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Database: UniProt
Entry: I3ULG6_9CAUD
LinkDB: I3ULG6_9CAUD
Original site: I3ULG6_9CAUD 
ID   I3ULG6_9CAUD            Unreviewed;       773 AA.
AC   I3ULG6;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   13-SEP-2023, entry version 28.
DE   RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU003410};
DE            EC=1.17.4.1 {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU003410};
GN   ORFNames=SWPG_00082 {ECO:0000313|EMBL:AFK66331.1};
OS   Synechococcus phage S-CBM2.
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Kyanoviridae.
OX   NCBI_TaxID=351708 {ECO:0000313|EMBL:AFK66331.1, ECO:0000313|Proteomes:UP000501889};
RN   [1] {ECO:0000313|EMBL:AFK66331.1, ECO:0000313|Proteomes:UP000501889}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S-CBM2 {ECO:0000313|EMBL:AFK66331.1,
RC   ECO:0000313|Proteomes:UP000501889};
RG   The Broad Institute Genome Sequencing Platform;
RA   Henn M.R., Chen F., Wang K., Levin J., Malboeuf C., Casali M., Russ C.,
RA   Lennon N., Chapman S.B., Erlich R., Young S.K., Yandava C., Zeng Q.,
RA   Alvarado L., Anderson S., Berlin A., Chen Z., Freedman E., Gellesch M.,
RA   Goldberg J., Green L., Griggs A., Gujja S., Heilman E.R., Heiman D.,
RA   Hollinger A., Howarth C., Larson L., Mehta T., Pearson M., Roberts A.,
RA   Ryan E., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S.,
RA   White J., Haas B., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Synechococcus phage S-CBM2.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Provides the precursors necessary for DNA synthesis.
CC       Catalyzes the biosynthesis of deoxyribonucleotides from the
CC       corresponding ribonucleotides. {ECO:0000256|RuleBase:RU003410}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-
CC         diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-
CC         diphosphate; Xref=Rhea:RHEA:23252, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC         COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC         ChEBI:CHEBI:57930, ChEBI:CHEBI:73316; EC=1.17.4.1;
CC         Evidence={ECO:0000256|RuleBase:RU003410};
CC   -!- PATHWAY: Genetic information processing; DNA replication.
CC       {ECO:0000256|ARBA:ARBA00005160, ECO:0000256|RuleBase:RU003410}.
CC   -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC       chain family. {ECO:0000256|ARBA:ARBA00010406,
CC       ECO:0000256|RuleBase:RU003410}.
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DR   EMBL; HQ633061; AFK66331.1; -; Genomic_DNA.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000501889; Genome.
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:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.70.20; -; 1.
DR   InterPro; IPR005144; ATP-cone_dom.
DR   InterPro; IPR013346; NrdE_NrdA_C.
DR   InterPro; IPR000788; RNR_lg_C.
DR   InterPro; IPR013509; RNR_lsu_N.
DR   InterPro; IPR008926; RNR_R1-su_N.
DR   InterPro; IPR039718; Rrm1.
DR   NCBIfam; TIGR02506; NrdE_NrdA; 1.
DR   PANTHER; PTHR11573; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN; 1.
DR   PANTHER; PTHR11573:SF6; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE SUBUNIT; 1.
DR   Pfam; PF03477; ATP-cone; 1.
DR   Pfam; PF02867; Ribonuc_red_lgC; 1.
DR   Pfam; PF00317; Ribonuc_red_lgN; 1.
DR   PRINTS; PR01183; RIBORDTASEM1.
DR   SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR   SUPFAM; SSF48168; R1 subunit of ribonucleotide reductase, N-terminal domain; 1.
DR   PROSITE; PS51161; ATP_CONE; 1.
DR   PROSITE; PS00089; RIBORED_LARGE; 1.
PE   3: Inferred from homology;
KW   Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00492};
KW   Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
KW   ECO:0000256|RuleBase:RU003410};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00492};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003410};
KW   Reference proteome {ECO:0000313|Proteomes:UP000501889}.
FT   DOMAIN          9..99
FT                   /note="ATP-cone"
FT                   /evidence="ECO:0000259|PROSITE:PS51161"
SQ   SEQUENCE   773 AA;  87956 MW;  0CDE893826E92956 CRC64;
     MEKSMSNGTK VKKRDGRIEH LDLDKMHVMV EEACKDLSGV SASLVEMNSG IQFYDGITTD
     EIQQILVKSA ANLITLDTPN YQFVAARLLL YGLRKQVFGK RYEHPDFITH IKRCVDLGVY
     DPAILDKYDE QEISHFDSWI DHDRDFLFTY AGLRQVVDKY LVQDRSSGEI YETPQFMYMM
     IAATIFQQYP KETRLDYVKR YYDAISKHKI NIPTPIMGGV RTPLRQFASC VLVDVDDTLD
     SIFTSDMAIG RYVAQRAGIG INAGRIRGVN SKIRGGEVTH TGVIPFLKKF EATVRCCTQN
     GIRGGSATVH FPIWHKEIED IIVLKNNKGT EDNRVRKLDY SIQISKIFYE RFIKNESMHL
     FSPHDVPGLY TAFGTDDFDA LYTKYEADPT IPKKSVSAQE LILDLLKERA ETGRVYIMNI
     DHCNSHSSFK DQVYMSNLCQ EITLPTDPIG HIDDPDGEIA LCILSAINVG KLKNLDDLEE
     LCDLSVRGLE ELIDYQGYPV AAAERATKYR RSLGVGFIGL AHYLAKLGAS YGDNYSLTEV
     HKLTEAFQYY LLKSSNQIAR EKGPCEGFER TKYADGILPI DTYKKDVDEL VASAYFYDWE
     NLRTSILEHG LRHSTLSAQM PSESSSVVSN ATNGIEPPRD FLSIKKSKKG PLPQIVPQYT
     TLKKNYTLLW DMPSNEGYIK IVAVMQKFFD QAISGNWSYN PENYPDNEVP VSVIANDFLT
     TYKYGWKTSY YQNTYDNKKD ADVEDNIKRV VELDQLIESI LESEEDDCES CKI
//
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