ID T1KN99_TETUR Unreviewed; 550 AA.
AC T1KN99;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN Name=107365914 {ECO:0000313|EnsemblMetazoa:tetur16g00200.1};
OS Tetranychus urticae (Two-spotted spider mite).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Trombidiformes; Prostigmata; Eleutherengona; Raphignathae;
OC Tetranychoidea; Tetranychidae; Tetranychus.
OX NCBI_TaxID=32264 {ECO:0000313|EnsemblMetazoa:tetur16g00200.1, ECO:0000313|Proteomes:UP000015104};
RN [1] {ECO:0000313|Proteomes:UP000015104}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=London {ECO:0000313|Proteomes:UP000015104};
RA Rombauts S.;
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:tetur16g00200.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) to UniProtKB.
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 ECO:0000256|RuleBase:RU366025};
CC -!- SIMILARITY: Belongs to the peptidase C19 family. UBP8 subfamily.
CC {ECO:0000256|ARBA:ARBA00038490}.
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DR EMBL; CAEY01000275; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015788973.1; XM_015933487.1.
DR AlphaFoldDB; T1KN99; -.
DR STRING; 32264.T1KN99; -.
DR EnsemblMetazoa; tetur16g00200.1; tetur16g00200.1; tetur16g00200.
DR GeneID; 107365914; -.
DR KEGG; tut:107365914; -.
DR eggNOG; KOG1867; Eukaryota.
DR HOGENOM; CLU_008279_11_0_1; -.
DR OMA; QRDQWFK; -.
DR OrthoDB; 227085at2759; -.
DR Proteomes; UP000015104; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02660; Peptidase_C19D; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001607; Znf_UBP.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF33; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 22; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU366025};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000015104};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00502}.
FT DOMAIN 42..162
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 201..545
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 550 AA; 63445 MW; BE69586B4F41394C CRC64;
MIKSYLTGNS DNKSTDERQD DLEDKGFKAI CDDREDLKYG SAGCSHVEAF KATKHGLKNF
TLIFSNFVVA ISVEAKKRKS QAMICFNCGP QKYPTRLHAC LECIYFGCYQ HKHIHEHAKT
TKHNLAIDIT WGYVYCYPCR DYVYDSELER IGKRKKWKAN KLMGTAFAQY YTWEPTLHEL
EILKQNSQRR RISDNSYIGL RGLINLGNTC FMNCIVQALT HTPLLRDYFL SDKHICQFRD
DPSMCLVCEM SRLFQEFYSG KSTPHIPFKL LHLVWTHARH LAGYEQQDAH EFFIATLDVL
HRHCKGSNGP SNSNPHHCTC IIDQIFTGNL QSDVVCQYCK GVSTTIDPFW DISLDLGPSL
HMRQQLAASS TTQTYCDESE PKSLLDCLER FTRPEHLGSS AKIKCSTCQI NQESTKQLSM
KKLPIVASFH LKRFEHSNRF HKKISTFISF PQYLDMSPFM ASRRGCKPTI DPPSPSYANG
SQLNENKYCL FAVVNHSGTI ETGHYTAYVR QHKDQWFKCD DHIITRASVQ DVLDSEGYLL
FYHKEFLEYE
//
