ID A0A7J7F331_DICBM Unreviewed; 839 AA. AC A0A7J7F331; DT 07-APR-2021, integrated into UniProtKB/TrEMBL. DT 07-APR-2021, sequence version 1. DT 12-OCT-2022, entry version 6. 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=HPG69_007072 {ECO:0000313|EMBL:KAF5922184.1}; OS Diceros bicornis minor (South-central black rhinoceros). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Perissodactyla; Rhinocerotidae; Diceros. OX NCBI_TaxID=77932 {ECO:0000313|EMBL:KAF5922184.1, ECO:0000313|Proteomes:UP000551758}; RN [1] {ECO:0000313|EMBL:KAF5922184.1, ECO:0000313|Proteomes:UP000551758} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SBR-YM {ECO:0000313|EMBL:KAF5922184.1}; RC TISSUE=Skin {ECO:0000313|EMBL:KAF5922184.1}; RX PubMed=32585004; RA Moodley Y., Westbury M.V., Russo I.M., Gopalakrishnan S., Rakotoarivelo A., RA Olsen R.A., Prost S., Tunstall T., Ryder O.A., Dalen L., Bruford M.W.; RT "Interspecific Gene Flow and the Evolution of Specialization in Black and RT White Rhinoceros."; RL Mol. Biol. Evol. 37:3105-3117(2020). CC -!- FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin CC from specific proteins to regulate different cellular processes. CC {ECO:0000256|RuleBase:RU366025}. 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:KAF5922184.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; JACDTQ010001514; KAF5922184.1; -; Genomic_DNA. DR Proteomes; UP000551758; 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:0016579; P:protein deubiquitination; IEA:UniProtKB-UniRule. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro. DR Gene3D; 3.30.40.10; -; 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 Pfam; PF00627; UBA; 2. DR Pfam; PF00443; UCH; 2. DR Pfam; PF02148; zf-UBP; 1. DR Pfam; PF17807; zf-UBP_var; 1. DR PIRSF; PIRSF016308; UBP; 2. DR SMART; SM00165; UBA; 2. DR SMART; SM00290; ZnF_UBP; 1. DR SUPFAM; SSF46934; SSF46934; 1. DR SUPFAM; SSF54001; SSF54001; 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|PIRNR:PIRNR016308, ECO:0000256|RuleBase:RU366025}; 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:UP000551758}; KW Thiol protease {ECO:0000256|PIRNR:PIRNR016308, KW ECO:0000256|RuleBase:RU366025}; KW Ubl conjugation pathway {ECO:0000256|PIRNR:PIRNR016308, KW ECO:0000256|RuleBase:RU366025}; 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 210..318 FT /note="UBP-type" FT /evidence="ECO:0000259|PROSITE:PS50271" FT DOMAIN 359..837 FT /note="USP" FT /evidence="ECO:0000259|PROSITE:PS50235" FT DOMAIN 631..672 FT /note="UBA" FT /evidence="ECO:0000259|PROSITE:PS50030" FT DOMAIN 703..743 FT /note="UBA" FT /evidence="ECO:0000259|PROSITE:PS50030" FT ACT_SITE 368 FT /note="Nucleophile" FT /evidence="ECO:0000256|PIRSR:PIRSR016308-1" FT ACT_SITE 799 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR016308-1" FT BINDING 234 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3" FT BINDING 237 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3" FT BINDING 254 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3" FT BINDING 267 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3" SQ SEQUENCE 839 AA; 94763 MW; FE307FAE17C454B6 CRC64; MQRRGALFGM PGGSGGRKMA AGDIGELLVP HMPTIRVPRS GDRVYKNECA FSYDSPNSEG GLYVCMNTFL AFGREHVERH FRKTGQSVYM HLKRHVRETL RFDFSYDYFH GRGYCQVTVL KINPKEKSTP SRYCQLIATV EDLDTDDDLN SDDYEYEDEA KLVIFPDHYE IALPNIEELP ALVTIACDAV LSSKSPYRKQ DPDTWENELP VSKYANNLAQ LDNGVRIPPS GWKCARCDLR ENLWLNLTDG SVLCGKWFFD SSGGNGHALE HYRDVGYPLA VKLGTITPDG ADVYSFQEEE PVLDPHLAKH LAHFGIDMLH MHGTENGLRD NDIKPRVSEW EVIQETGTKL KPMYGPGYTG LQNLGNSCYL SSVMQAVFSI PEFQRAYVGN LPRIFDYSPL DPTQDFNTQM TKLGHGLLSG QYSKPPVKSE LIEQVMKEEH KRNRIGSENP SDVFRFLVEE RIQCCQTRKV RYTERVDYLM QLPVAMEAAT NKDELIAYEL TRREAEANRR PLPELVRAKI PFSACLQAFS EPENVDDFWS SALQAKSAGV NPVVETVRTS RFASFPEYLV VQIKKFTFGL DWVPKKFDVS IDMPDLLDIN HLRAKGLQPG EEELPDISPP IVIPDDSKAS DIDESSVMQL AEMGFPLEAC RKAVYFTGNM GAEVAFNWII VHMEEPDFAE PLTMPGYGGA ASAVFGATGL DNQPPEEIVA IITSMGFHRN QAIQALRATN NNLERALDWI FSHPEFEEDS DFVIEMENNA NANIISEAKP EGPRVKDGSG MYELFAFISH MGTSTMSGHY VCHIKKEGRW VIYNDHKVCA SERPPKDLGY MYFYRRIPS //