ID A0A166EB04_9AGAM Unreviewed; 1072 AA.
AC A0A166EB04;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=RING-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=SISSUDRAFT_984899 {ECO:0000313|EMBL:KZT39391.1};
OS Sistotremastrum suecicum HHB10207 ss-3.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Trechisporales; Trechisporales incertae sedis; Sistotremastrum.
OX NCBI_TaxID=1314776 {ECO:0000313|EMBL:KZT39391.1, ECO:0000313|Proteomes:UP000076798};
RN [1] {ECO:0000313|EMBL:KZT39391.1, ECO:0000313|Proteomes:UP000076798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB10207 ss-3 {ECO:0000313|EMBL:KZT39391.1,
RC ECO:0000313|Proteomes:UP000076798};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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DR EMBL; KV428047; KZT39391.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166EB04; -.
DR STRING; 1314776.A0A166EB04; -.
DR Proteomes; UP000076798; Unassembled WGS sequence.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR CDD; cd13246; PH_Scd1; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR033511; Cdc24/Scd1_PH_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10579; CALCIUM-ACTIVATED CHLORIDE CHANNEL REGULATOR; 1.
DR PANTHER; PTHR10579:SF43; LOW QUALITY PROTEIN: EPITHELIAL CHLORIDE CHANNEL PROTEIN-LIKE ISOFORM X1-RELATED; 1.
DR Pfam; PF15411; PH_10; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF53300; vWA-like; 1.
DR PROSITE; PS50234; VWFA; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Reference proteome {ECO:0000313|Proteomes:UP000076798};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 43..101
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 560..756
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT REGION 17..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 484..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1072 AA; 116827 MW; 8F51756772827F89 CRC64;
MQGREDIHSW ASSSTVVSSG AYYPSSPPVP VVSNQDSDSE DDCPVCLEPL SFSFRLPGEK
PHIVPECGHA LHEACFSAVY GPVPRSGVAP QKSPGVCGVC RRPMKVGDSD SGRSNKLAAL
TGMADRVGPN TLYPGRDTPA GSRSTIMQTP QPRSPNDDDP LDFHGGSIKS SGSGEQTSSY
IVAPSIQARP EFSTITRTGD ASQPLTCIVV VELPSRRNAS RQVPGPVMSE YRPQVQPERQ
LSPGSRLEPP APYSPHRPPS PQESVTSQAY SYNPTPQNGS PPPDSPFGSI TEDLRNRIID
WKGHPLSRLG TLQMFDILNV RRDSLVREFF VYLFKEAIIC VVEERKRSIG RLLGSETATQ
ASQTKGVLRL KGRIYIKHIK RVSDTSVMNE LSLTIDMEDE RLESFILLFN NRSSLEAWRH
TISGLVARYQ KPSPSARHTE YDEFGGRLGS PPITGKAARM LSGSSQGTDF TRSSVSAADS
ILATGSPRDT VSSSTSQNSG PYSIANGRLA KMPEEPEDGA SMHSRDYQGH PSPPVVSLVT
PHITSGPSNS LPALPHPAMD VILIISLPPP NATRSTADLK LRVIKTSLDF ILASLGGNDR
LSIVTFEVGM GGRVRKTPFL RVGRGQGGAR LAAFVSTIGE SYEEGREDVF AIRTGKDEKT
DVVTAVNHAL DNVLQRKQRN SISGMLLVSD APDSARRAQM DLVLARAEAA NIAIHSFGYG
RSHDPASLWL MSNHTSGTYT FVKEWYDLRD CLAGCLGGMM SIGLNHMKMH LKVVDGHRFR
IRKVAGVTGA ILSSDGRNVD IELGEIRYGE KKEMLVELDL DNTEDTNGRA GAGQSRGPMN
GTDQYMQRLG IDSLSLSDSP SDLVDGIMDR MIDEVPVFEL DGSFFDPQAG KSVSRLAHPV
LLTVTLLPSP GSRPRTPSTP SDPVIVRRRM ELLASDMITR TLVLASKKNF PQASKILSET
KRILNTVLQN ITTGLPPPSS NGSTIRNRKE VLTLSAVRAL QSILQDIQTL SEALEENVQG
FAFDQRNFGA QQAMILRDQK SWTGRTATEH LFWTIDNSIE LFSRSTDWVG RE
//
