ID A0A1J8Q287_9AGAM Unreviewed; 950 AA.
AC A0A1J8Q287;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=BRCT domain-containing protein {ECO:0000259|PROSITE:PS50172};
GN ORFNames=AZE42_06358 {ECO:0000313|EMBL:OJA07841.1};
OS Rhizopogon vesiculosus.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Suillineae; Rhizopogonaceae; Rhizopogon.
OX NCBI_TaxID=180088 {ECO:0000313|EMBL:OJA07841.1, ECO:0000313|Proteomes:UP000183567};
RN [1] {ECO:0000313|EMBL:OJA07841.1, ECO:0000313|Proteomes:UP000183567}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM-OR11-056 {ECO:0000313|EMBL:OJA07841.1,
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=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|ARBA:ARBA00001962};
CC -!- SIMILARITY: Belongs to the PhyH family.
CC {ECO:0000256|ARBA:ARBA00005830}.
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:OJA07841.1}.
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DR EMBL; LVVM01006535; OJA07841.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J8Q287; -.
DR STRING; 180088.A0A1J8Q287; -.
DR OrthoDB; 1553at2759; -.
DR Proteomes; UP000183567; Unassembled WGS sequence.
DR CDD; cd00027; BRCT; 1.
DR Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR008775; Phytyl_CoA_dOase-like.
DR PANTHER; PTHR20883; PHYTANOYL-COA DIOXYGENASE DOMAIN CONTAINING 1; 1.
DR PANTHER; PTHR20883:SF15; PHYTANOYL-COA DIOXYGENASE DOMAIN-CONTAINING PROTEIN 1; 1.
DR Pfam; PF05721; PhyH; 1.
DR SUPFAM; SSF52113; BRCT domain; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR PROSITE; PS50172; BRCT; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000183567}.
FT DOMAIN 47..121
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 142..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 950 AA; 106910 MW; 23AAD4B1E51A5FA5 CRC64;
MAPARSTRRN QHEQSVSLRS AQPDPSPVAD GSPGSDLFLE PMMGTPLTVY IEKEVEDRDI
LVELITKHGG TTSPGYSGTP YILVDPHKES GQNLYRQYAG KKGKIVLHYR WVHECIRTGA
LQTFHSNWAG CKVTGMEKVT PPTIVSSQND QTRSTVSQPA QMQPIPPQPQ TIPHIPPGDP
MHPPQAPYGY PVYGHPMHGP PRGMQPPTAA PPQSWQTPNV IAPQQTHIAS PQTAAMLARQ
THPYRDEPWV TPFNQPPPHM VAGPSAPAYD YRYGEDRPEW VPPANEYSYD PTSYEHPYDQ
TAPYMSEAGL PAAGPSSVPA DNNPVEKPRG RKRTRNTAPP AASPSALVLN RRNPPARSPT
PPTRVIKSTY GGNLFTSDDV LYLKRYIDYC QEQGLVLSLR EICERIAVKA PHHTFYSWRR
YCNKHQIRLG GYSMDTGENN SPRPEGEGEP EEEEQPLPLG TTGPGIIAAA QARLQQDANR
PRNRSPTPPR ALFRSTTGKG VAFTDEDVAF LVRFMEYRKS QDRFDMVAFW KDVAAKAPHH
SRASWMKFWR RHKHELNRTE EDEPLPQPPE KKMRYSRGDD ILLAKYFFNK PEGTSDKIFQ
AFGRAHPHHP WKGWQEHHRI HKAKIDHFIQ QLANGENIDN DENAEESFIE MGRYLVVPGF
LSQEQTNSLM MRSKELLDEF TLEDHPLTKF TTSDKDHVGD DYFLNSGDKI RYFLEEDAID
GNGKLTRDKA KAVNKIGHAL HELDPAFRKV TLDNDRLKAL VRDLRFHHDP VALQSMVICK
QSQIGGAVPE HNDSTFLYTS PPTALGFWIA LEKCTPTNGA LSFLPGSHLT TPITKRFVRL
PGGGTGFEQL AASPPSSSDM SERTREIVSE GEYVLETCEP GDLVLIHGSV LHKSERNTSA
HTRYAYTFHM IDSSPYTEYD EKNWLQPTEA MPFSRMLDMP NESTLSIAVH
//