(data stored in SCRATCH zone)

SWISSPROT: Q757G0_ASHGO

ID   Q757G0_ASHGO            Unreviewed;      1013 AA.
AC   Q757G0;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 2.
DT   11-DEC-2019, entry version 96.
DE   SubName: Full=AER053Cp {ECO:0000313|EMBL:AAS52737.2};
GN   ORFNames=AGOS_AER053C {ECO:0000313|EMBL:AAS52737.2};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS52737.2, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS52737.2, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|RuleBase:RU004447}.
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DR   EMBL; AE016818; AAS52737.2; -; Genomic_DNA.
DR   RefSeq; NP_984913.2; NM_210267.2.
DR   STRING; 33169.AAS52737; -.
DR   MEROPS; M16.008; -.
DR   EnsemblFungi; AAS52737; AAS52737; AGOS_AER053C.
DR   GeneID; 4621116; -.
DR   KEGG; ago:AGOS_AER053C; -.
DR   HOGENOM; HOG000161331; -.
DR   InParanoid; Q757G0; -.
DR   KO; K01408; -.
DR   OMA; HGNLYKE; -.
DR   Proteomes; UP000000591; Chromosome V.
DR   GO; GO:0019898; C:extrinsic component of membrane; IEA:EnsemblFungi.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:EnsemblFungi.
DR   GO; GO:0071432; P:peptide mating pheromone maturation involved in positive regulation of conjugation with cellular fusion; IEA:EnsemblFungi.
DR   GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; IBA:GO_Central.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR001431; Pept_M16_Zn_BS.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   InterPro; IPR032632; Peptidase_M16_M.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 2.
DR   Pfam; PF16187; Peptidase_M16_M; 1.
DR   SUPFAM; SSF63411; SSF63411; 4.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q757G0.
DR   SWISS-2DPAGE; Q757G0.
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591}.
FT   DOMAIN          79..216
FT                   /note="Peptidase_M16"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          243..420
FT                   /note="Peptidase_M16_C"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          427..708
FT                   /note="Peptidase_M16_M"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          713..894
FT                   /note="Peptidase_M16_C"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   1013 AA;  116065 MW;  BF3B53699044669C CRC64;
     MIFLSSVQLR RFYTSHFIHR HLQVQSATRR SNLSPLFYSR SMSNNISGVS GLRELAATLE
     QPLLDDRKYR YIELPNHLRV LLVHDKNTDK SAASLDVNVG AFEDPEDLPG LAHFCEHLLF
     MGSKKFPNEN EYASFLSKHG GASNAYTASQ NTNYYFHVNH ENLYDALDRF SGFFSCPLFN
     ESSTEKEIKA VDSENKKNLQ NDMWRLYQLG KSLTNPIHPY HKFSTGNFET LWSIPRSKGV
     NVRDELLKFY NRSYSANLMK LVILGREDLD TLAQWAYELF KDVPNHGTKV PEYHAQAFTP
     EHLMKVIKVK PVKNLKSVEI SFVVPDMDKH WQVKPARYLS HLIGHEGTDS LLAYLKNNSW
     AIDLSAGATT VSEGNAYFSV NVDLTDEGVV QYEAVICAVF QYINMLKEVL PQEWVFTELK
     DIGEAHFKFK QKGNPAATVS SLSKNLQKAY LPVQVILNTS LMRQYEPGLI MEYLNSLTLE
     NSRVMLISQK VETNLSERWY GTEYSVADYT KDFVSKIRSL GANPALKIPA PNEFIATRFD
     VHKDEGNVKP LLEPFLLRDD RCGKLWYKKD DMFWVPKGYI YISMKLPHTH SSIVNSMLCT
     LYVDHINDSL KDLAYNAECA GLEISLRKTN QGLDLSLSGY NDKLLVLLAR FFEGIQKLFL
     REERFMVLKQ RLIQKLHNHL YDTPYTQIGR LYSSLINERS WTTQEKLDIT EQLTFDHLAN
     FVPTIYEQMY FELLVHGNFS HEEALEVYDL VSSLVPNEIR NSEGRNSKLR SYFIPAGGAY
     HYETALADKE NVNSCIQKVI QLGAYSELLS AKGSLLAQMV NEPCFNTLRT EEQLGYVVFS
     SKLNTHGTVN LRILVQSERS SSYLESRIDN FLSKFGSTLE MMSDAEFEKH KDALCKTLQQ
     KYRNLGEEND RYVTCIYLGD YNFLYKERKA QLVRQLTKKE MLDFYQQTIC SKQAASLVVH
     MQAQAGVQDS PADKVDGYPT GNAITDVGAF KSQLYLAPIR APIKKFEVTT PKL
//

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