ID A0A0S3RK52_PHAAN Unreviewed; 1168 AA.
AC A0A0S3RK52;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN Name=Vigan.03G058100 {ECO:0000313|EMBL:BAT80951.1};
GN ORFNames=VIGAN_03058100 {ECO:0000313|EMBL:BAT80951.1};
OS Vigna angularis var. angularis.
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; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=157739 {ECO:0000313|EMBL:BAT80951.1, ECO:0000313|Proteomes:UP000291084};
RN [1] {ECO:0000313|EMBL:BAT80951.1, ECO:0000313|Proteomes:UP000291084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Shumari {ECO:0000313|Proteomes:UP000291084};
RX PubMed=26616024; DOI=10.1038/srep16780;
RA Sakai H., Naito K., Ogiso-Tanaka E., Takahashi Y., Iseki K., Muto C.,
RA Satou K., Teruya K., Shiroma A., Shimoji M., Hirano T., Itoh T., Kaga A.,
RA Tomooka N.;
RT "The power of single molecule real-time sequencing technology in the de
RT novo assembly of a eukaryotic genome.";
RL Sci. Rep. 5:16780-16780(2015).
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; AP015036; BAT80951.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S3RK52; -.
DR Proteomes; UP000291084; Chromosome 3.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:SF929; UBIQUITINYL HYDROLASE 1; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000291084};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT TRANSMEM 1115..1136
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 54..179
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 199..523
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT COILED 532..563
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1168 AA; 137384 MW; 1427960C812B00A2 CRC64;
MTVMTPAPID QQEDEEMLVP HTDLAENNHQ PMEVVAQPDA ANTVESQPVE DPSSTRFTWK
IDNFSRMNSK KLYSEIFVVG GYKWRVLIFP KGNNVDYLSM YLDVADSSSL PYGWSRYAQF
SLAVINQIHN KYSVRKDTQH QFNARESDWG FTSFMPLGEL YDPTRGYLVN DTLVVEAEVL
VRRIVDYWTY DSKKETGYVG LKNQGATCYM NSLLQTLYHI PYFRKAVYHM PTTENDMPSA
SIPLALQSLF YKLQYSDTSV ATKELTKSFG WDTYDSFMQH DVQELNRVLS EKLEDKMKGT
VVEGTIQKLF EGHHMNYIEC INVDYKSTRK ESFYDLQLDV KGCPDVYASF DKYVEVERLE
GDNKYHAEQY GLQDAKKGVL FIDFPPVLQL QLKRFEYDFL RDTMVKINDR YEFPMQLDLD
RENGKYLSPE ADRNVRNLYT LHSVLVHSGG VHGGHYYAFI RPTLSEQWYK FDDERVTKED
TKRALEEQYG GEEELPQTNP GFNNTPFKFT KYSNAYMLVY IREADKDKVI CNVDEKDIAE
HLRERLKKEQ EEKEHKKKEK AEAHLYTIIK VARDEDLAEQ IGKDIYFDLV DHDKVRSFRV
QKQTSFNLFK DEVAKEFNIP VQFQRFWLWA KRQNHTYRPN RPLTPMEEAQ SVGQLREVSN
KVHNAELKLF LEVELGLDLR PIAPPDKTKD DILLFFKLYD PEKEELRYVG RLFVKNTGKP
LEILTKLNKM AGYDPDEEIG LYEEIKFEPN VMCEPIDKKL TFRASQLEDG DIICFQKAPA
IYNEEHVRHP DVPSYLEYVH NRQVVHFRSL DKPKEDDFCL EMSRLYKYDD VVERVAQQLG
LDDPSIIRLT PHNCYSQQPK PQPVKYRGVE HLSEMLVHYN QTSDILYYEV LDIPLPELQG
LKTLKVAFHH ATKDEVVIHT IRLPKQSTVG DVLDDLKTKV ELSSPEAELR LLEVFYHKIY
KVFPPNEKIE NINDQYWTLR AEEIPEEEKN LGPHDRLIHV YHFTKDTAQN QMQIQNFGEP
FFLVIREGET LTEIKVRIQK KLQVPDDEFA KWKFAFFSLG RPEYLQDSDI VSNRFQRRDV
YGAWEQYLGL EHTDNAPKRS YAVNQVSNLV YKNYFLKYIF FFYLFLLSLL TVLVILKFSL
KFKKTCLITH HFKFLGFCFR IAILLRSQ
//
