ID F2Q399_TRIEC Unreviewed; 597 AA.
AC F2Q399;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Nuclear architecture-related protein 1 {ECO:0000256|ARBA:ARBA00031269};
GN ORFNames=TEQG_07534 {ECO:0000313|EMBL:EGE08617.1};
OS Trichophyton equinum (strain ATCC MYA-4606 / CBS 127.97) (Horse ringworm
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559882 {ECO:0000313|Proteomes:UP000009169};
RN [1] {ECO:0000313|Proteomes:UP000009169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4606 / CBS 127.97 {ECO:0000313|Proteomes:UP000009169};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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. {ECO:0000256|ARBA:ARBA00025099}.
CC -!- SIMILARITY: Belongs to the NARF family.
CC {ECO:0000256|ARBA:ARBA00006596}.
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DR EMBL; DS995783; EGE08617.1; -; Genomic_DNA.
DR AlphaFoldDB; F2Q399; -.
DR VEuPathDB; FungiDB:TEQG_07534; -.
DR eggNOG; KOG2439; Eukaryota.
DR HOGENOM; CLU_018240_0_1_1; -.
DR Proteomes; UP000009169; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1780; -; 1.
DR InterPro; IPR009016; Fe_hydrogenase.
DR InterPro; IPR004108; Fe_hydrogenase_lsu_C.
DR PANTHER; PTHR11615:SF258; CYTOSOLIC FE-S CLUSTER ASSEMBLY FACTOR CG17683-RELATED; 1.
DR PANTHER; PTHR11615; NITRATE, FORMATE, IRON DEHYDROGENASE; 1.
DR Pfam; PF02906; Fe_hyd_lg_C; 1.
DR SUPFAM; SSF53920; Fe-only hydrogenase; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 106..473
FT /note="Iron hydrogenase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02906"
FT REGION 31..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 484..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..505
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 597 AA; 64050 MW; 869D20D91E8F23E4 CRC64;
MSAILSADDL NDFISPGVAC IKPVETLPKK QEENPYEVTT EDKLEEQNPP PAQISLTDCL
ACSGCVTSAE AVLVSLQSHA EVLNTLDANP EIRLDGEGGA EARDGKIFVA SVSPQVRASL
ASTYGISERN AGYMIEQFLS GPNGLRAGGQ HGSGFTWVVD TNIMRQAVLE LSTAEVAESL
NAAAPLTPHD ESGKFSIPNR PILASSCPGW ICYAEKTHPH VLPHLSRLKS PQALTGTFLK
TIISKKLNTP PSQIWHLAVM PCFDKKLEAS RQELTDVSWR GEALDKASSP VRDVDCVITS
KELLMLASSR NISLPSLPLE PLPTHLQTPF PDQTIAQFLS TSNTLHFTQP AAAGPSGGYL
HHLLTTYQSK HADSIIQSQR GRNADVVEYT LVSAAGEPII KAARYYGFRN IQNLVRKLKP
ARASRLPGSR ANGPGARARP APVSNGKPGA PIPPAEFAYV EVMACPGGCT NGGGQIRLED
ARQANSSLAL PEGSASEQSS KPTPHDQRAW LARVDEAYYS DSSEDGGQAD RPHRMSSAEE
IHSILRYWSD MIGVPLENLV YTTYRKVESD VGKQKGPAGS IDTARVAELA GKAGGGW
//
