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Database: UniProt
Entry: A0A0F4GJQ9_9PEZI
LinkDB: A0A0F4GJQ9_9PEZI
Original site: A0A0F4GJQ9_9PEZI 
ID   A0A0F4GJQ9_9PEZI        Unreviewed;       518 AA.
AC   A0A0F4GJQ9;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   22-NOV-2017, entry version 11.
DE   SubName: Full=Aspartyl aminopeptidase like protein {ECO:0000313|EMBL:KJX97626.1};
GN   ORFNames=TI39_contig476g00012 {ECO:0000313|EMBL:KJX97626.1};
OS   Zymoseptoria brevis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Dothideomycetidae; Capnodiales; Mycosphaerellaceae;
OC   Zymoseptoria.
OX   NCBI_TaxID=1047168 {ECO:0000313|EMBL:KJX97626.1, ECO:0000313|Proteomes:UP000033647};
RN   [1] {ECO:0000313|EMBL:KJX97626.1, ECO:0000313|Proteomes:UP000033647}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Zb18110 {ECO:0000313|EMBL:KJX97626.1,
RC   ECO:0000313|Proteomes:UP000033647};
RA   Grandaubert J., Bhattacharyya A., Stukenbrock E.H.;
RT   "RNA-seq based gene annotation and comparative genomics of four
RT   Zymoseptoria species reveal species-specific pathogenicity related
RT   genes and transposable element activity.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KJX97626.1}.
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DR   EMBL; LAFY01000468; KJX97626.1; -; Genomic_DNA.
DR   EnsemblFungi; KJX97626; KJX97626; TI39_contig476g00012.
DR   Proteomes; UP000033647; 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; 2.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:KJX97626.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000033647};
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:UP000033647};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   518 AA;  56393 MW;  E4D72F1CFE673F81 CRC64;
     MASQEALKRP ADFVDFLNAS PTPFHAVHSA KLRLEKAGFR QIKERDSWNS TLQPGGKYYL
     TRNTSTIVAF AIGSAWKPGN PVGMVGAHTD SPCLRIKPVS KRSADGFLQV GVETYGGGLW
     HTWFDRDLGV AGRVMVKGKG KDSLVEQKLV RISKPILRIP NLAVHFGGSE PFEFNKENQL
     FPITGLVSAE LNRTGKTAEQ SRTEESEKEK NADYEPLKTA TQRHHPYLIS MIAKEAGVQP
     DDILDFELVL FDTQPSCIGG LNDEFVFSAR LDNLGMTYCA VEGLIQSVAS TSALKDDPTI
     RLIACFDHEE IGSQSAQGAD SNMLPAVIRR LSCLPSSSTD SEKSYDKVSH SDAGADNSTA
     YEQTLSTSFL ISADMAHSVN PNYGAKYESE HRPHMNEGTV IKVNANVRYA TNAPGIVLLQ
     ECAKRAKPSS YQLPGAKSSS AGVPLQLFVV RNDSRCGSTI GPMLSAALGA RTIDVGNPQL
     AMHSIRETCG AYDAEHGVNL FDSFFEHFGE LEAKIMVD
//
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