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Database: UniProt
Entry: E9FTW0_DAPPU
LinkDB: E9FTW0_DAPPU
Original site: E9FTW0_DAPPU 
ID   E9FTW0_DAPPU            Unreviewed;       936 AA.
AC   E9FTW0;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE            EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN   ORFNames=DAPPUDRAFT_310510 {ECO:0000313|EMBL:EFX89435.1};
OS   Daphnia pulex (Water flea).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC   Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX   NCBI_TaxID=6669 {ECO:0000313|EMBL:EFX89435.1, ECO:0000313|Proteomes:UP000000305};
RN   [1] {ECO:0000313|EMBL:EFX89435.1, ECO:0000313|Proteomes:UP000000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21292972; DOI=10.1126/science.1197761;
RA   Colbourne J.K., Pfrender M.E., Gilbert D., Thomas W.K., Tucker A.,
RA   Oakley T.H., Tokishita S., Aerts A., Arnold G.J., Basu M.K., Bauer D.J.,
RA   Caceres C.E., Carmel L., Casola C., Choi J.H., Detter J.C., Dong Q.,
RA   Dusheyko S., Eads B.D., Frohlich T., Geiler-Samerotte K.A., Gerlach D.,
RA   Hatcher P., Jogdeo S., Krijgsveld J., Kriventseva E.V., Kultz D.,
RA   Laforsch C., Lindquist E., Lopez J., Manak J.R., Muller J., Pangilinan J.,
RA   Patwardhan R.P., Pitluck S., Pritham E.J., Rechtsteiner A., Rho M.,
RA   Rogozin I.B., Sakarya O., Salamov A., Schaack S., Shapiro H., Shiga Y.,
RA   Skalitzky C., Smith Z., Souvorov A., Sung W., Tang Z., Tsuchiya D., Tu H.,
RA   Vos H., Wang M., Wolf Y.I., Yamagata H., Yamada T., Ye Y., Shaw J.R.,
RA   Andrews J., Crease T.J., Tang H., Lucas S.M., Robertson H.M., Bork P.,
RA   Koonin E.V., Zdobnov E.M., Grigoriev I.V., Lynch M., Boore J.L.;
RT   "The ecoresponsive genome of Daphnia pulex.";
RL   Science 331:555-561(2011).
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|RuleBase:RU366025};
CC   -!- SIMILARITY: Belongs to the peptidase C19 family.
CC       {ECO:0000256|RuleBase:RU366025}.
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DR   EMBL; GL732524; EFX89435.1; -; Genomic_DNA.
DR   AlphaFoldDB; E9FTW0; -.
DR   STRING; 6669.E9FTW0; -.
DR   EnsemblMetazoa; EFX89435; EFX89435; DAPPUDRAFT_310510.
DR   KEGG; dpx:DAPPUDRAFT_310510; -.
DR   eggNOG; KOG1870; Eukaryota.
DR   HOGENOM; CLU_001060_8_1_1; -.
DR   InParanoid; E9FTW0; -.
DR   OMA; RIWPQRV; -.
DR   PhylomeDB; E9FTW0; -.
DR   Proteomes; UP000000305; Unassembled WGS sequence.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd06466; p23_CS_SGT1_like; 1.
DR   CDD; cd02674; Peptidase_C19R; 1.
DR   Gene3D; 2.60.40.790; -; 1.
DR   Gene3D; 6.10.140.2220; -; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR   InterPro; IPR007052; CS_dom.
DR   InterPro; IPR008978; HSP20-like_chaperone.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   InterPro; IPR002893; Znf_MYND.
DR   PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR21646:SF74; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 19; 1.
DR   Pfam; PF04969; CS; 1.
DR   Pfam; PF00443; UCH; 1.
DR   Pfam; PF01753; zf-MYND; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF144232; HIT/MYND zinc finger-like; 1.
DR   SUPFAM; SSF49764; HSP20-like chaperones; 1.
DR   PROSITE; PS51203; CS; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
DR   PROSITE; PS50865; ZF_MYND_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU366025};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protease {ECO:0000256|RuleBase:RU366025};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000305};
KW   Thiol protease {ECO:0000256|RuleBase:RU366025};
KW   Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00134}.
FT   DOMAIN          71..173
FT                   /note="CS"
FT                   /evidence="ECO:0000259|PROSITE:PS51203"
FT   DOMAIN          237..914
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   DOMAIN          545..584
FT                   /note="MYND-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50865"
FT   REGION          1..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          195..222
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          630..663
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          720..754
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          916..936
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..30
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..52
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        723..754
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   936 AA;  105003 MW;  CCD6FDDF62F1A33B CRC64;
     MVTCSLKGGA GERRPNNSVP SSSGVLDASN HPTGQAEVMC RSDDEEKHNG TNSNSLDDSL
     PMELCPTIHP VHNLKLDHHD HPETVSVTLY VKNIAKESLR VDFGETCISV TFRTSDPGFL
     KQYPAFGAED DLMQWQIETR GTIVPEKCTF RLKPTNLELK LIKAVTSKWE SLEATVDSSS
     AGPSIQKETW ISLAPPKAAK PSPASRKKFE EDASQETNSI SLSPSADSVM SFKAGYTGLG
     NLGNTCYMNA VLQALANTTP LKNYFLDKKF QADINRDNPL GFGGSLAIAF AIILRQLWSG
     QRDSIEPSHL KSLLANRASQ FSGYAQHDAQ EFMAFLLDGL HEDLNRVKTK PLTTPVESNG
     RPDHIVADEA WQVYKMRNDS VIDDLFQGQF KSTLVCPACQ NISVTFDPFL YLALPLPPSK
     SCFTVTVYFD GVDESVELTG TKRGAVKVSL WLDPSQRVQQ LKEELKRVCA GRFRHPDSEI
     ELVQVRDGLI RRWLVDAAPL SSLQNTNHSD ALLLAFETAP SDNGSLVHIA VIQRVLMPLD
     EHTHCTACKK ESDVLKRCMK CYSVAYCDKN CQRTHWTAVH RTMCRPKPDI IAQPFVVSLP
     PSSLTYQKLY RSMLYYSRFS VEVDCPPSAN NSCNQDMDSS SSSSSSSSSP QEEGQVDGLQ
     QSKQEQPKEY PLFFIKPIDS QGQGIEKKKR LEDLGDKPLD FDADESPIFL SLDWRNDERS
     PNHCSVTVKS PTDYEDLSQE NSDPSADGDT SPNQRRLTLH HCLQQFMQSE VLSKEEAWYC
     PKCKEHREAT KQMSVWRLPE ILTIQLKRFS FRNLMWRDKI DQKVHFPVEQ LDLSPYLSSI
     TEHGAVYDLY AVVNHYGGIL YGHYTSFARC PAATSDKSQK DVVGWRCMDD RQVRDICEES
     VVTSAAYLLL YQRRRRSPGP SASPVQLNYS DPEEID
//
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