ID A0A5N3XJ23_MUNRE Unreviewed; 794 AA.
AC A0A5N3XJ23;
DT 26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2020, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|PIRNR:PIRNR016308};
DE EC=3.4.19.12 {ECO:0000256|PIRNR:PIRNR016308};
GN ORFNames=FD755_014238 {ECO:0000313|EMBL:KAB0373982.1};
OS Muntiacus reevesi (Reeves' muntjac) (Cervus reevesi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Cervidae;
OC Muntiacinae; Muntiacus.
OX NCBI_TaxID=9886 {ECO:0000313|EMBL:KAB0373982.1, ECO:0000313|Proteomes:UP000326062};
RN [1] {ECO:0000313|EMBL:KAB0373982.1, ECO:0000313|Proteomes:UP000326062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCam_UCB_Mr {ECO:0000313|EMBL:KAB0373982.1};
RC TISSUE=Fibroblast cell line {ECO:0000313|EMBL:KAB0373982.1};
RA Mudd A.B., Bredeson J.V., Baum R., Hockemeyer D., Rokhsar D.S.;
RT "Discovery of a novel chromosome fission-fusion reversal in muntjac.";
RL Submitted (JUN-2019) 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|PIRNR:PIRNR016308};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085, ECO:0000256|PIRNR:PIRNR016308}.
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:KAB0373982.1}.
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DR EMBL; VCEB01000008; KAB0373982.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5N3XJ23; -.
DR Proteomes; UP000326062; Chromosome 8.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02658; Peptidase_C19B; 1.
DR CDD; cd14384; UBA1_UBP13; 1.
DR CDD; cd14386; UBA2_UBP5; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR016652; Ubiquitinyl_hydrolase.
DR InterPro; IPR041432; UBP13_Znf-UBP_var.
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:SF10; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 14; 1.
DR Pfam; PF00627; UBA; 2.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR Pfam; PF17807; zf-UBP_var; 1.
DR PIRSF; PIRSF016308; UBP; 3.
DR SMART; SM00165; UBA; 2.
DR SMART; SM00290; ZnF_UBP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF46934; UBA-like; 1.
DR PROSITE; PS50030; UBA; 2.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR016308};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR016308};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PIRNR:PIRNR016308};
KW Reference proteome {ECO:0000313|Proteomes:UP000326062};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807,
KW ECO:0000256|PIRNR:PIRNR016308};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PIRNR:PIRNR016308};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR016308};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00502}.
FT DOMAIN 145..253
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 294..792
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT DOMAIN 610..651
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 685..725
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT BINDING 169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT BINDING 172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT BINDING 202
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
SQ SEQUENCE 794 AA; 89104 MW; 732B89284921C894 CRC64;
MQRRGALFGM PGGSGSRKMA AGDIGELLVP HMPTIRVPRS GDRVYKNECA FSYDSPKVRG
ASGGALPKRR NSKIFLDLDT DDDLNSDDYE YEDEAKLVIF PDHYEIALPN IEELPALVTI
ACDAVLSSKS PYRKQDPDTW ENELPVSKYA NNLTQLDNGV RIPPSGWKCA RCDLRENLWL
NLTDGSVLCG KWFFDSSGGN GHALEHYRDT GYPLAVKLGT ITPDGADVYS FQEEEAVLDP
HLAKHLAHFG IDMLHMHGTE NGLQDNDIKP RVSEWEVIQE TGTKLKPMYG PGYTGLKNLG
NSCYLSSVMQ AIFSIPEFQR AYVGNLPRIF DYSPLDPTQD FNTQMTKLGH GLLSGQYSKP
PVKSELIEQV MKEELKPQQN GISPRMFKAF VSKSHPEFSS NRQQDAQEFF LHLVNLVERN
RIGSENPSDV FRFLVEERIQ CCQTRKVRYT ERVDYLMQLP VAMEAATNKD ELIAYELTRR
EAESNRRPLP ELVRAKIPFS ACLQAFSEPE NVDDFWSSAL QAKSAGVKTS RFASFPEYLV
VQIKKFTFGL DWVPKKFDVS IDMPDLLDIN HLRARGLQPG EEELPDISPP IVIPDDSKDR
LMTQLIDPSD IDESSVMQLA EMGFPLEACR KAVYFTGNMG AEVAFNWIVV HMEEPDFAEP
LTMPGYGGAA SAGASVFGAT GLDNQPPEET VAIITSMGFH RNQAIQALRA TNSNLERALD
WIFSHPEFEE DSDFVVEMEN NANANIVSEA KPEGPRVKDG SGSKWVIYND HKVCASERPP
KDLGYMYFYR RIPS
//
