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Database: UniProt
Entry: A0A1Q7QJ32_9CHLR
LinkDB: A0A1Q7QJ32_9CHLR
Original site: A0A1Q7QJ32_9CHLR 
ID   A0A1Q7QJ32_9CHLR        Unreviewed;       502 AA.
AC   A0A1Q7QJ32;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=MCM domain-containing protein {ECO:0000259|PROSITE:PS50051};
GN   ORFNames=AUI58_06290 {ECO:0000313|EMBL:OLD51730.1};
OS   Chloroflexi bacterium 13_1_40CM_2_70_6.
OC   Bacteria; Chloroflexota.
OX   NCBI_TaxID=1805070 {ECO:0000313|EMBL:OLD51730.1, ECO:0000313|Proteomes:UP000185765};
RN   [1] {ECO:0000313|EMBL:OLD51730.1, ECO:0000313|Proteomes:UP000185765}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27843720;
RA   Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA   Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA   Banfield J.F.;
RT   "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT   heterotrophy are prevalent below the grass root zone.";
RL   PeerJ 4:E2687-E2687(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:OLD51730.1}.
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DR   EMBL; MNHK01000082; OLD51730.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q7QJ32; -.
DR   Proteomes; UP000185765; 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; 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          293..351
FT                   /note="MCM"
FT                   /evidence="ECO:0000259|PROSITE:PS50051"
SQ   SEQUENCE   502 AA;  53008 MW;  EB4895978B23DEC8 CRC64;
     METAARAVAR IPACALWGLE TALVTVEVDV ANGLPAFVVV GLPDAAVQEA RERVRAAIRN
     SGYEFPLRRV TVNLAPAERR KEGTGFDLAI ALGILRASGQ LAVDVEALCL GELALDGALR
     PVRGTMPRVR HALARGIAAA LLASANAGEA AACGADAYGF GSLREAVDHV AGSARLAPTV
     APAPAPPERP AVDLADIAGQ ETPKRALEIA AAGAHSLLLV GPPGTGKTML ARALPSLLPP
     LDHDEALAAS AVHSVAGLVD PRHPLLRSRP FRAPHHTASP LALVGGGSPP RPGEVSLAHC
     GVLFLDELAE FSPSVLDTLR EPLEERSITI SRAGGAATYP ARFLLVAAMN PCPCGHLGDP
     AVECRCLPDA VERYRGRLSG PLLDRIDLRV NVPRVPYERL RDEGRESSAT VRGRVLAARE
     RMTARLVGTA RRTNAELTVA DIRRWCRVDD DGETLLGAAI RERRLSARGY HRLLRVARTV
     ADLAGSDRVR ADDVAVALLM RA
//
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