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Database: UniProt
Entry: A0A099Z3Q9_TINGU
LinkDB: A0A099Z3Q9_TINGU
Original site: A0A099Z3Q9_TINGU 
ID   A0A099Z3Q9_TINGU        Unreviewed;       897 AA.
AC   A0A099Z3Q9;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Alpha-actinin-2 {ECO:0000313|EMBL:KGL75430.1};
DE   Flags: Fragment;
GN   ORFNames=N309_13865 {ECO:0000313|EMBL:KGL75430.1};
OS   Tinamus guttatus (White-throated tinamou).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Palaeognathae; Tinamiformes; Tinamidae; Tinamus.
OX   NCBI_TaxID=94827 {ECO:0000313|EMBL:KGL75430.1, ECO:0000313|Proteomes:UP000053641};
RN   [1] {ECO:0000313|EMBL:KGL75430.1, ECO:0000313|Proteomes:UP000053641}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N309 {ECO:0000313|EMBL:KGL75430.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the alpha-actinin family.
CC       {ECO:0000256|ARBA:ARBA00010255}.
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DR   EMBL; KL887945; KGL75430.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A099Z3Q9; -.
DR   STRING; 94827.A0A099Z3Q9; -.
DR   Proteomes; UP000053641; Unassembled WGS sequence.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   CDD; cd21214; CH_ACTN_rpt1; 1.
DR   CDD; cd21216; CH_ACTN_rpt2; 1.
DR   CDD; cd00051; EFh; 1.
DR   CDD; cd00176; SPEC; 1.
DR   Gene3D; 1.20.58.60; -; 4.
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   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   InterPro; IPR002017; Spectrin_repeat.
DR   PANTHER; PTHR11915:SF429; ALPHA-ACTININ-2; 1.
DR   PANTHER; PTHR11915; SPECTRIN/FILAMIN RELATED CYTOSKELETAL PROTEIN; 1.
DR   Pfam; PF00307; CH; 2.
DR   Pfam; PF13499; EF-hand_7; 1.
DR   Pfam; PF08726; EFhand_Ca_insen; 1.
DR   Pfam; PF00435; Spectrin; 4.
DR   SMART; SM00033; CH; 2.
DR   SMART; SM00054; EFh; 2.
DR   SMART; SM01184; efhand_Ca_insen; 1.
DR   SMART; SM00150; SPEC; 2.
DR   SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF46966; Spectrin repeat; 4.
DR   PROSITE; PS00019; ACTININ_1; 1.
DR   PROSITE; PS00020; ACTININ_2; 1.
DR   PROSITE; PS50021; CH; 2.
DR   PROSITE; PS50222; EF_HAND_2; 2.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053641};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          41..145
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          154..260
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          756..791
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          792..827
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   COILED          275..302
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          674..701
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KGL75430.1"
FT   NON_TER         897
FT                   /evidence="ECO:0000313|EMBL:KGL75430.1"
SQ   SEQUENCE   897 AA;  104302 MW;  FFB91A0B85E4E8F0 CRC64;
     LGSMNQIETN MQYTYNYEED EYMIQEEEWD RDLLLDPAWE KQQRKTFTAW CNSHLRKAGT
     QIENIEEDFR NGLKLMLLLE VISGERLPKP DRGKMRFHKI ANVNKALDYI ASKGVKLVSI
     GAEEIVDGNV KMTLGMIWTI ILRFAIQDIS VEETSAKEGL LLWCQRKTAP YRNVNIQNFH
     LSWKDGLGLC ALIHRHRPDL IDYSKLTKDD PIGNINLAME IAEKHLDIPK MLDAEDIVNT
     PKPDERAIMT YVSCFYHAFA GAEQAETAAN RICKVLAVNQ ENERLMEEYE RLASELLEWI
     RRTIPWLENR TPEKTMQAMQ KKLEDFRDYR RKHKPPKVQE KCQLEINFNT LQTKLRISNR
     PAFMPSEGKM VSDIAGAWQR LEQAEKGYEE WLLNEIRRLE RLEHLAEKFR QKATTHEHWA
     YGKEQILLQK DYESASLTEV RAMLRKHEAF ESDLAAHQDR VEQIAAIAQE LNELDYHDAA
     SVNDRCQKIC DQWDRLGTLT QKRREALERT EKLLETIDQL HLEFAKRAAP FNNWMEGAME
     DLQDMFIVHS IEEIQSLISA HDQFKATLPE ADGERQAILS IQNEVEKVIQ SYNMRISATN
     PYSTVTVEEI RTKWEKVKQL VPQRDQSLQE ELARQHANER LRRQFAAQAN VIGPWIQTKM
     EEIARSSIEM TGPLEDQMNQ LKQYEHNIIN YKTNIDRLEG DHQLIQEALV FDNKHTNYTM
     EHIRVGWELL LTTIARTINE VETQILTRDA KGITQEQMNE FRASFNHFDR RKNGLMDHDD
     FRACLISMGY DLGEAEFARI MSLVDPNGQG TVTFQSFIDF MTRETADTDT AEQVIASFRI
     LASDKPYILA DELRRELPPD QAQYCIKRMP PYTGPGSVPG ALDYTSFSSA LYGESDL
//
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