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Database: UniProt
Entry: C3XXU3_BRAFL
LinkDB: C3XXU3_BRAFL
Original site: C3XXU3_BRAFL 
ID   C3XXU3_BRAFL            Unreviewed;      1152 AA.
AC   C3XXU3;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN   ORFNames=BRAFLDRAFT_63818 {ECO:0000313|EMBL:EEN67553.1};
OS   Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC   Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC   Branchiostomatidae; Branchiostoma.
OX   NCBI_TaxID=7739;
RN   [1] {ECO:0000313|EMBL:EEN67553.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN67553.1};
RC   TISSUE=Testes {ECO:0000313|EMBL:EEN67553.1};
RX   PubMed=18563158; DOI=10.1038/nature06967;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA   Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA   Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA   Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA   Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA   Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA   Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA   Satoh N., Rokhsar D.S.;
RT   "The amphioxus genome and the evolution of the chordate karyotype.";
RL   Nature 453:1064-1071(2008).
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};
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DR   EMBL; GG666471; EEN67553.1; -; Genomic_DNA.
DR   RefSeq; XP_002611543.1; XM_002611497.1.
DR   AlphaFoldDB; C3XXU3; -.
DR   STRING; 7739.C3XXU3; -.
DR   MEROPS; C85.002; -.
DR   eggNOG; KOG2605; Eukaryota.
DR   InParanoid; C3XXU3; -.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
DR   GO; GO:0004577; F:N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019538; P:protein metabolic process; IEA:UniProt.
DR   CDD; cd22794; OTU_OTUD4; 1.
DR   Gene3D; 3.90.70.80; -; 1.
DR   InterPro; IPR003323; OTU_dom.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   PANTHER; PTHR12419; OTU DOMAIN CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR12419:SF117; PROTEIN OVARIAN TUMOR LOCUS-RELATED; 1.
DR   Pfam; PF02338; OTU; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS50802; OTU; 1.
PE   4: Predicted;
FT   DOMAIN          28..149
FT                   /note="OTU"
FT                   /evidence="ECO:0000259|PROSITE:PS50802"
FT   REGION          188..253
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          327..458
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          495..527
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          543..636
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          730..992
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1096..1132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        210..239
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        334..392
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        590..621
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        730..791
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        804..909
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1107..1122
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1152 AA;  127752 MW;  DB26FBBF0C73BA18 CRC64;
     MSVVRGRKSP KAAESLQAMD DYLSSLGLVR KPIAKDGSCL FRAVAEQVFH CQARHLEVRE
     ACVRYMDRNR DIFEAFVPGP FDHHLWTLQN PKEWAGQVEI SALSLMYKCD FIIYQDVGRP
     PARVTENGFA DKVVLCFSHG NHYDSVYPKQ FQIDAAMCQS LVYELLYKDV FKMDHDIAVV
     KDMLGNKQQK IRKDSTSESE SSPSKNCGSD KPDSELEGST ELDVSTESDK SRDNTERPNE
     KATQANGAVE YSKKDGRRFP LPFKVAKALD PEFYRNVEYD TWMDSKKEQQ RQDMHLATMM
     QYAPGDKCQE NGIPPFMVQR VQPSLPPRLQ HEGQYSPKYH HHHGREYQGR DYQGRDYQGR
     DYQSREYQGR EYQGRDRDYQ PRDRDREFQR PPHGQRYNGQ ARNQPPRFMR QDQMDGRGPG
     PRPGSRYQYS HGRGRGRGRN TPTPPPGPPQ GEMDEKQAIE ESIVLYELQQ RDPDAFPALP
     TSNGQVQHVQ SNTVWGRGRG RGMGRRTPTP PPPSTTPSDG GHSMTMEEGS LCSSMQELNM
     NERASPDGER ICSPVSHQME VPPMKRVMTP TKEFVPRSSR TPSPYQNPTP PLQSQSANAE
     ISSSNSGSNQ QMSTDSTSSP ASTPNTPPPQ TVAPNGYVPY MQPMHVPFYP IMIQATDNLT
     GPVNLNFGPS RDPYGNDLPH SDVSTLRFFY NLGIEYYRCC MSMMAIQHQQ QEAAMANAYF
     YNQAQGQVQP QYQPASSTDG QNSSGQQAQE GEDPQQEGSD QLPPNGQSQD KPLPQGAHVY
     TSASSFNPGN PPVDYHTGAG SDYPPGKTNK SCSDDNSNDS VGNNKDVSVS RSNSMTSVQS
     SGDSASMNVQ YGSDSVCGSS VSYVQPSPNA LQQTSSSTTV GSEDSSPDYT DSGVASEGSG
     SQSSIPRPTS LGPGLPKRHY MEHRGSPKLI PGRWSTPERS GSSDSLNQEA FPMGRPPYGP
     KRGPRDRQPG FYRPSYFPNR PYMSQQPPRR QYEGQPLYHP QLYSNPVRYS NPTHHMSQPQ
     QYYMNQYTGP SRMALHGNMG GQPAGMYNRA AGMYSHPSQQ LNVPPGVTSV PYPPMSPSLH
     VPAAALHAPN IASSPSATGQ YYPAQAPGPV DPNPPGSQGP TPIPVPSSAA NATHRSQAIY
     RILPVGKKLA QN
//
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