ID A0A2D3V7A9_9PEZI Unreviewed; 1095 AA.
AC A0A2D3V7A9;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=RCC_11044 {ECO:0000313|EMBL:CZT25316.1};
OS Ramularia collo-cygni.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Ramularia.
OX NCBI_TaxID=112498 {ECO:0000313|EMBL:CZT25316.1, ECO:0000313|Proteomes:UP000225277};
RN [1] {ECO:0000313|EMBL:CZT25316.1, ECO:0000313|Proteomes:UP000225277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=URUG2 {ECO:0000313|EMBL:CZT25316.1,
RC ECO:0000313|Proteomes:UP000225277};
RA Ploux O.;
RL Submitted (MAR-2016) 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};
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DR EMBL; FJUY01000026; CZT25316.1; -; Genomic_DNA.
DR STRING; 112498.A0A2D3V7A9; -.
DR OrthoDB; 227085at2759; -.
DR Proteomes; UP000225277; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR GO; GO:0019538; P:protein metabolic process; IEA:UniProt.
DR CDD; cd02674; Peptidase_C19R; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 1.20.58.80; Phosphotransferase system, lactose/cellobiose-type IIA subunit; 1.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF23; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE USP2; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:CZT25316.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000225277}.
FT DOMAIN 718..1085
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..223
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..587
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..617
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..655
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..671
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..700
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1095 AA; 121163 MW; BD422E8F99166ED5 CRC64;
MSAAGPLPAF PSAPTGSPRG PASHGDSGGS VGINGGGGGG GGNGGERAFA HIDDIKADAL
SDVSPQQSIS NLIQHAERSL QQARGHIXFR RPDHAFMNYL RACEIVVEII PNHKDYIHFF
HDQYGGLRTR LLQQKVAGMS DQFANIKQII VNNNSRSGVQ PRASQQHASS PSHTRTGSES
VLMPSTRKVK PSISPKPDSM HARAISSVST PMNGASSSPS AEALSDRFAK LRGFGQTDSA
RPGSGASTSS VQGMPLSGPN GDDGGGSANF SRPLGPRGMP ENGTGLSRPS KLPLDIDWAI
SMPKPPSPTY SPARNMQTTG NIAAPRHSAR SLAGSNSRKS SLGPRSSASS TAPNGGSDYF
SAPVSNNTAM TTPLATPLGR RKSVHMPLET RIGAERLYDY LDRYSILLID FRPRDDFDQG
HIYHRSVICI EPLAMRPGMS AEEVSEGLVL SPEEEQDMFY NRDKYDVVVY FDADTQSDAY
LSRPSTESEM KLKCLHEALY DYNQDKPLQR PPIMLIGGMA AWVDLLGNQA LIASDTKARS
KQGRPLTRHP PQRDGAMRVT KRRLRDYNPL DPEEAKSWRD RAKSESVREA PPTAFTAGAG
KDEEQDDVED HFPSIEDFNA RFAEAATIGN EPYASSNGSG NRPTQESSSN IPQYPSRPTP
SVPPQVPARP APAAPRMGYA GVSDRAVSQN TPPPRTSSNL VPYISPRYLT ENLRIPKTGL
KNFGSTCYMN AXLQALSATT PLTVLFLNDG FKKLVQDNWK XSRGVLPEVY SNVIRELWKD
NVDFIKPSTF FNFCGRLNNM FRDPSQQQDT QEFFSFVVDC LHEDLNEHWK GSPLRHLTEK
EEAERERRPR QFVAKTEWDR YTHRENSFIT SLFYGQQSSR MRCRHCNVTN TTYDPWSTXQ
LEIPDAKEAQ LQSCLRHHFK DESLDENSMW RCPKCKVPRL ANKKFTITRA PHCLVIAFKR
FNTSDGRKLH TAVRFPLEGL DMGEFVLPAP SVEEEKSIRA TYGNTALDGL DPGMRGPFIY
DAYAVVRHQG STTRSGHYTS AVKDRARGVW RFFNDTQSSD FHPERLSSSQ ALDNDQAYLL
FYQRREVGKV GDGRL
//
