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Database: UniProt
Entry: A0A2H5QBI4_CITUN
LinkDB: A0A2H5QBI4_CITUN
Original site: A0A2H5QBI4_CITUN 
ID   A0A2H5QBI4_CITUN        Unreviewed;       348 AA.
AC   A0A2H5QBI4;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:GAY62010.1};
GN   ORFNames=CUMW_214510 {ECO:0000313|EMBL:GAY62010.1};
OS   Citrus unshiu (Satsuma mandarin) (Citrus nobilis var. unshiu).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX   NCBI_TaxID=55188 {ECO:0000313|EMBL:GAY62010.1, ECO:0000313|Proteomes:UP000236630};
RN   [1] {ECO:0000313|EMBL:GAY62010.1, ECO:0000313|Proteomes:UP000236630}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Miyagawa wase {ECO:0000313|Proteomes:UP000236630};
RX   PubMed=29259619; DOI=10.3389/fgene.2017.00180;
RA   Shimizu T., Tanizawa Y., Mochizuki T., Nagasaki H., Yoshioka T., Toyoda A.,
RA   Fujiyama A., Kaminuma E., Nakamura Y.;
RT   "Draft sequencing of the heterozygous diploid genome of Satsuma (Citrus
RT   unshiu Marc.) using a hybrid assembly approach.";
RL   Front. Genet. 8:180-180(2017).
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   -!- 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:GAY62010.1}.
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DR   EMBL; BDQV01000290; GAY62009.1; -; Genomic_DNA.
DR   EMBL; BDQV01000290; GAY62010.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2H5QBI4; -.
DR   STRING; 55188.A0A2H5QBI4; -.
DR   Proteomes; UP000236630; 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:SF35; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SMALL CHAIN A; 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:UP000236630}.
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        132
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000355-1"
FT   BINDING         94
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT   BINDING         125
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT   BINDING         125
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         187
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT   BINDING         221
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT   BINDING         224
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;  40652 MW;  132CF2C2A7ACCEDA CRC64;
     MGSLKNETEN EVNQREQGEQ EQEDQEPILM EQNQRFCMFP IRYKQVWEMY KKAQASFWTA
     EEVDLSQDVQ HWERLLDSEK HFISHVLAFF AASDGIVLEN LAARFLNDIQ IPEARAFYGF
     QIAMENIHSE MYSLLLETYI KDSKEKHRLF NAIENIPCVA QKAKWALDWI HSSDSFAERL
     VGFACVEGIF FSGSFCAIFW LKKRGLMPGL TFSNELISRD EGLHCDFACL LYSLLWKRLH
     WQKVHHMVHE AVEIETQFVC EALPCALIGM NSSLMSQYIK FVADRLLVAL GCQRKYNVEN
     PFDWMEFISL QGKANFFERR VGDYQKASVM SSLQNGEKSF VFKMDEDF
//
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