ID A0A0D1WLF4_EXOME Unreviewed; 1157 AA.
AC A0A0D1WLF4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=RING-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PV10_07196 {ECO:0000313|EMBL:KIV89825.1};
OS Exophiala mesophila (Black yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=212818 {ECO:0000313|EMBL:KIV89825.1, ECO:0000313|Proteomes:UP000054302};
RN [1] {ECO:0000313|EMBL:KIV89825.1, ECO:0000313|Proteomes:UP000054302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 40295 {ECO:0000313|EMBL:KIV89825.1,
RC ECO:0000313|Proteomes:UP000054302};
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 Exophiala mesophila CBS40295.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN847524; KIV89825.1; -; Genomic_DNA.
DR RefSeq; XP_016221399.1; XM_016372067.1.
DR AlphaFoldDB; A0A0D1WLF4; -.
DR STRING; 212818.A0A0D1WLF4; -.
DR GeneID; 27325041; -.
DR VEuPathDB; FungiDB:PV10_07196; -.
DR OrthoDB; 663280at2759; -.
DR Proteomes; UP000054302; Unassembled WGS sequence.
DR CDD; cd16448; RING-H2; 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; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
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 Pfam; PF00092; VWA; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00327; VWA; 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 Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Reference proteome {ECO:0000313|Proteomes:UP000054302};
KW Transferase {ECO:0000256|ARBA:ARBA00022676};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 141..187
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 639..815
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT REGION 1..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1015..1071
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..598
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1157 AA; 127585 MW; 2D153A0FFB5A3836 CRC64;
MSKHDLPSSS NKEEGEITEQ ALYELGLLNR HPRPGSRVTR PPETDKVAHY QPSRARNGNY
NSRTLSHSGS VQTPNFKQSS ISSGTLGRPR TPTDPRPRTR DRRGPPSPST SIPGAGHPMA
GMLDSDRSRS RRDRTFVGGE CAACEELLEH TLRGERVLQF SCGHVAHEAC FYEYIRDSDT
QYCPTCEAPL GLDSFRGGSI LDLTKLSNLV RAVAQKEVTS PRSTATTPMP WDRQTLQDDS
VSAREGGQRH SRDNSNRNSR DSQRLRIERL GVGLTSPPAQ QPQSILPPRE GREGSLQNGS
QHGPLSHIRT DSGNTSNDYT NDHAHSRKHD YDLHAMETTV PSPHMRQVTQ PIPFPTVTVR
SEYPTLTRSH QQQTLTCLVT IEVPESKWQP QFDEVQTTPP VPALPSDPGR GSSKTRQDIP
QPTAPVESPE VLEEITEELR NRVDNWHGLE FQRFGNLRLH SVIRVGKDRH SWQELECYLF
GEMLICVKEK KNGQGSVISE SSRKLSRCTL KGSILIKKHL RQVHASPDEN ILTLNLSVAE
LPTFHLHFSD RSQMEQWQRS LRNLHSSEPV SQLPTDYEQD TSGTDDEEFG RRHQGERRIP
SVASSYGAPK SATTAATEYS LHRPPTDKRM PTSLHVPVDL VVVIPVSSSM QGLKITLLKD
TLRFLVNSLG DRDRMGLVTF GSSGGGVPVV GMMGKQWSGW NKILNSIRPV GQKSLRADVV
EGANVAMDLL MQRKAENPIG TILLISDSST SESDSVDFVS QRAEAAKVGI YSFGLGLSHK
PESMIELSSR TKASYLYVKD WMMLRECAAG VLGSLQSISH QNVKLRLKLP EGSPAKFVKI
SGALQTTKRA TGRDAEAALG DLHFGDKRDI LVQLVIDPDS SSQEPAPQDP WESIVSGLEA
LGGPLDNEDA RVQSVEELPL LQADLHFGDF SRDGSVAHLS RPSLLAITML PANPRARQNG
RASTPPIPPY PHIVQRRMEL LTSDMLSRAL TLVARGQHDR AAHLLNETRT ILKGLGKGGL
PPLPPGAAQP AHKHNSPTVK ARSPRAATPD HARDQSPHSD TSSSTPIPRN AGVDQSVMSA
LDADIESSLE WIGHPAVFSR DSRKAVLQAI GVISSQRAYT FRSASESIWA ERVAGVKRLT
ELSREWRETV DDALTEE
//
