ID A0A1Q8RJG2_9PEZI Unreviewed; 579 AA.
AC A0A1Q8RJG2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 13-SEP-2023, entry version 23.
DE SubName: Full=Desumoylating isopeptidase 1 {ECO:0000313|EMBL:OLN84469.1};
GN ORFNames=CCHL11_08242 {ECO:0000313|EMBL:OLN84469.1};
OS Colletotrichum chlorophyti.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum.
OX NCBI_TaxID=708187 {ECO:0000313|EMBL:OLN84469.1, ECO:0000313|Proteomes:UP000186583};
RN [1] {ECO:0000313|EMBL:OLN84469.1, ECO:0000313|Proteomes:UP000186583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NTL11 {ECO:0000313|EMBL:OLN84469.1,
RC ECO:0000313|Proteomes:UP000186583};
RA Gan P., Narusaka M., Tsushima A., Narusaka Y., Takano Y., Shirasu K.;
RT "Draft Genome Assembly of Colletotrichum chlorophyti a pathogen of
RT herbaceous plants.";
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the DeSI family.
CC {ECO:0000256|ARBA:ARBA00008140}.
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:OLN84469.1}.
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DR EMBL; MPGH01000189; OLN84469.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q8RJG2; -.
DR STRING; 708187.A0A1Q8RJG2; -.
DR OrthoDB; 151499at2759; -.
DR Proteomes; UP000186583; Unassembled WGS sequence.
DR GO; GO:0008233; F:peptidase activity; IEA:InterPro.
DR CDD; cd02947; TRX_family; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 3.90.1720.30; PPPDE domains; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR008580; PPPDE_dom.
DR InterPro; IPR042266; PPPDE_sf.
DR InterPro; IPR013535; PUL_dom.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR12378; DESUMOYLATING ISOPEPTIDASE; 1.
DR PANTHER; PTHR12378:SF7; DESUMOYLATING ISOPEPTIDASE 1; 1.
DR Pfam; PF05903; Peptidase_C97; 1.
DR Pfam; PF08324; PUL; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR SMART; SM01179; DUF862; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51858; PPPDE; 1.
DR PROSITE; PS51396; PUL; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000186583}.
FT DOMAIN 1..141
FT /note="PPPDE"
FT /evidence="ECO:0000259|PROSITE:PS51858"
FT DOMAIN 298..574
FT /note="PUL"
FT /evidence="ECO:0000259|PROSITE:PS51396"
FT REGION 151..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 579 AA; 63835 MW; 8902C57FD56FD634 CRC64;
MDVHLLTYDL SRGLARQMSQ GMLGFHLDAV YHTSILLNGL EYVYDGGIVA IQLGSSHLGQ
PMEQIFLGKT ELPMEVIEEF LDSLRPIFTV EAYDLWKHNC NNFSDSFAQF LLGKGIPEHI
IKMPDAVLSS PLGRMLMPQL NQAINSNRQN GSILGLQNSS TNGHGSARQP MKPQANVKVV
HSSQELDDAL EASKKSCAVV LFTSATCPPC RVIAPVFDEL SAEAGDKATF IKVDVTQLTP
LPERNYPRAT PTFITYLHGE KENEWAGADP VALRGNIHLL LQMASLRHPH ESLNLPSFSN
PNAQPVLYSK IPPMAKLLVK MGSTADEPAV QRVKQFIEAR EKQGAAAAIL PDMAEFSAFV
RTSLQTLSIE VLFTIIDLFR CGLVDARFSG YFAEENDHRT VLAVLNYVNS RTECPYALRL
VTLQMACNFF STPLYPEEIL RNETLRAPII QLISSSFLDD SHNNIRVSAS SLMFNLALAS
NKARRENSGN ILSQEDSVEL AASVLEAIGQ EESSPEALQG MLLALGNLVY CTPSDSEVSD
LLRTMDAEDT IVAKKKQFPK EKMITEVGSE LLGKGLRRP
//
