ID A0A0D2CKW0_9EURO Unreviewed; 1341 AA.
AC A0A0D2CKW0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=PV07_02418 {ECO:0000313|EMBL:KIW30710.1};
OS Cladophialophora immunda.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=569365 {ECO:0000313|EMBL:KIW30710.1, ECO:0000313|Proteomes:UP000054466};
RN [1] {ECO:0000313|EMBL:KIW30710.1, ECO:0000313|Proteomes:UP000054466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 83496 {ECO:0000313|EMBL:KIW30710.1,
RC ECO:0000313|Proteomes:UP000054466};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Cladophialophora immunda CBS83496.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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; KN847041; KIW30710.1; -; Genomic_DNA.
DR RefSeq; XP_016250926.1; XM_016389024.1.
DR GeneID; 27341612; -.
DR VEuPathDB; FungiDB:PV07_02418; -.
DR HOGENOM; CLU_000445_3_1_1; -.
DR OrthoDB; 1222064at2759; -.
DR Proteomes; UP000054466; 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; 4.
DR Pfam; PF18947; HAMP_2; 1.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
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};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000054466};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 209..264
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 304..356
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 396..448
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 488..540
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 580..632
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 672..724
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 746..973
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1127..1246
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 22..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 73..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1256..1341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 187..217
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 698..725
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1294..1312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1176
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1341 AA; 146377 MW; E5D7120F86AC9979 CRC64;
MSRPDETLAA AAAILRGLAK GSTSSTYTNG LKLPPYKLPG EDTPGKEDFE AEIAALARRI
HYLESRADVV GRSLPDTPGE FQSPASPLSR PVEPRGSLGD PGADFAADSA ERTPTNSNHS
RRVNNLLAAR DSFRPSEPDR AVSEDDISIL REHVERQAEQ IKSQRDTIAE ISRGLRNSEE
QAKQAFMRVE NEDVSILERE LRKHQQANEA FQKALREIGG IITQVANGDL SKRVQIQATE
MDDEIAAFKV TINTMMDQLE IFGSEVTRVA REVGTEGILG GQAQISGVHG IWKELTDNVN
IMAANLTDQV REIATVTKAV ARGDLSQKVQ SRAKGEIFEL QHTINTMVDQ LRTFATEVTR
VATDVGTEGV LGGQAQIEGV QGTWNELTKS VNAMADNLTT QVRDIAMVTT AVAKGDLTRK
VTASCKGEIL RLKITINNMV DQLQQFAQEV TILAKEVGTN GVLGGQATVH DVEGTWKDLT
ENVNGMAMNL TTQVREIAAV TTAVANGDLS KKVTADVQGE ILDLKVTINS MVDRLNTFAF
EVSKVAREVG TDGTLGGQAK VDNVQGKWRD LTDNVNTMAS NLTDQVRSIS DVTQAIAAGN
LDKKIEVQAQ GEILTLKVTI NNMVDRLATF AHEVRRVARD VGVNGKMGGQ ANVHDVSGRW
KEITEDVNTM AENLTAQVRA FGEITDAATE GDFSKLISVN ASGEMDELKR KINQMISNLR
DSIQRNTAAR EAAELANRTK SEFLANMSHE IRTPMNGIIG MTQLTLDTDD LKPHSREMLN
TVHNLANSLL TIIDDILDIS KIEANRMAIE AIPYTIRGTV FNALKSLAVK ANEKSLCLAF
DVDNSVPDYV VGDPFRLRQI ILNLVGNAIK FTDQGEVKVT IKKSKDLLSN CAPDEFPFEF
VVSDTGIGIQ SDKLDLIFDT FQQADGSTTR KFGGTGLGLS ISKRLVNLMG GQVWVTSDFG
HGSEFHFSCI VKFATDDISV ISSQLYPFRK HKVLLVDKGV SKFFERVPAM IEELGLQVKV
VNDETEVPDP VTVTVERNRK GTDGGYDVIV IDELQTAQKL RELDKFKYIP MVLLNATVSI
SLKTVLDLGI ASYMTTPCQL IDLGNCMIPA LEGRSTPVIK DYKKSLNVLL AEDNEVNQKV
AIKILEKYNH VVTVVGNGLE AVNAIKHNRF DIVLMDVQMP VMGGFEATRE IRQYEKEKAL
PRTPIVALTA HAMLGDREKC IQAQMDEYLS KPLKQNLLMQ TILRVASDRV TDIFNKQARS
KSNGARNGHG GGMDGKEASS PANAGDTRVI SSLRPPFSER SVTSSGPVNH GSVESPSLGK
DGEPDPISAA NSSVRSMSWS G
//
