ID A0A0D2GZS9_9EURO Unreviewed; 1595 AA.
AC A0A0D2GZS9;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=Z517_07772 {ECO:0000313|EMBL:KIW77939.1};
OS Fonsecaea pedrosoi CBS 271.37.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1442368 {ECO:0000313|EMBL:KIW77939.1, ECO:0000313|Proteomes:UP000053029};
RN [1] {ECO:0000313|EMBL:KIW77939.1, ECO:0000313|Proteomes:UP000053029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 271.37 {ECO:0000313|EMBL:KIW77939.1,
RC ECO:0000313|Proteomes:UP000053029};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Fonsecaea pedrosoi CBS 271.37.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; KN846973; KIW77939.1; -; Genomic_DNA.
DR RefSeq; XP_013281747.1; XM_013426293.1.
DR AlphaFoldDB; A0A0D2GZS9; -.
DR STRING; 1442368.A0A0D2GZS9; -.
DR GeneID; 25307262; -.
DR VEuPathDB; FungiDB:Z517_07772; -.
DR HOGENOM; CLU_001060_9_0_1; -.
DR OrthoDB; 5474185at2759; -.
DR Proteomes; UP000053029; 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 Reference proteome {ECO:0000313|Proteomes:UP000053029}.
FT DOMAIN 158..282
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 506..1317
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 870..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 992..1104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1337..1442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1459..1595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1016..1032
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1067..1086
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1337..1355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1480..1502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1529..1543
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1595 AA; 175377 MW; A1C6E5AB36F5C9B1 CRC64;
MPASSQKHPN HQNQNLSQSK DDLGRHLRSA SPAVKRPASD MGAQDRESYN SDVEMGEGQI
PGSGSGFTPV NPDTVPAGSQ DTLKAKQQDT GSRHRDILAT NRLIHNSDPR AVQQSAAASL
SDNSGSSTTD SLFPSPSNRS TAATSLDADV PSTATSIPSI DDQIAQVTAL WQKELEEGQK
GYLISAKWFQ KVQARGSLPA GVGKIEKSAT EGEIGPVDNS DIAMVIDEDV KLTDEAGEKY
VPLRPGLTLD EDYRVFPQEA WDLIISWYGL AKDSPVITRY AHDWGGADAA MPNVTWELNP
PLFSFLKVPS EHTTQTQREK DLPPQRMIAS KKTLCNDWLK EGKRLLHVDM NTKVRVWRIL
GGLKNATASG GLTPSASRSV SPAPGAEIVA TAGDKMLLDV NTFIHLQIGE HRELLTEIKD
NTTNPNYNGK TLTLSLVGLG RNEEVIVLEE QKSGKDEWPS ESSKLNLTKG IKSAAKNLTP
SGRSSPAPGM MTRGRQKRDG RPRGITGLSN LGNTCYMNSA LQCIRSVEEL TQFFLHDQWK
QDLNVDNPLG HHGEIAKAYA NLLHQIYDEN ASSTNPSRFK ATIGKYGSSF SGYQQQDSQE
FLLFLLDGLQ EDLNRIHKKP YIEKPDSTDE MVHDSAALQA FAQKNWEIYK ARNDSVVTDL
FAGMYKSTLT CPVCNKVSII FDPFNNLTLQ LPIENNWQKE ILYFPLHKRP VRIDVDIDKH
STIKALKEFV ALRTHADVER LLVAESYKNK IYKIFDNYVV ISEANIQTSD IICMYELESV
PTNYNPNKAR KFSLYMTKSD ADDEMVEADS PEADRLLVPM YNRLVKNPSA RVSSKPFFGQ
PTYLVLSRED RSTYDGVMKK ILGNITGMTT KRIHDEEDSP SDDGLGTPEG SDTMVMTDDM
SSSGSGLPIA TSVQGEDGLV DVSMRDASQA PELRPQSTEA GLQKLLLSKS PVPRRFQQLF
DVQVTSTGEG IPTGWNQISE TGEYESIKNR IPKPVSRSVK PAGGLGLANG ESGSAESEDE
LADIETDDTP MDSNESGSEA SPVFPSGPDS ESELQEPQEI LPSRNKKAHK YGKNKNRGKF
SARRTQHRRS PLPPPQPLPK AQTGDLIRPG EAIILDWSQD GYDALFGGSE DGSEGYRGLP
TWKSVGLLPD PETAAKREQR NSRKKHGITL VDCLNEFGKS ETLSEQNAWY CPRCKEHRRA
DKMFELWKAP DILVMHLKRF SSNRNFRDKL EVKVDYPIEG LDLSEMVRDQ QDGKSLIYDL
IAVDNHYGGL GGGHYTAYAK NFYNNSWYEY NDSHVSSKTD PRSVVTSAAY LLFYRRRSDH
PLGGPRLQEL LQESNSNNND AAADSELPQD SRDSSPMTGE GRRLGDSSHN GSSSAFPVGH
GHRVGAGPGG SALGEGSQQS RGLLAGTESP PSLMLPTAAS SGGEYERPPG YDDAAAEADI
DEGVSMDYQW SRPTWDFARL ETSTQRAPAN SEEEGMFGDK GSSNDSTRVE GNHGSPAPSF
TDLEDNGSIH HDPNDNDLPL YSSEAGPVMH HEDFAHPRGA RESAPPPDEI ASGRGMSMPV
NMSVQDDNDD VDDPPVMELQ ADPANNNELR FNPAT
//
