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LOCUS XP_013107483 399 aa linear INV 02-SEP-2023 isoform X2 [Stomoxys calcitrans]. ACCESSION XP_013107483 VERSION XP_013107483.1 DBLINK BioProject: PRJNA1009844 DBSOURCE REFSEQ: accession XM_013252029.2 KEYWORDS RefSeq. SOURCE Stomoxys calcitrans (stable fly) ORGANISM Stomoxys calcitrans Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea; Muscidae; Stomoxys. COMMENT MODEL REFSEQ: This record is predicted by automated computational analysis. This record is derived from a genomic sequence (NC_081555) annotated using gene prediction method: Gnomon. Also see: Documentation of NCBI's Annotation Process ##Genome-Annotation-Data-START## Annotation Provider :: NCBI RefSeq Annotation Status :: Full annotation Annotation Name :: GCF_963082655.1-RS_2023_08 Annotation Pipeline :: NCBI eukaryotic genome annotation pipeline Annotation Software Version :: 10.1 Annotation Method :: Best-placed RefSeq; Gnomon; cmsearch; tRNAscan-SE Features Annotated :: Gene; mRNA; CDS; ncRNA Annotation Date :: 08/29/2023 ##Genome-Annotation-Data-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..399 /organism="Stomoxys calcitrans" /db_xref="taxon:35570" /chromosome="4" Protein 1..399 /product="pyruvate dehydrogenase E1 component subunit alpha, mitochondrial isoform X2" /calculated_mol_wt=43928 Region 34..391 /region_name="TPP_enzymes" /note="Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. These enzymes include, among others, the E1 components of the pyruvate, the acetoin and...; cl01629" /db_xref="CDD:470272" Site order(92,144,169..170,201,203..206,209,213,217,232..235, 249,299,303) /site_type="other" /note="tetramer interface [polypeptide binding]" /db_xref="CDD:238958" Site order(122..123,169,171,199..202,229,231,295) /site_type="other" /note="TPP-binding site [chemical binding]" /db_xref="CDD:238958" Site order(164,166,168,173,176..177,180..181,183..184,187, 206..207,213..214,217) /site_type="other" /note="heterodimer interface [polypeptide binding]" /db_xref="CDD:238958" Site order(290..296,298..308,317..319) /site_type="phosphorylation" /note="phosphorylation loop region [posttranslational modification]" /db_xref="CDD:238958" CDS 1..399 /gene="LOC106087108" /coded_by="XM_013252029.2:144..1343" /db_xref="GeneID:106087108" ORIGIN 1 mlrqlnrage fpkvvkqlqk ssavagtqks nnyateatvq vqrpyklhrl dqgpettvki 61 tkdqaltyyt qmqtirrlet sagnlykeki irgfchlysg qeacavgmra amrdvdniis 121 ayrvhgwtyl mgvsplgvla eltgrqsgca kgkggsmhmy cpnfyggngi vgaqvplgag 181 valackykgn ggmclalygd gaanqgqvfe aynmaylwkl pvifvcennn ygmgtsaera 241 ssntdyytrg dalpgiwvdg mdvlavrsat efaidyvnkn gplvmetnty rysghsmsdp 301 gtsyrtreei qevrqkrdpi tsfkemcieq glittdevka idtkvrkevd eataqakada 361 elplsglwtd vysqclepki rncvehnikh vqqnkganh