ID G2XJJ8_VERDV Unreviewed; 569 AA.
AC G2XJJ8;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN ORFNames=VDAG_10330 {ECO:0000313|EMBL:EGY20701.1};
OS Verticillium dahliae (strain VdLs.17 / ATCC MYA-4575 / FGSC 10137)
OS (Verticillium wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=498257 {ECO:0000313|EMBL:EGY20701.1};
RN [1] {ECO:0000313|EMBL:EGY20701.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VdLs.17 {ECO:0000313|EMBL:EGY20701.1};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J.J., Klosterman S.J., Subbarao K., Dobinson K., Veronese P.,
RA Kang S., Gold S.E., Young S., Jaffe D., Gnerre S., Berlin A., Heiman D.,
RA Hepburn T., Sykes S., Alvarado L., Kodira C.D., Lander E., Galagan J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Verticillium dahliae VdLs.17.";
RL Submitted (MAR-2008) 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.
CC {ECO:0000256|RuleBase:RU366025}.
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DR EMBL; DS572730; EGY20701.1; -; Genomic_DNA.
DR RefSeq; XP_009658094.1; XM_009659799.1.
DR AlphaFoldDB; G2XJJ8; -.
DR STRING; 498257.G2XJJ8; -.
DR EnsemblFungi; EGY20701; EGY20701; VDAG_10330.
DR GeneID; 20711793; -.
DR KEGG; vda:VDAG_10330; -.
DR eggNOG; KOG1872; Eukaryota.
DR HOGENOM; CLU_017549_2_0_1; -.
DR InParanoid; G2XJJ8; -.
DR OMA; FKSDAEY; -.
DR OrthoDB; 160664at2759; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd02657; Peptidase_C19A; 1.
DR CDD; cd16104; Ubl_USP14_like; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR044635; UBP14-like.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR43982; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR43982:SF1; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 14; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU366025, ECO:0000313|EMBL:EGY20701.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU366025};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807,
KW ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 4..78
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 109..559
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 377..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..395
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 569 AA; 62724 MW; A72A0F610E6DBEDE CRC64;
MATIPIVVKH SGKKYDVEVD TTANGETLKY QLYSLTGVEP ERQKILVRGG PLKDEADMSK
IAFKPGQVIM MMGSPADGSA TLARPKEAIK FVEDMTEAEA AQQEGATPAG LINLGNTCYL
NSTLQTLRSI PELQQSLTTY KAKGPAPRPV QGSLGLQPVS QADLATPLVD LYKMMAETQD
SVAPHTFLTV LRSVYPQFAE KSKQGNGFAQ QDAEEAWSQI VSQLKQRLGE GKDSSFIDKY
MAGEMTSTLE ADEQDARDGG EETSKSTETF FKLNCHIDGT INHLRDGIAA GLTEKIEKRS
AVLDRDTNFT KKSQISRLPK YLTVHCVRFF WRRDTQKKAK IMRKVVFPHE LDAVEFCNDE
LKSMLIPVRD KVREIRKDEE DVQRARKRRK INANDRGDVA GSSGAPQEKT ALEKANEKKA
PVSQLPKVSG DGDTEMTETY KTDAEFDAER DASLLTLKKE LDGLINPALK QDEGANQSGL
YELRGVVTHQ GSSADSGHYT AYVKKEGRVD PKTGKRGEED GNWWWFNDDK VSEVPSTSID
ALAGGGESHS ALILLYKAIP LPTAEEPSS
//
