ID A0A232EQ49_9HYME Unreviewed; 942 AA.
AC A0A232EQ49;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Alpha-actinin, sarcomeric {ECO:0008006|Google:ProtNLM};
GN ORFNames=TSAR_001427 {ECO:0000313|EMBL:OXU20484.1};
OS Trichomalopsis sarcophagae.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Proctotrupomorpha;
OC Chalcidoidea; Pteromalidae; Pteromalinae; Trichomalopsis.
OX NCBI_TaxID=543379 {ECO:0000313|EMBL:OXU20484.1, ECO:0000313|Proteomes:UP000215335};
RN [1] {ECO:0000313|EMBL:OXU20484.1, ECO:0000313|Proteomes:UP000215335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Alberta {ECO:0000313|EMBL:OXU20484.1,
RC ECO:0000313|Proteomes:UP000215335};
RC TISSUE=Whole body {ECO:0000313|EMBL:OXU20484.1};
RX PubMed=28648823; DOI=10.1016/j.cub.2017.05.032;
RA Martinson E.O., Mrinalini, Kelkar Y.D., Chang C.H., Werren J.H.;
RT "The Evolution of Venom by Co-option of Single-Copy Genes.";
RL Curr. Biol. 27:2007-2013(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:OXU20484.1}.
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DR EMBL; NNAY01002827; OXU20484.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A232EQ49; -.
DR STRING; 543379.A0A232EQ49; -.
DR Proteomes; UP000215335; Unassembled WGS sequence.
DR GO; GO:0043232; C:intracellular non-membrane-bounded organelle; IEA:UniProt.
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; cd21214; CH_ACTN_rpt1; 1.
DR CDD; cd21216; CH_ACTN_rpt2; 1.
DR CDD; cd00051; EFh; 1.
DR CDD; cd00176; SPEC; 3.
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; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
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; 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; 4.
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; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000215335};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 15..119
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 128..233
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 796..831
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 837..872
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT COILED 315..342
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 473..500
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 721..784
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 942 AA; 108561 MW; 1207117C46068B06 CRC64;
MRDEIGFSAF TELAYSESAT FTAWCNSHLR KAGTAIESIE EDFRNGLKLM LLLEVISGET
LPKPDRGKMR FHKIANVNKA LDYIASKGVK LVSIGAEEIV DGNLKMTLGM IWTIILRFAI
QDISVEEMTA KEGLLLWCQR KTAPYKNVNV QNFHLSFKDG LAFCALIHRH RPDLIDYHKL
SKDNPLENLN TAFDVAEKYL DIPRMLDPDG MEDTIWNLPM TIRLTVCFIL FTCTLLYSDI
DLINTPKPDE RAIMTYVSCY YHAFQGAQQN LDSLIDMRNT AMPDERAVMT YVSSYYHCFS
GAQKAETAAN RICKVLKVNQ ENERLMEEYE RLASDLLEWI RRTMPWLNSR QTDNSLAGCQ
KKLEEYRTYR RKHKPPRVEQ KAKLETNFNT LQTKLRLSNR PAYMPTEGKM VSDINKAWKG
LETAEKAFED WLLSEMMRLE RLEHLAQKFK HKADAHEDWT AGKEEMLTSQ HFRQCKLNEL
KALKKKHEAF ESDLAAHQDR VEQIAAIAQE LNTLEYHDSA SVNARCQRIC DQWDRLGTLT
QRRRQALDEA ERILEKIDVL HLEFAKRAAP FNNWLDGTRE DLVDMFIVHT MEEIQGLMDA
HSAFKATLGE ADKEYNSIVG LVREVESIVK QFQIPGGLEN PYTTLTALDL TKKWSDVRQL
VPQRDGTLAA ELRKQQNNEL LRRQFAEKAN AVGPWIERQL DAVTAIGLGL QGTLEDQLHR
LKEYEQAVYA YKAHLEELEK IHQAVQEGMI FENRYTQYTM ETLRVGWEQL LTSINRNINE
VENQILTRDS KGITQEQLSE FRSSFNHFDK NRTGRLSPEE FKSCLVSLGY SIGKDRQGDI
DFQRILAIVD PNNSGYVQFD AFLDFMTRES TDTDTAEQVI DSFRILAGDK PYILADELRR
ELPPDQAEYC ILRMPPYKGP NAIAGALDYR SFSTALYGES DL
//
