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Database: UniProt
Entry: A8Q512_MALGO
LinkDB: A8Q512_MALGO
Original site: A8Q512_MALGO 
ID   A8Q512_MALGO            Unreviewed;       351 AA.
AC   A8Q512;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   22-FEB-2023, entry version 78.
DE   RecName: Full=F-actin-capping protein subunit alpha {ECO:0000256|ARBA:ARBA00014038, ECO:0000256|RuleBase:RU365077};
GN   ORFNames=MGL_2694 {ECO:0000313|EMBL:EDP43098.1};
OS   Malassezia globosa (strain ATCC MYA-4612 / CBS 7966) (Dandruff-associated
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX   NCBI_TaxID=425265 {ECO:0000313|EMBL:EDP43098.1, ECO:0000313|Proteomes:UP000008837};
RN   [1] {ECO:0000313|EMBL:EDP43098.1, ECO:0000313|Proteomes:UP000008837}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4612 / CBS 7966 {ECO:0000313|Proteomes:UP000008837};
RX   PubMed=18000048; DOI=10.1073/pnas.0706756104;
RA   Xu J., Saunders C.W., Hu P., Grant R.A., Boekhout T., Kuramae E.E.,
RA   Kronstad J.W., Deangelis Y.M., Reeder N.L., Johnstone K.R., Leland M.,
RA   Fieno A.M., Begley W.M., Sun Y., Lacey M.P., Chaudhary T., Keough T.,
RA   Chu L., Sears R., Yuan B., Dawson T.L.Jr.;
RT   "Dandruff-associated Malassezia genomes reveal convergent and divergent
RT   virulence traits shared with plant and human fungal pathogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:18730-18735(2007).
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|ARBA:ARBA00010479, ECO:0000256|RuleBase:RU365077}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EDP43098.1}.
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DR   EMBL; AAYY01000009; EDP43098.1; -; Genomic_DNA.
DR   RefSeq; XP_001730312.1; XM_001730260.1.
DR   AlphaFoldDB; A8Q512; -.
DR   STRING; 425265.A8Q512; -.
DR   GeneID; 5854617; -.
DR   KEGG; mgl:MGL_2694; -.
DR   VEuPathDB; FungiDB:MGL_2694; -.
DR   InParanoid; A8Q512; -.
DR   OMA; YNLRNFW; -.
DR   OrthoDB; 179910at2759; -.
DR   Proteomes; UP000008837; 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: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.
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:UP000008837}.
SQ   SEQUENCE   351 AA;  39784 MW;  A184E6A62F9CCFBB CRC64;
     MSGVNNDAIQ ACLELILQSP PGQQSHIVSD LKGMLAGAVP DTEWMERVRS ILLQYTHEQL
     LHVTIEHEGK QDSAIVCDAA KMDDKYYHPR LSCSFSYDPI HESVSEVSSV PRSTGDIETL
     RAEVDQQLSK YVLNHYHTGV SCAYLPRLVP QATSDANAET VTINAMQDKQ KEKENNLELW
     DEANQEQPVQ QMQGRVDNCD SQVTSENDTP PAITSQPCIL TLHIVGNKYN LRNFWTGRWR
     STYKFDVSTQ AFKHADIQVQ THYFENGNVQ LQAQHSMALP DFVSTKPESL AKDVIQAIEH
     HEQVYQAKLF DATDTLREHA FKALRRTLPI TRQKIDWSKI VSYKVGSDMA K
//
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