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Database: UniProt
Entry: A0A072UH26_MEDTR
LinkDB: A0A072UH26_MEDTR
Original site: A0A072UH26_MEDTR 
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
//
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