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Database: UniProt
Entry: A0A166DLT2_9EURY
LinkDB: A0A166DLT2_9EURY
Original site: A0A166DLT2_9EURY 
ID   A0A166DLT2_9EURY        Unreviewed;       719 AA.
AC   A0A166DLT2;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Magnesium-chelatase 38 kDa subunit {ECO:0000313|EMBL:KZX15733.1};
DE            EC=6.6.1.1 {ECO:0000313|EMBL:KZX15733.1};
GN   Name=bchI {ECO:0000313|EMBL:KZX15733.1};
GN   ORFNames=MBFIL_05970 {ECO:0000313|EMBL:KZX15733.1};
OS   Methanobrevibacter filiformis.
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX   NCBI_TaxID=55758 {ECO:0000313|EMBL:KZX15733.1, ECO:0000313|Proteomes:UP000077066};
RN   [1] {ECO:0000313|EMBL:KZX15733.1, ECO:0000313|Proteomes:UP000077066}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11501 {ECO:0000313|EMBL:KZX15733.1,
RC   ECO:0000313|Proteomes:UP000077066};
RA   Poehlein A., Seedorf H., Daniel R.;
RT   "Genome sequence of Methanobrevibacter filiformis DSM 11501.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the Mg-chelatase subunits D/I family.
CC       {ECO:0000256|ARBA:ARBA00005799}.
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:KZX15733.1}.
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DR   EMBL; LWMT01000087; KZX15733.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A166DLT2; -.
DR   STRING; 55758.MBFIL_05970; -.
DR   PATRIC; fig|55758.3.peg.672; -.
DR   OrthoDB; 78368at2157; -.
DR   Proteomes; UP000077066; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0016851; F:magnesium chelatase activity; IEA:UniProtKB-EC.
DR   CDD; cd00009; AAA; 1.
DR   Gene3D; 1.10.8.80; Magnesium chelatase subunit I, C-Terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041628; ChlI/MoxR_AAA_lid.
DR   InterPro; IPR000523; Mg_chelatse_chII-like_cat_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   PANTHER; PTHR43473; MAGNESIUM-CHELATASE SUBUNIT CHLD, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR43473:SF2; MAGNESIUM-CHELATASE SUBUNIT CHLD, CHLOROPLASTIC; 1.
DR   Pfam; PF17863; AAA_lid_2; 1.
DR   Pfam; PF01078; Mg_chelatase; 1.
DR   Pfam; PF13519; VWA_2; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00327; VWA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF53300; vWA-like; 1.
DR   PROSITE; PS50234; VWFA; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KZX15733.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077066}.
FT   DOMAIN          534..715
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
FT   REGION          334..434
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        338..386
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        389..403
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        404..434
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   719 AA;  80442 MW;  A3B4C3F9B27B5A76 CRC64;
     MKKAIFPFTA IVCQEDIKKA LILNVINPSI GGVLIQGSRG TGKTTAVRSI ANLLPEIEMV
     ENSPFNCEYK DNCTICSLCQ NQVNIIKTPI KIVELPLGAT EDRVVGSLNI ENALNKGVKS
     LEPGILASAN RNILYIDEIN LLDDNLVDIL LDSAAMGTNI VEREGISVSH PSRFILVGTM
     NPEEGELRKQ LSDRIGLKIS SEDIIDIHDR ILIVKRKEEF EKNPSIFINK YKTKEIAIKN
     KIANAKNLIH EITISDYLIE IIGGISLNLG VEGHRSDITI LKTAKTIAAF NNHKDVNEND
     LEEAIKLVLG NVNQNCNTPE NIKNQINKAK QELGQENKDT GENSNSNNMD IDNSNNKDNN
     NGDNSNNGDI DNNEYTNSGT ENNENYDENE FNNELKDENS NNDSSQENND LSNNLNRENN
     SNTNNSNNSN TNVDFAENKY ERKLNSFLKR NDEVDINKLM KIKGREKKKA YGNRVNSITE
     KGKYVKSKNS KGNPTDIAID ATIRSAILHS KNGNIKVKKE DLKEKIRKHK SNGLIALVID
     LSGSMVSEEK VNKIKSIINL IIKNVNKHKD KLVVIGFKGK DSEIIIPNTK RPLSFSHKLD
     EITVGGTTPT ASGLYKGLEI LKREMVNKEY VPILMLLSDG MPNVGLKNHP VRDVLDIGHE
     IKKNNIYTII IDFDKKHKHG RNINMELAIT TNGRYYDLEG ISNQEIAINK ILDYERENI
//
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