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Database: UniProt
Entry: A0A371G3K2_MUCPR
LinkDB: A0A371G3K2_MUCPR
Original site: A0A371G3K2_MUCPR 
ID   A0A371G3K2_MUCPR        Unreviewed;       974 AA.
AC   A0A371G3K2;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Eukaryotic translation initiation factor 3 subunit C {ECO:0000313|EMBL:RDX85122.1};
DE   Flags: Fragment;
GN   Name=TIF3C1 {ECO:0000313|EMBL:RDX85122.1};
GN   ORFNames=CR513_33718 {ECO:0000313|EMBL:RDX85122.1};
OS   Mucuna pruriens (Velvet bean) (Dolichos pruriens).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Mucuna.
OX   NCBI_TaxID=157652 {ECO:0000313|EMBL:RDX85122.1, ECO:0000313|Proteomes:UP000257109};
RN   [1] {ECO:0000313|EMBL:RDX85122.1, ECO:0000313|Proteomes:UP000257109}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Jos {ECO:0000313|Proteomes:UP000257109};
RC   TISSUE=Seed {ECO:0000313|EMBL:RDX85122.1};
RA   Nnadi N.E., Vos R., Hasami M.H., Devisetty U.K., Aguiy J.C.;
RT   "Draft genome of Mucuna pruriens seed.";
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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:RDX85122.1}.
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DR   EMBL; QJKJ01006866; RDX85122.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A371G3K2; -.
DR   STRING; 157652.A0A371G3K2; -.
DR   Proteomes; UP000257109; Unassembled WGS sequence.
DR   GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:UniProt.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0031369; F:translation initiation factor binding; IEA:InterPro.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   HAMAP; MF_03002; eIF3c; 1.
DR   InterPro; IPR027516; EIF3C.
DR   InterPro; IPR008905; EIF3C_N_dom.
DR   InterPro; IPR000717; PCI_dom.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR13937; EUKARYOTIC TRANSLATION INITATION FACTOR 3, SUBUNIT 8 EIF3S8 -RELATED; 1.
DR   PANTHER; PTHR13937:SF0; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT C-RELATED; 1.
DR   Pfam; PF05470; eIF-3c_N; 1.
DR   Pfam; PF01399; PCI; 1.
DR   SMART; SM00088; PINT; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS50250; PCI; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Initiation factor {ECO:0000256|ARBA:ARBA00022540,
KW   ECO:0000313|EMBL:RDX85122.1};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT   DOMAIN          620..792
FT                   /note="PCI"
FT                   /evidence="ECO:0000259|PROSITE:PS50250"
FT   REGION          1..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          134..229
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          841..934
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..26
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..63
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        135..154
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        155..174
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        175..193
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        194..229
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        851..872
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         974
FT                   /evidence="ECO:0000313|EMBL:RDX85122.1"
SQ   SEQUENCE   974 AA;  109722 MW;  FF9108AE3F783431 CRC64;
     MASRFWNQGG SESEEEESDY DEEVEAAAGE SANQAVTSRY LQENASDSDD SDGQKRVVRS
     AKDKRFEEMA STVDQMKNAM KINDWVSLQE SFDKINKQLE KVMRVTESDK VPNLYIKALV
     MLEDFLAQAL ANKDAKKKMS SSNAKALNSM KQKLKKNNKQ YEDLINKCRE NPESEEEKEE
     EESEEEYESD DEIIEPEQLR KPEAKSDSEA SQYDDEKLDT GDGPWDQKLS KKDRLLDRQF
     MKDPSEITWD TVNKKFKEVV AARGRKGTGR FEQVEQLTFL TKVAKTPAQK LEILFSVVSA
     QFDVNPGLNG HMPINVWKKC VQNMLVILDI LVQYQNIVVD DSVEPDENET QKGTDYNGPI
     RVWGNLVAFL ERVDVEFFKS LQCIDPHTRD YVERLRDEPL FLVLAQNVQE YLERVGNFKA
     ASKVALRRVE LIYYKPQEVY DAMKKLTELT EDGDNGGEAS EESKGFDDSR IPTAFVVTPE
     VVARKPTFPE NSRSIMDELV SLIYKYGDER TKARAMLCDI YHHALVDEFS MARDLLLMSH
     LQDSVQHMDI STQILFNRAM SQLGLCAFRA GLISEAHGCL SELYSGGRVK ELLAQGVSQS
     RYHEKTPEQE RLERRRQMPY HMHINLELLE AVHLVSAMLL EVPNMAANVH DAKRKVISKT
     FRRLHEISEK QTFTGPPENV RDHVMAATRV LSKGDFQKAF DIIVSLDVWK FVRNRDTVLE
     MLKDKIKEEA LRTYLFTFSS SYESLSLDQL AKFFDITVSC THSIVSRMMI NEELHASWDQ
     PTGCIVFQDV EHSRLQALAF QLTEKLSILA ESNERATEAR IGGGGLDLPL RRRDGQDYAA
     AAAGSGAASS GGRWQDLSLS QPRPSSGRAG YGSSGGRSMA LGQAAGSGYS RDRMGRGTGA
     GYQSARYHDG SYGGSGKTAQ GGSALRGPQG DVSTRMVSLK EIACDSTETR VKVGKEIKFD
     GSKNLVGREL RNPN
//
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