ID A0A2H5QHS5_CITUN Unreviewed; 1121 AA.
AC A0A2H5QHS5;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=CUMW_231490 {ECO:0000313|EMBL:GAY64162.1};
OS Citrus unshiu (Satsuma mandarin) (Citrus nobilis var. unshiu).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX NCBI_TaxID=55188 {ECO:0000313|EMBL:GAY64162.1, ECO:0000313|Proteomes:UP000236630};
RN [1] {ECO:0000313|EMBL:GAY64162.1, ECO:0000313|Proteomes:UP000236630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Miyagawa wase {ECO:0000313|Proteomes:UP000236630};
RX PubMed=29259619; DOI=10.3389/fgene.2017.00180;
RA Shimizu T., Tanizawa Y., Mochizuki T., Nagasaki H., Yoshioka T., Toyoda A.,
RA Fujiyama A., Kaminuma E., Nakamura Y.;
RT "Draft sequencing of the heterozygous diploid genome of Satsuma (Citrus
RT unshiu Marc.) using a hybrid assembly approach.";
RL Front. Genet. 8:180-180(2017).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAY64162.1}.
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DR EMBL; BDQV01000397; GAY64162.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H5QHS5; -.
DR Proteomes; UP000236630; Unassembled WGS sequence.
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:UP000236630};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 98..223
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 243..567
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT COILED 576..607
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1121 AA; 131567 MW; 8923512D97F33C35 CRC64;
MTFLPLHPHL LCNLYNSFFL IPLFNSLIIL PFTTKRRVVH SPHTMTIMTP APIDQQEDEE
MLVPHSDLAD NHQPMEVVAQ PETANAVENN QPLDDPPSSR FTWRIENFSR LNTKKHYSEI
FIVGGFKWRV LIFPKGNNVD HLSMYLDVAD SSSLPYGWSR YAQFSLAVIN QIHSKYSVRK
DTQHQFNARE SDWGFTSFMP LGELYDPNRG YLVNDTLIVE AEVIVRRVVD YWSYDSKKET
GYVGLKNQGA TCYMNSLLQT LFHIPYFRKA VYHMPTTEND MPSGSIPLAL QSLFYKLQYS
DSSVATKELT KSFGWDTYDS FMQHDVQELN RVLSEKLEDK MKGTVVEGTI QQLFEGHHMN
YIECINVDYK STRKESFYDL QLDVKGCRDV YASFDKYVEV ERLEGDNKYH AEQYGLQDAK
KGVLFIDFPP VLQLQLKRFE YDFMRDTMVK INDRYEFPLQ LDLDRENGKY LSPDADRSVR
NLYTLHSVLV HSGGVHGGHY YAFIRPTLSD QWYKFDDERV TKEDLKRALE EQYGGEEELP
QTNPGFNNTP FKFTKYSNAY MLVYIRESDK DKIICNVDEQ DIAEHLRERL KKEQEEKEHK
KKEKAEAHLY TVIKVARDDD LLEQIGKDIY FDLVDHDKVR SFRIQKQIPF NLFKVGQLRE
VSNKVHNAEL KLFLEVERGP DLRPIAPPEK TKEDILLFFK LYDPEKEELR YVGRLFVKST
GKPMEYLPKL NEMAGYAPDE EIDLYEEIKF EPSVMCEPIE KRCTFRASQL EDGDIICFQK
STPIEGVGKF RYPEVPSFLD YVHNRQVVHF RSLEKPKEDD FCLEMSKLYT YDDVVERVAQ
QLGLDDPSKI RLTSHNCYSQ QPKPQPIKYR GVDHLSDMLI HYNQTSDVLY YEVLDIPLPE
LQCLKTLKVA FHHATKDEVS VHTIRLPKQS TVGDVINDLK TKVELSQPDA ELRLLEVFYH
KIYKIFPLNE KIENINDQYW TLRAEEIPEE EKNLGPHDRL IHVYHFTKET AQNQMQIQNF
GEPFFLVIHE GETLQEIKVR IQRKLQVPDE EFAKWKFAFL SLGRPEYLQD TDIVSSRFQR
RDVYGAWEQY LGLEHSDSAP KRAYAANQNR HTYEKPVKIY N
//
