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}.
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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
//