ID A0A1I8QBI1_STOCA Unreviewed; 1101 AA.
AC A0A1I8QBI1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=BPL/LPL catalytic domain-containing protein {ECO:0000259|PROSITE:PS51733};
GN Name=106086242 {ECO:0000313|EnsemblMetazoa:SCAU015647-PA};
OS Stomoxys calcitrans (Stable fly) (Conops calcitrans).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC Muscidae; Stomoxys.
OX NCBI_TaxID=35570 {ECO:0000313|EnsemblMetazoa:SCAU015647-PA, ECO:0000313|Proteomes:UP000095300};
RN [1] {ECO:0000313|EnsemblMetazoa:SCAU015647-PA}
RP IDENTIFICATION.
RC STRAIN=USDA {ECO:0000313|EnsemblMetazoa:SCAU015647-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- SIMILARITY: Belongs to the biotin--protein ligase family.
CC {ECO:0000256|ARBA:ARBA00009934}.
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DR RefSeq; XP_013106279.1; XM_013250825.1.
DR AlphaFoldDB; A0A1I8QBI1; -.
DR EnsemblMetazoa; SCAU015647-RA; SCAU015647-PA; SCAU015647.
DR VEuPathDB; VectorBase:SCAU015647; -.
DR OrthoDB; 317678at2759; -.
DR Proteomes; UP000095300; Unassembled WGS sequence.
DR GO; GO:0004077; F:biotin-[acetyl-CoA-carboxylase] ligase activity; IEA:InterPro.
DR GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004408; Biotin_CoA_COase_ligase.
DR InterPro; IPR003142; BPL_C.
DR InterPro; IPR004143; BPL_LPL_catalytic.
DR NCBIfam; TIGR00121; birA_ligase; 1.
DR PANTHER; PTHR12835; BIOTIN PROTEIN LIGASE; 1.
DR PANTHER; PTHR12835:SF5; BIOTIN--PROTEIN LIGASE; 1.
DR Pfam; PF02237; BPL_C; 1.
DR Pfam; PF03099; BPL_LplA_LipB; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000256|ARBA:ARBA00022598}.
FT DOMAIN 831..1025
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
FT REGION 209..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1101 AA; 122598 MW; E1478D01C1D3061F CRC64;
MLTLYYVSAT FLQSWRINKI CQKISEQLSQ QATIAFYALP QNRDDGFYSR LATSELCQNR
QVAKVTEILW LHDHYRGCCL MPLQSLHTSA WISFPEAPGL LPFHFGKAPE SLQRSLSLDR
HGGLIRLLLE TETTPCYDAE LWQKDIVRIE NYAVKNDGDP QPYSLLCSHL RKPVRSAEEC
LPEDWAKHLE DLRALSVLAN QAIEYTSSKS RNEPKATTGA IKPDLIPQEK RSEIEIKKEK
ESPKKPQKAM NKTLEEVPEI SKKDVLADVK PAEVKLAVRD TEKFIKAEQT NETKPNEAKT
SPNVQQASPS KLRAKPTEIR KPGALDTGRF KTTKASENLI EAESKKSSEL ERIAASKAAE
ISKSKSPTKD NEAKYAKQPS TTLTSSSPAV AGQNDVPSTK STASLSQVTK DQEKTPKIPQ
VAEPLSEPTK SIPTDSIPKI ESVDKTASKT TTPATTTAAS SNINTPKPTV ATTTASVSSA
GITSSPLKDN TKRPSLKRHK DSIKECKPLN VLVYAETATA RESAITILKE ILAENTYTIY
PMTQQQVEQQ HWLNTTALLV VCGSVVNSMG ELFVDYFLHG GKVLSLCSDV LHFILPTYRT
AEVREHELVQ FSYDKWQKVK MMHHIFCYQP SPVKKNFSTD SDDSAHATNR KPALVCLPRS
VELKDLKGHL HRLDVKVLGT EETWNTPSLL LAHNQKSGGS AVFSQVHLEI SPSEFESDEA
KYSILKQNDK IRHEIFSDLL KNHLSLSVKS EKVNANGSGP KCVFKKAYFL GKHEAKFELL
GKLKDKCDGD NVIATPNLMI KFCGPDDKLP NVNSNILPIL IHSCPEDFST VDYFDNLKTR
YVGRLVIYAP VVSSSQHVVA DLELSNGIAV IPRQQTDGVG RSNNQWLSPL GCVMYSIQLH
VSLNSPLGKR LPLLQHVIGA AMVHTLKGHD QYKVLNIGLK WPNDAYANGV TKIGGLMVRT
TLNGTNAIVN IGCGINLDNS KPTICVNDMI REYNHANQKN LPLLKYEQFI AMMFNEIEQL
VELIQNGDFD KFYKIYYDLW LHSDQSISIC DKDGSTKDVK ILGIDEYGFL QVKLANGLTE
IVHPDGNSFD ILKGLIVPKF N
//