ID A0A0B2X2T5_METAS Unreviewed; 553 AA.
AC A0A0B2X2T5;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Nuclear architecture-related protein 1 {ECO:0000256|ARBA:ARBA00031269};
GN ORFNames=MAM_01986 {ECO:0000313|EMBL:KHO00063.1};
OS Metarhizium album (strain ARSEF 1941).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=1081103 {ECO:0000313|EMBL:KHO00063.1, ECO:0000313|Proteomes:UP000030816};
RN [1] {ECO:0000313|EMBL:KHO00063.1, ECO:0000313|Proteomes:UP000030816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 1941 {ECO:0000313|EMBL:KHO00063.1,
RC ECO:0000313|Proteomes:UP000030816};
RX PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA St Leger R.J., Wang C.;
RT "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
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}.
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:KHO00063.1}.
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DR EMBL; AZHE01000003; KHO00063.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B2X2T5; -.
DR STRING; 1081103.A0A0B2X2T5; -.
DR HOGENOM; CLU_018240_0_1_1; -.
DR OrthoDB; 5477067at2759; -.
DR Proteomes; UP000030816; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000030816}.
FT DOMAIN 129..433
FT /note="Iron hydrogenase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02906"
FT REGION 391..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 553 AA; 58878 MW; 1C70770F43BA1050 CRC64;
MSAILSVDDL NDFISPGVAC IKPIETLPAA REQEQGQHET GVILDGQQPQ VGGAPAAQIS
LTDCLACSGC VTSAEAVLVS LQSHAEVLAT LDAAPALRGR AAVCRERRML ERLLRTERWG
LAGGGRWRNG FTWVVDTDVA REAALVLGAD EALGAPAAPG SGAPAPAPPV LSSACPGWVC
YAEKTHPHVL PHLSRVKSPQ ALMGTLLKTT LSRKLGIPPS RIWHLAVMPC FDKKLEASRE
ELTDEVWAAS GLPGRGVRDV DCVITSREII MLAESRGLNF FDIPCAEDDD TAGSLAEPAI
PFPDARIHNF LFPARAARRV PRMAGSSGGL LHHILQCKAA QIPGSEIQAT RGRNADVVEF
VVAVDGEPVF KAARYYGFRN IQNLVRRLKP ARPSRMPGGR PFGSARRPTG KSASLDYGYV
EVMACPGGCT NGGGQLKADD LVVRGRKKSA DKPGPQEQKE WLAEVDEAYF SGEEVDGAVK
VNGNDDGARN SEDVVGGISH SYIHDTLAYW CEATGISIDR LAFTTYREVI SDVGKGTGAE
NVVQLAGKVG GGW
//
