ID A0A1E3QIV6_9ASCO Unreviewed; 479 AA.
AC A0A1E3QIV6;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN ORFNames=BABINDRAFT_9967 {ECO:0000313|EMBL:ODQ77625.1};
OS Babjeviella inositovora NRRL Y-12698.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; CUG-Ser1 clade incertae sedis; Babjeviella.
OX NCBI_TaxID=984486 {ECO:0000313|EMBL:ODQ77625.1, ECO:0000313|Proteomes:UP000094336};
RN [1] {ECO:0000313|Proteomes:UP000094336}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-12698 {ECO:0000313|Proteomes:UP000094336};
RG DOE Joint Genome Institute;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
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 ECO:0000256|RuleBase:RU366025};
CC -!- SIMILARITY: Belongs to the peptidase C19 family. UBP8 subfamily.
CC {ECO:0000256|ARBA:ARBA00038490}.
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DR EMBL; KV454439; ODQ77625.1; -; Genomic_DNA.
DR RefSeq; XP_018982953.1; XM_019133048.1.
DR AlphaFoldDB; A0A1E3QIV6; -.
DR STRING; 984486.A0A1E3QIV6; -.
DR GeneID; 30150901; -.
DR OrthoDB; 74526at2759; -.
DR Proteomes; UP000094336; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; 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 SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU366025};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000094336};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00502}.
FT DOMAIN 65..166
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 179..477
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 479 AA; 52386 MW; B36D89F4F6399CB8 CRC64;
MTIARTNTPG KSVPGKTTPG IAAPASTPAS AFPRAAFGPC SHLTQVLGTA TVRTQFLKQY
ALGVRVARFV TRGADATTLD HALQAARAAT LKCHECALAT TLLFLCLQCS YIGCAAHFPR
HTDTSGHVFA VDILTGFLKC FKCGDFIGAH DLDANAHDDT NWIVEHSRLP SYKATTGLRG
MVNMGATCFI SSVLQTLIHN PYVRNHFLAG SHADCCVENC ITCCVDEIFT EFYSKSEVNG
YGPTRLLTVA WKTKRALAGY SEQDAHEFWQ FIVDEIHRAR VRDHAKGAHG EVCDCITHST
FRGELQSTTT CGSCGASTVT VDPMLDLSLE IPASRAPTLA SCLDKFTAEE HLDVQYPCSR
CGERARAISK RLRVQTLPRV FGVQLKRFEH NGASTKIETH VAFPLFVDLA PYTLAGETAT
YELFALVVHI GSVLTGHYIS VIKSQGQWFR LDDSMVALVT EKEVLLMKAY LLFYAVHVV
//
