ID A0A2H3HKA6_FUSOX Unreviewed; 1056 AA.
AC A0A2H3HKA6;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=AU210_006636 {ECO:0000313|EMBL:PCD38153.1};
OS Fusarium oxysporum f. sp. radicis-cucumerinum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=327505 {ECO:0000313|EMBL:PCD38153.1, ECO:0000313|Proteomes:UP000219602};
RN [1] {ECO:0000313|EMBL:PCD38153.1, ECO:0000313|Proteomes:UP000219602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Forc016 {ECO:0000313|EMBL:PCD38153.1,
RC ECO:0000313|Proteomes:UP000219602};
RX PubMed=27387256; DOI=10.1111/1462-2920.13445;
RA van Dam P., Fokkens L., Schmidt S.M., Linmans J.H., Kistler H.C., Ma L.J.,
RA Rep M.;
RT "Effector profiles distinguish formae speciales of Fusarium oxysporum.";
RL Environ. Microbiol. 18:4087-4102(2016).
RN [2] {ECO:0000313|EMBL:PCD38153.1, ECO:0000313|Proteomes:UP000219602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Forc016 {ECO:0000313|EMBL:PCD38153.1,
RC ECO:0000313|Proteomes:UP000219602};
RX PubMed=28831051; DOI=10.1038/s41598-017-07995-y;
RA van Dam P., Fokkens L., Ayukawa Y., van der Gragt M., Ter Horst A.,
RA Brankovics B., Houterman P.M., Arie T., Rep M.;
RT "A mobile pathogenicity chromosome in Fusarium oxysporum for infection of
RT multiple cucurbit species.";
RL Sci. Rep. 7:9042-9042(2017).
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:PCD38153.1}.
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DR EMBL; MABQ02000004; PCD38153.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3HKA6; -.
DR STRING; 327505.A0A2H3HKA6; -.
DR OrthoDB; 10990at2759; -.
DR Proteomes; UP000219602; Chromosome 5.
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 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:UP000219602};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_03000}.
FT DOMAIN 339..523
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT REGION 529..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 819..1056
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 607..673
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03000"
FT COMPBIAS 819..903
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 918..945
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1056 AA; 120246 MW; 37A42CD67DB8A1FA CRC64;
MPPPPHQKPE NVLKRAHELI GVGQAPAALT LLHEHITNKR SRNVPIMSLE PVMLLLVELS
VEQKKGKLAK DALYQYKNIS QNTNIATIEL VLKKFIELAV EKVTAAQQKA DEVQESIDAT
AGTSNIDDLE ATETPESILL ATVSGEQSRD RTDRAIVTPW LKFLWEAYRT VLDILRNNAR
LEILYQSTAT QAFDFCLKYT RKTEFRRLCE LLRNHVQTAA KYSSQMHAIN LSDPDTLQRH
LETRFQQLNV AVELELWQEA FRSVEDVHTL LSLSKRPPKN VMMANYYEKL TRIFLVGENY
LFHAAAWSRY YTLLRQSSVL VATGQGKKAD NPPASDAELQ KAASFVVLSA LAIPVISTSR
SRGAMVDFDE ARRNKNSRLT HLLGMSQAPT RARLFRDALS KSLLQRARPE IRELYEILEV
DFHPLSICQK ISPILTKIGA DSEMEKYILP LQQVILTRLF QQLSQVYETV DLSFVESLAQ
FPEPYQVTRG TIEKFIMNGN KKGDLSVRMA HATGVLSFDN DVFSSSKASH GGSSAGSAES
ETGTVQRLQS TPSEIVRSQL TRLAKSLFTT CHYVDPGFNK GRLEAREAAL ARAKAGAEEE
HLAILSRKDL IQKRKEVASE IQAKKEKENA RQKRLREQAL QEAEDLRLAN EQKEREAKRL
KAERDRVRKE ELKKQIADLK IGDKAIDIDL EDLDNLDSNR LRAMKLAQLE REKNDVNERL
RITGKRLDHL ERAFRKEEAK KLHEDYAKQI EQDRKIYETV KAQTLKDAEQ KHKESVELKH
RLSRLVPQYE EFRDSLHDRR RDEFEKRRRD AERELEKQIA QRKKEVRDRR LREKREREEK
ERELREAEER AAREKEEQRI RDEARKEELA KLKEQREKER QEMLEKAALQ QRREEEALAR
RKAEKAQGAG GFSRGPERTD SSEGRRPPVF GAGKWREREA ANRDAGDAPP SRAPPAERSG
SNDRPSAGGP PKLNLSGGKP SWREREAAKQ AAGGGADAGS SAPPPRFAPR GGAPPMDRSG
SGRAEEDRKQ SPAPPAESQP ASRTAGKWVP PHMRNK
//
