ID U6LTY6_9EIME Unreviewed; 1285 AA.
AC U6LTY6;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Ubiquitin carboxyl-terminal hydrolase, putative {ECO:0000313|EMBL:CDJ52738.1};
GN ORFNames=EBH_0004820 {ECO:0000313|EMBL:CDJ52738.1};
OS Eimeria brunetti.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX NCBI_TaxID=51314 {ECO:0000313|EMBL:CDJ52738.1};
RN [1] {ECO:0000313|EMBL:CDJ52738.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ52738.1};
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 chickens.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDJ52738.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ52738.1};
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, 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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the SRP14 family.
CC {ECO:0000256|ARBA:ARBA00010349}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085}.
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DR EMBL; HG713182; CDJ52738.1; -; Genomic_DNA.
DR EnsemblProtists; CDJ52738; CDJ52738; EBH_0004820.
DR VEuPathDB; ToxoDB:EBH_0004820; -.
DR OrthoDB; 166948at2759; -.
DR GO; GO:0005786; C:signal recognition particle, endoplasmic reticulum targeting; IEA:InterPro.
DR GO; GO:0008312; F:7S RNA binding; IEA:InterPro.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0030942; F:endoplasmic reticulum signal peptide binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0043170; P:macromolecule metabolic process; IEA:UniProt.
DR GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:InterPro.
DR CDD; cd02257; Peptidase_C19; 1.
DR CDD; cd14296; UBA1_scUBP14_like; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 2.
DR Gene3D; 3.30.720.10; Signal recognition particle alu RNA binding heterodimer, srp9/1; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR003210; Signal_recog_particle_SRP14.
DR InterPro; IPR009018; Signal_recog_particle_SRP9/14.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001607; Znf_UBP.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF10; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 14; 1.
DR Pfam; PF02290; SRP14; 1.
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; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF54762; Signal recognition particle alu RNA binding heterodimer, SRP9/14; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000313|EMBL:CDJ52738.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00502}.
FT DOMAIN 458..575
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 619..1270
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT DOMAIN 1020..1061
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT REGION 40..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 104..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 856..908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 993..1020
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1062..1097
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..394
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 863..878
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1285 AA; 137641 MW; 50CAECC6577FDE68 CRC64;
MGLLGEADFL EALRRLYEGS RNKNSGSVWI TFKRTFPEVG GSRGAKRRRK LQGCEEKPDA
TPVCLVRATD GKKKISIQVE GDRAAGFSKQ LLGVSRLYTD QVKRTTPEAA KEKQEKQKQL
QQQKQKQPQQ PKKQPQQAQK TKKNKKNEKS NSSFKREING AAAVPAAVNG PGCRGISSRS
SNSAAWPHQQ QQQQQRNMEV KLAQGEPRAA ALAVLQQAAA ATAAAPTPGK INKQCSDYSL
DMVHGPFGLF INLKTYLSVS LESLPADAAL SGSRVYVHLS SNVHEQNAKT ADSKRKQNQE
ASSSEAGAAG AAGRPTKLAI AVEGGFSADG DMIDPSGNFA AVEPTISYRL CVYTPASAAA
AAAVAGGLVD MYRRSSSKQQ QQKRAEVDED GQEQQQQWRS DLMLLQQYQE QLLQQLSFLS
IDDPDLPAAI AAAAKHVAET KHSVANTAPS AAWVEEILPS KYAEDLPVVE NPPKISPSNW
KCADCGASTN LWLNLSDGFI GCGRKLYGAG GGCADGREGA AIRHYKETGS KYPLIVKLGT
ISADSADVFS YAPDEDSTVI DPKLPEHLAR FGIETQQLRK TERSTNELAI DLNCKYDWAS
LTASATEQQQ NPQRGAGFVG LRNLGNTCYV NAVLQALFSV PRFCDKFLCM YEPLICCQGL
PSAAAAAGGP ATSLSLQLGA LAVALQTRRV CMQKGLGMML LQKALEQQDI KVEEKQLISD
LPYLAHDAVS PLSLRAIIGS LHAEFATSRQ QDAEEFLSLL LSWISDREGG DRRQLQQLRQ
LLQSGENPSL GAAAVELGVT DETLKAAEAA IGNGTVDSLF SFGVEQRLEC LQSRQVRYTY
SRQQVLALPI PLHVQQEEEE QQQQQQRQQK RRKGAEGTPA ESDTGAETGG DTTETRGESE
EPGIAAPSVP LSSCISAAAA AAAVNDYLSP ATGAKGDAEK TLRLTNYPEY LLVFLKRFYI
SDRWIPKKLK CSVEIPEEVS FEELRAFGLQ PEEHELPDEP PQQPLQQQPS NSSGAPAADT
ANDEVVATLE SMGFSSNAAK RAVRVTGGAS AESCVEWLMS HLDDPDINDP PPAAAAPASR
TADAAGPTGA AGAKDEPDAE AVANLMALGF DERSVRAAFF ATRGQPGSGG IPTTGGPFDA
GRAADWLLTQ GSGLAAAVDK ALADAAAAAA AAAAAAETEK ADAEEKQARE AAAAGLPPLD
RCRLGLKDGC GRYRLYAFVT HLGSSVSGGH YICHVRNKDG SGWLQYNDEK VTKLQSCDSR
QAYLLLFKRI DSEGKAPAAD TQKCA
//
