ID A0A2N5UF33_9BASI Unreviewed; 626 AA.
AC A0A2N5UF33;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=PCANC_16194 {ECO:0000313|EMBL:PLW36364.1};
OS Puccinia coronata f. sp. avenae.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=200324 {ECO:0000313|EMBL:PLW36364.1, ECO:0000313|Proteomes:UP000235388};
RN [1] {ECO:0000313|EMBL:PLW36364.1, ECO:0000313|Proteomes:UP000235388}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12NC29 {ECO:0000313|EMBL:PLW36364.1};
RA Miller M.E., Zhang Y., Omidvar V., Sperschneider J., Schwessinger B.,
RA Raley C., Palmer J.M., Garnica D., Upadhyaya N., Rathjen J., Taylor J.M.,
RA Park R.F., Dodds P.N., Hirsch C.D., Kianian S.F., Figueroa M.;
RT "De novo assembly and phasing of dikaryotic genomes from two isolates of
RT Puccinia coronata f. sp. avenae, the causal agent of oat crown rust.";
RL Submitted (NOV-2017) 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}.
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:PLW36364.1}.
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DR EMBL; PGCJ01000240; PLW36364.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N5UF33; -.
DR STRING; 200324.A0A2N5UF33; -.
DR Proteomes; UP000235388; 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 InterPro; IPR002083; MATH/TRAF_dom.
DR InterPro; IPR008974; TRAF-like.
DR InterPro; IPR024729; USP7_ICP0-binding_dom.
DR InterPro; IPR029346; USP_C.
DR Pfam; PF14533; USP7_C2; 1.
DR Pfam; PF12436; USP7_ICP0_bdg; 1.
DR SUPFAM; SSF49599; TRAF domain-like; 1.
DR PROSITE; PS50144; MATH; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000235388};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 1..77
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT REGION 586..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..603
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 626 AA; 72201 MW; 5A9051FA0C2EDC53 CRC64;
MNGTLSSTLK ATPYAFAISN PHDRTCYIQH HEQMYFTESV SGWGWPDFVE LRKLFSPADS
RVKPIIENDE TIVTAYVRVF DITEADTPAN LESQMEREQQ DHVNQKRKRE ETHLDFTTKI
ITDETFRAHQ GFDLALFDDR TIHPFDLPTF RVDKQQTFLD FKSKLAQDLG YQPNQIRLWV
LVTRGNKTIR PAVVVPEHDP TLTMEVVRDK MASKTQDLKF YLEVLDPAHE AQPVESKEGQ
LMILVKCFNV SHQTLVGVGH FYVHQNQPVG EVIPLINARM EFPENTPLML YEEIMPGMIN
EMRPEATFLQ SEIQDGDIIC FQIGLSDKQL AELKKQRLYL DPMAFYDFFT NRVLVQFKPL
HDDMATTIEF DLLLSNKLTY DQMASQVGER LQHDPMKLQF TSSHQGNPKD IIRRTAAQGT
LADMIQSSYK NAPNNVLFYE LLDMSIVEIE TKRNVKVTWT GAHNGEKAKH SFLMPKTSSM
HDVADKLSTL VKFSENSTRK IKLFTIHDGR IQKQFAGGEI LRDVADLEDI HAEEVSQDEL
THCHEKTGKT IDFLIEPGKA FAETKERMGL RLGLLEKRTG KMQFKKNQKM KKKAKKRKRT
KKTKEADSTK IHWTGRSENM KINGRM
//
