ID C2M5K3_CAPGI Unreviewed; 551 AA.
AC C2M5K3;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Ribonucleoside-diphosphate reductase, alpha chain {ECO:0000313|EMBL:EEK14464.1};
DE EC=1.17.4.1 {ECO:0000313|EMBL:EEK14464.1};
GN ORFNames=CAPGI0001_2079 {ECO:0000313|EMBL:EEK14464.1};
OS Capnocytophaga gingivalis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Capnocytophaga.
OX NCBI_TaxID=553178 {ECO:0000313|EMBL:EEK14464.1, ECO:0000313|Proteomes:UP000003622};
RN [1] {ECO:0000313|EMBL:EEK14464.1, ECO:0000313|Proteomes:UP000003622}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33624 / DSM 3290 / CIP 102945 / JCM 12953 / NCTC 12372 /
RC 27 {ECO:0000313|Proteomes:UP000003622};
RA Sebastian Y., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Strausberg R.L., Nelson K.E.;
RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC chain family. {ECO:0000256|ARBA:ARBA00010406}.
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:EEK14464.1}.
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DR EMBL; ACLQ01000019; EEK14464.1; -; Genomic_DNA.
DR RefSeq; WP_002668453.1; NZ_ACLQ01000019.1.
DR AlphaFoldDB; C2M5K3; -.
DR STRING; 553178.CAPGI0001_2079; -.
DR eggNOG; COG0209; Bacteria.
DR Proteomes; UP000003622; Unassembled WGS sequence.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR013350; RNR_alpha.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR039718; Rrm1.
DR NCBIfam; TIGR02510; NrdE-prime; 1.
DR PANTHER; PTHR11573; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN; 1.
DR PANTHER; PTHR11573:SF6; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE SUBUNIT; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 3.
DR PRINTS; PR01183; RIBORDTASEM1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000313|EMBL:EEK14464.1}.
FT DOMAIN 81..201
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 205..373
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 378..529
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 551 AA; 62613 MW; 4913F6585E0F937C CRC64;
MNQENDIWWL NDESEQILNR GYLLKGESVE GAIERITSAA AKRLYKPELQ PAFKEMITKG
WISFSSPIWA NMGTERGLPI SCFNVHIPDS IEGITHKLGE VIMQTKIGGG TSGYFGELRH
RGSAVTDNGK SSGAVSFMKL FDSAMDVVSQ GGVRRGAFAA YLDIDHPDAE EFLQIKDTGY
HIQNLFFGVC VPDYWMQEMI EGDTEKRKLW ARVLESRQQK GLPYIFFTDN VNRKRPQVYK
DNNMFIHASN LCSEIMLPSS EEESFICCLS SMNLELFDEW KDTKAVKLAI FFLDAVLSEF
IEKTKGNYYL QSARNFAIRH RAVGLGVLGY HSYLQKNMIP FESFEATQFN ARAFQHIQSE
AEKATQELAH IYGEPELLKG YGRRNATTMA IAPTTSSSAI LGQVSPGIEP FSSNYYKVGL
SKGNFMRKNK YLTQLLEEKG LNNEDIWRSI RLSDGSVQHL QELTQEEKNV FKTFKEISPM
EIITQAAQRQ QYIDQSQSLN LNIPPTMPIR DVNKVLIEAW KLGVKSLYYQ RSQSVAKEMI
MNFVNCSSCE S
//