ID A0A316YI46_9BASI Unreviewed; 1127 AA.
AC A0A316YI46;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Response regulatory domain-containing protein {ECO:0000259|PROSITE:PS50110};
GN ORFNames=FA10DRAFT_303277 {ECO:0000313|EMBL:PWN88298.1};
OS Acaromyces ingoldii.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Exobasidiales; Cryptobasidiaceae; Acaromyces.
OX NCBI_TaxID=215250 {ECO:0000313|EMBL:PWN88298.1, ECO:0000313|Proteomes:UP000245768};
RN [1] {ECO:0000313|EMBL:PWN88298.1, ECO:0000313|Proteomes:UP000245768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 4198 {ECO:0000313|EMBL:PWN88298.1,
RC ECO:0000313|Proteomes:UP000245768};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; KZ819638; PWN88298.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316YI46; -.
DR STRING; 215250.A0A316YI46; -.
DR InParanoid; A0A316YI46; -.
DR OrthoDB; 1117127at2759; -.
DR Proteomes; UP000245768; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR000232; HSF_DNA-bd.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF6; RESPONSE REGULATORY DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00447; HSF_DNA-bind; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00056; HSFDOMAIN.
DR SMART; SM00415; HSF; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000245768}.
FT DOMAIN 792..906
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 945..1017
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1074..1127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..600
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 996..1010
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 841
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1127 AA; 118237 MW; 5A600C5099839A64 CRC64;
MSGGRQGPGH WQGAPSHQPA SSGSSPQNGQ PTPPGFNPAA NSYGRPPQQQ TTSQHMQQRY
SGGPSNSASG AAGVGGGSGA GGSSSGGTYG QGNLSPRSMH PSAPYNQQQP GAAIPAMYGE
QRSSAGSSHN FYGGFSGDQQ HMLENNGFTS GFSYSQQPQG QHQAGPPHQA TGHHQMYHQQ
PLSTPPIAAS SQQQHGYGQQ WVNPAATQPH LMQAPAGPGA YGYGQQSQPV YKADDYMQQQ
YPGQMVNMMQ QQQQQQQQPH QQAQQAQQKA ALKDEDEDDL DGDEDGEGGA AGGRKGKDKK
STSDFVKKLF RMLDDTSYST IVSWGPAGDS FIVKDMNDFT KHVLPRHFRH SNFASFVRQL
NKYDFHKVKK PEEQGQMPQV GVEQLWEFRH PAFMQHREDL LEQVKRKVPA SKKTGKGNLD
GGSPRDQSPT MPGTIDAAEK GAEDYAKLKE QVAALTASQD QMTSHMNNLT KQYQGVIGEM
MTFQKNMVQQ DQLMQNLIQY LMNLEADRQL ENKAGGSSAG QANQHGQIEG HGPARQALEN
GNAFVSGSET SKIVTSYSEA AKGSFAQMSA MAHAVNPDNS THHSGSARGS ASNMETPLSP
KSTGDGGRGL SPDKGKRRAS STAEAGDGAV FLHPPHLDAD AGNNGSTSEL FNAAASAVGN
PSLAGFEGAG LRVFTVGTLQ PRSSSDSTGL APDGSTPAGA ALESAFLKDM AGEDDNGESK
PFGISVPNLE QLPEGMPKVD KRTTSMAPTP ATAGVAADGG HNKKASTPSE GGSNMLRVRR
STYVPGWAVP PRVLVVDDDD TCRKIGSKFL QVFGCAIDVA VDGVSAVNKM NLEQYDLVLM
DIVMPNLDGV SATSLIREFD PRTPIISMTS NSAPNELLSY MSSGMNDVLP KPFTKEGLLN
MLEKHLIHLK TVQKMDEIPK ALGLPPVSDE QLKNVLTATA HSATSLSLPT TGGASSPDGP
GLGPSPLAAV MGNGPEAAHR ASSFSPPAHG GGDAASGQND VTSAMSPTFS GSDEDDGVVN
PLAGMGFSDE EYISMLQNLI AAGAVSDTGR GPGGEVNSAA DTVANVMGVA RGEGVGVSRT
SKEGTPIGSG PFAPGAQAAS KKRAAEAASS SDQQSDGKRS RITELHA
//
