ID A0A091FWP9_9AVES Unreviewed; 333 AA.
AC A0A091FWP9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 22-FEB-2023, entry version 26.
DE SubName: Full=Ribonucleoside-diphosphate reductase subunit M2 B {ECO:0000313|EMBL:KFO74018.1};
DE Flags: Fragment;
GN ORFNames=N303_06327 {ECO:0000313|EMBL:KFO74018.1};
OS Cuculus canorus (common cuckoo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Cuculiformes; Cuculidae; Cuculus.
OX NCBI_TaxID=55661 {ECO:0000313|EMBL:KFO74018.1, ECO:0000313|Proteomes:UP000053760};
RN [1] {ECO:0000313|EMBL:KFO74018.1, ECO:0000313|Proteomes:UP000053760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N303 {ECO:0000313|EMBL:KFO74018.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|PIRSR:PIRSR000355-2};
CC Note=Binds 2 iron ions per subunit. {ECO:0000256|PIRSR:PIRSR000355-2};
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small
CC chain family. {ECO:0000256|ARBA:ARBA00009303}.
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DR EMBL; KL447477; KFO74018.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091FWP9; -.
DR STRING; 55661.A0A091FWP9; -.
DR Proteomes; UP000053760; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; IPR033909; RNR_small.
DR InterPro; IPR030475; RNR_small_AS.
DR InterPro; IPR000358; RNR_small_fam.
DR PANTHER; PTHR23409; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SMALL CHAIN; 1.
DR PANTHER; PTHR23409:SF19; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SUBUNIT M2 B; 1.
DR Pfam; PF00268; Ribonuc_red_sm; 1.
DR PIRSF; PIRSF000355; NrdB; 1.
DR SUPFAM; SSF47240; Ferritin-like; 1.
DR PROSITE; PS00368; RIBORED_SMALL; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|PIRSR:PIRSR000355-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000355-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000053760}.
FT ACT_SITE 120
FT /evidence="ECO:0000256|PIRSR:PIRSR000355-1"
FT BINDING 82
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT BINDING 113
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT BINDING 113
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT BINDING 116
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT BINDING 176
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT BINDING 210
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT BINDING 213
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO74018.1"
FT NON_TER 333
FT /evidence="ECO:0000313|EMBL:KFO74018.1"
SQ SEQUENCE 333 AA; 38673 MW; 6B5F17F209D1484A CRC64;
SPSAAESCLD CDEEPLLRKN PRRFVIFPIQ YPDIWKMYKQ AQASFWTAEE VDLSKDLPHW
NKLKADEKYF ISHVLAFFAA SDGIVNENLV ARFSQEVQIP EARCFYGFQI LIENVHSEMY
SLLIDTYIKD PEKRDFLFNA VETMPCVKKK ADWALKWIED RESTFGERVV AFAAVEGIFF
SGSFAAIFWL KKRGLMPGLT FSNELISRDE GLHCDFACLM FHYLVNRPSE ERVREIIVNA
VEIEQEFLTE ALPVGLIGMN CTLMKQYIEF VADRLLMELG FSKVFHAENP FDFMENISLE
GKTNFFEKRV SEYQRFAVMA ETMDNVFTLD ADF
//