ID A0A1R1PHV7_ZANCU Unreviewed; 838 AA.
AC A0A1R1PHV7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=AX774_g3314 {ECO:0000313|EMBL:OMH83184.1}, AX774_g6000
GN {ECO:0000313|EMBL:OMH80564.1};
OS Zancudomyces culisetae (Gut fungus) (Smittium culisetae).
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Harpellomycetes; Harpellales; Legeriomycetaceae; Zancudomyces.
OX NCBI_TaxID=1213189 {ECO:0000313|EMBL:OMH80564.1, ECO:0000313|Proteomes:UP000188320};
RN [1] {ECO:0000313|Proteomes:UP000188320}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL-18-3 {ECO:0000313|Proteomes:UP000188320};
RA Wang Y., White M., Kvist S., Moncalvo J.-M.;
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OMH80564.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL-18-3 {ECO:0000313|EMBL:OMH80564.1};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) 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|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|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:OMH80564.1}.
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DR EMBL; LSSK01001153; OMH80564.1; -; Genomic_DNA.
DR EMBL; LSSK01000484; OMH83184.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R1PHV7; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000188320; 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:UP000188320}.
FT DOMAIN 1..92
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT REGION 793..829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 838 AA; 93275 MW; C4394FA31E140A9C CRC64;
MYVLKRDGKS ERVQFDKITK RISHLCNGLD ADFVDAAAIA QKVIMGVYQG VTTVELDNLA
AETAATMTVQ HPDYAVLAAR LAISNLQKET DPKFSECAKK LYEYTNEKTG KHQPLISKQL
WELIQKNAKT IDEAVVDSRD FGYNYFGFKT LERSYLLRVN GKVVERPQYL LMRVSLGIHG
EDIEAAIETY NMMSQRLFTH ASPTLFNSGT NRPQLSSCFL LAMSDDSIEG IYDTLKQCAM
ISKSAGGIGL SVHNIRATGS YIAGTNGTSN GVVPMLRVFN QTARYVDQGG NKRPGAFAIY
LEPWHADVFD FLSLKKNHGK EENRARDLFY GMWIPDLFMK RVLENGEWSL FCPHEAPNLS
EVWGDEFEKL YTKYENTPGL ARKRVPAQQL WYAILDSQIE TGTPYMLYKD ACNSKSNQQN
LGTIKSSNLC TEIVEYTAPD EVAVCNLASI ALPSFVRPNA VRRPQASDGS NENGTPAFGV
FDKNDYDFAA LHAVAKRVAK NLDKIIDVNY YPVVEAANSN KRNRPIGIGV QGLADAFLML
RLPFESEGAR ELNLLIFETL YHAALEASCE LAEIHGPYPT YEGSPVSKGN LQMDMWGVTP
TNLWDWDSLR QKIAKHGVRN SLLMAPMPTA STSQILGFNE CFEPYTSNIY TRRVLAGEFQ
VVNPWLLKDL IDRKLWSDDM RQSIIAHNGS IQSIAEIPAD LKQLYKTVYE IKQKSFLDLA
ADRGAFIDQS QSLNIHMDNP NYQKLTSMHF YGWKKGLKTG MYYLRTKPAA DAIKFTIDSS
KLKAAKSTTG ITASASTTGD AAGTSLEDGS ANADEDDELN SGAACSRDNP EGCLMCSG
//
