ID A0A2S7PP12_9HELO Unreviewed; 1099 AA.
AC A0A2S7PP12;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=CJF32_00004913 {ECO:0000313|EMBL:PQE16022.1};
OS Rutstroemia sp. NJR-2017a WRK4.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Rutstroemiaceae; Rutstroemia.
OX NCBI_TaxID=2070412 {ECO:0000313|EMBL:PQE16022.1, ECO:0000313|Proteomes:UP000238813};
RN [1] {ECO:0000313|EMBL:PQE16022.1, ECO:0000313|Proteomes:UP000238813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJR-2017a WRK4 {ECO:0000313|EMBL:PQE16022.1,
RC ECO:0000313|Proteomes:UP000238813};
RA Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL Submitted (JAN-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:PQE16022.1}.
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DR EMBL; NJPR01000111; PQE16022.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S7PP12; -.
DR STRING; 2070412.A0A2S7PP12; -.
DR InParanoid; A0A2S7PP12; -.
DR OrthoDB; 10990at2759; -.
DR Proteomes; UP000238813; 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 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:PQE16022.1};
KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_03000};
KW Reference proteome {ECO:0000313|Proteomes:UP000238813};
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..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 828..866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 886..1099
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..911
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1037..1076
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1099 AA; 125294 MW; 9C7B5CB59B3AFBCE CRC64;
MPPPPHQKPE NVLKRAHELM GVGQSQAALV LLHEHVTSKR SRNAPITSLE PVMLLLVEQS
VEQKKGKLAK DALYQYKNIS QNTNVGTIEL VLKKFIELAE EKVKTAQAKA DEVQSTLDTT
AATASVDDLE ATETPESILL STVSGEQSRD RTDRAIVTPW LKFLWETYRT VLDILRNNAR
LEIMYQSTAM QAFEFCQKYT RKTEFRRLCE LLRNHVQTAA KYSAQMHAIN LNDPDTLQRH
LETRFQQLNV AVELELWQEA FRSVEDIHTL LNLSKRPPKN VMMANYYEKL TRIFLVGENY
LFHAAAWSRY YNLLRQSAQM VAAGTSKKSD NPATSEADLS KAASFVLLSA LAIPVISTSR
SRGALVDIDE QKKNKNSRLT HLLGMAQAPT RAVLFKDAMS KGLLKRARPE IRELYNILEV
DFHPLSICQK ISPILSQVGA DAEMEKYVLP LQQVILTRLF QQLSQVYETV DLNFVENLAK
FPEPFQVTRD TIEKFIMNGN KKGDLAIRMD HATGVLSFDT DVFSSSKAVH AGSGAGSAES
ETTSVQRLQN TPSEIVRTQL TRLAKSLFVT CQYIDPSFNE ARIKAREEAY ARAKAGADEE
HREILARKQT IQKRKEEASE IQSRKEKEEA TKKRIKAAQL QEAEDKRLAA EQKKREDDRL
KAELERVRRA ELQKQIDDLK LGTKALDIDL SNLDNLDANQ IRAMKLAQLE REKNDINEKL
RITGKRIDHL ERAFRKEEAK KLPEDYEAQR KRDLEAYEKI KAQTLKEAEA KHKENVELKH
RLTRLVPFYE SFREIIVERR HEEFDKRRRD AEKELEKQIA LRRKEFKERK VREKREREER
ERALREEEER AAKEAEEKAA REEQKRREFA ELKAIREKER QEALEMAALQ ERRAEEAAKR
RAEEKARGPI RGAAPIERTE SSEGSRRPPL PLAGAKMGWR EKEKLRAEGK EVPSSSPAPP
AGRTESPMAK ASPMGRAAPT MERTESNDRP SGPPRLALAG SKPSWRDREA AKNASGGGDS
APSSSRGPPP SERAPAYRGR PGRDQEPRDA RDSRDSREPR EPREPREPRE ERPAPSGESL
KPSGGAGKFV PPHLRNKQT
//
