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Database: UniProt
Entry: A0A133U373_9EURY
LinkDB: A0A133U373_9EURY
Original site: A0A133U373_9EURY 
ID   A0A133U373_9EURY        Unreviewed;       323 AA.
AC   A0A133U373;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=BPL/LPL catalytic domain-containing protein {ECO:0000259|PROSITE:PS51733};
GN   ORFNames=AKJ61_04515 {ECO:0000313|EMBL:KXA88633.1};
OS   candidate division MSBL1 archaeon SCGC-AAA259B11.
OC   Archaea; Euryarchaeota; candidate division MSBL1.
OX   NCBI_TaxID=1698260 {ECO:0000313|EMBL:KXA88633.1, ECO:0000313|Proteomes:UP000070184};
RN   [1] {ECO:0000313|EMBL:KXA88633.1, ECO:0000313|Proteomes:UP000070184}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCGC-AAA259B11 {ECO:0000313|EMBL:KXA88633.1};
RX   PubMed=26758088; DOI=10.1038/srep19181;
RA   Mwirichia R., Alam I., Rashid M., Vinu M., Ba-Alawi W., Anthony Kamau A.,
RA   Kamanda Ngugi D., Goker M., Klenk H.P., Bajic V., Stingl U.;
RT   "Metabolic traits of an uncultured archaeal lineage -MSBL1- from brine
RT   pools of the Red Sea.";
RL   Sci. Rep. 6:19181-19181(2016).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KXA88633.1}.
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DR   EMBL; LHXK01000096; KXA88633.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A133U373; -.
DR   Proteomes; UP000070184; 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   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd16442; BPL; 1.
DR   CDD; cd00090; HTH_ARSR; 1.
DR   Gene3D; 2.30.30.100; -; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   HAMAP; MF_00978; Bifunct_BirA; 1.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR011991; ArsR-like_HTH.
DR   InterPro; IPR030855; Bifunct_BirA.
DR   InterPro; IPR004408; Biotin_CoA_COase_ligase.
DR   InterPro; IPR003142; BPL_C.
DR   InterPro; IPR004143; BPL_LPL_catalytic.
DR   InterPro; IPR013196; HTH_11.
DR   InterPro; IPR008988; Transcriptional_repressor_C.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
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   Pfam; PF08279; HTH_11; 1.
DR   SUPFAM; SSF50037; C-terminal domain of transcriptional repressors; 1.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE   3: Inferred from homology;
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070184}.
FT   DOMAIN          67..254
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51733"
SQ   SEQUENCE   323 AA;  36155 MW;  9F287C0815C0171E CRC64;
     MDRPNTRWEI LRNLKKSETF LSGEELAKPL GVSRISVWKH IQNLKKMGYE IESKRGEGYK
     LLEPPDKLLP PEILPLDTEI VGREIIHYEE VKSTNLKMRE KSEEEEGLII LAERQTEGKG
     RLGRNWKSPK GGIWMSVLLK PNIPPVETPL LTMISSTSVF ESLQEIGIEG SIKWPNDVLV
     DGEKICGILT EMDAEMGALN YVIIGIGLNV NFDKNELPDT GATTVQSILE EKVDRKALTG
     SIITNLDKWY RKLKKNSKEE ILDSWRANSH NLGRKVDVEM VTGESFTGTA VDFTDTGGLV
     VKGENGSERT FLSGDVTLSS DSR
//
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