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Database: UniProt
Entry: A0A1J9RHJ1_9EURO
LinkDB: A0A1J9RHJ1_9EURO
Original site: A0A1J9RHJ1_9EURO 
ID   A0A1J9RHJ1_9EURO        Unreviewed;       658 AA.
AC   A0A1J9RHJ1;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   13-SEP-2023, entry version 29.
DE   RecName: Full=Alpha-actinin {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ACJ73_01501 {ECO:0000313|EMBL:OJD27101.1};
OS   Blastomyces percursus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX   NCBI_TaxID=1658174 {ECO:0000313|EMBL:OJD27101.1, ECO:0000313|Proteomes:UP000242791};
RN   [1] {ECO:0000313|EMBL:OJD27101.1, ECO:0000313|Proteomes:UP000242791}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EI222 {ECO:0000313|EMBL:OJD27101.1,
RC   ECO:0000313|Proteomes:UP000242791};
RA   Cuomo C.A., Schwartz I.S., Kenyon C., De Hoog G.S., Govender N.P.,
RA   Botha A., Moreno L., De Vries M., Munoz J.F., Stielow J.B.;
RT   "Emmonsia species relationships and genome sequence.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the alpha-actinin family.
CC       {ECO:0000256|ARBA:ARBA00010255}.
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:OJD27101.1}.
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DR   EMBL; LGTZ01000138; OJD27101.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J9RHJ1; -.
DR   STRING; 1658174.A0A1J9RHJ1; -.
DR   VEuPathDB; FungiDB:ACJ73_01501; -.
DR   OrthoDB; 2872403at2759; -.
DR   Proteomes; UP000242791; Unassembled WGS sequence.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR   CDD; cd21291; CH_SpAIN1-like_rpt2; 1.
DR   CDD; cd00051; EFh; 1.
DR   Gene3D; 1.20.58.60; -; 2.
DR   Gene3D; 1.10.418.10; Calponin-like domain; 2.
DR   Gene3D; 1.10.238.10; EF-hand; 2.
DR   InterPro; IPR001589; Actinin_actin-bd_CS.
DR   InterPro; IPR001715; CH_dom.
DR   InterPro; IPR036872; CH_dom_sf.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR014837; EF-hand_Ca_insen.
DR   InterPro; IPR002048; EF_hand_dom.
DR   PANTHER; PTHR11915:SF442; ALPHA-ACTININ, SARCOMERIC-RELATED; 1.
DR   PANTHER; PTHR11915; SPECTRIN/FILAMIN RELATED CYTOSKELETAL PROTEIN; 1.
DR   Pfam; PF00307; CH; 2.
DR   Pfam; PF08726; EFhand_Ca_insen; 1.
DR   SMART; SM00033; CH; 2.
DR   SMART; SM01184; efhand_Ca_insen; 1.
DR   SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF46966; Spectrin repeat; 2.
DR   PROSITE; PS00020; ACTININ_2; 1.
DR   PROSITE; PS50021; CH; 2.
DR   PROSITE; PS50222; EF_HAND_2; 1.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW   Reference proteome {ECO:0000313|Proteomes:UP000242791};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..658
FT                   /note="Alpha-actinin"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013221778"
FT   DOMAIN          14..121
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          130..236
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          490..525
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   REGION          636..658
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   658 AA;  75297 MW;  4BD7DF1FD47F8191 CRC64;
     MHGVLKSLML CSHWLIVAAA VTWLQLNNKL KVRNLAIDDL VKDLSDGVIL IHILEILGNE
     SLGRYASKPK LRVQKFENAN KSLDYVKGRG IQMTNIGAED IVDGNRKIIL GLIWTLILRF
     TISDISEEGM TAKEGLLLWC QRKTACYPGV EVRDFSASWN DGLAFCALLD IHRPDLIDFD
     SLDKNDHKGN MQLAFDIASS DIGIPDLLDV EDVCDVAKPD ERSLMTYIAY WFHAFSQLER
     VENAGRRVEK FVMNMQGAWE MQNSFERRMK ELLQAIRAQR AEWRESLFEG TYADAKEQAS
     KFGAYKRNQK RKWVAEKSDL AALLGNIKTK LSTYRLRAYE PPPELRLEVL DQEWSALTQN
     ERERSQLINE TIRDIKNALR RSFADKANDF ALTLNTLSLA ISGLEGDVED QLSHVQRLND
     NLPPLDAFLE TIAELEERCI EANIEENDFT TYTYDELAYE LGLVKSSVSK KLAFLENQTV
     ARNMTNLTPI QLEEFESVFR HFDRDSSNTL HEIEFSAALA SLGLVYDEEE MHEVFLETCG
     PTRVERNAGV SFEQFIRFMV SVTEDQNTAE QVFQSFKEVA DGKPYVTELD LRHSLIPEEL
     IDNLLETMPR HDGPDLLEDR DIPKYDYITF MERMMNDGDG DDESELSDTR NSHLVNGI
//
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