ID A0A072UH26_MEDTR Unreviewed; 488 AA.
AC A0A072UH26;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000313|EMBL:KEH28403.1};
GN Name=11437052 {ECO:0000313|EnsemblPlants:KEH28403};
GN OrderedLocusNames=MTR_5g091550 {ECO:0000313|EMBL:KEH28403.1};
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:KEH28403.1, ECO:0000313|Proteomes:UP000002051};
RN [1] {ECO:0000313|EMBL:KEH28403.1, ECO:0000313|Proteomes:UP000002051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A17 {ECO:0000313|EMBL:KEH28403.1}, and cv. Jemalong A17
RC {ECO:0000313|EnsemblPlants:KEH28403,
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:KEH28403.1, ECO:0000313|Proteomes:UP000002051}
RP GENOME REANNOTATION.
RC STRAIN=A17 {ECO:0000313|EMBL:KEH28403.1}, and cv. Jemalong A17
RC {ECO:0000313|EnsemblPlants:KEH28403,
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:KEH28403}
RP IDENTIFICATION.
RC STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:KEH28403};
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; CM001221; KEH28403.1; -; Genomic_DNA.
DR RefSeq; XP_013454372.1; XM_013598918.1.
DR AlphaFoldDB; A0A072UH26; -.
DR STRING; 3880.A0A072UH26; -.
DR PaxDb; 3880-AET00394; -.
DR EnsemblPlants; KEH28403; KEH28403; MTR_5g091550.
DR GeneID; 11437052; -.
DR Gramene; KEH28403; KEH28403; MTR_5g091550.
DR KEGG; mtr:11437052; -.
DR eggNOG; KOG1863; Eukaryota.
DR HOGENOM; CLU_043880_0_0_1; -.
DR OrthoDB; 51419at2759; -.
DR Proteomes; UP000002051; Chromosome 5.
DR ExpressionAtlas; A0A072UH26; differential.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00121; MATH; 1.
DR InterPro; IPR002083; MATH/TRAF_dom.
DR InterPro; IPR008974; TRAF-like.
DR InterPro; IPR024729; USP7_ICP0-binding_dom.
DR PANTHER; PTHR46236:SF35; TRAF-LIKE FAMILY PROTEIN-RELATED; 1.
DR PANTHER; PTHR46236; TRAF-LIKE SUPERFAMILY PROTEIN; 1.
DR Pfam; PF00917; MATH; 1.
DR Pfam; PF12436; USP7_ICP0_bdg; 1.
DR SMART; SM00061; MATH; 1.
DR SUPFAM; SSF49599; TRAF domain-like; 1.
DR PROSITE; PS50144; MATH; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KEH28403.1};
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 17..142
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT REGION 439..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..463
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 488 AA; 56827 MW; 87F3F8BA81464044 CRC64;
MGGSKYERRT SLTAPGIQSY TWRTERFSRV RATVLYSDVF EAGGYKWRAI IHPRGNNTDY
LSIYLCTADS ASLPDGWSSY VEFTLKVVNQ IEYKYSVTKV AKHKFTKLIS DWGHKNVIPL
GILFDPSRGY LVNDTLVVEI EVTYSEDEKD TAAHLRNGIM QERLKKDWEV KKLKNKEKED
AQLYTIIKVI RDEDLAEQIG KDIYFNLVDH GKVRSFCVQK QTSFNVFKEE VAKEFGIPAR
FQRFWLWAKR LNHTYRPFRP LTYIEEAAPV GQFRDVFGIH IAELELFLEV ERGPDLRPIA
PLKKRKDDIL LFFKLYDPER MELRYVGRLL VNCTDKPSQI LTKLNKLAGY DPDEEIELYE
EVFEPNVKCL PVDMKLTFQE SELENGDIIC FQKDSSMDIV KQIPFRDVCS YLEYVHKRYP
YVASSFEYVH NRQVPFCHPG IEFEDEDSSE EDSEDEDSSE EQNENITAEA SHYEGTSKAN
ASKPTKLS
//