ID A0A0B2PMP4_GLYSO Unreviewed; 938 AA.
AC A0A0B2PMP4;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN ORFNames=D0Y65_051304 {ECO:0000313|EMBL:RZB47657.1}, glysoja_029490
GN {ECO:0000313|EMBL:KHN08913.1};
OS Glycine soja (Wild soybean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3848 {ECO:0000313|EMBL:KHN08913.1};
RN [1] {ECO:0000313|EMBL:KHN08913.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Root {ECO:0000313|EMBL:KHN08913.1};
RA Lam H.-M., Qi X., Li M.-W., Liu X., Xie M., Ni M., Xu X.;
RT "Identification of a novel salt tolerance gene in wild soybean by whole-
RT genome sequencing.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RZB47657.1, ECO:0000313|Proteomes:UP000289340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. W05 {ECO:0000313|Proteomes:UP000289340};
RC TISSUE=Hypocotyl of etiolated seedlings {ECO:0000313|EMBL:RZB47657.1};
RA Xie M., Chung C.Y.L., Li M.-W., Wong F.-L., Chan T.-F., Lam H.-M.;
RT "A high-quality reference genome of wild soybean provides a powerful tool
RT to mine soybean genomes.";
RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Recognizes and hydrolyzes the peptide bond at the C-terminal
CC Gly of ubiquitin. Involved in the processing of poly-ubiquitin
CC precursors as well as that of ubiquitinated proteins.
CC {ECO:0000256|ARBA:ARBA00037450, ECO:0000256|RuleBase:RU366025}.
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|RuleBase:RU366025};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085, ECO:0000256|RuleBase:RU366025}.
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DR EMBL; KN665560; KHN08913.1; -; Genomic_DNA.
DR EMBL; QZWG01000019; RZB47657.1; -; Genomic_DNA.
DR OrthoDB; 653068at2759; -.
DR Proteomes; UP000053555; Unassembled WGS sequence.
DR Proteomes; UP000289340; Chromosome 19.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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:SF18; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 5; 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 Hydrolase {ECO:0000256|RuleBase:RU366025, ECO:0000313|EMBL:KHN08913.1};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000289340};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 14..143
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 320..927
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 278..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 938 AA; 106079 MW; B32081AF16061758 CRC64;
MTEVPMCIAS VCELSPDEER ILIRDIALTA QANSKEGDTF FLITQRWWQH WIEYVNQEQT
NTSYDASSLS EHCDLANSSV LKRPAGIDNS DLIDDAVSED TGMGIEIHDT LLEGRDYVLL
PQEVWNQLFR WYGGGPTLAR KVISSGLSQT ELAVEVYPLR LQLLMLPKND RFPIRISKKE
TIGQLHRKAC EIFDLQPDQV CIWDYYARRK HALMNDMDKT LDDANLQMDQ DILVEVINNT
NNTSFAQENG SAQREMNSAL VEPSKSSLSI AGGLSASRGA SRGHNMDLSS SQNLNSPVRD
VENPYGTSGV TTRGSFGGLT GLLNLGNTCY MNSAIQCLVH TPEFARYFRE DYHREINWQN
PLGMVGELAL AFGELLRKLW APGRTPIAPR PFKAKLVRFA PQFSGHNQHD SQELLAFLLD
GLHEDLNRVK HKPYIKSRDA DGRPDEEVAD EYWANHIARN DSIIVDVCQG QYKSTLVCPV
CNKVSVTFDP FMYLSLPLQP TTNRTMTVTV FACDGAALPS ACTVTVPKQG RCRDLIQALS
NACSLKHNER LVLVEIRNHL IHRYFEDPLQ LLSNIKDDDR LSAYKVPKID KNTKYLQLIH
RRREQSSDSH IISGWKPYGT PIVSLISCDD TVTRGDIQVI VNRMLSPLLR KGINVEQATT
SETSISKATS DQCSFNSSDD ACAANMVSNS VNKDTTNSKA PPVPLPTLPL LLVDDNNACI
DLSMGEEKVV KLSPLSPKIL VYIDWSQKLL EKYDTHPLET LPEVLKYGPV TKKARTEPLS
LYTCLEAFLR EEPLVPEDMW YCPKCKERRQ ASKKLDLWRL PEVLVIHLKR FSYSRSMKHK
LETFVNFPIH DFDLTNYIAN KNNTRRQLYE LYALTNHYGS MGSGHYTAHI KLLDENRWYN
FDDSHISLIS EDEVNTAAAY VLFYRRVKND DAAVSNGA
//
