ID A0A0R0L2F3_SOYBN Unreviewed; 1117 AA.
AC A0A0R0L2F3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 40.
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:KRH73402};
GN ORFNames=GLYMA_02G271500 {ECO:0000313|EMBL:KRH73402.1};
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:KRH73402.1};
RN [1] {ECO:0000313|EMBL:KRH73402.1, ECO:0000313|EnsemblPlants:KRH73402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH73402};
RC TISSUE=Callus {ECO:0000313|EMBL:KRH73402.1};
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:KRH73402}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH73402};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [3] {ECO:0000313|EMBL:KRH73402.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRH73402.1};
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}.
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DR EMBL; CM000835; KRH73402.1; -; Genomic_DNA.
DR RefSeq; XP_006575589.1; XM_006575526.2.
DR AlphaFoldDB; A0A0R0L2F3; -.
DR EnsemblPlants; KRH73402; KRH73402; GLYMA_02G271500.
DR GeneID; 100778442; -.
DR Gramene; KRH73402; KRH73402; GLYMA_02G271500.
DR OMA; HTAHHRF; -.
DR OrthoDB; 51419at2759; -.
DR Proteomes; UP000008827; Chromosome 2.
DR ExpressionAtlas; A0A0R0L2F3; baseline and differential.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 54..179
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 199..523
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT COILED 532..563
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1117 AA; 131031 MW; 8F420FA3710785C2 CRC64;
MTVMTPAPID QQEDEEMLVP HTDLAENNHQ PMEVVAQPDA ANTVESQPVE DPSTSRFTWK
IENFSRMNTK KLYSEIFVVG GYKWRVLIFP KGNNVDYLSM YLDVADSASL PYGWSRYAQF
SLAVVNQIHN KYSVRKDTQH QFNARESDWG FTSFMPLGEL YDPSRGYLVN DTLVVEAEVL
VRRIVDYWTY DSKKETGYVG LKNQGATCYM NSLLQTLYHI PYFRKAVYHM PTTENDMPSG
SIPLALQSLF YKLQYSDTSV ATKELTKSFG WDTYDSFMQH DVQELNRVLC EKLEDKMKGT
VVEGTIQKLF EGHHMNYIEC INVDYKSTRK ESFYDLQLDV KGCPDVYASF DKYVEVERLE
GDNKYHAEQY GLQDAKKGVL FIDFPPVLQL QLKRFEYDFM RDTMVKINDR YEFPLQLDLD
RENGKYLSPD ADRNVRNLYT LHSVLVHSGG VHGGHYYAFI RPTLSEQWYK FDDERVTKED
TKRALEEQYG GEEELPQTNP GFNNTPFKFT KYSNAYMLVY IREADKDKVI CNVDEKDIAE
HLRERLKKEQ EEKEHKKKEK AEAHLYTIIK VARDEDLAEQ IGKDIYFDLV DHDKVRSFRV
QKQTSFNLFK DEVAKEFGIP VQFQRFWLWA KRQNHTYRPN RPLTHMEEAQ SVGQLREVSN
KVHNAELKLF LEVELGLDLR PIAPPDKTKD DILLFFKLYD TEKEELRYVG RLFVKATGKP
SEILTRLNKM AGYDPDEEIG LYEEIKFEPN VMCEPIDKKV TFRASQLEDG DIICFQKAPA
IDNEHVRYPD VPSYLEYVHN RQVVHFRSLE KPKEDDFCLE MSRLYTYDDV VEKVAQQLGL
DDPSIIRLTP HNCYSQQPKP QPIKYRGVEH LSDMLVHYNQ TSDILYYEVL DIPLPELQGL
KTLKVAFHHA TKDEVVIHTI RLPKQSTVGD VLNDLKTKVE LSDPEAELRL LEVFYHKIYK
VFPPNEKIES INDQYWTLRA EEIPEEEKNL GPHDRLIHVY HFTKDTAQNQ MQIQNFGEPF
FLVIHEGETL AEIKVRIQKK LQVPDDEFVK WKFAFFSLGR PEYLQDSDIV SSRFQRRDVY
GAWEQYLGLE HTDNAPKRSY AVNQNRHTFE KPVKIYN
//
