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Database: UniProt
Entry: A0A3B3ZGT1_9GOBI
LinkDB: A0A3B3ZGT1_9GOBI
Original site: A0A3B3ZGT1_9GOBI 
ID   A0A3B3ZGT1_9GOBI        Unreviewed;      1134 AA.
AC   A0A3B3ZGT1;
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=Uncharacterized protein {ECO:0000313|Ensembl:ENSPMGP00000003606.1};
OS   Periophthalmus magnuspinnatus.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Gobiaria; Gobiiformes; Gobioidei; Gobiidae; Oxudercinae; Periophthalmus.
OX   NCBI_TaxID=409849 {ECO:0000313|Ensembl:ENSPMGP00000003606.1, ECO:0000313|Proteomes:UP000261520};
RN   [1] {ECO:0000313|Ensembl:ENSPMGP00000003606.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the formin homology family. Diaphanous
CC       subfamily. {ECO:0000256|ARBA:ARBA00008214}.
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DR   AlphaFoldDB; A0A3B3ZGT1; -.
DR   STRING; 409849.ENSPMGP00000003606; -.
DR   Ensembl; ENSPMGT00000003829.1; ENSPMGP00000003606.1; ENSPMGG00000003102.1.
DR   Proteomes; UP000261520; 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   Gene3D; 1.20.58.630; -; 1.
DR   Gene3D; 6.10.30.30; -; 1.
DR   Gene3D; 1.10.20.40; Formin, diaphanous GTPase-binding domain; 1.
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; IPR044933; DIA_GBD_sf.
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; PTHR45691; PROTEIN DIAPHANOUS; 1.
DR   PANTHER; PTHR45691:SF4; PROTEIN DIAPHANOUS HOMOLOG 1; 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   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils}.
FT   DOMAIN          57..420
FT                   /note="GBD/FH3"
FT                   /evidence="ECO:0000259|PROSITE:PS51232"
FT   DOMAIN          629..1025
FT                   /note="FH2"
FT                   /evidence="ECO:0000259|PROSITE:PS51444"
FT   DOMAIN          1047..1075
FT                   /note="DAD"
FT                   /evidence="ECO:0000259|PROSITE:PS51231"
FT   REGION          21..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          587..629
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          466..518
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1002..1043
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        21..37
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..54
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        587..628
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1134 AA;  129123 MW;  B529528CEF1C1F94 CRC64;
     QQGLGLGLGP FRKEIESSLE RFTSMRMKKD KEKPGQMPSQ RHSSAASYEF SSQSPMMQDH
     SDEYVLELFE QMLVDMNLNE EKQQPLREKD IVIKREMVSQ YLHTSKAGQN QKESSRSAVM
     YIHELQEDYR DPQLLLSCLE SLRVSLNNNP VSWVQTFGDQ GLTLLLTRLR GLQEDKHEMA
     IKCQHEIIRC LKAFMNNKYG LKSMLESGEG IPLLVRAMNP TVPHMMVDAV KLLSAISILE
     HPENLHERVL EAITEEAEKR NIERFQPLLS GMNIHNIALK VGGCMQLINA LISRGEELDF
     RIHIRSELLR LGLRHQLMEI RTIENEELRV QLAVFDEQAE DDSEDLRARL DDIRIEMEYL
     FNGVFEILVN TVKDSKAEGN FLSVMQHLLL IRNDYLARPQ YYKLIDECIG QIVLHKNGAD
     PDFKCRHLNL NIESLIDNMV DQTKVETSEA KATELEKKLN TELTARHELQ VELKKLEGDY
     EQKLQDLSQE KEQLASVKQE REKENQGLHK QLSSLQLQVP AHHLVLSFSL VNASHSTVGC
     PHHHLCLPQP LRVLELDLHH LLHAMQACLC PHLLRLLRLL HLPGMGPPPP PPPPGGPGVP
     PPPPGPGMPP PPFGGWTAAP PPLPYGLQPK KEYKPEVQLK RANWSKIGPE DLSESSFWTK
     AKEDQFGNNE LFAKLTLTFS SQTKTKNVPD GGDDKKNMQK KKAKELKVLD GKSAQNLSIF
     LGSFRLPYEE IKNAILEVNE KILTESMVQN LIKQLPSPEQ LSVLAEMKDE YDDLAESEQF
     GVVMSSVKKL TPRLQAILFK LQFEEQLNNI KPDVVSVTAA CEELTKSQSF SQLLQIILLM
     GNFMNAGSRN GKAFGFSISY LCKLRDTKST DLKMTLLHFL AEVCQEQYPE VMSFPDELIH
     VEKASRVSAE TIQKNLELMG RQIKNLQKDL ETFPPPQNEK DQFAENFVGT AQEQYEKLDL
     MHKNMDKQYT DLGNYFVFDP RKISVEEFFG DLKTFINMFQ QAVKENQKRK ESEEKIKRAK
     LAREKAEKEK EEKLKRSQLL DINAEGDETG IMDGLLEALQ SGAAFRRKRG PRQAVLRCTA
     AVSQCGLRMA ILVSTKLSTL SAFIPTIMSY LFYTVASFNT NKHGCLCVQP QLQQ
//
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