ID A0A0D2IMY2_9EURO Unreviewed; 587 AA.
AC A0A0D2IMY2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Rhinocladiella mackenziei CBS 650.93 unplaced genomic scaffold supercont1.2, whole genome shotgun sequence {ECO:0000313|EMBL:KIX07154.1};
DE Flags: Fragment;
GN ORFNames=Z518_01807 {ECO:0000313|EMBL:KIX07154.1};
OS Rhinocladiella mackenziei CBS 650.93.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Rhinocladiella.
OX NCBI_TaxID=1442369 {ECO:0000313|EMBL:KIX07154.1, ECO:0000313|Proteomes:UP000053617};
RN [1] {ECO:0000313|EMBL:KIX07154.1, ECO:0000313|Proteomes:UP000053617}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 650.93 {ECO:0000313|EMBL:KIX07154.1,
RC ECO:0000313|Proteomes:UP000053617};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Rhinocladiella mackenzie CBS 650.93.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN847476; KIX07154.1; -; Genomic_DNA.
DR RefSeq; XP_013274290.1; XM_013418836.1.
DR AlphaFoldDB; A0A0D2IMY2; -.
DR STRING; 1442369.A0A0D2IMY2; -.
DR GeneID; 25289878; -.
DR VEuPathDB; FungiDB:Z518_01807; -.
DR HOGENOM; CLU_465095_0_0_1; -.
DR OrthoDB; 954418at2759; -.
DR Proteomes; UP000053617; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00303; retropepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR032567; LDOC1-rel.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR005162; Retrotrans_gag_dom.
DR InterPro; IPR001878; Znf_CCHC.
DR PANTHER; PTHR15503:SF22; CCHC-TYPE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR15503; LDOC1 RELATED; 1.
DR Pfam; PF03732; Retrotrans_gag; 1.
DR Pfam; PF08284; RVP_2; 1.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 4: Predicted;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022750};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Protease {ECO:0000256|ARBA:ARBA00022750};
KW Reference proteome {ECO:0000313|Proteomes:UP000053617};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 331..346
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 587
FT /evidence="ECO:0000313|EMBL:KIX07154.1"
SQ SEQUENCE 587 AA; 65824 MW; FDDB882E2A2A952D CRC64;
MDTDMTNVDG SPFPSFGQNA HPQTSTGIPP TFPVPSSSGF QATPSTSQQG QADPTTLEAV
VPLELFQNIG GAGVEKPPKY GGQRENDAAR VWLIGMERWL WAKEILLRRN LTGPERIALT
TSYLEKAAAA WWNLTYIHNI DHQGHQLRIQ SWAEWKNTFL SQFGDVRTQD QRRDEFDSLR
QTGTVQAFRQ AIESRRLYLE PRPSDADCLL VFKRGLKTSI RNRIEILPDS IVPGTYTKYV
EFADKSEREM LATSNRVPFF KSRYGKPATS TSNGASHARN SAAPRRDHDG DVEMTLNGMR
TQPKSGNATS GQKASSKAPP SRQKCREENL CFGCGEPGHQ KKDSPDPSKH IGVAPLEAES
LTANPWDVSL ATANTFDKDL ERLQGHNLAS GNLGWTQNPY PVSILFDTGS DISYVSKKVV
NRLQGDLKIL ETNTLRVRLT NGETTTANQQ LTIGLTIGTF RARSTLRILD WDAYDVILGL
DWLQKHEASW DFARSCVTLR NGSRKSTAVE LRPFRTIDYE GLKEVGLNLL SYRRAEKALR
KPPAQDRPPV LYIVESPKKE QDSSPIPSVK NPRFRHLLQR FQHVLKE
//