Unfortunately due to lack of commercial feasibility, the SkyBLAST service has been suspended from December 1st, 2025.
All subscriptions for paid accounts have been paused. For further information or enquiries, please email [email protected]
LOCUS XP_013113312 531 aa linear INV 02-SEP-2023 ACCESSION XP_013113312 VERSION XP_013113312.1 DBLINK BioProject: PRJNA1009844 DBSOURCE REFSEQ: accession XM_013257858.2 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..531 /organism="Stomoxys calcitrans" /db_xref="taxon:35570" /chromosome="4" Protein 1..531 /product="T-complex protein 1 subunit zeta" /calculated_mol_wt=58219 Region 7..526 /region_name="TCP1_zeta" /note="TCP-1 (CTT or eukaryotic type II) chaperonin family, zeta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL)...; cd03342" /db_xref="CDD:239458" Site order(11,15,43..46,48,66,68,72,76,79,381,517..523) /site_type="other" /note="ring oligomerisation interface [polypeptide binding]" /db_xref="CDD:239458" Site order(38..40,90,94,154,393,411,451,494,496) /site_type="other" /note="ATP/Mg binding site [chemical binding]" /db_xref="CDD:239458" Site order(431,449,458,460..461,464) /site_type="active" /note="stacking interactions [active]" /db_xref="CDD:239458" CDS 1..531 /gene="LOC106091364" /coded_by="XM_013257858.2:134..1729" /db_xref="GeneID:106091364" ORIGIN 1 masisllnpk aefaraanal ainisaakgl qdvmrtnlgp kgtmkmlvsg agdikitkdg 61 nvllhemqiq hptasmiara staqddstgd gttstvllig ellkqadifl aeglhprivt 121 egfekareqa lavletmkip ievnkknlte vartslktkv haaladlltd vcvdailair 181 qdekpvdlhm veimemqhkt atdtslikgl vmdhgsrhpd mpkrlekayi ltcnvsmeye 241 ksevnsgffy ktaeerekfv kaerefidqr vqkiielkrk vcdgtdksfv vinqkgidpm 301 sldalakegi malrrakrrn merlalacgg tamnsvddle eshlgyagvv yehvlgenky 361 tfveecknpq svtilikgpn khtivqikda irdglrainn aindkcvvpg asafevrayn 421 qlmkhkdtvk gkvrlgiqaf aeallvipkn lainsgydaq dtivklteed rlnpdpvgld 481 lstgepmkpv dlgvydnyiv kkqtlnscsv iasnlllvde vmragmtslk g