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Database: UniProt
Entry: A0A0A2ID02_PENEN
LinkDB: A0A0A2ID02_PENEN
Original site: A0A0A2ID02_PENEN 
ID   A0A0A2ID02_PENEN        Unreviewed;       627 AA.
AC   A0A0A2ID02;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   SubName: Full=Translation elongation/initiation factor/Ribosomal, beta-barrel {ECO:0000313|EMBL:KGO61864.1};
GN   ORFNames=PEX2_015430 {ECO:0000313|EMBL:KGO61864.1};
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:KGO61864.1, ECO:0000313|Proteomes:UP000030143};
RN   [1] {ECO:0000313|EMBL:KGO61864.1, ECO:0000313|Proteomes:UP000030143}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MD-8 {ECO:0000313|EMBL:KGO61864.1,
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   -!- 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:KGO61864.1}.
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DR   EMBL; JQFZ01000028; KGO61864.1; -; Genomic_DNA.
DR   RefSeq; XP_016602551.1; XM_016738819.1.
DR   AlphaFoldDB; A0A0A2ID02; -.
DR   STRING; 27334.A0A0A2ID02; -.
DR   GeneID; 27674238; -.
DR   HOGENOM; CLU_012821_0_0_1; -.
DR   OrthoDB; 129286at2759; -.
DR   PhylomeDB; A0A0A2ID02; -.
DR   Proteomes; UP000030143; Unassembled WGS sequence.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   CDD; cd04165; GTPBP1_like; 1.
DR   CDD; cd03694; GTPBP_II; 1.
DR   CDD; cd03708; GTPBP_III; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 2.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR035531; GTPBP1-like.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR   PANTHER; PTHR43721; ELONGATION FACTOR TU-RELATED; 1.
DR   PANTHER; PTHR43721:SF9; GTP-BINDING PROTEIN 1; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50447; Translation proteins; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   4: Predicted;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Initiation factor {ECO:0000313|EMBL:KGO61864.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000313|EMBL:KGO61864.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030143}.
FT   DOMAIN          187..416
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          27..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          602..627
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..49
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        605..627
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   627 AA;  68268 MW;  0F2B5C2390AA2AE9 CRC64;
     MPATGKLSHE ERKRGEVALS EFAEYADKQQ AHRSGQVAPS DSGYSTASVS RDLEDHAELD
     ILDQLGLSDA PQTAKLKDLL LGTGDAIEDN LQMLAGTLQT RIDEGHGETI FDLGLEDGGE
     SMGFDLDQWK AALQRLREAA ETIPAHCRVL LTYNVGGPEE SPVTNDRVQG SWGKVLVRHH
     ADNIEEMAEL RIAVVGNVDA GKSTTLGVLV KGGLDDGRGR ARVNLFRHKH EIESGRTSSV
     GLEIMGFDSR GEIVGNTQGR KLSWEDIGKR SAKVIAFSDL AGHERYLRTT VFGMLSSSPN
     YCLLMVAANN GLIGMSKEHL GIALALNVPV MVIVTKIDIC PPHILQETLS QLTKILKSPG
     ARKIPIFVKD MEETINTAAQ FVSQRICPIF QVSNVTGENL DLVRTFLNIL PHRGQYDAAG
     AFEFLINDTF SVPHVGTVVA GVVKSGVIHA GDSVMVGPDS LGQFTTTVIK SIERKRIQVN
     ACFAGQSGSF ALKRVRRKEV RKGMVVLKKM EEAPKVYREF VAEVLILSHA TTIKPKYQAM
     LHVGAVSQTC SVIDIDRPFI RTGDRALVAF RFVQRPEFLA PGDRVLFREG KTKGLGIVKS
     IGYDPTQPLN PNAKEGASTP TPTTPHD
//
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