ID A0A1A9X2W0_9MUSC Unreviewed; 833 AA.
AC A0A1A9X2W0;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
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};
OS Glossina brevipalpis.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC Glossinidae; Glossina.
OX NCBI_TaxID=37001 {ECO:0000313|EnsemblMetazoa:GBRI042344-PA, ECO:0000313|Proteomes:UP000091820};
RN [1] {ECO:0000313|Proteomes:UP000091820}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAEA {ECO:0000313|Proteomes:UP000091820};
RA Aksoy S., Warren W., Wilson R.K.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:GBRI042344-PA}
RP IDENTIFICATION.
RC STRAIN=IAEA {ECO:0000313|EnsemblMetazoa:GBRI042344-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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|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}.
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DR AlphaFoldDB; A0A1A9X2W0; -.
DR STRING; 37001.A0A1A9X2W0; -.
DR EnsemblMetazoa; GBRI042344-RA; GBRI042344-PA; GBRI042344.
DR VEuPathDB; VectorBase:GBRI042344; -.
DR OrthoDB; 166948at2759; -.
DR Proteomes; UP000091820; 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; cd14294; UBA1_UBP5_like; 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; 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|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 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 193..302
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 345..832
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT DOMAIN 637..678
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 707..747
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT ACT_SITE 354
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-1"
FT ACT_SITE 794
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-1"
FT BINDING 217
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT BINDING 220
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 250
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
SQ SEQUENCE 833 AA; 94768 MW; D24D10CDC77E4004 CRC64;
MCKKEWSLDN TKIKFIALLM IMDSLCKYLS NIRIPCGKQP IYKDECVYSF DTPEISTGLY
VNLTTFLGFG ENYVLKYAEK TGNKVFLHIR REKFAKDNTM ETNKEETGPK SKITRLAIGI
EGGFNNNQTT KYEYKDTYSI VIMPDIKVKI PYPSHDLPII VNQSVEAVLA QDSAIIKLQK
EALTGSWDGE IRQNSKYSDE LHQLDNGKKI PPSGWKCEKC DLTSNLWLNL TDGSILCGRK
FFDGSGGNDH AVQHYQQFKY PLAVKLGTIT ADGKSDVFSY PEDDMVIDTK LAEHLSHFGI
NMAAMKKSEK SMVELELEIN QRIGEWSLLT ESESTLQPLA GPGYTGMRNL GNSCYINSVM
QVLFTVPDFI KRFVEKGAEM YFNEFPPDPA NDFNIQMAKL GNGLWSGKYS SIAQNTLDEC
LGISPAMFKN VVGKNHPDFG TKQQQDAYDF YLYLINLLER HSRNEFNPAE ALTFAIEERV
ECLTSKKVKY TRRDEYCLPL PIPLEKATNL DEVKDYLEKK SISTITKEGD KDIVRHNIPL
RECLERFFSS EHIEQFYSTA IKDTTSAKKS SRLVNMPDYL MMHLRKFTLG DDWVPKKLDV
SVQMPDELDM SKWRALGKQP NEEELPDTDL TKNINFIFDE NMVSSLMQMG FPQEACKRAV
FHTKNGGIDV ASDWLMEHIG DSDFSEPFVV PDFEPGNIAG KMKNTFVPNP ESLALLMSMG
FDEFKATKAL KATNGNLERA TDWIFSHIDD MDVDDTDTST SSGNQKQKVY RDGIGKYKLV
AFISHMGTSA QVGHYVCHIR KDGQWVIFND SKVALSQKPP KDLGYLYMYK REE
//
