ID A0A2G5B213_COERN Unreviewed; 1849 AA.
AC A0A2G5B213;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Actin-binding FH2 {ECO:0008006|Google:ProtNLM};
GN ORFNames=COEREDRAFT_83760 {ECO:0000313|EMBL:PIA13044.1};
OS Coemansia reversa (strain ATCC 12441 / NRRL 1564).
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Kickxellomycetes; Kickxellales; Kickxellaceae; Coemansia.
OX NCBI_TaxID=763665 {ECO:0000313|EMBL:PIA13044.1, ECO:0000313|Proteomes:UP000242474};
RN [1] {ECO:0000313|EMBL:PIA13044.1, ECO:0000313|Proteomes:UP000242474}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 1564 {ECO:0000313|EMBL:PIA13044.1,
RC ECO:0000313|Proteomes:UP000242474};
RX PubMed=25977457; DOI=10.1093/gbe/evv090;
RA Chang Y., Wang S., Sekimoto S., Aerts A.L., Choi C., Clum A., LaButti K.M.,
RA Lindquist E.A., Yee Ngan C., Ohm R.A., Salamov A.A., Grigoriev I.V.,
RA Spatafora J.W., Berbee M.L.;
RT "Phylogenomic Analyses Indicate that Early Fungi Evolved Digesting Cell
RT Walls of Algal Ancestors of Land Plants.";
RL Genome Biol. Evol. 7:1590-1601(2015).
CC -!- SIMILARITY: Belongs to the formin homology family. BNI1 subfamily.
CC {ECO:0000256|ARBA:ARBA00037935}.
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DR EMBL; KZ303550; PIA13044.1; -; Genomic_DNA.
DR STRING; 763665.A0A2G5B213; -.
DR OrthoDB; 1118745at2759; -.
DR Proteomes; UP000242474; Unassembled WGS sequence.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:UniProt.
DR GO; GO:0005938; C:cell cortex; IEA:UniProt.
DR GO; GO:0032153; C:cell division site; IEA:UniProt.
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 GO; GO:0051301; P:cell division; IEA:UniProt.
DR Gene3D; 6.10.30.50; -; 1.
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 PANTHER; PTHR47102; PROTEIN BNI1; 1.
DR PANTHER; PTHR47102:SF2; PROTEIN BNI1; 1.
DR Pfam; PF06367; Drf_FH3; 1.
DR Pfam; PF06371; Drf_GBD; 1.
DR Pfam; PF02181; FH2; 1.
DR PRINTS; PR01217; PRICHEXTENSN.
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 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000242474}.
FT DOMAIN 274..679
FT /note="GBD/FH3"
FT /evidence="ECO:0000259|PROSITE:PS51232"
FT DOMAIN 1176..1642
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT REGION 1..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 678..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 889..931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 967..1119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1131..1160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1502..1551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1795..1831
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 717..801
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1623..1650
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 10..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..94
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..697
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 988..1009
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1037..1109
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1135..1160
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1519..1533
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1801..1815
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1816..1830
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1849 AA; 204151 MW; 62A00BC4E765E155 CRC64;
MEFWKRKKGT PGTSQHNNSS GLTPVRISEP IHNIEVGGQF RSANNSTPPP PVGGGVFASS
PRSQGQTIGQ YQQSDDYNSG SDAEFRERYN SYRRQRRLSH TNSSARSSQL TATSDGGLTP
LATDSMMSQQ GPTVGVFNRQ WSHDSDTMQP LHRSGIADRQ LTPVSVGYAG DEQQGGLTKA
GVPGPPRGSL RSTRSAAIGR GVPGGAVATT PASGELQYGS LSMRGGSAAS RPGAFMSTGS
SMSVATTTTI NSAGSRRSGM TLGPANSGTG ELETENVSEE EINLMLGRLM DEMDIKDAQR
LQMQKMSIPN KLKLLKQQRQ LESFQMDSKG NAPEYFYRYL TETDIRSLPK QMLVHLRVCV
STQPVNWVKQ FVEIQGLEAL SECLGILNHA GMRKGDDITK EIEIIKCIKS VVNIQWGAQD
VLRYPTCVHN LSFSIDAPSL LTRRLISEIL TYICYLNVPT GHSTVLKGLD KLQKFREMQK
RFEPWMRALE AAVDGRGRMG SKVGASEELR QLGGTADRDL TDYVLSSMIF INAVVGVSDD
VEMRMHYRNQ LNVAGLSRIM KKLRSGFDSP LIALQINKFD KDAEQDHADV LDLYNQQIMQ
DMTDPEEVFQ AILAQIDDDD RAREHFLSIL QRLLLLRDDY ADATATGIEE HSNRANKARY
YQLLDEITTQ VVMDIRNGEP IDSDFDSDVD DGSRPRTRPG DGFTTQYGVS VAGIIDKFSN
EEQLEEAVRE SKDLREQLEK VTRQKNELEL EVSLKSEGLV GTLKTKIFAL EDLLRMSRHT
IEALQTQIKE LRDQFTQKLA KQDSQLKQLY SALQDEASEH DMLRRLKDDL TLENEVLHSG
IALEVSKDNP DHVVVNQELL LSEIERLKRQ RPELNRMTEA RQMLERILTE AGQGPSARKP
GVTKKSSERK TSLSGTAKDG GLISDTGLPE GAKVGTVTMD SVMSTPARLA DFASELEKKL
GGYKNHLGLQ PSTALETSPE TENVETAKDK QVQNNGELLG SNATVDSKTL AGADTDGGNA
IKSETEPSDT NAADDIPAAP PMPPSLGESP APPPAPPLPP SLGGTPAPPP APPLPPSLGG
SPAPPPAPPL PLSLGGSPAP PPAPPLPPMA GAGSGAGIKP TADALAEKLR SLGSGSPAPP
PPAPPPPPVA PPFGARVPGG VPAPPMPTFL GTLRRKELQY VPKVKLKALQ WDKLNDQNVE
GSMWLKLEDR AGLEEKYVLD TLHKSGTFES LEKLFAAKQA VDIFALREKR RKERESKRME
EITVLDSKRS YDVNILLGMM KKLSFRDIRR GLLRMDTSIV NENLLKQLLT FVPTPEERGM
LSAYQGRPDR KRLARAERFF METMKIWRYE QRLRVTTTWA AWPETFRDLQ SDIASVMTAA
HAVATSRHFP QVLEVVLSIG NFMNGSGFRG GAFGFKIASL NRLMDTKAED NKTTLLHFVA
ATVEESFPDA LEFLDELKPV DSGCRVSYTE MRAELGDMRV RLVEAKRELE LLREQREKEL
KEVAMENEKA TAAPPMDAAQ EDSEKKEEGA DAGDDSDSGS ESSAGAVTSA SDPHDRFLLT
IRRFVVEAEE QYESLSSQFT AMEEAYTNSM LLYGEEPRGT APEEFFGVFK TFTASFNQVH
RDNVRERERK RAAEKRRKHI EQQIEQKRMA KQNRAARLAT GASRIREQME AAEAIGNQEN
STASASANGG VAADENTAVS GTAGNLGAEN GAVDDLLKSL MAGTDLERVE ATKRRRRREL
MSIRRRSSVR RSIHRTSISI KALQMLRDIK EDEEDVDNLG IDELDENQRS IRAANRRSLL
RRHPNASERM STISEDDPTE NTNSASYADF DLTELRNARR RQRLEEEEE
//
