ID A0A1I8Q8K0_STOCA Unreviewed; 568 AA.
AC A0A1I8Q8K0;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial {ECO:0008006|Google:ProtNLM};
GN Name=106086249 {ECO:0000313|EnsemblMetazoa:SCAU014861-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:SCAU014861-PA, ECO:0000313|Proteomes:UP000095300};
RN [1] {ECO:0000313|EnsemblMetazoa:SCAU014861-PA}
RP IDENTIFICATION.
RC STRAIN=USDA {ECO:0000313|EnsemblMetazoa:SCAU014861-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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DR RefSeq; XP_013106292.1; XM_013250838.1.
DR AlphaFoldDB; A0A1I8Q8K0; -.
DR STRING; 35570.A0A1I8Q8K0; -.
DR EnsemblMetazoa; SCAU014861-RA; SCAU014861-PA; SCAU014861.
DR GeneID; 106086249; -.
DR KEGG; scac:106086249; -.
DR VEuPathDB; VectorBase:SCAU014861; -.
DR OrthoDB; 1129179at2759; -.
DR Proteomes; UP000095300; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.700.40; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR001882; Biotin_BS.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT DOMAIN 1..344
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 16..214
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 487..563
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 568 AA; 63035 MW; C235EF4F578C823D CRC64;
MGSPAIRAKG IKNTSKHIMD AAGVPIINGY HGEDQTDERL QQEAKKIGFP LMIKAVRGGG
GKGMRIAEKP EDFMDALNSA RTESQKSFGD SSVLLERYVR SPRHVEVQVF ADQYGNAVYL
WERDCSVQRR HQKIIEEAPA PGLSEELRRE LGEAAVRAAK AVGYVGAGTV EFIMDKEDLS
FHFMEMNTRL QVEHPISEMI TGTDLVEWQI RIAAGEPLPV TQEQVIRKGH AFEARIYAEN
PRGGFLPGAG PLRYLATPEP NDLVRVETGV REGDEVSVHY DPMIAKLVVW GENRAQALNS
LIARLSEYHI TGLQTNINFL IDLASHPEFQ AANVHTGFID QHFNTLFPPI EIKDDDLCKA
ALSLVFNELQ ASQTNSLQYN DPFAASPNLR LNYDLIRHYH LKANEKTYQI NVKYNSECIQ
IQIDNGQWHS VKADRIFDGE RLKIRSNIAN NISTYNAHID ESEVTIFLDN GKIAFELVQP
KFLETAVDQS GSAGSKVIAP MPGVLEKVLV KPGDSVKKGD NLAVLIAMKM EHILKAPKDA
VIKSIGGTEG SNVAKGAAVI TFEEEEEK
//
