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Database: UniProt
Entry: R5VI45_9CLOT
LinkDB: R5VI45_9CLOT
Original site: R5VI45_9CLOT 
ID   R5VI45_9CLOT            Unreviewed;       529 AA.
AC   R5VI45;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Anaerobic ribonucleoside-triphosphate reductase {ECO:0000313|EMBL:CCZ90358.1};
GN   ORFNames=BN512_01118 {ECO:0000313|EMBL:CCZ90358.1};
OS   Clostridium sp. CAG:167.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1262777 {ECO:0000313|EMBL:CCZ90358.1, ECO:0000313|Proteomes:UP000018023};
RN   [1] {ECO:0000313|EMBL:CCZ90358.1, ECO:0000313|Proteomes:UP000018023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:167 {ECO:0000313|Proteomes:UP000018023};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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:CCZ90358.1}.
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DR   EMBL; CBAV010000060; CCZ90358.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5VI45; -.
DR   STRING; 1262777.BN512_01118; -.
DR   Proteomes; UP000018023; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008998; F:ribonucleoside-triphosphate reductase activity; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR   Gene3D; 3.20.70.20; -; 1.
DR   InterPro; IPR005144; ATP-cone_dom.
DR   InterPro; IPR012833; NrdD.
DR   PANTHER; PTHR21075; ANAEROBIC RIBONUCLEOSIDE-TRIPHOSPHATE REDUCTASE; 1.
DR   PANTHER; PTHR21075:SF0; ANAEROBIC RIBONUCLEOSIDE-TRIPHOSPHATE REDUCTASE; 1.
DR   Pfam; PF03477; ATP-cone; 1.
DR   Pfam; PF13597; NRDD; 1.
DR   SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR   PROSITE; PS51161; ATP_CONE; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00492};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00492}; Reference proteome {ECO:0000313|Proteomes:UP000018023}.
FT   DOMAIN          1..91
FT                   /note="ATP-cone"
FT                   /evidence="ECO:0000259|PROSITE:PS51161"
SQ   SEQUENCE   529 AA;  60443 MW;  B60357D5CC4E145E CRC64;
     MKVIKRDGRT VPYDRNKIIV AIRKANAEVD AYERVEDDMI DGIVAGIEGT GRETIQVEDI
     QDIIEQKLMA AGKFALAKKY IIYRYSRELV RKANTTDDSI MSLIQNRNKD VMEENSNKNA
     YVASTQRDLI AGEVSKDLTK RMLLPEKITK AHEEGILHFH DMDYFIQPIF NCCLINIGDM
     LDNGTVMNGK LIESPKSFQV ACTVVTQIIS AVASSQYGGQ SVDIRHLGKY LRRSMEKYRR
     HYTERYGEIL EPEVIERFVM DRTKDELKSG VQTIQYQINT LMTTNGQSPF VTLFLNLDPE
     DEYIEENAMI IEEILRQRLE GIKNEKGVYV TPAFPKLIYV LDEHNALKGG KYDYITKLAV
     QCSAKRMYPD YISAKKMREN YEGNVFSCMG CRSFLTPWKD ENGNYKFEGR FNQGVVSLNL
     PQIGILAKED KEYFWQLLEE RLALCFEALM CRHRALEGVS SDVSPIHWQY GAIARLGKGE
     KIDKLLHGGY STLSLGYIGL YEVTKLMTGE SHTTEKGSEK GAVIFQRLS
//
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