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Database: UniProt
Entry: A0A1C4ZM93_MICVI
LinkDB: A0A1C4ZM93_MICVI
Original site: A0A1C4ZM93_MICVI 
ID   A0A1C4ZM93_MICVI        Unreviewed;       223 AA.
AC   A0A1C4ZM93;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Anaerobic ribonucleoside-triphosphate reductase activating protein {ECO:0000313|EMBL:SCF34042.1};
GN   ORFNames=GA0074695_5806 {ECO:0000313|EMBL:SCF34042.1};
OS   Micromonospora viridifaciens.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=1881 {ECO:0000313|EMBL:SCF34042.1, ECO:0000313|Proteomes:UP000198242};
RN   [1] {ECO:0000313|EMBL:SCF34042.1, ECO:0000313|Proteomes:UP000198242}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43909 {ECO:0000313|EMBL:SCF34042.1,
RC   ECO:0000313|Proteomes:UP000198242};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR   EMBL; LT607411; SCF34042.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C4ZM93; -.
DR   Proteomes; UP000198242; Chromosome i.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0043365; F:[formate-C-acetyltransferase]-activating enzyme activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR012837; NrdG.
DR   InterPro; IPR034457; Organic_radical-activating.
DR   InterPro; IPR007197; rSAM.
DR   PANTHER; PTHR30352:SF2; ANAEROBIC RIBONUCLEOSIDE-TRIPHOSPHATE REDUCTASE-ACTIVATING PROTEIN; 1.
DR   PANTHER; PTHR30352; PYRUVATE FORMATE-LYASE-ACTIVATING ENZYME; 1.
DR   Pfam; PF13353; Fer4_12; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   SFLD; SFLDF00299; anaerobic_ribonucleoside-triph; 1.
DR   SFLD; SFLDS00029; Radical_SAM; 1.
DR   SUPFAM; SSF102114; Radical SAM enzymes; 1.
PE   4: Predicted;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT   DOMAIN          22..117
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|Pfam:PF04055"
SQ   SEQUENCE   223 AA;  24013 MW;  F9A0C0B509C04A43 CRC64;
     MARFLRATRA EGPGERTAVW VQGCQIRCPG CFNPHLWSFR GGERVTPAHL ARRVLDAGTD
     GLTLLGGEPF DQAAALAAVA AEVRDAGRSV MTFTGYTTGQ LARAVDSGRD DVAALLAATD
     LLVAGPFRAD RLDRNRPWVG STNQEFVLLN DRFPGLLDEV SRSPDRIEVT VDPAGRVEVN
     GWAEVDALDA LLASVGRQQH VARARRAPRA PQDYSVSHES VGS
//
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