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Database: UniProt
Entry: A4J0R1_DESRM
LinkDB: A4J0R1_DESRM
Original site: A4J0R1_DESRM 
ID   A4J0R1_DESRM            Unreviewed;       505 AA.
AC   A4J0R1;
DT   01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   SubName: Full=MazG family protein {ECO:0000313|EMBL:ABO48664.1};
GN   OrderedLocusNames=Dred_0114 {ECO:0000313|EMBL:ABO48664.1};
OS   Desulforamulus reducens (strain ATCC BAA-1160 / DSM 100696 / MI-1)
OS   (Desulfotomaculum reducens).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC   Desulforamulus.
OX   NCBI_TaxID=349161 {ECO:0000313|EMBL:ABO48664.1, ECO:0000313|Proteomes:UP000001556};
RN   [1] {ECO:0000313|EMBL:ABO48664.1, ECO:0000313|Proteomes:UP000001556}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MI-1 {ECO:0000313|EMBL:ABO48664.1,
RC   ECO:0000313|Proteomes:UP000001556};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.;
RT   "Complete sequence of Desulfotomaculum reducens MI-1.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP000612; ABO48664.1; -; Genomic_DNA.
DR   RefSeq; WP_011876508.1; NC_009253.1.
DR   AlphaFoldDB; A4J0R1; -.
DR   STRING; 349161.Dred_0114; -.
DR   KEGG; drm:Dred_0114; -.
DR   eggNOG; COG3956; Bacteria.
DR   HOGENOM; CLU_038356_1_0_9; -.
DR   OrthoDB; 9808939at2; -.
DR   Proteomes; UP000001556; Chromosome.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:InterPro.
DR   GO; GO:0047429; F:nucleoside triphosphate diphosphatase activity; IEA:InterPro.
DR   CDD; cd11529; NTP-PPase_MazG_Cterm; 1.
DR   CDD; cd11528; NTP-PPase_MazG_Nterm; 1.
DR   CDD; cd11723; YabN_N_like; 1.
DR   Gene3D; 1.10.287.1080; MazG-like; 2.
DR   InterPro; IPR000878; 4pyrrol_Mease.
DR   InterPro; IPR035996; 4pyrrol_Methylase_sf.
DR   InterPro; IPR014777; 4pyrrole_Mease_sub1.
DR   InterPro; IPR004518; MazG-like_dom.
DR   InterPro; IPR048011; NTP-PPase_MazG-like_C.
DR   InterPro; IPR048015; NTP-PPase_MazG-like_N.
DR   InterPro; IPR011551; NTP_PyrPHydrolase_MazG.
DR   InterPro; IPR024180; Tetrapyrrole_Mease/MazG_pred.
DR   InterPro; IPR035013; YabN_N.
DR   NCBIfam; TIGR00444; mazG; 1.
DR   PANTHER; PTHR30522; NUCLEOSIDE TRIPHOSPHATE PYROPHOSPHOHYDROLASE; 1.
DR   PANTHER; PTHR30522:SF0; NUCLEOSIDE TRIPHOSPHATE PYROPHOSPHOHYDROLASE; 1.
DR   Pfam; PF03819; MazG; 2.
DR   Pfam; PF00590; TP_methylase; 1.
DR   PIRSF; PIRSF002845; Ttrprl_mtas_MazG; 1.
DR   SUPFAM; SSF101386; all-alpha NTP pyrophosphatases; 2.
DR   SUPFAM; SSF53790; Tetrapyrrole methylase; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001556}.
FT   DOMAIN          5..207
FT                   /note="Tetrapyrrole methylase"
FT                   /evidence="ECO:0000259|Pfam:PF00590"
FT   DOMAIN          269..342
FT                   /note="NTP pyrophosphohydrolase MazG-like"
FT                   /evidence="ECO:0000259|Pfam:PF03819"
FT   DOMAIN          411..467
FT                   /note="NTP pyrophosphohydrolase MazG-like"
FT                   /evidence="ECO:0000259|Pfam:PF03819"
SQ   SEQUENCE   505 AA;  57197 MW;  511D970AB5C45150 CRC64;
     MDKLITVVGL GPGDPGMLPL QVWELLNGGL PVYLRTEVHP TVDWLKQKGV KFSSMDHHYD
     HATTFEEVYS NIAQEILEVA EQTPVVYGVP GHPMVAEDSV RRVLELAAAR GIPTRVIPAM
     SFIDALSATL GIDPCKGLHI VDALRLDVQQ PDPLVGTIVT QIYDRMTAGE TKLSIMDHYP
     DEHMITVVRA AGVPKEERVQ RIPLYELDRL DWIDHLTSLY IEPLTKGSEH QKFNQPEIQN
     TEGSFPLDPL IEVMVTLREE NGCPWDREQT HKSLKPYLIE ETYEVLEALE QGQMYKICEE
     LGDLLLQIVF HAQIASENKQ FNMNDVVQSI TEKMIRRHPH VFGSTRVEDS QEVLVNWDKI
     KTQEQGAQAN EQPYLSGVPR ALPALLRAQK VQSKAARIGF DWPDYTGAVD KVKEELQEVL
     QEIGTGCTEA LSEEVGDLLF AVVNLARLLK IEAEDALSLT TNKFIQRFYY IEQKASDAGK
     KLTELTLEQM DLWWEEAKIL KKQEK
//
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