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Database: UniProt
Entry: M2RLG6_COCSN
LinkDB: M2RLG6_COCSN
Original site: M2RLG6_COCSN 
ID   M2RLG6_COCSN            Unreviewed;       788 AA.
AC   M2RLG6;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN   ORFNames=COCSADRAFT_197277 {ECO:0000313|EMBL:EMD67484.1};
OS   Cochliobolus sativus (strain ND90Pr / ATCC 201652) (Common root rot and
OS   spot blotch fungus) (Bipolaris sorokiniana).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX   NCBI_TaxID=665912 {ECO:0000313|EMBL:EMD67484.1, ECO:0000313|Proteomes:UP000016934};
RN   [1] {ECO:0000313|EMBL:EMD67484.1, ECO:0000313|Proteomes:UP000016934}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ND90Pr / ATCC 201652 {ECO:0000313|Proteomes:UP000016934};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
RN   [2] {ECO:0000313|Proteomes:UP000016934}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ND90Pr / ATCC 201652 {ECO:0000313|Proteomes:UP000016934};
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};
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DR   EMBL; KB445639; EMD67484.1; -; Genomic_DNA.
DR   RefSeq; XP_007697133.1; XM_007698943.1.
DR   AlphaFoldDB; M2RLG6; -.
DR   STRING; 665912.M2RLG6; -.
DR   GeneID; 19134008; -.
DR   KEGG; bsc:COCSADRAFT_197277; -.
DR   eggNOG; ENOG502QWTH; Eukaryota.
DR   HOGENOM; CLU_009919_1_1_1; -.
DR   OMA; AECGWED; -.
DR   OrthoDB; 1353379at2759; -.
DR   Proteomes; UP000016934; Unassembled WGS sequence.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR028889; USP_dom.
DR   PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR24006:SF758; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 36; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS50235; USP_3; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000016934}.
FT   DOMAIN          116..555
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          561..689
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          723..788
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        568..601
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        604..620
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        621..638
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        735..788
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   788 AA;  88461 MW;  10A7F9C59C59BAB9 CRC64;
     MHGVSRFLSR RDKHGEKRAS KHAKSKSQSP DTPLDLYRIF TSEGPRPPAN EHAEKNVKML
     LTRLHGSGIT KMAEEQAEHA LAWYPDDLDK AYDLLVLANE SLEGELKDYN PNVPMLGAIN
     RNMVTCYLDA LLFAMFARLD SFEAMLYDNF EDEPRKKLAA VLRLWVNLLR TGQLIRVDLT
     KHLQDSLARC GWEDAAQVRQ QDASEAFTFI TGALELPLLT LKMDIYHTGR EDKEDDHKFV
     NERLLEVAIP EPEEGRIVTL EDCLETYFNN RIEVKRYLQR QNTIASIRST RDEFTGKDPE
     KNESIHIETT EVDAPMTPII ASPISLEPTT TVAPVRPELE GRRRADSIFG KRYLRQPPEA
     QMFDEKKHVE DMLDNSSGGR PRSASLLKKE ILMPAWQFFS LIPWYTDNVP RSDAQVAAHF
     SAKRPVLGIC LKRYTMNSNG TPKRLDTYID IPLDIGLPHF ISDERMKEEG PLFGNFKLVL
     QSVVCHRGVS VDSGHYIALV RANARGRPGT ANSESDEEEA KWLRFDDLSS QRVTEVSIEQ
     ALHEESPYLL FYQVQPIDEE LASRGDPPTY TEAQSRIPSV DPSRETLASL PSTTTIDVDT
     TGDWEKISVP DAHTEPNRTD EPASRNSTSS NWRSSITIDD GEGSLRGRTQ PTTPAEDKTG
     FLSVSRRGSR IWMSGAGKSR PGSPSGENRL SITLSRLTGR GSNNKPITTE GVSVGDELSV
     VIDKATSPEG SQKSLSPVKE KKESGISRSK SKKEKKDRMR SKSREPGAVL DKGKSKGKTR
     PDRECIVM
//
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