ID A0A094B4Q9_9PEZI Unreviewed; 1587 AA.
AC A0A094B4Q9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=FH2 domain-containing protein {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=V494_06616 {ECO:0000313|EMBL:KFY34618.1};
OS Pseudogymnoascus sp. VKM F-4513 (FW-928).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420907 {ECO:0000313|EMBL:KFY34618.1, ECO:0000313|Proteomes:UP000029288};
RN [1] {ECO:0000313|EMBL:KFY34618.1, ECO:0000313|Proteomes:UP000029288}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4513 (FW-928) {ECO:0000313|Proteomes:UP000029288};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the formin homology family. BNI1 subfamily.
CC {ECO:0000256|ARBA:ARBA00037935}.
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:KFY34618.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JPJW01002193; KFY34618.1; -; Genomic_DNA.
DR STRING; 1420907.A0A094B4Q9; -.
DR HOGENOM; CLU_001313_1_0_1; -.
DR OrthoDB; 1118745at2759; -.
DR Proteomes; UP000029288; 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; 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; 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 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|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000029288}.
FT DOMAIN 273..702
FT /note="GBD/FH3"
FT /evidence="ECO:0000259|PROSITE:PS51232"
FT DOMAIN 1111..1532
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT DOMAIN 1551..1583
FT /note="DAD"
FT /evidence="ECO:0000259|PROSITE:PS51231"
FT REGION 1..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 891..937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 949..1110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1252..1271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1538..1587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 726..789
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 897..916
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 917..937
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1000..1095
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1540..1554
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1587
FT /evidence="ECO:0000313|EMBL:KFY34618.1"
SQ SEQUENCE 1587 AA; 176461 MW; 24A72A6283C6BE6F CRC64;
MSGSDSKARQ SSGGKSFFSR GKKERRQGSD EFLGSEFQDK GSVASRTSRH ARGISIASVD
QLPSPTTDSM SGVISSMPYD HAPDGRSPIP VDYLPRGDQM PMRREPQPHH LNMGGSDYHQ
YPGFDASSIQ NQQQNSPHVL SGPRPPPNSS NVTMASTGNR TTQLQQWGPG GSGRPGSSNA
NHNPRYDSYS TYSTNNSAVY PRQSFDQQSI GSAAERASVF SSNGSSRTVQ PSSSQVSLAP
SQSSSRDSHR TNKPPYHRPD TMMQSSPSNF DVTKPADERV IEQQFLALMQ KRGWHNLPDQ
ARRQMLAYPP GKKWTLVYQD RLTEWQGEQK RRTTARQSGI YGQAEVMLAN ADEEGTPEWF
VRKVMDNSIT QKQLASLAVS LRTQPISWVK TFVECQGQVA LTNVLGKINR RQANGPAPVD
GNTSDKDLDR EYDILKCLKA LLNNKYGADD ALHHQQVIVA LATSLISPRL TTRKLVSEML
TFLCHWGEGE GHLRVIQAMD HVKNQMGENG RFDAWMRIVE VTIDGRGKMG SLVGASEEVR
SGGIGMENLL MEYAVATLVL LNMTIDAPDK DLQLRVHIRA QFTACGIKRI LTKMEGFQYE
YIDKQIEKYR QNEAIDYEDL LERENSSMKD GEEPEIQDLS DPTQIVNAIM QKVNGSRTQD
YFVSALQHLL LIRDNDGEER LRMFQLVDSM LSYVAMDRRL PDMDLKQSLN FTVQSLLDKL
HTDSEARQAL DEAQEARQVA DAAMAERDEA KAQIELGADG LVAKLQKQLD EQAQVIEVQR
RQADGLKSEL ENMHSVRAKE AQRNELETRE LYLMLRDAQD IAASSGAKNG LGENDPQHMK
GILDRERLMD RLEMQLQRQK TQYKLEGRVW GADNGPSDRL RALREEMDGG DAILGSTQPR
DLTNSMLGSV SRSTRIQRKP VDSHALAESD REDEEAVFEK PRVVELRRPK VQGSKAVPAA
GASEDEDDGI TTGPSHPSLE SESPKTPSDE DAQKTNAAGF TGPPPPPPPP PPPMPGQAAA
GFNGPPPPPP PPPPGMPGAG FNGPPPPPPP PPPGMPGGGF SGPPPPPPPP PPGGAPGAPG
AMGPPPPPPL PGHTSGNFLP RPQFSTVPTL GLPVARPKKK LKALHWEKVD TPLTTHWAAH
APTPAEKEEK YAELTRKGVL DEVEKLFMAK EIKKIGTTTG NKTAKKQIIS SDLARTFQIS
LSKFSTYSVE KVIQMIIHCD KEVLDNTVVM EFLQKDDLCN IPDNTTKLMA PYSKDWTGPE
ANKESREMDP EELTREDQIY LQTAFELHHY WKSRIRALAL TRTYEAEYED ISTKLRQVVT
VSESLRDSVS LMNVLGLILD IGNYMNDSNK QASGFKLSSL ARLGMVKDEK NESTFADLVE
RIVRTQYPEW ENFTDDIGGV VTAQKLNVEQ LRTDAKKYID NIRNVQMSLD SGNLSDAKKF
HPQDRVSQVV LRSMKEARRK AEQMQLYLED MISTYDDIMV FYGEDSSDEN ARRDFFSKLA
IFVTEWKRSR DKNITFEETR RKNEASMKRK NAMLLKVNGS GLSDGTSAPP SPSSAGAMDS
LLEKLRAAAP QVRDQRDRRR RARLQTK
//
