ID W7A6V7_9APIC Unreviewed; 890 AA.
AC W7A6V7;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=C922_02552 {ECO:0000313|EMBL:EUD66968.1};
OS Plasmodium inui San Antonio 1.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=1237626 {ECO:0000313|EMBL:EUD66968.1, ECO:0000313|Proteomes:UP000030640};
RN [1] {ECO:0000313|EMBL:EUD66968.1, ECO:0000313|Proteomes:UP000030640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=San Antonio 1 {ECO:0000313|EMBL:EUD66968.1,
RC ECO:0000313|Proteomes:UP000030640};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Cheeseman I., Volkman S., Adams J., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Plasmodium inui San Antonio 1.";
RL Submitted (FEB-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 -!- SIMILARITY: Belongs to the peptidase C19 family. UBP8 subfamily.
CC {ECO:0000256|ARBA:ARBA00038490}.
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DR EMBL; KI965468; EUD66968.1; -; Genomic_DNA.
DR RefSeq; XP_008816373.1; XM_008818151.1.
DR AlphaFoldDB; W7A6V7; -.
DR EnsemblProtists; EUD66968; EUD66968; C922_02552.
DR GeneID; 20037826; -.
DR VEuPathDB; PlasmoDB:C922_02552; -.
DR OrthoDB; 166948at2759; -.
DR Proteomes; UP000030640; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0019538; P:protein metabolic process; IEA:UniProt.
DR CDD; cd14298; UBA2_scUBP14_like; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
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; IPR016652; Ubiquitinyl_hydrolase.
DR InterPro; IPR041432; UBP13_Znf-UBP_var.
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:SF33; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 22; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR Pfam; PF17807; zf-UBP_var; 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; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR016308-3};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR016308-3};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00502}.
FT DOMAIN 173..290
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 330..890
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT DOMAIN 769..809
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT REGION 484..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 680..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..526
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..694
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 339
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-1"
FT ACT_SITE 851
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-1"
FT BINDING 199
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT BINDING 216
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
SQ SEQUENCE 890 AA; 101687 MW; A6C8FD1A95B5B85A CRC64;
MTDIKSVLAS ISASIREPSK DDVIYLDECS VTGDKDIFED GVFVDLVSFE SFGLKCLQHN
YNRAQQGSGQ SSDQSPGVPA GRFYLNIKKK KKLLDKIEKS EIKNLTLNVE GGFKESRVYE
YQCEYALYDL EENLYILLDQ VEDERVKNIC KSIISHKNEI KKESPNKWVN EIKESKYAKD
LIQLPNITIK NENLECAVCK AKKNIWLNLS DGYIGCGRKI FNYGGGCLNN EEGAALKHYY
ESGKKYPLVV KLGTITKEGE ADVFSYADDE NDSVIDPYIN VHLKNLGINI TNLNKTEVTT
LEKEIKENQN INFTSILDKD TQLVCKEGKV GFLNLGNTCY MNCALQVLLS IKEVSYRYID
NQVDFLLTLE REKKTHLDMF IQYAKLCCMI FKEDYIKKKK KYIKKFKEEC VNRNVEVNYD
SDVDEENCVS INPSMFRRCL NQKGNSFCNN SQQDIFEFLT YFLNELIENE NVIFQRLLNG
GNSDKRKMSQ MEKSQQGGKT QQGGETQKGD KFNKSNNNMS AAEGENREGD NQQKSEKSLF
NLFTFEMEQT IVSDENNISK SSFHNNILSL DIPLDNAVLK KLEGQDTSLT SPSHVTLLDC
LNNFIKKDHI DEYYSEEKKM KIFAQKDIKF KTFPPYLFIH IKRFYADENW SAKKINIPIQ
TDEYINLEFM RSEKTPTAAI TATSSGSGYG EGQGKNSADA SHARKSNEEY IMQQHKDLFN
SLLDLGFEKE KILEAIRKVK VKNVNNCISY IYGEDSVELE LQEISQGTDV NSENLNAIVS
MGVNRDVAMA SLLINKNDLQ KSIDYIFSNL DVLTEMKCAA IVNRNKCEDG LANYELVASI
VHMGSNANSG HYICYIKDDA QWYVYNDNKI GLCDTNKGRD TAYIHLYKRI
//
