ID A0A0C3QJ63_9AGAM Unreviewed; 579 AA.
AC A0A0C3QJ63;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=RING-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=M407DRAFT_66866 {ECO:0000313|EMBL:KIO32260.1};
OS Tulasnella calospora MUT 4182.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Tulasnellaceae; Tulasnella.
OX NCBI_TaxID=1051891 {ECO:0000313|EMBL:KIO32260.1, ECO:0000313|Proteomes:UP000054248};
RN [1] {ECO:0000313|EMBL:KIO32260.1, ECO:0000313|Proteomes:UP000054248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUT 4182 {ECO:0000313|EMBL:KIO32260.1,
RC ECO:0000313|Proteomes:UP000054248};
RG DOE Joint Genome Institute;
RA Kuo A., Girlanda M., Perotto S., Kohler A., Nagy L.G., Floudas D.,
RA Copeland A., Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K.,
RA Lindquist E.A., Lipzen A., Lundell T., Morin E., Murat C., Sun H.,
RA Tunlid A., Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.,
RA Nordberg H.P., Cantor M.N., Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUT 4182 {ECO:0000313|Proteomes:UP000054248};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN822956; KIO32260.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C3QJ63; -.
DR STRING; 1051891.A0A0C3QJ63; -.
DR HOGENOM; CLU_019709_0_0_1; -.
DR OrthoDB; 3088759at2759; -.
DR Proteomes; UP000054248; Unassembled WGS sequence.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 3.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR InterPro; IPR001293; Znf_TRAF.
DR PANTHER; PTHR10131:SF157; RING-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR10131; TNF RECEPTOR ASSOCIATED FACTOR; 1.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR Pfam; PF02176; zf-TRAF; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF49599; TRAF domain-like; 2.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS50145; ZF_TRAF; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00207}; Reference proteome {ECO:0000313|Proteomes:UP000054248};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00207};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00207}.
FT DOMAIN 18..57
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 101..155
FT /note="TRAF-type"
FT /evidence="ECO:0000259|PROSITE:PS50145"
FT DOMAIN 156..201
FT /note="TRAF-type"
FT /evidence="ECO:0000259|PROSITE:PS50145"
FT ZN_FING 101..155
FT /note="TRAF-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00207"
FT ZN_FING 156..201
FT /note="TRAF-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00207"
FT REGION 289..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 234..268
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 289..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 579 AA; 62423 MW; 4AF062C82B677512 CRC64;
MNSAQYTYVD QVNGNLVCCI CRNPFIDPVS TTTCSHTFCT ECIASALLVT QQCPVDRSPL
TSTQLQPAAT IVRNLVDELS VECPHAPAGC SLTCQRQHLP VHLASNCDYV QVQCSEEGCT
HTVLRKDLGK HAADCTHRLV ECEACGRDVR LSEIESHPDE CPATEITCVH CAATLPRASL
SAHLGSCDLI PIPCAHSSNG CSWIGPRHLL DTHHLPLCPY EAIKGFFAIH SVRQKDLELE
NADLRRRLED TERTVRSHQR DLERAKVKLG TWFQPMGPET PPAIVETTSL ASSQNSTASG
AGTPTRPEAR RRLSVPFNSA VFGVDDTADN MSSVQNRRST VSTAAPERHA ESVASGSRPN
SFDDPYAAFT ASNPMAHPIL TGTGGAGPST FYRAHSSNSN PVAPLNLNGS LEGTLSSLRS
SIVSLSQSLE SLERKQDIML TTETLRMHED VASLRAIVHG LRMQVHNIMM DRNSYFTNRA
GPTVPAVPGH IAPALSRQPS SPNLPTTSSA TVGVEPIHRP SASVGGTSYT VSQFPLSSFA
ADGDPAGPAQ YLNQRPPIYY NLSPNIITSS VRRGPEGKL
//
