ID Q0UYI0_PHANO Unreviewed; 2299 AA.
AC Q0UYI0;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 2.
DT 27-MAR-2024, entry version 104.
DE RecName: Full=Histidine kinase HHK1p {ECO:0008006|Google:ProtNLM};
GN ORFNames=SNOG_03184 {ECO:0000313|EMBL:EAT89915.2};
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614 {ECO:0000313|EMBL:EAT89915.2, ECO:0000313|Proteomes:UP000001055};
RN [1] {ECO:0000313|Proteomes:UP000001055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173
RC {ECO:0000313|Proteomes:UP000001055};
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G., Solomon P.S., Tan K.C., Schoch C.L., Spatafora J.W.,
RA Crous P.W., Kodira C., Birren B.W., Galagan J.E., Torriani S.F.,
RA McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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DR EMBL; CH445328; EAT89915.2; -; Genomic_DNA.
DR RefSeq; XP_001793763.1; XM_001793711.1.
DR EnsemblFungi; SNOT_03184; SNOT_03184; SNOG_03184.
DR GeneID; 5970620; -.
DR KEGG; pno:SNOG_03184; -.
DR VEuPathDB; FungiDB:JI435_031840; -.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_001037_0_0_1; -.
DR InParanoid; Q0UYI0; -.
DR OrthoDB; 1222064at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0009927; F:histidine phosphotransfer kinase activity; IBA:GO_Central.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IBA:GO_Central.
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; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR041664; AAA_16.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43047:SF46; HISTIDINE KINASE_RESPONSE REGULATOR, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G12550)-RELATED; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF13191; AAA_16; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
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; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000001055};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 40..428
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1824..2049
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 2097..2220
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 56..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2242..2299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2250..2276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2151
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 2299 AA; 256610 MW; 3ADCF9D86D8AC49A CRC64;
MAPGDTETGR AARFSHIFAR LIELHNYVWD PKIEPFHSSY DNWHFFGYEK TSSAERPSSR
SALTSPTPFS SHSPDSSRPG LTRSHRSSGS DTSAITHNHG AEILQGRPVV CRVSTHTLRL
EREFQLSKLV VKKSDPECRH FVRPIEFVRL PTKAGEEPLV ASIFEAPGPN FLKDLVTFGP
NWYRFTGAEN NWRSSTPQPD AGVPLLTFLD FAIGATECLE ILHHGHEIVH GELRGDAFHF
ASDGTVKMIN FGSGARSFEN GLTSAGWNSL SREVGIELKL AFVAPEQTGR MPAEPDSRTD
IYSLGILFYA MLCGTTPFDG TTALDVMQSD SGGLKSFEVG TKDISCFFNL PLKLIAREKE
RQIIINVIER AAKRRRGGLK NFNSLSLSST SSYSDQRLEI LDDVLSDSNS SRGSESRLNS
ISSAAPVFMD SARSIHQRSQ DSVATEKSLS DETPVRPPLQ QSSRGPSNNS VEGNMSHSRS
YQTASATESS LLRTVSNTRK FRHKARCEVV AISGATGLGK SRLVQSIQST ARRSGYFATA
KFDTNRRAPF EPILRLMSSL FRQIFSEADV STDFHNSLRG FLKNTGVWTV LRTYLDLPDW
LLNTGASKSQ KVVETSRVTE RDRRASSPAI HCGSSGHTAE AWLRSGGASK SSKFMNVFID
VLRLLAVQKL CIWNLDDVHN ADQESAELIH HIIQAKIPLV FMLTFTDENV LPRELRSLLP
NATRVQLSTF TEAQTAEYVA ETLHRDKDYI LPLVAVVQEK SHGNFYRKKC VYYSWRENNW
MFDLDKVFEV FESPEYGSSV TNDFIAKRLL ELPPSTRKLV AWASLLGGSF SFDMVKQLMN
PKYAPADAKR IPLLEGKESA IEALNLALAA YVLMPGENDS RFRFSHDRYL TAASSSLDQE
WDVQMMHYLI AKMATSGVVY HDELILGSKA LYMRSRHICL AADLIKSRET KRAPFRDVLY
QAGEAACESG ARSTGIYYFA HCLVLLQDHP WDDTQPDVSY QETLQLFVRS AECYWHQSML
DEALSLIRTT FKFARNPVDL ASSFILQSRV FAVRGDSFGA FQALKDCLSL LGCPIERTTW
EACDDEFQKI YAKMQEVDKE ELLARRLSAD NRILLTMGPI FVELLSAAFW SNSLLFYQAT
LKLINTHLEG GSISQVALAY VHLGTIAAGR FQMMNFAVDM GAMAKRLFQM YPDDNYTVGR
TQTLLPLFLG HLETPVRDLI PDLEAALEVT LSAGDRILTL LNLGVQAHFR VMASQDVTEV
EASIEETPLD TKNWQRDMRG GTFLMGSRQY CRALQGKTGV QKASLIFTDD EHSSAEYVKY
LEETASNPKR PKSIYLAMKM PVLTLYGYVA EAVELGELLL PMLSSLWCER LNYSVRYHLS
LCYMATLRDD PKNARKEEMT KFVQDTIQLL EACSTVTDVN YRGWIHLLLA VLAEVQRDPP
SALQNYEAAM DHGEENEFVL DLAFAHELYG EWLVRKKAYR AARHSFKDCM STYRRISAHG
KANHVATKYD WLLCDKSSVM TVSNGTQTTV IDTGNTTLRL EQNEDQEQYL AAETAVDRTQ
NWIVPETGRR HESSQDLHNG FTAVGLDMLD LSSILESSQV LSKELKVDKL MAKMAAIILE
STGGSLCGIV IEDSQIEWSI ACIATNEPNS ETGFAPGVRS YPTGQPLDTV DDVVARQVTL
YTLRFRETVF VQNLLEDDRF SNVSGSYLAR NPEGKAVICI PIVHSDHLLG SIYVEGPPNS
FTERNTQVLR LLVNQISISL ANALLFKEIE RVSASNEAML EMQKRALAQA RAAEIKAKEA
EAIAIRNMKL KEEAAKAKSL FLANVSHELR TPLNGVIGMS ELLKASILNS EQTGYADSIR
VCADTLLSII NDLLDYSKLE AGKMSVMEMP LSLTETITEV VRALAYTNAE RGLKTVEQLE
LNPEMMVMGD PVRLHQILMN LLSNSYKFTP KGSVTVRAVI DQETDEYADV TISVIDTGIG
IPAEQKKKLF LPFSQIESSS SRSYGGTGLG LSICKALIEN VMHGKVWLDS RDSGPDRGTT
VSFSLRFRKV AKTSVLDRRN TRETDLMAKF SSQDNNGHEA QSGACIDLST IPRNELRVCI
AEDNLINQRI AISFVQKLGF RCDAYLDGLK TIDALERASD NGRPFHLVLM DVQMPHCDGY
EATKRIRKHP NPDIRNILII AMTASAIQGD REKCLESGMN NYLAKPVRAQ TLKALLESYL
NKDQEKEIPN LEAEAQKLVK QALNETGSSD KDSGMKKSQD ALLDGETGEK KMMRNRPSSV
RSVTQRWLGP SGKDGAAPN
//
