAFRS IEDVHHLMRI AKRPPKPSVL ANYYENLAKI FFVSGNYLLH
AAAWEKFYNL YLKNPNATDE DFKFYASQFL LSALAIQLDD LPIAGFDPQI RLCDLLDLES
KPKRKDLIAA ATDSKILEKA DPEILKFFDI LETNFNVRTV KDQLSELLPK LQDKPYFAQY
VTPLRNLFIR RSIIEVAKEQ TSIHLVELHE LLSLPAPFEL SVFELEKYLI QAAMDDYVSI
TIDHETDTVT FAQDPFDAWQ ASLVETASDE TKENDSEEET QEGSEESSEE EQVEQVFTRN
SEVRSKLTDL SKILKANEEY EKGSYYLRVK LVREELVRQK EEVIKREKEA AEIRAKNNAE
RKKRNEEEKK LAAKRAMEER HRRMIEEKAA VESSMEKEAE RRAQEMMERE REAIHEQEMK
KLIEETNANG VIYIDPKEAK NMTSEKINQM VIEQVAKNKK DMTERMTFAF KRLDHLERAY
RQMELPLLEK DAQQQKDRDM ENYEAFKKKL IESAKADFEK KLELHNRLNK IYGSFKEYRT
AVSKAKKEQI EQEKELKKSQ LEEAKKQRIE QVRKERYEAK VAEIKAAIEA EEQRKEALAK
EAELEKRRAE RDRINRERDE IARKQREIEE LLEKKNSASR ASASPIPARA SPSPAASTST
PPPSNKPMSM AEKLRLKRMQ KEAGRG
//
