ID A0A0L6V6Q9_9BASI Unreviewed; 1164 AA.
AC A0A0L6V6Q9;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=VP01_2415g1 {ECO:0000313|EMBL:KNZ56389.1};
OS Puccinia sorghi.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=27349 {ECO:0000313|EMBL:KNZ56389.1, ECO:0000313|Proteomes:UP000037035};
RN [1] {ECO:0000313|EMBL:KNZ56389.1, ECO:0000313|Proteomes:UP000037035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RO10H11247 {ECO:0000313|EMBL:KNZ56389.1,
RC ECO:0000313|Proteomes:UP000037035};
RA Rochi L., Burguener G., Darino M., Turjanski A., Kreff E., Dieguez M.J.,
RA Sacco F.;
RT "Next Generation Sequencing and Analysis of the Genome of Puccinia sorghi L
RT Schw, the Causal Agent of Maize Common Rust.";
RL Submitted (AUG-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}.
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:KNZ56389.1}.
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DR EMBL; LAVV01007298; KNZ56389.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L6V6Q9; -.
DR STRING; 27349.A0A0L6V6Q9; -.
DR VEuPathDB; FungiDB:VP01_2415g1; -.
DR OrthoDB; 51419at2759; -.
DR Proteomes; UP000037035; 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; 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 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, ECO:0000313|EMBL:KNZ56389.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000037035};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 48..206
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 232..586
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
SQ SEQUENCE 1164 AA; 133617 MW; C0B0F7597BC9EB64 CRC64;
MDPLEGPSNI IPDSMASPPL ELETVSVDDP EAFAAKHLSD LGIPVEDFKK HSWRIPNYRK
LPKRVTSDTF TAGGHEWNIL LFPQGNSNGQ ANDMVSIYLN YGDPKKQPEG WHVCAQFALA
ISNPHDGTCY IQSRKHVSHP NAASLVACRF SNMFRRHYSE AQHRFTNDEQ DWGFTRFVEL
RKLFSPADSR VKPIIENDET IITAYVRVLK DETGVLWHNF VNYDSKKETG YVGLKNQGAT
CYMNSLLQSL FLTNYFRKAV YQIPTEHDGP DSVPLALQRV FYQLQTSDQS VGTTELTKSF
GWKSLDAFLQ HDVQEFSRVL QDKLESKMKG TPADGAIQYL FAGKYKTYLK CINVDYESSR
EETFLDVQLD IKDLQGRPFK TLQESLEAYV TPETMDGDNK YHAGDDHGLQ DARKGTIFME
FPPVLHLHLK RFEYDFQRDM QVKVCVACSP FLTILSIHSS SNPYQLDTQI NDRHEFPFEL
DLAPYLDESA DKSANWNYRL HGVLVHSGDV HGGHYFVLIK PHPESKWYKF DDDRVTPVTD
REVSEDNFGG ELIINGAAVN GGGKGLGGKG GMKRFTNAYM LVYVRESAAA EILAPITQAD
TPTHLKSRLE REQREHDKKK REKEEMHLYL TTKIITDETF RAHQGFDLAL FDDRTMPPSD
LPTFRVAKQQ PFLDFKSKLA QDLGYQPNQI RLWVLVNRQN KTVRPDTVVP EHDPTLTMEV
VRDKMASKAQ DLKLYLEVLD PAHEAQPAES KEGQLMIFVK YFDVSDQTLA GIGHFYVHRT
QRVGEVIPLI NARMNFPENT PLKLYEVRAL LFSLMLRTGQ NYEIKPGMID PMKPKATFLQ
SEIQDGDIIC FQIELSDKEL SELEKQRLYL DPVAFYDFFT NRVLVQFKPR YDDMPTTIEF
DLLLSKKFTY DQMASRGNPK NVIRRAAAQG TVADMIQSSY NNAPSNVLFY ELLDMSIVEI
ETKRNVKVTW TGAYNREEGQ HSFLMPKTSS MHDVADKLST LVKFSETSTR KIKLFTIHDG
RIQKQFAGGE ILRDVTDVED IYAEEVHQDE LTHCDEKDGK IIDVYHFQKE LTRNHGIPFK
FLIKPGELFT ETKERLRLRL GLSEKEISKM KFSIAQFNTY TKPSYILDTD VIFDHKWMKG
DLLGIDHLDK SRKTTGIEKA VYIK
//