ID   ACT_AJECG               Reviewed;         375 AA.
AC   P53455; C0NZY1;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 2.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Actin;
GN   ORFNames=HCBG_08711;
OS   Ajellomyces capsulatus (strain G186AR / H82 / ATCC MYA-2454 / RMSCC 2432)
OS   (Darling's disease fungus) (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=447093;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9229331; DOI=10.1080/02681219780001091;
RA   El-Rady J., Shearer G. Jr.;
RT   "Cloning and analysis of an actin-encoding cDNA from the dimorphic
RT   pathogenic fungus Histoplasma capsulatum.";
RL   J. Med. Vet. Mycol. 35:159-166(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G186AR / H82 / ATCC MYA-2454 / RMSCC 2432;
RA   Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA   Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA   Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA   Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA   Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA   Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA   San-Blas G., Taylor J., Mendoza L., Galagan J.E., Nusbaum C., Birren B.W.;
RT   "The genome sequence of Ajellomyces capsulatus strain G186AR.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Actins are highly conserved proteins that are involved in
CC       various types of cell motility and are ubiquitously expressed in all
CC       eukaryotic cells.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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DR   EMBL; U17498; AAA57122.1; -; mRNA.
DR   EMBL; GG663379; EEH03071.1; -; Genomic_DNA.
DR   AlphaFoldDB; P53455; -.
DR   SMR; P53455; -.
DR   STRING; 447093.P53455; -.
DR   PRIDE; P53455; -.
DR   EnsemblFungi; EEH03071; EEH03071; HCBG_08711.
DR   VEuPathDB; FungiDB:HCBG_08711; -.
DR   HOGENOM; CLU_027965_0_2_1; -.
DR   InParanoid; P53455; -.
DR   OrthoDB; 649708at2759; -.
DR   Proteomes; UP000001631; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   InterPro; IPR004000; Actin.
DR   InterPro; IPR020902; Actin/actin-like_CS.
DR   InterPro; IPR004001; Actin_CS.
DR   InterPro; IPR043129; ATPase_NBD.
DR   PANTHER; PTHR11937; PTHR11937; 1.
DR   Pfam; PF00022; Actin; 1.
DR   PRINTS; PR00190; ACTIN.
DR   SMART; SM00268; ACTIN; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
DR   PROSITE; PS00406; ACTINS_1; 1.
DR   PROSITE; PS00432; ACTINS_2; 1.
DR   PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Cytoskeleton; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..375
FT                   /note="Actin"
FT                   /id="PRO_0000088887"
FT   CONFLICT        29
FT                   /note="A -> S (in Ref. 1; AAA57122)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        319
FT                   /note="A -> R (in Ref. 1; AAA57122)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   375 AA;  41609 MW;  74F3A52CAA8BF2B3 CRC64;
     MEEEVAALVI DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH HGIMIGMGQK DSYVGDEAQS
     KRGILTLRYP IEHGVVTNWD DMEKIWHHTF YNELRVAPEE HPVLLTEAPI NPKSNREKMT
     QIVFETFNAP AFYVSIQAVL SLYASGRTTG IVLDSGDGVT HVVPIYEGFA LPHAISRIDM
     AGRDLTNYLM KILAERGYSF STTAEREIVR DIKEKLCYVA LDFQQEIQTA SQSSSLEKSY
     ELPDGQVITI GNERFRAPEA LFQPSVLGLE SGGIHATTYN AIMKCDVDVR KDLYGNIVMS
     GGTTMYPGIS DRMQKEITAL APSSMKVKII APPERKYSVW IGGSILASLS TFQQMWISKQ
     EYDESGPSIV HRKCF