ID A0A0D2RMH7_GOSRA Unreviewed; 917 AA.
AC A0A0D2RMH7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN ORFNames=B456_008G259900 {ECO:0000313|EMBL:KJB52398.1};
OS Gossypium raimondii (New World cotton).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB52398.1, ECO:0000313|Proteomes:UP000032304};
RN [1] {ECO:0000313|EMBL:KJB52398.1, ECO:0000313|Proteomes:UP000032304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23257886; DOI=10.1038/nature11798;
RA Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D.,
RA Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R.,
RA Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., Grover C.,
RA Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., Marler B.S., Page J.T.,
RA Roberts A.W., Romanel E., Sanders W.S., Szadkowski E., Tan X., Tang H.,
RA Xu C., Wang J., Wang Z., Zhang D., Zhang L., Ashrafi H., Bedon F.,
RA Bowers J.E., Brubaker C.L., Chee P.W., Das S., Gingle A.R., Haigler C.H.,
RA Harker D., Hoffmann L.V., Hovav R., Jones D.C., Lemke C., Mansoor S.,
RA ur Rahman M., Rainville L.N., Rambani A., Reddy U.K., Rong J.K.,
RA Saranga Y., Scheffler B.E., Scheffler J.A., Stelly D.M., Triplett B.A.,
RA Van Deynze A., Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J.,
RA Zaki E.A., Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S.,
RA Wang X., Schmutz J.;
RT "Repeated polyploidization of Gossypium genomes and the evolution of
RT spinnable cotton fibres.";
RL Nature 492:423-427(2012).
CC -!- FUNCTION: Recognizes and hydrolyzes the peptide bond at the C-terminal
CC Gly of ubiquitin. Involved in the processing of poly-ubiquitin
CC precursors as well as that of ubiquitinated proteins.
CC {ECO:0000256|ARBA:ARBA00037450, ECO:0000256|RuleBase:RU366025}.
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|RuleBase:RU366025};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085, ECO:0000256|RuleBase:RU366025}.
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DR EMBL; CM001747; KJB52398.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D2RMH7; -.
DR EnsemblPlants; KJB52398; KJB52398; B456_008G259900.
DR Gramene; KJB52398; KJB52398; B456_008G259900.
DR Proteomes; UP000032304; Chromosome 8.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02674; Peptidase_C19R; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR Gene3D; 3.30.2230.10; DUSP-like; 1.
DR InterPro; IPR035927; DUSP-like_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR006615; Pept_C19_DUSP.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF46; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 10-RELATED; 1.
DR Pfam; PF06337; DUSP; 1.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM00695; DUSP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF143791; DUSP-like; 1.
DR PROSITE; PS51283; DUSP; 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|RuleBase:RU366025};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000032304};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 10..141
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 315..899
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 80..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 917 AA; 102972 MW; 09417E2D6349424D CRC64;
MENGASCLPC TPEEEKKIVT DLRNESERNL KEGNLYFVIS SSWFRKWERY VGIDGDENLI
GNQSSDSRHI NGASSVVAER PGPIDNSDIV ENGSDSDGKG NDIQLRRMLI EGQDYVLVPQ
GVWEKLHGWY KGGPELPRKM ILQGVYHKKF DVEVYPLCLK LVDSRDESQS TIWLSRKASL
TELFQKVCAL KGIEQDKVRI WDYFNKRKYA QLYVSNKTLE ESNLQMDQDI LLELVDGHQS
SKIGMDSTGN DLALVSLEPS RSPLTIAGGP TLSNGHSGYR SNLYPGSSLG SGLTDMDDGF
DACNSARKGE KGGLAGLQNL GNTCFMNSAL QCLVHTPPLV EYFLKDCRAE INTDNPLGMH
GELALAFGDL LRKLWSSGRT AIAPRVFKGK LARFAPQFSG YNQHDSQELL AFLLDGLHED
LNRVKQKPYI EMKDSDGRPD EEVAAECWKN HKARNDSVIV DVCQGQYKST LVCPVCSKIS
ITFDPFMYLS LPLPSTITRT MTVTVFYGDG SRLPMPFTVS VLKNGFCKDL LLALGTACGL
KSDESLMLAE VYENKIYRYL EMPLEPLSSI KDDEHIVAFR FQKKEIGKTR LVIFHRWQEK
AELFGTPLVT YLVADQSSGA DIEAAVSKVL SPFKKISSAK AHVGKENGIL LDGLDEECSC
SDAQSVENAE LEGTSCTDLS IPLRLTDDRV MNFNAFKKDT LFESGKIIGK LLRVVLDWTD
KEQELYDSSY LKDIPEVYKA GLAAKKTQQE AISLSSCLDA FLIEEPLGPD DMWYCPRCKE
HRQAIKKLDL WMLPEIIVFH LKRFTYGRYL KNKIDTFVNF PIHDLDLSKY VMSKDGQSYL
YELYAISNHY GGLGGGHYTA YAKLIDENRW YHFDDSHVSA VNESDIKTSA AYLLFYKRVR
SESKVEAGEA SHSHSIS
//
