ID K1WGM5_MARBU Unreviewed; 1300 AA.
AC K1WGM5;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000313|EMBL:EKD16685.1};
GN ORFNames=MBM_05154 {ECO:0000313|EMBL:EKD16685.1};
OS Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Drepanopezizaceae; Drepanopeziza.
OX NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD16685.1, ECO:0000313|Proteomes:UP000006753};
RN [1] {ECO:0000313|EMBL:EKD16685.1, ECO:0000313|Proteomes:UP000006753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB_m1 {ECO:0000313|EMBL:EKD16685.1,
RC ECO:0000313|Proteomes:UP000006753};
RX PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA Huang M.-R., Wu R., Zhou Y.;
RT "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT evolution.";
RL BMC Genomics 13:382-382(2012).
CC -!- SIMILARITY: Belongs to the peptidase C48 family.
CC {ECO:0000256|ARBA:ARBA00005234}.
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; JH921438; EKD16685.1; -; Genomic_DNA.
DR RefSeq; XP_007293043.1; XM_007292981.1.
DR STRING; 1072389.K1WGM5; -.
DR GeneID; 18761089; -.
DR KEGG; mbe:MBM_05154; -.
DR eggNOG; KOG1868; Eukaryota.
DR HOGENOM; CLU_005922_0_0_1; -.
DR InParanoid; K1WGM5; -.
DR OMA; EWAIYRQ; -.
DR OrthoDB; 227085at2759; -.
DR Proteomes; UP000006753; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd02257; Peptidase_C19; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR003653; Peptidase_C48_C.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR Pfam; PF02902; Peptidase_C48; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 2.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR PROSITE; PS50600; ULP_PROTEASE; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:EKD16685.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006753}.
FT DOMAIN 684..1063
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT DOMAIN 1090..1261
FT /note="Ubiquitin-like protease family profile"
FT /evidence="ECO:0000259|PROSITE:PS50600"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1300 AA; 143403 MW; 4BBF12578E74922C CRC64;
MSPAATSGLP HTRATSISGG PVGMANGAKP IATDGWRGGN RVLPSLDELL AVRPQPEMIH
WAMRRLLLQG ESMSKQADTH LDFHRPEVAL QDYLKASIIV VDYIPRHRDY PSLQADRGEL
HRLYAKLQKR INEQHGTFAS VKTMIKENNA RSGVTSTSSV NDSGDSTAVG NGHLPTQSIP
DGPVNDTNGT NTRKRPAPPV QPKPEALHGN SIQTDLASRF ALLRNPEPVN SVQQDPRIKT
QPIVIPGMPS GSPAPQTKHT KTSSMSRPTG PREMPSVPQT IPSHIRIPLG VSIPTMPRAP
DAIYSPASGV DDAATINLPS SIARSSSYMA NGRPNFAPPV STVGPTPDLN ESRKDYFSIP
RTIPDNDDGP EALKPQTPVF PDASTITAEE LVKYQSQSVS ILIVDLRSRE EFDRGHIMSQ
SIICIEPMTL KNGITAEVLG ETMVVVPDLE QSLFETRNDF DLVVYYDQSS KSVNARASEG
VLQYFATAVY DYGYEKRVKR RPLLLVGGLD AWIDLLGPNS LRSSSTDNSI SIAKQAGSAR
SVGRFNMPAS QLGRMRSRSS RLLSSDEEMK WDLALKQEDA PNSPGSNDQL DLNEFVYART
VDAFLNKYPE MPVIQESMVS QSPPVRYKHA TPDDIDNSVP QLPTRPAPAL PRQRSGGIFD
RTTVTSYAAG PGTISTLQVS PGLTGLDNPR YLCYFNSSIQ ALSATPFIRD FVRNFTPGSF
DVPARRGETT RPPQLLLRFL SNLFRNMWSG QYDYVGPTSL ARYVNTIHFM SRHATASNVK
GFCFGGVDRQ HDAAEFLLWF LDVLDDEINP GRDQRPDFGR TNLTSKELTL QAALPLNQAS
QYAWSIMMRG QSSMLAQRSW GQTCNVVTCM SCNTSNRNWN DFQQLPVTIT TDQPTDLRAL
LGGLVDCDSE ICKRQENWVE GQPLPRRTKV QNAYITRLPE YLMITLNRFV NDPVTGISRR
VNTVVTFPET GINFEPYFCP RDASPEPLKD QEHKAPYEYA VYAVQRHSGT LDTGHYTTMA
RHPGLPRNDP NSAGGWHHYN DKFVSPYTPT VSLHSQPELY ESTQNLQPRP NQLEQDMETH
PIHGRGFSNH PIEPADLSSV SNARGWLTDT AIRQIVSAKG NTSPSSRVHF VDPTWLSQWA
LDNRPDLAAL ERSNAVPAFL AAARDPAVQG LALPFNEGNS HWVTIYLNLE EGGAIYFNSL
GSGGGVNARR LMEDFYAKFG GLSPHRTGPM SALRWQVDTG CAQQMDGSSC GIYTVRNCLD
LLERRVPGGE ILSPGQIANF RRNGTGVLKE VLRGQREVGG
//