ID A0A167RZA9_CALVF Unreviewed; 1399 AA.
AC A0A167RZA9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=CALVIDRAFT_507975 {ECO:0000313|EMBL:KZP01433.1};
OS Calocera viscosa (strain TUFC12733).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1330018 {ECO:0000313|EMBL:KZP01433.1, ECO:0000313|Proteomes:UP000076738};
RN [1] {ECO:0000313|EMBL:KZP01433.1, ECO:0000313|Proteomes:UP000076738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TUFC12733 {ECO:0000313|EMBL:KZP01433.1,
RC ECO:0000313|Proteomes:UP000076738};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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; KV417266; KZP01433.1; -; Genomic_DNA.
DR STRING; 1330018.A0A167RZA9; -.
DR OrthoDB; 5474185at2759; -.
DR Proteomes; UP000076738; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
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:UP000076738}.
FT DOMAIN 98..206
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 454..1192
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 835..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1198..1237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1255..1287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1317..1399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 864..888
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1199..1214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1255..1271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1351..1372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1399 AA; 153364 MW; A8DE376678C00863 CRC64;
MAAQPVPSPL ESRKRLRSPS SSSVCSTPKR QASEDPSDSP NTPTPPSTAT PSTTLTIPLE
SQLSLQSPAS TSTSELPMQT PTESSSSMNQ PLSPEPADTL VPPHDRWSHI VGLRNASQIP
GATWHLVSSK WLKRLEIACT GKAGKDEELV TQETLGPVDN SDIVDADGEL RRDLEGDEYE
PLPQEAWDAL QRWYGPSSTP LSRTVYAGPS GSTMLHYHPH LFRLFLLTTS PPMAPSMGTT
TTTLPPSAPL LRLYEPQPLA DLYAAASSQL PVLSLPKPVP TPTPTFRLWR LDEAESADLI
KSPHYPLQRL LAKGARLLPP PSDMNTSALN PPLTIQGSLL SSGDCLMMEL LDETGKYPIT
NPQSVPGNSS AVPSPAPSNI ALPPAAPLFG SGASNAGQKD FFSRYESEAA KGAAAPLFSV
KGLSKSTNFG STSAAVTEVK GKEKEEKKGK RGTMGLANLG NTCFMNSALQ CLAHTEELAE
YFLTGVFRTE INRSNPLGMG GQIAEAFGAL MNRLWAPVAG SSSSFSSGSS YSPREFKSIL
AKFAPQFSGY MQHDSQELLA FLLDGLHEDL NRVLKKPYVE KPDWPGKGGP KELIAFAEEC
WDGYLKRNDS VIVDLFQGQY KSTLVCPECG KVSITFDPYM YLTLPLPVNR KWRGKVHFIP
WSLDKPRQRI TLELPKDADF KRLKQHVGAL TGADPAHLLA AEPYQHVFWK LWEDAAPVGD
INTASDDIAL YELPCSFSQL RAQGSDRSSP VRLADSSWIL VPIFLSTPRA RYSPDSRFGT
RRFGGGEKFP VFGQPFMLAL TRQEASNEDV IYERIAQRLS QVTSRKLELY DDDVLPVTPA
PPNTETLGPQ AEVEDATPPR EQPEEAEAST STFVPPPSQS KLTNGEPVEH QRSWTARKNM
FKMHILQHNR DLGEGHLVTG WSIETTNRVV DFADRKEEVS GTVRVLPGGF QEDIEEEEDA
AEGSSEDPYK PLLRLGEAIM CEWNAEAARY FFDDQSGTWD EFKDLTDPGI ATSDDAEKAA
GKKDISLYDC MSEFTREEQL GEDDLWYCPQ CKKHRQATKK FEIWSVPDIL VVHLKRFSSG
RLLRDKLDMM VDFPLEGLDL EGRVEEKLEW KRMREQEGTA GEKHGDPEEE PIVYDLFAVD
EHLGGLGGGH YRAYAKNYAD GQWYHFDDSH VSLAVPSAAV NRNAYLLFYR RRTARHLGGK
THEKIEEARK AGPPPVQEDA DQPVKSTNPF RDVAPTRSDY SVPLPLLSLL PPASGMISPA
SSESSDSGGG PAYSPPSPPA FDLSGNDPLL LSSNLDLEDS DAYNGQLIVR GAAPSPFSGS
ASAEMGDSGI ITPLDSEMDD VPASSDAWED DQPGENGRFA RAFDDDDELT KGYLPTPPDV
EMNGGELQKS QPGDKGTNE
//
