ID A0A238VZH6_HALVU Unreviewed; 1878 AA.
AC A0A238VZH6;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|RuleBase:RU003410};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU003410};
GN ORFNames=SAMN06264855_104235 {ECO:0000313|EMBL:SNR39514.1};
OS Halorubrum vacuolatum (Natronobacterium vacuolatum).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halorubrum.
OX NCBI_TaxID=63740 {ECO:0000313|EMBL:SNR39514.1, ECO:0000313|Proteomes:UP000198397};
RN [1] {ECO:0000313|EMBL:SNR39514.1, ECO:0000313|Proteomes:UP000198397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8800 {ECO:0000313|EMBL:SNR39514.1,
RC ECO:0000313|Proteomes:UP000198397};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-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|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; FZNQ01000004; SNR39514.1; -; Genomic_DNA.
DR OrthoDB; 6188at2157; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000198397; 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; 4.
DR Gene3D; 3.20.70.20; -; 3.
DR Gene3D; 2.170.16.10; Hedgehog/Intein (Hint) domain; 2.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
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; 2.
DR NCBIfam; TIGR01445; intein_Nterm; 1.
DR PANTHER; PTHR43371:SF1; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE; 1.
DR PANTHER; PTHR43371; VITAMIN B12-DEPENDENT RIBONUCLEOTIDE REDUCTASE; 1.
DR Pfam; PF13384; HTH_23; 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; 2.
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:UP000198397}.
FT DOMAIN 436..568
FT /note="DOD-type homing endonuclease"
FT /evidence="ECO:0000259|PROSITE:PS50819"
FT DOMAIN 644..666
FT /note="Intein C-terminal splicing"
FT /evidence="ECO:0000259|PROSITE:PS50818"
FT DOMAIN 1008..1159
FT /note="DOD-type homing endonuclease"
FT /evidence="ECO:0000259|PROSITE:PS50819"
FT DOMAIN 1248..1270
FT /note="Intein C-terminal splicing"
FT /evidence="ECO:0000259|PROSITE:PS50818"
FT REGION 348..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1815..1835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1878 AA; 207996 MW; 94A23B007B249870 CRC64;
MSSDGLSADE LELPIKRTTG ETLKERLTGN AYHNILPARY FRKDADGELT ETPEEIFVRV
ARNVALADAV FEAERRDIEI TVTPDQLKPD HPRRDELAAE VFGAGTTVDD DAETTLSVYN
VNKFAYETVV PELPAEIRAH VEEVAETFQE GMESLSFMPN SPTLMNAGDE LQQLSACFVD
SPGDDITDIH QTAKEAAEVF QCLTEESTVT LEEDGIVSVA DVEVGDRIAQ RTDSGFQYKP
VEETHVYEDA ETLTVTLTNG LSVRGTPNHR LMVDGDWTRL DEIRAGQEIH YALGWLRELD
RERPELMSVA SGGQWSENRT VENAEILELY RQGYSDYEIA EQLDCGKSTV QRRRSTELEL
PPNGEGGRTP GPTSFDESTA HELYRDGHTD AEIAAELGVH QTTVGQFRAR EQLVPNGTPV
KSVHQPERLD EELAELVGLW VGDGSWHQDG VRFHVGRESV AEYIDQLARR LFGTKTSSSF
TDGCYEIGIN SHEIKRWWKA NFDCKPDGAR SARVPDAIKR APAEVVEAFL RGYFTADGTL
LDDTYPKLYS SSEDAIDDVA TLMMGLGYPV KKSVIRDEDA HPYYGLIPTT GEGRKAFLRD
VGFIDERREV GLSNIDSVSA RDAYRVGEEY TVKVESVVES EPTTVYDITV ADTHEYVTDG
IVSHNSGGGM GYAFWQLRPY GDAVGSTGGI ASGPITFMRT FDQMCETIAQ GGARRGAQMG
VMRVSHPDVI QFIHAKNKDV SLAHSLRLND PDDFTHTSFA DALEEARELI DDEGRVPEHL
RNAVEGHLSN FNISVGVTDD FMEALYADEE FVFTNPRTEE PHIATPETKE IYEMFDLGHH
VEVGEVLSVP AAELWEHIID GAHENGEPGV IYLERVNKQH SFDVEKHPDH RILATNPCVT
GDTLISTENG LIEAEELYEQ GVARDVVVDG RLSEETLKEA SSVYKTGEKD VYKLTTEEGY
ELRLTADHRV MTDDGWIEAG DLDAGDTVHI QNRKGSFGQH GTAAEGRVLG WLVGDGHLKN
GEERAVLNFY DEDATIAESL AEDVNEIIRE PIGNADYEVG VSDISRGESY RGAQAIEQRI
RSTRLYEYAE EAGLVDQKHQ VPEAVLRGSE EMARAFLQTL FTADGSVQGS SKNGRSIRLA
SSELGLLKQT QRLLLNFGVA SRIYENRRPA RTRELPDGKG GTKEYETKAQ HELVITKDNQ
QRFAEEVGFL REDKAEQLRE NLDSYTYSPQ NEPFTATVEA VTPDGYETVY DLTEPETHSF
VANGLVVHNC GEQPLEEYEA CNLGHINLST VADLDAPDWR VWSAEHADEY DSQEAAVDAF
LQEAIDFETL DARIDYGTRF LENVVTMSDF PVEKIEEKVR DMRKIGLGIM GLAQLYIQLG
VRYGSEEGNE IARQLMTHIN HESKWTSHEL AEERGVFNDW ADSKYADPVE YREWFEHHTG
LDADDWEDGF PIRNHNTTTI APTGTTSMVG NTTGGCEPIY NVAYYKNVSD DVQGDEMLVE
FDDYFLRTLE ANDIDVDEVK REAQEQMANN EFDGVEGLST VPNAIGELFV VTGDLTGKEH
AAVQCACQQG VDSAISKTCN FPNSASIEDM DEVYRYIYDH GGKGVTVYRD GTRSKQVLTT
RAKNTEFADE SEALETIIEG IEEVFGGLES FLGNEEVREA LDAEIEGLLE ASDEPTFEYT
ETRPRPDSLS GVTQRVETGY GKLYVTVNED EDGRPFELFA NIGHSGGYTN SFTEALAKVI
STALRSGVDP EEIVDELQGT RSPKVAWDKG EQIQSIPDAI GTALRRYLDD EIDKGIPQQQ
SLDDVEGDVA GAADAETADA ADASQTDGGA VAADAGGDDM TDALIAAGES PECPDCGGMS
LYYSEGCKTC ESCGWSEC
//
