ID A0A2U9CNI9_SCOMX Unreviewed; 1044 AA.
AC A0A2U9CNI9;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 22-FEB-2023, entry version 16.
DE SubName: Full=Putative formin-like protein 1 {ECO:0000313|EMBL:AWP18131.1};
GN ORFNames=SMAX5B_020549 {ECO:0000313|EMBL:AWP18131.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP18131.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP18131.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the formin homology family.
CC {ECO:0000256|ARBA:ARBA00023449}.
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DR EMBL; CP026260; AWP18131.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9CNI9; -.
DR STRING; 52904.ENSSMAP00000017725; -.
DR Proteomes; UP000246464; Chromosome 18.
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:0022604; P:regulation of cell morphogenesis; IEA:InterPro.
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; IPR043592; FMNL_animal.
DR InterPro; IPR014768; GBD/FH3_dom.
DR InterPro; IPR010473; GTPase-bd.
DR PANTHER; PTHR45857; FORMIN-LIKE PROTEIN; 1.
DR PANTHER; PTHR45857:SF2; FORMIN-LIKE PROTEIN 1; 1.
DR Pfam; PF06367; Drf_FH3; 1.
DR Pfam; PF06371; Drf_GBD; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000246464}.
FT DOMAIN 1..447
FT /note="GBD/FH3"
FT /evidence="ECO:0000259|PROSITE:PS51232"
FT DOMAIN 576..968
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT DOMAIN 999..1029
FT /note="DAD"
FT /evidence="ECO:0000259|PROSITE:PS51231"
FT REGION 134..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 501..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1017..1044
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..402
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..457
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..521
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..567
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1044 AA; 117786 MW; 8AE8E17F0B874CA1 CRC64;
MSHIDIFAVG ASHLCSFFAQ NSMNLPPDKV KILSQYDNEK KWDLICDQER FQVKNPPSAY
LEKLKSFLDH GGVGRKFKRR VQESTQILRE LEISLRTNHI GWAQEFLSEE NNGLDVLVDY
LSFAHSAVTY DADASDNCSP ATDKGKTMDR SVEDVSKSAS NSPSHSSSKT SKAFITRFNS
LQNRKVARNS RVVSQNDDVH LCIMCLRAIM NYQSGFNLVM KHPNCVNEIT LSLNNRNPRT
RALVLELLAA VCLVRGGHDI ILSAFDNFEE VCAEKSRFEK LMEFFCSDES NIDFMVACMQ
FINIVVHSVE NMNFRVHLQY EFTRHGLDEY LERLKFTESD RLLVQIQAYL DNVFDVGALL
EDAETKNALL EHMEELQGHN AQLSSRLQES ERESEDRASE LEKKLIQMTK EVELLKESLR
ESSSQVTLLQ QRERESEERE RQSEIERARE RDRSGRALSE LEAKVQTLAE QGLVRTERSP
SGHLEVQVVP VVQCEIQKEV ADTGNEREAT PTSSDPPPCL SEGSSQALME EAPAPPPPPP
PPPPPPPPPV APPPPSVAPP PPLLPPVADG SSGSKKKRTI QTKYRMPLLN WQALKSSQVA
GTVFSELDDE HVLEELDMAA FEEQFKTKAQ STPVDPGTFK MKLAHKTPSK VSILEPNRAK
NLAITLRKEG MAASDICCAI ETYNQKALSL DFLELLERFI PTEYDMKLIH SYECDGRPLD
ELSEEDRFMV RFSKIQRLSQ RISALTFMGN FPESVQLIQP QLNAVIAASM SIKSSSKLKK
ILEIILAFGN YMNSSKRGAA YGFRLQSLDL LLETKSTDRT QTLLHFIVSI IQEKYPELQG
FYTELHFLDK ASMVSLDIIL QDVRALERGM EATGTEFSLE QENPVLQTFL SRNAELLDSL
VADGRTAQDV YDSAVEYFGE NSKTTPPSMF FPVFVRFIKA YKQAEQENKL KGKHVLNCDA
PSTPPKPEVV ENKVSLVPKL PQMDLIAELK RRQVSPLVRE GKDGAIEDII TDLRNQPYRR
TDGSRRSAKW KPGQQLHVSS DISL
//
