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Database: UniProt
Entry: A0A667WX63_9TELE
LinkDB: A0A667WX63_9TELE
Original site: A0A667WX63_9TELE 
ID   A0A667WX63_9TELE        Unreviewed;       788 AA.
AC   A0A667WX63;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Si:dkey-178k16.1 {ECO:0000313|Ensembl:ENSMMDP00005010180.1};
OS   Myripristis murdjan (pinecone soldierfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Holocentriformes; Holocentridae; Myripristis.
OX   NCBI_TaxID=586833 {ECO:0000313|Ensembl:ENSMMDP00005010180.1, ECO:0000313|Proteomes:UP000472263};
RN   [1] {ECO:0000313|Ensembl:ENSMMDP00005010180.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A667WX63; -.
DR   Ensembl; ENSMMDT00005010490.1; ENSMMDP00005010180.1; ENSMMDG00005005467.1.
DR   GeneTree; ENSGT00940000155617; -.
DR   InParanoid; A0A667WX63; -.
DR   Proteomes; UP000472263; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000472263}.
FT   DOMAIN          26..304
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          362..405
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          435..502
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          573..620
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          768..788
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..24
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        365..388
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        479..502
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        577..594
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        605..620
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        774..788
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   788 AA;  88135 MW;  28BF058FAE35B60A CRC64;
     MDDSSEKTPS KASKSPQKSS KRPKTVPVKV TLLDGSDYET AVEKFAKGQT LLDMVCGHLN
     LLERDYFGFL SSVYQNWLDP SKEIKKQIRV GSWSFGFSVK FYPPDPSILI EDITRYYLCL
     QLRDDILSGR LPCSFVTHAL LGSYTVQAEL GDYEAEEHGP DYVSDFRFAP NQTRELEERV
     MELHRTYRGM SPAEAEVNFL ENAKKLSMYG VDLHHAKDSE GIDIMLGVSA NGLLIYRDRL
     RINRFAWPKI LKISYKRSNF YIKIRPGEYE QFESTIGFKL PNHRASKRLW KVCIEHHTFF
     RLVSPEPPPK GFLVIGSKFR YSGRTQAQTR QASALIDRPA PQFDRSVSKR YLLPRSMDGA
     SALGDSMDQL SQRSSSEHHD QAPVSTSGKT LELKGEEAGS PVDSKPEVFW PWTLQQFLDK
     PEDVLQKHQA SINELKRALR QPNSKLAQRE KRLSSATPPG GTPERKPETP PTPAIHEEPL
     NEASREPWER RLGSVSEDDQ DHETLYLKET HLGIERKCSS ITVSSTSSLE AEVDFTVLMD
     LHTGMEEFSR GMTELGERDL SPDGGLCLGI DLLQQQGPSE PPPPLMSAPV RPEPVVPKKP
     KRSVPVSSSV DRDHLHRDGS RVTTITALSR EASDVMVTPT VRKTDVRTET QPNGSEVTTT
     IVEFTDQDHG IGGLSQVSYS TRESVSPVHM SSLGREASGS PILVTENVTS ATTHVTKTVK
     GGYSETRIEK RIIITGDDDV DQEQALAIAI QEAKQQHPDM QVTKAVVVRE TESSTEDPYG
     TSEVQVPS
//
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