ID A0A091QME8_MERNU Unreviewed; 274 AA.
AC A0A091QME8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 22-FEB-2023, entry version 28.
DE RecName: Full=F-actin-capping protein subunit alpha {ECO:0000256|RuleBase:RU365077};
DE Flags: Fragment;
GN ORFNames=N331_02906 {ECO:0000313|EMBL:KFQ28114.1};
OS Merops nubicus (Northern carmine bee-eater).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Coraciiformes; Meropidae; Merops.
OX NCBI_TaxID=57421 {ECO:0000313|EMBL:KFQ28114.1, ECO:0000313|Proteomes:UP000052967};
RN [1] {ECO:0000313|EMBL:KFQ28114.1, ECO:0000313|Proteomes:UP000052967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N331 {ECO:0000313|EMBL:KFQ28114.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: F-actin-capping proteins bind in a Ca(2+)-independent manner
CC to the fast growing ends of actin filaments (barbed end) thereby
CC blocking the exchange of subunits at these ends. Unlike other capping
CC proteins (such as gelsolin and severin), these proteins do not sever
CC actin filaments. {ECO:0000256|RuleBase:RU365077}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit.
CC {ECO:0000256|RuleBase:RU365077}.
CC -!- SIMILARITY: Belongs to the F-actin-capping protein alpha subunit
CC family. {ECO:0000256|ARBA:ARBA00010479, ECO:0000256|RuleBase:RU365077}.
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DR EMBL; KK702392; KFQ28114.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091QME8; -.
DR Proteomes; UP000052967; Unassembled WGS sequence.
DR GO; GO:0008290; C:F-actin capping protein complex; IEA:UniProtKB-UniRule.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0051016; P:barbed-end actin filament capping; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.1140.60; F-actin capping protein, alpha subunit; 1.
DR Gene3D; 3.90.1150.210; F-actin capping protein, beta subunit; 1.
DR InterPro; IPR002189; CapZ_alpha.
DR InterPro; IPR037282; CapZ_alpha/beta.
DR InterPro; IPR042276; CapZ_alpha/beta_2.
DR InterPro; IPR042489; CapZ_alpha_1.
DR InterPro; IPR017865; F-actin_cap_asu_CS.
DR PANTHER; PTHR10653; F-ACTIN-CAPPING PROTEIN SUBUNIT ALPHA; 1.
DR PANTHER; PTHR10653:SF2; F-ACTIN-CAPPING PROTEIN SUBUNIT ALPHA-2; 1.
DR Pfam; PF01267; F-actin_cap_A; 1.
DR PRINTS; PR00191; FACTINCAPA.
DR SUPFAM; SSF90096; Subunits of heterodimeric actin filament capping protein Capz; 1.
DR PROSITE; PS00748; F_ACTIN_CAPPING_A_1; 1.
DR PROSITE; PS00749; F_ACTIN_CAPPING_A_2; 1.
PE 3: Inferred from homology;
KW Actin capping {ECO:0000256|RuleBase:RU365077};
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203,
KW ECO:0000256|RuleBase:RU365077};
KW Reference proteome {ECO:0000313|Proteomes:UP000052967}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ28114.1"
FT NON_TER 274
FT /evidence="ECO:0000313|EMBL:KFQ28114.1"
SQ SEQUENCE 274 AA; 31468 MW; 08ABD5EB23F43CEF CRC64;
KVRIAAKFII HAPPGEFNEV FNDVRLLLNN DNLLREGAAH AFAQYNLDQF TPVKIDGYDE
QVLITEHGDL GNGKFLDPKN KISFKFDHLR KEATDPRPHE VENAIESWRN SVETAMKAYV
KEHYPNGVCT VYGKTIDGQQ TIIACIESHQ FQAKNFWNGR WRSEWKFTIT PSTTQVAGIL
KIQVHYYEDG NVQLVSHKDI QDSLTVSNEA QTAKEFIKIV EAAENEYQTA ISENYQTMSD
TTFKALRRQL PVTRTKIDWN KILSYKIGKE MQNA
//