Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
The radical SAM protein HemW is a heme chaperone.
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Bacterial HemW binds one heme per subunit, requires an intact iron-sulfur cluster for dimerization and for heme transfer (but not for heme binding), interacts with bacterioferritins and with the heme-containing NarI subunit of respiratory nitrate reductase, and transfers its covalently bound heme to a heme-depleted, inactive nitrate reductase, restoring activity.
"Of note, heme that was covalently bound to HemW was actively transferred to a"
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The human orthologue RSAD1 stably binds heme, leading the authors to conclude that the whole HemW/RSAD1 family acts as heme chaperones.
"domain-containing 1 (RSAD1) stably bound heme. In conclusion, our findings"
Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context.
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RSAD1 is a member of MitoCoP, a high-confidence human mitochondrial proteome of 1,134 protein-coding genes assembled from subtractive proteomics, spatial proteomics, importomics and stringent curation.
"We defined a human mitochondrial high-confidence proteome (MitoCoP) of 1,134 protein-coding genes"
Lactococcus lactis HemW (HemN) is a haem-binding protein with a putative role in haem trafficking.
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Lactococcus lactis HemW has no coproporphyrinogen III dehydrogenase activity in vivo or in vitro, despite HemW-like proteins being routinely annotated as such; no HemW-like protein has ever been shown to catalyse the reaction.
"showed that it is devoid of CPDH activity in vivo and in vitro. Recombinantly"
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Purified HemW contains an Fe-S cluster, is dimeric when the cluster is intact, and binds haem b covalently at one haem per monomer; in vivo it occurs as a haem-free cytosolic form and a haem-loaded membrane-associated form, and membranes trigger haem release, suggesting a haem trafficking role.
"covalently bound haem b in vitro, with a stoichiometry of one haem per monomer"
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HemW-like proteins constitute a distinct phylogenetic clade, separate from catalytic HemN.
"HemW-like proteins form a distinct phylogenetic clade that has not previously"
Human radical S-adenosylmethionine domain-containing 1 (RSAD1) is a Heme-binding protein.
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Purified human RSAD1 can be reconstituted with a [4Fe-4S] cluster that is reducible to the 1+ state, characterized by UV-visible and EPR spectroscopy.
"a [4Fe-4S]2+ cluster that could be reduced to the [4Fe-4S]+ state, and was"
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Protoporphyrin IX and its metal analogues, including Fe(II)-, Fe(III)- and Zn(II)-PPIX, bind the reconstituted [4Fe-4S] protein, and the heme complex binds oxygen, carbon monoxide and cyanide.
"bind porphyrins was evaluated, revealing that protoporphyrin IX (PPIX) and its"
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The authors describe human RSAD1 as a mitochondrial protein whose cellular role is not fully understood and conclude only that it may act in heme-related metabolism.
"discovered mitochondrial protein that plays an important yet not fully"
Radical SAM Enzymes Involved in Tetrapyrrole Biosynthesis and Insertion.
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Review distinguishing the catalytic radical SAM enzymes of tetrapyrrole biosynthesis (CgdH/HemN, AhbC, AhbD, NirJ, BchE) from HemW, the structurally related cytoplasmic heme chaperone that inserts heme into enzymes.
"heme is inserted into enzymes by the cytoplasmic heme chaperone HemW, a radical SAM enzyme structurally highly related to CgdH"
Mycobacterium lepromatosis MLPM_5000 is a potential heme chaperone protein HemW and mis-annotation of its orthologues in mycobacteria.
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HemW-like proteins lack the fourth cysteine of the HemN CX3CX2CXC motif, and genes annotated as mycobacterial HemN are in fact HemW orthologues, i.e. the HemN annotation of this clade is a systematic mis-annotation in protein databases.
"Therefore, the current annotations of mycobacterial HemN sequences should be corrected to heme chaperone 'HemW' in various protein databases"
Radical S-Adenosylmethionine Enzymes in Human Health and Disease.
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Authoritative review of the eight human radical SAM enzymes lists RSAD1 (with viperin) as being of unknown function.
"and RSAD1 and viperin, both of unknown function"
Redox cycling of viral RNA polymerase controls picornavirus replication.
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RSAD1 is reported to catalyse methionine oxidation of the picornaviral 3D RNA polymerase (FMDV, EV71, EMCV), promoting its ubiquitination, aggregation and autophagic degradation; the effect requires the SAM domain and the cluster-binding cysteines, and Rsad1 knockout mice are more susceptible to picornavirus challenge.
"radical SAM domain-containing protein 1 (RSAD1) catalyzes methionine oxidation of FMDV 3D polymerase and promotes its aggregation and subsequent degradation through the autophagy-lysosome pathway"
Exome sequencing in patients with chronic central serous chorioretinopathy.
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Rare-variant burden testing associated RSAD1 (among PIGZ, DUOX1 and LAMB3) with chronic central serous chorioretinopathy in female patients only, an association the authors state requires replication.
"but replication of these findings in additional cohorts of cCSC patients is necessary"