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Database: UniProt
Entry: U6H3K2_9EIME
LinkDB: U6H3K2_9EIME
Original site: U6H3K2_9EIME 
ID   U6H3K2_9EIME            Unreviewed;      1051 AA.
AC   U6H3K2;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   31-JUL-2019, entry version 33.
DE   RecName: Full=Ubiquitinyl hydrolase 1 {ECO:0000256|SAAS:SAAS01044305};
DE            EC=3.4.19.12 {ECO:0000256|SAAS:SAAS01044305};
GN   ORFNames=EPH_0067350 {ECO:0000313|EMBL:CDI86043.1};
OS   Eimeria praecox.
OC   Eukaryota; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX   NCBI_TaxID=51316 {ECO:0000313|EMBL:CDI86043.1};
RN   [1] {ECO:0000313|EMBL:CDI86043.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Houghton {ECO:0000313|EMBL:CDI86043.1};
RA   Reid A.J., Blake D., Billington K., Browne H., Dunn M., Hung S.,
RA   Kawahara F., Miranda-Saavedra D., Mourier T., Nagra H., Otto T.D.,
RA   Rawlings N., Sanchez A., Sanders M., Subramaniam C., Tay Y., Dear P.,
RA   Doerig C., Gruber A., Parkinson J., Shirley M., Wan K.L., Berriman M.,
RA   Tomley F., Pain A.;
RT   "Genomic analysis of the causative agents of coccidiosis in
RT   chickens.";
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CDI86043.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Houghton {ECO:0000313|EMBL:CDI86043.1};
RA   Aslett M.;
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Thiol-dependent hydrolysis of ester, thioester, amide,
CC         peptide and isopeptide bonds formed by the C-terminal Gly of
CC         ubiquitin (a 76-residue protein attached to proteins as an
CC         intracellular targeting signal).; EC=3.4.19.12;
CC         Evidence={ECO:0000256|SAAS:SAAS01117307};
CC   -!- SIMILARITY: Belongs to the peptidase C19 family.
CC       {ECO:0000256|SAAS:SAAS01045498}.
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DR   EMBL; HG694678; CDI86043.1; -; Genomic_DNA.
DR   EnsemblProtists; CDI86043; CDI86043; EPH_0067350.
DR   OrthoDB; 556111at2759; -.
DR   GO; GO:0036459; F:thiol-dependent ubiquitinyl hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0016579; P:protein deubiquitination; IEA:InterPro.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   Gene3D; 3.30.40.10; -; 1.
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; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR001607; Znf_UBP.
DR   Pfam; PF00627; UBA; 1.
DR   Pfam; PF00443; UCH; 1.
DR   Pfam; PF02148; zf-UBP; 1.
DR   SMART; SM00165; UBA; 2.
DR   SMART; SM00290; ZnF_UBP; 1.
DR   SUPFAM; SSF46934; SSF46934; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   PROSITE; PS50030; UBA; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
DR   PROSITE; PS50271; ZF_UBP; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000256|SAAS:SAAS01044238,
KW   ECO:0000313|EMBL:CDI86043.1};
KW   Metal-binding {ECO:0000256|SAAS:SAAS01044152};
KW   Protease {ECO:0000256|SAAS:SAAS01044292};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Thiol protease {ECO:0000256|SAAS:SAAS01044269};
KW   Ubl conjugation pathway {ECO:0000256|SAAS:SAAS01044331};
KW   Zinc {ECO:0000256|SAAS:SAAS01044373};
KW   Zinc-finger {ECO:0000256|SAAS:SAAS01044352}.
FT   SIGNAL        1     20       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        21   1051       Ubiquitinyl hydrolase 1.
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5004670493.
FT   DOMAIN      239    320       UBP-type. {ECO:0000259|PROSITE:PS50271}.
FT   DOMAIN      378   1036       USP. {ECO:0000259|PROSITE:PS50235}.
FT   DOMAIN      785    826       UBA. {ECO:0000259|PROSITE:PS50030}.
FT   ZN_FING     239    320       UBP-type. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00502}.
FT   REGION       51     70       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      617    670       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      752    784       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COILED      136    156       {ECO:0000256|SAM:Coils}.
FT   COILED      930    958       {ECO:0000256|SAM:Coils}.
FT   COMPBIAS    618    639       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    762    781       Polar. {ECO:0000256|SAM:MobiDB-lite}.
SQ   SEQUENCE   1051 AA;  112079 MW;  63C1130CCEBBE1C1 CRC64;
     MVHGPFGLFI NLKTFLSVSL ESLPVDSALS GSRVYVHLSS NVHELNATTA NNKRKQAQDE
     ATADDSAAGR ANKPTKMAIA VEGGFSADGD MIDPSGNFAA VEPTISYRLC VYTAASTAAT
     AAVARGLADI YRSSSIKQQQ QKRAEVDEEG QEQQQQWRSD MTLLQQYQEQ LLQQLAFLPL
     DDPDVPAAVA AAAKHLAETK HTVADSAPSA AWVEEILPSK YAEDLPVVEN PPKISPSNWK
     CADCGASTNL WLNLSDGFIG CGRKLYGAGG GCADGREGAA IRHYKETGSI YPLIVKLGTI
     SADSADVFSY APDEDSTVID PKLPEHLARF GIETQQLRKT ERSTNELAID LNCKYDWASL
     TASASEQQQQ QQKGAGFVGL RNLGNTCYVN AVLQALFSVP RFCEKFLRMY EPLICCQGLP
     SAAAAAAGGG PAKCLSLQLG ALSVALQTRR VCMQKALGLV LLQRVLQQQD IQIEEKQLIS
     DLPYLAHDAV SPLSLRAIIG SLHAEFATSR QQDAEEFLSL LLSWIGDREA GDRRQLQQLR
     QQLQSGESSA VAAAAAALGV TDDSLQATEE VLREGAVDAL FSFGVEQRLE CLQSRQVRYT
     YSRQQVLALP IPLHVQQEEE EQQQEQQRQQ KRRKGAEGTP TESDTGAETG GDTTETHCET
     EEPVAPAAPS VPLSSCISAA AAAAAVNDYL SPATGAKGDA EKTLRLTNYP EYLLVFLKRF
     YISDRWIPKK LKCSVEIPEE VSFEELRASG LQPEERELPD EPPQPQQQQQ QGNNSGTAAA
     AAQAAANDEV VATLESMGFS SNAAKRALRA TGGAAAESCV EWLMGHLDDP DLNDPIPAPA
     AASASGAAEA AGGAAAADAK DQPDAEAVAN LMALGFDERS VRAAFFATRG QTSSGGIATE
     GGPFDAGRAA DWLLSQGSGL AAAVEEALAA AAAAAAAAAA AEEAREAEAQ EKQALEAAAA
     GLSPLERCRL GLEDGCGKYR LFAFVSHLGS SVSGGHYICH VRSKDGSGWL QYNDEKVTKL
     QSCDSRQAYL LLFKRVETES KEPPAAMQKD A
//
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