DHKD_DICDI
ID DHKD_DICDI Reviewed; 1546 AA.
AC Q54SP4; O15783; Q95PI1;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Hybrid signal transduction histidine kinase D;
DE EC=2.7.13.3;
GN Name=dhkD; ORFNames=DDB_G0282289;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Anjard C., Loomis W.F.;
RT "The histidine kinases of Dictyostelium.";
RL (In) Inouye M., Dutta R. (eds.);
RL Histidine kinases in signal transduction, pp.1-1, Academic press, San Diego
RL (2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-744.
RA Singleton C.K., Zinda M.;
RT "dhkD, a histidine kinase gene of Dictyostelium discoideum.";
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as a receptor histidine kinase for a signal transduction
CC pathway. This protein undergoes an ATP-dependent autophosphorylation at
CC a conserved histidine residue in the kinase core, and a phosphoryl
CC group is then transferred to a conserved aspartate residue in the
CC receiver domain (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- DOMAIN: Atypical domain architecture: contains 2 histidine
CC kinase/receiver domain modules.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB84171.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF361475; AAK50005.1; -; Genomic_DNA.
DR EMBL; AAFI02000047; EAL66266.1; -; Genomic_DNA.
DR EMBL; AF029704; AAB84171.1; ALT_FRAME; mRNA.
DR RefSeq; XP_640257.1; XM_635165.1.
DR AlphaFoldDB; Q54SP4; -.
DR SMR; Q54SP4; -.
DR STRING; 44689.DDB0215384; -.
DR PaxDb; Q54SP4; -.
DR EnsemblProtists; EAL66266; EAL66266; DDB_G0282289.
DR GeneID; 8623516; -.
DR KEGG; ddi:DDB_G0282289; -.
DR dictyBase; DDB_G0282289; dhkD.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_246615_0_0_1; -.
DR InParanoid; Q54SP4; -.
DR OMA; EMYQFVA; -.
DR PhylomeDB; Q54SP4; -.
DR PRO; PR:Q54SP4; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IBA:GO_Central.
DR GO; GO:0031288; P:sorocarp morphogenesis; IMP:dictyBase.
DR GO; GO:0044671; P:sorocarp spore cell differentiation; IMP:dictyBase.
DR GO; GO:0031149; P:sorocarp stalk cell differentiation; IMP:dictyBase.
DR CDD; cd00082; HisKA; 2.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 3.30.565.10; -; 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; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR Pfam; PF02518; HATPase_c; 2.
DR Pfam; PF00512; HisKA; 2.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 2.
DR SMART; SM00388; HisKA; 2.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF47384; SSF47384; 2.
DR SUPFAM; SSF52172; SSF52172; 2.
DR SUPFAM; SSF55785; SSF55785; 1.
DR SUPFAM; SSF55874; SSF55874; 2.
DR PROSITE; PS50109; HIS_KIN; 2.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 2: Evidence at transcript level;
KW ATP-binding; Coiled coil; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Transducer; Transferase;
KW Two-component regulatory system.
FT CHAIN 1..1546
FT /note="Hybrid signal transduction histidine kinase D"
FT /id="PRO_0000328270"
FT DOMAIN 65..131
FT /note="PAS"
FT DOMAIN 139..193
FT /note="PAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT DOMAIN 218..440
FT /note="Histidine kinase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 571..686
FT /note="Response regulatory 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DOMAIN 747..1010
FT /note="Histidine kinase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 1359..1483
FT /note="Response regulatory 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT REGION 1013..1148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1266..1285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1313..1350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1500..1546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 36..63
FT /evidence="ECO:0000255"
FT COMPBIAS 1013..1147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 221
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 619
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT MOD_RES 750
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 1412
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT CONFLICT 114..115
FT /note="RW -> SR (in Ref. 1; AAK50005 and 3; AAB84171)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="G -> C (in Ref. 3; AAB84171)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="V -> A (in Ref. 3; AAB84171)"
FT /evidence="ECO:0000305"
FT CONFLICT 349
FT /note="V -> G (in Ref. 3; AAB84171)"
FT /evidence="ECO:0000305"
FT CONFLICT 471
FT /note="Missing (in Ref. 3; AAB84171)"
FT /evidence="ECO:0000305"
FT CONFLICT 520
FT /note="K -> R (in Ref. 3; AAB84171)"
FT /evidence="ECO:0000305"
FT CONFLICT 1150
FT /note="G -> R (in Ref. 1; AAK50005)"
FT /evidence="ECO:0000305"
FT CONFLICT 1158
FT /note="N -> T (in Ref. 1; AAK50005)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1546 AA; 172908 MW; 095D000FE94C245E CRC64;
MQDISTTTAS TNYLKADGDT GAVFSITSQQ QQIHYMRKQK PDHEKTREEL IEEINHLRAV
SNSNKNARIM LDEMYQFVAL LDVNGNLLDV NEPALQGGGM IRSSIQGIPF WDCRWWATSQ
ENIDNVREAV HKASKGEFIR YETEIFGKSA GTEKITIDFS LMPLFNDKGE VSLILPEGRN
ITEKRLGELE IERKNNELRS LYEKIKELDE LKTQFFANVS HELRTPLALI VGPTDKLLKD
ENVDINVRKD LEIVARNARG LLKIVNNLLD ISRLEAGKMN LNYSMVNLGQ TVHLIASCFE
ILAREKSLDF SIITPSEPMM AAIDADKMQR VITNLISNAF KFTPSGGAVK CILEKFDLSP
NKPGFQIVVS DTGPGIPDNL HEIIFERFRQ VDGSSTRKHG GTGLGLSIVK EFVTLHGGTV
TIHNISTGGA QFTLRLPLTP NMDEHLYKKT ISDQNISEIQ QQLYQQQQQE QQQQQQQQQN
LQQPKLILNN IDNKYKINDD DNDDDDDDDD EDGLNFNILK KTNTSSDIAS NALKDNMGSI
MGVHAIAQQA VEELTEKQFY QSQENIHNKP IVLVVEDNPE MNRFIAELLS KYYFVVTAFD
GVEGIEKTRA ITPDLIVTDC MMPRMSGDEM VEQLRSDEQF DNIPILLLTA KADENLRIKL
LQNGVSDYVN KPFSSEELVA RVVNLMTMKK AKQFLQEELS SANTDLQELI NQLTNKKRDL
QTLVGELEKE RNLLNNTNKS KDEFFMNLSH ELRTPLNGIL GWCQLLLYDI DSGGSSGGGS
GSISGDDSTV RTGLETIERC ASSQNQLIND LLDMSLIIGD KFSLILGDVD LPILIENAIS
SILVTAQSKK ISVHSNIQGE GEEESSILRN IVGDKARLQQ VIWNLLSNSI KFTKEKGRIH
LNLKVVNQIP SREVLGFCSN PMFNTINRHG DRWILFTITD NGKGIPKQFL PSVFDRFKQA
DCSSTRSYGG LGIGLSITQN IIHLHKGAVY ANSEGENKGS QFTVVLPIIK GSSSSNSSPS
NQLSCSSSPP LIKKPFFSQP TNYINNNNNN NNNNNNNNNN NNNNNNNNNN NNNYNNYNNN
NSNNNNNSNN NNNNNNNNNN NNNNNNNNNN NNNNNLNINN LINNNHNNNN NNYHHNNNNN
NNSNNNEKLG KRQREEINNN ENNNVDLRLR TPPPPPTSSI SENFLVNSSN LIPSPALNPI
NNNNNSNNNN NNIGDIKKIN LEISQIPSTN LNPKLSLVIN NNNNNNNNNN SLLKTIITNA
INNNINNSNN DDNSNNTTIP TPPSSAINMI NSLPLPSPSP SFILPTLSPF SSPLSELKSS
SNNNNNNNNN SNNNNNNSMS PNLRSPKANS NKNLLGGIQI MLVDDLEETT HLFSSMLYKL
GAKRIDTFQR VSDAYAFLCD SSKPQPDIIL SDLTMPFEDG YSMVRKLRDR EKINTQNKKT
PIIALTASVS SSDKEKVLKS GFDLHCSKPV NFLELSNSIL TLIEKYNTTV NIDLIKEQEQ
NNNNNNNNNN NNNNNNNNNN NNINNGNDDD SLLLTDSRPC KKANSQ
