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Database: UniProt
Entry: A0A139HGF7_9PEZI
LinkDB: A0A139HGF7_9PEZI
Original site: A0A139HGF7_9PEZI 
ID   A0A139HGF7_9PEZI        Unreviewed;      1737 AA.
AC   A0A139HGF7;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=FH2 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AC578_6327 {ECO:0000313|EMBL:KXT01564.1};
OS   Pseudocercospora eumusae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX   NCBI_TaxID=321146 {ECO:0000313|EMBL:KXT01564.1, ECO:0000313|Proteomes:UP000070133};
RN   [1] {ECO:0000313|EMBL:KXT01564.1, ECO:0000313|Proteomes:UP000070133}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 114824 {ECO:0000313|EMBL:KXT01564.1,
RC   ECO:0000313|Proteomes:UP000070133};
RA   Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT   "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT   link between parallel evolutionary changes in Pseudocercospora fijiensis
RT   and Pseudocercospora eumusae and increased virulence on the banana host.";
RL   Submitted (JUL-2015) 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:KXT01564.1}.
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DR   EMBL; LFZN01000053; KXT01564.1; -; Genomic_DNA.
DR   STRING; 321146.A0A139HGF7; -.
DR   OrthoDB; 1118745at2759; -.
DR   Proteomes; UP000070133; 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:UP000070133}.
FT   DOMAIN          236..665
FT                   /note="GBD/FH3"
FT                   /evidence="ECO:0000259|PROSITE:PS51232"
FT   DOMAIN          1090..1512
FT                   /note="FH2"
FT                   /evidence="ECO:0000259|PROSITE:PS51444"
FT   DOMAIN          1529..1561
FT                   /note="DAD"
FT                   /evidence="ECO:0000259|PROSITE:PS51231"
FT   REGION          1..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          95..208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          934..1093
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1505..1533
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1545..1737
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          689..716
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        41..61
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        101..115
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        145..208
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        953..969
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        979..1069
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1512..1529
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1578..1604
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1635..1664
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1679..1706
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1737 AA;  193220 MW;  A4504249B960BF4B CRC64;
     MFSSSDKSAR QSSGGKSFFS RNKKDKGSEH GPSHGHAQAT SHESTARHSH SHRSSTSTID
     QEEYMKNGHD PLAMQAGVIT SIPYDAMAKD TRPPVLVDSA DRPASKREPL PHHLNKGGGD
     FHQYPAFDAS SLPPRPPTHG SSYRGRLDSD ATTLNAYPAS RSSSDHGSIR SNWSGDRRQY
     YNGNTSQASL GVGMTGYAPE QSSASQRDRN NQYLNAHNPS AFSSAASFSP EGLLQHRPAD
     DKVIEKEFLE LMLKRGWKSL PEQARRQMEA YPISKKWTLV YQDRLAEWQG EQKRRNMARN
     TMQSVHGAFD IGRMEEEGSP EWYVKKILDN SITAKQLQSL AVSLRTQPIA WVKAFVEAQG
     QIALTNLLGK LNRRQASGPV SVEGSKQEKD LDREYDIVKC LKALMNNKYG ADNALQHDSI
     VMALASSLTT PRLHTRKLVS ELLTFLCHWA DGQGHVKVLQ AMDHLKAQQS ENGRFDAWLR
     IVEVTIDGRG KMGSLVGASD EVRSGGVGME NLLMEYAVAS LFLVNSIVDA PERDLQLRCH
     IRAQFVACGL KRIFTKMEDF QYEVIDKQIE RYRNNEAIDY EDLLERENSS MHESMEGEGR
     DLNDPVQIVE AIQQRVAGSR EGDYFLSALQ HLLLIRDNEG EDRVKLFQLV ENMLSYVAMD
     RRLPDMDLKQ SLNFSVQSLL DKLYTDSEAR QAREAANEAK LVADAAIAER DEMKSQVEMG
     AEGLVAKLQK QIDEQAAVID LQSRQTEAMK SELGELQRVR AQDLQRQELE TRELYLMLRD
     AQNIAESNSK KGGKNGETTD PARLQGILDR ERLMDRLEMQ LERAKTQAKL EGKVWQQFNP
     SDKLRELREK MEGAGMEPDG LEAQMSYLGQ TAPRRGTGIA RKPVRKAADG DNVDDTIMED
     DAVFEKPRLV EYTRPKVPSS VANAQRGMLA ELQSRAPRVD GSDDEGDGVT TGPSHPSLES
     ESPKTPTSTD LPEPAKEKFD GPAAPPPPPM PEFDGAAPPP PPPPPGFSND APPPPPPPMP
     GFGSSAPPPP PMPGFNGAAP PPPPPPPEMG FKGGAPPPPP PPPGAPPLPG KLHGGFLPKQ
     MHTSPNGGIG AVAPRPKKKL KALHWEKVDS PEVTLWSLHT PTFEQKEEKY QELSRKGILD
     EIEKLFMAKE IKQIGKGGAK VKTDKKQVIS RDLMHMMQIS LAKFSNVEAD DIVRMVIHCD
     REILENSTVM DFLQHEHLCT IPDNVAKLMA PYSKDWTGPD AIKSTREQDP SELTREDQIY
     LYTAYELHHY WKARMRALAL TKNFEPEYDE ISGKLKQVVQ VSESLRDSVK LMPVFGLILD
     IGNYMNDSNK QAVGFKLSSL ARLGMVKDKD NESTLLDYVE RVVRKQYPQY EGFYEDISGV
     LTTQKINIEQ LQGDAKKYID NINNVQSSLD SGNLSDPKRF HPEDRVSQVV QRSMKEARRK
     AEQMALYLDE MNRVYDDILT YFGDDNKDEN ARREFFSKLA NFLQEYKKSH EKNLVLEEAW
     RRNEENMRRK QMKSGQGSSS ASVSDAPASP VSTGAMDDLL QKLRAAAPVA KDTRERRRRA
     RLKDRHQVRV ASGQKIPETG ENMVTDESGL LSPAKTNDSA DSNEPVEGGV SEGEDIADRA
     ASMLQGLRGD AEPAESGSES IRVRRRRESA DDERARRRAR RRAAGGSTDT TAATITEEGD
     EAAVDKPGEA RIVEEDEEKS GGSDGKRDSG ESPLPTPTTV VVPPSPTASE HSPEKAE
//
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