ID G4TQ41_SERID Unreviewed; 1417 AA.
AC G4TQ41;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=PIIN_07388 {ECO:0000313|EMBL:CCA73434.1};
OS Serendipita indica (strain DSM 11827) (Root endophyte fungus)
OS (Piriformospora indica).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Sebacinales; Serendipitaceae; Serendipita.
OX NCBI_TaxID=1109443 {ECO:0000313|EMBL:CCA73434.1, ECO:0000313|Proteomes:UP000007148};
RN [1] {ECO:0000313|EMBL:CCA73434.1, ECO:0000313|Proteomes:UP000007148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11827 {ECO:0000313|EMBL:CCA73434.1,
RC ECO:0000313|Proteomes:UP000007148};
RX PubMed=22022265; DOI=10.1371/journal.ppat.1002290;
RA Zuccaro A., Lahrmann U., Guldener U., Langen G., Pfiffi S., Biedenkopf D.,
RA Wong P., Samans B., Grimm C., Basiewicz M., Murat C., Martin F.,
RA Kogel K.H.;
RT "Endophytic Life Strategies Decoded by Genome and Transcriptome Analyses of
RT the Mutualistic Root Symbiont Piriformospora indica.";
RL PLoS Pathog. 7:e1002290-e1002290(2011).
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};
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:CCA73434.1}.
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DR EMBL; CAFZ01000225; CCA73434.1; -; Genomic_DNA.
DR STRING; 1109443.G4TQ41; -.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_000445_3_0_1; -.
DR InParanoid; G4TQ41; -.
DR OMA; CLAAQMD; -.
DR OrthoDB; 1222064at2759; -.
DR Proteomes; UP000007148; 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; 4.
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; 5.
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; 7.
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; 2.
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; 7.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000007148};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 286..339
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 379..431
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 471..523
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 563..615
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 655..707
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 747..800
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 840..892
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 914..1140
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1284..1409
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 62..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1339
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1417 AA; 153021 MW; F6C416134EC4F2B0 CRC64;
MSADIMALAP QGLDHQALAS PLMSSAMLDD HPFLSHLVAL LSVYELPPTM HTLPPAATSS
NEQATQTVST NHLNSSTAPV GRTPGIPTPR YDGPRTAQTD AIERSVNLIA SRMRSAEETL
GWTHPWLAPP LMDQYMKSVQ ASEDDTTPTT TASTASTNSA VNEPSQEINP FTVALQAPTP
VSVISPTSKQ SRAPSPMQIS LQGINNNARN QPPQGGIQSP TTEHRSPHSP YPCPMCRRPL
ARGISASTSS AHTILPSPNG SPLVVPPGPL STAAFESGLS AVEELRLLKA QVQDVARVCK
AVADGDLTQK IEVGVQGPVM VQLKDVINTM VDKLGQFAQE VTRVSLEVGT EGILGGQAHV
TGVEGTWQEL TDVVNRLAAN LSTQVRSIAI VTTAVARGDL SQMIEVDAKG EILALKNTVN
SMVLRLRNLA AEVTRVTLEV GSQGKLGGSA QVNDVEGVWL DLTTNVNRMC YNLTNQVRSI
AEVTTAVAKG DLRKSVEIEV EGELATLKDT VNSMVSQLRT FAAEVTRVAL EVGTEGILGG
QATVEGVQGV WADLTTNVNN MARNLTNQVR SIAEVTTAVA DGDLSKKVMV DVRGEMLDLK
NTVNSMVTRL HILANEVTRV SLEVGTEGIL GGQAKVPGVE GMWKVLTDNV NLMASNLTTQ
VRSIAAVTTA VARGDLTKKI TVDVKGEILA LKETVNSMTE SLSVFAAEVT RVAKEVGTDG
ILGGQASVEN VAGTWKDLTD NVNTMASNLT QQVRAIALST RAVAAGDLTR KVEGLQVSGE
MLDLVNTINT MIFQLGIFAA EVTRVAREVG TEGKLGVQAE VANLRGTWQS ITMSVNTMAA
NLTSQVRGFA QISAAATDGD FTRFITVEAS GEMDSLKTQI NQMVFNLRES IQKNTAARKA
AELANRSKSE FLANMSHEIR TPMNGIIGMT ELTLDSDLTR SQRESLLLVH SLARSLLLII
DDILDISKIE AGRMTMEQVS YSVRHTVFGI LKTLVVRASQ NNLDLTYDMD PDIPDQLIGD
SLRLRQVITN LLGNAIKFSP SKHHCKGHVS LSCRLIAIDE TCVTLEFCVS DTGIGIAKDK
LNLIFDTFCQ ADGSTTREYG GTGLGLSISK RLVSLMQGNM WVESELGRGS KFFFTVTSQL
SDSPMEQILL KVQPYTGRHV LFVDTLGDMT NVSEQITKLG LVPYVVHDVQ KLLERSRLPH
IDTILVDSLH VTEVLREMEH LRYIPVVLIA PSIPRLNLKW CLDNSISSHL TTPVSLPDLA
AALVAALEAN SVNPPVTSTD TSFDILLAED NLVNQRLAVR ILEKYGHTVE IAENGSVALN
KFKERWQRAG NRFDVILMDV SMPFMGGMEA TELIRAYEAE HHLERTPIIA LTAHAMIGDR
ERCLQAGMDD HITKPLRRAD LLNAITKQVG HKDARVS
//
