ID A0A074WV36_9PEZI Unreviewed; 1329 AA.
AC A0A074WV36;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Histidine kinase HHK6p {ECO:0008006|Google:ProtNLM};
GN ORFNames=M436DRAFT_38017 {ECO:0000313|EMBL:KEQ77038.1};
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:KEQ77038.1, ECO:0000313|Proteomes:UP000027730};
RN [1] {ECO:0000313|EMBL:KEQ77038.1, ECO:0000313|Proteomes:UP000027730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 147.97 {ECO:0000313|EMBL:KEQ77038.1,
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).
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DR EMBL; KL584703; KEQ77038.1; -; Genomic_DNA.
DR RefSeq; XP_013430740.1; XM_013575286.1.
DR STRING; 1043004.A0A074WV36; -.
DR GeneID; 25408944; -.
DR HOGENOM; CLU_000445_114_5_1; -.
DR OrthoDB; 1222064at2759; -.
DR Proteomes; UP000027730; 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; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 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; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000027730}.
FT DOMAIN 494..546
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 715..939
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1012..1140
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 103..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 965..998
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1152..1192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1279..1329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1173..1187
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1288..1313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1067
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1329 AA; 147578 MW; 2DE66465153D1697 CRC64;
MTDTALTALQ YLPMPVLVLS SEKTIVLANE AMGRLLGIDL QQSPAVPDSA GINEHEDLRS
ASDVLGGVAM DNLGMDLLQN ANPVWMRWED FLNTIKQDAI DASAQSEAKS DGGDITPTAE
SYDGSAVRPS PVPLTRANLA RTTVHDAAVD VVFSTNRNPT TGLPRTKEVN HDASGHIQAT
VIITVWSADD VDYYTLMFTS AAETQSSSSR SSHRTVARTH TTFSSGLGSG SSSSSSGRRT
QHQHRTSLSG SPSVFAPQAL PSGPPSLTTS AAAPSLFSKS NRLKDALLNS LSDPAFAMWK
DESFGIPNKA AIRMVDPDSE EGITGVRDQR DFLQKYVLWK EDFSELLPMS EFPIMHLMTT
EKRFSGRRLG MHHPKTGAKI IYDVDGETIT DSKTGEFLGG LVIFHNVTEY ANTITAQKAQ
NERQFEDITN MIPQMIWTTT PTGQHDYYSR RWYEYTGMTV EASLGNGWEN PFHPDDMELT
GKRWAHSLAT GEEYRTEYRC LSSDGEWRWM LGRAVPMKDD TGKIVKWFGT CTDIHELVLA
REDARQTKLR LSQVIEMAKI TLWSVNPERN LSMLEGAIVW NDNSKSSDEE IRRKAIGKNV
FELFDKDAIL DGDHHREYIE NILTGKQIDE TTELHLKETN RWVRTRFVPL QRMERNAGVE
GGTFVDGVVA VSMDVTDLRK REEQLRERDR ENSRLLAQSE AAKEASKMKS QFLANMSHEI
RTPIAGVIGM SELLLDDTES TLTEEQRECA ENLQRSANGL LTVINDILDF SKVESGRLDI
EDVQFDLNVV VRDVNKMLTF AAERKGLMYV DETQELERLK VMGDPGRLRQ ILTNLLTNSI
KFTSEGSVTM QVKIREETAE TVAVEFTVED TGIGIEEEVR KRLFQPFSQA DSSTARRFGG
TGLGLTISKN LVELMHGEIS LESSLGLGTK ASFWIPFNKA TYLSGDSPLL DMGPIPHRLQ
SELSISEYSG PQPPGSPLKP GLRQASLDSR RGSPAHFDVP LTLSDEERRN TQVLVVEDNP
INQQIALKTI RKLKFSVNAV WNGQEALDYL SKPESPDHPR PDVILMDVQM PVMDGYKATY
TIRHCEPFIA DQQIQNTPIV AMTASAIQGD REKCENAGMN DYLAKPVKGK TLEQMLLKWA
VEKKRKAALS SSPAAAARAV DVPQPALPRS VVQKERKTSE DSLTPKKDQG ASDVLATKLN
KLNFQSDTVF ARSAETAESR SMDRLRNEEK AMQLRDQQLF ASAATPKKLL GVLGDTATQE
EATETRPSAL TRENIEKLTR NAPLDHVTQP DVDTSSLDVT VDSNTQSRPG RPSMGTRMKS
DGDKTVLPE
//
