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Database: UniProt
Entry: A0A177DPQ3_ALTAL
LinkDB: A0A177DPQ3_ALTAL
Original site: A0A177DPQ3_ALTAL 
ID   A0A177DPQ3_ALTAL        Unreviewed;       962 AA.
AC   A0A177DPQ3;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Putative histidine kinase HHK15p {ECO:0000313|EMBL:OAG21486.1};
GN   ORFNames=CC77DRAFT_804033 {ECO:0000313|EMBL:OAG21486.1};
OS   Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC   Alternaria sect. Alternaria; Alternaria alternata complex.
OX   NCBI_TaxID=5599 {ECO:0000313|EMBL:OAG21486.1, ECO:0000313|Proteomes:UP000077248};
RN   [1] {ECO:0000313|EMBL:OAG21486.1, ECO:0000313|Proteomes:UP000077248}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG21486.1,
RC   ECO:0000313|Proteomes:UP000077248};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ERT1/acuK family.
CC       {ECO:0000256|ARBA:ARBA00010855}.
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DR   EMBL; KV441476; OAG21486.1; -; Genomic_DNA.
DR   RefSeq; XP_018386907.1; XM_018533264.1.
DR   AlphaFoldDB; A0A177DPQ3; -.
DR   GeneID; 29118858; -.
DR   KEGG; aalt:CC77DRAFT_804033; -.
DR   VEuPathDB; FungiDB:CC77DRAFT_804033; -.
DR   OMA; HEAHKME; -.
DR   OrthoDB; 1222064at2759; -.
DR   Proteomes; UP000077248; Unassembled WGS sequence.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
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; 1.
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; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR43719:SF31; -; 1.
DR   PANTHER; PTHR43719; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 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; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50112; PAS; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000313|EMBL:OAG21486.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000077248};
KW   Transferase {ECO:0000313|EMBL:OAG21486.1};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   DOMAIN          369..440
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          519..792
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          817..938
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          942..962
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         866
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   962 AA;  106347 MW;  B75E6F021178F856 CRC64;
     MQMLTPPPDE EGLGAPPMSP PDQDKGCAYD WTAALPQTDH IRFFCNTDWS RTSLGPTSTW
     SQTLRLFASY VLSDSRGACL WWGDISNLTA IYNEAYAPLA AGVHPKLMGS LFQEGYPDLW
     PSIRQYFVEA KRTGAGVNYS SATSTVVERK GYTEETFFSG GFVPVGMPGA IEGFINTTYE
     VTSQKLADRR TNCLNTLASV PSQCVDDVCS HILTTLESNA NDVPMAMLYR IDETPGSNRL
     RLHGCNGLPE GHGLIVEEAT IDSEEGLIPD LRRAGAEQTV IEHDDRFLAT SWGGWGAPSK
     KIIISPIMCG TRLFGYLVFG TNPYRPHDDI CKQFIRDLSR MVSSIVSSAV DCEANRKRQE
     QLEADLAFSD LKLRHLIDHA SVGMCHVSLD GLMLWANDHY YQLAGKSASD HAVGLAFLEA
     YHDDDRAKAD DVWERLIKGA DHVTADLRLK RMYTPPTGDP EPAQLQVLAF PYRDEHGSVI
     SVMACTTDIS RLCWAQNFQA RLAAEAREAK RQQEAFIDVV SHEMRNPLSA IVHCADAIAN
     AIEECQTQLA DIPVPCLDTL NDNIQSANVI MQCANHQKRI IDDVLTLSKL DSMLLSITPV
     AVKPTKLVDS IVNIFQAELK TNKISYNITP DKSFLALGID HVYLDPSRVT QVFINLLTNA
     IKFVKPSKEP NISIRFGAST SDPRDLFPRN MFWATDGKQD GDVTSNPDWG TGEEIYLAFT
     VKDSGIGLQE KEIYKIFERF RQANVKTHVK YGGSGLGLFI SKALTEKQGG EIGVSSVLGQ
     GSTFGFYVKT RRVEWQPRTL KEMFQQAGQE AAARQLHVLL VEDNIINQQV LGKQLKKAGC
     HVSVANHGLE ALEILERETF DIVLMDLEMP VLDGLGAMRE IRRREKEQVY ASERLPVIAV
     TANVRKEQID TAIAAGADRV MQKPFKAADL VSMMKSLMPQ LAPSSIEPPT PGLGLQSSAL
     VP
//
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