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Database: UniProt
Entry: A0A1F6EJL1_9BACT
LinkDB: A0A1F6EJL1_9BACT
Original site: A0A1F6EJL1_9BACT 
ID   A0A1F6EJL1_9BACT        Unreviewed;       514 AA.
AC   A0A1F6EJL1;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=MCM domain-containing protein {ECO:0000259|PROSITE:PS50051};
GN   ORFNames=A3A40_00840 {ECO:0000313|EMBL:OGG73502.1};
OS   Candidatus Kaiserbacteria bacterium RIFCSPLOWO2_01_FULL_54_20.
OC   Bacteria; Candidatus Kaiserbacteria.
OX   NCBI_TaxID=1798513 {ECO:0000313|EMBL:OGG73502.1, ECO:0000313|Proteomes:UP000178427};
RN   [1] {ECO:0000313|EMBL:OGG73502.1, ECO:0000313|Proteomes:UP000178427}
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:OGG73502.1}.
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DR   EMBL; MFMA01000052; OGG73502.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F6EJL1; -.
DR   STRING; 1798513.A3A40_00840; -.
DR   Proteomes; UP000178427; 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          298..359
FT                   /note="MCM"
FT                   /evidence="ECO:0000259|PROSITE:PS50051"
SQ   SEQUENCE   514 AA;  55405 MW;  76FA2BCBE031DEC0 CRC64;
     MAEKQKIASG FARVYGAQPA LPAAHIVTVE CDIVKGLHAF TIVGLPDKSV EEAKDRLAAA
     IKNTRALESP KRSNKKIVLS LAPAALKKEG AVFDLPLALS FLLASEQTTF DPKGRLFAGE
     LALDGTIRPI LGSLSIASAA HDAGFTDLYV PEDNFEEASL ISNLTIHAVS SLEHVLAMLQ
     DPDYKATVRK PLRRRVLEDD SALDEIRGQA GAKRGLIIAA AGGHNIALYG PPGTGKTLLA
     RATAAILPDL SEKAMIEVTT IHSLTGTLAG GVMFRPPFRS PHHTSSYASL IGGGSAALRP
     GEVTLAHRGV LFADEFPEFH RDVINALREP LEDRVVSISR ARGTAIFPAN FMLIAALNPC
     PCGFAGSARC QCMPHTIEKY RRKIGGPVAD RIDMWVRVGE MPLETLSVRA KRVGGETKAA
     REHIAKARER QRARFEKAGI FTNADMKPKH IESLANLSDK AESTLVAAAN SMKLSPRGYH
     RTIKLARTVA DLAGGEMIEP PHMLEALQYR AREI
//
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