ID A0A5J5F8B1_9PEZI Unreviewed; 1052 AA.
AC A0A5J5F8B1;
DT 11-DEC-2019, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
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 ORFNames=FN846DRAFT_930417 {ECO:0000313|EMBL:KAA8913279.1};
OS Sphaerosporella brunnea.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Pyronemataceae; Sphaerosporella.
OX NCBI_TaxID=1250544 {ECO:0000313|EMBL:KAA8913279.1, ECO:0000313|Proteomes:UP000326924};
RN [1] {ECO:0000313|EMBL:KAA8913279.1, ECO:0000313|Proteomes:UP000326924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sb_GMNB300 {ECO:0000313|EMBL:KAA8913279.1,
RC ECO:0000313|Proteomes:UP000326924};
RG DOE Joint Genome Institute;
RA Benucci G.M., Marozzi G., Antonielli L., Sanchez S., Marco P., Wang X.,
RA Falini L.B., Barry K., Haridas S., Lipzen A., Labutti K., Grigoriev I.V.,
RA Murat C., Martin F., Albertini E., Donnini D., Bonito G.;
RT "Draft genome of the ectomycorrhizal ascomycete Sphaerosporella brunnea.";
RL Submitted (SEP-2019) 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.
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}.
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:KAA8913279.1}.
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DR EMBL; VXIS01000016; KAA8913279.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5J5F8B1; -.
DR InParanoid; A0A5J5F8B1; -.
DR Proteomes; UP000326924; 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: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; -; 2.
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|HAMAP-Rule:MF_03000};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03000};
KW Initiation factor {ECO:0000256|HAMAP-Rule:MF_03000};
KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_03000};
KW Reference proteome {ECO:0000313|Proteomes:UP000326924};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_03000}.
FT DOMAIN 331..515
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT REGION 521..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 788..883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 903..1052
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 571..721
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03000"
FT COMPBIAS 970..993
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1029..1052
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1052 AA; 119405 MW; 2ACCD70F2DBE81E8 CRC64;
MPPPPHAKPE NVLKRAQELV AVNKNLGALE LLHDHVTSKR TRNSPIASLE PVMILFVELC
VSLRKGKTAK DGLYQYKNIA QNTSVQTIEL VLKRFIELAE AKVTEAQERA EQIALDQIED
LEASETPESI LLSTVSGEQS KDRTDRAVVT PWLKFLWETY RTVLDILRNN ARLETMYQST
ALQAFQFCLK YTRKTEFRRL CELLRNHVQN AAKYASQMHA INLNDPDTLQ RHLDTRFQQL
NVAVELELWQ EAFRSVEDIH TLLNLSKRPA KNIMMANYYQ NLTRIFLVSD NYLFHAAAWS
RYYNLLRSSA AQVASGQALK KDSPSTTDAD WTRVSSLYLL AALSIPVISQ ARSKGALLDV
DEAKRTKNTR LTNLLGLAKA PTRASLFKDI LNKGLLKRAR PEIRDLYTIL EVDFHPLSIC
KKISPILVQI ANDPDMEPYV QPLQQVILTR LFQQLSQVYD SVQLSFVLEL ASFPSPFEIT
PTVIEKFIMN GCKKGDLSIR IDHSAGVLTF ESDIFSTTKA LHPGSGAGSA EKDTSVQKLQ
STPSEIVRTQ LSRLAKAMYL TCTHVDPTFL AEREEAKAAS QQRALAGAQK EHAETLARRN
IIEKKKELAE ATLLKKEKEE AQFRAARVEE ARLAEAARIA DQQKKRELER VKAEQERIRK
EELKKQVEEL ALDTKIDLEN IGDLDSNQIR LLKLQQLEKE KRQMSERLHQ TGKRIDHLER
AYRREEVKVL PQDWERQKAE DLAAYEAAKK ITLDAAKAQH EEAVALKNRL GRLVGAYEAF
RDEIKQQRSQ EFEQRRKAAE RELQKAMEKR RKDVRERSER KRREKEAEEE RIRLQKEKEE
REAREAQERR ILEEKEKARR DAEHREAMIK LKEERKAADE KAAIQRQREI EAEERLVARR
LAAAAAATPA AASSDEGRWR TGAAGGRPLW RDREAAKVAA GGAAPPPEPA AAPAGERRRL
NLAPRTLPRE EQPVAPPAPS VQDATPSPPP AAETKPSGGA YRPPARRGPE RSDTPPSGGG
GRWVPPARRG NGEGEKKDNR DQKPRATGDK WR
//
