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Database: UniProt
Entry: F4REQ0_MELLP
LinkDB: F4REQ0_MELLP
Original site: F4REQ0_MELLP 
ID   F4REQ0_MELLP            Unreviewed;       280 AA.
AC   F4REQ0;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=F-actin-capping protein subunit alpha {ECO:0000256|RuleBase:RU365077};
GN   ORFNames=MELLADRAFT_34510 {ECO:0000313|EMBL:EGG09139.1};
OS   Melampsora larici-populina (strain 98AG31 / pathotype 3-4-7) (Poplar leaf
OS   rust fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Melampsoraceae; Melampsora.
OX   NCBI_TaxID=747676 {ECO:0000313|Proteomes:UP000001072};
RN   [1] {ECO:0000313|Proteomes:UP000001072}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=98AG31 / pathotype 3-4-7 {ECO:0000313|Proteomes:UP000001072};
RX   PubMed=21536894; DOI=10.1073/pnas.1019315108;
RA   Duplessis S., Cuomo C.A., Lin Y.-C., Aerts A., Tisserant E.,
RA   Veneault-Fourrey C., Joly D.L., Hacquard S., Amselem J., Cantarel B.L.,
RA   Chiu R., Coutinho P.M., Feau N., Field M., Frey P., Gelhaye E.,
RA   Goldberg J., Grabherr M.G., Kodira C.D., Kohler A., Kuees U.,
RA   Lindquist E.A., Lucas S.M., Mago R., Mauceli E., Morin E., Murat C.,
RA   Pangilinan J.L., Park R., Pearson M., Quesneville H., Rouhier N.,
RA   Sakthikumar S., Salamov A.A., Schmutz J., Selles B., Shapiro H.,
RA   Tanguay P., Tuskan G.A., Henrissat B., Van de Peer Y., Rouze P.,
RA   Ellis J.G., Dodds P.N., Schein J.E., Zhong S., Hamelin R.C.,
RA   Grigoriev I.V., Szabo L.J., Martin F.;
RT   "Obligate biotrophy features unraveled by the genomic analysis of rust
RT   fungi.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:9166-9171(2011).
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|ARBA:ARBA00011355, ECO:0000256|RuleBase:RU365077}.
CC   -!- SIMILARITY: Belongs to the F-actin-capping protein alpha subunit
CC       family. {ECO:0000256|RuleBase:RU365077}.
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DR   EMBL; GL883098; EGG09139.1; -; Genomic_DNA.
DR   RefSeq; XP_007407499.1; XM_007407437.1.
DR   AlphaFoldDB; F4REQ0; -.
DR   STRING; 747676.F4REQ0; -.
DR   EnsemblFungi; EGG09139; EGG09139; MELLADRAFT_34510.
DR   GeneID; 18927391; -.
DR   KEGG; mlr:MELLADRAFT_34510; -.
DR   VEuPathDB; FungiDB:MELLADRAFT_34510; -.
DR   eggNOG; KOG0836; Eukaryota.
DR   HOGENOM; CLU_045161_3_0_1; -.
DR   InParanoid; F4REQ0; -.
DR   OrthoDB; 179910at2759; -.
DR   Proteomes; UP000001072; 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   PANTHER; PTHR10653; F-ACTIN-CAPPING PROTEIN SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR10653:SF0; F-ACTIN-CAPPING PROTEIN SUBUNIT ALPHA; 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.
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:UP000001072}.
SQ   SEQUENCE   280 AA;  31693 MW;  FD519D0E0D8E0524 CRC64;
     MEHEPSLEEK ISVASNFILQ SPPGEVNDVF NDVRPIVGDD AELENGLLPA LSQYNTEQLT
     LVELPNAKIP AMICEAAKLN EGIENLYMDP NSSQTFIFDH LRLTVKDVKA YTPKKDTIEE
     TRFEISNQAE KYVKEHYQGG VWKVSNEVED EEKKFQLYIV GNKYNPGNYW TGRWRSIYEI
     DLTSGTVKGQ IQVNVHYYEQ GNVSLSSSFL TNSCSGSGSV TASQVIKSIS QAETAYQKSV
     NLAYMELGDD TFKQLRRALP VTKQKIDWNN IKTKIVFNDK
//
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