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Database: UniProt
Entry: A0A0A2K8V7_PENEN
LinkDB: A0A0A2K8V7_PENEN
Original site: A0A0A2K8V7_PENEN 
ID   A0A0A2K8V7_PENEN        Unreviewed;       518 AA.
AC   A0A0A2K8V7;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   11-DEC-2019, entry version 19.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KGO60815.1};
GN   ORFNames=PEX2_100800 {ECO:0000313|EMBL:KGO60815.1};
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:KGO60815.1, ECO:0000313|Proteomes:UP000030143};
RN   [1] {ECO:0000313|EMBL:KGO60815.1, ECO:0000313|Proteomes:UP000030143}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MD-8 {ECO:0000313|EMBL:KGO60815.1,
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   -!- PTM: Carbamylation allows a single lysine to coordinate two divalent
CC       metal cations. {ECO:0000256|PIRSR:PIRSR611778-50}.
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:KGO60815.1}.
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DR   EMBL; JQFZ01000062; KGO60815.1; -; Genomic_DNA.
DR   RefSeq; XP_016601825.1; XM_016747350.1.
DR   EnsemblFungi; KGO60815; KGO60815; PEX2_100800.
DR   GeneID; 27682770; -.
DR   OrthoDB; 719800at2759; -.
DR   Proteomes; UP000030143; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   CDD; cd01314; D-HYD; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR011778; Hydantoinase/dihydroPyrase.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR011612; Urease_alpha_N_dom.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   Pfam; PF00449; Urease_alpha; 1.
DR   SUPFAM; SSF51338; SSF51338; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000030143}.
FT   DOMAIN          5..45
FT                   /note="Urease_alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00449"
FT   DOMAIN          56..489
FT                   /note="Amidohydro-rel"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
FT   MOD_RES         168
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611778-50"
SQ   SEQUENCE   518 AA;  57276 MW;  00FB0A2FDEFFDDA5 CRC64;
     MAPNFDLVVI NATIVTASDI SKCCIGIKDG KIQSLANSFT DDELTGAEII DAEGAYVMPG
     GVDAHVHLCQ DLKTGPHGLG GECSDNFETG SRSAVAGGTT TIITFATQTR AEEDRSLLKV
     AERYNARAEE TGSYVDYGFH IIIVRNDADI LENELPVLIK DWGISSCKLF LTYATQRLTD
     SQMLDVMFAA RKNSITTMIH AENGDMIEWL TEKLESKGMV APYYHALSRP PIVEGEATNR
     AIALAQLIQN PILFVHVGSV LGAANVRRAQ TMGLPVYAET CPQYFHLTWD DLKRFHSPTC
     FENSKMICSP PPPPTKADHE ELFVGLSNGT FTIYSSDHCP FRYDHPHGKP SGVLEHEASM
     AGEKPCSGEE LQDLLERKEG AFRFIPNGIP GVETRLPLLY TGALASGRIT PQRFVELTST
     NPAKLYGLYP KKGALMPGSD ADFVIWHPEK TFSPFNLTNS MLHHNVDYTP YEGMRFTNWP
     RYTILRGKVM WANGKITGKV RDGEADRDAR SVADWLYE
//
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