ID A0A074W5V8_9PEZI Unreviewed; 1312 AA.
AC A0A074W5V8;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-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=M436DRAFT_86387 {ECO:0000313|EMBL:KEQ68505.1};
OS Aureobasidium namibiae CBS 147.97.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043004 {ECO:0000313|EMBL:KEQ68505.1, ECO:0000313|Proteomes:UP000027730};
RN [1] {ECO:0000313|EMBL:KEQ68505.1, ECO:0000313|Proteomes:UP000027730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 147.97 {ECO:0000313|EMBL:KEQ68505.1,
RC ECO:0000313|Proteomes:UP000027730};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
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; KL584729; KEQ68505.1; -; Genomic_DNA.
DR RefSeq; XP_013422693.1; XM_013567239.1.
DR STRING; 1043004.A0A074W5V8; -.
DR GeneID; 25417707; -.
DR HOGENOM; CLU_000445_3_1_1; -.
DR OrthoDB; 1222064at2759; -.
DR Proteomes; UP000027730; 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 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; 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 Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000027730};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 203..258
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 298..350
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 390..442
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 482..534
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 574..626
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 666..718
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 740..964
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1112..1231
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1241..1312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1253..1269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1280..1294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1161
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1312 AA; 143546 MW; B85901D692C2A782 CRC64;
MAEEDSYAAL AAIISNLGKQ YTPAHDDFNS RVAANSVESN RTPLPGADSD AKQQLEREVA
ALASRVQYLE NRVASSASTV YPITPNEPLQ SAFSTDSSPT AARVLSSRPR SASLVNSLLA
KSESPKGTAV PRQLTEEELG VLRDHVDRQS EEIKAQREYI DSINETLQQQ RQATEQALGG
IESSMDDVET LKRELSKNQQ INATYQKVLR EIGSIVTAVA NGDLSKKVLI SAKERDPEIA
TFKRTINKMV DQLQDFASQV THLAREVGTE GRLGGQAVLP GVSGIWAELT QNVNIMADNL
TNQVREIAVV TTAVAQGDLS RKIQRPARGE ILQLQQTING MVDQLRTFAT EVTRVSRDVG
TEGVLGGQAQ IEGVQGMWND LTVNVNAMAN NLTTQVRDIA EVTTAVARGD LTQKVKAECK
GEILELKSTI NSMVDQLRQF AHEVTKIARE VGTEGRLGGQ ATVHGVEGTW KDLTENVNGM
ANNLTTQVRE IAHVTKAVAR GDLSKKVGAE VKGEILELKV TINTMVDRLS TFAFEVSKVA
REVGTEGVLG GQAQVENVEG KWKDLTDNVN TMANNLTNQV RNISDVTQAI ARGDMTQVIK
VHAQGEILLL KNTINDMVGR LDNWSLAVKR VARDVGVDGK MGGQAEVEGI SGRWKEITSD
VNTMAQNLTS QVRAFGDITN AAMDGDFTKM ITVEASGEMN ELKNKINKMV TGLRESIQKN
TAAREAAELA NKTKSEFLAN MSHEIRTPMN GIIGMTQLTL DTDLNQNQRE MLNLVFNLAN
SLLTIIDDIL DISKIEANRM VVEEIPFSLR GQVFNGLKGL AVKANEKHLD LAYYVDSSVP
DYVIGDSFRL RQIILNLVGN AIKFTDKGEV RISISAADQL GCEDGEYAVQ FAVRDTGIGI
PSNKLDLIFD TFQQADGSTT RRFGGTGLGL SISRRLVSLM NGRMWVESDF GQGSCFYFTV
KFKVGDPDVA AIDKQLRAYR KHHVLFIDTG KTGCSEEIAQ HLVNLQLMPM VVHTEAEVPS
PQAAIAAGKA YDCILVDSRE TARKLRNVED FKYIPIVMLA PVISMSFKSA LEDGIASYMT
TPCLSIDLGN ALIPALEGRA APTSADPSMK FDILLAEDNA VNQRLAVRIL QKHHHTVTVA
NNGLEAFEAI KKKRYDVVLM DVQMPIMGGF EATANIRQYE RENQLTRSPI IALTAHAMLG
DREKCIQAQM DEYLSKPLKP NQLIQTLLKC ATMGGALLER NKDQRMTLTQ GDDGKQEDST
GSSSKVSTPR RPILDIRGYT DSPTNPTKSP SIVTADLSDP IEREMLMRSN SS
//
