GenomeNet

Database: UniProt
Entry: S7ZJA8_PENO1
LinkDB: S7ZJA8_PENO1
Original site: S7ZJA8_PENO1 
ID   S7ZJA8_PENO1            Unreviewed;      1523 AA.
AC   S7ZJA8;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=MIF4G domain-containing protein {ECO:0000259|SMART:SM00543};
GN   ORFNames=PDE_03707 {ECO:0000313|EMBL:EPS28761.1};
OS   Penicillium oxalicum (strain 114-2 / CGMCC 5302) (Penicillium decumbens).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=933388 {ECO:0000313|EMBL:EPS28761.1, ECO:0000313|Proteomes:UP000019376};
RN   [1] {ECO:0000313|EMBL:EPS28761.1, ECO:0000313|Proteomes:UP000019376}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=114-2 / CGMCC 5302 {ECO:0000313|Proteomes:UP000019376};
RX   PubMed=23383313; DOI=10.1371/journal.pone.0055185;
RA   Liu G., Zhang L., Wei X., Zou G., Qin Y., Ma L., Li J., Zheng H., Wang S.,
RA   Wang C., Xun L., Zhao G.-P., Zhou Z., Qu Y.;
RT   "Genomic and secretomic analyses reveal unique features of the
RT   lignocellulolytic enzyme system of Penicillium decumbens.";
RL   PLoS ONE 8:E55185-E55185(2013).
CC   -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4G family.
CC       {ECO:0000256|ARBA:ARBA00005775}.
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DR   EMBL; KB644411; EPS28761.1; -; Genomic_DNA.
DR   STRING; 933388.S7ZJA8; -.
DR   eggNOG; KOG0401; Eukaryota.
DR   HOGENOM; CLU_003998_0_0_1; -.
DR   OrthoDB; 92033at2759; -.
DR   PhylomeDB; S7ZJA8; -.
DR   Proteomes; UP000019376; Unassembled WGS sequence.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:InterPro.
DR   Gene3D; 1.25.40.180; -; 1.
DR   Gene3D; 1.20.970.30; eIF4G, eIF4E-binding domain; 1.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR022745; eIF4G1_eIF4E-bd.
DR   InterPro; IPR036211; eIF4G_eIF4E-bd_sf.
DR   InterPro; IPR045208; IF4G.
DR   InterPro; IPR003890; MIF4G-like_typ-3.
DR   PANTHER; PTHR23253; EUKARYOTIC TRANSLATION INITIATION FACTOR 4 GAMMA; 1.
DR   PANTHER; PTHR23253:SF9; EUKARYOTIC TRANSLATION INITIATION FACTOR 4G1, ISOFORM B-RELATED; 1.
DR   Pfam; PF12152; eIF_4G1; 1.
DR   Pfam; PF02854; MIF4G; 1.
DR   SMART; SM00543; MIF4G; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF101489; Eukaryotic initiation factor 4f subunit eIF4g, eIF4e-binding domain; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000019376}.
FT   DOMAIN          1090..1329
FT                   /note="MIF4G"
FT                   /evidence="ECO:0000259|SMART:SM00543"
FT   REGION          1..417
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          456..872
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          933..1044
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1058..1086
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1346..1523
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..30
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..90
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..175
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        189..211
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        225..240
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        260..289
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        314..335
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        354..374
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        460..493
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        586..600
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        601..710
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        711..725
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        726..807
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        812..826
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        938..953
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        967..992
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1346..1362
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1410..1430
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1487..1523
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1523 AA;  162568 MW;  749AAEF617ACBCED CRC64;
     MTSNPPQSGV QPGQSTATSA ATSSTPVAAT APAAKSYANA TKKSTTDSSS APVTVGGSTQ
     HGKSSSVSPV NGNPMQNQST AQQAQSGVTI VNGAPAAPAA NAQNDHSRKP SVTITSAGAS
     GYIPNGGSAS RPNSLQFGFA NQQSSPNMGN PAVLASSQAH SGLGAPATNP RVTSPQTSPS
     PIPQPASSGG RPPSTYQAQG NVPNFGSFGE NAGDNSAPLG PGQQHVRRES SQSTHSDMSN
     PMGGAPGRGG YPPQGGRGRG YSQSGYQGGQ MPYSPGPSFR QTPNQPRGGP NMGPQFHGPN
     QGRPMPPFPN SPHQANRSPA LANAHPTTPQ MNQVPMAHPQ MPPQPYPGYG QHMGPQTVRS
     SPPTSRQPQR YTRQGPRGNH RGGFNPRRAR RGVENYASWR NPPQETRAPA VPVPLPNLAP
     ESGQFEQCLT ILRNQGFPPY DPNYYNYPGY NMQNMQYMTP PSPQPRPGMP FNPQAPYMQP
     QYPVQPPPQS TPLSRTPSQV STDRPGSSLG HAAPAGPAGP AHTHTGSRSS NSPAPVKPHF
     VIPSAKKSPI IIKDPNSGSV KTFDKTPASP ARATPSPVKA ATPTATPPPR TASASDHTRT
     ESKAANAKTD EEKKQALKDA VRQKILDDEA AQKRKEEEAS RKSAEEAKPA EAEPVEVKPV
     EDKPAAESKS EEKKPEDAVE SARAAVEDLS LKEKATPSEE PKKEAEPNPA AAPADDDEID
     YDAIERELAE IEAKERAAEE DYNRKKQEKK EEAERKEREE REQYEINMKK AEREAEEREL
     AREAARAKGD NTEDEANRKE REELFASLKK GGFTATESST PADSGAATPV SDMGPPAKPA
     SAAGKKSAGL KIDTPKSNEP PQPSAAMKSL QNAKFLEDLS KVTYPASVKG PDASLNVNSP
     AGRQFHYDRD FLLQFQAAFK DKISVDWDAR VRETVGDSES SSRPQSARTP SMGRNPSHKG
     LGAFPSQMGN FAQTSRPGVP SVNSSMGNRN VSAFGSIGRP GMPGMPGSFR NNSSPMPPRV
     PSSKGGPGSK RGKGGKKEED TNKAMPLTAG MELKALQQSA TGWKPRSVGT NAAAGPAPGG
     DGHLPPDVVQ RKVKAALNKM TPEKFDRISS QILEIVSQSK DESDGRTLRQ VIQLTFEKAT
     DEAHWAPMYA KFCKSMLESM SPEIKDENIR DKSGNIVTGG SLFRKYLLNR CQEEFERGWK
     VNLPPKPEGV TDEIAMLSDE YYIAAAAKRR GLGLVKFIGE LYKLGMLTER IMHECTKRLL
     DFEGVPEEAE VESLCNLLRT IGASLDASEK GPAMMDAYFA RINLMMEMPG LPSRLKFMLM
     DIVDLRNQRW KSKDADKGPK TIQQIREEAA RAQAEAEQER QRQQASRGGG GRPAMGRGDA
     RGFGYGNQAP PPDFASSKVG SDDLRRLRAT RNTNQPMSFG PSSLLGSRSS SGRKGLGPGG
     NLVRGSDDSA ASSRTGTPPA GKKEDKEAAS SINAFSALAA LEDRDNMATS PPSNPTSPML
     TKSQPASSER RPSKTPTEGE NAA
//
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