ID A0A165G9N6_9APHY Unreviewed; 825 AA.
AC A0A165G9N6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Formin binding protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=LAESUDRAFT_722178 {ECO:0000313|EMBL:KZT10033.1};
OS Laetiporus sulphureus 93-53.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Laetiporus.
OX NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT10033.1, ECO:0000313|Proteomes:UP000076871};
RN [1] {ECO:0000313|EMBL:KZT10033.1, ECO:0000313|Proteomes:UP000076871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-53 {ECO:0000313|EMBL:KZT10033.1,
RC ECO:0000313|Proteomes:UP000076871};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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DR EMBL; KV427610; KZT10033.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165G9N6; -.
DR STRING; 1314785.A0A165G9N6; -.
DR InParanoid; A0A165G9N6; -.
DR OrthoDB; 25674at2759; -.
DR Proteomes; UP000076871; Unassembled WGS sequence.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IEA:InterPro.
DR CDD; cd00201; WW; 2.
DR Gene3D; 2.20.70.10; -; 2.
DR Gene3D; 1.10.10.440; FF domain; 4.
DR InterPro; IPR002713; FF_domain.
DR InterPro; IPR036517; FF_domain_sf.
DR InterPro; IPR039726; Prp40-like.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR11864; PRE-MRNA-PROCESSING PROTEIN PRP40; 1.
DR PANTHER; PTHR11864:SF0; PRP40 PRE-MRNA PROCESSING FACTOR 40 HOMOLOG A (YEAST); 1.
DR Pfam; PF01846; FF; 2.
DR Pfam; PF00397; WW; 2.
DR SMART; SM00441; FF; 4.
DR SMART; SM00456; WW; 2.
DR SUPFAM; SSF81698; FF domain; 4.
DR SUPFAM; SSF51045; WW domain; 2.
DR PROSITE; PS51676; FF; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000076871}.
FT DOMAIN 1..31
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 45..71
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 388..449
FT /note="FF"
FT /evidence="ECO:0000259|PROSITE:PS51676"
FT REGION 598..825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 371..398
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 598..742
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..800
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..825
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 825 AA; 96497 MW; 7F1D99225DE3A48B CRC64;
MNVWTEHRNP EGRTYWFNTG TRESVWEKPD DLKTPFERAL NQTKWKEYFS GGRKYYYNTE
TKESKWDMPD ELILLLEKVE KEGKAAQQPN NALVAPAFTS AGNLGTPMQG APAALGGTDQ
SLSAPGSQTH PNGHIGELAV GMHTGALPFA PTSVLPPRPN MPDDPVIPHN GFATVEEGEK
AFTHLLRKAG VDANWTWDQT MRACITDPLY KALNTLAEKK ACWQKYTDAL RAKEQEERDA
RLSKLRPAIR NMLKGNPNVF HYTTFATADR LFAQHPIWQQ AKFEAERRLI FEEYVNELKQ
REVQESRASR ARSVSKIVAL YKRLDVDVTT RWRQAHQMVL DSDEWKDDPE LQKLPTLDIL
LAFEDYSRVR EREFEEQMRR AQVEKTRKER KAREAFRELL QSLVKSGQIK ARTKWKEVYP
VFSEDSRYLN MLGNPGSNPL ELFWDVIDEF DQQLDAKIDT VEGAMRRHNR NLELQQAKPE
GEKAEGQEAT DGGVKLFKIG PETTEEAFMV VMKAEEDDAM RKLSQADLKE AYNTLYLQAV
KQQADEKRRA ERKQRHLQDD FRYALKKLPE PLDLNLSYEE AVQFMQDLPE FKAIEEEEGR
RAAHAKFVKR QKERLRERER EASEDGGSTT SRKRKEPSKD EQERGRDHRE KDRELEHHDK
RTHRVHDEYD SHGRRSSRDY ANVRDRDYPR EKAYAGREKE REKEKDRDYA YRSSRHHKEY
ERDDRRRDRR GSRADYDAYG GREWDDGAGP PPPPLAQYRE DRERSASLYH EDPREKRDRT
IYEDRLYEER PDKKARYSVP PEASVEEAPK QEPPARAETP EEGEI
//