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Database: UniProt
Entry: A0A075AT29_ROZAC
LinkDB: A0A075AT29_ROZAC
Original site: A0A075AT29_ROZAC 
ID   A0A075AT29_ROZAC        Unreviewed;      1067 AA.
AC   A0A075AT29;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Actin-binding FH2 domain-containing protein {ECO:0000313|EMBL:EPZ31653.1};
GN   ORFNames=O9G_000132 {ECO:0000313|EMBL:EPZ31653.1};
OS   Rozella allomycis (strain CSF55).
OC   Eukaryota; Fungi; Fungi incertae sedis; Cryptomycota;
OC   Cryptomycota incertae sedis; Rozella.
OX   NCBI_TaxID=988480 {ECO:0000313|EMBL:EPZ31653.1, ECO:0000313|Proteomes:UP000030755};
RN   [1] {ECO:0000313|EMBL:EPZ31653.1, ECO:0000313|Proteomes:UP000030755}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CSF55 {ECO:0000313|EMBL:EPZ31653.1,
RC   ECO:0000313|Proteomes:UP000030755};
RX   PubMed=23932404; DOI=10.1016/j.cub.2013.06.057;
RA   James T.Y., Pelin A., Bonen L., Ahrendt S., Sain D., Corradi N.,
RA   Stajich J.E.;
RT   "Shared signatures of parasitism and phylogenomics unite Cryptomycota and
RT   microsporidia.";
RL   Curr. Biol. 23:1548-1553(2013).
CC   -!- SIMILARITY: Belongs to the formin homology family. Diaphanous
CC       subfamily. {ECO:0000256|ARBA:ARBA00008214}.
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DR   EMBL; KE561209; EPZ31653.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A075AT29; -.
DR   STRING; 988480.A0A075AT29; -.
DR   EnsemblFungi; EPZ31653; EPZ31653; O9G_000132.
DR   HOGENOM; CLU_002356_1_0_1; -.
DR   OMA; MMPGFSP; -.
DR   OrthoDB; 1331417at2759; -.
DR   Proteomes; UP000030755; Unassembled WGS sequence.
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; 1.20.58.630; -; 1.
DR   Gene3D; 6.10.30.50; -; 1.
DR   Gene3D; 1.20.58.2220; Formin, FH2 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; IPR014767; DAD_dom.
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   PANTHER; PTHR45691; PROTEIN DIAPHANOUS; 1.
DR   PANTHER; PTHR45691:SF6; PROTEIN DIAPHANOUS; 1.
DR   Pfam; PF06367; Drf_FH3; 1.
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; PS51231; DAD; 1.
DR   PROSITE; PS51444; FH2; 1.
DR   PROSITE; PS51232; GBD_FH3; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030755}.
FT   DOMAIN          36..386
FT                   /note="GBD/FH3"
FT                   /evidence="ECO:0000259|PROSITE:PS51232"
FT   DOMAIN          592..999
FT                   /note="FH2"
FT                   /evidence="ECO:0000259|PROSITE:PS51444"
FT   DOMAIN          1010..1038
FT                   /note="DAD"
FT                   /evidence="ECO:0000259|PROSITE:PS51231"
FT   REGION          506..563
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1031..1051
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          918..952
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        507..563
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1067 AA;  121139 MW;  DA7D0D64A37DBEE9 CRC64;
     MGHKFSKASK QKLKVASTNS LNSFGTGSKF QASPVEPMPP IEELESEFGQ FLKELALPQE
     KFEAMSQFDV NKKWMIVQQE RAKKKMQTAN VKSDIRTPGQ FVDLLKSYSF TTDFAKDLQT
     LEVLMRTEAI SWVKEFISKG GVLEFYDMVQ RECQHQMIRI LKALMNNSNG LNVMMTTKRA
     VNILCLCLDC DNLKIKAIVL QLLAAVCFVP NGHVKVLEGM HEFSLIKKEK TRFMNIVTDM
     WRDDIEYQIA CMIFINAIVN IVEDATFRLN LRQEFISLGL NDHLERLGKL KDESLVTQLT
     YFMDEDIEDK KVIGLEYNIN ELDISTIDKV INLIETNFKE PYQLSLVHQI LIQILLLPFE
     NNDRTFYLTI GLSFLKDLVY QSQGKESNGV PSFHFDTNAL LTEIKLIEKN KTEQAQAKKE
     KKQLPKTPCK IQVKGRFIEI PSELNSEETL NFIKPLVEKI LSEEDAKNSN KSPPQIETSI
     TLDIPLPPLN TPSIPQANTN VASELKTIPP PPEPPMSSSI PPPPLMPLTP GVSVVPPNDS
     SIPPPPPPPM APGMPPPPPP MMPGIPPPPM TPGMPPPPGM PSIGVAKMGL PNKKKVVPSI
     KMKPLQWNKV PNSNVEKTIW KSMDAEEKIR KMIDLKEFEL SFGATVTSPV SPVGNAGKVD
     EVEKKKSVSV LEPKRAYNLC KEYFEIKLAI MLSRIKMTFP EVKEAILRVD EEKITEQMIK
     QFLNFIPTQE ETGLLMEYEN SSEQLEKADQ FFIQMIKIPR YEQRLNCILY KFRFQERYKE
     LKPDLDAVIN ASNEVMKSKM FSQILEIILT LGNYMNGDSF RGGAYGFSID TLNKLNDTRS
     SNGKGTFLHY LVNLLETKFS NTLDFPKELS NVEAACRVSI SSVMQEVSEM VKGMKQIESE
     IETLNESSSE EDCFHKVFKN FHQSNENKIK ELENLKQEME NSFQKCVEYF NEDPKSSTPE
     TFFPFFWNFI QNKTRKELAL NAKKVELKKS RSKLSVNGNS NTNLNASMEE DRRGVMDELI
     SSLRTGDAFK AKSKRRRTVN SKDNPNASST DMLALNATEL LATIQND
//
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