ID F8MKP2_NEUT8 Unreviewed; 1161 AA.
AC F8MKP2;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=von Willebrand and RING finger domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=NEUTE1DRAFT_130007 {ECO:0000313|EMBL:EGO58270.1};
OS Neurospora tetrasperma (strain FGSC 2508 / ATCC MYA-4615 / P0657).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=510951 {ECO:0000313|EMBL:EGO58270.1};
RN [1] {ECO:0000313|EMBL:EGO58270.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FGSC 2508 {ECO:0000313|EMBL:EGO58270.1};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Ellison C.E., Stajich J.E., Jacobson D.J., Lindquist E., Lapidus A.,
RA Foster B., Aerts A., Riley R., Grigoriev I.V., Taylor J.W.;
RT "Massive changes in genome architecture accompany the transition to self-
RT fertility in the filamentous fungus Neurospora tetrasperma.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; GL891304; EGO58270.1; -; Genomic_DNA.
DR RefSeq; XP_009851323.1; XM_009853021.1.
DR AlphaFoldDB; F8MKP2; -.
DR GeneID; 20825375; -.
DR KEGG; nte:NEUTE1DRAFT130007; -.
DR VEuPathDB; FungiDB:NEUTE1DRAFT_130007; -.
DR HOGENOM; CLU_006368_0_0_1; -.
DR OrthoDB; 663280at2759; -.
DR Proteomes; UP000008065; Unassembled WGS sequence.
DR CDD; cd16448; RING-H2; 1.
DR CDD; cd01466; vWA_C3HC4_type; 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; 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 Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 130..176
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 432..553
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 623..796
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT REGION 1..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 997..1040
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..224
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..278
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..580
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1002..1016
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1017..1040
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1161 AA; 126641 MW; E1D40EF9E9C1E047 CRC64;
MFSRLHSKHK GHSKEQQNRR PPDHQASTLH DLGMLGPSST SILSASGGSR RPDFDRSNHS
YHNHSSVPAR QYPATSYSER DSPIPNGHLG AQSHYSLVTP NSPSQSREST MMNSNASRGR
RERTFVGSEC AVCEEPLEHT LQGERILQFS CTHVSHEACF YEFIREFESQ FCPTCNAPLH
LDTSRGGNVL DIEKISSMVR SVSVNDTRSP PAPTPAPAPA PAPSQQPWDD QLARAPSRAS
SARQDGGLAP HTMARVSQRD SRDAPSSSDH RYTPNSRHAR SDSETTGATG GMASSGGYPE
TMQSGPPRRH DYDVQAMETS ISSPPRAITR NPIPAPTVTI RSEFPTISKS RQQQTLTCLV
TVEVPDNKWR PDPEDLQNGQ PMLPPSRAEE PYPRAPSPAR SVPRFYPYES PEVLAEMTEN
LRSRVDNWHG LDFSRFGKLR LYGTLRVGKD KVSWQELECF LFAEMLICVK EKKNVPSAPG
QWEDEAARKT GRCTLKGSIL IKKHLNGVSE TGSVDENILT LSLSVNELPQ FHLRFENRNQ
LKLWQQALLD LNAVETSPMR SPEYDREFSE ADEDEWNRSA GSKQRVSSQA SSWGGARSAT
TAPTEYTNVR SPGLLPSIHV PVDVVVVVPI SASMQGVKIN LVRDALRFMV SSLGDRDRMG
LVTFGSSGGG VPVVGMTTKA WPGWSNVLAS VKPVGQKSHR ADVVEGANVA MDLLMGRKYN
NPIATIMLIS DASTSDADSV DFVVSRAEAA KITIHSFGLG TTHKPDTMIE LSTRTKASYT
YVKDWMMLRE CLAGCLGAMQ SLSHQNVKLK LKLPEGSPAK LGKISGALQI TKRATGRDAE
ANLGDLRFGD KRDVLVQLTI MPDTSSEEPQ SHAYWDTVVS GLEAIGGPMD DEDQRAMSVE
EVPLIQADLS WGDILREGAT QHTRPSLLAI TMLPATPGSK KHWTASPAIP PHPYIVQRRM
EILTSDMLTR ALTLVSRGQH DRAHTLLSET RSILKGLGKG GLPPVPPAPG GPPTKSLPST
PLRTHSPIPA TPDRKNTPSP TMANHPMGLG GGFTISSRRS NDALGAMNTG ASAIDPTTVS
ALDAELESSL EWINHPAIFG RDSRKAVLQA IGVISSQRAF TFRTPIESLW AGRVSGIKKL
TEKSQEWTVE GGGEGGIMEE A
//
