ID A0A1A8VTG2_PLAMA Unreviewed; 853 AA.
AC A0A1A8VTG2;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 08-NOV-2023, entry version 36.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|PIRNR:PIRNR016308};
DE EC=3.4.19.12 {ECO:0000256|PIRNR:PIRNR016308};
GN ORFNames=PMALA_005060 {ECO:0000313|EMBL:SBS82968.1};
OS Plasmodium malariae.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=5858 {ECO:0000313|EMBL:SBS82968.1, ECO:0000313|Proteomes:UP000078597};
RN [1] {ECO:0000313|Proteomes:UP000078597}
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|PIRNR:PIRNR016308};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085, ECO:0000256|PIRNR:PIRNR016308}.
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DR EMBL; FLQW01000273; SBS82968.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1A8VTG2; -.
DR VEuPathDB; PlasmoDB:PmUG01_05029800; -.
DR OMA; KVKYKTR; -.
DR Proteomes; UP000078597; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd14298; UBA2_scUBP14_like; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 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; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR033864; UBA2_scUBP14-like.
DR InterPro; IPR015368; UBA_C_fun.
DR InterPro; IPR016652; Ubiquitinyl_hydrolase.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001607; Znf_UBP.
DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF664; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR Pfam; PF09288; UBA_3; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR PIRSF; PIRSF016308; 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; SSF46934; UBA-like; 1.
DR PROSITE; PS50030; UBA; 2.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PIRNR:PIRNR016308, ECO:0000313|EMBL:SBS82968.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR016308}; Protease {ECO:0000256|PIRNR:PIRNR016308};
KW Thiol protease {ECO:0000256|PIRNR:PIRNR016308};
KW Ubl conjugation pathway {ECO:0000256|PIRNR:PIRNR016308};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR016308};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00502}.
FT DOMAIN 137..254
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 294..853
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT DOMAIN 676..717
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 732..772
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT REGION 448..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 630..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..671
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 303
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-1"
FT ACT_SITE 814
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-1"
FT BINDING 160
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
SQ SEQUENCE 853 AA; 98676 MW; 8D10197E7F6DAA86 CRC64;
MFCRGHKDIF DEGVFIDLLS FESFSLKCLK YNYNRLNPAS VSKKHRFYLN IKKKKKLLEN
IEEKSDITNL NLNAKGGFNE KKVYEYEWNY SIYDFETGIY IKLEQLDENT RKICNSIINH
KNELKKESIN KWVNEIKESK YAKDLIQLPN IRIKNEHIAC AVCKSTKNIW LNLSDGYIGC
GRKIYNYGGG CLNNEEGASL KHYYESGKKY PLVVKLGTIT KEGEADVFSY ADDENDSVID
PYIAVHLKNL GINIMNLEKT EITTLEKEIQ ENQNINFSSI LDKDIQTVCE QGKVGFINLG
NTCYMNSALQ VLLSIKDISY RYYNNMYDFL LSLDFKKKTH EDMFLQYSKL CYMIYQPDDY
IKKKKNYIKK FKEECVDRNI QVNYDSDIDD ENCVSINPSM FRNCLNQKSN SFSNNNQQDI
YEYLSFLINE LIDNENNIFD RTLKSNNNKR KLENGDNAEY GQYTQEGEAN KSEKMMESTA
TSTIITGSPK AEREKSIFNY FTFEIEQTIV SNEENKSVSS FQNIILSLDI PLDSIILKKN
EQEELTNVKI SLLDCLKNYI KKDHIDEYYC EKEKTKVSAH RVMKFKSFPP YLFIHLKRFY
ADENWCAKKI NIPVETDEYI NLEFMRSENG AHSGNDGDHN NDNNNVNNGV NNDSRSRGIP
NSANNNNRNS ESNILEQYKE LVESLLDFGF EKDKVIEAIK KVKVKNVNNC ISYIYGEDSV
ELDLEANDNK TEIYTNNLDS IISMGIKKEV AMASLLINKN DLQKSIDYIF SNMDLLTDSK
CDLIISSNKC DDGLANYELV ASIVHIGNNA NSGHYICYIK DNSQWYVCND NKIGLCGANL
GKDVAYIHLY KRV
//
