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Database: UniProt
Entry: M2WLE1_DOTSN
LinkDB: M2WLE1_DOTSN
Original site: M2WLE1_DOTSN 
ID   M2WLE1_DOTSN            Unreviewed;      1174 AA.
AC   M2WLE1;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN   ORFNames=DOTSEDRAFT_24854 {ECO:0000313|EMBL:EME42838.1};
OS   Dothistroma septosporum (strain NZE10 / CBS 128990) (Red band needle blight
OS   fungus) (Mycosphaerella pini).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Dothistroma.
OX   NCBI_TaxID=675120 {ECO:0000313|EMBL:EME42838.1, ECO:0000313|Proteomes:UP000016933};
RN   [1] {ECO:0000313|Proteomes:UP000016933}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NZE10 / CBS 128990 {ECO:0000313|Proteomes:UP000016933};
RX   PubMed=23209441; DOI=10.1371/journal.pgen.1003088;
RA   de Wit P.J.G.M., van der Burgt A., Oekmen B., Stergiopoulos I.,
RA   Abd-Elsalam K.A., Aerts A.L., Bahkali A.H., Beenen H.G., Chettri P.,
RA   Cox M.P., Datema E., de Vries R.P., Dhillon B., Ganley A.R.,
RA   Griffiths S.A., Guo Y., Hamelin R.C., Henrissat B., Kabir M.S.,
RA   Jashni M.K., Kema G., Klaubauf S., Lapidus A., Levasseur A., Lindquist E.,
RA   Mehrabi R., Ohm R.A., Owen T.J., Salamov A., Schwelm A., Schijlen E.,
RA   Sun H., van den Burg H.A., van Ham R.C.H.J., Zhang S., Goodwin S.B.,
RA   Grigoriev I.V., Collemare J., Bradshaw R.E.;
RT   "The genomes of the fungal plant pathogens Cladosporium fulvum and
RT   Dothistroma septosporum reveal adaptation to different hosts and lifestyles
RT   but also signatures of common ancestry.";
RL   PLoS Genet. 8:E1003088-E1003088(2012).
RN   [2] {ECO:0000313|EMBL:EME42838.1, ECO:0000313|Proteomes:UP000016933}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NZE10 / CBS 128990 {ECO:0000313|Proteomes:UP000016933};
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).
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; KB446540; EME42838.1; -; Genomic_DNA.
DR   AlphaFoldDB; M2WLE1; -.
DR   STRING; 675120.M2WLE1; -.
DR   EnsemblFungi; EME42838; EME42838; DOTSEDRAFT_24854.
DR   eggNOG; KOG1863; Eukaryota.
DR   HOGENOM; CLU_003532_2_1_1; -.
DR   OMA; HTAHHRF; -.
DR   OrthoDB; 51419at2759; -.
DR   Proteomes; UP000016933; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000016933};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   DOMAIN          69..200
FT                   /note="MATH"
FT                   /evidence="ECO:0000259|PROSITE:PS50144"
FT   DOMAIN          226..551
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1174 AA;  134848 MW;  E91E305B072250D7 CRC64;
     MLLDSDYDEK RLTPNDENDN VAIISPDDAD SMVDDPEPGA EPALPSADDH EAMMARFMPA
     SPDYETEAEI VHTWDITNWR TLPKRTHGPV FQCAGHPWRI LFFPAGNSAS ESVSFYLEQG
     FGDEKPPQDW YACAQFMLVL HNPKDPSIYI HHEANHRFTA EEGDWGFTRF VDKNRIFAAK
     FDNADRPLVE DDGARMTAYV RVLKDPTGVL WHNFINYDSK KETGMVGLRN QGATCYLNSL
     LQSLYLTGAF RKAVYQIPTE TPEDKEASQS AYMLQRLFYR LQADPAAVGT QELTHSFGWE
     SRQIFEQQDV QELSRILMEK LETRMKGTEA ENALNNMFVG KMKTYLKCVN VEYESSRIEE
     FWDLQLNVSG CKSLDDSFRD YIQKELLEGD NKYAAEGYGL QDAEKGVIFE SFPNVLHLQL
     KRFEYDFQRD AMMKVNDRYE FPEIFDATPY LDETADKSEP YVYHLHGVLV HSGDLNAGHY
     YAFLKPEKNG QFYRFDDDRV TRATKREAID ENFGGDYGAN GTYGQKGQNP YTRQWSTKRS
     NNAYMLVYIR ESRLDQIILP DTDVKPPAHL PAKIAEEREL AERRRKEKEE AHLYMNVLVA
     TEANFKAYQG VDLIPWTSEQ SDDPAVPKVH RLLRDMTIQD FTTFLAQQQG LDKDLVRPWI
     MVNRQNGTVR PDHPLSWPDM TLQEAADKFS TRQSGFRVFV EETTRDDKGL PVWPDDDEVV
     QPATPLVNGN ATQQQKPIIL FLKYFDVDRQ LLIGVGHVYM NPLDKAQDLA TPILEIMKWE
     AGSIHLELFE EIKQNYIEPM KPRNTLIASE IQDGDIICFQ RHLEDPESAT IKTRSPGACL
     TAPAYYDFMM NRLFVDFTPK TLPAQNLQVK DGDERFKLAL SKKDSYDAIA HKVAEHLSKV
     NPTPVDPTHL RFTTTNIQSG KPRAIVKRVQ GATVSTILLG TSGYGGYSYA PSQAPDHLFY
     EVLEMSLTDL EQRKNVRVTW LSEGITKEEQ VDLLVHKQSQ FDAVLEALHK KLQLPDEILD
     HIRFYEAHSN KVYKIIPNSH GVLALNEFMS VYAERIPEEE KQLDADKGDR LLNCFHFEKD
     PSKSHGVPFI CLMKDGEVFK ETKERISKRT GIKGKNLEKV RFAVIKGGQN YSRPQWVEDD
     DILSEKLSPD DHLGLEHPNR NRNNWARYES LNIR
//
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