ID A0A1F6E4N8_9BACT Unreviewed; 497 AA.
AC A0A1F6E4N8;
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=A3C95_00750 {ECO:0000313|EMBL:OGG68675.1};
OS Candidatus Kaiserbacteria bacterium RIFCSPHIGHO2_02_FULL_56_30.
OC Bacteria; Candidatus Kaiserbacteria.
OX NCBI_TaxID=1798499 {ECO:0000313|EMBL:OGG68675.1, ECO:0000313|Proteomes:UP000177107};
RN [1] {ECO:0000313|EMBL:OGG68675.1, ECO:0000313|Proteomes:UP000177107}
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:OGG68675.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MFLM01000005; OGG68675.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6E4N8; -.
DR STRING; 1798499.A3C95_00750; -.
DR Proteomes; UP000177107; 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 284..376
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
SQ SEQUENCE 497 AA; 53571 MW; E92B8327669D0AEC CRC64;
MTAQPIAAAA EMITVEADLT RGLHSFSIVG LPDKAVEEAR DRIAAAIRHS GFKSPKQENR
RIVLSLSPAD LKKEGSHYDL PLALAYLIAS GNLQPLTPHL LFAGELALDG TLRRVRGILP
QVLAAKRAGI KAVFVPSSTA HEALLAEGIA VYAPASLAEV VAHLKGEKRL PALTRDPREE
LPPPSIDLAD IKGQESAKRA LEIAAAGRHN IVFYGPPGTG KTMLARALSG ILPPLTPDEV
LEVTAIHSTA GLLGGGEAVY HPPFRAPHHS VSHVAIVGGG AFPKAGEVTL AHKGVLFLDE
FTEFDARALE ALRQPLEDRV VTVSRARASI TFPADCMIVA AMNPAETISD DVRTTLRAAA
RQSRRLSRPI VDRLDLWIEV PLVPHETLAR LATGEPSEVV RKRVIAARTH AEKRMKKRGT
TNAHLSGREL DEKSGFSPAV KEVLMHAAAR MNLSPRAYHR TMRVARTIAD LAGAHEVAPA
HVHEALQYRP RGMFGFE
//
