ID A0A0Q3LVS0_AMAAE Unreviewed; 1115 AA.
AC A0A0Q3LVS0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 22-FEB-2023, entry version 19.
DE SubName: Full=Disheveled-associated activator of morphogenesis 2 isoform X2 {ECO:0000313|EMBL:KQK74559.1};
GN ORFNames=AAES_154865 {ECO:0000313|EMBL:KQK74559.1};
OS Amazona aestiva (Blue-fronted Amazon parrot).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Amazona.
OX NCBI_TaxID=12930 {ECO:0000313|EMBL:KQK74559.1, ECO:0000313|Proteomes:UP000051836};
RN [1] {ECO:0000313|EMBL:KQK74559.1, ECO:0000313|Proteomes:UP000051836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FVVF132 {ECO:0000313|EMBL:KQK74559.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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:KQK74559.1}.
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DR EMBL; LMAW01003032; KQK74559.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q3LVS0; -.
DR STRING; 12930.A0A0Q3LVS0; -.
DR Proteomes; UP000051836; Unassembled WGS sequence.
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 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; PTHR45725:SF7; DISHEVELED-ASSOCIATED ACTIVATOR OF MORPHOGENESIS 2; 1.
DR PANTHER; PTHR45725; FORMIN HOMOLOGY 2 FAMILY MEMBER; 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 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000051836}.
FT DOMAIN 73..449
FT /note="GBD/FH3"
FT /evidence="ECO:0000259|PROSITE:PS51232"
FT DOMAIN 634..1044
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT DOMAIN 1064..1095
FT /note="DAD"
FT /evidence="ECO:0000259|PROSITE:PS51231"
FT REGION 549..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1046..1069
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1088..1115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 474..543
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 735..765
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 553..567
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..617
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..643
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1046..1066
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1088..1102
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1115 AA; 128876 MW; 02A34972233079C8 CRC64;
MIVFVPKRRR EEQIRNYRDH PEHDQKIASY TMTMAPRKRN RHALGFLCCF GGSDLPEINL
KDNNPLQFLE FSVPIPPAEE LNARFSELVD ELDLTDKNRE AMFALPPEKK WQIYCSKKKE
QEDPNKLATS WPDYYIDRIN SMAAMQTLYA FDEEETEMKN KIVEDLKTAL RTQPMRFVTR
FIELDGLSCL LNFLKSMDYE TSESRIHTSV IGCIKALMNN SQGRAHVLAH PESINIISQS
LRTENIKTKI AVLEILGAVC LVPDGHKKVL QAMLHYQVYA AERTRFQTLL NELDRSMGRY
RDEVNLKTAI MSFINAVLNA GAGEDNLEFR LHLRYEFLML GIQPVIDKLR GHENATLDRH
LDFFEMVRNE DDLELAKQFE LIHIDTKSAS QMFELIKKRL KHTDAYPYLL SILQHCLQMP
YKRNGGNFQQ WQLLDRILQQ IVLQDERGDD PDIAPLENFN VKNIIKMLVN ENEVKQWRDQ
AEKFRKDHAE LMSRLEKKER ECETKTQEKD EMMKTLNKMK DKLQKESLEL RQTRDQMNDL
VAQLNEFSQG SSISFPPPPP PPPGGPLALS SSHMSENLPP LPPPLPFSSC PPPPAPPPPP
GGPPPPPGAP PFFSMGIPPP STTTFSSSGT SLKKKSVPQP SHPLKSFNWA KLSEERIHGT
IWNEIDDLKA FKVLDLEDFE KMFSAYQRHQ DLLTNPSSCK QKEMGSTEDL YLSTRKVKEL
SVIDGRRAQN CVILLSKLKL TNEEIRQAIL KMDEQEDLAK DMLEQLLKFV PEKSDTDLLE
EHKHEIERMA RADRFLFEMS RIDHYQQRLQ ALFFKKKFPE RLAEAKPKVE AILLASKELI
RSKRLRQLLE VVLAFGNFMN KGQRGSAYGF KVSSLNKIAD TKSSIDRNIT LLHYLIMIFE
KNYPDILDIQ SELQHLPEAA KVNLVELEKE VNNIKNGLKA VEAELDYQKR RMRESGDRFV
PVMSDFITVA SFSFSELEDL LNEARDKYAK ALKHFGESEG KMQPDEFFGI FDTFLQSFAE
AKQDLENMRK KKEEEERRAR MEAMLKEQRE KERRQKKAKA GSISEESGEF DDLVSALRSG
EVFDKDLSKL KRNRKRSGNQ GLETSRERVV TKLNY
//
