ID A0AA96HGX5_9CAUD Unreviewed; 317 AA. AC A0AA96HGX5; DT 27-MAR-2024, integrated into UniProtKB/TrEMBL. DT 27-MAR-2024, sequence version 1. DT 24-JUL-2024, entry version 3. DE RecName: Full=ribonucleoside-diphosphate reductase {ECO:0000256|ARBA:ARBA00012274}; DE EC=1.17.4.1 {ECO:0000256|ARBA:ARBA00012274}; GN Name=110 {ECO:0000313|EMBL:WNN95675.1}; GN ORFNames=SEA_GLASKE16_110 {ECO:0000313|EMBL:WNN95675.1}; OS Mycobacterium phage Glaske16. OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes; OC Vilmaviridae; Mclasvirinae; Bongovirus. OX NCBI_TaxID=3035378 {ECO:0000313|EMBL:WNN95675.1}; RN [1] {ECO:0000313|EMBL:WNN95675.1} RP NUCLEOTIDE SEQUENCE. RA Baliraine F.N., McLoud J.D., Feroz T., Andrade C., Donnelly O.L., RA Harbison Z.J., Livingston E.G., Martinez C.A., Mathews K.E., Pledger T.M., RA Schlimme S.G., Williams D.C., Ko C., Russell D.A., Jacobs-Sera D., RA Hatfull G.F.; RL Submitted (SEP-2023) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; CC Evidence={ECO:0000256|PIRSR:PIRSR000355-2}; CC Note=Binds 2 iron ions per subunit. {ECO:0000256|PIRSR:PIRSR000355-2}; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; OR553909; WNN95675.1; -; Genomic_DNA. DR GO; GO:0005971; C:ribonucleoside-diphosphate reductase complex; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:TreeGrafter. 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; IPR009078; Ferritin-like_SF. DR InterPro; IPR012348; RNR-like. DR InterPro; IPR026494; RNR_NrdF-like. DR InterPro; IPR033909; RNR_small. DR InterPro; IPR030475; RNR_small_AS. 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; PF00268; Ribonuc_red_sm; 1. DR PIRSF; PIRSF000355; NrdB; 1. DR SUPFAM; SSF47240; Ferritin-like; 1. DR PROSITE; PS00368; RIBORED_SMALL; 1. PE 3: Inferred from homology; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000355-2}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR000355-2}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}. FT ACT_SITE 103 FT /evidence="ECO:0000256|PIRSR:PIRSR000355-1" FT BINDING 65 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2" FT BINDING 96 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2" FT BINDING 96 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2" FT BINDING 99 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2" FT BINDING 156 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2" FT BINDING 190 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2" FT BINDING 193 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2" SQ SEQUENCE 317 AA; 36313 MW; E4581A5FD8D645B9 CRC64; MALTRAINWN RVFDDKDLEV WNRLTNNFWL PEKIPVSNDI PAWGTLTEEE QVLTMRVFTG LTMLDTIQGT VGAVSLIPDA ITPHEEAVYT NIAFMESVHA KSYSNIFSTL CSSKEIDAAF RWSEENPNLQ RKAQIVLDYY QGDDPLKRKV ASTLLEGFLF YSGFYLPMYW SSRGKLTNTA DMIRLIIRDE AVHGYYIGYK FQRGLETQNE ARREELKDYT YGLLLELYDN EIEYTQDLYD GVGLTEDVKM FLRYNANKAL MNLGYEALFP RDETEVNAAI LAALSPGGDE NHDFFSGSGS TYVIGKAEVT EDEDWDF //