RSAD1_DICDI
ID RSAD1_DICDI Reviewed; 446 AA.
AC Q54VE8;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Radical S-adenosyl methionine domain-containing protein 1, mitochondrial;
DE AltName: Full=Putative heme chaperone;
DE Flags: Precursor;
GN Name=rsad1; ORFNames=DDB_G0280411;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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 -!- 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; AAFI02000036; EAL67184.1; -; Genomic_DNA.
DR RefSeq; XP_641161.1; XM_636069.1.
DR AlphaFoldDB; Q54VE8; -.
DR SMR; Q54VE8; -.
DR STRING; 44689.DDB0205185; -.
DR PaxDb; Q54VE8; -.
DR PRIDE; Q54VE8; -.
DR EnsemblProtists; EAL67184; EAL67184; DDB_G0280411.
DR GeneID; 8622541; -.
DR KEGG; ddi:DDB_G0280411; -.
DR dictyBase; DDB_G0280411; -.
DR eggNOG; ENOG502QRH0; Eukaryota.
DR HOGENOM; CLU_027579_0_1_1; -.
DR InParanoid; Q54VE8; -.
DR OMA; HIPWCVR; -.
DR PhylomeDB; Q54VE8; -.
DR PRO; PR:Q54VE8; -.
DR Proteomes; UP000002195; Chromosome 3.
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 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 3: Inferred from homology;
KW 4Fe-4S; Chaperone; Heme; Iron; Iron-sulfur; Metal-binding; Mitochondrion;
KW Reference proteome; S-adenosyl-L-methionine; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..446
FT /note="Radical S-adenosyl methionine domain-containing
FT protein 1, mitochondrial"
FT /id="PRO_0000330867"
FT DOMAIN 15..277
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 34
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 38
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 41
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 94
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 95..96
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 130
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 159
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 171
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 446 AA; 51495 MW; 6580DDEF7E2F136C CRC64;
MINKIVKNVI ENQFKGYNKL KDLPISLFVY WPYCSKICPY CNFNKYRDSD KVDHERMSKS
LSRELESFVK NIYLNSNENS FIRERPITSI YFGGGTPSLA KISTFVETIE TMKKLFPSSL
SIEDIEITLE VNPDQKDLKN LLKDFKKYVG VNRVSLGVQS LVDKDLHFLG RTHNRIQAEE
SIKIARDLFD HVTFDLIYSR TIDQTLEQWR NELRYALNLA DGNGHVSLYT LTFEQGTSFY
RRLSSKGNKF KIIPPDDQKS SDLYDLTVCE AEAMGFQQYE ISSFASSHNQ KGKHNLNYWR
SGDFIGIGPG ASSRLTTLNN NNNNNNQISR YSFKNILHPK EWMEKLNSKE ILCNAFIEDE
FNPTIPLTNF EVAEEMLLNG LRTIEGVQLS TFTFQTNGLT FDQFLNMKQV EILQEQGFLI
LEPTCLKLTG NGRKLLDTII PKILKY
