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Database: UniProt
Entry: A0A074WT59_9PEZI
LinkDB: A0A074WT59_9PEZI
Original site: A0A074WT59_9PEZI 
ID   A0A074WT59_9PEZI        Unreviewed;       465 AA.
AC   A0A074WT59;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   22-NOV-2017, entry version 12.
DE   SubName: Full=Peptidase M18, aminopeptidase I {ECO:0000313|EMBL:KEQ74739.1};
GN   ORFNames=M436DRAFT_71250 {ECO:0000313|EMBL:KEQ74739.1};
OS   Aureobasidium namibiae CBS 147.97.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Dothideomycetidae; Dothideales; Saccotheciaceae;
OC   Aureobasidium.
OX   NCBI_TaxID=1043004 {ECO:0000313|EMBL:KEQ74739.1, ECO:0000313|Proteomes:UP000027730};
RN   [1] {ECO:0000313|EMBL:KEQ74739.1, ECO:0000313|Proteomes:UP000027730}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 147.97 {ECO:0000313|EMBL:KEQ74739.1,
RC   ECO:0000313|Proteomes:UP000027730};
RX   PubMed=24984952;
RA   Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J.,
RA   Zalar P., Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y.,
RA   Lipzen A., Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT   "Genome sequencing of four Aureobasidium pullulans varieties:
RT   biotechnological potential, stress tolerance, and description of new
RT   species.";
RL   BMC Genomics 15:549-549(2014).
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; KL584706; KEQ74739.1; -; Genomic_DNA.
DR   RefSeq; XP_013429222.1; XM_013573768.1.
DR   EnsemblFungi; KEQ74739; KEQ74739; M436DRAFT_71250.
DR   GeneID; 25414917; -.
DR   Proteomes; UP000027730; Unassembled WGS sequence.
DR   GO; GO:0000324; C:fungal-type vacuole; IEA:EnsemblFungi.
DR   GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:EnsemblFungi.
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:KEQ74739.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000027730};
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:UP000027730};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   465 AA;  49207 MW;  DBD42B42C18010BA CRC64;
     MAVPGNAESY AKPFCDFLTE NPTVFHAVDS MAQGLKHYGF TKLSERDSWR VEPGGKYFVE
     RNGSSLIAFV VGDDYKAGNG AAVLAGHVDA LTAKLKPVSK LPTKAGYVEL GVAPYAGGLG
     PTWWDRDLSI GGRVLVKEGN KIVTKLVKLG WPIAKIPTLA PHFGAPANGP FNLETQVVPI
     IGLESSAKNQ IEPQAKAGTF ASTQPPRLVR AIAKELGLSD GSNIVNWELE LYDIQPATLA
     GLDKEFITAG RIDDKLCSWA ALEALKQSAR NGTTGSGIIK IVGLFDDEEI GSGLRQGARG
     NFLPTVMERA VGSLAGQHPA SDLMGRTYAN SFLVSSDVTH AVNPNFESVY LANHAPELNV
     GVSVSADSNG HMTTDAASTA ILTRCAEKVG ATLQVFQIRN DSRSGGTVGP MLSCATGMRA
     IDAGIPQLSM HSIRATTGTS DPGLGVQMFQ GFLDSFESVD AEFRD
//
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