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Database: UniProt
Entry: V5HRK6_BYSSN
LinkDB: V5HRK6_BYSSN
Original site: V5HRK6_BYSSN 
ID   V5HRK6_BYSSN            Unreviewed;       523 AA.
AC   V5HRK6;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   25-OCT-2017, entry version 14.
DE   SubName: Full=Vacuolar aspartyl aminopeptidase Lap4 {ECO:0000313|EMBL:GAD91980.1};
GN   ORFNames=PVAR5_0566 {ECO:0000313|EMBL:GAD91980.1};
OS   Byssochlamys spectabilis (strain No. 5 / NBRC 109023) (Paecilomyces
OS   variotii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Thermoascaceae; Byssochlamys.
OX   NCBI_TaxID=1356009 {ECO:0000313|EMBL:GAD91980.1, ECO:0000313|Proteomes:UP000018001};
RN   [1] {ECO:0000313|Proteomes:UP000018001}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=No. 5 / NBRC 109023 {ECO:0000313|Proteomes:UP000018001};
RX   PubMed=24407650; DOI=10.1128/genomeA.01162-13;
RA   Oka T., Ekino K., Fukuda K., Nomura Y.;
RT   "Draft genome sequence of the formaldehyde-resistant fungus
RT   Byssochlamys spectabilis No. 5 (anamorph Paecilomyces variotii No. 5)
RT   (NBRC109023).";
RL   Genome Announc. 2:E0116213-E0116213(2014).
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:GAD91980.1}.
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DR   EMBL; BAUL01000013; GAD91980.1; -; Genomic_DNA.
DR   EnsemblFungi; GAD91980; GAD91980; PVAR5_0566.
DR   OrthoDB; EOG092C3JCE; -.
DR   Proteomes; UP000018001; 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   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:GAD91980.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000018001};
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:UP000018001};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   523 AA;  56798 MW;  031E02FDC77762A6 CRC64;
     MTKKRVADLQ ASVSTLRLDS DHPSQARYIP VSVHSSQVLP PRLSQPRAAV DSVSPDAYSK
     PFCEFMSSNP TIFHAVEHFS KQLEDHGYKR LSEREVWTSE LKRGGKYYTT RNGSALIAFA
     VGKDYKSGNG VGIVAGHIDA LTAKLKPVPK LPNKAGFRQL GVAPYAGALN STWWDRDLSL
     GGRVLVRDPN TGKVETKLVK LDWPIARIPT LAPHFGAASQ GPFNQETQMV PIIGVDNSDL
     FSESNKAESR SDIPSGTFAA TQPEKLVKVV SKELGITDYS SIVNWELELF DSQPAQLGGL
     EKDLIFAGRI DDKLCCYAAQ EALLASPDEN SPGIVKMVGM FDDEEVGSLL RQGARSNFMS
     SVIERIAEAF APENSYGPNL LSQTVANSFL VSSDVIHAVN PNFLNVYLEN HSPRLNVGVA
     VSADPNGHMT TDSVSSAILK RVADKCGSTL QVFQIRNDSR SGGTIGPMTS ARIGMRAIDA
     GIPQLSMHSI RATTGSLDPG LGVKIFKGFF DYFEEVDAEF QDF
//
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