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Database: UniProt
Entry: G2XPF9_BOTF4
LinkDB: G2XPF9_BOTF4
Original site: G2XPF9_BOTF4 
ID   G2XPF9_BOTF4            Unreviewed;       526 AA.
AC   G2XPF9;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Similar to endosome-associated ubiquitin isopeptidase (AmsH) {ECO:0000313|EMBL:CCD42765.1};
GN   ORFNames=BofuT4_P073770.1 {ECO:0000313|EMBL:CCD42765.1};
OS   Botryotinia fuckeliana (strain T4) (Noble rot fungus) (Botrytis cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=999810 {ECO:0000313|EMBL:CCD42765.1, ECO:0000313|Proteomes:UP000008177};
RN   [1] {ECO:0000313|Proteomes:UP000008177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T4 {ECO:0000313|Proteomes:UP000008177};
RX   PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA   Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA   Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA   Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA   Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA   Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA   Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA   Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA   Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA   Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA   Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA   Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA   Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA   Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT   "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT   sclerotiorum and Botrytis cinerea.";
RL   PLoS Genet. 7:E1002230-E1002230(2011).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M67C family.
CC       {ECO:0000256|ARBA:ARBA00010981}.
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DR   EMBL; FQ790248; CCD42765.1; -; Genomic_DNA.
DR   AlphaFoldDB; G2XPF9; -.
DR   STRING; 999810.G2XPF9; -.
DR   MEROPS; M67.A14; -.
DR   eggNOG; KOG2880; Eukaryota.
DR   HOGENOM; CLU_023304_4_0_1; -.
DR   InParanoid; G2XPF9; -.
DR   Proteomes; UP000008177; Unplaced contigs.
DR   GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0061578; F:K63-linked deubiquitinase activity; IEA:InterPro.
DR   GO; GO:0140492; F:metal-dependent deubiquitinase activity; IEA:InterPro.
DR   CDD; cd08066; MPN_AMSH_like; 1.
DR   Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 1.
DR   Gene3D; 1.20.58.80; Phosphotransferase system, lactose/cellobiose-type IIA subunit; 1.
DR   InterPro; IPR000555; JAMM/MPN+_dom.
DR   InterPro; IPR037518; MPN.
DR   InterPro; IPR044098; STAMBP/STALP-like_MPN.
DR   InterPro; IPR015063; USP8_dimer.
DR   PANTHER; PTHR12947; AMSH-LIKE PROTEASE; 1.
DR   PANTHER; PTHR12947:SF13; FI19924P1; 1.
DR   Pfam; PF01398; JAB; 1.
DR   Pfam; PF08969; USP8_dimer; 1.
DR   SMART; SM00232; JAB_MPN; 1.
DR   SUPFAM; SSF102712; JAB1/MPN domain; 1.
DR   SUPFAM; SSF140856; USP8 N-terminal domain-like; 1.
DR   PROSITE; PS50249; MPN; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000008177};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   DOMAIN          350..477
FT                   /note="MPN"
FT                   /evidence="ECO:0000259|PROSITE:PS50249"
FT   REGION          128..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          228..330
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        228..249
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        257..279
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        280..295
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        296..319
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   526 AA;  58735 MW;  9AF11DEC66BAE63E CRC64;
     MAGSTLQFSK PMSIKEISAK ASDFEFNPTI ALKYWLRTAD TLLREAYIYQ AEDNDQQAYL
     LLMRYAALVA EKLPGHPSAK DPETRSALRA AQKNLPDVLD GLERLKPRIN ARYNNWQKAL
     ERRKEIHAAR ENDTSRPSSR ADLAASDPAI AGNTTTLGAA ENSDLAVKLA HKEFRRRDAA
     RLATRQAGVT EEEEQERRTA GLWDDWESAL SKSGRNDDED VIRRNMEASR RRLDGSHDIS
     PDGTKKKPAR PARYVQTKAR NASSAYRYPS ISKSQPLVSD SGPFPPPGPL PPKPPKEEFE
     TPHFDTPPPR PEKQSSDTHE ISSSDVVGQD PKFTFRPSAY LENGKPLRTV FLPPTLRQQF
     LACAASNTRA NLETCGMLCG TLISNALFIS RLVIPEQTST SDTCETTNES AFFDYCASED
     LMVLGWIHTH PTQSCFMSSR DLHTHCGYQI MMPESIAIVC APSKNPSWGV FRLTDPPGMP
     AVLNCKQTGL FHPHEERNIY TDALRPGHVF EAEGLEFQVV DQRPNP
//
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