ID A0A0D2IDM8_9EURO Unreviewed; 655 AA.
AC A0A0D2IDM8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KIX03919.1};
GN ORFNames=Z518_07472 {ECO:0000313|EMBL:KIX03919.1};
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:KIX03919.1, ECO:0000313|Proteomes:UP000053617};
RN [1] {ECO:0000313|EMBL:KIX03919.1, ECO:0000313|Proteomes:UP000053617}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 650.93 {ECO:0000313|EMBL:KIX03919.1,
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; KN847479; KIX03919.1; -; Genomic_DNA.
DR RefSeq; XP_013271055.1; XM_013415601.1.
DR AlphaFoldDB; A0A0D2IDM8; -.
DR STRING; 1442369.A0A0D2IDM8; -.
DR GeneID; 25295543; -.
DR VEuPathDB; FungiDB:Z518_07472; -.
DR HOGENOM; CLU_019105_1_0_1; -.
DR OrthoDB; 150979at2759; -.
DR Proteomes; UP000053617; Unassembled WGS sequence.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR CDD; cd16620; vRING-HC-C4C4_RBBP6; 1.
DR Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR014891; DWNN_domain.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR025829; Zn_knuckle_CX2CX3GHX4C.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR15439; RETINOBLASTOMA-BINDING PROTEIN 6; 1.
DR PANTHER; PTHR15439:SF0; SOMETHING THAT STICKS LIKE GLUE, ISOFORM A; 1.
DR Pfam; PF08783; DWNN; 1.
DR Pfam; PF04564; U-box; 1.
DR Pfam; PF13696; zf-CCHC_2; 1.
DR SMART; SM01180; DWNN; 1.
DR SMART; SM00343; ZnF_C2HC; 1.
DR SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51282; DWNN; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000053617};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00047}.
FT DOMAIN 5..78
FT /note="DWNN"
FT /evidence="ECO:0000259|PROSITE:PS51282"
FT DOMAIN 174..188
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 83..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 533..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..624
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 655 AA; 73055 MW; B80E169C373F355F CRC64;
MASYVYFKFK SQKEPQRVTI DGPHTDVWNL KREIITISRL GDGTDFDLKI YKENGDEEYT
DDTEIIPKDS TVLARRLPAS APGKGRAARY VSGKPPVSAK PTAANAASKS VKTVDMDKAM
TEQEKLQAMF QFTDAQWQQK QEEMAHETRV PMQGGKPFKK ANVPEGEPPH GYICYRCGKK
GHWIQACPTN DDANYDNKNR IKRTTGIPRS MLKKIDQSDI DKLDDVQRQN LMVNAEGEYV
FAQADEKAWK KHLEQVKAAE AAQKKVQIGD KELQDRGLEC SIDKRLFVDP MKTPCCGKTY
CHDCIENALL ENDLTCPGCE TENISLERLE PDEDMKARIK EYEAEKAEAK RRSRSPTVTA
DSPKANGSGS RSRSNSRQGS GSPQSTSGQA RKRSASDVDG PSASGNLAAP AMKRQKSGEA
ASSSTTPKPE ADAKKDGIKE SSTPESNNML PTNMMPPDLS QMQPGNNMPF PMMTGFNPFM
MNPMAMNMGM NGMNLTNPNF NMMTGMNGMN MFPQTNGNIG FPNMNQMPTW NMNMNQSQNQ
NQNQNQASNN MGPKGYNSNF NTNRPNRNTS FQPPKPTSQQ PAGMTGVPTG PKALMQQQNP
NQSFYPPTGP ASSKFSNQQR HIGNEEDNAY MRQPVNPHRH MNRNRRARQA DYREL
//
