ID A0A226MIG9_CALSU Unreviewed; 853 AA.
AC A0A226MIG9;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|PIRNR:PIRNR016308, ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|PIRNR:PIRNR016308, ECO:0000256|RuleBase:RU366025};
GN ORFNames=ASZ78_016452 {ECO:0000313|EMBL:OXB54839.1};
OS Callipepla squamata (Scaled quail).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Odontophoridae;
OC Callipepla.
OX NCBI_TaxID=9009 {ECO:0000313|EMBL:OXB54839.1, ECO:0000313|Proteomes:UP000198323};
RN [1] {ECO:0000313|EMBL:OXB54839.1, ECO:0000313|Proteomes:UP000198323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Texas {ECO:0000313|EMBL:OXB54839.1,
RC ECO:0000313|Proteomes:UP000198323};
RC TISSUE=Leg muscle {ECO:0000313|EMBL:OXB54839.1};
RA Oldeschulte D.L., Halley Y.A., Bhattarai E.K., Brashear W.A., Hill J.,
RA Metz R.P., Johnson C.D., Rollins D., Peterson M.J., Bickhart D.M.,
RA Decker J.E., Seabury C.M.;
RT "Disparate Historic Effective Population Sizes Predicted by Modern Levels
RT of Genome Diversity for the Scaled Quail (Callipepla squamata) and the
RT Northern Bobwhite (Colinus virginianus): Inferences from First and Second
RT Generation Draft Genome Assemblies for Sympatric New World Quail.";
RL Submitted (JUL-2016) 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, ECO:0000256|RuleBase:RU366025};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085, ECO:0000256|PIRNR:PIRNR016308,
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:OXB54839.1}.
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DR EMBL; MCFN01000847; OXB54839.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A226MIG9; -.
DR STRING; 9009.A0A226MIG9; -.
DR Proteomes; UP000198323; Unassembled WGS sequence.
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; 2.
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; 1.
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; 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|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR016308};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR016308};
KW Protease {ECO:0000256|PIRNR:PIRNR016308, ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000198323};
KW Thiol protease {ECO:0000256|PIRNR:PIRNR016308,
KW ECO:0000256|RuleBase:RU366025};
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 183..293
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 334..851
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT DOMAIN 641..682
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 713..753
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT ACT_SITE 343
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-1"
FT ACT_SITE 813
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-1"
FT BINDING 209
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT BINDING 212
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT BINDING 229
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT BINDING 242
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
SQ SEQUENCE 853 AA; 95633 MW; 66A286412A7C5824 CRC64;
MQRAALFGGG GDAQMAAGDL GELLVPYMPT IRVPKSGDRV YKTECAFSYD SPDSEGGLYV
CMNTFLGFGR EHIERHYRKT GQCVYLHLKR HVIEKVPGAS GGALPKRRNA KLFLDLEANG
DLSSDDFEYE DEAKLVIFPD HYEISLPNIE ELPALVTIAS DALLSAKSPY RKQDPDSWEE
ELQASKHAKS LVQLDNGVRI PPRQVGWKCS KCDLRENLWL NLTDGSVLCG KWFFDGSGGN
GHAIEHYKET GYPLAVKLGT ITPDGADVYS FDEEEPVLDP HIAKHLAHFG IDMLQMQVAE
NGLRDNDIKP RVSEWEVIQE AGVKLKPMYG PGYTGMKNLG NSCYLNAVMQ AIFSIPEFQR
AYVGNLPRIF DYSPLDPTQD FNTQMAKLGH GLLSGQYSKP PMKSELIEQV MKEEHKPQHN
GISPQMFKAF ISKDHTEFSS NRQQDAQEFF LHLINLVERN PVGSENPSDV FRFLVEERTQ
CCQSRKVRYT ERVDYIMQLP VAMEAATNKD ELIAYELKRR EAEAARRAPP ELVRAKIPFS
ACLQAFSEPS NVEDFWSSAL QAKSAGVKTS RFASFPQYLV VQIKKFTFGL DWIPKKLDVS
IDMPDFLDIN HLRATGLQPG EEELPDIAPP IIIPEEPKAL DIDESSVMQL AEMGFPLEAC
RKAVYYTGNL GAEVAFNWII AHMEEPDFAE PLIVPLFGGA ASGGLGAVGL DNQPPEEMVS
IIISMGFQRN LAIQALKATN NNLERAMEWI FSHPELEEED GEPALNVMDL ENRTNANILA
ETRSEGPSIK DGPGRYELFG FISHMGTSTM SGHYVCHLKK EGRWVIYNDL RVCASERPPK
DLGYIYFYHR IPS
//
