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Database: UniProt
Entry: A0A4W6D5Y8_LATCA
LinkDB: A0A4W6D5Y8_LATCA
Original site: A0A4W6D5Y8_LATCA 
ID   A0A4W6D5Y8_LATCA        Unreviewed;      1282 AA.
AC   A0A4W6D5Y8;
DT   18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=FERM domain-containing protein {ECO:0000259|PROSITE:PS50057};
OS   Lates calcarifer (Barramundi) (Holocentrus calcarifer).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangaria incertae sedis; Centropomidae; Lates.
OX   NCBI_TaxID=8187 {ECO:0000313|Ensembl:ENSLCAP00010020197.1, ECO:0000313|Proteomes:UP000314980};
RN   [1] {ECO:0000313|Proteomes:UP000314980}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Sai Rama Sridatta P.;
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLCAP00010020197.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   Ensembl; ENSLCAT00010020647.1; ENSLCAP00010020197.1; ENSLCAG00010009543.1.
DR   GeneTree; ENSGT00940000158442; -.
DR   Proteomes; UP000314980; Unassembled WGS sequence.
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:SF20; BAND 4.1-LIKE PROTEIN 3; 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   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:UP000314980}.
FT   DOMAIN          52..333
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          404..458
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          486..554
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          567..750
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          804..850
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          919..1023
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1102..1128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1141..1192
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..34
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        404..423
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        425..441
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        442..458
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        497..511
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        516..554
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        567..588
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        680..704
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        706..733
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        734..750
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        831..845
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        919..939
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        974..988
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        999..1023
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1104..1125
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1143..1168
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1282 AA;  144648 MW;  4D06C6231EA3725F CRC64;
     MQDSASDSKM AKQEQNSKHL DEHRETDEMS EKTSPNKNLK SPQKGSKRLK TIPFKVTLLD
     SSEFEGEIEK HSKGQTLMDM VCEHLNLLEK DYFGLTFADT DTQKNWLDPS KEIKKQMRNS
     PWHVAFAVKF YPPDPSQLTE DITRYYLCLQ LRDDMLSGRL PCSFVTHALL GSYTVQAELG
     DYDQDDHGSD YVSDFRFAPN QTRELEERVM ELHRNYKGMT PAEAEMNFLE NAKKLSMYGV
     DLHHAKDSEG IDIMLGVCAN GLLIYRDRLR INRFAWPKIL KISYKRSNFY IKIRPGEYEQ
     FESTIGFKLP NHRAAKRLWK VCIEHHTFFR LVSPEPPPKG FLVMGSKFRY SGRTQAQTRQ
     ASALIDRPAP HFERSTSKRY LLSRSLDGEF SRPVSAMCEN HDGLSHRSIS EQRRLHSPSV
     DEQETELEPS LEQDEEDKDQ ERDLSEQDKN DDGNITPNRK KEIMFLDKSQ DVLLKHQASI
     NELKRALREP NSKLMNREKR LSATSPTGTP EKKAGSEEWV LIEKQQPYQR DHDWKAEEKN
     KSFTSDSSWE TKELEKEIDV TKMIHKEVTG YDRKEMKSHT DEFPSTKSSS EADVRPESWP
     TNKSPFVIEL SENADPFRDK SQSKPSQASD PEANSDVALG LRQIKERTAS KQRKKRRPQS
     LNLGMPAELI YRKGGSDSTG EENEGSNSDI SPEKTFQTGN HYESSKVVVK KGDQGSGKDQ
     SVKDSKQEEI SIGENREVST QGTEQVKRKV SQVGTTDIDL GSVNGPGKIE HDSSLAGVKG
     ECTMKVRGKS LIDNKELAEV KLRQVRTHEQ KISSSAAEDI EGFMGERGQR TSFHRLSSSG
     YQSEITRIVP LKPERSKSVV CKDERDRTGQ DEPTRVIRRE YRWSVGSPEG SSDLNWTDVS
     TFHSAFAADL EVVAKTEQPD NSYQFGRGPT ESQSFGSKIS ALPKMAPPAP PVKTQKARES
     GLILRNSRNA GREPSLDAAK KRHSEPVSTP AIYEEPFADF KEGLGDRKPQ PSVAPEEEQE
     RDTVTCMRET HLGIERKCSS MTVSSTSSLE AEVDFTIITD LHSGVEDFSK GLLDLGERER
     QPEVGREDFE ETSRFYSARL MGSRDKSPIE EKLPEGTHHE PPVAKKDPTA VSMAHMLRRA
     DTKTQTHTNG SEVHPHIMNV SPQNYGAVSP QEAPAALKEN GSPVKASTQG RESVVSPLTI
     TAESVTSATT TQVTKTVKGG YSETRIEKRI IITGDDDVDQ HQALAMAIQE AKQQHPDMLV
     TKAVVIRETD SPTEELQQKS ES
//
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