(data stored in SCRATCH zone)

SWISSPROT: Q4WCT7_ASPFU

ID   Q4WCT7_ASPFU            Unreviewed;       571 AA.
AC   Q4WCT7;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   11-DEC-2019, entry version 98.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE            EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN   ORFNames=AFUA_6G02380 {ECO:0000313|EMBL:EAL85801.1};
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL85801.1, ECO:0000313|Proteomes:UP000002530};
RN   [1] {ECO:0000313|EMBL:EAL85801.1, ECO:0000313|Proteomes:UP000002530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC   {ECO:0000313|Proteomes:UP000002530};
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.,
RA   Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A.,
RA   Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H.,
RA   Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K.,
RA   Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P.,
RA   Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y.,
RA   Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S.,
RA   Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA   Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H.,
RA   Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M.,
RA   Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D.,
RA   Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G.,
RA   Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H.,
RA   Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.,
RA   Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC         and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC         residue protein attached to proteins as an intracellular targeting
CC         signal).; EC=3.4.19.12; Evidence={ECO:0000256|RuleBase:RU366025};
CC   -!- SIMILARITY: Belongs to the peptidase C19 family.
CC       {ECO:0000256|RuleBase:RU366025, ECO:0000256|SAAS:SAAS01045498}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EAL85801.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AAHF01000012; EAL85801.1; -; Genomic_DNA.
DR   RefSeq; XP_747839.1; XM_742746.1.
DR   STRING; 746128.CADAFUBP00009325; -.
DR   PRIDE; Q4WCT7; -.
DR   EnsemblFungi; EAL85801; EAL85801; AFUA_6G02380.
DR   GeneID; 3505260; -.
DR   KEGG; afm:AFUA_6G02380; -.
DR   EuPathDB; FungiDB:Afu6g02380; -.
DR   HOGENOM; HOG000202292; -.
DR   InParanoid; Q4WCT7; -.
DR   KO; K11843; -.
DR   OMA; NNSGYYE; -.
DR   OrthoDB; 600543at2759; -.
DR   Proteomes; UP000002530; Chromosome 6.
DR   GO; GO:0036459; F:thiol-dependent ubiquitinyl hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016579; P:protein deubiquitination; IEA:UniProtKB-UniRule.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   Pfam; PF00240; ubiquitin; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SMART; SM00213; UBQ; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 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; Q4WCT7.
DR   SWISS-2DPAGE; Q4WCT7.
KW   Hydrolase {ECO:0000256|RuleBase:RU366025, ECO:0000313|EMBL:EAL85801.1};
KW   Protease {ECO:0000256|RuleBase:RU366025};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002530};
KW   Thiol protease {ECO:0000256|RuleBase:RU366025};
KW   Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT   DOMAIN          2..76
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50053"
FT   DOMAIN          109..565
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          395..447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        395..441
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   571 AA;  63221 MW;  CF843B544E36E308 CRC64;
     MFSVIVKHQG KRHEVELDPS ANGETLKYQM YSLTGVEPER QKILVKGGQL KDETPLSALN
     AKPGQTFMMM GTPSGGQDAV DLGRPKEPVK FLEDMTEAEA ARAEGAIPAG LQNLGNTCYL
     NSTLQTLRSV PELQQELLNY KPSAGSSAGS RLSDLSSLGL GGLGASMDLV SSLRDLFKQM
     SETQEGFPPL MFLNALRSVF PQFAQKDRNG HGYAQQDAEE AWSQIVTQLR SKLVIKEGEG
     DSATEVSFVD KFLAGRFESV TECDDPAAKA AGEEATKSSD IFFKLDCHIG KETNHLHDGI
     LAGLEEKIEK RSPTLDRDAV YTKRSRIARL PKYLTVHFVR FFWKRETQKK AKIMRKVTFP
     AELDVVEFCT EELKKQLIPI RDKVRDIRKE EVDVERARKR QKLAHQREEE LKRAAESDAG
     LEPLQKKKAT EGQKEATKSG EQDGDTAMTD VFKSDAEYEA EKYASILAAK KELAALIDPK
     LASDAGTNNS GLYELRAVIT HQGASADSGH YTSYVKKQPN GKGVEDGKWW WFNDEKVTEV
     DGEKIETLAG GGESHSALIL LYRAVDLPTA E
//

If you have problems or comments...

PBIL Back to PBIL home page