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Database: UniProt
Entry: A0A2K5L763_CERAT
LinkDB: A0A2K5L763_CERAT
Original site: A0A2K5L763_CERAT 
ID   A0A2K5L763_CERAT        Unreviewed;       299 AA.
AC   A0A2K5L763;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Ribonucleotide reductase regulatory TP53 inducible subunit M2B {ECO:0000313|Ensembl:ENSCATP00000008780.1};
GN   Name=RRM2B {ECO:0000313|Ensembl:ENSCATP00000008780.1};
OS   Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Cercocebus.
OX   NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000008780.1, ECO:0000313|Proteomes:UP000233060};
RN   [1] {ECO:0000313|Ensembl:ENSCATP00000008780.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small
CC       chain family. {ECO:0000256|ARBA:ARBA00009303}.
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DR   AlphaFoldDB; A0A2K5L763; -.
DR   Ensembl; ENSCATT00000030831.1; ENSCATP00000008780.1; ENSCATG00000026045.1.
DR   GeneTree; ENSGT00390000013305; -.
DR   Proteomes; UP000233060; Unplaced.
DR   Bgee; ENSCATG00000026045; Expressed in pituitary gland and 12 other cell types or tissues.
DR   GO; GO:0016020; C:membrane; 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   SUPFAM; SSF47240; Ferritin-like; 1.
DR   PROSITE; PS00368; RIBORED_SMALL; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233060};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        135..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   299 AA;  34516 MW;  5E85A73DEC941D5D CRC64;
     MGDAERPEAA GLDLDEVDLS KDLPHWNKLK ADEKYFISHI LAFFAASDGI VNENLVERFS
     QEVQVPEARC FYGFQILIEN VHSEMYSLLI DTYIRDPKKR EFLFNAIETM PYVKKKADWA
     LRWIADRKST FGERVVAFAA VEGIFFSGSF AAIFWLKKRG LMPGLTFSNE LISRDEGLHC
     DFACLMFQYL VNKPSEERVR EIIVDAVQIE QEFLTEALPV GLIGMNCILM KQYIEFVADR
     LLVELGFSKI FQAENPFDFM ENISLEGKTN FFEKRVSEYQ RFAVMAETTD NVFTLDADF
//
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