RSAD1_BOVIN
ID RSAD1_BOVIN Reviewed; 442 AA.
AC A5D7B1;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (APR-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; BC140491; AAI40492.1; -; mRNA.
DR RefSeq; NP_001091605.1; NM_001098136.1.
DR AlphaFoldDB; A5D7B1; -.
DR SMR; A5D7B1; -.
DR STRING; 9913.ENSBTAP00000028387; -.
DR PaxDb; A5D7B1; -.
DR GeneID; 615755; -.
DR KEGG; bta:615755; -.
DR CTD; 55316; -.
DR eggNOG; ENOG502QRH0; Eukaryota.
DR InParanoid; A5D7B1; -.
DR OrthoDB; 1201842at2759; -.
DR Proteomes; UP000009136; 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; 1.
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..22
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 23..442
FT /note="Radical S-adenosyl methionine domain-containing
FT protein 1, mitochondrial"
FT /id="PRO_0000330865"
FT DOMAIN 34..270
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 43
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 49
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 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 56
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 98
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 99..100
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 131
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 158
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 170
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 195
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P32131"
SQ SEQUENCE 442 AA; 48722 MW; 9B1C87C3208721A2 CRC64;
MALPRSQARG WVKAAKMAQR RRPADDTGGP QSPAPGSQRA ALYVHWPYCE KRCSYCNFNK
YIPRGVDEAA LRRCLVIEAQ TLLRLSGVRR VESVFFGGGT PSLASPHTVA AVLEAVAQAA
HLPADSEVTL EANPTSASGS RLAAFGAAGV NRLSIGLQSL DDTELQLLGR THSARDALQT
LAEAQRLFPG RVSVDLMLGL PAQQVGPWLR QLQGLLRCCD DHVSLYQLSL ERGTTLFTQV
QQGALPAPDP ELAAEMYQEG RAVLREAGFR QYEVSNFARN GALSTHNWTY WQCGQYLGVG
PGAHGRFIPQ GAGGHTREAR IQTLEPDSWM KEVMLFGHGT RRRVPLSELE LLEEVLAMGL
RTDVGITHQH WQQFEPQLTL WDLFGASKEV KELQEQGLLL LDHRGLRCSW EGLAVLDSLL
LSLLSRLQEA WQQRTPSSVP RG
