DHKJ_DICDI
ID DHKJ_DICDI Reviewed; 2062 AA.
AC Q54YZ9; Q95PH6;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 2.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Hybrid signal transduction histidine kinase J;
DE EC=2.7.13.3;
GN Name=dhkJ; ORFNames=DDB_G0277883;
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].
RC STRAIN=AX4;
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).
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 12 HAMP domains and two
CC receiver domains.
CC -!- PTM: Activation probably requires transfer of a phosphate group between
CC a histidine in the kinase core (transmitter) domain and an aspartate of
CC the receiver domain. {ECO:0000250}.
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DR EMBL; AF362372; AAK54091.2; -; Genomic_DNA.
DR EMBL; AAFI02000023; EAL68114.2; -; Genomic_DNA.
DR RefSeq; XP_642053.2; XM_636961.2.
DR AlphaFoldDB; Q54YZ9; -.
DR SMR; Q54YZ9; -.
DR STRING; 44689.DDB0215385; -.
DR PaxDb; Q54YZ9; -.
DR EnsemblProtists; EAL68114; EAL68114; DDB_G0277883.
DR GeneID; 8621265; -.
DR KEGG; ddi:DDB_G0277883; -.
DR dictyBase; DDB_G0277883; dhkJ.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_000445_3_0_1; -.
DR InParanoid; Q54YZ9; -.
DR OMA; VNNMVDF; -.
DR PhylomeDB; Q54YZ9; -.
DR PRO; PR:Q54YZ9; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0004673; F:protein histidine kinase activity; IBA:GO_Central.
DR GO; GO:0071474; P:cellular hyperosmotic response; IBA:GO_Central.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003660; HAMP_dom.
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 Pfam; PF00672; HAMP; 3.
DR Pfam; PF18947; HAMP_2; 9.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 12.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF52172; SSF52172; 2.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50885; HAMP; 12.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Transducer; Transferase;
KW Two-component regulatory system.
FT CHAIN 1..2062
FT /note="Hybrid signal transduction histidine kinase J"
FT /id="PRO_0000328340"
FT DOMAIN 259..317
FT /note="HAMP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 357..409
FT /note="HAMP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 449..501
FT /note="HAMP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 541..593
FT /note="HAMP 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 633..685
FT /note="HAMP 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 725..777
FT /note="HAMP 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 819..871
FT /note="HAMP 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 911..963
FT /note="HAMP 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 1003..1055
FT /note="HAMP 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 1095..1147
FT /note="HAMP 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 1187..1239
FT /note="HAMP 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 1279..1331
FT /note="HAMP 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 1353..1575
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 1590..1708
FT /note="Response regulatory 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DOMAIN 1730..1848
FT /note="Response regulatory 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT REGION 64..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 120..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1877..2062
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1877..1956
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1957..1978
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1987..2062
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1356
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 1644
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT MOD_RES 1779
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT CONFLICT 2
FT /note="E -> D (in Ref. 1; AAK54091)"
FT /evidence="ECO:0000305"
FT CONFLICT 7
FT /note="E -> G (in Ref. 1; AAK54091)"
FT /evidence="ECO:0000305"
FT CONFLICT 10
FT /note="N -> T (in Ref. 1; AAK54091)"
FT /evidence="ECO:0000305"
FT CONFLICT 1188..1189
FT /note="NL -> KF (in Ref. 1; AAK54091)"
FT /evidence="ECO:0000305"
FT CONFLICT 1330
FT /note="T -> P (in Ref. 1; AAK54091)"
FT /evidence="ECO:0000305"
FT CONFLICT 2025
FT /note="S -> F (in Ref. 1; AAK54091)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2062 AA; 224160 MW; 1853D64C9C7E680C CRC64;
MELELDELLN QCIHCCPHCK NKISISQLSA CNLIKNRFYE LNNKYNNFKN NNIYDIDCNN
NSNLNNTNNN NNNNNNNDNN NSNNSFRNIL NKDKDITNNN SHFNISDSFI NFNNKIKNKS
NKIKNGGNNN NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN NNGESYNLFL DSLLKSLETV
KGGDFKSRVK SNEQLFTEKE NKIISTYNEI LNFQDSTVTE FKRIEKQVGK EGNVMSRAFL
PNAVGSWEFC IEFVNNLIGD MIQPTEEVIK VITSVARGDL SQTINLELGQ GRKLTGEFLR
IAKVVNTMVS QLNSFSSEVT RVAREVGTDG KLGGQAVVTG VDGIWKDLTD NVNTMAANLT
GQVREIALVT TAVATGDLSK KITLDVKGEI QELKLTINTM VDQLKSFSSE VTRVSREVGT
EGILGGQAQV KGVDGVWKDL TDNVNTMAAN LTGQVRSIAE VTTAVAEGDL SKNITIDAQG
EILQLKNTIN TMVQQLKGFS SEVTRVAREV GTKGILGGQA EVTGVGGVWK GLTDNVNTMA
ANLTGQVRSI AEVTTAVAKG DLSKNITIDA QGEILQLKNT INTMVDQLKS FSSEVTRVSR
EVGTEGILGG QAEVTGVDGV WKGLTDNVNT MAANLTGQVR SIAEVTTAVA KGDLSKNITI
DAQGEILQLK NTINTMVQQL KSFSSEVTRV SREVGTEGIL GGQAQVEGVG GVWKDLTDNV
NTMAANLTGQ VRSIAEVTTA VACGDLSKNI TIDAEGEILQ LKNTINTMVD QLKSFSSEVT
RVAREVGTEG ILGGQAQVEG LGVGGVWKDL TDNVNTMAAN LTGQVRSIAE VTTAVAEGDL
SKQVSINAQG EILQLKNTIN TMVDQLKSFS SEVTRVSREV GTEGILGGQA QVKGVGGVWK
DLTENVNTMA ANLTGQVRSI AEVTTAVACG DLSKNITIDA KGEILQLKNT INTMVQQLKG
FSSEVTRVSR EVGTEGILGG QAQVEGVGGV WKDLTDNVNT MAANLTGQVR SIAEVTTAVA
CGDLSKKISI DAQGEICELK NTINTMVDQL KSFSSEVTRV AREVGTEGIL GGQAEVKDVG
GVWKGLTDNV NTMAANLTGQ VRSIAEVTTA VACGDLSKKI SIDVRGEFLE LKITINTMVD
LLNSFSSEVT RVALEVGTEG ILGGQAQVEG VDGVWKYLTQ NVNTMAANLT SQVREIANVT
TAVANGDLSK KVNLDVRGEI LQLKITINTM VDQLNSFSSE VTRVAREVGT EGMLGGQAQV
EGVGGVWKDL TDNVNTMAAN LTTQVRSIAE IAKAVTKGDF TRVISVDAKG EVNLLKLIIN
EMIHNLKETT LKNTLAKETA EAASRAKSDF MANMSHEIRT PMNGIIGMTD LTLDTELTAE
QREYLSMVQS SAGSLLTIIN DILDFSKIEA GRLELDQAEF SLRAHLYDAL KTLSWRAHQK
CIELVCDIAS DVPDSLIGDP GRLRQIVNNL VGNAIKFTSQ GEVDLVVKVE KSLSCGEVVL
KFSVIDTGIG IPKDKLHLIF EAFSQADGSI TRRYGGTGLG LTISTRLVEL MKGKLSVVSK
SGKGSTFEFT AQFPTSPNQL PLTEKLNDVH TLIVDDNKST LKVLKQILSE FGITSEVSNN
TQDAFNMIVK ATKTTKPFEF IFVDAQLGTS LIDMMVEKNM NHCKTKIIML ISGGGQRGYP
DSSSNFITGY LSKPVSPSEI FDILTRQGIT RQIPKQLCKK IQLTSEIFGD ILLAEDNAVN
QRLAIRLLEK FGHRVQLAEN GLQAVASSQL RKFDLILMDV QMPHCGGFEA TAQIRKREHE
QGIHTPIIAM TAHALARDRV KCLEAGMDDY ISKPINPDQL KAMIEKYLFI SKSCNSYEQF
QQLQAQKSAN YINSTSYYGQ LTPTTTTTTT TTTALPSPQK ILSIEDDKNL NSNDNNEKDN
NNQNNNNNQN DNNKNDNNQN DFDQIKTISN NKESGVGENK KTTRNTSDNE RIPKKSDMFD
GDFVVQPQLV NRSSSNNKKS NDINGKPQQS QQQPHQQEQQ QDIYSSKHQQ QSNSPPLANT
KRKENDLSNS SIPASKKNNT KQ
