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Database: UniProt
Entry: A0A1F1KTT3_9CORY
LinkDB: A0A1F1KTT3_9CORY
Original site: A0A1F1KTT3_9CORY 
ID   A0A1F1KTT3_9CORY        Unreviewed;       341 AA.
AC   A0A1F1KTT3;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=ribonucleoside-diphosphate reductase {ECO:0000256|ARBA:ARBA00012274};
DE            EC=1.17.4.1 {ECO:0000256|ARBA:ARBA00012274};
GN   ORFNames=HMPREF3067_07795 {ECO:0000313|EMBL:OFS20144.1};
OS   Corynebacterium sp. HMSC04H06.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1581050 {ECO:0000313|EMBL:OFS20144.1, ECO:0000313|Proteomes:UP000177657};
RN   [1] {ECO:0000313|EMBL:OFS20144.1, ECO:0000313|Proteomes:UP000177657}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HMSC04H06 {ECO:0000313|EMBL:OFS20144.1,
RC   ECO:0000313|Proteomes:UP000177657};
RA   Ploux O.;
RL   Submitted (MAR-2016) 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}.
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:OFS20144.1}.
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DR   EMBL; LWPR01000057; OFS20144.1; -; Genomic_DNA.
DR   RefSeq; WP_034666259.1; NZ_KV823440.1.
DR   AlphaFoldDB; A0A1F1KTT3; -.
DR   STRING; 1581050.HMPREF3067_07795; -.
DR   GeneID; 34027290; -.
DR   OrthoDB; 9766544at2; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000177657; Unassembled WGS sequence.
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:UP000177657}.
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   341 AA;  38670 MW;  D3B6F3F6B1E7FCDD CRC64;
     MSSTSNTAEL TSISVTPPSY RHDPSARIRA INWNRVSDEK DLEVWNRLTA NFWLPEKVPL
     SNDLPAWQRM TPEERNLTMR VFTGLTTLDT VQATVGEICQ IQDARTEHEE AVYTNIAFMQ
     SVHARSYSSV FSTLSSTKEI DEAYRWAVNN DLLQARAKKV LTHYFGPDPL KRKVSSTLLS
     SLLLYAGFYL PLHFSVHATL TNTADMIRLI LRDKAVHGYY SGYKYQRGLE TSAPQRQQEM
     HDFTISLLEE LYALELDYSG ELYEPLGLMD DVAVFVRYNA NKALMNLGYP DYFPPEETEV
     NPEILAALAP GADENHDFFS GSGSSYVIGT AEETSDDDWD F
//
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