ID A0A540L6S8_MALBA Unreviewed; 906 AA.
AC A0A540L6S8;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
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 subunit 10 {ECO:0000256|HAMAP-Rule:MF_03000};
GN ORFNames=C1H46_032399 {ECO:0000313|EMBL:TQD82049.1};
OS Malus baccata (Siberian crab apple) (Pyrus baccata).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX NCBI_TaxID=106549 {ECO:0000313|EMBL:TQD82049.1, ECO:0000313|Proteomes:UP000315295};
RN [1] {ECO:0000313|EMBL:TQD82049.1, ECO:0000313|Proteomes:UP000315295}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Shandingzi {ECO:0000313|Proteomes:UP000315295};
RC TISSUE=Leaves {ECO:0000313|EMBL:TQD82049.1};
RA Chen X.;
RT "Sequencing of a Wild Apple (Malus baccata) Genome Unravels the Differences
RT Between Cultivated and Wild Apple Species Regarding Disease Resistance and
RT Cold Tolerance.";
RL G3 (Bethesda) 9:1785-1793(2019).
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:TQD82049.1}.
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DR EMBL; VIEB01000741; TQD82049.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A540L6S8; -.
DR STRING; 106549.A0A540L6S8; -.
DR Proteomes; UP000315295; 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 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:UP000315295};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_03000}.
FT DOMAIN 322..513
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT REGION 807..906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 93..120
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03000"
FT COILED 561..685
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03000"
FT COMPBIAS 807..822
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 825..839
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 863..890
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 906 AA; 105795 MW; C5D43FA610375FCC CRC64;
MANFAKPENA LKRAEELINV GQKQDALQSL HDLITSKRYR AWQKPLEKIM FKYVELCVDL
RKGRFAKDGL IQYRIICQQV NVSSLEEVIK HFMQLSTEKA EQARTQAQAL EEALDVDDLE
ADKRPEDLML SYVSGEKGKD RSDREVVTPW FKFLWETYRT VLEILRNNSK LEALYAMTAH
RAFQFCKQYK RTTEFRRLCE IIRNHLANLN KYRDQRDRPD LSAPESLQLY LDTRFEQLKI
ATELELWQEA FRSVEDIHGL MCMVKKTPKA SLMVVYYAKL TEIFWISASH LNHAYAWFKL
FTLQKSFNKN LNQKDLQLIA SSVILAALSV APYDQTRATS HLELENEKER NLRMANLIGF
NLEPRVDRGD VLSRSALLSE LVSKGVLSCA TQEVKDLYHL LEHEFLPLDL AIKMQPLLTK
ISKFGGKLSS ASSVPEVQLS QYVPALEKLG TLRLLHQVSQ VYQIMKIECL SQMIPFYDFS
VVEKIYVDAV KHNFIAMKVD HMKGVMLFGN LGLESDGLRD HLTNLAESLN KARSMMYPPI
KGESKLVEIL PSLADTVDKE HKRLLARKSI IEKRKEEQER QLLEMEREEE SKRLKQQKIT
EVAEQKRLAE EAEQRRNQRI RKEIEEKEID EAQKLLDETR KKKKGKKHIL DGGKVTKQSL
MELALSEQLR ERQEMEKKLL KLGKTMDYLE RAKREESAPL IEAAYQQRLV EEQLLHEREQ
TLEVELSQQR HEGDLKEKNR LSRMMDNKTI FQERVLHRRH EEYERRRAER EEQISQLIWA
RKQERDAKRK KIFFVRSEEE RLRKLREEEE ARKREAEIPR PAEPRTEPAS APPAVAPSPG
KYVPRHLRQR GAEAPGQAPP EPDRRGIRPD DRPPPSSDRW RSDSDERRPA LGGGGPKWSS
SRGPTR
//
