ID E4X569_OIKDI Unreviewed; 838 AA.
AC E4X569;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=GSOID_T00002299001 {ECO:0000313|EMBL:CBY18438.1};
OS Oikopleura dioica (Tunicate).
OC Eukaryota; Metazoa; Chordata; Tunicata; Appendicularia; Copelata;
OC Oikopleuridae; Oikopleura.
OX NCBI_TaxID=34765 {ECO:0000313|EMBL:CBY18438.1};
RN [1] {ECO:0000313|EMBL:CBY18438.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21097902; DOI=10.1126/science.1194167;
RA Denoeud F., Henriet S., Mungpakdee S., Aury J.M., Da Silva C.,
RA Brinkmann H., Mikhaleva J., Olsen L.C., Jubin C., Canestro C.,
RA Bouquet J.M., Danks G., Poulain J., Campsteijn C., Adamski M., Cross I.,
RA Yadetie F., Muffato M., Louis A., Butcher S., Tsagkogeorga G., Konrad A.,
RA Singh S., Jensen M.F., Cong E.H., Eikeseth-Otteraa H., Noel B.,
RA Anthouard V., Porcel B.M., Kachouri-Lafond R., Nishino A., Ugolini M.,
RA Chourrout P., Nishida H., Aasland R., Huzurbazar S., Westhof E., Delsuc F.,
RA Lehrach H., Reinhardt R., Weissenbach J., Roy S.W., Artiguenave F.,
RA Postlethwait J.H., Manak J.R., Thompson E.M., Jaillon O., Du Pasquier L.,
RA Boudinot P., Liberles D.A., Volff J.N., Philippe H., Lenhard B.,
RA Roest Crollius H., Wincker P., Chourrout D.;
RT "Plasticity of animal genome architecture unmasked by rapid evolution of a
RT pelagic tunicate.";
RL Science 330:1381-1385(2010).
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 -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085}.
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DR EMBL; FN653025; CBY18438.1; -; Genomic_DNA.
DR AlphaFoldDB; E4X569; -.
DR MEROPS; C19.001; -.
DR InParanoid; E4X569; -.
DR Proteomes; UP000001307; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0019538; P:protein metabolic process; IEA:UniProt.
DR CDD; cd14296; UBA1_scUBP14_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; 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; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF664; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 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 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; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001307};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00502}.
FT DOMAIN 205..315
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 359..838
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT DOMAIN 648..688
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 705..750
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT REGION 758..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 761..778
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 838 AA; 93692 MW; AD1BD3C212BE28A3 CRC64;
MVTDLEKHAT TLHIDDADYD AEFTEPQATG TDSSVPTKPS ESELNGLPDE FIIFKDVING
IECPTQNDKI FKEECIVTCD SCFSEMGLYI CLKTFKSFGF KSLSDYTSKT GNKTFLNIQK
SRLTKSPEEE PEAKRLAIGG EDGFKPDILP WKETQTERIY VHPDQYFPVD SIPIEYVKRV
AKTILDSTSA EFKAEVAAWK PDPPKKSIHA DSLVQLDNGV KVLSDPSKWK CCKCDLTENL
WLNLSDGSLL CGRKNWDGSG GNGHALEHFN ETKYPLCVKL GTITSEGGDV FSYAEDDMVT
DPHLAKHLSH WGIDVANSKK TEMSMAEMEL EMNKKVGSEY AAIIESGQEL EPLFGAFHTG
IKNLGNTCYI GSILQSLFSL PYFREKFQQP AEYDANCHEN FWKQFQRVGH ALCSGDYAQP
IIAKDSSGNS VPQGAEQEGI SPGLFKSIVS KGHADFQTNQ QQDAVEFLLH LLDVIKKEAK
KGNREDASSS FAFEIEERVQ FGNSVQYKNN NELMLGLPVD ESDIQNLAEF KEYEQKLAQA
REAKQADPEV VRGVVPFESS FSHLLSAEAI DHFKSPVDGT LLTAHRAARI SKFPKYLLLQ
CRRFTIGANW QPKKLNVSLE MPEELDLEAM RAKGPQPGED VFNTDAPKVD EQKINQLVDM
GYPFNAAMKA LYHTNESLEL AMEWLMSNLD SPDFNEPLKL DKNAKKEEKT FSPEIIAMVT
SMGFTDKQSK KALSATDGNV ERAIDWIFSH LDELNADDST VSPAVPESDS GTNQLAGSDS
SKYRLRAFVS HMGSSTACGH YVAHVKEDLR WILFNDNKVA VSQKPPRDLG YLYVYEQI
//
