ID A0A151RAP6_CAJCA Unreviewed; 218 AA.
AC A0A151RAP6;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Ubiquitin thioesterase OTU {ECO:0000256|RuleBase:RU367104};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU367104};
GN ORFNames=KK1_039097 {ECO:0000313|EMBL:KYP39576.1};
OS Cajanus cajan (Pigeon pea) (Cajanus indicus).
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; Cajanus.
OX NCBI_TaxID=3821 {ECO:0000313|EMBL:KYP39576.1, ECO:0000313|Proteomes:UP000075243};
RN [1] {ECO:0000313|EMBL:KYP39576.1, ECO:0000313|Proteomes:UP000075243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Asha {ECO:0000313|Proteomes:UP000075243};
RX PubMed=22057054; DOI=10.1038/nbt.2022;
RA Varshney R.K., Chen W., Li Y., Bharti A.K., Saxena R.K., Schlueter J.A.,
RA Donoghue M.T., Azam S., Fan G., Whaley A.M., Farmer A.D., Sheridan J.,
RA Iwata A., Tuteja R., Penmetsa R.V., Wu W., Upadhyaya H.D., Yang S.P.,
RA Shah T., Saxena K.B., Michael T., McCombie W.R., Yang B., Zhang G.,
RA Yang H., Wang J., Spillane C., Cook D.R., May G.D., Xu X., Jackson S.A.;
RT "Draft genome sequence of pigeonpea (Cajanus cajan), an orphan legume crop
RT of resource-poor farmers.";
RL Nat. Biotechnol. 30:83-89(2012).
CC -!- FUNCTION: Hydrolase that can remove conjugated ubiquitin from proteins
CC and may therefore play an important regulatory role at the level of
CC protein turnover by preventing degradation.
CC {ECO:0000256|RuleBase:RU367104}.
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:RU367104};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU367104}.
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DR EMBL; KQ483896; KYP39576.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151RAP6; -.
DR STRING; 3821.A0A151RAP6; -.
DR OMA; NRYCQRI; -.
DR Proteomes; UP000075243; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.90.70.80; -; 1.
DR InterPro; IPR003323; OTU_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR PANTHER; PTHR13312; HIV-INDUCED PROTEIN-7-LIKE PROTEASE; 1.
DR PANTHER; PTHR13312:SF3; OVARIAN TUMOR DOMAIN-CONTAINING DEUBIQUITINATING ENZYME 3; 1.
DR Pfam; PF02338; OTU; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS50802; OTU; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|RuleBase:RU367104};
KW Hydrolase {ECO:0000256|RuleBase:RU367104};
KW Protease {ECO:0000256|RuleBase:RU367104};
KW Reference proteome {ECO:0000313|Proteomes:UP000075243};
KW Thiol protease {ECO:0000256|RuleBase:RU367104};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU367104}.
FT DOMAIN 67..218
FT /note="OTU"
FT /evidence="ECO:0000259|PROSITE:PS50802"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KYP39576.1"
SQ SEQUENCE 218 AA; 24217 MW; 35E23D353FC29FB0 CRC64;
LSEDVLQQLR NGSAKFEVVS SPVPSVAAPP NNNASLFGIG NCSTLFFARI APSFGGHSPA
MKKLERFSVQ KVTGDGRCLF RALVKGMAYN KGTVLNQREE RENADELRMA VKEAICENEG
ERNLYEEALI AITVDEPLKR YCQRIVRSDF WGGESELLVL SKLCKQPIIV YIPEHEHRGG
GFGSGFIIAE YGSEFRKGSS RKAVRLLYSG KNHYDLLV
//
