ID C6HCC6_AJECH Unreviewed; 1911 AA.
AC C6HCC6;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Histidine kinase {ECO:0000313|EMBL:EER42216.1};
GN ORFNames=HCDG_03675 {ECO:0000313|EMBL:EER42216.1};
OS Ajellomyces capsulatus (strain H143) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=544712 {ECO:0000313|EMBL:EER42216.1, ECO:0000313|Proteomes:UP000002624};
RN [1] {ECO:0000313|Proteomes:UP000002624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H143 {ECO:0000313|Proteomes:UP000002624};
RA Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.M.,
RA Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S.,
RA Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J.,
RA Yandava C., Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S.,
RA Nino-Vega G., San-Blas G., Taylor J.W., Mendoza L., Galagan J.E.,
RA Nusbaum C., Birren B.W.;
RT "The genome sequence of Ajellomyces capsulatus strain H143.";
RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; GG692422; EER42216.1; -; Genomic_DNA.
DR STRING; 544712.C6HCC6; -.
DR VEuPathDB; FungiDB:HCDG_03675; -.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_000263_0_0_1; -.
DR OMA; WGQKATF; -.
DR Proteomes; UP000002624; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43719:SF76; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK1; 1.
DR PANTHER; PTHR43719; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:EER42216.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000002624};
KW Transferase {ECO:0000313|EMBL:EER42216.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 977..1031
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1188..1242
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1253..1479
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1775..1897
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 74..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 593..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1121..1153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1528..1574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..111
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..483
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..626
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1827
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1911 AA; 211349 MW; 3F03187A7F292D71 CRC64;
MRTPPPPSPV DAASSTASSK CPHRLPSRSR LSAAFPFVSY DPDPSAFSMH QYDFSADDAP
VHSLKSSSSV VAAAAAAAAA SMRESFAEPT PPPEHSHHHH HHQHQHRRPG LPPRGQRQSM
HTLEELRNQM EGVSVFHSRS SSHTFSTKPP PVSSHEMKSP RKAKKSIRST PSSPSNIPVP
PASLKPSGHP DSSSSSCTVK SPKRTDHSEL SAFPFPPPSS LVASVDQSLD SLVDARPIVK
RLSIRRTRDR RNKSPSAASE SAELNGSTWQ DPFMPHDSDT AADDPRYPTP NLYDITLALN
SEAGLDAWWS NTVRVLHTHF GAERAALAVP GDSTDLENVP WGQKATYSLY GYRSSSPSAG
TTQGSCGAEA PLKDSPDQET VDVDRGQNNS ISTKPNGHVL TPSEKRPPVV ARHSFAGFGG
PGNVGSRDKN VRPDVLKRTK SSLGSATLQH GTKGDKDSTV LADHALASSS DQRPSQASVD
SRERTPCPSV AVFPVPRALE VESDPLIRRT GVVKLFGRTK PAVLTRQYSH DPMASPIYDS
VMKQASKNDA HQTASDVPVL SEPATCDVPI GRVSIYSASS TSTTTQTIME LPRTSAADYS
RNGASPPSSS CSDSYEEYEQ IPQSPWSQSP APSPAPISDP EKNPFFNTNK VDEDAFASSP
PLRDYSTNQP IEAIGVDRAK TIIHIPLVHS SSSKQSISNT LRFPVAIISV LTSTIPYPAN
LRKSLEYLLP HLTTSFCLAQ QYSQLERQLS TSRTQRFGHI LGLGGTFSDA SSEMELVAGL
SNHVNYPLGE NVSLQAHSTI SSPLQRSDTS RSNSAISGVN TPGMEIGVGM PRDIYLTPGL
LSKQTSEYSD SYFNLKQQPG GIIPTPPSRT PSMSALPQGF SRFASPVSIA TQLHRELPPR
PFPDTIAQLM LNSVPLHLFL AKPHTGEVIW TNDKFDSYRT SQPHEQRARD PWLDVHDSER
ENLLKQWEKA LRSGSQFTER VRVKRYNDES AYRWFIFRAN PLLSQAGELL YWIGSFLDVH
EQRIAEMKAA QEREVFATNA KYKALANSIP QVVFEAAEYH GLISANEQWQ QYTGQSLEDA
LNLGFAKHIH RDDLEKCGIL LPPNIIPESD NPIEFGRIIN SLRGSEPSNG TPKSDSSELR
NKRPFSRTNS FHDKNGCSKY QGLTHALHEL VEKGVVTIQK DENERYSYTT EIRLRSRGGD
FRWHLVRLVK VETTSFGDGE ASWYGTCTDI NDRKLLERKL NREMESKTKF FSNMSHEIRT
PLNGILGTIP FILDTQLDND QRRMLDTIQN SSTNLRELVD NILDVSKVEA GKMNMVRQWF
HVRSVVEDVI DTIGSRAIDK GLELNYLVEP DVPAMVIGDR FRIRQILINL MGNAVKFTSQ
GEIYTRCSIH RDPSVPVNGT EILLNFEVVD TGKGFSSTDA ERLMQRFSQI EGSGSQQHSG
SGLGLFLSKQ LVEMHGGRLT PTSKEGQGAK FSFFVKVDAP PPPPPQDSSN LNLEDRYLQP
IDDISPFKSP NKQEFHLTQD MLSLHSSTNS DVMSLPSKQL SGSSWGSNQI NTPPSSRSGG
TPSKPDQPNQ IIPLDISSPS MAATEVMVSS SSSQNIAPAL PSSYDVLIIC PFDYAREALK
QHIEQVIPLE VTCKETAILD VEDWKDLVTG GECPKFSHLV VCLPDANDVK ETMQIIIQFG
WDNNNIKHMP ALIIVSDIYQ KREISEAYDR FCAAGGKGFL VPKPVKPSSF SRIFDPSNQR
DLSNDRNQDM AREINNSFKT MSKIVKEVIG NKGYRILLVE DDETNRTVML KYLDKVKLAS
ETAGNGQECI DMVFSKEPGY YSLIICDIQM PIKNGYETCQ EIRSWEQRNH FPQIPIMALS
ANAMMDQIDD ASRAGFNDYV TKPIKHNELG KMMMELLDPS VPQVLLRDRN K
//
