RSAD1_DANRE
ID RSAD1_DANRE Reviewed; 444 AA.
AC A4IGH2;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Radical S-adenosyl methionine domain-containing protein 1, mitochondrial;
DE AltName: Full=Putative heme chaperone;
DE Flags: Precursor;
GN Name=rsad1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May be a heme chaperone, appears to bind heme. Homologous
CC bacterial proteins do not have oxygen-independent coproporphyrinogen-
CC III oxidase activity (By similarity). Binds 1 [4Fe-4S] cluster. The
CC cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-
CC L-methionine (By similarity). {ECO:0000250|UniProtKB:P32131,
CC ECO:0000250|UniProtKB:Q9HA92}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01266};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC -!- MISCELLANEOUS: Might carry two S-adenosyl-L-methionine binding sites
CC with only one binding to the iron-sulfur cluster.
CC {ECO:0000250|UniProtKB:P32131}.
CC -!- SIMILARITY: Belongs to the anaerobic coproporphyrinogen-III oxidase
CC family. HemW subfamily. {ECO:0000305}.
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DR EMBL; BC135099; AAI35100.1; -; mRNA.
DR RefSeq; NP_001077026.1; NM_001083557.1.
DR AlphaFoldDB; A4IGH2; -.
DR SMR; A4IGH2; -.
DR STRING; 7955.ENSDARP00000101526; -.
DR PaxDb; A4IGH2; -.
DR GeneID; 565897; -.
DR KEGG; dre:565897; -.
DR CTD; 55316; -.
DR ZFIN; ZDB-GENE-030131-2508; rsad1.
DR eggNOG; ENOG502QRH0; Eukaryota.
DR InParanoid; A4IGH2; -.
DR OrthoDB; 1201842at2759; -.
DR PRO; PR:A4IGH2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0004109; F:coproporphyrinogen oxidase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR034505; Coproporphyrinogen-III_oxidase.
DR InterPro; IPR006638; Elp3/MiaB/NifB.
DR InterPro; IPR010723; HemN_C.
DR InterPro; IPR004559; HemW-like.
DR InterPro; IPR007197; rSAM.
DR PANTHER; PTHR13932; PTHR13932; 1.
DR Pfam; PF06969; HemN_C; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDF00562; HemN-like__clustered_with_heat; 1.
DR SFLD; SFLDS00029; Radical_SAM; 2.
DR SMART; SM00729; Elp3; 1.
DR TIGRFAMs; TIGR00539; hemN_rel; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 2: Evidence at transcript level;
KW 4Fe-4S; Chaperone; Heme; Iron; Iron-sulfur; Metal-binding; Mitochondrion;
KW Reference proteome; S-adenosyl-L-methionine; Transit peptide.
FT TRANSIT 1..39
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 40..444
FT /note="Radical S-adenosyl methionine domain-containing
FT protein 1, mitochondrial"
FT /id="PRO_0000330866"
FT DOMAIN 40..274
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 47
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 53
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 57
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 60
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 102
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 103..104
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 135
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 162
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 174
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 199
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P32131"
SQ SEQUENCE 444 AA; 50036 MW; 7BC537C92A80F7CF CRC64;
MSTRVLTLTL LKKRHLMQCF WSTVGSVHLR SIASDKIPSH AVEASLYVHW PYCLKRCSYC
NFNKYISRSE NHDTMTECLQ KETETLLKLS QVSRITSVFF GGGTPSLAQP STIAAVLETV
TKNSNLSDLA EVTLEVNPTP AGKARLKDFT LAGVNRFSIG VQSLNADHLR ILGRDHSVQH
ALQTVSEARK LCPGRVSVDI MFALPGQSVS CWQKQLEELL YVCDDHISLY QLTLERGTQL
FKQVESGKLS VPGDEVTAIM YKTACRVLEE SGFHQYEVSN FARNNAVSEH NMGYWRGHQY
IGVGPGAHGR FVPHGDGGVQ REARTQTLEP DVWIKEVQSR GRGTRRRITL HHLQLLEEVL
VMGLRMNEGI THQHWELFSP EANLQQVFGK SANIQELQGG RFLILDDRGL RCSWEGLVLL
DSILPTILLE LEMFFHSRGI KRTQ
