ID A0A1A8VSK5_9APIC Unreviewed; 1578 AA.
AC A0A1A8VSK5;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=POVCU2_0012150 {ECO:0000313|EMBL:SBS81802.1};
OS Plasmodium ovale curtisi.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=864141 {ECO:0000313|EMBL:SBS81802.1, ECO:0000313|Proteomes:UP000078560};
RN [1] {ECO:0000313|Proteomes:UP000078560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Naeem Raeece;
RL Submitted (MAY-2016) 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 -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085}.
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DR EMBL; FLQU01000186; SBS81802.1; -; Genomic_DNA.
DR Proteomes; UP000078560; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 3.30.2230.10; DUSP-like; 1.
DR InterPro; IPR035927; DUSP-like_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR006615; Pept_C19_DUSP.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF24; USP DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF06337; DUSP; 1.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM00695; DUSP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF143791; DUSP-like; 1.
DR PROSITE; PS51283; DUSP; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:SBS81802.1};
KW Protease {ECO:0000313|EMBL:SBS81802.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000078560}.
FT DOMAIN 421..533
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 1226..1578
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 163..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 748..938
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 964..1191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..206
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..387
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..714
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..834
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 835..868
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 869..885
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 904..938
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 964..991
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 992..1025
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1027..1058
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1069..1086
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1107..1180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1578 AA; 179792 MW; 9FC150D8AEBE2A06 CRC64;
MIKDNKLTID NINYTVTSPV NVDGKNSKIC ELKDYTKKRT SEYMNNDVSS ENLSYGINNF
INNKNSNSGL ETNELLTNNV PLIKACVNCT EKIGETYSEI CLQESRSSTS FHADISNDVM
QYVNEIGKDS SSASNNEGCA LHKNDKVEKV QYLKHCQGEH TLMEESNKTK SDTATKISDI
GNRDIGSSEE KDVNVSEGNK NEERNKQIGG TILRKESTIF EKEKVRNSIQ GDVVFTPKVQ
EPPDTKIDTI LKPPDVKIED QPSNIEITEK EENSLVNFEK KDIRQFFKNY SNSAIINVLH
STMRKEDYAK FFSTNEDTEK SGNSEENEEN EENNSDGYYG PDGGYYNLEG GGCYPDERKG
RSRSIEPGGG EDQIKGEHSN RSDRGNKSLI QWKKEKEKIK KLLKQNIGQN ELISINKNLI
FLKKMQQYFY RKYINIKFPN DENNYYYFIH VKWFNSLKKF LFTDSGSYPG YITNYKLYKS
NVSNPMHSVY MINKENLKEN LKEGKDYICT NKYMWRFLHF LFKGGPCIKR NCNNIYDQFV
PISNNDMMNK NIIYLIEPKY IDNLFSLFNY SNEVNNDISI NCSEKNVNGL LATPSNSFTK
TNMPTDNGNN NKKKKHFAHS YYDLLQFYKL KEKENDNSFY IEYDPLNTKI MKRIIELKNK
NFDHSTYSFK MEKKETSSED SSVHNRASTH NDKKKNEERK KEELERKEKK SVNNFDIASD
GNRHDALYVN NNTPSDSQQF IAQDILTNQC KPSDGSPSRS MNSLGKREAS TGGKGSSNNR
SGNNNNNNNN NNNNTNTNTN TNNNNNNNNN NNNNNNNNNN NNNNNNNNDN SGGKSNKSDD
SRGEKGEEKT EGSDGNSEES KNQDNTRRGS NTKEGNSSGD FKRESFVNSG VSYFGPKAKV
GSPNILCSSY STKKGNASKM NSNKSSNPND NATSAGKNYL AVPQKKNSIG CHSSNGNDVY
KSCEEYNIDN GGTSSNGYLT TTETESKGTT ENTAKSSHDE KYKDKTFYDI KEKEEVMEKS
KKGIKGSTGR RNSSSSSGSS GSSGKSDGSG GSDGGGTQQS RKAEKKRKHI SSSRNDEGKE
ELNKNMNSMK NRMNEEGVRK DVSKGIGSTM SVGNLISMGK SNCSSNRRNP NVSSSGSSFQ
SSFRSSDSNG NSNGDSNSNS DSNSDSDSSN FSIRNQTISN HNHFRVKENR KGMKHMKNTM
AHNSSKRESE AFSNSPNAIT TKEQPAGIVN YSMTCYINVV MQCLSVFFKL IYTLHNYATL
KYKNFNFSSD DTDHMNTSFM NKNFFTNSIP FNIFGNNNKK KDECLLVTFS YKLFQLNKMH
NKRKVLCINK LLNLLNDKYS YLFEYHEQQD CHEFLLLVFD FIHNMMKVID ENVDKNNKID
YYLKKEQSII SDLFLGLIEE KITCSQCEYI NYIYQPVYNL SVNVFKKNPD NNLNDNLIEY
FKKEEVNSTC EKCKCKKMYK YSYVYKQPNI LIIHLIRLLE DGSKIDKPIK FDMMDFSIQN
VLKKTNDEYI EIPKKYNLCG VIVHRGLNSN YGHYICYTKR KHSNGVTMWY KFDDSLVTVV
DPSEVESSKA YCLFYQSQ
//
