ID A0A0W4ZVS6_PNEJ7 Unreviewed; 958 AA.
AC A0A0W4ZVS6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
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=T551_00556 {ECO:0000313|EMBL:KTW32466.1};
OS Pneumocystis jirovecii (strain RU7) (Human pneumocystis pneumonia agent).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Pneumocystomycetes; Pneumocystaceae; Pneumocystis.
OX NCBI_TaxID=1408657 {ECO:0000313|EMBL:KTW32466.1, ECO:0000313|Proteomes:UP000053447};
RN [1] {ECO:0000313|Proteomes:UP000053447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RU7 {ECO:0000313|Proteomes:UP000053447};
RX PubMed=26899007; DOI=10.1038/ncomms10740;
RA Ma L., Chen Z., Huang D.W., Kutty G., Ishihara M., Wang H., Abouelleil A.,
RA Bishop L., Davey E., Deng R., Deng X., Fan L., Fantoni G., Fitzgerald M.,
RA Gogineni E., Goldberg J.M., Handley G., Hu X., Huber C., Jiao X., Jones K.,
RA Levin J.Z., Liu Y., Macdonald P., Melnikov A., Raley C., Sassi M.,
RA Sherman B.T., Song X., Sykes S., Tran B., Walsh L., Xia Y., Yang J.,
RA Young S., Zeng Q., Zheng X., Stephens R., Nusbaum C., Birren B.W.,
RA Azadi P., Lempicki R.A., Cuomo C.A., Kovacs J.A.;
RT "Genome analysis of three Pneumocystis species reveals adaptation
RT mechanisms to life exclusively in mammalian hosts.";
RL Nat. Commun. 7:10740-10740(2016).
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:KTW32466.1}.
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DR EMBL; LFWA01000002; KTW32466.1; -; Genomic_DNA.
DR RefSeq; XP_018231158.1; XM_018372822.1.
DR AlphaFoldDB; A0A0W4ZVS6; -.
DR STRING; 1408657.A0A0W4ZVS6; -.
DR GeneID; 28939077; -.
DR VEuPathDB; FungiDB:T551_00556; -.
DR eggNOG; KOG2072; Eukaryota.
DR OrthoDB; 10990at2759; -.
DR Proteomes; UP000053447; 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 Reference proteome {ECO:0000313|Proteomes:UP000053447};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_03000}.
FT DOMAIN 317..500
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT REGION 835..958
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 585..638
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03000"
FT COILED 670..697
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03000"
FT COMPBIAS 835..918
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 919..943
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 958 AA; 111653 MW; D6C2CC368BD6C31C CRC64;
MLIPQSKPEN VLRRAEELIA VGQSAAALQS LHELILSKCS RNTSVSSLKP IMLRFVALCV
DLRKGKMAKE ALYQYKNIAQ NTSVGTIEVV LKKFIDLVEE KVSEAQVHAE KLVLDAIDDL
EASETPENII LSTVSGDQSK DRTDRAVVTP WLKFLWETYR TVLEILKNNA RLEQAYQSTV
NQAFDFCLKY SRKTEFRRLC DILRTHLQNA TKYSGQQHSI NFNDPETLQR HLDTRFSQLN
AAVELELWQE AFRSVEDINN LLALSKRQPK LFVMANYYEK LGKIFAVSEN YLFHAVIWNK
YYGLISSQNK GADDKELERV ASLVLLSALA IPVISTTRSK GSIMEIDDTK IRNTKLAALL
SLSKLPTRNS LLKEALGKNI LVYVRKEIKE LCNILEVEFH PLSICQKVEP LIKIISQDPD
MIQYIKPLQH VILTRLFQQL SQVYETIKLD FILSLLNFSE PFHIDSIYIE KFIMNASKKG
ELSIRIDHSS NSLIFETNIF ASHHTIADSN VRLQSTPSEL IRSQLSRIGK CLLTTVCIID
KSFLHELEDQ KNIANEHTAN GIEKEQKDTL ARRAIIEHRK EVAENMMIYK EKEAATKRAQ
KLQQEQEAEQ RRVAEEAKKR EAERIKKETD AIRAEEARKL ADELKAKGAL KVDVDGLEGL
DTSKLRAIQL EQLEKETRDL NEKLRVTSKR IDHLERAYRK EELPLLKQKA IEQFTSDKIF
YEKARKLQLE ASRVKHDHMV ALKHRFQRLY PDYVIYRETF LEKCRKEFDQ HCKIANEALE
KAKEERRMAY RLKKEEEERQ RLEEEERKRK KEEERERIRQ EELRLKAIEE ENRARKEEEL
RKLDQMAEKQ KQKELEVERK LQRKKEELKS LDHNYDRWTK KDRLPPSDPS GEEKWRPGKG
SWRLRVSERQ ELTDPHSSPN ETKPDPQSKP TSTRPSTTDP PSTGIYKPPA ARKENSRW
//