ID A0A0G2ETG7_9PEZI Unreviewed; 927 AA.
AC A0A0G2ETG7;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Putative histidine kinase hhk6p {ECO:0000313|EMBL:KKY26027.1};
GN ORFNames=UCDDS831_g01537 {ECO:0000313|EMBL:KKY26027.1};
OS Diplodia seriata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Diplodia.
OX NCBI_TaxID=420778 {ECO:0000313|EMBL:KKY26027.1, ECO:0000313|Proteomes:UP000034182};
RN [1] {ECO:0000313|EMBL:KKY26027.1, ECO:0000313|Proteomes:UP000034182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS831 {ECO:0000313|EMBL:KKY26027.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKY26027.1, ECO:0000313|Proteomes:UP000034182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS831 {ECO:0000313|EMBL:KKY26027.1};
RA Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT "Distinctive expansion of gene families associated with plant cell wall
RT degradation and secondary metabolism in the genomes of grapevine trunk
RT pathogens.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKY26027.1}.
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DR EMBL; LAQI01000033; KKY26027.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2ETG7; -.
DR Proteomes; UP000034182; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00091; PAS; 2.
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; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:KKY26027.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:KKY26027.1}.
FT DOMAIN 208..278
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 281..333
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 411..471
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 499..722
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 810..927
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 865
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 927 AA; 104029 MW; B4894DADC3795B60 CRC64;
MHRSAPPLHL AAGASNGQPI RDAAEPQYAA QKTQMPLPVN DLSEPASYFD LHDRDPPSPG
SARSEQLSII MPPTPTTTAM ALATLQYLPV PVLVLSSLKT VVLANEAMGR LLEVDRPAGD
EKDRDDVHTV TDTLHGQTML DLGIEMLQDG SPIRISWEDF LDSVWKQAQG EAEGNVGGPS
EMVDESDQMV FKDVTEYTKR IAEQIEENEK QFEYITNLIP IMVWTTKPNG DHDWFSKRWY
DYTGLTEEES LGKGWKLPFH EDDMPETSKR WQHSLKTGEE YNTEYRCRRY DGQWRWMLGR
AVPFRDDLGK VIKWFGTCTD IHELVELRET AKQMRAQLLR VLEHARVTLW AVNRDRKIVL
LEGSLLNDSF SHVTREKIGT DMYDLFSRDE AGRKTISELE GSVDRILDGK DSTEVVEMQF
DGNNRWYRTR IAPLMVTSRQ AGIEKESYID GVYGVSMDIT ELRKRREELQ AREEENSKLI
ANAVAAKEAS RMKSQFLANM SHEIRTPIAG VIGMSELLLD TKLDQEQKDC AENIQRSANG
LLTVINDILD LSKVESGRLD VEEVQFSLLV VLRDVNKMMA FAALRKNISY ESNIPPEIER
DLKVMGDPGR LRQILTNLLT NSIKFTSEGH VSLSVSINSE NDETINVHFV VEDTGIGIEE
EVRQRLFKPF SQADSSTARR FGGTGLGLAI SKNLVDLMHG NIDLQSTLGQ GTRASFSIPF
NKAQYQDEGS PLIDLASIPD RLQSDISVSC GSSEDYGTPP LTPVVPNSGK SPLRHGRAQS
IVSLPGNGNF HHALPDHLFS LAETERKNVH VLVVEDNQVN QQIALKTIRK QGFAVDAVWN
GKEALEYLVD AKDGKRDRPD IILMDVQMPI MDGYKATHTI RTQAPFKDTP SIRNIPIVAM
TASAIQGDKE KCQKAGMDDY LSKPCYA
//
