ID I1JN11_SOYBN Unreviewed; 938 AA.
AC I1JN11;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN Name=100785944 {ECO:0000313|EnsemblPlants:KRH66691};
GN ORFNames=GLYMA_03G122400 {ECO:0000313|EMBL:KRH66691.1};
OS Glycine max (Soybean) (Glycine hispida).
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=3847 {ECO:0000313|EnsemblPlants:KRH66691};
RN [1] {ECO:0000313|EMBL:KRH66691.1, ECO:0000313|EnsemblPlants:KRH66691}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH66691};
RC TISSUE=Callus {ECO:0000313|EMBL:KRH66691.1};
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [2] {ECO:0000313|EnsemblPlants:KRH66691}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH66691};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [3] {ECO:0000313|EMBL:KRH66691.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRH66691.1};
RA Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA Jackson S.;
RT "WGS assembly of Glycine max.";
RL Submitted (JUL-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; CM000836; KRH66691.1; -; Genomic_DNA.
DR RefSeq; XP_003520476.1; XM_003520428.3.
DR AlphaFoldDB; I1JN11; -.
DR MEROPS; C19.093; -.
DR PaxDb; 3847-GLYMA03G27790-1; -.
DR EnsemblPlants; KRH66691; KRH66691; GLYMA_03G122400.
DR GeneID; 100785944; -.
DR Gramene; KRH66691; KRH66691; GLYMA_03G122400.
DR KEGG; gmx:100785944; -.
DR eggNOG; KOG1870; Eukaryota.
DR HOGENOM; CLU_001060_7_0_1; -.
DR OMA; WERVGHR; -.
DR OrthoDB; 653068at2759; -.
DR Proteomes; UP000008827; Chromosome 3.
DR ExpressionAtlas; I1JN11; baseline.
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};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000008827};
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 282..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 938 AA; 106171 MW; 217320A0D6C94411 CRC64;
MTEVLMCIAS VSELSPDEER ILIRDIALAS QANSKEGDTF FLITQRWWQH WIEYVNQDQT
NTSYDASSLS EQFDLANSSA LKRPAGIDNS DLIDDAVLED SGTGIEIHDT LLEGRDYVLL
PQEVWNQLFR WYGGGPTLAR KVISSGLSQT ELAVEVYPLR LQLLMLPKND RFPIRISKKE
TIGQLHRKAC EIFDLQPDQV CIWDYYARRR HALMNDMDKT LDDANLQMDQ DILVEVINNT
NNTSFAQENG SAQREANSAL VEPSKSSLSI AGGLSASRGA SKGYNTDLSS SQNLNSPVRD
VENPYGTSGV TTRSSFLGLT GLLNLGNTCY MNSAIQCLVH TPEFARYFRE DYHREINWQN
PLGMVGELAL AFGELLRKLW APGRTPIAPR PFKAKLVRFA PQFSGHNQHD SQELLAFLLD
GLHEDLNRVK HKPYIKSRDA DGRPDEEVAD EYWANHIARN DSIIVDVCQG QYKSTLVCPV
CNKVSVTFDP FMYLSLPLQP TTNRTMTVTV FACDGASLPF SCTVTVPKQG RCRDLIQALS
NACSLKHNER LVLVEIRNHL IHRYFEDPLQ LLSNIKDDDR LAAYKVPKID KNTKYLQLIH
RQREQSSDSH IISGWKPYGT PIVSLISCDD TVTRGDIQVI VNCMLSPLLR KGINVEQATT
SETSIPKATS DHCSFNSDDD ACAPNMMSNS VNKDTTNSKA PPMPLPTLPL LLVDDNNACI
DLSMGEEKVV KLSPLSPKIL VYIDWSQKLL EKYDTHTLET LPEVLKYGPV TKKARTEPLS
LYTCLEAFLR EEPLVPEDMW YCPKCKERRQ ASKKLDLWRL PEVLVIHLKR FSYSRSMKHK
LETFVNFPIH DFDLTNYIAN KNNSRRQLYE LYALTNHYGS MGSGHYTAHI KLLDENRWYN
FDDSHISLIS EDEVNTAAAY VLFYRRVKTD DAAVSNGA
//
