ID Q4N1H2_THEPA Unreviewed; 526 AA.
AC Q4N1H2;
DT 02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT 02-AUG-2005, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN OrderedLocusNames=TP04_0767 {ECO:0000313|EMBL:EAN32120.1};
OS Theileria parva (East coast fever infection agent).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Theileriidae; Theileria.
OX NCBI_TaxID=5875 {ECO:0000313|EMBL:EAN32120.1, ECO:0000313|Proteomes:UP000001949};
RN [1] {ECO:0000313|EMBL:EAN32120.1, ECO:0000313|Proteomes:UP000001949}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Muguga {ECO:0000313|EMBL:EAN32120.1,
RC ECO:0000313|Proteomes:UP000001949};
RX PubMed=15994558; DOI=10.1126/science.1110439;
RA Gardner M.J., Bishop R., Shah T., de Villiers E.P., Carlton J.M., Hall N.,
RA Ren Q., Paulsen I.T., Pain A., Berriman M., Wilson R.J.M., Sato S.,
RA Ralph S.A., Mann D.J., Xiong Z., Shallom S.J., Weidman J., Jiang L.,
RA Lynn J., Weaver B., Shoaibi A., Domingo A.R., Wasawo D., Crabtree J.,
RA Wortman J.R., Haas B., Angiuoli S.V., Creasy T.H., Lu C., Suh B.,
RA Silva J.C., Utterback T.R., Feldblyum T.V., Pertea M., Allen J.,
RA Nierman W.C., Taracha E.L.N., Salzberg S.L., White O.R., Fitzhugh H.A.,
RA Morzaria S., Venter J.C., Fraser C.M., Nene V.;
RT "Genome sequence of Theileria parva, a bovine pathogen that transforms
RT lymphocytes.";
RL Science 309:134-137(2005).
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 ECO:0000256|RuleBase:RU366025};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|RuleBase:RU366025}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAN32120.1}.
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DR EMBL; AAGK01000004; EAN32120.1; -; Genomic_DNA.
DR RefSeq; XP_764403.1; XM_759310.1.
DR AlphaFoldDB; Q4N1H2; -.
DR STRING; 5875.Q4N1H2; -.
DR MEROPS; C19.A78; -.
DR EnsemblProtists; EAN32120; EAN32120; TP04_0767.
DR GeneID; 3501386; -.
DR KEGG; tpv:TP04_0767; -.
DR VEuPathDB; PiroplasmaDB:TpMuguga_04g00767; -.
DR eggNOG; KOG1872; Eukaryota.
DR InParanoid; Q4N1H2; -.
DR OMA; FKSDAEY; -.
DR Proteomes; UP000001949; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd16104; Ubl_USP14_like; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR019954; Ubiquitin_CS.
DR InterPro; IPR044635; UBP14-like.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR43982; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR43982:SF1; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 14; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS00299; UBIQUITIN_1; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU366025, ECO:0000313|EMBL:EAN32120.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000001949};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807,
KW ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 8..82
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 114..522
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 239..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..483
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 526 AA; 59796 MW; F2F0381F470AB8EB CRC64;
MENQDNTVSV NVKWMGKQYE GLKMSLDEPL ESFKNQLCSL TGVPPERQKI MFKGIIPNDA
DLSKIKITNG ARLMLIGSAE KPPECIEKVR FFEELSSQEK AKIMNDNIIV KLPPGIMNLG
NTCYFNSVVQ FLFPVTELWN SVSKCLEVNG NSPDVHFAKS LLDMKNQLNH TLERFVPLVQ
IQFLRKINPL FCRKDEKTGM YMQQDAEECL NCILGNLNSL SEDKIAENVF GFSMVSKTKP
VKPEGSDSEP SETDTNPGEN VSSVEHNLVL SCYMGTPLKS VGTLMDGINL SLNEELLKFS
EKDGCDVLHN KVSKLSSLPK YLIVHLVRFE WKQKSQVSHT DAIKAKVCRR VNFERYIDIT
SICSEELQQK LRAAKSHQIK KEDKLKEELN GQEKVENKNE GENLDVEMVN LDGYEISPGE
YATGKYELIS IVTHQGRTAD AGHYICWTKD SREYPTKNPS NSNEKDMDNQ RDGEKESKKK
KQEDRWIKFD DDVVSEQDWG SFDLCGGRSD YHIAVLLLYK SQNTTL
//
