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Database: UniProt
Entry: A0A364L7D3_9EURO
LinkDB: A0A364L7D3_9EURO
Original site: A0A364L7D3_9EURO 
ID   A0A364L7D3_9EURO        Unreviewed;       641 AA.
AC   A0A364L7D3;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Alpha-actinin {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BHQ10_007737 {ECO:0000313|EMBL:RAO71725.1};
OS   Talaromyces amestolkiae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=1196081 {ECO:0000313|EMBL:RAO71725.1, ECO:0000313|Proteomes:UP000249363};
RN   [1] {ECO:0000313|EMBL:RAO71725.1, ECO:0000313|Proteomes:UP000249363}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIB {ECO:0000313|EMBL:RAO71725.1,
RC   ECO:0000313|Proteomes:UP000249363};
RX   PubMed=28649280; DOI=10.1186/s13068-017-0844-7;
RA   de Eugenio L.I., Mendez-Liter J.A., Nieto-Dominguez M., Alonso L.,
RA   Gil-Munoz J., Barriuso J., Prieto A., Martinez M.J.;
RT   "Differential ?-glucosidase expression as a function of carbon source
RT   availability in Talaromyces amestolkiae: a genomic and proteomic
RT   approach.";
RL   Biotechnol. Biofuels 10:161-161(2017).
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:RAO71725.1}.
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DR   EMBL; MIKG01000016; RAO71725.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A364L7D3; -.
DR   STRING; 1196081.A0A364L7D3; -.
DR   OrthoDB; 2872403at2759; -.
DR   Proteomes; UP000249363; 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; IPR018247; EF_Hand_1_Ca_BS.
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; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Reference proteome {ECO:0000313|Proteomes:UP000249363};
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"
SQ   SEQUENCE   641 AA;  73456 MW;  92872596F3F49F44 CRC64;
     MLMVEKQWIL VQQKTFTKWL NNKLKVRNLA ISDLTQDLSD GVNLIHLLEI LGDESLGRYA
     SKPKLRVQKF ENVNKGLDFI KLRGIQMTNI GAGDIVDGNQ KIILGLIWTL ISKFTISDIS
     SEGMSAKEGL LLWCQRKTAC YPEVEVRDFS ASWNDGLAFC ALLDIHRPDL IDFDSLDKND
     HRGNMQLAFD IAANEIGIPD LLDVEDVCDV DKPDERSLMT YIAYWFHAFS QLEKVENAGR
     RVEKFVSNMQ GAWEMQSSYE KRMKELLAQI ANQRAEWQGA SFEGTYTDAK VQLAEFSHYK
     RNQKRKWVAE KSDLAALLGN IKTKLSTYRL RPYEPPADLS LDRCDRDWEG LMQEEQGRSQ
     LINETIRDIK NKLRRSFADK ANDFALTLKT LTLAISGLEG DVEDQLTHVK RLNDNLPPLD
     AFLETIADLE EQCVEANIDE NDYTTYTLDE LSYELGLVKS SVAKKLAFLE NQMVARNMTN
     LTPIQLEEFE SVFRHFDRDG SNTLQEIEFS AALASLGLVY DEEEMHEVFL ETCGRNSTVS
     FEQFIRFMVS VTEDQNTAEQ VFQSFREVAD GKPYVTELDL RHSLIPDELI DNLLESMPKH
     EGPDLLEDRD LPKYDYITFM EKMMDNQGTS EDTKRSLNGG H
//
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