ID A0A0D2R342_GOSRA Unreviewed; 989 AA.
AC A0A0D2R342;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=B456_004G238100 {ECO:0000313|EMBL:KJB26359.1};
OS Gossypium raimondii (New World cotton).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB26359.1, ECO:0000313|Proteomes:UP000032304};
RN [1] {ECO:0000313|EMBL:KJB26359.1, ECO:0000313|Proteomes:UP000032304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23257886; DOI=10.1038/nature11798;
RA Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D.,
RA Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R.,
RA Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., Grover C.,
RA Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., Marler B.S., Page J.T.,
RA Roberts A.W., Romanel E., Sanders W.S., Szadkowski E., Tan X., Tang H.,
RA Xu C., Wang J., Wang Z., Zhang D., Zhang L., Ashrafi H., Bedon F.,
RA Bowers J.E., Brubaker C.L., Chee P.W., Das S., Gingle A.R., Haigler C.H.,
RA Harker D., Hoffmann L.V., Hovav R., Jones D.C., Lemke C., Mansoor S.,
RA ur Rahman M., Rainville L.N., Rambani A., Reddy U.K., Rong J.K.,
RA Saranga Y., Scheffler B.E., Scheffler J.A., Stelly D.M., Triplett B.A.,
RA Van Deynze A., Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J.,
RA Zaki E.A., Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S.,
RA Wang X., Schmutz J.;
RT "Repeated polyploidization of Gossypium genomes and the evolution of
RT spinnable cotton fibres.";
RL Nature 492:423-427(2012).
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}.
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DR EMBL; CM001743; KJB26359.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D2R342; -.
DR EnsemblPlants; KJB26359; KJB26359; B456_004G238100.
DR Gramene; KJB26359; KJB26359; B456_004G238100.
DR Proteomes; UP000032304; Chromosome 4.
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:UP000032304};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_03000}.
FT DOMAIN 316..503
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT REGION 798..989
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 93..120
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03000"
FT COILED 551..684
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03000"
FT COMPBIAS 798..851
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 931..945
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 989 AA; 114422 MW; F7C30172FDAE3D13 CRC64;
MANFAKPENA LKRAEELINV GQKQDALQAL HNLITSKRYR AWQKPLEKIM FKYVELCVDM
RKGRFAKDGL IQYRIVCQQV NVSSLEEVIK HFMHLSTQKA EQARSQAEAL EEALDVDDLE
ADKRPEDLML SYVSGEKGKD RSDRELVTPW FKFLWETYRT VLEILRNNSK LEALYAMTAH
RAFQFCKQYK RTTEFRRLCE IIRNHLANLN KYKDQRDRPD LSAPESLQLY LDTRFEQLKI
ATELGLWQEA FRSVEDIHGL MSIVKKTPKA SLMVVYYAKL TEIFWISGSH LYHAYAWFKL
FSLQKSFNKN LSQKDLQLIA SSVVLTALSV SPYNQTRGAS HLELENEKER NLRMANLIGF
NLESKLENRE VVSKGVLSCA TQEVKDLYHL LENDFLPLDV ASKIHPLLMK ISKLGGKLTS
ASSVAEVQLS QYVPSLERLA TLRLLKQVSQ LYQTMKIESL SQMIPFFEFS MVEKISVDAV
KHKFISMKVD HMKGAVLFGN TGLESDKLQD HLAVLAESLN KARAMIYPTP KKASKLGEVL
PGLGEIVDKE HKRLLARKSI IEKRKEEQER QLLEMEREEE SKRQNLLKKT EEAEKKRLAA
MFEQQRAERI RKEIEERELE EAQALLQETE KHLKRGKKKP ILDGEKLTKQ TLIERALSEQ
LKERQEQEKR LQKVAKTMDH LERAKREEAA PLIEAAFQRR LVEEKVLHER EQQLEVELSR
QRHDGDLKEK NRLARMLENK MIFQERVISR RQAEFDQRRV EGEERIKQII QARKQERDIK
RKKIFFVRSE EERIKKMREE EEARKREEAE RRRKEEAEHK AKMDEIAEKQ RQRERELEEK
ERLRREALLG RAPEGISRPS ELPAGSRTTE PVVATPAAAA AAAAPTTGKY VPKFRLRPES
SGPAPPSEPD RWGKPAPLEP DRWAAGSRAP PSQSDRWTSG SRAPPQDSDR LAGGGSRATP
PDSNRFGGGS GSSKAEPWRP SRARNPQRG
//
