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LOCUS XP_016996044 336 aa linear INV 09-DEC-2024 ACCESSION XP_016996044 VERSION XP_016996044.3 DBLINK BioProject: PRJNA1194641 DBSOURCE REFSEQ: accession XM_017140555.3 KEYWORDS RefSeq; includes ab initio. SOURCE Drosophila takahashii ORGANISM Drosophila takahashii Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; Drosophilidae; Drosophila; Sophophora. COMMENT MODEL REFSEQ: This record is predicted by automated computational analysis. This record is derived from a genomic sequence (NC_091683) annotated using gene prediction method: Gnomon. Also see: Documentation of NCBI's Annotation Process On Dec 9, 2024 this sequence version replaced XP_016996044.2. ##Genome-Annotation-Data-START## Annotation Provider :: NCBI RefSeq Annotation Status :: Full annotation Annotation Name :: GCF_030179915.1-RS_2024_12 Annotation Pipeline :: NCBI eukaryotic genome annotation pipeline Annotation Software Version :: 10.3 Annotation Method :: Gnomon; cmsearch; tRNAscan-SE Features Annotated :: Gene; mRNA; CDS; ncRNA Annotation Date :: 12/07/2024 ##Genome-Annotation-Data-END## ##RefSeq-Attributes-START## ab initio :: 41% of CDS bases ##RefSeq-Attributes-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..336 /organism="Drosophila takahashii" /strain="IR98-3 E-12201" /db_xref="taxon:29030" /chromosome="X" /sex="female" /tissue_type="Whole fly" /dev_stage="Adult fly" /collected_by="Originally obtained from EHIME-Fly" Protein 1..336 /product="fibroleukin-like" /calculated_mol_wt=38524 Region 43..>120 /region_name="EnvC" /note="Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning]; COG4942" /db_xref="CDD:443969" Region 132..330 /region_name="FReD" /note="Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is involved in blood clotting, being activated by thrombin to assemble into fibrin clots. The N-termini of 2 times 3 chains come together to form a globular...; cd00087" /db_xref="CDD:238040" Site 235 /site_type="other" /note="gamma-gamma dimer interface [polypeptide binding]" /db_xref="CDD:238040" Site order(264,266,268) /site_type="other" /note="Ca2+ binding site [ion binding]" /db_xref="CDD:238040" Site order(272,275..276,285..286) /site_type="active" /note="polymerization pocket [active]" /db_xref="CDD:238040" CDS 1..336 /gene="LOC108056674" /coded_by="XM_017140555.3:1..1011" /db_xref="GeneID:108056674" ORIGIN 1 misrlaflls vflinelsii ganpdnfeik nvvvmninhq ptanqdnqir dqneelknqi 61 knitqllknt dekvsfmsts ignlqrnlei arneiqnket qinditkkls nqiselkddl 121 fkcqprsscp vegpngiyni tvgdihafea pcnstgwlti qkrfdgsenf drtwkdykdg 181 fgniegeffi glerlhimtq aqphelriel gmvngstsya hyddfkigse eelyeleslg 241 iyngtagdsl kdhnekkftt hdrdndeskr ncatkewggw wytscarskl nakyhkegys 301 ehndgitwgs whnsnytysl tfvemmirpk tlktev