ID A0A0D2E625_9EURO Unreviewed; 1342 AA.
AC A0A0D2E625;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=PV04_02128 {ECO:0000313|EMBL:KIW69797.1};
OS Phialophora macrospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX NCBI_TaxID=1851006 {ECO:0000313|EMBL:KIW69797.1, ECO:0000313|Proteomes:UP000054266};
RN [1] {ECO:0000313|EMBL:KIW69797.1, ECO:0000313|Proteomes:UP000054266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 27337 {ECO:0000313|EMBL:KIW69797.1,
RC ECO:0000313|Proteomes:UP000054266};
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 Capronia semiimmersa CBS27337.";
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; KN846957; KIW69797.1; -; Genomic_DNA.
DR STRING; 5601.A0A0D2E625; -.
DR OrthoDB; 1222064at2759; -.
DR Proteomes; UP000054266; 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; -; 4.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 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; 3.
DR Pfam; PF18947; HAMP_2; 2.
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; 2.
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}; 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 1126..1245
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 71..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1257..1342
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 102..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1292..1313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1175
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1342 AA; 146138 MW; A977D98355A399A9 CRC64;
MSRPDETLAA AAAILRGLAK GSTTSAYANG LKLPPYKLPG DDTASKEDLE AEIVALARRI
HYLESRADVL GRSLPDTPGE FQSPTSPLGH PAEPRVSLGD ASTDLSADSS ERAASNGTQS
KRVNNLLAAR HSLRPSASDR TVSEDDISIL 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 QVRDIAGVTT AVAKGDLTQK
VTASCKGEIL QLKITINDMV DQLQQFAQEV TILAKEVGTN GVLGGQATVH DVEGTWKDLT
ENVNGMAMNL TTQVREIATV TTAVANGDLS KKVTANVQGE ILDLKITINA MVDRLNTFAF
EVSKVAREVG TDGTLGGQAK VDNVQGKWRD LTDNVNTMAS NLTNQVRSIS DVTQAIAAGN
LDKKIEVPAH GEILTLKVTI NNMVDRLATF AHELRRVARD VGVNGKMGGQ ANVHDVSGRW
KEITEDVNTM AENLTAQVRA FGEITDAATE GDFSKLISVN ASGEMDELKR KINQMISNLR
DSIQRNTAAR EAAELANQTK SEFLANMSHE IRTPMNGIIG MTQLTLDTDD LKPHSREMLN
TVHNLANSLL TIIDDILDIS KIEANRMAIE AIPYTVRGTV FNALKSLAVK ANEKTLCLAF
DVDNSVPDYV VGDPFRLRQI ILNLVGNAIK FTDQGEVKVT IKKSRDLISN CAPDEFPFEF
VVSDTGIGIQ SDKLDLIFDT FQQADGSTTR KFGGTGLGLS ISKRLVNLMG GQVWVTSDFG
HGSEFHFSCI VKYATDDISV ISSQLYPFRK HRVLVVDKGV SKFFERVPAM IEELGLHVQV
VRSEIEVPDP VAAVDRKGRT SDGGYDVIVI DELETAQRLR ELDKFKYIPM VLLNPTVSIS
LKTVLDLGIA SYMTTPCQLI DLGNCLIPAL EGRSTPIIKD YKKSLNVLLA EDNEVNQKVA
IKILEKYNHV VTVVGNGLEA VNAIKNSRFD IVLMDVQMPV MGGFEATREI RQYEKEHGLP
RTPIVALTAH AMLGDREKCI QAQMDEYLSK PLKQNLLMQT ILRVASDRVT DIFHEHARSK
ANGTGNGNDG AAEDRPSALP PKPAGASKDS NSGLRPPFSE RSITTSGSVI HGSVESPSVG
RDGEPDPMSV ANSSVRSMSW SG
//
