ID A0A059J3C1_TRIIM Unreviewed; 474 AA.
AC A0A059J3C1;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Deubiquitination-protection protein dph1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=H109_06133 {ECO:0000313|EMBL:KDB21992.1};
OS Trichophyton interdigitale (strain MR816).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=1215338 {ECO:0000313|EMBL:KDB21992.1, ECO:0000313|Proteomes:UP000024533};
RN [1] {ECO:0000313|EMBL:KDB21992.1, ECO:0000313|Proteomes:UP000024533}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR816 {ECO:0000313|EMBL:KDB21992.1,
RC ECO:0000313|Proteomes:UP000024533};
RG The Broad Institute Genomics Platform;
RA Cuomo C.A., White T.C., Graser Y., Martinez-Rossi N., Heitman J.,
RA Young S.K., Zeng Q., Gargeya S., Abouelleil A., Alvarado L., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., Martinez D., Murphy C., Pearson M.D.,
RA Persinoti G., Poon T., Priest M., Roberts A.D., Saif S., Shea T.D.,
RA Sykes S.N., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Trichophyton interdigitale MR816.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KDB21992.1}.
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DR EMBL; AOKY01000387; KDB21992.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A059J3C1; -.
DR STRING; 1215338.A0A059J3C1; -.
DR HOGENOM; CLU_024293_0_1_1; -.
DR OMA; PGMDMFG; -.
DR Proteomes; UP000024533; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR CDD; cd14324; UBA_Dsk2p_like; 1.
DR CDD; cd16106; Ubl_Dsk2p_like; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR InterPro; IPR006636; STI1_HS-bd.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR015496; Ubiquilin.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10677:SF3; FI07626P-RELATED; 1.
DR PANTHER; PTHR10677; UBIQUILIN; 1.
DR Pfam; PF00627; UBA; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR SMART; SM00727; STI1; 2.
DR SMART; SM00165; UBA; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF46934; UBA-like; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50030; UBA; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000024533}.
FT DOMAIN 8..79
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 429..473
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT REGION 82..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 474 AA; 49880 MW; DFD65C4B673C4D01 CRC64;
MAEEDAPFTF HVKSSAEPKF SLTLKPSSTV AEIKQILAGE EYANVPPERQ RLIYSGRVLK
DTDTLASHKV KEGHTIHLVK SAVPAGGSSS GSASASASNT TTASNAAGRG TQSTPSGAAG
VPTNLAAGTG NSMLAGLTGA RYAGFSQLPG AGMFGPDGGM GPLPDTDQIL SMMENPQFQS
TMNEALQNPQ IIDMMIQQNP MLRDMPNARQ ILQSPEFRRM LTDPNMLRYM TQMQRAMGQG
GGGGQSAFPA PGVTNTTQRD AGSQDSNNNN NNNNNNNQNQ PQMPPFNPFL AMPGAGGNPF
SFLAGMQQPP AGAASGDAGT ARSNNNNTTS SSNNQQQQQQ QHQPNPFASL FNPALFGQPP
NADGQAAQPI PNPFVQNPAL FSQLMQAMGG GPGADANSNA GANANANASN PLLHSLFGGQ
PPQPPDNRPP EERYAEQLRQ LNDMGFFEFD RNIEALRRSG GSVQGAVEYL LNSP
//