(data stored in ACNUC7421 zone)

SWISSPROT: Q75CT3_ASHGO

ID   Q75CT3_ASHGO            Unreviewed;      1389 AA.
AC   Q75CT3;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 2.
DT   11-DEC-2019, entry version 107.
DE   SubName: Full=ACL164Cp {ECO:0000313|EMBL:AAS51064.2};
GN   ORFNames=AGOS_ACL164C {ECO:0000313|EMBL:AAS51064.2};
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:AAS51064.2, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS51064.2, 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 C19 family.
CC       {ECO:0000256|SAAS:SAAS01045498}.
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DR   EMBL; AE016816; AAS51064.2; -; Genomic_DNA.
DR   RefSeq; NP_983240.2; NM_208593.2.
DR   STRING; 33169.AAS51064; -.
DR   MEROPS; C19.003; -.
DR   EnsemblFungi; AAS51064; AAS51064; AGOS_ACL164C.
DR   GeneID; 4619360; -.
DR   KEGG; ago:AGOS_ACL164C; -.
DR   HOGENOM; HOG000094458; -.
DR   InParanoid; Q75CT3; -.
DR   KO; K11849; -.
DR   OMA; CDIKVDV; -.
DR   Proteomes; UP000000591; Chromosome III.
DR   GO; GO:0005623; C:cell; IEA:GOC.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; IBA:GO_Central.
DR   GO; GO:0010636; P:positive regulation of mitochondrial fusion; IEA:EnsemblFungi.
DR   GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
DR   GO; GO:0010992; P:ubiquitin recycling; IEA:EnsemblFungi.
DR   GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IEA:EnsemblFungi.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR025305; UCH_repeat_domain.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   Pfam; PF13446; RPT; 3.
DR   Pfam; PF00443; UCH; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q75CT3.
DR   SWISS-2DPAGE; Q75CT3.
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591}.
FT   DOMAIN          677..1375
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          904..930
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          967..1032
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          255..275
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1202..1232
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        967..997
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1389 AA;  157648 MW;  C2603EFE8C371E97 CRC64;
     MNQESREQIE TEQNCELEQG DDGRTVLYGN LARQGPVKTS DRLLDDVRVT VSLSEEGREV
     LRAPMLEYAR QRANARTWSV GYLLDQVVLQ TSFEYTSRTC AQNRVHVFMG VLCDPGQRFA
     SQDELVNYRI YHLRVTVKIR PQLERARQHY GVAQYHLVDE LHPWDKPDFC LFEDGDPAVV
     DSATYVASGT NRLVRIEVLR PEFGPDELQE FTGERIRARY LEVCKRHPDL DPSDIPSQAE
     CLNTLFKVFK NPLSRQKAQD ELKTISADNK VLNSQLEANW LVTKFGFELC EIEEDGQKIY
     EYKPPDFTEH VENWEVRRFR ESYIRKSLEL IFLGKQSLRL VPKDVVVSNS KLRSFQLYQT
     HFSHSFWYHL MGEYDHNDFN QQMHPYDTNY HFVHLSSNYY YSDRDIIKNY EAQIALDPAN
     ASIYYDDLSF VANSKGSKQL LTYTYKQNVV GHEALMSALR LFHLDPSSTD PRQLSDEFLL
     ESYKEVCKDS GPQKHADLRN ALRLLARYKE SDKLKFYVEV EPFPNELQAY KLLEIDESVD
     IDIIETAYSI KVSDAPGLKM DCIRALYTLA VAKRSIILFN ILFQQCPKFH QFYHMSYLSY
     QSALQYLHVN VNATDDLILE IFQRKWSYDP LVSPEQLLNL KIALTKIGFE RNSKLINHFL
     ETGLVDINYL PAGNWPTGIN NIGNTCYLNS LLQYYFTISP LREYILAYDH TASNLLNNAV
     SSSDMGRRRI GGRAISQAEV ERSVQFVYQL RSLFHEMVHS RERYVTPTRE LAYLSFSPSS
     TEVEFEPVPP AVGTASNALV ANEVYNEDTE VIDISMEECD EDSAINELGA SNISVKLDSD
     IGTDSNSNLA TGAQTGIPLD GHTDLNTGIR TCMPNDTAIN MATGNATAPN KGIVNSEANF
     EHLMTPAPHE GTDKPIGNDQ SVVPNLGTSK DTLSAYPKSG YAKTAASALS TNNSAASPDD
     FSVRYQASSD TANTGSTRPN PSSTPESGLS DSAANAEYTS AGPLEDRQAV ENDDSGKDIT
     MVGSPEAEGP ETSTYVAKIS SDQLENTLEI GRQQDVTECI GNVLYQIESA SVPLSLDEEG
     EQFDLVKQLF YGKLKQELIP LEFPDRKRTK IERFMSLLVN IGDHPKDIYD ALDSYFKDDL
     LTLDEDDGKV RRSVAVAELP IMLQIQIQRV YYDREKFMPF KSTEPLPFGE KLYMDRYLAT
     DNAELNAKKQ QAIGLREELE RLRERRRRLL AKNDHGVTLS AALADTRRFL DAAELTSGSR
     QLQEQYHATT SHLDALRVAL DEELAALDAH IASVQDAIAH RFDAFSSYGY SLGAVFIHRG
     EASYGHYWVY IKDCQNGGIW RKYNDESVTE VPESEVFDFS EENTATPYFL VYVKEAHELD
     IEPLKRLLA
//

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