ID A0A1E4T1K5_9ASCO Unreviewed; 976 AA.
AC A0A1E4T1K5;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=CANARDRAFT_23162 {ECO:0000313|EMBL:ODV85635.1};
OS [Candida] arabinofermentans NRRL YB-2248.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Ogataea; Ogataea/Candida clade.
OX NCBI_TaxID=983967 {ECO:0000313|EMBL:ODV85635.1, ECO:0000313|Proteomes:UP000094801};
RN [1] {ECO:0000313|Proteomes:UP000094801}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL YB-2248 {ECO:0000313|Proteomes:UP000094801};
RG DOE Joint Genome Institute;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Submitted (APR-2016) 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}.
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DR EMBL; KV453852; ODV85635.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E4T1K5; -.
DR STRING; 983967.A0A1E4T1K5; -.
DR OrthoDB; 10990at2759; -.
DR Proteomes; UP000094801; 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|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 Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_03000};
KW Reference proteome {ECO:0000313|Proteomes:UP000094801};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_03000}.
FT DOMAIN 342..519
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT REGION 869..942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 954..976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 588..660
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03000"
FT COILED 787..854
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03000"
SQ SEQUENCE 976 AA; 111161 MW; 478063208FD8354D CRC64;
MAPSHIIRPE NILRRAEDLI AVDQRDAALQ TLYDFVTSKR TRSLLPVDLE PIAILFVTLG
VELRNGKLVK DGLHQYKKNV QANEKGLSSV ENVTKKFLEI AESKLNEAQS KADAANAAYD
ADQFHDDVDE DDDDDESSPI TISPEDILMS TVSTDDTKDR SDRELVVPWL KFLWEAFRTV
LDILRNNSKL EIAYASVVSS AFQFCVKYNR KAEFRRLCEM LRTHLQSVSQ KPLYNKQIIE
HPIDLSDPET LQRYLETRFN QLNVSVKLEL WQESFRSVED VHTLMSVSKR QPKPAMMINY
YENLAKIFAV SENHLFHAAA RERFFSLFVQ SPIATEDELK HFASLQLLSA LSVQQINESS
IFAGDDFNKR KNHRLASLLN LSRVPTRESL LAQILSKDLL TIVDPILVKL YNLLEDNFHP
LSFSKNVKDI FAEIELNKDY KSYIKPLLTV VLNKLFEQVS EVYETVKLDF LIKLATFEGE
FKLSSIEIQS YLLNAASSNI LSAKIDHESK VVAFKSDPFD ESLSYTDSTS ISNSLQLSPS
ELIRYQLSSL AKTLSSSVKL IDPSIKESEI ALRDRSLKAA QEEFDLEREA LLKRSELLEA
KQKEIEELKR IEEEEAAKAK IEKQIAMRKA EQERMEIENA KRAEEKKAKL LEAIKIAEKQ
KLINDVNSQG IITLDINEVE NIDAQAIRQM QVEKLDQDRK ALDERNEVTY KRIDYLERAQ
RQYELTFLQK DAEEQKGKEL EIYQSLKSKL TEKAKKEHEQ AIQIRDRLKR VVPDYKSFVD
ELKSKSHVAY LEEKKLVEEK LQAAKDARIA EFIAKKKAEF EAAQKLEQAK IAAEKAREAE
LERIKKEEEE FEAKWKTLSP VEKIQYRKMG KVPASQRAIP GTAPAPMRSS PIPSAASSTP
MRGEFARGGY GSSAPAPAPG PMRGGFGSSS SSPAASAASG IDAERAEYER LKAAEADGSL
KFNQRRRFKE LTQKFA
//
