ID A0A0D2UWQ3_GOSRA Unreviewed; 1097 AA.
AC A0A0D2UWQ3;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=B456_011G226800 {ECO:0000313|EMBL:KJB73309.1};
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:KJB73309.1, ECO:0000313|Proteomes:UP000032304};
RN [1] {ECO:0000313|EMBL:KJB73309.1, 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 -!- 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; CM001750; KJB73309.1; -; Genomic_DNA.
DR RefSeq; XP_012454523.1; XM_012599069.1.
DR AlphaFoldDB; A0A0D2UWQ3; -.
DR EnsemblPlants; KJB73309; KJB73309; B456_011G226800.
DR Gramene; KJB73309; KJB73309; B456_011G226800.
DR OMA; ISCYEIT; -.
DR OrthoDB; 51419at2759; -.
DR Proteomes; UP000032304; Chromosome 11.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000032304};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 35..160
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 180..504
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT COILED 517..545
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1097 AA; 128660 MW; 69F8681F4F66E586 CRC64;
MLVPHNDFVD GPQPLEVAKE AASKVDAQAV DDPPSGRFTW TIENFSRLNT KKLYSDIFFV
GGYKWRILIF PKGNNVDHLS MYLDVADSAT LPYGWSRYAQ FSLAVCNQIH NKYTIRKDTQ
HQFNVRESDW GFTSFMPLGE LYDPSRGFLV NDTCVVEADV AVRKVADYWS HDSKKETGYV
GLKNQGATCY MNSLLQTLYH IPYFRKAVYH MPTTENDMPT GSIPLALQSL FYKLQYSDTS
VATKELTKSF GWDTYDSFMQ HDVQELNRVL CEKLEDKMKG TVVEGTIQQL FEGHHMNYIE
CINVDYKSTR KESFYDLQLD VKGCKDVYAS FDKYVEVECL EGDNRYHAEQ FGLQDARKGV
LFIDFPPVLQ LQLKRFEYDF MRDTMVKIND RYEFPLQLDL DREDGKYLSP EADRSVRNLY
TLHSVLVHSG GVHGGHYYAY IRPTLSDQWF KFDDERVTKE DVKRALEEQY GGEEELPQTN
PGFNNTPFKF TKYSNAYMLV YIRESDKDKI ICNVDEKDIA EHLRIRLKKE QEEKEQKRKE
KAEAHLYTVI KVARNEDLVE QIGRDIYFDL VDHEKVRSFR IQKQMPFNVF KEEVAKEFGI
PVQYQRFWLW AKRQNHTYRP NRPLTYQEEA QSVGQLREVS NKANNAELKL FLEVELGPDL
QPVPPPEKTK EDILLFFKLY DPVKEELRYI GRMFVKGAGK PMEILARINK MAGFGPDEEI
ELYEEIKFEP NVMCEHIDKK LTFRTSQLED GDIICLQKYS EVASEQCRYP DVPSFLEYVH
NRQVVRFRSL EKPKEDEFSL ELSKLHNYDD VVERVAHHLG LDDPSKIRLT SHNCYSQQPK
PQPIKYRGVE HLSDMLIHYN QTSDILYYEV LDIPLPELQG LKTLKVAFHH ATKDEVVIHT
IRLPKQSTVG DVLDDLKTKV ELSHPGAELR LLEVFYHKIY KIFPLSEKIE NINDQYWTLR
AEEIPEEEKD LGPHDRLIHV YHFMKDTTQN QQVQNFGEPF FLVIHETETL AEVKVRVQKR
LQVPDEEFAK WKFAFLSLGR PEYLQDSDVV STRFQRRDVY GAWDQYLGLE HSDNAPKRSY
AANQNRHTFE KPVKIYN
//
