ID L5KRC3_PTEAL Unreviewed; 364 AA.
AC L5KRC3;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Ribonucleoside-diphosphate reductase subunit M2 {ECO:0000256|ARBA:ARBA00040401};
DE EC=1.17.4.1 {ECO:0000256|ARBA:ARBA00012274};
DE AltName: Full=Ribonucleotide reductase small chain {ECO:0000256|ARBA:ARBA00042512};
GN ORFNames=PAL_GLEAN10020126 {ECO:0000313|EMBL:ELK13974.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK13974.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|ARBA:ARBA00001962};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small
CC chain family. {ECO:0000256|ARBA:ARBA00009303}.
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DR EMBL; KB030580; ELK13974.1; -; Genomic_DNA.
DR RefSeq; XP_006910291.1; XM_006910229.2.
DR RefSeq; XP_015443661.1; XM_015588175.1.
DR RefSeq; XP_015443662.1; XM_015588176.1.
DR RefSeq; XP_015443663.1; XM_015588177.1.
DR RefSeq; XP_015443664.1; XM_015588178.1.
DR RefSeq; XP_015443665.1; XM_015588179.1.
DR RefSeq; XP_015443666.1; XM_015588180.1.
DR RefSeq; XP_015443667.1; XM_015588181.1.
DR RefSeq; XP_015443668.1; XM_015588182.1.
DR AlphaFoldDB; L5KRC3; -.
DR STRING; 9402.L5KRC3; -.
DR GeneID; 112469018; -.
DR KEGG; pale:112469018; -.
DR CTD; 6241; -.
DR eggNOG; KOG1567; Eukaryota.
DR InParanoid; L5KRC3; -.
DR OrthoDB; 5487627at2759; -.
DR Proteomes; UP000010552; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:SF20; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SUBUNIT M2; 1.
DR Pfam; PF00268; Ribonuc_red_sm; 1.
DR SUPFAM; SSF47240; Ferritin-like; 1.
DR PROSITE; PS00368; RIBORED_SMALL; 1.
PE 3: Inferred from homology;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000010552}.
SQ SEQUENCE 364 AA; 42560 MW; C2DB351F486400A4 CRC64;
MKLPAAERVR PGKRQFHMVR RMLNIFMTFS PPQKTKVPAL SVQDEPLLRE NPRRFVIFPI
EYHDIWQMYK KAEASFWTAE EVDLSKDLQH WETLKPEERH FISHVLAFFA ASDGIVNENL
VERFSQEVQI TEARCFYGFQ IAMENIHSEM YSLLIDTYIK DSKEREFLFN AIETMPCVKK
KADWALRWIG DKEATYGERV VAFAAVEGIF FSGSFASIFW LKKRGLMPGL TFSNELISRD
EGLHCDFACL MFRHLLHKPS EQRVKEIIIN AVRIEQEFLT EALPVKLIGM NCTLMEQYIE
FVADRLMLEL GFNKVFRAEN PFDFMENISL EGKTNFFEKR VGEYQKMGVM SGPTENSFTL
DADF
//
