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Database: UniProt
Entry: A0A137PJ51_CONC2
LinkDB: A0A137PJ51_CONC2
Original site: A0A137PJ51_CONC2 
ID   A0A137PJ51_CONC2        Unreviewed;       481 AA.
AC   A0A137PJ51;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   22-NOV-2017, entry version 8.
DE   SubName: Full=Peptidase M18, aminopeptidase I {ECO:0000313|EMBL:KXN75024.1};
GN   ORFNames=CONCODRAFT_54022 {ECO:0000313|EMBL:KXN75024.1};
OS   Conidiobolus coronatus (strain ATCC 28846 / CBS 209.66 / NRRL 28638)
OS   (Delacroixia coronata).
OC   Eukaryota; Fungi; Zoopagomycota; Entomophthoromycotina;
OC   Entomophthoromycetes; Entomophthorales; Ancylistaceae; Conidiobolus.
OX   NCBI_TaxID=796925 {ECO:0000313|EMBL:KXN75024.1, ECO:0000313|Proteomes:UP000070444};
RN   [1] {ECO:0000313|EMBL:KXN75024.1, ECO:0000313|Proteomes:UP000070444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 28638 {ECO:0000313|EMBL:KXN75024.1,
RC   ECO:0000313|Proteomes:UP000070444};
RX   PubMed=25977457; DOI=10.1093/gbe/evv090;
RA   Chang Y., Wang S., Sekimoto S., Aerts A.L., Choi C., Clum A.,
RA   LaButti K.M., Lindquist E.A., Yee Ngan C., Ohm R.A., Salamov A.A.,
RA   Grigoriev I.V., Spatafora J.W., Berbee M.L.;
RT   "Phylogenomic Analyses Indicate that Early Fungi Evolved Digesting
RT   Cell Walls of Algal Ancestors of Land Plants.";
RL   Genome Biol. Evol. 7:1590-1601(2015).
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; KQ964418; KXN75024.1; -; Genomic_DNA.
DR   EnsemblFungi; KXN75024; KXN75024; CONCODRAFT_54022.
DR   Proteomes; UP000070444; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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:KXN75024.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000070444};
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:UP000070444};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
FT   SIGNAL        1     20       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        21    481       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5007294906.
SQ   SEQUENCE   481 AA;  52799 MW;  0A11E7F7CE6420A9 CRC64;
     MANLLKYCSV LSFIVGQLTA QENGYPVKND LVGDFINYVN SSPSTYHSVA SSQERLEKAG
     YKRLSEQANW KDQVKPNGKY YVIRGKSSLV AFSVGGNYKS GNGFSIIASH DDSPSLRLKP
     KYNKSNKQYL SAGFATYGDG AWYSWFDRDL GLAGRLVIED KPNHYVSKLV NLNKPIFRIP
     TLAIHLDNTI DRDGFTINPE TELVPIAGTF NAPGAINNTL FVHQLLAEEY KLNPNQIADQ
     DLALYDLNPA TVSLVTEDII TGHRLDSLTM TYAGLRSLID STNDDSLKGD SRVRVFVQFD
     HEKVGSSSYQ GAKSTFLPSI LKRITYTSPS DDGSLQEQAL SDSLLVSAEQ GHAYNPSGAG
     LYESENLVKL NEGPFIGFNL GTKYATNSAT SSHLDSVAKA VNVTLQRRTH RNDVSERATF
     GSALSSLLGV STVDFGTGQL SKNAIREAIG TKDLEQSVQV LTKFYQLPPI KLEDEEGFDE
     L
//
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