EIF3A_CRYNB
ID EIF3A_CRYNB Reviewed; 952 AA.
AC P0CN43; Q55S53; Q5KGK5;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit A {ECO:0000255|HAMAP-Rule:MF_03000};
DE Short=eIF3a {ECO:0000255|HAMAP-Rule:MF_03000};
DE AltName: Full=Eukaryotic translation initiation factor 3 110 kDa subunit homolog {ECO:0000255|HAMAP-Rule:MF_03000};
DE Short=eIF3 p110 {ECO:0000255|HAMAP-Rule:MF_03000};
DE AltName: Full=Translation initiation factor eIF3, p110 subunit homolog {ECO:0000255|HAMAP-Rule:MF_03000};
GN Name=TIF32 {ECO:0000255|HAMAP-Rule:MF_03000}; OrderedLocusNames=CNBE3290;
OS Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=283643;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B-3501A;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
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:0000255|HAMAP-Rule:MF_03000}.
CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex. {ECO:0000255|HAMAP-Rule:MF_03000}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03000}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit A family. {ECO:0000255|HAMAP-
CC Rule:MF_03000}.
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DR EMBL; AAEY01000026; EAL20621.1; -; Genomic_DNA.
DR RefSeq; XP_775268.1; XM_770175.1.
DR AlphaFoldDB; P0CN43; -.
DR SMR; P0CN43; -.
DR PRIDE; P0CN43; -.
DR EnsemblFungi; AAW43583; AAW43583; CNE03290.
DR EnsemblFungi; EAL20621; EAL20621; CNBE3290.
DR GeneID; 4936339; -.
DR KEGG; cnb:CNBE3290; -.
DR VEuPathDB; FungiDB:CNBE3290; -.
DR HOGENOM; CLU_002096_2_1_1; -.
DR Proteomes; UP000001435; 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 HAMAP; MF_03000; eIF3a; 1.
DR InterPro; IPR027512; EIF3A.
DR InterPro; IPR000717; PCI_dom.
DR PANTHER; PTHR14005; PTHR14005; 1.
DR Pfam; PF01399; PCI; 1.
DR SMART; SM00088; PINT; 1.
DR PROSITE; PS50250; PCI; 1.
PE 3: Inferred from homology;
KW Coiled coil; Cytoplasm; Initiation factor; Protein biosynthesis;
KW RNA-binding.
FT CHAIN 1..952
FT /note="Eukaryotic translation initiation factor 3 subunit
FT A"
FT /id="PRO_0000410075"
FT DOMAIN 315..491
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 757..952
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 522..849
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT COMPBIAS 757..800
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..843
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 900..914
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 952 AA; 106269 MW; 996635B7FD0069C6 CRC64;
MPPIYVKPEN ALKRSEELLA LGTPQSQQQA FDNLVEVFQS KRFKQTPINV LEPIVTKFID
LCVVLSRKAH AKSGLLVFKS AAQTTNVGAI ERVLNHFIAK AEARLAAAVE QAKKEVAALP
DVPVVDDDLP LQPASLMLDC FVDSAGDRER IERRLIAPAQ KFCWDSYDIC LDIAKSNDRL
EVIYQSIAHR AFHFCKIHQR KADFRRLCEQ RLRKDLANAA KYSHQQHAIN LSDPETLGRF
LDTRFLQLET AVELELWQEA FRSIEDVHGL IAGRKGTKPS MMANYYEKLT QIFKAEGGKQ
TAVFHAAAWA RYFQHAERAG IVNDKASGCV LLSALAVPLG EVEVKQRLVA LLNLPKTPTR
EALVQDAAAK HLKRVPADIR QIYKILEVDF EPTTASKVLA PLITSLSPEY QPYLPALRDV
VLSRLLQALA QVYDSVTLSH ILDLVKPLDN TPWATDMSSL EKFLVTACRR GDIRASVDHV
AQTITFVSTP PDANGLQTLA VCLYNTIQYL NPSRLAPVSR SDAFAAAIAQ AEEERKAASH
KRQIVIRRRE LLEEAKLRRE KEASTALAER LKIKAEEDAR RAKEEAKQAE IDRVRKQIHE
TKQAEAKQLA ASLAAQGALK VDISSIEDLD SSKLVAMQVE QLAKEKKELS ERLRIVGKRV
DHLERAMRKE ERPLLAQDYE RQKAEDRAAH DRANQIAREQ AIEQQRAARE LKQRLGRMLE
DYEAVKERIE SQMQEELKAA KEEARRKIEE EKAQLREKVI KRKREEKERK LKEAREAEER
KRKEEEEAAQ KAEEEARAAA ALEAEAAAAE QRRAEREAQR QSDLERIRAQ QEREEEALRR
RQAEKAAATS GGSAYRPPAR AGTTPPTASP APSSGGPSWL ARRKAMEAQS AGGAPVASSP
KPVPSNSAAA SAPASNGPES IAGEAEKPAL TGSVWRRGMG ARRGMPSTRG GA
