ID   A0A0F4YF94_TALEM        Unreviewed;       648 AA.
AC   A0A0F4YF94;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   03-MAY-2023, entry version 34.
DE   SubName: Full=Alpha-actinin, sarcomeric (F-actin cross linking protein) {ECO:0000313|EMBL:KKA16308.1};
GN   ORFNames=T310_10105 {ECO:0000313|EMBL:KKA16308.1};
OS   Rasamsonia emersonii CBS 393.64.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Rasamsonia.
OX   NCBI_TaxID=1408163 {ECO:0000313|EMBL:KKA16308.1, ECO:0000313|Proteomes:UP000053958};
RN   [1] {ECO:0000313|EMBL:KKA16308.1, ECO:0000313|Proteomes:UP000053958}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 393.64 {ECO:0000313|EMBL:KKA16308.1,
RC   ECO:0000313|Proteomes:UP000053958};
RA   Heijne W.H., Fedorova N.D., Nierman W.C., Vollebregt A.W., Zhao Z., Wu L.,
RA   Kumar M., Stam H., van den Berg M.A., Pel H.J.;
RL   Submitted (APR-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:KKA16308.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LASV01000793; KKA16308.1; -; Genomic_DNA.
DR   RefSeq; XP_013322920.1; XM_013467466.1.
DR   AlphaFoldDB; A0A0F4YF94; -.
DR   STRING; 1408163.A0A0F4YF94; -.
DR   GeneID; 25313170; -.
DR   OrthoDB; 2872403at2759; -.
DR   Proteomes; UP000053958; 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   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: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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053958};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          10..115
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          124..230
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          484..519
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   REGION          624..648
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          256..306
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   648 AA;  74452 MW;  8CB7314FE186F623 CRC64;
     MLPVEKQWIN VQQKTFTKWI NNKLKVRNIT VEDLVHDLSD GVILIHLLEI LGGESLGRYA
     SKPKLRVQKF ENVNKSLDFI KGRGIQMTNI GAEDVVDGNR KIILGLIWTL ILRFTISDIN
     QEGLSAKEGL LLWCQRKTAC YPEVEIKDFS TSWNDGLAFC ALLDIHRPDL IDFDSLDKND
     HRGNMKLAFD IATNEIGIPD LLDVEDVCDV AKPDERSLMT YIAYWFHAFS QLEKVENAGR
     RVEKFITNMQ GAWEMQSSYE RRMRELLRQI AEQRAQWRES SFEGTYADAK EQLNQLSQYK
     RDKKRKWVAE KSDLAALLGN IKTKLSTYRL RAYEPPPELR PEVLDREWEG LTKDEQERSQ
     LINETIRDIK NALRRSFADK ANDFALTLKT LSMAISGLEG DVEDQLAHVQ RLNDNLPPLD
     AFLETIAELD KQCAEANIEE NDYTTYTLDD LSYELGLVKA SVAKKLAFLE NQMVARNMTN
     LTPIQLEEFE SVFRHFDRDG SNTLHEIEFS AALASLGLVY DEDEMHEVFL QTSGGKSSVT
     FEQFIRFMVS VTEDQNTAEQ VFQSFREVAD GKPYVTELDL RHSLIPDDLI ENLIQTMPRH
     EGPDLLEDRD VPKYDYITFM ERMMDTGNNN GQDQSSGHQK QPSINGGH
//