ID I1JIM7_SOYBN Unreviewed; 1118 AA.
AC I1JIM7;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN Name=100778442 {ECO:0000313|EnsemblPlants:KRH73403};
GN ORFNames=GLYMA_02G271500 {ECO:0000313|EMBL:KRH73403.1};
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|EMBL:KRH73403.1};
RN [1] {ECO:0000313|EMBL:KRH73403.1, ECO:0000313|EnsemblPlants:KRH73403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH73403};
RC TISSUE=Callus {ECO:0000313|EMBL:KRH73403.1};
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:KRH73403}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH73403};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [3] {ECO:0000313|EMBL:KRH73403.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRH73403.1};
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 -!- 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM000835; KRH73403.1; -; Genomic_DNA.
DR RefSeq; XP_003519464.1; XM_003519416.3.
DR AlphaFoldDB; I1JIM7; -.
DR SMR; I1JIM7; -.
DR STRING; 3847.I1JIM7; -.
DR MEROPS; C19.A53; -.
DR PaxDb; 3847-GLYMA02G43930-1; -.
DR EnsemblPlants; KRH73403; KRH73403; GLYMA_02G271500.
DR GeneID; 100778442; -.
DR Gramene; KRH73403; KRH73403; GLYMA_02G271500.
DR KEGG; gmx:100778442; -.
DR eggNOG; KOG1863; Eukaryota.
DR HOGENOM; CLU_003532_0_1_1; -.
DR InParanoid; I1JIM7; -.
DR OrthoDB; 51419at2759; -.
DR Proteomes; UP000008827; Chromosome 2.
DR ExpressionAtlas; I1JIM7; baseline and differential.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0031647; P:regulation of protein stability; IBA:GO_Central.
DR CDD; cd00121; MATH; 1.
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:SF929; UBIQUITINYL HYDROLASE 1; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000008827};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 55..180
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 200..524
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT COILED 533..564
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1118 AA; 131159 MW; 6EA5ED6B13ABE326 CRC64;
MTVMTPAPID QQQEDEEMLV PHTDLAENNH QPMEVVAQPD AANTVESQPV EDPSTSRFTW
KIENFSRMNT KKLYSEIFVV GGYKWRVLIF PKGNNVDYLS MYLDVADSAS LPYGWSRYAQ
FSLAVVNQIH NKYSVRKDTQ HQFNARESDW GFTSFMPLGE LYDPSRGYLV NDTLVVEAEV
LVRRIVDYWT YDSKKETGYV GLKNQGATCY MNSLLQTLYH IPYFRKAVYH MPTTENDMPS
GSIPLALQSL FYKLQYSDTS VATKELTKSF GWDTYDSFMQ HDVQELNRVL CEKLEDKMKG
TVVEGTIQKL FEGHHMNYIE CINVDYKSTR KESFYDLQLD VKGCPDVYAS FDKYVEVERL
EGDNKYHAEQ YGLQDAKKGV LFIDFPPVLQ LQLKRFEYDF MRDTMVKIND RYEFPLQLDL
DRENGKYLSP DADRNVRNLY TLHSVLVHSG GVHGGHYYAF IRPTLSEQWY KFDDERVTKE
DTKRALEEQY GGEEELPQTN PGFNNTPFKF TKYSNAYMLV YIREADKDKV ICNVDEKDIA
EHLRERLKKE QEEKEHKKKE KAEAHLYTII KVARDEDLAE QIGKDIYFDL VDHDKVRSFR
VQKQTSFNLF KDEVAKEFGI PVQFQRFWLW AKRQNHTYRP NRPLTHMEEA QSVGQLREVS
NKVHNAELKL FLEVELGLDL RPIAPPDKTK DDILLFFKLY DTEKEELRYV GRLFVKATGK
PSEILTRLNK MAGYDPDEEI GLYEEIKFEP NVMCEPIDKK VTFRASQLED GDIICFQKAP
AIDNEHVRYP DVPSYLEYVH NRQVVHFRSL EKPKEDDFCL EMSRLYTYDD VVEKVAQQLG
LDDPSIIRLT PHNCYSQQPK PQPIKYRGVE HLSDMLVHYN QTSDILYYEV LDIPLPELQG
LKTLKVAFHH ATKDEVVIHT IRLPKQSTVG DVLNDLKTKV ELSDPEAELR LLEVFYHKIY
KVFPPNEKIE SINDQYWTLR AEEIPEEEKN LGPHDRLIHV YHFTKDTAQN QMQIQNFGEP
FFLVIHEGET LAEIKVRIQK KLQVPDDEFV KWKFAFFSLG RPEYLQDSDI VSSRFQRRDV
YGAWEQYLGL EHTDNAPKRS YAVNQNRHTF EKPVKIYN
//
