ID A0A0D3AG25_BRAOL Unreviewed; 1513 AA.
AC A0A0D3AG25;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit M {ECO:0000256|HAMAP-Rule:MF_03012};
DE Short=eIF3m {ECO:0000256|HAMAP-Rule:MF_03012};
GN Name=106341286 {ECO:0000313|EnsemblPlants:Bo1g157490.1};
OS Brassica oleracea var. oleracea.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=109376 {ECO:0000313|EnsemblPlants:Bo1g157490.1, ECO:0000313|Proteomes:UP000032141};
RN [1] {ECO:0000313|EnsemblPlants:Bo1g157490.1, ECO:0000313|Proteomes:UP000032141}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. TO1000 {ECO:0000313|Proteomes:UP000032141};
RX PubMed=24916971; DOI=10.1186/gb-2014-15-6-r77;
RA Parkin I.A., Koh C., Tang H., Robinson S.J., Kagale S., Clarke W.E.,
RA Town C.D., Nixon J., Krishnakumar V., Bidwell S.L., Denoeud F., Belcram H.,
RA Links M.G., Just J., Clarke C., Bender T., Huebert T., Mason A.S.,
RA Pires J.C., Barker G., Moore J., Walley P.G., Manoli S., Batley J.,
RA Edwards D., Nelson M.N., Wang X., Paterson A.H., King G., Bancroft I.,
RA Chalhoub B., Sharpe A.G.;
RT "Transcriptome and methylome profiling reveals relics of genome dominance
RT in the mesopolyploid Brassica oleracea.";
RL Genome Biol. 15:R77-R77(2014).
RN [2] {ECO:0000313|EnsemblPlants:Bo1g157490.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2015) to UniProtKB.
CC -!- FUNCTION: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex, which is involved in protein synthesis of a
CC specialized repertoire of mRNAs and, together with other initiation
CC factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S
CC 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_03012}.
CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex. {ECO:0000256|HAMAP-Rule:MF_03012}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03012}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit M family. {ECO:0000256|HAMAP-
CC Rule:MF_03012}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000256|ARBA:ARBA00008684}.
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DR RefSeq; XP_013635565.1; XM_013780111.1.
DR STRING; 109376.A0A0D3AG25; -.
DR EnsemblPlants; Bo1g157490.1; Bo1g157490.1; Bo1g157490.
DR GeneID; 106341286; -.
DR Gramene; Bo1g157490.1; Bo1g157490.1; Bo1g157490.
DR KEGG; boe:106341286; -.
DR eggNOG; KOG2753; Eukaryota.
DR HOGENOM; CLU_000288_22_2_1; -.
DR OMA; DIGDNCG; -.
DR OrthoDB; 449350at2759; -.
DR Proteomes; UP000032141; Chromosome C1.
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:0071541; C:eukaryotic translation initiation factor 3 complex, eIF3m; IEA:UniProtKB-UniRule.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
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 GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0099402; P:plant organ development; IEA:UniProt.
DR CDD; cd14066; STKc_IRAK; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 4.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR HAMAP; MF_03012; eIF3m; 1.
DR InterPro; IPR027528; eIF3m.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR45974:SF242; LEUCINE-RICH REPEAT PROTEIN KINASE FAMILY PROTEIN; 1.
DR PANTHER; PTHR45974; RECEPTOR-LIKE PROTEIN 55; 1.
DR Pfam; PF00560; LRR_1; 3.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF01399; PCI; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 8.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF52047; RNI-like; 1.
DR PROSITE; PS50250; PCI; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03012};
KW Initiation factor {ECO:0000256|HAMAP-Rule:MF_03012};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_03012};
KW Reference proteome {ECO:0000313|Proteomes:UP000032141};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1173..1196
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 194..360
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT DOMAIN 1235..1513
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1133..1163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1263
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1513 AA; 165692 MW; BF607CA40B54E8A9 CRC64;
MTTTTTILPT SEGDPFLSVV RFTSQLAEAS EPEIARLCKE AEEFIVARKW LELASLLVAS
AELASSKISQ KDFECTYSII CSIVKNANSP EDDVLDMVKV ISAKLVQQPN DKASLRLKIL
FNLYSLLDHP YARFQVYMKA LTLALEGKVT EYIIPSFKKI DSFLEEWNID IKDQRELFLA
VTNVLRENKS LVKESLKFLT KYLATFSKED AQALGEAKEG AVCAVIAFVK ASSIFQCDLL
DLPAVAQLEK DPKYAPVYQL LKIFLTQRLN AYREFQTANS ECLQSYGLVD EDCVTKMRLL
SLVHLASDEF GKIPYTSIKD TLQLKGEEVE PWIVKATTAK LIDCKIDQIN QVVIISRCSE
RKFGSDGFSP PRKMPPIILF SFWLLCIITC LPGRITVLAD SDKSVLLRFK ETVSDPGSIL
ASWVNESEDY CSWFGVSCDS TSRVMALNIS GSGSDKGSSK ISRNRFTCAD IGKFPLYGFG
IRRVCAGKLG TLVGNLPSVI VGLTELRVLS LPFNSFSGEI PVGIWGMEKL EVLDLEGNLM
TGSLPVQFTG LRSLRVMNLG FNRFSGEIPS SLQNLSKLEI LNLGGNKLNG TVPGFVGRFR
VVHLLLNWLE GSLPKDIGDN CGKLEHLDLS GNFLSGRIPE SLGSCRGLKS LLLYMNTLEE
TIPSEFGNLG KLEVLDVSKN TLSGPLPAEL GNCSSLCVLV LSNLYNVYED ISSVRGESDQ
LPGADLTSMT EDFNFYQGGI PEEITRLPKL KILWVPRATL EGRFPGDWGS CQSLEMVNLG
QNFFKGEIPV GLSKCNNLRL LDLSSNVLTG ELLKEMSVPC MSVFDVGGNS LSGLIPEFLS
NTTTSCPPVV YFDGFSIESY NTDPSSVYLS FFTEKAQVGA SLTAVGGDGG PAVFHNFADN
NFTGTLKSVP LAQERLGKSI SYIFSGGGNQ LYGQFPGNLF DSCDKLKAVY VNVSFNKLSG
RIPEGLSNMC PSLKILDASL NQIFGPIPSS LGDLASLVAL NLSWNQLQGH IPGSVGKKMN
ALTFLSFANN NLKGQIPESF GQLHSLQVLD LSSNYLSGGI PHGFVNLKNL TVLLLNNNNL
SGQIPTGFST FAVFNVSSNN MSGPVPPTNG LTKCSSVVGN MYLQPCRVFS LTTPSSDPRG
PMADSSTQDY ASSPVENAPS QNSGRDGFNS LEIASIASAS AIVSVLIALV ILFFYTRKWH
PKSKVMATTK REVTMFMDMG VAITFDNVVR ATGNFNANNL IGNGGFGATY RAVISQEVIV
AIKRLSIGRF QGVQQFHAEI KTLGRLRHPN LVTLIGYHAS ETEMFLVYNY LPGGNLEKFI
QERSTRAVDW RNLHKIALDI ARALAYLHDQ CVPRVLHRDV KPSNILLDND HNAYLSDFGL
ARLLGTSETH ATTGVAGTFG YVAPEYAMTC RVSDKADVYS YGVVLLELLS DKKALDPSFV
SYGNGFNIVQ WGCMLLKQGR AKEFFTAGLW DAGPHDDLVE VLHLAVICTV DSLSTRPTMK
QVVRRLKQLQ PPY
//