ID A0A0T6B0K4_9SCAR Unreviewed; 844 AA.
AC A0A0T6B0K4;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
DE Flags: Fragment;
GN ORFNames=AMK59_6061 {ECO:0000313|EMBL:KRT80908.1};
OS Oryctes borbonicus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Scarabaeiformia;
OC Scarabaeidae; Dynastinae; Oryctes.
OX NCBI_TaxID=1629725 {ECO:0000313|EMBL:KRT80908.1, ECO:0000313|Proteomes:UP000051574};
RN [1] {ECO:0000313|EMBL:KRT80908.1, ECO:0000313|Proteomes:UP000051574}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OB123 {ECO:0000313|EMBL:KRT80908.1};
RC TISSUE=Whole animal {ECO:0000313|EMBL:KRT80908.1};
RA Meyer J.M., Markov G.V., Baskaran P., Herrmann M., Sommer R.J.,
RA Roedelsperger C.;
RT "Draft genome of the scarab beetle Oryctes borbonicus.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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.
CC {ECO:0000256|RuleBase:RU366025}.
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:KRT80908.1}.
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DR EMBL; LJIG01016336; KRT80908.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T6B0K4; -.
DR OrthoDB; 227085at2759; -.
DR Proteomes; UP000051574; Unassembled WGS sequence.
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; cd02667; Peptidase_C19K; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
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:SF39; UBIQUITINYL HYDROLASE 1; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR SMART; SM00290; ZnF_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:UP000051574};
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 25..146
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 188..844
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..486
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 844
FT /evidence="ECO:0000313|EMBL:KRT80908.1"
SQ SEQUENCE 844 AA; 94939 MW; 48784259EB95FE66 CRC64;
MGKKKHQTGP NHNSDESTES CDEITSCPHI GKSTSLTVLK QAINEKGIQK DCEECLNSPV
VNGFDLPSEF EVDDSLWMCL MCGNQGCGRA ANKHALKHYN SLHPENHSLC INTTLIRVWC
YDCDNQININ ASKKLREISD FLAEVAEKDH RKYERTKKSN FNNISPIIQT DSSTKATKAK
TVTLPKVCGL RNLGNTCFFN SVLQCLGQTP YLAELLEETS ISGQYFKLPG GSLVFDDNNS
TILEPLDGNL ESWRLLPRVL AETLRTLQSG NIQVYSPSAL LSKLIQRMPQ FGGGDQHDSH
ELLRHLLEAV REEDLRRYQA IILDKLGLSK KTDPSVVEGN KKKIIRYYGT QASEMLSPTE
QVFRGILVST LQCEDCSHTS HREEFFLDLS LPITEKTIPP LLRRKADEIE DKSKHQIKKE
KRAAKKNKKY KGQKNLILPM KSVDVLTKSE SNSGSESDAD VEDNLEDNKH TQVNEEKLKG
LESGYNSDKV DNDSPVNNRI ASPDMHIDDS GVPSPAVGML CVSPLEAGSL ETSPSSSEMC
GINIGSPTGG HLSPNEEMVE EFERPESRLS FVNNKNGDIK EDLEKLSLLN EGDGGKIDMF
ARKNLYDEAC CKMEDDKEEK MEEDEDLELW TGTMSQRYQC EEGELSVQSC LNQFTACELM
TSNNKVSCEL CTKRYGGQEK KTVYTTATKQ LLIYNPPAVL ILHLKRFQVY HFRPTKVSKH
VTFPTLLDLA PYCSKRSQSL PTFEVGQTQV LYSLYGVVEH SGSIHGGHYV AYIKVRPKLE
KTSYRWQFLP KNQKERKPSD GLKGAQGIPD VPPGKWYYVS DSHVTEVQES KVLNAQAYLL
FYER
//
