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Database: UniProt
Entry: A0A139GTY5_9PEZI
LinkDB: A0A139GTY5_9PEZI
Original site: A0A139GTY5_9PEZI 
ID   A0A139GTY5_9PEZI        Unreviewed;       538 AA.
AC   A0A139GTY5;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   07-JUN-2017, entry version 5.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KXS93627.1};
GN   ORFNames=AC578_782 {ECO:0000313|EMBL:KXS93627.1};
OS   Mycosphaerella eumusae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Dothideomycetidae; Capnodiales; Mycosphaerellaceae;
OC   Mycosphaerella.
OX   NCBI_TaxID=321146 {ECO:0000313|EMBL:KXS93627.1, ECO:0000313|Proteomes:UP000070133};
RN   [1] {ECO:0000313|EMBL:KXS93627.1, ECO:0000313|Proteomes:UP000070133}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 114824 {ECO:0000313|EMBL:KXS93627.1,
RC   ECO:0000313|Proteomes:UP000070133};
RA   Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT   "Comparative genomics of the Sigatoka disease complex on banana
RT   suggests a link between parallel evolutionary changes in
RT   Pseudocercospora fijiensis and Pseudocercospora eumusae and increased
RT   virulence on the banana host.";
RL   Submitted (JUL-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:KXS93627.1}.
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DR   EMBL; LFZN01000428; KXS93627.1; -; Genomic_DNA.
DR   EnsemblFungi; KXS93627; KXS93627; AC578_782.
DR   Proteomes; UP000070133; 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   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:UP000070133};
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:UP000070133};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   538 AA;  59252 MW;  B960E284FC30CEE9 CRC64;
     MLLGHKLRPA VRECSAIRTR VVRIRILSTM ANRRANDFIS FLNASPSPFF AVRSSIERLE
     KAGFTPIKER DSWNQTLQPG GKYYLTRNAS TIVAFAIGHK WKPGNPVAMV GAHTDSPCLR
     VKPVSKRSAD GFLQVGVELY GGGMWHTWFD RDLGVAGRVM VKSKEGVIEQ RLVQISKPVC
     RIPNLAVHFG QPFEPYNKET QLFPVLGLVT AELNRQGKSA EQIKKEEAQK QSSAGFQPLK
     TTVQRHHPYL VELIAKEAGC QAEDVEDFEL VLYDTQPACL GGINEEFVYS ARLDNLGMTY
     CAVEGLIQSL ENDTLKGDST IRLIACFDHE EIGSQSAQGA DSNMLPSVIR RLSCLPPSSD
     DSEKSYDKVN GDANAENSTA YEQTLSTSFL ISADMAHSVN PNYGGSYESE HRPHMNEGTV
     IKINANVRYA TNSPGIVLLQ ECARRAKAAS WQLPEAKTAE GGVPLQLFVV RNDFRCGSTI
     GPMLSAALGA RTIDVGNPQL SMHSIRETGG AYDPEHGVNL FDSFFQHYGE LESKILVD
//
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