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Database: UniProt
Entry: A1YTS7_9CAUD
LinkDB: A1YTS7_9CAUD
Original site: A1YTS7_9CAUD 
ID   A1YTS7_9CAUD            Unreviewed;       349 AA.
AC   A1YTS7;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   RecName: Full=ribonucleoside-diphosphate reductase {ECO:0000256|ARBA:ARBA00012274};
DE            EC=1.17.4.1 {ECO:0000256|ARBA:ARBA00012274};
GN   ORFNames=812_138 {ECO:0000313|EMBL:QVD57867.1}, 812_141
GN   {ECO:0000313|EMBL:AHY25669.1}, 812a_141 {ECO:0000313|EMBL:AHY25889.1},
GN   812F1_141 {ECO:0000313|EMBL:AHY26322.1}, K1/420_141
GN   {ECO:0000313|EMBL:AHY26538.1}, K1_141 {ECO:0000313|EMBL:AHY26106.1};
OS   Staphylococcus phage 812.
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Herelleviridae; Twortvirinae; Kayvirus.
OX   NCBI_TaxID=307898 {ECO:0000313|EMBL:ABL87153.1};
RN   [1] {ECO:0000313|EMBL:AHY25669.1, ECO:0000313|Proteomes:UP000203789}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=9657943; DOI=10.1006/viro.1998.9203;
RA   Pantucek R., Rosypalova A., Doskar J., Kailerova J., Ruzickova V.,
RA   Borecka P., Snopkova S., Horvath R., Gotz F., Rosypal S.;
RT   "The polyvalent staphylococcal phage phi 812: its host-range mutants and
RT   related phages.";
RL   Virology 246:241-252(1998).
RN   [2] {ECO:0000313|EMBL:ABL87153.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Phi812 {ECO:0000313|EMBL:ABL87153.1};
RX   PubMed=18062181; DOI=10.1007/BF02932087;
RA   Kasparek P., Pantucek R., Kahankova J., Ruzickova V., Doskar J.;
RT   "Genome rearrangements in host-range mutants of the polyvalent
RT   staphylococcal bacteriophage 812.";
RL   Folia Microbiol. (Praha) 52:331-338(2007).
RN   [3] {ECO:0000313|EMBL:AHY26538.1, ECO:0000313|Proteomes:UP000241717}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Host-range mutant K1/420 {ECO:0000313|EMBL:AHY26538.1};
RX   PubMed=27469164; DOI=10.1073/pnas.1605883113;
RA   Novacek J., Siborova M., Benesik M., Pantucek R., Doskar J., Plevka P.;
RT   "Structure and genome release of Twort-like Myoviridae phage with a double-
RT   layered baseplate.";
RL   Proc. Natl. Acad. Sci. U.S.A. 113:9351-9356(2016).
RN   [4] {ECO:0000313|Proteomes:UP000240332, ECO:0000313|Proteomes:UP000240672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Host-range mutant 812a {ECO:0000313|EMBL:AHY25889.1},
RC   Host-range mutant 812F1 {ECO:0000313|EMBL:AHY26322.1}, Host-range
RC   mutant K1 {ECO:0000313|EMBL:AHY26106.1}, and Host-range mutant K1/420
RC   {ECO:0000313|EMBL:AHY26538.1};
RX   PubMed=28852930; DOI=10.1007/s11262-017-1507-2;
RA   Benesik M., Novacek J., Janda L., Dopitova R., Pernisova M., Melkova K.,
RA   Tisakova L., Doskar J., Zidek L., Hejatko J., Pantucek R.;
RT   "Role of SH3b binding domain in a natural deletion mutant of Kayvirus
RT   endolysin LysF1 with a broad range of lytic activity.";
RL   Virus Genes 54:130-139(2018).
RN   [5] {ECO:0000313|EMBL:AZB49847.1, ECO:0000313|Proteomes:UP000267657}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Botka T., Pantucek R., Benesik M., Maslanova I., Petras P., Ruzickova V.,
RA   Havlickova P., Varga M., Zemlickova H., Kolackova I., Florianova M.,
RA   Jakubu V., Karpiskova R., Doskar J.;
RT   "Lytic and genomic properties of spontaneous host-range Kayvirus mutants
RT   prove their suitability for phage therapy of staphylococcal infections.";
RL   Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
RN   [6] {ECO:0000313|EMBL:AHY25889.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Host-range mutant 812a {ECO:0000313|EMBL:AHY25889.1};
RX   PubMed=36779718;
RA   Kuntova L., Maslanova I., Oborilova R., Simeckova H., Finstrlova A.,
RA   Bardy P., Siborova M., Troianovska L., Botka T., Gintar P., Sedo O.,
RA   Farka Z., Doskar J., Pantucek R.;
RT   "Staphylococcus aureus Prophage-Encoded Protein Causes Abortive Infection
RT   and Provides Population Immunity against Kayviruses.";
RL   MBio 0:0-0(2023).
RN   [7] {ECO:0000313|EMBL:QVD57867.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=33918287;
RA   Saez Moreno D., Visram Z., Mutti M., Restrepo-Cordoba M., Hartmann S.,
RA   Kremers A.I., Tisakova L., Schertler S., Wittmann J., Kalali B.,
RA   Monecke S., Ehricht R., Resch G., Corsini L.;
RT   "epsilon(2)-Phages Are Naturally Bred and Have a Vastly Improved Host Range
RT   in Staphylococcus aureus over Wild Type Phages.";
RL   Pharmaceuticals (Basel) 1:0-0(0).
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000256|ARBA:ARBA00001962};
CC   -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small
CC       chain family. {ECO:0000256|ARBA:ARBA00009303}.
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DR   EMBL; EF136589; ABL87153.1; -; Genomic_DNA.
DR   EMBL; KJ206559; AHY25669.1; -; Genomic_DNA.
DR   EMBL; KJ206560; AHY25889.1; -; Genomic_DNA.
DR   EMBL; KJ206561; AHY26106.1; -; Genomic_DNA.
DR   EMBL; KJ206562; AHY26322.1; -; Genomic_DNA.
DR   EMBL; KJ206563; AHY26538.1; -; Genomic_DNA.
DR   EMBL; MH844528; AZB49847.1; -; Genomic_DNA.
DR   EMBL; MW546072; QVD57867.1; -; Genomic_DNA.
DR   RefSeq; YP_009224551.1; NC_029080.1.
DR   GeneID; 26795703; -.
DR   KEGG; vg:26795703; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000203789; Genome.
DR   Proteomes; UP000240332; Genome.
DR   Proteomes; UP000240672; Genome.
DR   Proteomes; UP000241717; Genome.
DR   Proteomes; UP000241865; Genome.
DR   Proteomes; UP000267657; Genome.
DR   Proteomes; UP000680916; Genome.
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: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; IPR009078; Ferritin-like_SF.
DR   InterPro; IPR012348; RNR-like.
DR   InterPro; IPR033909; RNR_small.
DR   InterPro; IPR000358; RNR_small_fam.
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   SUPFAM; SSF47240; Ferritin-like; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000240672}.
SQ   SEQUENCE   349 AA;  40446 MW;  23BD79557ECCE263 CRC64;
     MDITQKVKQH NKNAVLKATN WNIEDDGMSD IYWEQGISQF WTPEEFDVSR DLSSWNSLTE
     SEKNTYKKVL AGLTGLDTKQ GGEGMNLVSY HEPRPKYQAV FAFMGGMEEI HAKSYSHIFT
     TLLSNKETSY LLDTWVEEND FLKVKAQFIG YYYDQLLKPN PTIFDRYMAK VASAFLESAL
     FYSGFYYPLL LAGRGQMTQS GAIIYKITQD EAYHGSAVGL TAQYDYNLLT EEEKKQADKE
     TYELLDILYT NEVAYTHSLY DPLELSEDVI NYVQYNFNRA LQNLGREDYF NPEPYNPIVE
     NQTNVDRLRN VDFFSGKADY EKSTNIKDIK DEDFSFLDSK EYSTAKEFL
//
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