ID A0A3D8R4W5_9EURO Unreviewed; 1136 AA.
AC A0A3D8R4W5;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=von Willebrand and RING finger domain protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=DSM5745_08853 {ECO:0000313|EMBL:RDW69093.1};
OS Aspergillus mulundensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1810919 {ECO:0000313|EMBL:RDW69093.1, ECO:0000313|Proteomes:UP000256690};
RN [1] {ECO:0000313|EMBL:RDW69093.1, ECO:0000313|Proteomes:UP000256690}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5745 {ECO:0000313|EMBL:RDW69093.1,
RC ECO:0000313|Proteomes:UP000256690};
RX PubMed=30018880; DOI=10.5598/imafungus.2018.09.01.13;
RA Wingfield B.D., Bills G.F., Dong Y., Huang W., Nel W.J.,
RA Swalarsk-Parry B.S., Vaghefi N., Wilken P.M., An Z., de Beer Z.W.,
RA De Vos L., Chen L., Duong T.A., Gao Y., Hammerbacher A., Kikkert J.R.,
RA Li Y., Li H., Li K., Li Q., Liu X., Ma X., Naidoo K., Pethybridge S.J.,
RA Sun J., Steenkamp E.T., van der Nest M.A., van Wyk S., Wingfield M.J.,
RA Xiong C., Yue Q., Zhang X.;
RT "IMA Genome-F 9: Draft genome sequence of Annulohypoxylon stygium,
RT Aspergillus mulundensis, Berkeleyomyces basicola (syn. Thielaviopsis
RT basicola), Ceratocystis smalleyi, two Cercospora beticola strains,
RT Coleophoma cylindrospora, Fusarium fracticaudum, Phialophora cf. hyalina,
RT and Morchella septimelata.";
RL IMA Fungus 9:199-223(2018).
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:RDW69093.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PVWQ01000011; RDW69093.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D8R4W5; -.
DR STRING; 1810919.A0A3D8R4W5; -.
DR OrthoDB; 663280at2759; -.
DR Proteomes; UP000256690; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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:UP000256690};
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 622..795
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 995..1042
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..304
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1015..1042
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1136 AA; 125540 MW; 30CA8E3A6A7FCC6B CRC64;
MWKHRPPSRS DSKSGTVDSG ERGFFGWSKK KTPHSSARPE SPARSPLRPF RSFSRSDRAD
TGFSSYTAGS RARAPSSVTA DSYYSDVPRS TAQFSAYSNH TVARTASHET FNNTPVGPMA
GLMDVDRSRT RRERTFVGSE CAVCEEPLEH TLRGERVLQF SCAHVAHEAC FYEYLREIEG
QYCPTCDAPL GLDSTRGGNV LDIVRSVNSD AMTQRSGLTT PTPWDSVTSR QHSVSEAGSR
PYPTSDAGSR PYPPSDVGSR PYPQSDAGSR PYNRDSRDTY GNRRDSKDTG IQRERIERLA
SVSRHHSRNG SAAGSSGEYH EGRRHDYDVQ AMESDLSPRT THITKNPIPA PTVTIRSEFP
TVNRSRQQQS LTCLITVEVP EGNWYPDTDD LRTGSTKDEP YPSRFPSVPE KFAPFEPQEN
LNEIAEELRA KVDNWHGLEF QRFGKLRLHG HMRVGKDRES WQDLECYLFH EMLICVKEKR
VPDHHYDPQM VKPRPRYTLK GSILIKKHLK HIEDVADEPI LTLHLSVSEL PCFYLRFPNR
SQLEIWRRAL ENNNLESLRS PELDFDRHSG MEEDDYRTGN MKRQASLNSS HGAARSNNTA
ITDYTNMGVE GALSPSIHIP VDIVVVIPVS SSMQGLKITL LRDSLKFLVH NLGPRDRMGL
VTFGSSGGGV PLVGMTTKSW GGWSKILSSI RPVGQKSLRA DVVEGANVAM DLLMQRKSSN
PVSSILLISD SSTSDPESVD FVVSRAEAAK VGIHSFGLGL THKPDTMIEL STRTKGSYLY
VKDWMMLREC VAGCLGAIQT TSHQNVKLKL RLPEGSPAKF VKISGALHTT KRATGRDAEA
ALGDLRFGDK RDVLVQLVIP PDNVTHESAP QDPWESLVSG LEALGGGSDG DDQRILSVEE
VPLIQADLTY GDLLRDGHLQ HSPRPSLLAI TMLPPNPRYK GARPSTPPIP PHPSIVQRRM
ELLTSDMLTR SLTLASRAQH DRAQHLLNET RSILKGLGKG SLPPLPPPAS KGSAEPESRG
QTPTSDSPKS STFASHSSAA SDAATITPVA AVDAHTMTAL DGDLQAALEW INHPAVFGRD
SRKAVLQSIG VISSQRAYTL RSPSEAHWAQ RIAGVRRLIE RSKDWRETGD DALTEE
//