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Database: UniProt/TrEMBL
Entry: A2QFL7_ASPNC
LinkDB: A2QFL7_ASPNC
Original site: A2QFL7_ASPNC 
ID   A2QFL7_ASPNC            Unreviewed;       779 AA.
AC   A2QFL7;
DT   06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2007, sequence version 1.
DT   19-MAR-2014, entry version 51.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase;
DE            EC=3.4.19.12;
GN   ORFNames=An02g14990;
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=425011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513;
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G.,
RA   Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K.,
RA   Andersen M.R., Bendtsen J.D., Benen J.A.E., van den Berg M.,
RA   Breestraat S., Caddick M.X., Contreras R., Cornell M., Coutinho P.M.,
RA   Danchin E.G.J., Debets A.J.M., Dekker P., van Dijck P.W.M.,
RA   van Dijk A., Dijkhuizen L., Driessen A.J.M., d'Enfert C., Geysens S.,
RA   Goosen C., Groot G.S.P., de Groot P.W.J., Guillemette T.,
RA   Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA   van den Hondel C.A.M.J.J., van der Heijden R.T.J.M.,
RA   van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P.,
RA   van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J.E.C.,
RA   Meulenberg R., Menke H., Mortimer M.A., Nielsen J., Oliver S.G.,
RA   Olsthoorn M., Pal K., van Peij N.N.M.E., Ram A.F.J., Rinas U.,
RA   Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., Ussery D., Varga J.,
RA   Vervecken W., van de Vondervoort P.J.J., Wedler H., Woesten H.A.B.,
RA   Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory
RT   Aspergillus niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
CC   -!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
CC       thioester, amide, peptide and isopeptide bonds formed by the C-
CC       terminal Gly of ubiquitin (a 76-residue protein attached to
CC       proteins as an intracellular targeting signal).
CC   -!- SIMILARITY: Belongs to the peptidase C19 family.
CC   -!- SIMILARITY: Contains USP domain.
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DR   EMBL; AM270041; CAK37985.1; -; Genomic_DNA.
DR   RefSeq; XP_001400628.1; XM_001400591.2.
DR   RefSeq; XP_003188599.1; XM_003188551.1.
DR   ProteinModelPortal; A2QFL7; -.
DR   STRING; 5061.CADANGAP00002950; -.
DR   MEROPS; C19.A65; -.
DR   EnsemblFungi; CADANGAT00003024; CADANGAP00002950; CADANGAG00003024.
DR   GeneID; 4980038; -.
DR   KEGG; ang:ANI_1_2082024; -.
DR   HOGENOM; HOG000162311; -.
DR   KO; K11836; -.
DR   OrthoDB; EOG74TX7J; -.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008242; F:omega peptidase activity; IEA:InterPro.
DR   GO; GO:0004221; F:ubiquitin thiolesterase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   Gene3D; 3.30.40.10; -; 3.
DR   InterPro; IPR018200; Pept_C19ubi-hydrolase_C_CS.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR009060; UBA-like.
DR   InterPro; IPR015940; UBA/transl_elong_EF1B_N_euk.
DR   InterPro; IPR000449; UBA/Ts_N.
DR   InterPro; IPR016652; Ubiquitinyl_hydrolase.
DR   InterPro; IPR028889; UCH/PAN2.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR001607; Znf_UBP.
DR   Pfam; PF00627; UBA; 2.
DR   Pfam; PF00443; UCH; 1.
DR   Pfam; PF02148; zf-UBP; 2.
DR   PIRSF; PIRSF016308; UBP; 1.
DR   SMART; SM00165; UBA; 2.
DR   SMART; SM00290; ZnF_UBP; 2.
DR   SUPFAM; SSF46934; SSF46934; 1.
DR   PROSITE; PS50030; UBA; 2.
DR   PROSITE; PS00972; UCH_2_1; 1.
DR   PROSITE; PS00973; UCH_2_2; 1.
DR   PROSITE; PS50235; UCH_2_3; 1.
DR   PROSITE; PS50271; ZF_UBP; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Hydrolase; Metal-binding; Protease; Thiol protease;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
SQ   SEQUENCE   779 AA;  86773 MW;  9A7E4965561C8AE1 CRC64;
     MASCCHVTSE GLRIPASSQV VYREDCTQCF DSIDEEHGLN VCLTCFNGGC AGDRNHAFLH
     YERCSHPLAL NIKRSRKNVQ RDEPPQKISK LAIAAETDED RYVTKTRVVC YPCCQNDLDA
     SRGRLPAVID GVMKAMTFSK REEVKAWEQE FIPCEHTINL IQGASRQIES KELVQCSMCN
     LKENLWLCLE CGNLGCGRSQ FGGVGGNSHA LAHSDIKSHA VAVKLGSITA DGSADVYCYR
     CNEERTDPNL ATHLANWGIN LAGREKTEKS LMEMQVEQNM RWEFSMTSED GHELTPVFGP
     GLTGLTNLGN SCYLSSVVQC LFALPEFQKR YYHPNSEPPH TQRPAEDLET QLRKLADGIL
     SGRYSRPDSD VRSSPDSAEV PHQKGLAPAM FKHLVGRNHE EFSTMRQQDA FEFMLHLFKQ
     INLSKHPGGL DNPITSFGFS MQQRLQCLQC KKVRYRADAQ DNISIPVPAR RLPDANASGS
     TNEYESVTLA ECLDAFTAEE VVEFSCPSCG STEGFNKQSS FKTLPQKLVI NARRFELINW
     VPTKLNIPVE VDEEPIDFGT YLSSGPNPDE ELLPDIQEPE NTFKPNEIAM EQLVGMGFPN
     TRCERALYVT GNSDVEAAMN WLFAHMEDPD IDEPLDKVVT STSGSQQDPA KVAQLTEMGI
     NSGHARRALA ATEGDLNRAI DWVFTHPEDS MDIGSDSDIP ESSDIHLDSD ATPAKYQLQS
     IVCHKGSSVH AGHYVAIVRK AVPGSNGTRW VMFNDEKVVQ VDDIQEMKKF AYIYVFSRT
//
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