ID A0A072VGZ9_MEDTR Unreviewed; 1117 AA.
AC A0A072VGZ9;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN Name=11418867 {ECO:0000313|EnsemblPlants:KEH41314};
GN OrderedLocusNames=MTR_1g041240 {ECO:0000313|EMBL:KEH41314.1};
OS Medicago truncatula (Barrel medic) (Medicago tribuloides).
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; Hologalegina; IRL clade; Trifolieae; Medicago.
OX NCBI_TaxID=3880 {ECO:0000313|EMBL:KEH41314.1, ECO:0000313|Proteomes:UP000002051};
RN [1] {ECO:0000313|EMBL:KEH41314.1, ECO:0000313|Proteomes:UP000002051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A17 {ECO:0000313|EMBL:KEH41314.1}, and cv. Jemalong A17
RC {ECO:0000313|EnsemblPlants:KEH41314,
RC ECO:0000313|Proteomes:UP000002051};
RX PubMed=22089132; DOI=10.1038/nature10625;
RA Young N.D., Debelle F., Oldroyd G.E., Geurts R., Cannon S.B., Udvardi M.K.,
RA Benedito V.A., Mayer K.F., Gouzy J., Schoof H., Van de Peer Y., Proost S.,
RA Cook D.R., Meyers B.C., Spannagl M., Cheung F., De Mita S.,
RA Krishnakumar V., Gundlach H., Zhou S., Mudge J., Bharti A.K., Murray J.D.,
RA Naoumkina M.A., Rosen B., Silverstein K.A., Tang H., Rombauts S.,
RA Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M., Bellec A., Berger A.,
RA Berges H., Bidwell S., Bisseling T., Choisne N., Couloux A., Denny R.,
RA Deshpande S., Dai X., Doyle J.J., Dudez A.M., Farmer A.D., Fouteau S.,
RA Franken C., Gibelin C., Gish J., Goldstein S., Gonzalez A.J., Green P.J.,
RA Hallab A., Hartog M., Hua A., Humphray S.J., Jeong D.H., Jing Y.,
RA Jocker A., Kenton S.M., Kim D.J., Klee K., Lai H., Lang C., Lin S.,
RA Macmil S.L., Magdelenat G., Matthews L., McCorrison J., Monaghan E.L.,
RA Mun J.H., Najar F.Z., Nicholson C., Noirot C., O'Bleness M., Paule C.R.,
RA Poulain J., Prion F., Qin B., Qu C., Retzel E.F., Riddle C., Sallet E.,
RA Samain S., Samson N., Sanders I., Saurat O., Scarpelli C., Schiex T.,
RA Segurens B., Severin A.J., Sherrier D.J., Shi R., Sims S., Singer S.R.,
RA Sinharoy S., Sterck L., Viollet A., Wang B.B., Wang K., Wang M., Wang X.,
RA Warfsmann J., Weissenbach J., White D.D., White J.D., Wiley G.B.,
RA Wincker P., Xing Y., Yang L., Yao Z., Ying F., Zhai J., Zhou L., Zuber A.,
RA Denarie J., Dixon R.A., May G.D., Schwartz D.C., Rogers J., Quetier F.,
RA Town C.D., Roe B.A.;
RT "The Medicago genome provides insight into the evolution of rhizobial
RT symbioses.";
RL Nature 480:520-524(2011).
RN [2] {ECO:0000313|EMBL:KEH41314.1, ECO:0000313|Proteomes:UP000002051}
RP GENOME REANNOTATION.
RC STRAIN=A17 {ECO:0000313|EMBL:KEH41314.1}, and cv. Jemalong A17
RC {ECO:0000313|EnsemblPlants:KEH41314,
RC ECO:0000313|Proteomes:UP000002051};
RX PubMed=24767513; DOI=10.1186/1471-2164-15-312;
RA Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S.,
RA Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F.,
RA Schwartz D.C., Town C.D.;
RT "An improved genome release (version Mt4.0) for the model legume Medicago
RT truncatula.";
RL BMC Genomics 15:312-312(2014).
RN [3] {ECO:0000313|EnsemblPlants:KEH41314}
RP IDENTIFICATION.
RC STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:KEH41314};
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
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; CM001217; KEH41314.1; -; Genomic_DNA.
DR RefSeq; XP_013467206.1; XM_013611752.1.
DR AlphaFoldDB; A0A072VGZ9; -.
DR EnsemblPlants; KEH41314; KEH41314; MTR_1g041240.
DR Gramene; KEH41314; KEH41314; MTR_1g041240.
DR HOGENOM; CLU_003532_0_1_1; -.
DR Proteomes; UP000002051; Chromosome 1.
DR ExpressionAtlas; A0A072VGZ9; 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: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:KEH41314.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000002051};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 55..179
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 199..523
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
SQ SEQUENCE 1117 AA; 130824 MW; 5CDC13E6E2D3E030 CRC64;
MTITTTPPLE NLEEDTEMLV PNSDAVVVEG PQPMEVVQAE NTSTVDAVAV EDPPIGRFTW
TIDNFSRLPK KHYSDVFTVG GYKWRILIFP KGNNAEHLSM YIDVADAGSM PYGWTRFAQF
SLTVVNQVHS KYSVRKETQH QFNARESDWG FTNFMPLAEL YDPSRGYVVE DRCILEADVN
VRKDLDYWAH DSKKETGCVG LKNQGATCYM NSLLQTLYHI PYFRKAVYHM PTTENDMPSG
SIPLALQSLF YKLQYNDSSV STKELTKSFG WDTYDSFMQH DVQELNRVLC EKLEDKMKGT
VVEGTIQKLF EGHHMNYIEC MNVDYKSTRK ESFYDLQLDV KGCTDVYASF DKYVEVEQLE
GDNKYHAEQY GLQEARKGVL FIDFPPVLQL QLKRFEYDFA RDTMVKINDR YEFPLQLDLD
RDDGKYLSPD ADRSIRNLYT LHSVLVHSGG VHGGHYYAYI RPTLSNQWFK FDDERVTKED
TNRALEEQYG GEEELPLTNP GFNNSPFKFT KYSNAYMLVY VRESDKDKII CNVDEKDIAR
HLQIRLKKEQ EEKEKKKKEK AEAHLYTIVK IARDDDLHEQ IGKDIFFDLV DHDKVRSFRI
QKQMPFTIFK EEVAKEFGIP VEYQRFWMWA KRQNHTFRPS RPVTAQEEAQ AVGQLREVSN
KANNGELKLF LEIEMGQDLR PIPPPEKLKE ELLLFFKLYE PSSQKLRYVG RLFVVGSRKP
VDILKKLNEM AGFDPDEEID LFEEIKFDPK IMCEHVDQKS TFRDNQLEDG DIICFQKSPP
AGDGQQQYCY PDVPSFFEYV QNRQVVRFRF LEKPKEDEFS LELSKLHTYD DVVERVSQHL
GLNDPSKIRL TSHNCYSQQP KPQPIKYRGV DHLSEMLVHY NQASDILYYE VLDIPLPELQ
NLKTLKIAFH HDAKDEVMII RLQKHSTVAD VINDLKSKVD LSHPDAELRL VEVFNHKIYK
IFHVNEKIEN INDHYWTLRA EEIPEEEKSL GPHDRMIHVY HFLKDTAQNQ MHVQNFGDPF
FLVIREGETL ADVKLRVQKK LQVPNEEFLK WKFAFVSLGR PEYLQDSDII SSRFQRRDIY
GAWEQYLGLE HTDNSPKRSY TANQNRHAFD KPIKIYN
//
