ID A0A0G2ICF2_9EURO Unreviewed; 726 AA.
AC A0A0G2ICF2;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 13-SEP-2023, entry version 34.
DE RecName: Full=Alpha-actinin {ECO:0008006|Google:ProtNLM};
GN ORFNames=EMCG_06382 {ECO:0000313|EMBL:KKZ67950.1};
OS Emmonsia crescens UAMH 3008.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emmonsia.
OX NCBI_TaxID=1247875 {ECO:0000313|EMBL:KKZ67950.1, ECO:0000313|Proteomes:UP000034164};
RN [1] {ECO:0000313|Proteomes:UP000034164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 3008 {ECO:0000313|Proteomes:UP000034164};
RX PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA Clay O.K., Klein B.S., Cuomo C.A.;
RT "The dynamic genome and transcriptome of the human fungal pathogen
RT Blastomyces and close relative Emmonsia.";
RL PLoS Genet. 11:E1005493-E1005493(2015).
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:KKZ67950.1}.
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DR EMBL; LCZI01000173; KKZ67950.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2ICF2; -.
DR VEuPathDB; FungiDB:EMCG_06382; -.
DR Proteomes; UP000034164; 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; cd21215; CH_SpAIN1-like_rpt1; 1.
DR CDD; cd21291; CH_SpAIN1-like_rpt2; 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:SF435; SPECTRIN BETA CHAIN, NON-ERYTHROCYTIC 5; 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; PS00019; ACTININ_1; 1.
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 Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 86..191
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 200..306
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 560..595
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 705..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 726 AA; 83455 MW; 0E080123819B1346 CRC64;
MQLPHPPQLI HHSSSSSSSS SSSHNLPPPQ SHRHYNHYDF FPNRTLNPYR CFHSNSYLYH
RRTGTGIGFA SPNRVMLLME EKQWITVQQK TFTKWLNNKL KARDLTIDDL VKDLSDGVIL
IHILEILGNE SLGRYASKPK LRVQKFENAN KSLDYVKGRG IQMTNIGAED IVDGNRKIIL
GLIWTLILRF TISDISEEGM TAKEGLLLWC QRKTACYPGV EVRDFSASWN DGLAFCALLD
IHRPDLIDFD SLDKNDHKGN MQLAFDIASN DIGIPDLLDV EDVCDVAKPD ERSLMTYIAY
WFHAFSQLER VENAGRRVEK FVMNMQGAWE MQNSFERRMK ELLQAIRGQR AEWHESSFEG
TYTDAKEQAS KFGAYKRNQK RKWVAEKSDL AALLGNIKTK LSTYRLRAYE PPPELRLEVL
DQEWSTLTQN ERERSQLINE TIRDIKNALR RSFADKANDF ALTLNTLSLA ISGLEGDVED
QLSHVQRLSD NLPPLDAFLE TIAEMEERCI EANIEENDFT TYTYDELAYE LGLVKSSVSK
KLAFLENQTV ARNMTNLTPI QLEEFESVFR HFDRDASNTL HEIEFSAALA SLGLVYDEEE
MHEVYLETCG PARVERNAGV SFEQFIRFMV SVTEDQNTAE QVFQSFKEVA DGKPYVTELD
LRHSLIPEEL IDNLLETMPR HDGPDLLEDR EMPKYDYITF MEKMMNDGDG DDEDERGESS
RLVNGI
//
