ID A0A0A2KBZ4_PENEN Unreviewed; 181 AA.
AC A0A0A2KBZ4;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 13-SEP-2023, entry version 34.
DE RecName: Full=Translation machinery-associated protein 20 {ECO:0000256|PIRNR:PIRNR005067};
GN ORFNames=PEX2_032240 {ECO:0000313|EMBL:KGO54447.1};
OS Penicillium expansum (Blue mold rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO54447.1, ECO:0000313|Proteomes:UP000030143};
RN [1] {ECO:0000313|EMBL:KGO54447.1, ECO:0000313|Proteomes:UP000030143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8 {ECO:0000313|EMBL:KGO54447.1,
RC ECO:0000313|Proteomes:UP000030143};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
CC -!- FUNCTION: Involved in translation. {ECO:0000256|PIRNR:PIRNR005067}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|PIRNR:PIRNR005067}.
CC -!- SIMILARITY: Belongs to the TMA20 family.
CC {ECO:0000256|PIRNR:PIRNR005067}.
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:KGO54447.1}.
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DR EMBL; JQFZ01000226; KGO54447.1; -; Genomic_DNA.
DR RefSeq; XP_016596887.1; XM_016740499.1.
DR AlphaFoldDB; A0A0A2KBZ4; -.
DR STRING; 27334.A0A0A2KBZ4; -.
DR GeneID; 27675918; -.
DR HOGENOM; CLU_090468_0_1_1; -.
DR OrthoDB; 5036262at2759; -.
DR PhylomeDB; A0A0A2KBZ4; -.
DR Proteomes; UP000030143; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR CDD; cd11609; MCT1_N; 1.
DR CDD; cd21155; PUA_MCTS-1-like; 1.
DR Gene3D; 3.10.400.20; -; 1.
DR InterPro; IPR016437; MCT-1/Tma20.
DR InterPro; IPR041366; Pre-PUA.
DR InterPro; IPR002478; PUA.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR004521; Uncharacterised_CHP00451.
DR NCBIfam; TIGR00451; unchar_dom_2; 1.
DR PANTHER; PTHR22798:SF0; MALIGNANT T-CELL-AMPLIFIED SEQUENCE 1; 1.
DR PANTHER; PTHR22798; MCT-1 PROTEIN; 1.
DR Pfam; PF17832; Pre-PUA; 1.
DR Pfam; PF01472; PUA; 1.
DR PIRSF; PIRSF005067; Tma_RNA-bind_prd; 1.
DR SMART; SM00359; PUA; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
DR PROSITE; PS50890; PUA; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR005067};
KW Reference proteome {ECO:0000313|Proteomes:UP000030143}.
FT DOMAIN 90..172
FT /note="PUA"
FT /evidence="ECO:0000259|SMART:SM00359"
SQ SEQUENCE 181 AA; 19776 MW; 72E1BF33F4092BDD CRC64;
MFKKDIPPSN RSKVKSSVQR GLRQKLLETY PGLEPFIEDV MPKKASLEAV KLPDRVTLYT
IDSTPLFFQP IDGPPVPHLR LIHAYPSAVP TIQIDRGAIR FVLSGATLMA PGLTSPGGRL
PDAEHALEAG QIVGVKAEGK EEICMIGMLK VGTEEIKSKG KGVVIDEGHY LGDGLWRMHL
D
//
