ID A0A395HXE5_ASPHC Unreviewed; 584 AA.
AC A0A395HXE5;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Nuclear architecture-related protein 1 {ECO:0000256|ARBA:ARBA00031269};
GN ORFNames=BO97DRAFT_405427 {ECO:0000313|EMBL:RAL12460.1};
OS Aspergillus homomorphus (strain CBS 101889).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450537 {ECO:0000313|EMBL:RAL12460.1, ECO:0000313|Proteomes:UP000248961};
RN [1] {ECO:0000313|EMBL:RAL12460.1, ECO:0000313|Proteomes:UP000248961}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101889 {ECO:0000313|EMBL:RAL12460.1,
RC ECO:0000313|Proteomes:UP000248961};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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; KZ824283; RAL12460.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395HXE5; -.
DR STRING; 1450537.A0A395HXE5; -.
DR VEuPathDB; FungiDB:BO97DRAFT_405427; -.
DR OrthoDB; 5477067at2759; -.
DR Proteomes; UP000248961; 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:UP000248961}.
FT DOMAIN 110..463
FT /note="Iron hydrogenase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02906"
FT REGION 27..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 584 AA; 63006 MW; 387FEFBB7DE1DD4F CRC64;
MSAILSADDL NDFISPGVAC IKPVETLPKK EESSSDNPYE VTKEDKVQPE NLPPAQISLT
DCLACSGCVT SAEAVLISLQ SHAEVLNTLD TYPELSLSGD DVHDDESRIF VASVSPQVRA
SLAATYGITE KDANNIIHQF LSGPQGLRAG GAKNSGFSWV VDTNVMREAV LTLTADEISE
SLVATADSAG SSLPKRPILS SACPGWICYA EKTHPFILPH LSRLKSPQAL TGTFLKTVLS
KALGIPTSRI WHLAIMPCFD KKLEASREEL TDAAWSPSPS DSTTPIRDVD CVITTRELLS
LASSRGISLP DLPSKPFTQP QFPDPVLNDF LFSRKGSEQN ATTGTSGGYL YHVLKAFQSR
NPGSEIEIQR GRNADVVEYF LMSPEKQPIM KAARYYGFRN IQNLVRKLKP ARVSRLPGVK
AANGAMGGAR RQPMARNAAS GGSGSDYTYV EVMACPGGCT NGGGQIRIED AREATSSTPN
EEVATSKPSP HEQRAWLARV DEAYYSAESD SESEVNSQSQ PLSLQEQEAR VHNALTHWST
FMGVPLSKLA YTTYREVESD VGKPQGPPDA TRVVELAGKI GGGW
//
