ID G3XLJ4_ASPNA Unreviewed; 1114 AA.
AC G3XLJ4;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=ASPNIDRAFT_212470 {ECO:0000313|EMBL:EHA28506.1};
OS Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 /
OS NCTC 3858a / NRRL 328 / USDA 3528.7).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=380704 {ECO:0000313|EMBL:EHA28506.1, ECO:0000313|Proteomes:UP000009038};
RN [1] {ECO:0000313|EMBL:EHA28506.1, ECO:0000313|Proteomes:UP000009038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a /
RC NRRL 328 / USDA 3528.7 {ECO:0000313|Proteomes:UP000009038};
RX PubMed=21543515; DOI=10.1101/gr.112169.110;
RA Andersen M.R., Salazar M.P., Schaap P.J., van de Vondervoort P.J.,
RA Culley D., Thykaer J., Frisvad J.C., Nielsen K.F., Albang R., Albermann K.,
RA Berka R.M., Braus G.H., Braus-Stromeyer S.A., Corrochano L.M., Dai Z.,
RA van Dijck P.W., Hofmann G., Lasure L.L., Magnuson J.K., Menke H.,
RA Meijer M., Meijer S.L., Nielsen J.B., Nielsen M.L., van Ooyen A.J.,
RA Pel H.J., Poulsen L., Samson R.A., Stam H., Tsang A., van den Brink J.M.,
RA Atkins A., Aerts A., Shapiro H., Pangilinan J., Salamov A., Lou Y.,
RA Lindquist E., Lucas S., Grimwood J., Grigoriev I.V., Kubicek C.P.,
RA Martinez D., van Peij N.N., Roubos J.A., Nielsen J., Baker S.E.;
RT "Comparative genomics of citric-acid-producing Aspergillus niger ATCC 1015
RT versus enzyme-producing CBS 513.88.";
RL Genome Res. 21:885-897(2011).
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 -!- 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:EHA28506.1}.
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DR EMBL; ACJE01000001; EHA28506.1; -; Genomic_DNA.
DR AlphaFoldDB; G3XLJ4; -.
DR STRING; 380704.G3XLJ4; -.
DR MEROPS; C19.099; -.
DR HOGENOM; CLU_003532_2_1_1; -.
DR Proteomes; UP000009038; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02659; peptidase_C19C; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR002083; MATH/TRAF_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR008974; TRAF-like.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR024729; USP7_ICP0-binding_dom.
DR InterPro; IPR029346; USP_C.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF644; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 7; 1.
DR Pfam; PF00917; MATH; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF14533; USP7_C2; 1.
DR Pfam; PF12436; USP7_ICP0_bdg; 1.
DR SMART; SM00061; MATH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF49599; TRAF domain-like; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50144; MATH; 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:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 55..184
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 210..533
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1114 AA; 128660 MW; 0C2B5FF9FBF39B9C CRC64;
MLVDEYEQYH NDRTDEVVVS RSGSEEPEPE PLADDHAAMM ARILPKDPDL ETEDETYHTW
HIQDWRKLKK KEHGPVFQCA GFPWRVLFFP YGNHVEHASF YLEHAWENEP PANWYACVQF
ALVLSNVNDP SIYISHVATH RFNADEGDWG FTRFCELRRL FSVPWEGRGV PLVQNEEAKI
TAYVRVVKDP TGVLWHSFQN YDSKKETGMV GLKNQGATCY LNSLLQSLYF TNKFRKAVYE
IPTEAEASRD NSAWTLQRLF YNLQTSENSV STTELTASFG WESRQIFEQQ DVQELSRKLM
ERMEEKMKGT PAEKALPEMF VGKTKTYISC INVDYESSRV EDFWDIQLNV RGNKTLDDSF
KDYIQVETLE GENKYDAGQP YGLQDAKKGV IFESFPPVLH LHLKRFEYDI HRDAMMKIND
RHAFPMEFDA SPYLSNDADK SEPWIYELHG VLVHSGDLNA GHYYAFLKPT KDGFWYRFDD
DRVTRATDKE VLEENYGGEY ELANGAAGVR QPYTRGLSTK RSMNAYMLVY VRKSRLDDVL
LPITKEQVPS HIENRLVEER IELARRKKER EEAHLYINVG VLSDESFQAH HGFDLTSADL
PATDPAVPKQ YRILRAKKVG EFAQQLAEEK GLNPEQVRFW VMVNRQNKTT RPDQVIKDQD
MTVEEAYNRY GTKGNPFKVW MEVGQPSADG SISWPDSNSV LVFLKHFDAP SQTIAGVGAV
YVRKTQKVAD LAPIILEKMG WPAGTEFMLF EEIKHNMIDV MKPKQTFQQS EIQDGDIITF
QRTIKESELP ATALYTDARQ YYDYLLNRIN ITFAPIKADE GDEFTLTLSR KMTYDQFSKK
VGEHLNVEST HLRFAPVLAS TGKPKAFIKR NPNQPNQTLY HILGGQATTY GYSMHRQDAL
YYEVLETSLS DFESKTCLKV TWLPEGITKE QLVEVLVPRD GTIADLVAGL QKKANLDDET
IRETRVYETH GGKIYREFQA DSKIAGINEF VSLYAERVPE EEANMQDGER TINAFNFDRE
VNRPHGVPFK FVMKPGEIFK QTKERLSKRT GIKGKQFEKI KFAVVSRNMY SNPRYVEDDD
ILSDIIGDSD DLLGLEHVNK NRNFWNRSES FFIR
//
