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Database: UniProt
Entry: U4LP22_PYROM
LinkDB: U4LP22_PYROM
Original site: U4LP22_PYROM 
ID   U4LP22_PYROM            Unreviewed;       512 AA.
AC   U4LP22;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   22-NOV-2017, entry version 16.
DE   SubName: Full=Similar to Aspartyl aminopeptidase acc. no. Q2UPZ7 {ECO:0000313|EMBL:CCX33896.1};
GN   ORFNames=PCON_02138 {ECO:0000313|EMBL:CCX33896.1};
OS   Pyronema omphalodes (strain CBS 100304) (Pyronema confluens).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC   Pezizales; Pyronemataceae; Pyronema.
OX   NCBI_TaxID=1076935 {ECO:0000313|EMBL:CCX33896.1, ECO:0000313|Proteomes:UP000018144};
RN   [1] {ECO:0000313|EMBL:CCX33896.1, ECO:0000313|Proteomes:UP000018144}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 100304 {ECO:0000313|Proteomes:UP000018144};
RC   TISSUE=Vegetative mycelium {ECO:0000313|EMBL:CCX33896.1};
RX   PubMed=24068976; DOI=10.1371/journal.pgen.1003820;
RA   Traeger S., Altegoer F., Freitag M., Gabaldon T., Kempken F.,
RA   Kumar A., Marcet-Houben M., Poggeler S., Stajich J.E., Nowrousian M.;
RT   "The genome and development-dependent transcriptomes of Pyronema
RT   confluens: a window into fungal evolution.";
RL   PLoS Genet. 9:e1003820-e1003820(2013).
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; HF936249; CCX33896.1; -; Genomic_DNA.
DR   EnsemblFungi; CCX33896; CCX33896; PCON_02138.
DR   OrthoDB; EOG092C3JCE; -.
DR   Proteomes; UP000018144; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; 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   InterPro; IPR023367; Peptidase_M42_dom2.
DR   PANTHER; PTHR28570; PTHR28570; 1.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
DR   SUPFAM; SSF101821; SSF101821; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:CCX33896.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000018144};
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:UP000018144};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   512 AA;  55947 MW;  E8B712FA2CA7B6F5 CRC64;
     MSALSQSSRK YALDFLSFVN ASPTPFHAVE SAKQRLLKAG FSEIRERDSW TNTVKKGGRY
     FLTRNGSSII AFGVGKKWQP GNGMALLGAH TDSPALRIKP VSKKFGENGS YIQVGVETYG
     GGLWHTWFDR DLSIAGRAMV KGENGNIISK LIKIDAPILR IPTLAIHLDR QENFAFNKET
     QLFPIAGLAT AALNKKDGND NTASADASDE FSPLAAITER HHAPIVERIA KEAGVNVKDI
     IDFEMILYDT HQSCLGGMND EFIYSGRLDN LMMSYCSVEG LIESLAHSTS LDEESGIRLI
     SLFDHEEIGS QTAQGADSNL LPAVIRRLSI LPCEGAAKVP EGSAYEECLI KSMLWSCDQA
     HAVHPNYPAK YESSHRPEMN KGPVIKINAN ARYATNSPGI VLTQEVAKLA EVPLQLFVVR
     NDSSCGSTIG PMLSAALGAR TVDMGNPQLS MHSIRETGGS ADVEHAVKLF RSYFEHYSAL
     EPKILVDHID SGTVIEFVLW VPVKLIRKWS GG
//
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