ID A0A1J8Q2J9_9AGAM Unreviewed; 627 AA.
AC A0A1J8Q2J9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Fork-head domain-containing protein {ECO:0000259|PROSITE:PS50039};
GN ORFNames=AZE42_00937 {ECO:0000313|EMBL:OJA15301.1};
OS Rhizopogon vesiculosus.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Suillineae; Rhizopogonaceae; Rhizopogon.
OX NCBI_TaxID=180088 {ECO:0000313|EMBL:OJA15301.1, ECO:0000313|Proteomes:UP000183567};
RN [1] {ECO:0000313|EMBL:OJA15301.1, ECO:0000313|Proteomes:UP000183567}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM-OR11-056 {ECO:0000313|EMBL:OJA15301.1,
RC ECO:0000313|Proteomes:UP000183567};
RA Mujic A.B., Kuo A., Tritt A., Lipzen A., Chen C., Johnson J., Sharma A.,
RA Barry K., Grigoriev I.V., Spatafora J.W.;
RT "Comparative genomics of the ectomycorrhizal sister species Rhizopogon
RT vinicolor and Rhizopogon vesiculosus (Basidiomycota: Boletales) reveals a
RT divergence of the mating type B locus.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03115};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966,
CC ECO:0000256|HAMAP-Rule:MF_03115};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03115}.
CC Mitochondrion intermembrane space {ECO:0000256|HAMAP-Rule:MF_03115}.
CC Nucleus {ECO:0000256|PROSITE-ProRule:PRU00089}.
CC -!- DOMAIN: The C-terminal domain binds 2 Fe-S clusters but is otherwise
CC mostly in an intrinsically disordered conformation. {ECO:0000256|HAMAP-
CC Rule:MF_03115}.
CC -!- DOMAIN: The N-terminal domain has structural similarity with S-
CC adenosyl-L-methionine-dependent methyltransferases, but does not bind
CC S-adenosyl-L-methionine. It is required for correct assembly of the 2
CC Fe-S clusters. {ECO:0000256|HAMAP-Rule:MF_03115}.
CC -!- DOMAIN: The twin Cx2C motifs are involved in the recognition by the
CC mitochondrial MIA40-ERV1 disulfide relay system. The formation of 2
CC disulfide bonds in the Cx2C motifs through dithiol/disulfide exchange
CC reactions effectively traps the protein in the mitochondrial
CC intermembrane space. {ECO:0000256|HAMAP-Rule:MF_03115}.
CC -!- SIMILARITY: Belongs to the anamorsin family. {ECO:0000256|HAMAP-
CC Rule:MF_03115}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03115}.
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:OJA15301.1}.
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DR EMBL; LVVM01003199; OJA15301.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J8Q2J9; -.
DR STRING; 180088.A0A1J8Q2J9; -.
DR OrthoDB; 5385885at2759; -.
DR Proteomes; UP000183567; Unassembled WGS sequence.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:UniProtKB-UniRule.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:UniProt.
DR CDD; cd00059; FH_FOX; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR HAMAP; MF_03115; Anamorsin; 1.
DR InterPro; IPR007785; Anamorsin.
DR InterPro; IPR046408; CIAPIN1.
DR InterPro; IPR031838; Dre2_N.
DR InterPro; IPR001766; Fork_head_dom.
DR InterPro; IPR030456; TF_fork_head_CS_2.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11829:SF343; FORK HEAD DOMAIN TRANSCRIPTION FACTOR SLP1-RELATED; 1.
DR PANTHER; PTHR11829; FORKHEAD BOX PROTEIN; 1.
DR Pfam; PF05093; CIAPIN1; 1.
DR Pfam; PF16803; DRE2_N; 1.
DR Pfam; PF00250; Forkhead; 1.
DR PRINTS; PR00053; FORKHEAD.
DR SMART; SM00339; FH; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS00658; FORK_HEAD_2; 1.
DR PROSITE; PS50039; FORK_HEAD_3; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|HAMAP-Rule:MF_03115};
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_03115};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03115};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW ProRule:PRU00089}; Iron {ECO:0000256|HAMAP-Rule:MF_03115};
KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_03115};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_03115};
KW Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03115};
KW Nucleus {ECO:0000256|PROSITE-ProRule:PRU00089};
KW Reference proteome {ECO:0000313|Proteomes:UP000183567}.
FT DOMAIN 55..148
FT /note="Fork-head"
FT /evidence="ECO:0000259|PROSITE:PS50039"
FT DNA_BIND 55..148
FT /note="Fork-head"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00089"
FT REGION 139..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..604
FT /note="Fe-S binding site B"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03115"
FT MOTIF 590..593
FT /note="Cx2C motif 1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03115"
FT MOTIF 601..604
FT /note="Cx2C motif 2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03115"
FT COMPBIAS 153..167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..203
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 521
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03115"
FT BINDING 535
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03115"
FT BINDING 538
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03115"
FT BINDING 540
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03115"
FT BINDING 590
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03115"
FT BINDING 593
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03115"
FT BINDING 601
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03115"
FT BINDING 604
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03115"
SQ SEQUENCE 627 AA; 68250 MW; 346BBEA2997B6495 CRC64;
MSQQPPPTVM PQNMLPPGEA ELAQANSYYP QEPADLTGGL PINLDSLRDG PPGSKPFYPY
STLIRYAIKG SPNQKLLLED IYYAIESRFP YFRSAPSGWK NSVRHNLSLN PCFEKVPRPL
TDRGKGSYWT VNDNVDPRTG VHRVRKKKPK GAKRRLSEED QDVDYHPEVF NDPNAQFVPQ
PPMHPDEAGP SRQAPYPPYP PTFDPNFQMM PPPPGLRFPP VPIDDLEVDE SGNILWRLSF
MKELAHLQQI SSDKDMGEDW YRMMLLRMRG AVMAPPPAYH DGMHPPPGMP PPPPPNPEMQ
ECLAFMAPTA IYTSPDLITP EVKKPLLNGS PCEAVKGPAL AIGSLDTAQD GQYQSLVFRL
DAQLGQAAER QMLNRLVNGA ITLAPSSYAS IHVLLSPTEY GALLPSLQPL LKQILAGLTP
LGTLYLLNLT TGLLSLPHDL TLAGFTIIEA VHDGADPKIV AQRPLPIAMP LLSALPLRRK
TDPAKQSSKK ALWALTTPST PTIDAESLLT AADRVRPIPT CEPVTAATPR RKKACKNCSC
GLAELEAEEA QTGKVLLLDS DSVVEVGAGD VAKERLIAAA KAAPKATSSC GNCFLGDAFR
CAGCPYLGLP AFNPGEKVEI DVGMDDI
//
