GenomeNet

Database: UniProt
Entry: A0A094HPN5_9PEZI
LinkDB: A0A094HPN5_9PEZI
Original site: A0A094HPN5_9PEZI 
ID   A0A094HPN5_9PEZI        Unreviewed;      1224 AA.
AC   A0A094HPN5;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 44.
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=V498_07573 {ECO:0000313|EMBL:KFY86207.1};
OS   Pseudogymnoascus sp. VKM F-4517 (FW-2822).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420911 {ECO:0000313|EMBL:KFY86207.1, ECO:0000313|Proteomes:UP000029270};
RN   [1] {ECO:0000313|EMBL:KFY86207.1, ECO:0000313|Proteomes:UP000029270}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4517 (FW-2822) {ECO:0000313|Proteomes:UP000029270};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) 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:KFY86207.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JPKA01002113; KFY86207.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094HPN5; -.
DR   HOGENOM; CLU_002096_2_1_1; -.
DR   Proteomes; UP000029270; 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   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_03000}.
FT   DOMAIN          496..680
FT                   /note="PCI"
FT                   /evidence="ECO:0000259|PROSITE:PS50250"
FT   REGION          136..164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          783..814
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          964..1224
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          252..279
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03000"
FT   COMPBIAS        143..159
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        964..980
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        988..1058
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1186..1200
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1224 AA;  138282 MW;  FCCB41E06815EAAE CRC64;
     MYPDFQPTTL ICCAGHANPL SHVCTDSVAV DIGCGGHPAT EEENQKNNRL VVQFGRCQIQ
     NALDCMRPSR DVRCCVVEVI VAPAVSKVRG LRFNWTGKRG IFERCKRVGR IEQLNSFDRW
     PEIRCAYSLT LSGSTPHPEL QKLESKAAQH HDKTAKMPPP PHQKPENVLK RAHELMGVGQ
     SSAALVLLHE HITSKRSRNV PIASLEPVML LLVEQSVEQK KGKLAKDALY QYKNISQNTN
     VGTIELVLKK FIELAENKVQ EAQAKADEIQ STLETTQATA SVDDLEASET PESILLSTVS
     GEQSRDRTDR AIVTPWLKFL WETYRTVLDI LRNNARLEIM YQSTAMQAFA FCQKYARKTE
     FRRLCELLRN HVQTAAKYST QQMHAINLND PDTLQRHLET RFQQLNVAVE LELWQEAFRS
     VEDIHTLLNL SKRPPKNIMM ANYYEKLTRI FLVGENYLFH AAAWSRYYNL LRQSAAIVAS
     GQGKKSENPA ASEADLTKAA SFVLLSALAI PVISTSRSRG ALIDVDQAKN NKNSRLTHLL
     GMSAAPTRAV LFKDAMSKGL LSRARPEIRA LYNILEVDFH PLSICQKISP ILAKIGADEE
     MAKYIAPLQQ VILTRLFQQL SQVYETVDVK FVENLARFPA PFDVSRDTIE KFIMNGNKKG
     DLAIRLDHAT GVLSFDTDVF SSAKAVHTGS AAGSAESESQ SVQRLQSTPS EIVRTQLTRL
     AKSLYVTCQY VDPSYNQARV KARDTALAKA KAGAEQEHQE TLARKEIIHK RKEAANEIIA
     RKEKEDATKK KIRAAQLQEA EDKRLAQEQK EREEKRMKAE LDRVRKDELK KQIADLKIGT
     KALDIDLEDL DNLDGNRLRA MKLAQLEREK NDTSEKLRIA GKRIDHIERA FRKEEAKKLP
     ADYEEQRKRD LEAYDKTKSQ VLRDAEAKHA EDLELSRRLT RITPIYEEFK TDVVARRHDE
     FEKRRRDAEK ELEKQISQRR KEHRDRKIRE KREREEQERI LREEEERAAV ELAEKSAREE
     RRRQEFAELK AQRDKERQEG LEKATLQARR EEEALARRAG ARNTGGLPVR AAEPERSASS
     DRRPPLPLAG AKLGWREKEA LRAAGQEVPS ERTASPAAPT APFARTDSND RPSGPPRLAL
     AGAKPSWRDK EAARAASGTS PAPESRDREA PVISRTASGS GPVRGRTDRA ENERESRSPA
     PPAEPLKASG GAGKYIPKHL RDKA
//
DBGET integrated database retrieval system