ID A0A0G0XSD0_9BACT Unreviewed; 512 AA.
AC A0A0G0XSD0;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Mg chelatase, subunit ChlI {ECO:0000313|EMBL:KKS27317.1};
GN ORFNames=UU88_C0008G0016 {ECO:0000313|EMBL:KKS27317.1};
OS Parcubacteria group bacterium GW2011_GWC1_42_11.
OC Bacteria.
OX NCBI_TaxID=1618905 {ECO:0000313|EMBL:KKS27317.1, ECO:0000313|Proteomes:UP000034518};
RN [1] {ECO:0000313|EMBL:KKS27317.1, ECO:0000313|Proteomes:UP000034518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKS27317.1}.
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DR EMBL; LCCI01000008; KKS27317.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0XSD0; -.
DR PATRIC; fig|1618905.3.peg.478; -.
DR Proteomes; UP000034518; 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 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; PR00830; ENDOLAPTASE.
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 297..355
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
SQ SEQUENCE 512 AA; 56379 MW; DCE3B4C914FBDD7D CRC64;
MQFSKLFSAQ IVGLVAHIID VEVDLSKGLN AFSLVGLPSA SVDESRDRVS AAVKNSGFTS
PKQKNQKVVI ALAPAELKKE GSHYDLAIAL AYLMASGETR FDPKGKLFLG ELSLDGVVRP
IHGALLIANA AKKAGFSEIF LPEKNMREAA LVSDIKVYGV RNLSEILQHL DKNQKYKLAP
HINTDTNNAE IILDKTIVDL SHIKGQEFAK RALEIAAAGN HNLAMWGPPG TGKTMLAQAF
QHILPDLHNE HSLEVTGIHS VAGTLRENIM TRPPLRAPHH TASYPAVIGG GAIPKPGEIT
LAHRGVLFLD EFPEFDRRVI ESLREPLEEG HIRITRAKGH DTFPARFILL AAMNPCPCGK
YGSEDRCICM PGTLASYTRK VSGPIMDRIE LWVKVSHMSH DKLAEASTGE TTKDVCARIT
RARGMQEARF ANHARKITTN SEMRADDIEV FIKLTPKLRT LFNTSAERLK LSPRAHHKTI
KVARTIADLD SSDDIQEKHI LEALAYRPTE LK
//
