ID I4Y693_WALMC Unreviewed; 831 AA.
AC I4Y693;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|PIRNR:PIRNR016308, ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|PIRNR:PIRNR016308, ECO:0000256|RuleBase:RU366025};
GN ORFNames=WALSEDRAFT_49014 {ECO:0000313|EMBL:EIM19485.1};
OS Wallemia mellicola (strain ATCC MYA-4683 / CBS 633.66) (Wallemia sebi (CBS
OS 633.66)).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Wallemiomycotina;
OC Wallemiomycetes; Wallemiales; Wallemiaceae; Wallemia.
OX NCBI_TaxID=671144 {ECO:0000313|EMBL:EIM19485.1, ECO:0000313|Proteomes:UP000005242};
RN [1] {ECO:0000313|EMBL:EIM19485.1, ECO:0000313|Proteomes:UP000005242}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4683 / CBS 633.66 {ECO:0000313|Proteomes:UP000005242};
RX PubMed=22326418; DOI=10.1016/j.fgb.2012.01.007;
RA Padamsee M., Kumar T.K.A., Riley R., Binder M., Boyd A., Calvo A.M.,
RA Furukawa K., Hesse C., Hohmann S., James T.Y., LaButti K., Lapidus A.,
RA Lindquist E., Lucas S., Miller K., Shantappa S., Grigoriev I.V.,
RA Hibbett D.S., McLaughlin D.J., Spatafora J.W., Aime M.C.;
RT "The genome of the xerotolerant mold Wallemia sebi reveals adaptations to
RT osmotic stress and suggests cryptic sexual reproduction.";
RL Fungal Genet. Biol. 49:217-226(2012).
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, ECO:0000256|RuleBase:RU366025};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085, ECO:0000256|PIRNR:PIRNR016308,
CC ECO:0000256|RuleBase:RU366025}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JH668250; EIM19485.1; -; Genomic_DNA.
DR RefSeq; XP_006960517.1; XM_006960455.1.
DR AlphaFoldDB; I4Y693; -.
DR STRING; 671144.I4Y693; -.
DR GeneID; 18472478; -.
DR KEGG; wse:WALSEDRAFT_49014; -.
DR eggNOG; KOG0944; Eukaryota.
DR HOGENOM; CLU_009884_1_0_1; -.
DR InParanoid; I4Y693; -.
DR OMA; KVKYKTR; -.
DR OrthoDB; 166948at2759; -.
DR Proteomes; UP000005242; 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; cd14297; UBA2_spUBP14_like; 2.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 3.
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; 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; 3.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR Pfam; PF17807; zf-UBP_var; 1.
DR PIRSF; PIRSF016308; UBP; 2.
DR SMART; SM00165; UBA; 3.
DR SMART; SM00290; ZnF_UBP; 2.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR SUPFAM; SSF46934; UBA-like; 2.
DR PROSITE; PS50030; UBA; 3.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS50271; ZF_UBP; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PIRNR:PIRNR016308, ECO:0000256|RuleBase:RU366025};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR016308};
KW Protease {ECO:0000256|PIRNR:PIRNR016308, ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000005242};
KW Thiol protease {ECO:0000256|PIRNR:PIRNR016308,
KW ECO:0000256|RuleBase:RU366025};
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 2..114
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 158..268
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 310..831
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT DOMAIN 581..628
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 642..688
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 697..744
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT REGION 562..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 319
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-1"
FT ACT_SITE 789
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-1"
FT BINDING 183
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT BINDING 203
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 831 AA; 92637 MW; BE145B7CF4444F07 CRC64;
MGVCEHVETL GQSLRAPSIS DTVYKDECMR CFDSQDSENG VDVCLHCFHG GCATADNNSH
QHAYNHAKEK NHPLAVNIKR RIKKSQVEKE EPPLKKLAIE EERDEDIHSY DYNLKCLECN
AVYPSTSNST IESQIDAIVK ADSNAHKSEV KAWEEELTGC EHSVSISQTQ VPKKDVQMSG
AHCHACELSD NLWLCLTCGE LGCGRAQFGG LKGNSHALAH FENTGHAVAV KLGTITAEGS
ADIYCYACNE ERLNPNLATD LSNFGINIAA QVKTTKNLTE LQLEQNSKFD FSMTGEDGHE
LQPVFGNWLT GLKNLGNSCY MNSTIQSLFS YEEVKKYYSE LFAKLNKETV DDPANNLDIQ
LAKIADGLGS GRYSKQSRLG GQFQDGIKPA MFKNLIGKGH PEFSSMRQQD SEEFLGHFLE
VLRRTSKNTP KDLKNMFAFV AEQKLQCTSC NKVRYRYDNH DSLSVNIPVI EKGKVYDESS
KSDKIAYEDV DMQDCLSALI QPEQLEYSCP SCQTQVNAIK TWKLDTFPNA LVIHSRKFHL
VNWVPTKLDI QVNGVEKVDV TQMKSQGRQE GEVDLPDSND DKDDEIKFDG DSMTALTGMG
FSENRSKRAL INTNHSGAEA AMEWLFSHME DEGLDEPIEV KETEENQDVP AELINTVAEM
GFTQNQARKA LKSTQNSVEM AVGWLFENPT DPGEEAPIKE SSKGGEDDLI NVVTSMGFTE
NQARKALRLS SNNVEMAVSW LFENPTDAGE EAAEPMDEDD SKPGHVNSPA SYKLKAFISH
KGPSVHSGHY VVHVKHGDNW ILFNDEKVVK ESETNLNSLL GKGYVYFYEK I
//
