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Database: UniProt
Entry: A0A1G1JSH1_9BACT
LinkDB: A0A1G1JSH1_9BACT
Original site: A0A1G1JSH1_9BACT 
ID   A0A1G1JSH1_9BACT        Unreviewed;       508 AA.
AC   A0A1G1JSH1;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=MCM domain-containing protein {ECO:0000259|PROSITE:PS50051};
DE   Flags: Fragment;
GN   ORFNames=A3C47_05520 {ECO:0000313|EMBL:OGW83627.1};
OS   Omnitrophica bacterium RIFCSPHIGHO2_02_FULL_51_18.
OC   Bacteria; Candidatus Omnitrophota.
OX   NCBI_TaxID=1801823 {ECO:0000313|EMBL:OGW83627.1, ECO:0000313|Proteomes:UP000179119};
RN   [1] {ECO:0000313|EMBL:OGW83627.1, ECO:0000313|Proteomes:UP000179119}
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:OGW83627.1}.
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DR   EMBL; MHFI01000014; OGW83627.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G1JSH1; -.
DR   STRING; 1801823.A3C47_05520; -.
DR   Proteomes; UP000179119; 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          296..354
FT                   /note="MCM"
FT                   /evidence="ECO:0000259|PROSITE:PS50051"
FT   REGION          406..432
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         508
FT                   /evidence="ECO:0000313|EMBL:OGW83627.1"
SQ   SEQUENCE   508 AA;  55491 MW;  5D813A1E399D64CD CRC64;
     MLSTVLSSAV VGIDAYIVEV EVDISNGLPA FNIVGLPDAA CRESADRVRA AIKNSELPFP
     SRKITVNLAP AGLKKEGSGF DLAIAVGILV ANEVLDKTLV ENKIFCGELS LDGKIRPIPG
     ILPRAVSLLS EEKKKDFVIP YANAREGACV RDLNICPAKN LFEVVRFLKG ETALPCPKAV
     DSVKTKSEIK HHPSGDFSDV KGQPHAKRGL EIAAAGGHNV LMIGPPGSGK TMLAKRIPTI
     LSPITFEEAI ETTKIHSVAG LLSGKSTLLE TRPFRDPHHT ISDAALVGGG TYPKPGEISL
     AHNGVLFLDE LAEFRRNVLE VLRQPLEEGR ITITRASSSL TLPARFMLVA AMNPCPCGYF
     TDPKKECNCT SVQIKNYMSK ISGPLLDRID IQLEVPRLKV TEITDKSKAE SSKQIRERVE
     KARQRQRNRY AEDKIASNSE LEPSQMQKHC LVTEEGERLL KMAIQELGFS ARAYHKVLKV
     ARTIADLDGS ELIEPHHVSE AIHYRALD
//
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