ID D3ASY1_9CLOT Unreviewed; 787 AA.
AC D3ASY1;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE SubName: Full=Anaerobic ribonucleoside-triphosphate reductase {ECO:0000313|EMBL:EFC95075.1};
DE EC=1.17.4.2 {ECO:0000313|EMBL:EFC95075.1};
GN Name=nrdD {ECO:0000313|EMBL:EFC95075.1};
GN ORFNames=CLOSTHATH_06740 {ECO:0000313|EMBL:EFC95075.1};
OS Hungatella hathewayi DSM 13479.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; Hungatella.
OX NCBI_TaxID=566550 {ECO:0000313|EMBL:EFC95075.1, ECO:0000313|Proteomes:UP000004968};
RN [1] {ECO:0000313|EMBL:EFC95075.1, ECO:0000313|Proteomes:UP000004968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13479 {ECO:0000313|EMBL:EFC95075.1,
RC ECO:0000313|Proteomes:UP000004968};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
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:EFC95075.1}.
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DR EMBL; ACIO01000840; EFC95075.1; -; Genomic_DNA.
DR RefSeq; WP_006777146.1; NZ_GG667881.1.
DR AlphaFoldDB; D3ASY1; -.
DR HOGENOM; CLU_002707_0_2_9; -.
DR Proteomes; UP000004968; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008998; F:ribonucleoside-triphosphate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR CDD; cd01675; RNR_III; 1.
DR CDD; cd02947; TRX_family; 1.
DR Gene3D; 3.20.70.20; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR005144; ATP-cone_dom.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR012833; NrdD.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR NCBIfam; TIGR02487; NrdD; 1.
DR PANTHER; PTHR21075; ANAEROBIC RIBONUCLEOSIDE-TRIPHOSPHATE REDUCTASE; 1.
DR PANTHER; PTHR21075:SF0; ANAEROBIC RIBONUCLEOSIDE-TRIPHOSPHATE REDUCTASE; 1.
DR Pfam; PF03477; ATP-cone; 1.
DR Pfam; PF00462; Glutaredoxin; 1.
DR Pfam; PF13597; NRDD; 1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51161; ATP_CONE; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00492};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00492}; Oxidoreductase {ECO:0000313|EMBL:EFC95075.1}.
FT DOMAIN 2..95
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 787 AA; 89014 MW; CC365D2DF2F650E5 CRC64;
MIAVLKRDGE VAEFSLNKIT EAIKKAFKAT KKDYNNEILE LLSLRVTADF QEKMRDGQIT
VEQIQDSVEH VLEQTGYTDV AKAYILYRKQ REKIRNMKNT ILDYKDVVNS YVKVEDWRVK
ENSTVTYSVG GLILSNSGAV TANYWLSEIY DQEIADAHRN ADIHIHDLSM LTGYCAGWSL
KQLLMEGLGG IPGKITSSPA KHLSVLCNQM VNFLGIMQNE WAGAQAFSSF DTYLAPFVKI
DNLTYPEVKK CIESFIYGVN TPSRWGTQAP FSNITLDWTV PGDMAELPAI IGGKEADFKY
KDCKAEMDMI NKAFIETMIE GDANGRGFQY PIPTYSITKD FDWSDTENNR LLFEMTSKYG
TPYFSNYINS DMEPSDVRSM CCRLRLDLRE LRRKTGGFFG SGESTGSVGV VTINMPRIAY
LAKDEADFYS RLDHMMDVSA RSLKTKREVI TKLLNQGLYP YTKRYLGTFE NHFSTIGLIG
MNEVGLNAVW LGEDMTSTKT QEFTKNVLNH MRERLSDYQE KYGDLYNLEA TPAESTTYRL
AKHDRKKYPD IRTAGAEGDT PYYTNSSHLP VDYTADIFDA LDIQDELQTL YTSGTVFHAF
LGEKLPDWAA AARLVRTIAE NYKLPYYTLS PTYSICAEHG YLIGEHSVCP ICGKRAEIYS
RITGYYRPVQ NWNEGKTQEY KNRTTYDITG SVLKKGNKGA ETVKEAVHNA EIPAGSYLFT
TKTCPNCKMA KQFLKDVDYE VVDAEENAEL AEQLGIMQAP TLVVIKDGQV KKIANASNIR
KYAETIA
//
