ID A0A2G4SPF5_RHIZD Unreviewed; 748 AA.
AC A0A2G4SPF5;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Histidine kinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=RHIMIDRAFT_259363 {ECO:0000313|EMBL:PHZ10625.1};
OS Rhizopus microsporus ATCC 52813.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX NCBI_TaxID=1340429 {ECO:0000313|EMBL:PHZ10625.1, ECO:0000313|Proteomes:UP000242254};
RN [1] {ECO:0000313|EMBL:PHZ10625.1, ECO:0000313|Proteomes:UP000242254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 52813 {ECO:0000313|EMBL:PHZ10625.1,
RC ECO:0000313|Proteomes:UP000242254};
RX PubMed=27956601; DOI=10.1073/pnas.1615148113;
RA Lastovetsky O.A., Gaspar M.L., Mondo S.J., LaButti K.M., Sandor L.,
RA Grigoriev I.V., Henry S.A., Pawlowska T.E.;
RT "Lipid metabolic changes in an early divergent fungus govern the
RT establishment of a mutualistic symbiosis with endobacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:15102-15107(2016).
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DR EMBL; KZ303854; PHZ10625.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G4SPF5; -.
DR STRING; 1340429.A0A2G4SPF5; -.
DR OrthoDB; 1222064at2759; -.
DR Proteomes; UP000242254; 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; 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 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; 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:SF6; RESPONSE REGULATORY DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 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:UP000242254}.
FT DOMAIN 218..541
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 629..745
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 547..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 679
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 748 AA; 83934 MW; 2D7566CD6A761BC6 CRC64;
MPKPAIKKTI QGIYEATFSE VGDQFLDVLV KEIAILFNVQ TVMIHRLLSA KEFRDMKHSE
GCPSIQLIKT PNAHLSADEQ YLFIKACHST LPQQPALAKY SAVALSSFPD NSPHIKTLED
AAHYVTQDAS LSGTVYPSYS SFVGLRLDLD SREPIGLISI MHDKSLEKQQ LDHISCILKA
VQRRVTNEIS RLRQRDNLIV IKNAALQDAE YKLRFLADMS HEIRTPLNAV VALTDLLLQE
KQSLNEEQVE HLQVIQTSGN HLLTVINDIL DFSKMNHGSK FKLEYRKFSL RKCIKDALNM
ARHQAANSQY PKQIHIVECP LEIKDDIPVP QLLQQLEASG ILAHKHGTNQ QTSLPFIWKV
DPDIPDYLMG DSMRLTQILI NLCSNAAKFT KQGGIHIKIS KPDTDKSNFR ERYDARVESV
YQKYAMRRRK KAPMVTSSDS SDSCYYYETE DEQTVPQEDQ NGRVVLEISV TDTGIGMPAS
RLPLLFKSFS QIDISTARKY GGTGLGLAIS SMLVNRMGGG LWVESEEGVG SRFALTLPIA
IAQDIPTSPS SSISSTESLC TPRPSEPKAQ STIQTNIHSH SHNLQHNNIP DTKSTASGLQ
NMISKTHRPE TVPRKVQQEE NLALEHPIKV LLAEDNILNQ KIALSILKRL GYQDVTIASN
GKEALDLILK QEFDVVFMDL YMPEMDGLEA TRHIRQELKK NVYIIALTAS ASKQDRNICI
ESGMNDFISK PFTMTEMKAA LRKVYTAK
//
