GenomeNet

Database: UniProt
Entry: A0A452FNT9_CAPHI
LinkDB: A0A452FNT9_CAPHI
Original site: A0A452FNT9_CAPHI 
ID   A0A452FNT9_CAPHI        Unreviewed;       348 AA.
AC   A0A452FNT9;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Ribonucleotide reductase regulatory TP53 inducible subunit M2B {ECO:0000313|Ensembl:ENSCHIP00000025925.1};
GN   Name=RRM2B {ECO:0000313|Ensembl:ENSCHIP00000025925.1};
OS   Capra hircus (Goat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Capra.
OX   NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000025925.1, ECO:0000313|Proteomes:UP000291000};
RN   [1] {ECO:0000313|Ensembl:ENSCHIP00000025925.1, ECO:0000313|Proteomes:UP000291000}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA   Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA   Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA   Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA   Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT   "Polished mammalian reference genomes with single-molecule sequencing and
RT   chromosome conformation capture applied to the Capra hircus genome.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCHIP00000025925.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LWLT01000011; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A452FNT9; -.
DR   Ensembl; ENSCHIT00000033787.1; ENSCHIP00000025925.1; ENSCHIG00000022467.1.
DR   GeneTree; ENSGT00390000013305; -.
DR   Proteomes; UP000291000; Chromosome 14.
DR   Bgee; ENSCHIG00000022467; Expressed in ileum and 18 other cell types or tissues.
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:UP000291000}.
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        135
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000355-1"
FT   BINDING         97
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT   BINDING         128
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT   BINDING         128
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT   BINDING         131
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT   BINDING         191
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT   BINDING         225
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT   BINDING         228
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
SQ   SEQUENCE   348 AA;  40210 MW;  562B53BDBC1A5469 CRC64;
     QGLNLPPAAP ALQTLSSDPN ENGAESDEEP LLRKSSRRFV IFPIQYPDIW KMYKQAQASF
     WTAEEVDLSK DLPHWNKLKS EEKYFISHIL AFFAASDGIV NENLVERFSQ EVQVPEARCF
     YGFQILIENV HSEMYSLLID TYIRDPKKRE FLFNAIETMP YVKKKADWAL RWIADRKSTF
     GERVVAFAAV EGIFFSGSFA AIFWLKKRGL MPGLTFSNEL ISRDEGLHCD FACLMFQYLV
     NKPSEERVRE IIVNAVEIEQ EFLTEALPVG LIGMNCVLMK QYIEFVADRL LTELGFSKVF
     QAENPFDFME NISLEGKTNF FEKRVSEYQR FAVMAETTDN VFTLDADF
//
DBGET integrated database retrieval system