NAR1_KLULA
ID NAR1_KLULA Reviewed; 469 AA.
AC P53998; Q6CQ46;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Cytosolic Fe-S cluster assembly factor NAR1;
DE AltName: Full=Nuclear architecture-related protein 1;
GN Name=NAR1; Synonyms=LET1; OrderedLocusNames=KLLA0D19833g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 76492 / CBS 2359/152 / CLIB 210;
RA Wesolowski-Louvel M., Tanguy-Rougeau C., Fukuhara H.;
RL Submitted (FEB-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Component of the cytosolic Fe/S protein assembly machinery.
CC Required for maturation of extramitochondrial Fe/S proteins. May play a
CC role in the transfer of pre-assembled Fe/S clusters to target
CC apoproteins (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NARF family. {ECO:0000305}.
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; X70373; CAA49833.1; -; Genomic_DNA.
DR EMBL; CR382124; CAH01039.1; -; Genomic_DNA.
DR PIR; S31336; S31336.
DR RefSeq; XP_453943.1; XM_453943.1.
DR AlphaFoldDB; P53998; -.
DR SMR; P53998; -.
DR STRING; 28985.XP_453943.1; -.
DR EnsemblFungi; CAH01039; CAH01039; KLLA0_D19833g.
DR GeneID; 2892895; -.
DR KEGG; kla:KLLA0_D19833g; -.
DR eggNOG; KOG2439; Eukaryota.
DR HOGENOM; CLU_018240_0_1_1; -.
DR InParanoid; P53998; -.
DR OMA; EVMNCAG; -.
DR Proteomes; UP000000598; Chromosome D.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR GO; GO:0016020; C:membrane; IEA:EnsemblFungi.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0051536; F:iron-sulfur cluster binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; ISS:UniProtKB.
DR InterPro; IPR009016; Fe_hydrogenase.
DR InterPro; IPR004108; Fe_hydrogenase_lsu_C.
DR Pfam; PF02906; Fe_hyd_lg_C; 1.
DR SUPFAM; SSF53920; SSF53920; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Reference proteome.
FT CHAIN 1..469
FT /note="Cytosolic Fe-S cluster assembly factor NAR1"
FT /id="PRO_0000084407"
FT BINDING 20
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 56
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 59
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 62
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 168
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 215
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 394
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 398
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT CONFLICT 239
FT /note="E -> Q (in Ref. 1; CAA49833)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 469 AA; 52073 MW; 97968D79A71C06A2 CRC64;
MSALLRDADL NDFISPGLAC VKPAQPQKVE KKPSFEVEVG IESSEPEKVS ISLQDCLACA
GCITSSEEIL LSKQSHKVFL EKWSELEELD ERSLAVSISP QCRLSLADYY SMCLADLDRC
FQNFMKTKFN AKYVVGTQFG RSISISRINA TLKDRVPENE GPLLCSVCPG FVLYAEKTKP
ELIPHMLDVK SPQQITGNLL KQADPTCYHL SIMPCFDKKL EASREECEKE VDCVITPKEF
VAMLGDLSID FKSYMTEYDS SKELCPSGWD YKLHWLSNEG SSSGGYAYQY LLSLQSSNPE
SDIITIEGKN SDVTEYRLVS KSKGVIASSS EVYGFRNIQN LVRKLSQSAS VKKRGIKVKR
RGQSVLKSGE TSEKTTKVLT ADPAKTDFVE VMACPSGCIN GGGLLNEEKN ANRRKQLAQD
LSLAYTKVHS VNIPDIVHAY DDKSNDFKYN LRVIEPSTSS DVVAVGNTW
