ID A0A1I8CHH3_9BILA Unreviewed; 923 AA.
AC A0A1I8CHH3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
OS Rhabditophanes sp. KR3021.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Alloionematidae;
OC Rhabditophanes.
OX NCBI_TaxID=114890 {ECO:0000313|Proteomes:UP000095286, ECO:0000313|WBParaSite:RSKR_0000425700.1};
RN [1] {ECO:0000313|WBParaSite:RSKR_0000425700.1}
RP IDENTIFICATION.
RC STRAIN=KR3021 {ECO:0000313|WBParaSite:RSKR_0000425700.1};
RG WormBaseParasite;
RL Submitted (NOV-2016) 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|RuleBase:RU366025};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085, ECO:0000256|RuleBase:RU366025}.
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DR AlphaFoldDB; A0A1I8CHH3; -.
DR WBParaSite; RSKR_0000425700.1; RSKR_0000425700.1; RSKR_0000425700.
DR Proteomes; UP000095286; Unplaced.
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 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; PF00443; UCH; 1.
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; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF46934; UBA-like; 2.
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|RuleBase:RU366025};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR016308-3}; Protease {ECO:0000256|RuleBase:RU366025};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU366025};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR016308-3};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00502}.
FT DOMAIN 198..312
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 354..921
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT DOMAIN 725..766
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 789..829
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT REGION 830..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 363
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-1"
FT ACT_SITE 883
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-1"
FT BINDING 222
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT BINDING 227
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT BINDING 244
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT BINDING 261
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
SQ SEQUENCE 923 AA; 104725 MW; CDCB083F339B410B CRC64;
MDVERSAFPV LKIKESLVLP EEFPICDSWE IASKREKVFK EECMYCFKNL DDSEGIFICM
NTFSCFCKDH VSDYSLTSHK TAFVNLVNIK TDVPADITDE DEEEDEMSSE PSTKLSKLDV
DVPAIKETPV KRVQMVTETL ESHYICHVKG TDVTRVPIDR VKSRGIRSIA DSIITHETVS
VQERMAGQVS EWDGTSRVIT KHSKNLEQIC TEKLIPTSGW ICEVAGCGIS ENLWLNLTDG
AIKCGRTQYI SEGNVTVGNN HMHQHYEDTG YPLVVKLGTI TSEDADVYSY DEDDSVIDLN
LSLHLANFGI DRHSIAKTEK STYEMEMDFN QKYEWNLIQE EGSTLKIAYG VGFTGLINIG
SSCYINSAIQ MLCVVPTFVD TFRTHAMQIL KSMQPKETHG DFMAQTAKLI SSMLSGEFSI
PGDNIHVIKP TQFRKVVGEG HCEFSTGKQQ DVEEYIRYFF ELLTKNIGSY QNPVNDFRLK
LEHKFTDASS GHVRYNDREE VIISVSVPQD KLAKATLLNP RRSISIEDCL DAYFGREFIP
DFESPITKEK AGAYNSCMLK NMPDFLLIHI RKFEVTPQFT LKKMDIDVNM ADVLDFEKYR
AKEHDPSEIL LPEDIEEDAM RAPSGKKEES LIEGNVNKKF LKDMLETGFS ELCCRKALIA
TQNQITPQFT LKKMDIDVNM ADVLDFEKYR AKEHDPSEVL LPEDIEEDAM RAPSGKKEES
LIEGNVNKKF LKDMLETGFS ELCCRKALIA TQNQSMDIAI DYLMNHMDDA GFMNDPIPAS
KLRPINISRW NKEDIGNLLS MGFTPHQANY AMTEMKGNLM NAADFLIQSG GAVPPPDEDD
EEDEVKNEDD VKQQQNIRFK DGQGKYKLVG FISHMGTSTS CGHYVVHLKK GDHWYIYNDE
KVGISQKPPL SLGYVYIYER ENV
//
