ID A0A066X9B3_COLSU Unreviewed; 1139 AA.
AC A0A066X9B3;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Putative von Willebrand factor type A domain-containing protein {ECO:0000313|EMBL:KDN65547.1};
GN ORFNames=CSUB01_01109 {ECO:0000313|EMBL:KDN65547.1};
OS Colletotrichum sublineola (Sorghum anthracnose fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN65547.1, ECO:0000313|Proteomes:UP000027238};
RN [1] {ECO:0000313|Proteomes:UP000027238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT "Draft genome sequence of Colletotrichum sublineola, a destructive pathogen
RT of cultivated sorghum.";
RL Genome Announc. 2:E0054014-E0054014(2014).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KDN65547.1}.
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DR EMBL; JMSE01001025; KDN65547.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A066X9B3; -.
DR STRING; 1173701.A0A066X9B3; -.
DR eggNOG; ENOG502QTWJ; Eukaryota.
DR HOGENOM; CLU_006368_0_0_1; -.
DR OMA; SEAHWAQ; -.
DR OrthoDB; 663280at2759; -.
DR Proteomes; UP000027238; Unassembled WGS sequence.
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; 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; PS50003; PH_DOMAIN; 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:UP000027238};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 113..159
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 411..531
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 602..775
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT REGION 1..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 975..1028
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 981..998
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 999..1028
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1139 AA; 124455 MW; CAB0382A47B202AF CRC64;
MFARSRKGSK GFNFGPSSSK ESQGSHLLDF GLASPKLAPE PYRPGTSGTT RTNNTWTDAP
SFPEKTRGTG QRSTSSVRSG GSTHRRGDSY SSNNMASGAG RNRRERTFVG SECAVCEEPL
EHTLQGERIL QFSCSHVSHE ACFYEFIREF EAQYCPSCDA PLHLDTSRGG NVLDIANSVP
ATEKISSLVK SSHSSENRSN HTPTPTATQW DNPTPRPTSI ESNQRNMHST HTRENAPRSS
GRDRDGSQPA TSERYGPSRH ARSDSEATGV ASSGGYPETT QSGPPRRHDY DVQAMETTPG
SPRGITRNPI PAPTVTVRSE FPTINRSRQQ QTLTCLITVE VPDNKWRPDP EDLGSAPPGP
PAVNARIDDA FARPPSPARS APRFYPYESR EVLEEMTENL RNRVDNWHGL DFSRFGKLRL
YGTLRVGKDK QSWQELECFL FAEMLICVKE KKVPLAGQWD ENGMPKKAVR CTLKGSILIK
KHLNEVSETG NIDENVLTLN LSVAELPQFH LRFENRNQLK LWHQALLDLN AVETSPVRSP
VYDRGEFSET EEEDWQRLSQ QQRVSSVASS WGGPKSVTTA PTEYTNFQRS PTMPASIHVP
IDVVVVVPIS SSMQGVKINL VRDALKFMVN TLGERDRMGL VTFGSGGGGV PIVGMTTKAW
PGWGNVLSSI KPVGQKSHRA DVVEGANVAM DLLMQRKYNN PIATIMLISD ASTSDADSVD
FVVSRAEAAK ITIHSFGLGM THKPDTMIEL STRTKASYTY VKDWMMLREC LAGCLGAMQT
LSHQNVKLKL KLPEGSPAKF HKISGALQIT KRATGRDAEA SLGDLRFGDK RDVLVQLVIV
PDNTSQEQLP QDPWDNIVSG LEALGGTVDG DDQRVTSVEE VPLIQADLTW GDILRDGTLS
HLPRPSLLAI TMLPALAKQK NSWANSPPIP PHPHIVQRRM ELLTSDMLTR ALTLVSRGQH
DRAHTLLNET RSILKGLGKG GLPPIPPPTA PPNRSLPSTP HPGNDASPSF APDRKQTPSP
TQSANSSAIN GYPVAAIGRS RSNDGLGLGA GIDANTVAAL DAELESSLEW ISHPAVFGRD
SRKAVLQAIG VISSQRAFTF RTPIESLWAG RVAGVKKLTS KSREWRDEGG GEGGIMEEA
//
