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Database: UniProt
Entry: C9SHQ5_VERA1
LinkDB: C9SHQ5_VERA1
Original site: C9SHQ5_VERA1 
ID   C9SHQ5_VERA1            Unreviewed;      1100 AA.
AC   C9SHQ5;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=VDBG_04587 {ECO:0000313|EMBL:EEY18478.1};
OS   Verticillium alfalfae (strain VaMs.102 / ATCC MYA-4576 / FGSC 10136)
OS   (Verticillium wilt of alfalfa) (Verticillium albo-atrum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=526221 {ECO:0000313|Proteomes:UP000008698};
RN   [1] {ECO:0000313|Proteomes:UP000008698}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VaMs.102 / ATCC MYA-4576 / FGSC 10136
RC   {ECO:0000313|Proteomes:UP000008698};
RX   PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA   Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA   Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA   Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA   Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA   Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA   Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT   "Comparative genomics yields insights into niche adaptation of plant
RT   vascular wilt pathogens.";
RL   PLoS Pathog. 7:E1002137-E1002137(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};
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DR   EMBL; DS985218; EEY18478.1; -; Genomic_DNA.
DR   RefSeq; XP_003004981.1; XM_003004935.1.
DR   AlphaFoldDB; C9SHQ5; -.
DR   SMR; C9SHQ5; -.
DR   STRING; 526221.C9SHQ5; -.
DR   GeneID; 9530196; -.
DR   KEGG; val:VDBG_04587; -.
DR   eggNOG; KOG0519; Eukaryota.
DR   HOGENOM; CLU_000445_3_2_1; -.
DR   OMA; CLAAQMD; -.
DR   OrthoDB; 1222064at2759; -.
DR   Proteomes; UP000008698; 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; -; 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; 2.
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; 4.
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; 4.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EEY18478.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000008698};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          190..245
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          297..349
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          389..441
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          484..536
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          558..753
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          903..1022
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   REGION          67..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1031..1100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        109..123
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1031..1053
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         952
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1100 AA;  121132 MW;  31C8881954DAF62F CRC64;
     MVDDSALAAA AAIVQSFAAD GSTPMSLPFR KDTTRIELPG RDTPAKRSLE LELAKLAQRI
     DKLENRAHSA PTAFPETPNE VNDSLFGDDP TGTFPSLGGR VVSRPPLQRE GTQADSGSAG
     SPLTDEALES LQEKVLDQEK GISSAREEIT SVSAQLLEQK ELQEQAFSRI EQDRVARLER
     ELWKHQKANE AFQKALREIG EIVTAVARGD LSKKVRMNSV EMDPEITTFK RTINTMMDQL
     QVFSSEVSRV AREVGTEGLL GGQARIEGVD GTWKELTDNG VKGMWNELTV NVNAMANNLT
     TQVRDIIEVT TAVAKGDLTQ KVQADCRGEI FELKSTINSM VDQLQQFARE VTKIAREVGT
     EGRLGGQATV HDVEGTWKDL TENVNGMAMN LTTQVREIAR ITTAVAKGDL TKKIGVPAQG
     EILDLKNTIN TMVDRLGTFA FEVSKVAREV GTDGTLGGQA QVNNVEGKWK DLTENVNTMA
     SNLTLQTTQV RAFSDITNLA TDGDFTKLVE VEASGEMDEL KRKINQMVSN LRDSIQRNTQ
     AREAAELANK TKSEFLANMS HEIRTPMNGI IGMTQLTLDT DLTQYQREML NIVNSLANSL
     LTIIDDILDL SKIEARRMVI EEIPYTLRGT VFNALKTLAI ILNLVGNAIK FTEHGEVSLT
     IKKADELKFP CGPNQYAIEF VVTDTGIGIA ADKLDLIFDT FQQADGSMTR KFGGTGLGLS
     ISKRLVKLMG GDLWVKSNHG KGSAFHFTCK VRLCDVGFES IEKQIKPYKG HQVLFVDKTQ
     TAYGMEIRDM LGAIGLIPVV VDSEKSPSLD RVRGMAAASM PYDVIIVDSI DTARRLRSVD
     DFKYLPIVLL APIVNVRMKA CLDLGITSYM TTPCKAVDLG NGMIPALENR ATPSLADNTK
     SFEILLAEDN RVNQRLAVKI LEKYHHVVTV VGNGHEAVEA IKRKRFDVIL MDVQMPIMGG
     FEATGKIRDY EREAGSHRTP IIALTAHAMM GDREKCIQAQ MDEYLSKPLQ QNHLIQTILK
     CATLGGQLLE KNRERDQPHK KEDADKKTDD SGSSLRPSLE TRAFTSRDPL VGQGLDSPAL
     VTADQEDPIS RFHSMRSHST
//
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