ID A0A4P9Z8L3_9ASCO Unreviewed; 782 AA.
AC A0A4P9Z8L3;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|PIRNR:PIRNR016308};
DE EC=3.4.19.12 {ECO:0000256|PIRNR:PIRNR016308};
GN ORFNames=METBISCDRAFT_19623 {ECO:0000313|EMBL:RKP29035.1};
OS Metschnikowia bicuspidata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Metschnikowia.
OX NCBI_TaxID=27322 {ECO:0000313|EMBL:RKP29035.1, ECO:0000313|Proteomes:UP000268321};
RN [1] {ECO:0000313|Proteomes:UP000268321}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Baker2002 {ECO:0000313|Proteomes:UP000268321};
RX PubMed=30297742; DOI=10.1038/s41564-018-0261-0;
RA Ahrendt S.R., Quandt C.A., Ciobanu D., Clum A., Salamov A.,
RA Andreopoulos B., Cheng J.F., Woyke T., Pelin A., Henrissat B.,
RA Reynolds N.K., Benny G.L., Smith M.E., James T.Y., Grigoriev I.V.;
RT "Leveraging single-cell genomics to expand the fungal tree of life.";
RL Nat. Microbiol. 3:1417-1428(2018).
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|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; ML004518; RKP29035.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4P9Z8L3; -.
DR Proteomes; UP000268321; 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; cd02658; Peptidase_C19B; 1.
DR CDD; cd14385; UBA1_spUBP14_like; 1.
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; 2.
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:SF10; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 14; 1.
DR Pfam; PF00627; UBA; 2.
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; 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:RKP29035.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR016308}; Protease {ECO:0000256|PIRNR:PIRNR016308};
KW Reference proteome {ECO:0000313|Proteomes:UP000268321};
KW Thiol protease {ECO:0000256|PIRNR:PIRNR016308};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW 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 168..273
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 315..782
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT DOMAIN 581..622
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 643..683
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT ACT_SITE 324
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-1"
FT ACT_SITE 741
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-1"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT BINDING 206
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT BINDING 220
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
SQ SEQUENCE 782 AA; 87086 MW; EBDB5AB8E29307B0 CRC64;
MSVYEYIQNA SFSLPAAVTP VDKVYKDDCM YSFDTAENNA LGIDVCMTCF QSFARTEHRD
WTAAHYAQKR HAVFLNIVKV LIPESKRQSP FRLLLTNSRV PKAPKLEIVQ QTDLDLYTTT
IQIYVALLDR TLELNASPEP VQALAAQILR TNSANTNNDI TAWEHEIFAC EHSLALCQVD
ENTLQCSGCE LTLNLWICLT CGTMSCGREN FGSDIKGNSH ALAHFDAYRH PVAAKLGSLS
ADEDKCDCYC YKCNDEVKVP HLGRILRRFG IDLAMAVKSE KTLVEMNVET NQNWQFNLEG
SDGEKLAPVL GPGLTGMQNL GNSCYVNSVV QALFSLAAYR DYFAQMSFDF SVENPAQDLA
SQLLKLYDGL ISGRYSRPSG LKGDQYQEGI KPHTFKNLVG ANHAEFRTNK QQDASEFLHY
LLDKIDKELG LSVNRDLKFV YSSKLVCTGC NSGSTTRELV DTVTLPLHVA VIGTEDGKKI
YASTTFDESL QMLTHPEIIE GYQCEACGQR TEAHKQGGFE TFPKYLLASL QRIQLENWAP
VKVDVPVETP DRVDLAAYRA PKFAENETEI RKEKPAAGHF KPNAEALLTL QSMGFSENRS
CRALYHTGNK DAETAMNWIF GHMEEAEIDA PFAFPAGETT SSLVLQEAID NLVSMGFPAK
DAKKALVLYL GDANSAVEWL FSHPDDDGEH AEQRPKINVQ EESRQLQQAL LDVASASPVP
TANYRVKAVV CHKGSLPHTG HYVVFVKVDG RWVLFNDEKV VDCGASTDEI RTSSYIYVLE
KI
//
