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Database: UniProt
Entry: A0A074YBB0_9PEZI
LinkDB: A0A074YBB0_9PEZI
Original site: A0A074YBB0_9PEZI 
ID   A0A074YBB0_9PEZI        Unreviewed;       465 AA.
AC   A0A074YBB0;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   22-NOV-2017, entry version 11.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KEQ95055.1};
GN   ORFNames=AUEXF2481DRAFT_65707 {ECO:0000313|EMBL:KEQ95055.1};
OS   Aureobasidium subglaciale EXF-2481.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Dothideomycetidae; Dothideales; Saccotheciaceae;
OC   Aureobasidium.
OX   NCBI_TaxID=1043005 {ECO:0000313|EMBL:KEQ95055.1, ECO:0000313|Proteomes:UP000030641};
RN   [1] {ECO:0000313|EMBL:KEQ95055.1, ECO:0000313|Proteomes:UP000030641}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EXF-2481 {ECO:0000313|EMBL:KEQ95055.1,
RC   ECO:0000313|Proteomes:UP000030641};
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; KL584760; KEQ95055.1; -; Genomic_DNA.
DR   RefSeq; XP_013343581.1; XM_013488127.1.
DR   EnsemblFungi; KEQ95055; KEQ95055; AUEXF2481DRAFT_65707.
DR   GeneID; 25370133; -.
DR   Proteomes; UP000030641; 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   Complete proteome {ECO:0000313|Proteomes:UP000030641};
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:UP000030641};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   465 AA;  49336 MW;  140DF0235E4A2162 CRC64;
     MATSDNVETY AKPFCDFLTN NPTVFHAVDD MAQGLKRDGF TKLSERDSWR IEAGGKYFVE
     RNGSSLIAFV VGDDYKSGNG AAVLAGHVDA LTAKLKPVSK VPNKAGYVEL GVAPYAGGLG
     PTWWDRDLSI GGRVLVKEGN KIATKLVKLG WPIAKIPTLA PHFGAPANGP FNLETQVVPI
     IGLESSAKSQ IETQGKVGSF AATQPPRLVR AITKELGVSD ASSIVNWELE LFDLQPATLA
     GLDKEFITAG RIDDKLCSWA ALEALKQSAR NGTSGSGIIK MVGLFDDEEI GSGLRQGARG
     NFLPIVMERA VGSLAGQHPA SDLMGRTYAN SFLVSSDVTH AVNPNFENVY LANHAPELNV
     GVVVSADSNG HMTTDGVSTA IFTRCAEKVN ATLQVFQIRN DSRSGGTVGP MLSCATGMRA
     IDAGIPQLSM HSIRATTGTS DPGLGVQMFQ GFLDGFESVD AEFRD
//
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