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Database: UniProt
Entry: U7PJR2_SPOS1
LinkDB: U7PJR2_SPOS1
Original site: U7PJR2_SPOS1 
ID   U7PJR2_SPOS1            Unreviewed;      1075 AA.
AC   U7PJR2;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   22-FEB-2023, entry version 27.
DE   RecName: Full=MINDY deubiquitinase domain-containing protein {ECO:0000259|Pfam:PF04424};
GN   ORFNames=HMPREF1624_08660 {ECO:0000313|EMBL:ERS94949.1};
OS   Sporothrix schenckii (strain ATCC 58251 / de Perez 2211183) (Rose-picker's
OS   disease fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Sporothrix.
OX   NCBI_TaxID=1391915 {ECO:0000313|EMBL:ERS94949.1, ECO:0000313|Proteomes:UP000018087};
RN   [1] {ECO:0000313|Proteomes:UP000018087}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58251 / de Perez 2211183
RC   {ECO:0000313|Proteomes:UP000018087};
RX   PubMed=24855299; DOI=10.1128/genomea.00446-14;
RA   Cuomo C.A., Rodriguez-Del Valle N., Perez-Sanchez L., Abouelleil A.,
RA   Goldberg J., Young S., Zeng Q., Birren B.W.;
RT   "Genome sequence of the pathogenic fungus Sporothrix schenckii (ATCC
RT   58251).";
RL   Genome Announc. 2:E0044614-E0044614(2014).
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DR   EMBL; KI440857; ERS94949.1; -; Genomic_DNA.
DR   AlphaFoldDB; U7PJR2; -.
DR   STRING; 1391915.U7PJR2; -.
DR   eggNOG; KOG2427; Eukaryota.
DR   HOGENOM; CLU_007080_0_0_1; -.
DR   OrthoDB; 9158at2759; -.
DR   Proteomes; UP000018087; Unassembled WGS sequence.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR   GO; GO:1990380; F:K48-linked deubiquitinase activity; IEA:InterPro.
DR   InterPro; IPR007518; MINDY.
DR   InterPro; IPR033979; MINDY_domain.
DR   PANTHER; PTHR18063; NF-E2 INDUCIBLE PROTEIN; 1.
DR   PANTHER; PTHR18063:SF6; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   Pfam; PF04424; MINDY_DUB; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000018087}.
FT   DOMAIN          497..647
FT                   /note="MINDY deubiquitinase"
FT                   /evidence="ECO:0000259|Pfam:PF04424"
FT   REGION          1..459
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          771..830
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          861..1075
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..61
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        69..83
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..116
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        135..159
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        160..185
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        205..235
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        771..803
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        804..830
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        861..972
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1013..1075
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1075 AA;  115366 MW;  3B5CB59C5717B7E9 CRC64;
     MVVRKPLPQT YDGTGSGSPG GVNSDSVPDV LRPGRNPHPN AYSPAPPSPY SNFQTDEQSA
     WAQPAPPAMP QGMTSQNDSS QQPTPQQQPP PIPTAVPTIL LQSATGSSTA SGFSETNPFK
     RKAVMSAESP VQSPAVAVPP LPSAPAPPPP PPPASQPLPP TTSFSQLSMD DQTGNPWQPT
     PIDSRRGSQA PIPVIPENEA VGGGENAWAS QNATESPFRR PSPNPAASNR DSNLISFPPD
     EDADIAGWDE VASPVAAPGA GAASLPPPRA PFTPLNGKET ASDSNPVFED RNAWDDLGAR
     SGQPQPLPTN LVTEPAGEGW NLVDNEPVPG QLSRQSTWEN FTDDEEDVEQ PNSSQAKPAK
     PPLKPKPKNK NKLKEKNVVP SVPVGAVDTS APLISIDSPP PTSKPDEPVP AAAPTDSLQA
     VSQEAEEPAP LLPLRSMLDV DGDTPPRQPP RPSQSAKAET YQVKNISWYD VSASQNPRVS
     PILVQNANGP CPLVALVNAL TLTTPADIST ALVETLRSRE QVSLSFLLDA VFDELMSSRR
     SSRNSDLPDV DELYKFLKGL HTGMNVNPRF IPTQQVITAF RRTSLTHLHP TERDDMIPGT
     FEDTREMQLY ATFSIPLIHG WLPKKGDGAY EALSRQAASY EDVQNLLFRE EELEEKLSSP
     SGDGLTEDEQ QVFQDILEIK NFLHGSATQL TPFGLDIVAK AMRPGTFAIL FRNDHFSTLY
     RHPQTMQLLS LVTDAGYASH DEVIWETLVD VNGEHAEFYS GDFRLVGNSM QQNASSRTAG
     SGSRHGGSAS NNQNGWTTVR GRRQNQSEQH ESHSPLLSND ELSRHEQEDR DLALALQLQE
     EEEEQQRADE AHRNSRLSEQ FIEQNARPAN QSRRPSNAAG GGRYNSSQPV PVSSRRSSAG
     FPPGSLLDSN PNHRRTSSSS ASGSALGSTM SNGQRIGQYS SGRTPSRSPS HQQVVRPLVP
     PTSTSRVNTR PAVNRPADND ENDEAPPSYE QAAKLAPYHP PPGAPGSESA AGGRNSAAGS
     SSNLGGSSRA SISTPSPRPL GGYATTSGRQ NFAPGTYSAY QQQQAARSDR DCTIM
//
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