ID V4YA77_9ARCH Unreviewed; 1288 AA.
AC V4YA77;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|RuleBase:RU003410};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU003410};
GN ORFNames=A07HR60_01231 {ECO:0000313|EMBL:ESS11893.1};
OS uncultured archaeon A07HR60.
OC Archaea; environmental samples.
OX NCBI_TaxID=1412874 {ECO:0000313|EMBL:ESS11893.1, ECO:0000313|Proteomes:UP000030679};
RN [1] {ECO:0000313|Proteomes:UP000030679}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24335829;
RA Podell S., Emerson J.B., Jones C.M., Ugalde J.A., Welch S.,
RA Heidelberg K.B., Banfield J.F., Allen E.E.;
RT "Seasonal fluctuations in ionic concentrations drive microbial succession
RT in a hypersaline lake community.";
RL ISME J. 0:0-0(2013).
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 -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000256|ARBA:ARBA00001922};
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC chain family. {ECO:0000256|RuleBase:RU003410}.
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DR EMBL; KI543230; ESS11893.1; -; Genomic_DNA.
DR STRING; 1412874.A07HR60_01231; -.
DR PATRIC; fig|1412874.3.peg.1408; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000030679; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
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; 2.
DR Gene3D; 3.20.70.20; -; 2.
DR Gene3D; 2.170.16.10; Hedgehog/Intein (Hint) domain; 3.
DR Gene3D; 3.10.28.10; Homing endonucleases; 2.
DR InterPro; IPR003586; Hint_dom_C.
DR InterPro; IPR003587; Hint_dom_N.
DR InterPro; IPR036844; Hint_dom_sf.
DR InterPro; IPR027434; Homing_endonucl.
DR InterPro; IPR006142; INTEIN.
DR InterPro; IPR030934; Intein_C.
DR InterPro; IPR004042; Intein_endonuc.
DR InterPro; IPR006141; Intein_N.
DR InterPro; IPR004860; LAGLIDADG_2.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR NCBIfam; TIGR01443; intein_Cterm; 1.
DR PANTHER; PTHR43371:SF1; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE; 1.
DR PANTHER; PTHR43371; VITAMIN B12-DEPENDENT RIBONUCLEOTIDE REDUCTASE; 1.
DR Pfam; PF14890; Intein_splicing; 2.
DR Pfam; PF14528; LAGLIDADG_3; 2.
DR Pfam; PF02867; Ribonuc_red_lgC; 1.
DR Pfam; PF00317; Ribonuc_red_lgN; 1.
DR PRINTS; PR00379; INTEIN.
DR SMART; SM00305; HintC; 2.
DR SMART; SM00306; HintN; 2.
DR SUPFAM; SSF51294; Hedgehog/intein (Hint) domain; 2.
DR SUPFAM; SSF55608; Homing endonucleases; 2.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR PROSITE; PS50818; INTEIN_C_TER; 1.
DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 2.
DR PROSITE; PS50817; INTEIN_N_TER; 2.
PE 3: Inferred from homology;
KW Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813};
KW Cobalamin {ECO:0000256|ARBA:ARBA00022628};
KW Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW Deoxyribonucleotide synthesis {ECO:0000256|RuleBase:RU003410};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003410};
KW Protein splicing {ECO:0000256|ARBA:ARBA00023000};
KW Reference proteome {ECO:0000313|Proteomes:UP000030679}.
FT DOMAIN 303..437
FT /note="DOD-type homing endonuclease"
FT /evidence="ECO:0000259|PROSITE:PS50819"
FT DOMAIN 869..1001
FT /note="DOD-type homing endonuclease"
FT /evidence="ECO:0000259|PROSITE:PS50819"
FT DOMAIN 1080..1102
FT /note="Intein C-terminal splicing"
FT /evidence="ECO:0000259|PROSITE:PS50818"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 788..807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1288 AA; 142355 MW; 3584348BDBBFF4C0 CRC64;
MSDANDSANE IQLPIKRTEG DTMEERLTSN AYSNVLPARY LRKDSDGNLA EDQDELFARV
GKNIALAEAV FESRKQDVDV SVTPAQLKPD HPRRDELAAE VFGAGTTADD DVETTLTERN
VNKFAYETIV SELPDEVKGH VEQKASEFTD AMEQLSFMPN CVPPNSMVAS GGGLKQLTDI
EPGERVYDDE DGQARVESKF ENGEKLVREI TTRSGYTVRA TPEHYFRVIT EDGSYEWRQV
KNLRPDDSLA LQKNFLDDDG SRSTLRPNGA ADGGVVADTS ENTGRPRLAI NTPDRMTPAL
AEWLGLYVGD GTARESGVRV AFDAQDEDLV DYFQDLTDTI FGFEPTRRDR SDADCVIGQA
CRRALYEFLD RNDLLKETSK TATIPPAVLE SGRSCIARFL RGLFEADGTV GDRSIELYTH
SESLAGEVQQ SLLGLGIRST VTPKRDGYRV TVRKNVCGSR FVDRVGFRSD RKQAGAEAFE
TVADSATSVK IPNQSERLHD WYQTSDLGQD AYRALSQFLI DPDSEYHQEI GVGIFRRYAD
EYPELWDSPV AALVERDQFY DSIAEISDVG RMAVEDMQVP RRNTYVVEGF VSHNSPSLMN
AGDELQQLSA CFVDSPDDDI TDIHNTAKEA AEVFQCLTAE TTVHVDGKGT VSIADVEPGD
DIRQRDGDEY TTRRVAETHA YDDAPVYEVQ TDSGIELTGT PNHELSVNGD WKRIDEIEVG
DTLSACLGWL PETTDAPSLT SVPSSGQWDS TRTVDNDAVR ELHGAGLSDY QIAERLDCSA
STVQRRRANE LDLEPNGSGG RTPGSVSFDT AEFETLYQRG QSDREIASQL DVHTTTVGQY
RHRQSLAPNG DQVKSVAQPS TLTPDLAELL GMWVGDGSKH EDGIRFHLNR EENLEHVDHV
CRRLFDEGLD WRFEDGCYDA VLHSHEVKRF WLRNFGDAKP DAPSAQVPEQ IWDAGRETVA
AFLRGLFSTD GSLQKDTYPR LRSASEDLVT GVQQLLVGLG MPALVWDIDS EEREYYNVGP
TGERGLTAFA ERVGFTDARD DDIAAALDRT SLQGTSVGTV RDDGVWEVPV TAVEDAGTST
VYDVTVADNH EYLANSVVSH NSGGGMGYAF WQLRPYGDPV GSTGGIASGP ITFMRTYDQL
CETIAQGGAR RGAQMGVMRV SHPDVIQFIH AKNKDVSLAN TLRLNDPDDF THNSFADALE
EARDLIDDDG KVPEHLRNAV EGHLSNFNIS VGITDDFMTA VKNDEEFTFT NPRTEEPHIA
TAETKELYDM YGLGAHVAGR RDTVDPSR
//
