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Database: UniProt
Entry: A0A3M6VAG7_9STRA
LinkDB: A0A3M6VAG7_9STRA
Original site: A0A3M6VAG7_9STRA 
ID   A0A3M6VAG7_9STRA        Unreviewed;      1138 AA.
AC   A0A3M6VAG7;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=HP domain-containing protein {ECO:0000259|PROSITE:PS51089};
GN   ORFNames=DD238_006349 {ECO:0000313|EMBL:RMX63734.1};
OS   Peronospora effusa.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Peronospora.
OX   NCBI_TaxID=542832 {ECO:0000313|EMBL:RMX63734.1, ECO:0000313|Proteomes:UP000282087};
RN   [1] {ECO:0000313|EMBL:RMX63734.1, ECO:0000313|Proteomes:UP000282087}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R14 {ECO:0000313|EMBL:RMX63734.1,
RC   ECO:0000313|Proteomes:UP000282087};
RA   Fletcher K., Klosterman S.J., Derevnina L., Martin F., Koike S.,
RA   Reyes Chin-Wo S., Mou B., Michelmore R.;
RT   "Comparative genomics of downy mildews reveals potential adaptations to
RT   biotrophy.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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:RMX63734.1}.
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DR   EMBL; QLLG01000370; RMX63734.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M6VAG7; -.
DR   STRING; 542832.A0A3M6VAG7; -.
DR   VEuPathDB; FungiDB:DD237_006711; -.
DR   Proteomes; UP000282087; Unassembled WGS sequence.
DR   GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0007010; P:cytoskeleton organization; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   CDD; cd11290; gelsolin_S1_like; 1.
DR   CDD; cd11292; gelsolin_S3_like; 1.
DR   CDD; cd11293; gelsolin_S4_like; 1.
DR   CDD; cd11288; gelsolin_S5_like; 1.
DR   CDD; cd11291; gelsolin_S6_like; 1.
DR   Gene3D; 3.40.20.10; Severin; 6.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   Gene3D; 1.10.950.10; Villin headpiece domain; 1.
DR   InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR   InterPro; IPR007123; Gelsolin-like_dom.
DR   InterPro; IPR025714; Methyltranfer_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR007122; Villin/Gelsolin.
DR   InterPro; IPR003128; Villin_headpiece.
DR   InterPro; IPR036886; Villin_headpiece_dom_sf.
DR   PANTHER; PTHR11977:SF51; PROTEIN FLIGHTLESS-1 HOMOLOG; 1.
DR   PANTHER; PTHR11977; VILLIN; 1.
DR   Pfam; PF00626; Gelsolin; 6.
DR   Pfam; PF13847; Methyltransf_31; 1.
DR   Pfam; PF02209; VHP; 1.
DR   PRINTS; PR00597; GELSOLIN.
DR   SMART; SM00262; GEL; 6.
DR   SMART; SM00153; VHP; 1.
DR   SUPFAM; SSF55753; Actin depolymerizing proteins; 6.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   SUPFAM; SSF47050; VHP, Villin headpiece domain; 1.
DR   PROSITE; PS51089; HP; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000282087}.
FT   DOMAIN          916..977
FT                   /note="HP"
FT                   /evidence="ECO:0000259|PROSITE:PS51089"
FT   REGION          741..769
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          787..916
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        741..763
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        790..818
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        839..857
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        865..910
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1138 AA;  123977 MW;  F8A1CB7345D02E88 CRC64;
     MTTENAFREA GKKAGLEAWR IVDFKPIVVP STEQHKLYSG DSYIFLKTNE TSTGLTRHIH
     FWLGKDSSMD ESGVAAYKTV ELDDSLGGVP VQHRECQGYE SPLFLSYFKA TGLQYLKGGV
     ASGFNEVKRD EYVTCLYRIK GKHTARVEQV PLQSSSLNVD DAYVLDAGLD LYVYAGKEAN
     RLEKAKALEF VSKTREARGG RPNVTFIDEE PKNAAFWKAL GGFTTVTRSG VSDEYYENAV
     KKNTTVLRVS GSGDDNVQVA DVTPSSGVLT KDMLKTENVF IIDVGNEVFV WVGKAASESE
     RKNALAIAVH YLKKEGRPSH TPITRVVEEG ETPVFTLLFK AWTEPKVLKF GYQLSQGVAR
     MQNDKQVDVK EMVKSALQSE EDIGVDPNGD GKHEVTVWRI EELAKVGVPK EQYGHFYNGD
     SYIVLHVVTP SSGKPTQVIY FWQGRSSTTD EKAASAILST FLDDSLGGAP VQVRVTQGKE
     PAHFRALFNG RMIVHAGGKA SAFANRDDED SYDTDGVLLY QVKGTSAKNT MAVQVDEKAS
     NLNSGDCFVL VTPSMVYEWQ GAGSSSAERE IASKIASILK KSRETEVVEE GSEAKEFWDF
     LGGKGEYATS KLSFETPHDP RLFQCSNSYG YFDAREIVNF AQDDLNTDDV FILDTFTTLY
     VWIGAGANES ERREAMSLAE KYLAVVQSDG RGKGTSIVAV HCNSEPLMFT SNFLAWDNEF
     FTKSEFLDPY EARLKKLKAE KEKNTPKDLP GTVTNEKIRE KETPTSAPVA AKAVPVLPLN
     AHVPEAAPIS SETTPASPKA APISSKATSA SIKAAPISSK ATPASPKAAP ISSKATPASP
     MAAPISSRAT TTSFEAMPAS PKAAPISSKA TTASFEATPA SPMAAPVSST ATSASIKPAP
     GSSRATSVPT AGKATGRAGE TFSYEQLKAG VEGIDITVKE NYLTDAEFQT VMEMSKDEFA
     KLPKWKKQAK KKETVTQLET VLLGPKLAPF TPSGDGVLSH ALDLLALTEK DVLFDLGCGD
     ARILVHAADK TGARCVGVEY NEDLVKRALT RVEEHGVKEL VDIRHGDALK VDLTTATAMF
     LYLVPQGIKM LLPKLEEARE LHVRIVTYVF SIPGWKPDDQ RIYKGTRVYL YNSPATQH
//
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