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Database: UniProt
Entry: A0A0C3P3Z9_PHLGI
LinkDB: A0A0C3P3Z9_PHLGI
Original site: A0A0C3P3Z9_PHLGI 
ID   A0A0C3P3Z9_PHLGI        Unreviewed;       466 AA.
AC   A0A0C3P3Z9;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   07-JUN-2017, entry version 10.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KIP12679.1};
GN   ORFNames=PHLGIDRAFT_97275 {ECO:0000313|EMBL:KIP12679.1};
OS   Phlebiopsis gigantea 11061_1 CR5-6.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Polyporales; Phanerochaetaceae; Phlebiopsis.
OX   NCBI_TaxID=745531 {ECO:0000313|EMBL:KIP12679.1, ECO:0000313|Proteomes:UP000053257};
RN   [1] {ECO:0000313|EMBL:KIP12679.1, ECO:0000313|Proteomes:UP000053257}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=11061_1 CR5-6 {ECO:0000313|EMBL:KIP12679.1,
RC   ECO:0000313|Proteomes:UP000053257};
RX   PubMed=25474575;
RA   Hori C., Ishida T., Igarashi K., Samejima M., Suzuki H., Master E.,
RA   Ferreira P., Ruiz-Duenas F.J., Held B., Canessa P., Larrondo L.F.,
RA   Schmoll M., Druzhinina I.S., Kubicek C.P., Gaskell J.A., Kersten P.,
RA   St John F., Glasner J., Sabat G., Splinter BonDurant S., Syed K.,
RA   Yadav J., Mgbeahuruike A.C., Kovalchuk A., Asiegbu F.O., Lackner G.,
RA   Hoffmeister D., Rencoret J., Gutierrez A., Sun H., Lindquist E.,
RA   Barry K., Riley R., Grigoriev I.V., Henrissat B., Kues U., Berka R.M.,
RA   Martinez A.T., Covert S.F., Blanchette R.A., Cullen D.;
RT   "Analysis of the Phlebiopsis gigantea genome, transcriptome and
RT   secretome provides insight into its pioneer colonization strategies of
RT   wood.";
RL   PLoS Genet. 10:E1004759-E1004759(2014).
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; KN840438; KIP12679.1; -; Genomic_DNA.
DR   EnsemblFungi; KIP12679; KIP12679; PHLGIDRAFT_97275.
DR   Proteomes; UP000053257; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR   GO; GO:0000328; C:fungal-type vacuole lumen; IEA:EnsemblFungi.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:EnsemblFungi.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0061077; P:chaperone-mediated protein folding; IEA:EnsemblFungi.
DR   InterPro; IPR001948; Peptidase_M18.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386};
KW   Complete proteome {ECO:0000313|Proteomes:UP000053257};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|RuleBase:RU004386};
KW   Protease {ECO:0000256|RuleBase:RU004386};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053257};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   466 AA;  50656 MW;  3785B85914C1007A CRC64;
     MMIPQAGPEA ATRLISFVNA SPTPFHAVRT ASVRLEQAGF RKIREADDWD GVLQPGGKYY
     LTRNQSALLA FTLPQKWKPG AGLSIVATHI DSPNLRVRPV SKKTKYGYLQ VGVETYGGGI
     WHSWFDRDLS LAGRVVVTNK NGGFTPKLIK IDRPLLRIPT LAIHLDRTVS DGFKFNKETE
     FTPIAGLAEN ELNSDKPADK EAGASSIQNN HHSALLAVLS EELSVAPEEI HDFELHLYDV
     QPASFAGLSN EFIFSPRLDN QLSSFAAVDA IAGHVSSPAF TTLEGNVNCI ALFNHEEIGS
     VSTSGAESSL IPSLLHRLSP SPQVAAQSIA RSFLVSCDVG HAIHPNYSSK HEENHAPKMN
     GGVVIKTNAS QRYASDSIGS FVIKKLIEKK GGKVQEYEVR NDMACGSTVG PMLSKIGIRT
     VDIGLGILSM HSIREQCGAK DPQNLIDLFT SFFEGFAELD KELIVD
//
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