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Database: UniProt
Entry: A0A1F6Y974_9BACT
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Original site: A0A1F6Y974_9BACT 
ID   A0A1F6Y974_9BACT        Unreviewed;       486 AA.
AC   A0A1F6Y974;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Magnesium chelatase {ECO:0000313|EMBL:OGJ02964.1};
DE   Flags: Fragment;
GN   ORFNames=A3G06_01390 {ECO:0000313|EMBL:OGJ02964.1};
OS   Candidatus Nomurabacteria bacterium RIFCSPLOWO2_12_FULL_46_14.
OC   Bacteria; Candidatus Nomurabacteria.
OX   NCBI_TaxID=1801797 {ECO:0000313|EMBL:OGJ02964.1, ECO:0000313|Proteomes:UP000176192};
RN   [1] {ECO:0000313|EMBL:OGJ02964.1, ECO:0000313|Proteomes:UP000176192}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
CC   -!- SIMILARITY: Belongs to the Mg-chelatase subunits D/I family. ComM
CC       subfamily. {ECO:0000256|ARBA:ARBA00006354}.
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:OGJ02964.1}.
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DR   EMBL; MFVV01000030; OGJ02964.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F6Y974; -.
DR   STRING; 1801797.A3G06_01390; -.
DR   Proteomes; UP000176192; 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:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0032508; P:DNA duplex unwinding; IEA:InterPro.
DR   CDD; cd00009; AAA; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR045006; CHLI-like.
DR   InterPro; IPR001208; MCM_dom.
DR   InterPro; IPR004482; Mg_chelat-rel.
DR   InterPro; IPR025158; Mg_chelat-rel_C.
DR   InterPro; IPR000523; Mg_chelatse_chII-like_cat_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   NCBIfam; TIGR00368; YifB family Mg chelatase-like AAA ATPase; 1.
DR   PANTHER; PTHR32039:SF7; COMPETENCE PROTEIN COMM; 1.
DR   PANTHER; PTHR32039; MAGNESIUM-CHELATASE SUBUNIT CHLI; 1.
DR   Pfam; PF13541; ChlI; 1.
DR   Pfam; PF01078; Mg_chelatase; 1.
DR   Pfam; PF13335; Mg_chelatase_C; 1.
DR   PRINTS; PR01657; MCMFAMILY.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   PROSITE; PS50051; MCM_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          300..361
FT                   /note="MCM"
FT                   /evidence="ECO:0000259|PROSITE:PS50051"
FT   REGION          172..191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         486
FT                   /evidence="ECO:0000313|EMBL:OGJ02964.1"
SQ   SEQUENCE   486 AA;  53057 MW;  B4170B09B90CE6D5 CRC64;
     MSFARVYSAQ VNLLSGAIVT IEVDLSKGLH TFSVVGLPDK AVDESKDRVS SAIKNSGFKS
     PKAKNQKVVV SLSPADLKKE GPFFDLAIAL AYLLAADHLE FNPEKKIFLG ELGLDGTLRR
     VRGALPLAEE AKRRGFAEIY LPRENAAEAA LVDGIKIFGA RNLEEVMEHL DENLSKDSSP
     RGALKKIKPQ PKTEVSYKKA KPISDFSDIR GQESAKRGLE IAAAGGHNIA MYGPPGTGKT
     MLARAFAGLL PDLTLPEILE ITGIHSVAGT IEGELQVEPP FRSPHHTSSY VSIVGGGANL
     KPGEVTLAHR GVLFLDEFPE FEKRVLEALR QPLEDNLISI SRARGSATFP SNFILVAAMN
     PCPCGNTGSK KKACVCRPSD LDRYRRKLSG PIMDRIDLWV SVGNVEYKKL GGEGDGEKSA
     VIKKRVAVAQ KIQRERYKKL RRDIKLNSEM NVKDLSGIVK LKDEVRAMLD DSAERLGLSA
     RAYHRV
//
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