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Database: UniProt
Entry: A0A094LIG1_ANTCR
LinkDB: A0A094LIG1_ANTCR
Original site: A0A094LIG1_ANTCR 
ID   A0A094LIG1_ANTCR        Unreviewed;       970 AA.
AC   A0A094LIG1;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Band 4.1-like 3 {ECO:0000313|EMBL:KFZ63694.1};
DE   Flags: Fragment;
GN   ORFNames=N321_02670 {ECO:0000313|EMBL:KFZ63694.1};
OS   Antrostomus carolinensis (Chuck-will's-widow) (Caprimulgus carolinensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Caprimulgiformes;
OC   Caprimulgidae; Antrostomus.
OX   NCBI_TaxID=279965 {ECO:0000313|EMBL:KFZ63694.1, ECO:0000313|Proteomes:UP000053620};
RN   [1] {ECO:0000313|EMBL:KFZ63694.1, ECO:0000313|Proteomes:UP000053620}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N321 {ECO:0000313|EMBL:KFZ63694.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KL358345; KFZ63694.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094LIG1; -.
DR   Proteomes; UP000053620; Unassembled WGS sequence.
DR   GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:UP000053620}.
FT   DOMAIN          1..265
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   REGION          335..439
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          558..591
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          768..833
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        344..370
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        424..439
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        779..796
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        805..832
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFZ63694.1"
FT   NON_TER         970
FT                   /evidence="ECO:0000313|EMBL:KFZ63694.1"
SQ   SEQUENCE   970 AA;  107598 MW;  44A880AFBD16EFCB CRC64;
     QKRSRGQVLF DKVCEHLNLL EKDYFGLTYR DTENQKNWLD PAKEIKKQIR SGAWQFAFNV
     KFYPPDPAQL SEDITRYYLC LQLRDDIVSG RLPCSFVTLA LLGSYTVQSE LGDYDPDEYG
     SDYVSEFRFA PNHTKELEDK VIELHKSHRG MTPAEAEMHF LENAKKLSMY GVDLHHAKDS
     EGVEIMLGVC ASGLLIYRDR LRINRFAWPK VLKISYKRNN FYIKIRPGEF EQFESTIGFK
     LPNHRAAKRL WKVCVEHHTF FRLLLPEAPP KKFLTLGSKF RYSGRTQAQT RRASALIDRP
     APYFERSSSK RYTMSRSLDG EVGTGQYATT KGISQTNLIT TVTPEKKAEE EKDDEEGKKK
     REEEVTPVSA IRHDTKPSLL GTESRHPSPP SQPGPHASSA KLRRRCKESA RTKSFSCEAP
     NESPAKHGEL EPGSDRKGRV CSTEQDVAFG YKQKAGKGGT LFSFSLQLPE SFPSLLDDDG
     YLSLPNLSET NLLPASVQHY LPIRSPSLVP CFLFIFFFLL SASFSVPYAL TLSFPLAMCL
     CYLEPKAASL SASLANDLSD SSEEETDSEQ TDTAADGETT ATESDQEEDG DLKAQDLDKT
     QEDLMKHQTN ISELKRTFLE TSTETAVSNE WEKRLSTSPV RLAARQEEAP MIEPLVPEET
     KQSTGEKTLD GSDIFSLIES ARKPTEFIGG VTSTSHSWAQ RIDTTTSQEI TSSEMKQAVQ
     PHQETVKKVV QETVVMEERR GMSVHASGDP VKVAGLALDA QAEAASGVAA GLKGKEGSAG
     TEGAKEEKRE EAGKAPAKQE GVAAASREQA EERGTTVHLS ESLERKPHFE SPVVKTETIS
     FSSVSAGGEN LEISTKEVPV VHTETKTITY ESSQVDCSAD SEPGVLMSAQ TITSETTSTT
     TTTHITKTVK GGISETRIEK RIVITGDADI DHDQALAQAI KEAKEQHPDM SVTKVVVHKE
     TEITPEDGED
//
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