ID A0A427YCI4_9TREE Unreviewed; 976 AA.
AC A0A427YCI4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
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:RSH88773.1};
GN ORFNames=EHS25_003001 {ECO:0000313|EMBL:RSH88773.1};
OS Saitozyma podzolica.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Trimorphomycetaceae; Saitozyma.
OX NCBI_TaxID=1890683 {ECO:0000313|EMBL:RSH88773.1, ECO:0000313|Proteomes:UP000279259};
RN [1] {ECO:0000313|EMBL:RSH88773.1, ECO:0000313|Proteomes:UP000279259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27192 {ECO:0000313|EMBL:RSH88773.1,
RC ECO:0000313|Proteomes:UP000279259};
RA Aliyu H., Gorte O., Ochsenreither K.;
RT "Genome sequence of Saitozyma podzolica DSM 27192.";
RL Submitted (NOV-2018) 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:RSH88773.1}.
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DR EMBL; RSCD01000016; RSH88773.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A427YCI4; -.
DR STRING; 1890683.A0A427YCI4; -.
DR Proteomes; UP000279259; 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; -; 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 SMART; SM00088; PINT; 1.
DR PROSITE; PS50250; PCI; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03000};
KW Initiation factor {ECO:0000256|HAMAP-Rule:MF_03000,
KW ECO:0000313|EMBL:RSH88773.1};
KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_03000};
KW Reference proteome {ECO:0000313|Proteomes:UP000279259};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_03000}.
FT DOMAIN 315..491
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT REGION 554..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..857
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..926
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 976 AA; 109013 MW; 0F35090237A880CA CRC64;
MPPIYVKPEN ALKRSEELLA LGTPQSQQQA FENLVEVFQS KRFKHTPVPV LEPIMNKFID
LCVSMSRKSH IRAGLLNYRN AVQSTSIQSI ENALNHFIAK AEERLAVATE QAKQEVAALP
ETPVVDDELP LQPASLLLDT FVDSAGDRER IERRLIAPAQ KFCWDAYDIC LDVAKGNDRL
EVVYQSIAHR AFNFCKVHQR KTDFRRLCEQ RLRKDLANAA KYAHQQHAVN LADPETLSRH
LDTRFLQLET AVELELWQEA FRSVEDVHGL VAGKKSAKPS MMANYYEKLT QIFKAEGGKQ
TAVFHAAAWA RYFQYAERAG SVPEKASGCV LLSALAVPLG DVESKQRLVA LLNLPKMPTR
DALVKDAAAK HLRRVPQEIR QLYNILEVDF QPLKASKLLA PVISSLPAEY QSYLPALRDV
VLSRLLQELS QVYDTVTLSH VLDLVKPFDG TAWATDMPAL EKFLMTAARR GDINASVDHV
AQSISFVTKT TDVNRLSNLA VCLYNTIQYL NPAPTTTRAE AFAQAIAQAE EERKAVAQRR
QIVTKRRELL EEANARRERE ETTAKAERQK QIAEENARRE KELARQGEID RLQKQMDATR
REEARKLAES LAATGALKID MSKVEDLDSN EVLALQVQQL DKEKRDLNDR LRIVGKRVDH
LERAMRKEER HLLADDYERQ KQTDKVSHEQ ANKVAREIAI AQNQAAKELK ERLARMLPDY
LEARKEVESQ REVEFQQARE AAQRKIEEEK AKFRASVIAR RKADRERREQ ERLREEEEER
LAKERAEAEA AAAAQEEQRE AEARAEIEKR NAEAAERAAK QRAERDAERA AAAEAARKQR
EREEEAERRR AERASGGGAY RRPEPPAAAA ATSTSPAPVA PTAVKAGGWR DRLAAKQAGG
GEPSPASPAG PSPTTSPAPA PAPANGTTSP APAQGEAAPE RGVFRPGRGS WSARGRGGGS
TPPTSTRGGA AGGSRW
//
