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Database: UniProt
Entry: A0A087XKJ7_POEFO
LinkDB: A0A087XKJ7_POEFO
Original site: A0A087XKJ7_POEFO 
ID   A0A087XKJ7_POEFO        Unreviewed;      1081 AA.
AC   A0A087XKJ7;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 2.
DT   24-JAN-2024, entry version 51.
DE   SubName: Full=Disheveled-associated activator of morphogenesis 1-like {ECO:0000313|Ensembl:ENSPFOP00000006300.2};
OS   Poecilia formosa (Amazon molly) (Limia formosa).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000006300.2, ECO:0000313|Proteomes:UP000028760};
RN   [1] {ECO:0000313|Proteomes:UP000028760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA   Schartl M., Warren W.;
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPFOP00000006300.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   EMBL; AYCK01005087; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_007552942.1; XM_007552880.2.
DR   RefSeq; XP_016527379.1; XM_016671893.1.
DR   AlphaFoldDB; A0A087XKJ7; -.
DR   STRING; 48698.ENSPFOP00000006300; -.
DR   Ensembl; ENSPFOT00000006311.2; ENSPFOP00000006300.2; ENSPFOG00000005990.2.
DR   GeneID; 103138613; -.
DR   KEGG; pfor:103138613; -.
DR   eggNOG; KOG1922; Eukaryota.
DR   GeneTree; ENSGT00940000156452; -.
DR   OMA; HSERTRF; -.
DR   OrthoDB; 5485896at2759; -.
DR   Proteomes; UP000028760; 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   GO; GO:0060026; P:convergent extension; IEA:Ensembl.
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:SF16; DISHEVELED-ASSOCIATED ACTIVATOR OF MORPHOGENESIS 1; 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:UP000028760}.
FT   DOMAIN          47..422
FT                   /note="GBD/FH3"
FT                   /evidence="ECO:0000259|PROSITE:PS51232"
FT   DOMAIN          605..1011
FT                   /note="FH2"
FT                   /evidence="ECO:0000259|PROSITE:PS51444"
FT   DOMAIN          1029..1061
FT                   /note="DAD"
FT                   /evidence="ECO:0000259|PROSITE:PS51231"
FT   REGION          521..617
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          990..1036
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1055..1081
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          114..146
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        530..600
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        991..1033
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1081 AA;  123505 MW;  4109C9934371D99E CRC64;
     MAPRKRGGGG SRGGLSFVFC CFSSNDHPEI TYKLREDFAL QSMEPSLPMP GYDELDNMFS
     DLVDELDLTE KHREAMFALP AEKKWQIYCS KKKEQEENKS ATSWPEYYID QLNLMAARKT
     LLALEKEDEE ERNKTIESLK TALRTQPMSF VTRFIDLDGL TCILNFLKSM DYDTTESQIH
     TSLIGCIKAL MNNSQGRAHV LAHSESINII AQSLATENIK TKVAVLEIMG AVCLVPGGHK
     KILEAMLHYQ RFACERTRFQ TLINELDRST GRYRDEVSLK TAIMSFINAV LSQGAGETSL
     EFRIHLRYEF LMLGIQPVID KLRSHENSTL DRHLDYFEML RNDDELALSK RFESVHIDTK
     SATQVFDLIR KKMNLTDAYP HFMSVLHHCL LMPHKRSGNT VQYWLLLDRI VQQMVLQNDK
     GHDPDIAPLE NFNVKNVVRM LVNENEVKQW KEQAEKMRKE HHELQQKFEK KERECDAKTQ
     EKEEMMQTLN KMKEKLEKES NEHKNVKQQV AELTAQLHEL STRQAAAVVP GGPPLPPGPP
     GSPLPPPPMP SLAGMCPPPP PPPGGAMPPP PPPPPPGGPP PPPGHAPMGG IPPPPGAPLG
     PSLKKKTIPQ PTNPLKSFNW SKLAENKLEG TVWMDVDDAR VFKVLDLVDI EKTFSAYQRQ
     QDFLMINNSK QKEAEDDTLS SKKVKELSVI DGRRAQNCNI LLSRLKLSNE EIKRAILTMD
     EHEDLPKDML EQLLKFVPEK SDVDLLEEHK HELDRMAKPD RFLYEMSRIN HYQQRLQSLY
     FKKKFAERIA EIKPKIEALT KASKEILHSR NLKQLLEVVL AFGNYMNKGQ RGNAYGFKVS
     SLNKIADTKS SIDKNITLLH YLITILEKKY PKVLKFQDDL QSVSEAAKVN MTELEKDIGN
     LRSGLKSVES ELDFQKNRPQ EVGDKFVSVV SQFITVASFS FSDVEDSLAE AKELFLRAVK
     HFGEDASKMQ PDEFFGIFDQ FLQSFTEAQQ ENENIRKRKE EEERRAKMEA QLKEQREKER
     KARKAKANGE DDGGEFDDLV SALWSGEVFD KDLSKMKRNR KRINNQSTDS SRERPVTKLN
     I
//
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