ID A0A0J8UN37_COCIT Unreviewed; 1285 AA.
AC A0A0J8UN37;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=CIHG_06779 {ECO:0000313|EMBL:KMU88978.1};
OS Coccidioides immitis H538.4.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=396776 {ECO:0000313|EMBL:KMU88978.1, ECO:0000313|Proteomes:UP000054563};
RN [1] {ECO:0000313|Proteomes:UP000054563}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H538.4 {ECO:0000313|Proteomes:UP000054563};
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
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DR EMBL; DS017009; KMU88978.1; -; Genomic_DNA.
DR STRING; 396776.A0A0J8UN37; -.
DR VEuPathDB; FungiDB:CIHG_06779; -.
DR eggNOG; KOG0519; Eukaryota.
DR Proteomes; UP000054563; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 5.
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; 1.20.120.1530; -; 3.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003660; HAMP_dom.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF18947; HAMP_2; 4.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 6.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
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; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 2.
DR PROSITE; PS50885; HAMP; 6.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KMU88978.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000054563};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 189..244
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 284..336
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 376..428
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 468..520
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 560..612
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 652..704
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 726..951
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1104..1223
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 29..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 75..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1233..1285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 141..197
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 29..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..123
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1263..1285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1153
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1285 AA; 141230 MW; 32BAB3976412C04E CRC64;
MASSDETLAA AAAIIQGLAK DVPESISLPF NGRKQTQPTN GIDSVKVKLP GEDSEGKVAL
ERELSALVRR VNTMQTFVPP SRRSGRTSSL MSARSLKNGQ NNESSVDNSD EVNDEDSDSE
DNYEDNISYL RNRVQLQAEQ IQLQKDIISQ VREELRHQEE RTQQALVKVE HEDVRVLERE
LKKHQQANEA FQKALREIGG IITQVANGDL SMKVQIHQLE MDPEITSFKR TINTMMDQLQ
VFGSEVSRVA REVGTEGILG GQVQITGVHG IWKELTDNVN FMASNLTNQV REIATVTTAV
AHGDLSQKIK SWGQGEILEL QQTINTMVDQ LRTFATEVTR VARDVGTEGV LGGQAQIDGV
QGMWNELTVN VNAMAENLST QVRDIATVTA AVAKGDLTQK VKANCKGEIL AMKTIINSMV
DQLKQFAQEV TKIAKEVGTD GVLGGQATVH DVEGTWKDLT ENVNGMAMNL TTQVREIADV
TTAVARGDLT KKVTSDVKGE FSDLKNTINS MVDRLNTFAF EVSKVAREVG IDGILGGQAK
VDNVEGKWKD LTDNVNTMAQ NLTIQVRAIS DVTQAIAKGD LSRKIEVHAQ GEILTLKDTI
NNMVDRLANF AHELKRVARD VGVDGKMGGQ ANVEGISGRW KEITEDVNTM ADNLTAQVRA
FGEITDAATD GDFTKLITVN ASGEMDELKR KINKMVSNLR DSIQRNTQAR EAAELANRTK
SEFLANMSHE IRTPMNGIIG MTQLTLDTDD LKPYPREMLN VVHSLANSLL TIIDDILDIS
KIEANRMVIE SIPFTMRGTV FNALKTLAVK ANEKFLNLTY QVDSSVPDYV IGDPFRLRQI
ILNLVGNAIK FTEHGEVKLT ISKSTRELCQ DEEYAFEFSV SDTGIGIEED KLDMIFDTFQ
QADGSTTRKF GGTGLGLSIS KRLVNLMGGD VWVTSEFGHG STFHFTCKVN LADQSLDVIL
PQLLPYQNHH VLFIDKGETG DDALSITRML RQLGLEPLVV RSETNVPPPE IQDSSGKESG
HAYDVIIVDS VETARTLRTF GEFKYIPIVL LCPVVSVSLK SALDLGITSY MTTPCRPIDL
GNGMLPALEG RSTPLTTDNT RSFDILLAED NDVNQKVAVK ILEKCNHGVT VVSNGLAAVE
AVKQHRYDVI LMDVQMPIMG GFEATGKIRE WEKENGLQRT PIIALTAHAM LGDREKCLQA
QMDEYLAKPL KQNQMMQTIL KCATLGSPLF EKGKDSRFGG HHSSSTLAGA SSPEAKHQRP
SLESRALTAT NRTSVPEPIL RSNSS
//
