ID G0QNI9_ICHMG Unreviewed; 735 AA. AC G0QNI9; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 03-AUG-2022, entry version 41. DE RecName: Full=Ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759}; DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759}; GN ORFNames=IMG5_058990 {ECO:0000313|EMBL:EGR33224.1}; OS Ichthyophthirius multifiliis (strain G5) (White spot disease agent) (Ich). OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; OC Oligohymenophorea; Hymenostomatida; Ophryoglenina; Ichthyophthirius. OX NCBI_TaxID=857967 {ECO:0000313|Proteomes:UP000008983}; RN [1] {ECO:0000313|EMBL:EGR33224.1, ECO:0000313|Proteomes:UP000008983} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=G5 {ECO:0000313|EMBL:EGR33224.1, RC ECO:0000313|Proteomes:UP000008983}; RA Coyne R., Brami D., Johnson J., Hostetler J., Hannick L., Clark T., RA Cassidy-Hanley D., Inman J.; RL Submitted (JUL-2011) 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 --------------------------------------------------------------------------- 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; GL983490; EGR33224.1; -; Genomic_DNA. DR RefSeq; XP_004037210.1; XM_004037162.1. DR STRING; 857967.G0QNI9; -. DR EnsemblProtists; EGR33224; EGR33224; IMG5_058990. DR GeneID; 14909397; -. DR eggNOG; KOG0605; Eukaryota. DR eggNOG; KOG2935; Eukaryota. DR InParanoid; G0QNI9; -. DR OMA; WINQKIT; -. DR Proteomes; UP000008983; Unassembled WGS sequence. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC. DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro. DR GO; GO:0016579; P:protein deubiquitination; IEA:InterPro. DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro. DR InterPro; IPR006155; Josephin. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR Pfam; PF02099; Josephin; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM01246; Josephin; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; SSF56112; 1. DR PROSITE; PS50957; JOSEPHIN; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU10141}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE- KW ProRule:PRU00331}; Kinase {ECO:0000313|EMBL:EGR33224.1}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Protease {ECO:0000256|ARBA:ARBA00022670}; KW Reference proteome {ECO:0000313|Proteomes:UP000008983}; KW Transferase {ECO:0000313|EMBL:EGR33224.1}. FT DOMAIN 1..158 FT /note="Josephin" FT /evidence="ECO:0000259|PROSITE:PS50957" FT DOMAIN 406..698 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 199..228 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 209..228 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 5 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00331" FT ACT_SITE 96 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00331" FT ACT_SITE 111 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00331" FT BINDING 435 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 735 AA; 85858 MW; D89042F08CA8DC4E CRC64; MDMLCGVHCI NSLLQGPFFN EIELASIARE LDEQEKLLMI QQGSQNVGDD GNYSIQVLQQ ALQKMGNLII ESVDSQINKA QDLSSEQGFI CNSANHWFAI RKVNNIWYNL NSTNQFGPEI ISEFYLSAFL LSVKENGYSI FVVRGDYPNN DQSPFQKWFI ESELKQIHQQ RIKDKDKNYK LNIGGTDERD LERAIKKSMK QYTQDNQQKQ KMEQEDDDYE SKQKEQEESN KFIAFQGQGH SLIQQQQKKD EPLEEYFSQF AVNQEDPELL FVLKMSLEQK FEKRPEQGIT LQFRFTEGFK KDWTFNQQDQ IRPQANKYFK NQPVNNVRIT AATKDRAEAA KLYIEKKYAK MLQKEIENKE YWNELYKKMQ EMQFTPQEQM IIKHNIIQKE GEHLRKFRSK KSTKDYEPLT IIGRGAFGEV RICRDKQTQE IVAIKRMKKQ DMSSKAQIGH IRSERDVLST SGNPWIIELK QSFQDDKYLY LVMDYMPGGD LMNVLIKKDI LTEEEAKFYI AEILLAIESV HKMNYIHRDL KPDNILIGAD GHIKLSDFGL CKQTEIRPLI TFGKKEELDQ DAIKANPNLL LTKRPLNYKK NRHLAFSTVG TPDYIAPEVF GQSGYTETVD WWSLGIILFE MLVGYPPFYS DDPPITCQKI IQWKKIFSIP AEANLSIAAQ DLIRKLIADS QERLGRNGAT EIKIHPFFEG INWKKIREKK APYIPEVLFF IIKKQKQKSK GQEHR //