ID A1C7E2_ASPCL Unreviewed; 1480 AA.
AC A1C7E2;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=ACLA_073480 {ECO:0000313|EMBL:EAW14313.1};
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW14313.1, ECO:0000313|Proteomes:UP000006701};
RN [1] {ECO:0000313|EMBL:EAW14313.1, ECO:0000313|Proteomes:UP000006701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC {ECO:0000313|Proteomes:UP000006701};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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|ARBA:ARBA00000707};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085}.
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; DS027045; EAW14313.1; -; Genomic_DNA.
DR RefSeq; XP_001275739.1; XM_001275738.1.
DR STRING; 344612.A1C7E2; -.
DR EnsemblFungi; EAW14313; EAW14313; ACLA_073480.
DR GeneID; 4707925; -.
DR KEGG; act:ACLA_073480; -.
DR VEuPathDB; FungiDB:ACLA_073480; -.
DR eggNOG; KOG1870; Eukaryota.
DR HOGENOM; CLU_001060_9_0_1; -.
DR OMA; KPRGCTG; -.
DR OrthoDB; 5474185at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR CDD; cd02674; Peptidase_C19R; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR Gene3D; 3.30.2230.10; DUSP-like; 1.
DR InterPro; IPR035927; DUSP-like_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR006615; Pept_C19_DUSP.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF24; USP DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF06337; DUSP; 1.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM00695; DUSP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF143791; DUSP-like; 1.
DR PROSITE; PS51283; DUSP; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:EAW14313.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006701}.
FT DOMAIN 111..234
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 466..1241
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 430..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 861..910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 952..1032
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1254..1480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 863..900
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 997..1023
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1256..1296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1366..1394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1480 AA; 162782 MW; 9D6C9C9C1DA2DF3F CRC64;
MTDMSGSDKG DGSVPPVGDD VRSSSPGVKR TAPDVDHDVE MDLDTTEKRS ASRPQPSTVM
DTTGAEDNGK NGNASSDSVY PTLSSMSTYT APTATRNDSQ SQAARAPHDL PPIDDQVAQV
TCTMAQPLKE KQKGYLLSMS WLSRVLARSS THADKVDKSA AEGEIGPVDN TDLVLVTDPA
STGFKDEAGE PFVPLRPGLQ IGEDFEIVPQ EGWDLIMQWY GLAAQSPAIV RYAHNTVDEG
DAQNIQYELN PPIFTILKLP SPSAGTTPQT LREKNMPPAK VLSSRHTNFQ KWLKQVKGLA
NIDMSTKVRV WRILGGLGSA TASAAITPAA SRSASPAPTV SLVANAGNNL VLDLNTFLSL
SDGAQRELLE IAKDQTNNPN FNGRSTLDRV GLSSSDVVVL EERVGSEWAS ELSKQTLNRL
GVPAGNIKTA VPAKLKNKSP PTSGRSSPIP EPARGRRKDG KPRGCTGLSN LGNTCYMNSA
LQCVRSVEEL TYYFLNDVYK KDLNPSNPLA HNGDVAKAYA NLLRMIYDEA GQSSFAPRQL
KHTIGRYGPA FSGYGQQDSQ EFLLFLLDGL QEDLNRIQKK PYIEKPDSTD EMVHNKDALR
DFATKCWEIY KARNDSVITD LFAGMYKSTL ICPTCEKVSI IFDPFNNLTL QLPIENLWSK
EIFYFPRHRK PVIIDVEIDK NSSIKALKEL VAKKMGSDPQ RLVMAEIYKF KFYKMFDNNT
SIAEYSIGEG DDIAIFELES VPTNYNPDKT QKSFYSYGRS DYEQIPSFDS PKADRMLVPV
FNRVCRPKSN NSRNMQRSLF GAPSYVVINR EDAQDYDAIL RKILEEVATM TTRDILHEQT
ILGVDEQEAS QEDSDTVIMN DEDAESADSK IKTSSVDGED GMVDVSMRDA SDEMDTTSSQ
DTKRDGNSIN PDLRSLFDVK IMKSSTEVVP LGWSSVDEVK DFPLMSSRIK ARPAAKQKKV
NTVDDTGGMK LMQVQKSRPT SVISDVVERK TSDDSDQEGS AGSASDSGSD IFANINRPKT
PKPQSNERPL IRPGEGIVLD WNERAHDALF GWDKKKPDSG LGRPTWTDIE RIPDPELAER
RKLRQTRKKR GVTLYECLDE FNKEEILSEN DAWYCPRCKE HRRASKKFEL WKTPDILVMH
LKRFSASRGF RDKLDVLVDF PVEGLDMSGR VEAPEEGKSL IYDLFAVDNH YGGLGGGHYT
AYAKNFMSGE WNEYNDSSVS RPIDPQSVVT PAAYLLFYRR RSDRPLGGKV LEEITESSTR
PASENNSPAG SRGQSPSGDG RRLGGSSRNG SSSALAGVGA AHQAGDGGLR TGVRARVNDE
DDEDDAPPDY SNSPASGEKS LGKSNRLEGM SFDEDEFGDG AFANPLPYSS QPTWSFDRVT
NAHGLSQMTT VPPGSISDDE EDLFDDDASN KAVGGGDLSD SDLRLGALTG SPISRGVFPS
TPMDEEPPFQ DIPPPLDGDD DEELPVVELR VNDEDRIVSD
//
