ID A0A024G8M9_9STRA Unreviewed; 1719 AA.
AC A0A024G8M9;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=FH2 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BN9_036590 {ECO:0000313|EMBL:CCI42875.1};
OS Albugo candida.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX NCBI_TaxID=65357 {ECO:0000313|EMBL:CCI42875.1, ECO:0000313|Proteomes:UP000053237};
RN [1] {ECO:0000313|EMBL:CCI42875.1, ECO:0000313|Proteomes:UP000053237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ac Nc2 {ECO:0000313|EMBL:CCI42875.1,
RC ECO:0000313|Proteomes:UP000053237};
RA Gardiner A., Kemen E., Schultz-Larsen T., MacLean D., Van Oosterhout C.,
RA Jones J.D.G.;
RT "Recombination and specialization in a pathogen metapopulation.";
RL Submitted (MAY-2012) 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:CCI42875.1}.
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DR EMBL; CAIX01000040; CCI42875.1; -; Genomic_DNA.
DR STRING; 65357.A0A024G8M9; -.
DR InParanoid; A0A024G8M9; -.
DR OrthoDB; 5491073at2759; -.
DR Proteomes; UP000053237; Unassembled WGS sequence.
DR GO; GO:0071203; C:WASH complex; IEA:InterPro.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR Gene3D; 1.20.58.2220; Formin, FH2 domain; 1.
DR Gene3D; 1.10.238.150; Formin, FH3 diaphanous domain; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR015425; FH2_Formin.
DR InterPro; IPR042201; FH2_Formin_sf.
DR InterPro; IPR010472; FH3_dom.
DR InterPro; IPR014768; GBD/FH3_dom.
DR InterPro; IPR010473; GTPase-bd.
DR InterPro; IPR027649; Inf2.
DR InterPro; IPR019309; WASHC3.
DR PANTHER; PTHR46345:SF8; FORMIN 3, ISOFORM B; 1.
DR PANTHER; PTHR46345; INVERTED FORMIN-2; 1.
DR Pfam; PF10152; CCDC53; 5.
DR Pfam; PF06367; Drf_FH3; 2.
DR Pfam; PF06371; Drf_GBD; 1.
DR Pfam; PF02181; FH2; 1.
DR SMART; SM01139; Drf_FH3; 1.
DR SMART; SM01140; Drf_GBD; 1.
DR SMART; SM00498; FH2; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 1.
DR PROSITE; PS51444; FH2; 1.
DR PROSITE; PS51232; GBD_FH3; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000053237}.
FT DOMAIN 211..694
FT /note="GBD/FH3"
FT /evidence="ECO:0000259|PROSITE:PS51232"
FT DOMAIN 1224..1641
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 753..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1071..1100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1257..1279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..596
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..777
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1071..1091
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1719 AA; 194479 MW; D3B268C7A5853CD5 CRC64;
MWRRRSSLNT NPNPREKEST RASLSALPSS LSFGLHTSSR RRSIYSNDPR VTKERPLIFT
IDVPTSGPLG IDLQARHVEK GKPQRGAIVR GFRLLDGTTK GYVESSGRVK IGDILQMMHE
LHLDDLPFEQ IINYAMQMQK DPSVWPLRLE FRRNPPNFSA NQESHSKSRI SDFFSLNPAQ
DSNFNEKLQY FRGFFANRIP TSNSAKIKER PPMPKEETVN EMYRDLLIKR RVPDDVMDEL
VRIEPIDNKW NIVWCAQQHE NDEDKPQLNI AEAARMAESL VELKWDSKGV KELEQLVIKI
STNSIEWAGS FLDHFGLDYL TMKLPDPSPY SIEINKFDKA VNFCKVLLRV LRSLTHFTTG
IEALISIPGL VKKVALCFHT DDVELKKQTL QFLGIICYNS AAGHGAVIEA FDHYQEAKGE
AIRFSCLRDA LKSARYSLAF KEDVLSFINI IVNKAIRLED RLAIRGDFMA LKMAGYFEQV
RAKSVAVQRQ TNHRRNSCES VMEGCRTPQE HLHSASVPRT PAIMTPPAIK VESGFGPVAK
DVVVSPGHVT PVTTGGSSQS VGHGVGTPRE ENHSNGARGS IVSDSNGETT NSDNSVEQLR
SQLDNMEKQI EVFEAFMEDD RKDTIYETTD LSSHQSIFDR LMQSAASDNE LQEYFLSILQ
QLLFYPADRI IGKEMWALSE RLIRQVSLLA PVEEVREFKM SYDDRKLVLQ LRDRYTEFLE
KYTSENPSIE YHPGPIILLS NKELYHDYEE ESLIDGEEGE TDSDHSSSQQ RDENMQVAAE
DHPDLAKYFK LLKLGMARSH VEMQMRVDGV QSFESEILET PDRLVSFKTT ETQNEMAKTH
VSMESIACGN HVKAKDHPKY AKYLKLLAFG MPQEHVAQKA EAEGVDSTIL QTPDAMVDSD
GKIVVIDKAG SDNAFMKEVP EIAKYAKLLK TGMPLDQARA TAEAEGLNPA FLNSPDIEQP
DVSSDSSKNA FRLAKNYEHY AKYFDMIQNG TPMDEIVAEM KRNDLDPNIL TCPNACVDVK
GNRVDGNKKG IQVCEHEKYA KYFKLLKLGM PKEQIKMKAF ADGVNGDFLD SPETRLDETG
NPVDEIKHNR DTSSSVPPSS NLTVKGHVKY AKFFKLLRMG MPMEQVKLKM SAEGFDAEIL
TSPEAPVDAD GNIIGAIVPD TTAHRARDHP EYAKYFKLQK MGMPRQQLEL RMAAEGLDAK
YLDLPDEIVT TKAPALRKKS PSPTKTPIKT KPKLRNLYWE TLSNECTAGT IWDKLQPISS
KNGDMKKTPS PSDKSSQSEN IAHYIDKLTT LFVNEPPPKK ALRKTTSRRR APTRIALIDV
KRANNIGIML ARFRLPYDRI REAVLQVDKE VLYAERVAAL LQFAPNETEL TAIKAYKGDP
KLLGDAEQYF FEMQNVPRLK TRLQAIHATW QFDSYTEDQR KLMETVCTAC QEVKACADLG
QIFEIILSLG NRLNDGTARG GAKAFRLDTL LKLGQVKASD NSITLLNYTA SILRLKDPSI
IHFDEKLKSV EAASRLTMQM LNAGDAVIHK AAKLIVSELQ QHAKLPDISE NDGFQAIIGP
FAEHADRISQ ELRQSLDEMK QMFEETVRFF GEDPTSSDCG PNSFFSVITS FAKLLQSADR
DNERKRIAEE RRVRREEATR KRMEELHRRK QARIDEADVV AHLKDDEEQH LVSLKEGDVE
EIMKRIRQKR VAEKREEILA KSFDSFSSSE AVEPHFEST
//
