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Database: UniProt
Entry: A0A120JTY1_9FIRM
LinkDB: A0A120JTY1_9FIRM
Original site: A0A120JTY1_9FIRM 
ID   A0A120JTY1_9FIRM        Unreviewed;       353 AA.
AC   A0A120JTY1;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=ribonucleoside-diphosphate reductase {ECO:0000256|ARBA:ARBA00012274};
DE            EC=1.17.4.1 {ECO:0000256|ARBA:ARBA00012274};
GN   ORFNames=AOC36_10165 {ECO:0000313|EMBL:AMC94322.1};
OS   Erysipelothrix larvae.
OC   Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC   Erysipelotrichaceae; Erysipelothrix.
OX   NCBI_TaxID=1514105 {ECO:0000313|EMBL:AMC94322.1, ECO:0000313|Proteomes:UP000063781};
RN   [1] {ECO:0000313|EMBL:AMC94322.1, ECO:0000313|Proteomes:UP000063781}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LV19 {ECO:0000313|EMBL:AMC94322.1,
RC   ECO:0000313|Proteomes:UP000063781};
RA   Lim S., Kim B.-C.;
RT   "Erysipelothrix larvae sp. LV19 isolated from the larval gut of the
RT   rhinoceros beetle, Trypoxylus dichotomus.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000256|ARBA:ARBA00001962};
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC       {ECO:0000256|ARBA:ARBA00011209}.
CC   -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small
CC       chain family. {ECO:0000256|ARBA:ARBA00009303}.
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DR   EMBL; CP013213; AMC94322.1; -; Genomic_DNA.
DR   RefSeq; WP_067633920.1; NZ_CP013213.1.
DR   AlphaFoldDB; A0A120JTY1; -.
DR   STRING; 1514105.AOC36_10165; -.
DR   KEGG; erl:AOC36_10165; -.
DR   OrthoDB; 9766544at2; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000063781; Chromosome.
DR   GO; GO:0005971; C:ribonucleoside-diphosphate reductase complex; 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:InterPro.
DR   CDD; cd01049; RNRR2; 1.
DR   Gene3D; 1.10.620.20; Ribonucleotide Reductase, subunit A; 1.
DR   InterPro; IPR009078; Ferritin-like_SF.
DR   InterPro; IPR012348; RNR-like.
DR   InterPro; IPR026494; RNR_NrdF-like.
DR   InterPro; IPR033909; RNR_small.
DR   InterPro; IPR000358; RNR_small_fam.
DR   NCBIfam; TIGR04171; RNR_1b_NrdF; 1.
DR   PANTHER; PTHR23409; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SMALL CHAIN; 1.
DR   PANTHER; PTHR23409:SF18; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SUBUNIT M2; 1.
DR   Pfam; PF00268; Ribonuc_red_sm; 1.
DR   SUPFAM; SSF47240; Ferritin-like; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000063781}.
SQ   SEQUENCE   353 AA;  41481 MW;  076F22AF28BAA2BF CRC64;
     MPKTIQAVRA DRDYTGANWN THEDNFTQTF YDQNLSQFWR PEDISLQPDL NVWNVLDPKI
     KRAYSLNLLV LTFLDTYQGD IGMPVVARSM DESFHQRKSV LNFMAAMENA VHAKSYSNIF
     MTYLMNDEID ELFVWGEKNK NLQNIMALIV GYYENLDKMT YQKRYELAFV DELEYKEAQW
     KAMVASVFLE TCLFYSGFYY PLYFYGQGKL MQAGEIINLI LRDESIHGLY VGNLAIELYE
     SFSEEKQKEL YAWLESYLNA LYEEEKELIE TIYDPVELAH DVKIFVRYNA NKAMMNLGFD
     PFFEYEEVNP VVLNGLNTET KTMDNFSMKG NGYQKMKSES LKDSDFIFDQ PKV
//
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