ID   W6Z355_COCMI            Unreviewed;      1131 AA.
AC   W6Z355;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN   ORFNames=COCMIDRAFT_8267 {ECO:0000313|EMBL:EUC42089.1};
OS   Bipolaris oryzae ATCC 44560.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX   NCBI_TaxID=930090 {ECO:0000313|EMBL:EUC42089.1};
RN   [1] {ECO:0000313|EMBL:EUC42089.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 44560 {ECO:0000313|EMBL:EUC42089.1};
RX   PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA   Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA   Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA   Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA   LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA   Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT   "Comparative genome structure, secondary metabolite, and effector coding
RT   capacity across Cochliobolus pathogens.";
RL   PLoS Genet. 9:E1003233-E1003233(2013).
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   -!- SIMILARITY: Belongs to the peptidase C19 family.
CC       {ECO:0000256|ARBA:ARBA00009085}.
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DR   EMBL; KI964073; EUC42089.1; -; Genomic_DNA.
DR   RefSeq; XP_007691368.1; XM_007693178.1.
DR   AlphaFoldDB; W6Z355; -.
DR   STRING; 930090.W6Z355; -.
DR   GeneID; 19126102; -.
DR   KEGG; bor:COCMIDRAFT_8267; -.
DR   eggNOG; KOG1863; Eukaryota.
DR   HOGENOM; CLU_003532_2_1_1; -.
DR   OrthoDB; 51419at2759; -.
DR   Proteomes; UP000054032; Unassembled WGS sequence.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd03775; MATH_Ubp21p; 1.
DR   CDD; cd02659; peptidase_C19C; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   InterPro; IPR002083; MATH/TRAF_dom.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR008974; TRAF-like.
DR   InterPro; IPR024729; USP7_ICP0-binding_dom.
DR   InterPro; IPR029346; USP_C.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR24006:SF644; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 7; 1.
DR   Pfam; PF00443; UCH; 1.
DR   Pfam; PF14533; USP7_C2; 1.
DR   Pfam; PF12436; USP7_ICP0_bdg; 1.
DR   SMART; SM00061; MATH; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF49599; TRAF domain-like; 1.
DR   PROSITE; PS50144; MATH; 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|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   DOMAIN          64..194
FT                   /note="MATH"
FT                   /evidence="ECO:0000259|PROSITE:PS50144"
FT   DOMAIN          220..542
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
SQ   SEQUENCE   1131 AA;  129800 MW;  4A13AC6924EBF663 CRC64;
     MDQLESDMLV DHEYDEKADV AIITPDTDDA MDDVDADAEP RADEYDAFMK RHMPKTAEYE
     TEAEAYHTWE IRDWRTLTRR EHGPIFECGG HPWRILFFPY GNNVDFASFY LEQAYDEKQM
     PEDWYACVEF MLVLWNPNDP SIFTTHTAHH RFTADEGDWG FTRFAELRKL FSNSWEDRGR
     PMVEDNAANV TAYVRVLKDP TGVLWHNFIN YDSKKETGMV GLKNQGATCY LNSLLQSLFF
     TTAFRQAVYQ IPTAEEADRS NSAYALQRLF YLLQTSTTAV GTTELTHSFG WDSKQIFEQQ
     DVQELSRVLM DKLDERMKGT EAEGALTKMF VGKMKTYISC INVDYESSRV EEFWDIQLNV
     SGNKNLDDSF RDYVQVETMD GENKYFAEGF GLQDARKGVI FESFPPVLHL QLKRFEYDFQ
     RDAMMKVNDR YEFPEVWDAA PYLSEGADRS ESWVYHLHGV LVHSGDLNAG HYYAFLKPTK
     DGHYYKFDDD RVTRATLREA LEENFGGDYV QANGNTGQRN PYTRAWSAKR SMSAYMLVYI
     RETRLDQVLM DSKAVEPPKH LAERLAEERA ALERRKKERE EAHLYMDVAV ASNDQFSVYQ
     GFDIVPWKNE VETPASPKIY RVLRATTMAD FAATVAQDLG TQADMLRPWS MVNRQNGTVR
     PDTALEFPEM TVEEAASKHG TKQAQFRMWI EKAEDRDETG APIFGERLVD LKGQANNRPL
     MIFLKHFDAN QQSLFGMGTF YAAYQDKVSD LTPTILKMMG WPAGTQIKLS EEIKQNMIEA
     MKPKVTLAAS EIQDGDIITV QRVLSEKEAA QITAAGGYTE AKEFYDYLLN KINIEFVPRV
     PEADLPTFSL TLSKKMAYDQ FASKVAEQLK TDPSHLRFTT VSTAGKPKQA IKYSATSTLN
     NILFPGPYNY SASAMQRNDA LFYEVLDMSL KELEQRKPVK VTWLPDGLSK EEEHTLMVPK
     NAQVSDLLEA LQKKAGISDE IMQKTRAYEA HMHKFHKVLP PDHSIMSLYD YTQIFVAPYS
     DDESSKKITV FHYDKEPSKP HGVPFQLSIK EGEPFSETKQ RLSDFTKIKG KQLDKIKFAL
     VSRSQYSKPE PLDDDDVLWD AIAGRDDVSL GLDHPAKTRT LWGKTDSIFI R
//