ID Q4C9K9_CROWT Unreviewed; 1116 AA.
AC Q4C9K9;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 96.
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=CwatDRAFT_6464 {ECO:0000313|EMBL:EAM53277.1};
OS Crocosphaera watsonii WH 8501.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Aphanothecaceae; Crocosphaera.
OX NCBI_TaxID=165597 {ECO:0000313|EMBL:EAM53277.1, ECO:0000313|Proteomes:UP000003922};
RN [1] {ECO:0000313|EMBL:EAM53277.1, ECO:0000313|Proteomes:UP000003922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH 8501 {ECO:0000313|EMBL:EAM53277.1,
RC ECO:0000313|Proteomes:UP000003922};
RG DOE Joint Genome Institute;
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EAM53277.1, ECO:0000313|Proteomes:UP000003922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH 8501 {ECO:0000313|EMBL:EAM53277.1,
RC ECO:0000313|Proteomes:UP000003922};
RG US DOE Joint Genome Institute (JGI-ORNL);
RA Larimer F., Land M.;
RT "Annotation of the draft genome assembly of Crocosphaera watsonii WH
RT 8501.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:EAM53277.1, ECO:0000313|Proteomes:UP000003922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH 8501 {ECO:0000313|EMBL:EAM53277.1,
RC ECO:0000313|Proteomes:UP000003922};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Richardson P.;
RT "Sequencing of the draft genome and assembly of Crocosphaera watsonii WH
RT 8501.";
RL Submitted (JUN-2005) 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|ARBA:ARBA00000206,
CC 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}.
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:EAM53277.1}.
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DR EMBL; AADV02000001; EAM53277.1; -; Genomic_DNA.
DR AlphaFoldDB; Q4C9K9; -.
DR KEGG; cwa:CwatDRAFT_6464; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000003922; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro.
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:InterPro.
DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR CDD; cd00081; Hint; 1.
DR Gene3D; 3.20.70.20; -; 2.
DR Gene3D; 3.10.28.10; Homing endonucleases; 1.
DR InterPro; IPR005144; ATP-cone_dom.
DR InterPro; IPR003587; Hint_dom_N.
DR InterPro; IPR036844; Hint_dom_sf.
DR InterPro; IPR027434; Homing_endonucl.
DR InterPro; IPR006142; INTEIN.
DR InterPro; IPR004042; Intein_endonuc.
DR InterPro; IPR006141; Intein_N.
DR InterPro; IPR004860; LAGLIDADG_2.
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; TIGR01445; intein_Nterm; 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; PF14528; LAGLIDADG_3; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 1.
DR Pfam; PF00317; Ribonuc_red_lgN; 1.
DR PRINTS; PR00379; INTEIN.
DR SMART; SM00306; HintN; 1.
DR SUPFAM; SSF51294; Hedgehog/intein (Hint) domain; 1.
DR SUPFAM; SSF55608; Homing endonucleases; 1.
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; PS50819; INTEIN_ENDONUCLEASE; 1.
DR PROSITE; PS50817; INTEIN_N_TER; 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}; Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813};
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 Protein splicing {ECO:0000256|ARBA:ARBA00023000};
KW Reference proteome {ECO:0000313|Proteomes:UP000003922}.
FT DOMAIN 33..122
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT DOMAIN 665..708
FT /note="DOD-type homing endonuclease"
FT /evidence="ECO:0000259|PROSITE:PS50819"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1116 AA; 126386 MW; 2C3D14E5D1C55EBE CRC64;
MMQPTVLTSP KQTSHGDTQT SSLYHSQLGE SKIRVRRRDG SWTALNIVKI RAVVDWACAD
REVNSIALEA GLTTRLRDGI TTREIQDNLI NCALEMCSPD EPDWRYIAGR LHIWSLWKDT
LVSRGYQYGN YEIVAKTKID AKQYDNRLLT YSTAELQEAG SWINPDWDTD YDYAGAVLLT
SRYLLDDELP QEAFLTCALL LATVESPENR LPWAKRFYEA IAKGKVSLAT PILANLRVPG
GSLTSCFILS IDDNLESIFE EITNTARISK NGGGVGVNVS RIRATGSWVM GKNNASGGVI
PWIKLLNDTA IAVNQGGRRA GAVTVGLDIW HLDVPEFLEI QTENGDQRRK AYDVFPQLIL
TDEFMRRVEN KEEWTLVDPY QVKEKLGIEL AELWGEKFEE AYGLIEAELD REITLYKRVN
ARELFKTIMR SQVETGMPYL AFKDTINKAN PNKHVGYIPG VNLCVAPETK ILTDRGQIAI
ADVAGEKVNI WNGSEWSEVL VKKTGENQPL LKVHFSNGES LDCTYYHKFH VQENYKGKVK
IVEAKDLQEG DKLIKYRLPL VESENDIDFP YAYTSGFFSG DGSHDGMGKP EIDLYGEKKE
LLPFVTVRNK YYGGSYGDKS WRIERDEVAV YDDVNQDRIV CKLPLDIPAK FTVPVNGYTI
QSRLEWLAGL LDADGTVARN GDNESLQVAS THQQFLLDIR LMLQTLGVDS KVVKMDEMGY
RSLPDGKGGY QDYFCQAKYR LLISSNGLFQ LGELGLKTNR LQWNLREPQR EASQFIRVEK
VELTCRYDDT YCFSEPKRHL GMFNGILTGQ CTESFSNVTP GKFAHCCNLV SLNLANIEEE
ELDYLCNISV RILDNTIDIT NPPFNDAKAH NDRYRTVGVG CMGLADWLAK KGLTYENITE
ISNLFEEVGY WCTHTSMELA KERSPYNAFE GSDWSKGLLI GSKPVDWFVE NASKKERWVQ
LSEDIKTYGI RNSHITAIAP NTSSSLVQGC TASILPVYSR FFYDKWAKGT IPIAPPFIKE
SFWFYHENKT LEQQKVVKAV ATIQQWIDTG ISMELLFNLN QGVYFADEPE RCLTAKDIFE
TLLLAWKEGC KAIYYVRTVQ KDDFKESDNN CTACAN
//
