NAR1_PHANO
ID NAR1_PHANO Reviewed; 632 AA.
AC Q0UM75;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Cytosolic Fe-S cluster assembly factor NAR1;
DE AltName: Full=Nuclear architecture-related protein 1;
GN Name=NAR1; ORFNames=SNOG_07139;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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}.
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DR EMBL; CH445334; EAT85790.1; -; Genomic_DNA.
DR RefSeq; XP_001797492.1; XM_001797440.1.
DR AlphaFoldDB; Q0UM75; -.
DR SMR; Q0UM75; -.
DR STRING; 13684.SNOT_07139; -.
DR EnsemblFungi; SNOT_07139; SNOT_07139; SNOG_07139.
DR GeneID; 5974382; -.
DR KEGG; pno:SNOG_07139; -.
DR eggNOG; KOG2439; Eukaryota.
DR HOGENOM; CLU_018240_0_1_1; -.
DR InParanoid; Q0UM75; -.
DR OMA; PHEQRAW; -.
DR OrthoDB; 705416at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0097361; C:CIA complex; IBA:GO_Central.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central.
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..632
FT /note="Cytosolic Fe-S cluster assembly factor NAR1"
FT /id="PRO_0000383735"
FT REGION 27..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 210..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..571
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 20
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 65
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 68
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 240
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 295
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 486
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 490
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
SQ SEQUENCE 632 AA; 67399 MW; 9BB41B74438B5BCD CRC64;
MSAILSADDL NDFISPGVAC IKPIETLPAK PEDSSNPYEV TTEDKAAASQ PPPPASISLT
DCLACSGCVT SAEAVLVSLQ SHSEVLTTLD TYRSLRAPWQ TQNGTNGTNG TNGTTNGHST
NGTTTNGING HSHEGKLFVA SVSPQSRASI AAVFNVSEAE AGNMIAQLLS GPSGLKTGGH
QGSDFTWVLD TNVVREACLV AAADEVANAL SPETSNPSTK PGSEGAIDTT PKQPILTSAC
PGWICYAEKT HPYILPHLSR LKSPQALTGT LIKSVLSQQY NIPPSQIWHV AIMPCFDKKL
EASRSELTSS AWLPNHDATQ DPVRDVDCVI TARELLHLAS ARGINFASLP RTPLSASERT
PFPDPKLDAF LFPHTRRKNQ DVVAGSSGGY LYHILQTYQA QNPGSSISVS RGRNADVVEY
SLVRGSETII RAARFYGFRN IQNLVRRLKP AKASRLPGGK TGVSRKPGAA AGGDVKDYAY
VEVMACPGGC TNGGGQVKIT EVEEVRAYEG VESTNGDTLA PKPGPKEQKE WLAKVDEAYF
SGSDSEEEKV DQDGDQNMQD ATTNGHTSEP DIVNGISRRK INDVVAHWSH LTGVDTQKLL
YTSYRKVESD VGKKQSDMER VAGLAVTVGG GW
