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
//