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Database: UniProt
Entry: A0A3B4A2S8_9GOBI
LinkDB: A0A3B4A2S8_9GOBI
Original site: A0A3B4A2S8_9GOBI 
ID   A0A3B4A2S8_9GOBI        Unreviewed;       831 AA.
AC   A0A3B4A2S8;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=FERM domain-containing protein {ECO:0000259|PROSITE:PS50057};
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:ENSPMGP00000011338.1, ECO:0000313|Proteomes:UP000261520};
RN   [1] {ECO:0000313|Ensembl:ENSPMGP00000011338.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A3B4A2S8; -.
DR   STRING; 409849.ENSPMGP00000011338; -.
DR   Ensembl; ENSPMGT00000012095.1; ENSPMGP00000011338.1; ENSPMGG00000009378.1.
DR   Proteomes; UP000261520; Unplaced.
DR   GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0030866; P:cortical actin cytoskeleton organization; IEA:InterPro.
DR   CDD; cd14473; FERM_B-lobe; 1.
DR   CDD; cd13184; FERM_C_4_1_family; 1.
DR   Gene3D; 1.20.80.10; -; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR008379; Band_4.1_C.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR000798; Ez/rad/moesin-like.
DR   InterPro; IPR014847; FA.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR   InterPro; IPR035963; FERM_2.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR019747; FERM_CS.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR018979; FERM_N.
DR   InterPro; IPR018980; FERM_PH-like_C.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR007477; SAB_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR23280; 4.1 G PROTEIN; 1.
DR   PANTHER; PTHR23280:SF24; BAND 4.1-LIKE PROTEIN 1; 1.
DR   Pfam; PF05902; 4_1_CTD; 1.
DR   Pfam; PF08736; FA; 1.
DR   Pfam; PF09380; FERM_C; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF09379; FERM_N; 1.
DR   Pfam; PF04382; SAB; 1.
DR   PIRSF; PIRSF002304; Membrane_skeletal_4_1; 1.
DR   PRINTS; PR00935; BAND41.
DR   PRINTS; PR00661; ERMFAMILY.
DR   SMART; SM00295; B41; 1.
DR   SMART; SM01195; FA; 1.
DR   SMART; SM01196; FERM_C; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF47031; Second domain of FERM; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS00660; FERM_1; 1.
DR   PROSITE; PS00661; FERM_2; 1.
DR   PROSITE; PS50057; FERM_3; 1.
PE   4: Predicted;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203}.
FT   DOMAIN          42..323
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          477..541
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          620..679
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..25
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..40
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        485..502
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        518..541
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   831 AA;  93372 MW;  97A65CF05A2E2B1E CRC64;
     VGEKNSAFKI SHNDHEVDDS SEKTPSKASK SPQKSSKRPK TVPVKVTLLD GSDYDTAVEK
     FAKGQTLLDM VCGHLNLLER DYFGLMFQDT DNSKNWLDPS KEIKKQIRVG SWVFAFSVKF
     YPPDPSVLIE DITRYYLCLQ LRDDILSGRL PCSFVTHALL GSYTVQAEIG DYEPEEHGPD
     YVNDFRFAPN QTRELEERVM ELHRNYRGMS PAEAEMNFLE NAKKLSMYGV DLHQAKDSEG
     IDIMLGVSAS GLLIYRDRLR INRFAWPKIL KISYKRSNFY IKIRPGEYEQ FESTIGFKLP
     NHRASKRLWK VCIEHHTFFR LVSPEPPPKG FLVIGSKFRY SGRTQAQTRQ ASALIDRPAP
     LFERSVSKRY MLPRSLDGAS ALGDSMDQLS QRSSSDRTQF MSRDDLDQEG SLDLDHDQYH
     YEDQDQGDFT DQELDQEEAG SPLDSKPEVF WPRGQCQFLD KSEDVLQKHQ ASINELKRAL
     KQPNSKKRVP SSTSSTSPGG TPERKPETPP TPAIHEEPPS EASREPWERR LGSVSEDDQD
     HESLYLKETH LGIERKCSSI TVSSTSSLEA EVDFTVLTDL HSGMEEFSRG MSELGERDLS
     PDRGLCLGID LLHQHPPEPL PPLVAPVVPK KPKRSVPVSS SVDRDGGRVG AVTPLSREAS
     DLMPTPAPRK TDVRTETQPN GAEVTTTIVE FTDQDHGLSG LSDTTPYSTR QSVSPVSFGY
     SNAGSPILMT ENVTSATTHV TKTVKGGYSE TRIEKRIIIT GDDDVDQEQA LAIAIQEARQ
     QHPDMQVTKA VVVRETESST EDRHGASEVQ LLPFTHNTLR TTRNTWVHCV T
//
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