ID M9XC12_MEIRD Unreviewed; 436 AA.
AC M9XC12;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=ribonucleoside-diphosphate reductase {ECO:0000256|ARBA:ARBA00012274};
DE EC=1.17.4.1 {ECO:0000256|ARBA:ARBA00012274};
GN ORFNames=K649_04480 {ECO:0000313|EMBL:AGK04198.1};
OS Meiothermus ruber (strain ATCC 35948 / DSM 1279 / VKM B-1258 / 21) (Thermus
OS ruber).
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Meiothermus.
OX NCBI_TaxID=504728 {ECO:0000313|EMBL:AGK04198.1, ECO:0000313|Proteomes:UP000013026};
RN [1] {ECO:0000313|EMBL:AGK04198.1, ECO:0000313|Proteomes:UP000013026}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35948 / DSM 1279 / VKM B-1258 / 21
RC {ECO:0000313|Proteomes:UP000013026};
RA Chin J., Alexander D.H., Marks P., Korlach J., Clum A., Copeland A.;
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|ARBA:ARBA00001962};
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC {ECO:0000256|ARBA:ARBA00011209}.
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small
CC chain family. {ECO:0000256|ARBA:ARBA00009303}.
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DR EMBL; CP005385; AGK04198.1; -; Genomic_DNA.
DR AlphaFoldDB; M9XC12; -.
DR STRING; 504728.K649_04480; -.
DR KEGG; mre:K649_04480; -.
DR PATRIC; fig|504728.9.peg.926; -.
DR eggNOG; COG0208; Bacteria.
DR eggNOG; COG1328; Bacteria.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000013026; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005971; C:ribonucleoside-diphosphate reductase complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC.
DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IEA:InterPro.
DR CDD; cd01049; RNRR2; 1.
DR Gene3D; 1.10.620.20; Ribonucleotide Reductase, subunit A; 1.
DR InterPro; IPR005144; ATP-cone_dom.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR012348; RNR-like.
DR InterPro; IPR026494; RNR_NrdF-like.
DR InterPro; IPR033909; RNR_small.
DR InterPro; IPR000358; RNR_small_fam.
DR NCBIfam; TIGR04171; RNR_1b_NrdF; 1.
DR PANTHER; PTHR23409; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SMALL CHAIN; 1.
DR PANTHER; PTHR23409:SF18; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SUBUNIT M2; 1.
DR Pfam; PF03477; ATP-cone; 1.
DR Pfam; PF00268; Ribonuc_red_sm; 1.
DR SUPFAM; SSF47240; Ferritin-like; 1.
DR PROSITE; PS51161; ATP_CONE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00492}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00492}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 159..184
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 340..429
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 436 AA; 49242 MW; 475D1A4B1C9F62E0 CRC64;
MRFEGAKMSQ SLSVLSAVNW NRPDDGYTKM FWDQNVRQFW VDEEIPLADD KLTWMTLSRE
EQRVYEQVLA GLTLLDTVQG SVGMPLLSQH IESLQAKAVM GFMGAMEHMH AKSYSSIFST
LCTSERIAEL FDWVRSEPVL QEKQTFVHRR YLGVQDEQSL YLGLAASVLL ESFLFYSGFF
YPLLLAGQGR MTSSGEIINL IIRDESIHGV YVGLLAQEVY AGLPEAQQKT AREGVYSMLE
HLAGLEERYS RMLYTPLGLT EAVVTFSRYN ADKALMNLGL EPYFGVSAEA VNPVVLAGLS
THTKNHDFFS TKGNGYVKAI RVEPIQDEDF IFEGLAPEYQ PVVKRDGRVV PFDELRIVRA
VEKAGAATGV ALDPGVIERQ VLGPIKRKAR QQRLHIEEIQ NLVEEGLMKS YPAVARAYIL
YREERAKARR DQPYGC
//
