EIF3M_ASPCL
ID EIF3M_ASPCL Reviewed; 471 AA.
AC A1CD85;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 62.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit M {ECO:0000255|HAMAP-Rule:MF_03012};
DE Short=eIF3m {ECO:0000255|HAMAP-Rule:MF_03012};
GN ORFNames=ACLA_005680;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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:0000255|HAMAP-Rule:MF_03012}.
CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex. {ECO:0000255|HAMAP-Rule:MF_03012}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03012}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit M family. {ECO:0000255|HAMAP-
CC Rule:MF_03012}.
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DR EMBL; DS027051; EAW11812.1; -; Genomic_DNA.
DR RefSeq; XP_001273238.1; XM_001273237.1.
DR AlphaFoldDB; A1CD85; -.
DR SMR; A1CD85; -.
DR STRING; 5057.CADACLAP00000424; -.
DR EnsemblFungi; EAW11812; EAW11812; ACLA_005680.
DR GeneID; 4705565; -.
DR KEGG; act:ACLA_005680; -.
DR VEuPathDB; FungiDB:ACLA_005680; -.
DR eggNOG; KOG2753; Eukaryota.
DR HOGENOM; CLU_035254_0_1_1; -.
DR OMA; REDAQRC; -.
DR OrthoDB; 679771at2759; -.
DR Proteomes; UP000006701; 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:0071541; C:eukaryotic translation initiation factor 3 complex, eIF3m; 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 HAMAP; MF_03012; eIF3m; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR045237; COPS7/eIF3m.
DR InterPro; IPR027528; eIF3m.
DR InterPro; IPR040750; eIF3m_C_helix.
DR InterPro; IPR000717; PCI_dom.
DR PANTHER; PTHR15350; PTHR15350; 1.
DR Pfam; PF18005; eIF3m_C_helix; 1.
DR Pfam; PF01399; PCI; 1.
DR SMART; SM00088; PINT; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50250; PCI; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Initiation factor; Protein biosynthesis; Reference proteome.
FT CHAIN 1..471
FT /note="Eukaryotic translation initiation factor 3 subunit
FT M"
FT /id="PRO_0000366011"
FT DOMAIN 206..377
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 39..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..443
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 471 AA; 51486 MW; 778074F292867423 CRC64;
MPAPTNTLLI EGTFTELADE FAQYIDALRK NEGSSLQSEI SSLLEPLRQQ EQSEEEPDRK
QRDEVLKKLV AAAAVLNAAP EKEIISAYNL LVHLVHQASN PDMFLSRICT YLAKPITTSP
QFGPTLAISI LTTIFNTLTS SDSSRYHVLL AIVAVIRQSG SSYAFEALKP QLTAQLPTWL
AAWELDEEEA QKLHLAVADA AQASGDFELA QSHVVQALQT IPANESSSKE ARDLAVRALA
SALKSPAVFD FTSLTAADAI QALRTSDSSL FELLEIFTAD TLDAYEDFVA ATPLASISGG
VLADAGEALQ NKLRLLTLAS IAASAPSRSL PYATIASALR VPTEDVEKWV IDTIRAGLVE
GKLSQLRSEF LVHRATYRVF GEKQWAEVQG RLMVWRRSLE NVLGVVRAER ERFIRESLQA
ATEEANQGKS GEKGGKGGDR RRNPQHQQQQ QQSQPSQPQQ PRETELVAGA E