ID   A0A3B4XJV8_SERLL        Unreviewed;      1080 AA.
AC   A0A3B4XJV8;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Dishevelled associated activator of morphogenesis 1 {ECO:0000313|Ensembl:ENSSLDP00000016542.1};
OS   Seriola lalandi dorsalis.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Seriola.
OX   NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000016542.1, ECO:0000313|Proteomes:UP000261360};
RN   [1] {ECO:0000313|Ensembl:ENSSLDP00000016542.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   STRING; 1841481.ENSSLDP00000016542; -.
DR   Ensembl; ENSSLDT00000017110.1; ENSSLDP00000016513.1; ENSSLDG00000013098.1.
DR   Ensembl; ENSSLDT00000017139.1; ENSSLDP00000016542.1; ENSSLDG00000013098.1.
DR   GeneTree; ENSGT00940000156452; -.
DR   OrthoDB; 5485896at2759; -.
DR   Proteomes; UP000261360; Unplaced.
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}.
FT   DOMAIN          46..421
FT                   /note="GBD/FH3"
FT                   /evidence="ECO:0000259|PROSITE:PS51232"
FT   DOMAIN          604..1010
FT                   /note="FH2"
FT                   /evidence="ECO:0000259|PROSITE:PS51444"
FT   DOMAIN          1028..1060
FT                   /note="DAD"
FT                   /evidence="ECO:0000259|PROSITE:PS51231"
FT   REGION          523..615
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          988..1036
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1050..1080
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          439..522
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        530..599
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        990..1032
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1050..1067
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1080 AA;  123861 MW;  FB1A467D933672EB CRC64;
     MAPRKRGGGG RGGLSFIFCC FNSSDHPEIT YRLREDFALQ TMEPALPMPG YDELDGMFSE
     LVDELDLTEK HREAMFALPA EKKWQIYCSK KKEQEENKSA TSWPEYYIDQ LNSMAARKTL
     LALEKEDEEE RNKTIESLKT ALRTQPMRFV TRFIDLDGLT CILNFLKSMD YETTESQIHT
     SLIGCIKALM NNSQGRAHVL SHSESINIIA QSLATENIKT KVAVLEIMGA VCLVPGGHKK
     ILEAMLHYQR FACERTRFQT LINDLDRSTG RYRDEVNLKT AIMSFINAVL SQGAGETSLE
     FRIHLRYEFL MLGIQPVIDK LRSHENSTLD RHLDYFEMLR NEDELALSKR FESAHIDTKS
     ATQVFDLIRK KMNHTDAYPH FMSVLHHCLL MPHKRSGNTV QYWLLLDRIV QQMVLQNDKG
     HDPDVTPLEN FNVKNVVRML VNENEVKQWK EQAEKMRKEH HELQQRFEKK ERECDAKTQE
     KEDMMQTLNK MKEKLEKEST EHKNVKQQVA ELTARLHELS TRQAAVVPGG PPLTPGPPGG
     PLPLPPMPAF AGLCPPPPPP PGGMMPPPPP PPPPPGGPPP PPGRPPIGGI PPPPGAPLGP
     SLKKKNIPQP ANPLKSFNWS KLAENKLEGT VWMEVDDGKV FKILDLEDLE KTFSAYQRQQ
     DFFMINNSKQ KEAEDDTLSS KKVKELSVID GRRAQNCNIL LSRLKLSNEE MKRAILTMDE
     QEDLPKDMLE QLLKFVPEKS DVDLLEEHKH ELDRMAKPDR FLYEMSRINH YQQRLQSLYF
     KKKFAERIAE IKPKVEALTK ASKEILHSRN LKQLLEVVLA FGNYMNKGQR GNAYGFKVSS
     LNKIADTKSS IDKNITLLHY LITILEKKYP KVLMFQEDLQ SISEAAKVNM TELEKDICNL
     RSGLKSVESE LEYQKKRPQE LGDKFVSVVS QFITVASFSF SDVEDSLTES KELFLRAVKH
     FGEDASKMQP DEFFGIFDQF LQSFGEAQQE NENMRKRKEE EERRAKMEAQ LKEQREKERK
     ARKAKANGED DGGEFDDLVS ALRSGEVFDK DLSKMKRNRK RINNQTTDSS RERPVTKLNF
//