ID E0VP30_PEDHC Unreviewed; 795 AA.
AC E0VP30;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|RuleBase:RU003410};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU003410};
GN Name=8231961 {ECO:0000313|EnsemblMetazoa:PHUM350970-PA};
GN ORFNames=Phum_PHUM350970 {ECO:0000313|EMBL:EEB15136.1};
OS Pediculus humanus subsp. corporis (Body louse).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Psocodea; Phthiraptera; Anoplura; Pediculidae;
OC Pediculus.
OX NCBI_TaxID=121224;
RN [1] {ECO:0000313|EMBL:EEB15136.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=USDA {ECO:0000313|EMBL:EEB15136.1};
RA Kirkness E., Hannick L., Hass B., Bruggner R., Lawson D., Bidwell S.,
RA Joardar V., Caler E., Walenz B., Inman J., Schobel S., Galinsky K.,
RA Amedeo P., Strausberg R.;
RT "Annotation of Pediculus humanus corporis strain USDA.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEB15136.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=USDA {ECO:0000313|EMBL:EEB15136.1};
RG The Human Body Louse Genome Consortium;
RA Kirkness E., Walenz B., Hass B., Bruggner R., Strausberg R.;
RT "The genome of the human body louse.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblMetazoa:PHUM350970-PA}
RP IDENTIFICATION.
RC STRAIN=USDA {ECO:0000313|EnsemblMetazoa:PHUM350970-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- FUNCTION: Provides the precursors necessary for DNA synthesis.
CC Catalyzes the biosynthesis of deoxyribonucleotides from the
CC corresponding ribonucleotides. {ECO:0000256|ARBA:ARBA00024942,
CC 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}.
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DR EMBL; AAZO01004081; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DS235354; EEB15136.1; -; Genomic_DNA.
DR RefSeq; XP_002427874.1; XM_002427829.1.
DR AlphaFoldDB; E0VP30; -.
DR STRING; 121224.E0VP30; -.
DR EnsemblMetazoa; PHUM350970-RA; PHUM350970-PA; PHUM350970.
DR GeneID; 8231961; -.
DR KEGG; phu:Phum_PHUM350970; -.
DR CTD; 8231961; -.
DR VEuPathDB; VectorBase:PHUM350970; -.
DR eggNOG; KOG1112; Eukaryota.
DR HOGENOM; CLU_000404_1_0_1; -.
DR InParanoid; E0VP30; -.
DR OMA; QMSSCYL; -.
DR OrthoDB; 5472715at2759; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000009046; Unassembled WGS sequence.
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:InterPro.
DR CDD; cd01679; RNR_I; 1.
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:UP000009046}.
FT DOMAIN 4..95
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 795 AA; 89935 MW; 85498CFF65DA5CDB CRC64;
MNKMFVIKRG GRNEEVHFDK ITSRIQKLCY GLNLDYVDPI AITVKVINGL YSGVTTAELD
SLAAEVSASM TTQHPDYAIL AARIAVSNLH KETKVSFSDV MTDLYNMKNS FNQQPTPMLS
DYHYDIIIKH ADELNAAIIY ERDYNYNYFG FKTLERSYLL KINGKVVERP QHMLMRVAVG
LHGDDISSAI ETYNLLSEKY FTHASPTLFS AATRKPQLSS CFLLTMKEDS IDGIYETLKQ
CALISKSAGG IGVNIHCIRS KGTYIAGTNG ISNGIVPMLR VFNNTARYVD QGGNKRPGAF
AIYLEPWHAD IFEFLDLKKN TGKEETRARD LFYALWIPDL FMERVEQNQE WCLMCPKTCP
GLSDCWGEEF NKLYLSYEEK GLYVKKVKAQ SLWYAIIESQ VETGTPYMLY KDACNRKSNQ
QNLGTIKCSN LCTEIVEYSS PEEIAVCNLA SIAVNMFVKP DKTYNFEKLK DVTKIITKNL
NKVIDITYYP VPEAKLSNLR HRPIGIGIQG LADAFILMRL PFDSPEAQKL NIQIFETIYY
GALEASSELA AIHGPYETYE GSPASKGILQ YDMWGVTPTN LWDWDALKNK IKKWGIRNSL
LIAPMPTAST AQILGNNESF EPYTTNIYTR RVLSGEFQVV NQHLLKDLTE IGLWNDEMKN
TIIANGGSIQ NIDSIPKELK ALYKTVWEIS QKVILKMAAD RGAFIDQSQS LNIHIAQPNY
GKLTSMHFYA WKLGLKTGMY YLRTKPAAQP IQFTVDKTKV NNANVKEVST EKDKFNMESI
SCSLQNKDDC LMCGS
//
