ID T1EDT8_HELRO Unreviewed; 819 AA.
AC T1EDT8;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 73.
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 Name=20194740 {ECO:0000313|EnsemblMetazoa:HelroP105332};
GN ORFNames=HELRODRAFT_105332 {ECO:0000313|EMBL:ESO12425.1};
OS Helobdella robusta (Californian leech).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata;
OC Hirudinea; Rhynchobdellida; Glossiphoniidae; Helobdella.
OX NCBI_TaxID=6412 {ECO:0000313|EnsemblMetazoa:HelroP105332, ECO:0000313|Proteomes:UP000015101};
RN [1] {ECO:0000313|Proteomes:UP000015101}
RP NUCLEOTIDE SEQUENCE.
RA Hellsten U., Grimwood J., Chapman J.A., Shapiro H., Aerts A., Otillar R.P.,
RA Terry A.Y., Boore J.L., Simakov O., Marletaz F., Cho S.-J.,
RA Edsinger-Gonzales E., Havlak P., Kuo D.-H., Larsson T., Lv J., Arendt D.,
RA Savage R., Osoegawa K., de Jong P., Lindberg D.R., Seaver E.C.,
RA Weisblat D.A., Putnam N.H., Grigoriev I.V., Rokhsar D.S.;
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ESO12425.1, ECO:0000313|Proteomes:UP000015101}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23254933; DOI=10.1038/nature11696;
RA Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT "Insights into bilaterian evolution from three spiralian genomes.";
RL Nature 493:526-531(2013).
RN [3] {ECO:0000313|EnsemblMetazoa:HelroP105332}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) 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}.
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; AMQM01000166; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KB095811; ESO12425.1; -; Genomic_DNA.
DR RefSeq; XP_009009145.1; XM_009010897.1.
DR AlphaFoldDB; T1EDT8; -.
DR STRING; 6412.T1EDT8; -.
DR EnsemblMetazoa; HelroT105332; HelroP105332; HelroG105332.
DR GeneID; 20194740; -.
DR KEGG; hro:HELRODRAFT_105332; -.
DR CTD; 20194740; -.
DR eggNOG; KOG0944; Eukaryota.
DR HOGENOM; CLU_009884_1_0_1; -.
DR InParanoid; T1EDT8; -.
DR OMA; KVKYKTR; -.
DR OrthoDB; 166948at2759; -.
DR Proteomes; UP000015101; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
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; 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|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:UP000015101};
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 165..273
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 316..819
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT DOMAIN 623..664
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 686..726
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT REGION 738..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..754
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 325
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-1"
FT ACT_SITE 781
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-1"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT BINDING 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT BINDING 199
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-2"
FT BINDING 209
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT BINDING 211..214
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-2"
FT BINDING 222
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT BINDING 249
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-2"
FT BINDING 251
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-2"
FT BINDING 254
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-2"
SQ SEQUENCE 819 AA; 92107 MW; D4604A9966C2C947 CRC64;
MASDEQCFLN VRIPDERDRI HKDECCLSFD NAESENGLYI CMNKFLAFGK RHLETYSKRT
NSMVFLNVKR LVKEKECIIS EPEAKKPTRL AIGFEGGFPM DDDKHEYEDI YTIVVLPSWT
EYSLNDSTLP PHVIASAKSI ISAESAARKT EIENLAGTWD GEKRSISKFA ADLLQLNNNK
KVAPSGWKCE KCDKVDNLWL NLTDGSILCG RKFFDGTGGN NHASEHYLAT NYPLAVKLGT
ITKDSADVYS YAEDDMVEDP FLAHHLAHFG IDIMRMHKTE KTMLELELDL NQRAWEWSAL
TECHSQLQPI YGPGYTGMYN LGNSCYINSV VQMLFNCLPS FVEKYYTPSE KVFSGASYED
PTSNFNVQMC KLAHGLLSGE YSRPSLKDAC NSDTPTSSNH SCQGIKPQMF KNLVGRGHAE
FSSNKQQDAA EYMLHLFSVI ERHCVGSSNP TDHLRFQIEE RIQCSASNKV KYVERKDFIL
SLSVDADDAV NKDDVLVYEE RKKKAEALGQ KLDCAETVRP KILLSSSIAS FASQCTVEDF
YSSAINGKTT AFKTTRFKTF PEFLLIQLQK FTIGTDWLEK KLDVSVDMPD ILDISHLRGS
GLQPGEEELP DATKCGDVPN EPVFDENIVS EMVMMGFPLE GCKKAVYYTK SQSLDAAVDW
IMEHIADSDL SSPMVLNAKE VPSEFMADEE ALLTITSMGF TRKMALTALQ ATDNNMERAM
DWIFSHPEAT DASLEQQQHQ LSANQQQVSA PLSTPKLTDG PGRYRLTGMI SHMGSSCKCG
HYVCHILKDG KWVIYNDEKV ALSEKPPKDL AYLYLYQRI
//
