ID A2QFL7_ASPNC Unreviewed; 779 AA.
AC A2QFL7;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 03-APR-2013, entry version 43.
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; Trichocomaceae;
OC mitosporic Trichocomaceae; 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.
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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 EnsemblFungi; CADANGAT00003024; CADANGAP00002950; CADANGAG00003024.
DR GeneID; 4980038; -.
DR KEGG; ang:ANI_1_2082024; -.
DR HOGENOM; HOG000162311; -.
DR KO; K11836; -.
DR OrthoDB; EOG470XRN; -.
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.
DR InterPro; IPR009060; UBA-like.
DR InterPro; IPR000449; UBA/transl_elong_EF1B_N.
DR InterPro; IPR015940; UBA/transl_elong_EF1B_N_euk.
DR InterPro; IPR016652; Ubiquitinyl_hydrolase.
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; UBA_like; 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
//
