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Database: UniProt
Entry: Q4RYN3_TETNG
LinkDB: Q4RYN3_TETNG
Original site: Q4RYN3_TETNG 
ID   Q4RYN3_TETNG            Unreviewed;      1669 AA.
AC   Q4RYN3;
DT   19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2005, sequence version 1.
DT   27-MAR-2024, entry version 106.
DE   RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
DE   Flags: Fragment;
GN   ORFNames=GSTENG00026865001 {ECO:0000313|EMBL:CAG06499.1};
OS   Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS   nigroviridis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX   NCBI_TaxID=99883 {ECO:0000313|EMBL:CAG06499.1};
RN   [1] {ECO:0000313|EMBL:CAG06499.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15496914; DOI=10.1038/nature03025;
RA   Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA   Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA   Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA   Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA   Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA   Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA   Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA   McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA   Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA   Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA   Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT   "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT   early vertebrate proto-karyotype.";
RL   Nature 431:946-957(2004).
RN   [2] {ECO:0000313|EMBL:CAG06499.1}
RP   NUCLEOTIDE SEQUENCE.
RG   Genoscope;
RG   Whitehead Institute Centre for Genome Research;
RL   Submitted (FEB-2004) 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};
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DR   EMBL; CAAE01014974; CAG06499.1; -; Genomic_DNA.
DR   MEROPS; C19.009; -.
DR   KEGG; tng:GSTEN00026865G001; -.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   CDD; cd00051; EFh; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR   Gene3D; 3.30.2230.10; DUSP-like; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   InterPro; IPR035927; DUSP-like_sf.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR006615; Pept_C19_DUSP.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR028135; Ub_USP-typ.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR21646:SF76; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 32; 1.
DR   Pfam; PF06337; DUSP; 1.
DR   Pfam; PF13202; EF-hand_5; 2.
DR   Pfam; PF14836; Ubiquitin_3; 1.
DR   Pfam; PF00443; UCH; 1.
DR   PRINTS; PR00450; RECOVERIN.
DR   SMART; SM00695; DUSP; 1.
DR   SMART; SM00054; EFh; 2.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF143791; DUSP-like; 1.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   PROSITE; PS51283; DUSP; 1.
DR   PROSITE; PS00018; EF_HAND_1; 2.
DR   PROSITE; PS50222; EF_HAND_2; 2.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          230..265
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          266..301
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          371..601
FT                   /note="DUSP"
FT                   /evidence="ECO:0000259|PROSITE:PS51283"
FT   DOMAIN          766..1632
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          438..495
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1428..1535
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        453..495
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1428..1464
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:CAG06499.1"
SQ   SEQUENCE   1669 AA;  186335 MW;  14E93DA8DA7CF25F CRC64;
     NEGSMGAKES RIGFLSYDEA VKRVTDVELK RLKDAFKRTS GLTCYMTQQC FFREVLGDGV
     PPKVAEVIYT SFGGSSKGLH FNNLIVGLVL LTRGRDEEKS KCTLFASDLG GYAAREDIEA
     VLRILDGETP ASLQKCFLES DKVSYERFRA WLFLNKDAFT LSRWLLSGGV CVTLTDDSDT
     PTFYQTLAGV THLEESDIID LEKRYWLLKA QSRTGRFDLE TFIPLVSPPI HASLSEGLFN
     AFDENRDNHI DFKEISCGLS ACCRGPIAER QKFCFKVFDV DHDGVLSRDE LHEMVVALLE
     VWKDNRTDTL PELTSTVSDI VEGILKMHDT TKLGHLTLED YQIWSVSSAL ANEFLNLLFQ
     VCHIVLGLRP GTPEEEGQII RGWLERESRH GLQQGQNWFL ISMLWWQQWK DYVKYEHKGI
     VSEQPTLLSA LRNSVSASTV EPMPPDRLGG LGTFSSVSPT EERSPDCVSS ASEATEAGQH
     PGLAQNASGV SALSPQVAPS STESCFARQH NVSENNNQCF SGANGHLPSQ LAAQRPGAID
     NQSLVNTDPM KAAPTLTLEG GRLKRSLQLV PGRDFETMPE PVWRALYHWY GANLSLPRPV
     ILDSKTGQAE LELFPRYLLF LRQQPATRSP QSNIWVNMGM TTMRMFPPYM IPPRGSVPSP
     NAPLKRVLAY TGCFSRVDTI KDIHLYLSQR LRIKEEDMRL WLFMSENYLT LLDDEDHTLE
     NLKIQDEQQL VIEVRNKDMS WPEEMSFIAN SSKMDRHKVP TEKGATGLSN LGNTCFMNSS
     IQCVSNTKPL TDYFLSGRHL YELNRTNPIG MRGHMAKCYG DLVMELWSGT QKSVAPLKLR
     WTIAKYAPRF NGFQQQDSQE LLAFLLDGLH EDLNRVHEKP YVELKDSNGR PDWEVASEAW
     ENHLRRNRSI VVDLFHGQLK SQVKCKTCGH ISARFDPFNF LSLPLPMDSY MHLEITVIKL
     EGSTPVRYGL RLNMDEKYMG LKKQLSELCN LKPEQILLTE VHTSNIKNFP LDNQKVRLSV
     NGFLCAFEIP VPGSPTSLSS PTLTGAADRP SLFLKFTSEM LLKMDSVKLA HLLSLDLTPI
     ANGSAGGDNL TDNPALIPNG GPNTVVPCSP ETPVANGVAN GHATPVQESP FIGYIIAMHR
     KMMRTELYFL SSQKNRPSLF GMPLIVPCTV HTTKKDLYDA VWIQVSRLAS PLPPQEASNH
     AQDCDDSMGY QYPFTLRVVG KDGNTCAWCP WYRFCRGCVI ECTDDRASLG NAYIAVDWDP
     TALHLRYQTS QERIVEEHCS VEQSRRAQAE PISLDSCLKA FTSEEELGED ELYYCSKCKT
     HRLATKKLDL WRLPPILIVH LKRFQLVNGR WIKSQKIVKF PRENFDPSAF LAPRDLGQHC
     LHSRSQSEDL LRVGEDNLSS VSAPAGLYNL PKVSPVICVT QSQSQRGSGL NLVVSPTASP
     ATSRKSAPSL SRTSSPSGSP KSSSGGRRAA RLRLAKRSGK HWLSNSKENL DAAANPEADT
     HAEAEAEAEA EAEAEAGAPL APGETTESPP SSHCDVVLLN GDSNGLSLDL STDSSLDPDA
     SLLQHRGNTC LDAIYNLYAI SCHSGIMGGG HYVTYAKNPK KKWYCYNDSS CKEVQSEEID
     ADSAYILFYE QQGVEYSHFL PQIDGKKMAD TSSMDEDFES DYKKYCVLQ
//
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