ID A0A922LAD4_DERFA Unreviewed; 241 AA. AC A0A922LAD4; DT 22-FEB-2023, integrated into UniProtKB/TrEMBL. DT 22-FEB-2023, sequence version 1. DT 03-MAY-2023, entry version 2. DE RecName: Full=Anamorsin homolog {ECO:0000256|HAMAP-Rule:MF_03115}; DE AltName: Full=Fe-S cluster assembly protein DRE2 homolog {ECO:0000256|HAMAP-Rule:MF_03115}; GN Name=CIAPIN1 {ECO:0000313|EMBL:KAH9529346.1}; GN ORFNames=DERF_003236 {ECO:0000313|EMBL:KAH9529346.1}, HUG17_5241 GN {ECO:0000313|EMBL:KAH7642196.1}; OS Dermatophagoides farinae (American house dust mite). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari; OC Acariformes; Sarcoptiformes; Astigmata; Psoroptidia; Analgoidea; OC Pyroglyphidae; Dermatophagoidinae; Dermatophagoides. OX NCBI_TaxID=6954 {ECO:0000313|EMBL:KAH9529346.1, ECO:0000313|Proteomes:UP000790347}; RN [1] {ECO:0000313|EMBL:KAH9529346.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Derf {ECO:0000313|EMBL:KAH9529346.1}; RC TISSUE=Whole organism {ECO:0000313|EMBL:KAH9529346.1}; RA Yim A.K.Y., Chan T.F., Ji K.M., Liu X.Y., Zhou J.W., Li R.Q., Yang K.Y., RA Li J., Li M., Law P.T.W., Wu Y.L., Cai Z.L., Qin H., Bao Y., Leung R.K.K., RA Ng P.K.S., Zou J., Zhong X.J., Ran P.X., Zhong N.S., Liu Z.G., Tsui S.K.W.; RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KAH7642196.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=JKM2019 {ECO:0000313|EMBL:KAH7642196.1}; RC TISSUE=Whole body {ECO:0000313|EMBL:KAH7642196.1}; RA Ji K., Li J.; RL Submitted (JUN-2020) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:KAH7642196.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=JKM2019 {ECO:0000313|EMBL:KAH7642196.1}; RX PubMed=34659625; RA Chen J., Cai Z., Fan D., Hu J., Hou Y., He Y., Zhang Z., Zhao Z., Gao P., RA Hu W., Sun J., Li J., Ji K.; RT "Chromosome-level assembly of Dermatophagoides farinae genome and RT transcriptome reveals two novel allergens Der f 37 and Der f 39."; RL World Allergy Organ J 14:0-0(2021). RN [4] {ECO:0000313|EMBL:KAH9529346.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Derf {ECO:0000313|EMBL:KAH9529346.1}; RC TISSUE=Whole organism {ECO:0000313|EMBL:KAH9529346.1}; RA Xiong Q., Wan A.T.-Y., Liu X.-Y., Fung C.S.-H., Xiao X., Malainual N., RA Hou J., Wang L., Wang M., Yang K., Cui Y., Leung E., Nong W., Shin S.-K., RA Au S., Jeong K.Y., Chew F.T., Hui J., Leung T.F., Tungtrongchitr A., RA Zhong N., Liu Z., Tsui S.; RT "Comparative Genomics Reveals Insights into the Divergent Evolution of RT Astigmatic Mites and Household Pest Adaptations."; RL Res Sq 0:0-0(2022). CC -!- FUNCTION: Component of the cytosolic iron-sulfur (Fe-S) protein CC assembly (CIA) machinery. Required for the maturation of CC extramitochondrial Fe-S proteins. Part of an electron transfer chain CC functioning in an early step of cytosolic Fe-S biogenesis, facilitating CC the de novo assembly of a [4Fe-4S] cluster on the cytosolic Fe-S CC scaffold complex. Electrons are transferred from NADPH via a FAD- and CC FMN-containing diflavin oxidoreductase. Together with the diflavin CC oxidoreductase, also required for the assembly of the diferric tyrosyl CC radical cofactor of ribonucleotide reductase (RNR), probably by CC providing electrons for reduction during radical cofactor maturation in CC the catalytic small subunit. {ECO:0000256|HAMAP-Rule:MF_03115}. CC -!- COFACTOR: CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; CC Evidence={ECO:0000256|HAMAP-Rule:MF_03115}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000256|ARBA:ARBA00001966, CC ECO:0000256|HAMAP-Rule:MF_03115}; CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_03115}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03115}. CC Mitochondrion intermembrane space {ECO:0000256|HAMAP-Rule:MF_03115}. CC -!- DOMAIN: The C-terminal domain binds 2 Fe-S clusters but is otherwise CC mostly in an intrinsically disordered conformation. {ECO:0000256|HAMAP- CC Rule:MF_03115}. CC -!- DOMAIN: The N-terminal domain has structural similarity with S- CC adenosyl-L-methionine-dependent methyltransferases, but does not bind CC S-adenosyl-L-methionine. It is required for correct assembly of the 2 CC Fe-S clusters. {ECO:0000256|HAMAP-Rule:MF_03115}. CC -!- DOMAIN: The twin Cx2C motifs are involved in the recognition by the CC mitochondrial MIA40-ERV1 disulfide relay system. The formation of 2 CC disulfide bonds in the Cx2C motifs through dithiol/disulfide exchange CC reactions effectively traps the protein in the mitochondrial CC intermembrane space. {ECO:0000256|HAMAP-Rule:MF_03115}. CC -!- SIMILARITY: Belongs to the anamorsin family. CC {ECO:0000256|ARBA:ARBA00008169, ECO:0000256|HAMAP-Rule:MF_03115}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03115}. 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:KAH9529346.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; SDOV01000004; KAH7642196.1; -; Genomic_DNA. DR EMBL; ASGP02000001; KAH9529346.1; -; Genomic_DNA. DR Proteomes; UP000790347; Unassembled WGS sequence. DR HAMAP; MF_03115; Anamorsin; 1. DR InterPro; IPR007785; Anamorsin. DR InterPro; IPR046408; CIAPIN1. DR PANTHER; PTHR13273; ANAMORSIN; 1. DR PANTHER; PTHR13273:SF14; ANAMORSIN; 1. DR Pfam; PF05093; CIAPIN1; 1. PE 3: Inferred from homology; KW 2Fe-2S {ECO:0000256|HAMAP-Rule:MF_03115}; KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_03115}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03115}; KW Iron {ECO:0000256|HAMAP-Rule:MF_03115}; KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_03115}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_03115}; KW Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03115}. FT DOMAIN 186..234 FT /note="Anamorsin C-terminal" FT /evidence="ECO:0000259|Pfam:PF05093" FT REGION 205..219 FT /note="Fe-S binding site B" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03115" FT MOTIF 205..208 FT /note="Cx2C motif 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03115" FT MOTIF 216..219 FT /note="Cx2C motif 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03115" FT BINDING 166 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03115" FT BINDING 175 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03115" FT BINDING 178 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03115" FT BINDING 180 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03115" FT BINDING 205 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03115" FT BINDING 208 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03115" FT BINDING 216 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03115" FT BINDING 219 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03115" SQ SEQUENCE 241 AA; 27335 MW; E6050FB49AED00BD CRC64; MDFSDCKECL TVLSLDQSLD EKLLKNSYVS NICCKSKLTI AINDLPSEKE AYDAIFTIEQ SFTDEQLKHL YKLLKPRSKF VIVRSRQVSN LTFLIKSNGF VVDRNEQDLI LAHKPEYEIG SAVEIDTKKI WTLAADEITD GDLIDDDELL DEQDKMKPKA EDLRVCATTK QRKACANCSC GLKEELEKSE MDKIRSNSQN LKSSCGNCYL GDAFRCESCP YRGFPAFKPG EKVILNNMDD L //