DHKM_DICDI
ID DHKM_DICDI Reviewed; 2388 AA.
AC Q54SK5; Q95PH4;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Hybrid signal transduction histidine kinase M;
DE EC=2.7.13.3;
GN Name=dhkM; ORFNames=DDB_G0282377;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1071-2388.
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).
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- DOMAIN: Atypical domain architecture: contains 2 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; AAFI02000047; EAL66048.1; -; Genomic_DNA.
DR EMBL; AF362374; AAK54093.1; -; Genomic_DNA.
DR RefSeq; XP_640034.1; XM_634942.1.
DR AlphaFoldDB; Q54SK5; -.
DR SMR; Q54SK5; -.
DR STRING; 44689.DDB0220020; -.
DR PaxDb; Q54SK5; -.
DR PRIDE; Q54SK5; -.
DR EnsemblProtists; EAL66048; EAL66048; DDB_G0282377.
DR GeneID; 8623560; -.
DR KEGG; ddi:DDB_G0282377; -.
DR dictyBase; DDB_G0282377; dhkM.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_229367_0_0_1; -.
DR InParanoid; Q54SK5; -.
DR OMA; CNEFMSK; -.
DR PRO; PR:Q54SK5; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0048102; P:autophagic cell death; IMP:dictyBase.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF52172; SSF52172; 2.
DR SUPFAM; SSF55874; SSF55874; 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Membrane; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Transducer; Transferase; Transmembrane;
KW Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..2388
FT /note="Hybrid signal transduction histidine kinase M"
FT /id="PRO_0000328370"
FT TRANSMEM 550..570
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 589..609
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 645..665
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 679..699
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 896..916
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 953..973
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1025..1045
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 1093..1499
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 1541..1656
FT /note="Response regulatory 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DOMAIN 2262..2383
FT /note="Response regulatory 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 42..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 69..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 123..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 430..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 732..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1236..1410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1666..1702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1960..2022
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2036..2121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2133..2183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2218..2256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..505
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..542
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..879
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1236..1255
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1285..1313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1314..1409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2046..2065
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2076..2121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2133..2159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2169..2183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1592
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT MOD_RES 2313
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 2388 AA; 264817 MW; 4176445E80E95489 CRC64;
MSNYLNANST ENNNNNNNNN NNNNNNINNN FNTTDFKIVG NFNTPPIGSN NNNNNNNNSI
STQSLQTINE CNSGGEQSPK IKTNNNSYNT PVSSSTSTTG TNTTPMKSTP IHNSLQNIFK
NANRSNLNNN NNNNNNNNNN NNNNNNNNNN NNSGCGSGSL NSVNNNNNNN NNNNNNSNNN
NSNSNSNSNN NNNSNSNNNN NNSNSNAYPL KYYQHPQQSC SNLDSFENLS PLRQSSTLLN
FSSNNNNNNN NNNNNNNNNS NNNSSNNNNK NNSSKNKVGG GNNKNNGGDD SAQFISSDNK
YNTVGNETHH HHHHQLHNHR HSNVQGSSSP IKSSPKLISS QSLGNIFSQI SPNIALTTNI
SPHGSPFSSS SSSRKSSSSP SFLNQNNQNN PNNQNNQNNS TSPHEKSFLN NSNDSFDYND
NSKRLRNRLT RNTGYSSTGS IGNSSSSSFY NNNNENSNIY SKIKHTRSSS GGNKPSPKYF
QTSQAIYTPP YPQPYPQPPQ LPPPSSSSSL SKENDNVDNN NTNNNNNNNN NNNNNNNNNN
NESFFSSKGT MNLIHISLLS VLAFYIFLMV SKKFLFRVFQ WNNNINSLFI LIFSFHFIFS
SILMFLLVVL LKMKKYSHSI SQSARESLRN SRVIPSLLNF FLSDYIFLGL VLSGLVNILQ
VNLFFNPKDP LLNLDSISNI STAIEFLVVG IVLNFSHIPK KMYNSRYSEF RVSSSISPYF
QDESYNVNNI INNDNKNKIN DKSDNSNSIT NNNNINNNID NNNNSSSNTK INNDLNFDNN
IKNNDINNNI TNNNNNNNNN NNNNNNTNNN NNNNNNNSNN NNNNNNNNSN KNNNTNSNNN
NNNSSNNNNT NNNKINDNKN NNNNNNNNNN NNNNNNNNNN NEEDDEEEKN DWSYSFQIFF
TRIFLCLSIT YTLIVLRLNY DPLNQFLQQS SSFGSGANGN SGGGNVNTII SPVQFQAPLA
TLLHFIQLVL LLVNYNRFRT NRFFSLILST IFIEVSSWET FGLNSRLFES YIFEALLIRR
WIRACSVGFP IVGIILDIYS GWMSINQSIK SIDQQNIMIV NRFNYLCSNV KKQEELTQYN
SQFYIESMNQ FKRLVQNTGS IISLIYDTDV QPNQEAYLSK FSSSYEQLSK LTKECLFYSE
IKQLKRNDVE NLSFVVSNLL EDLISTPSIR TQFEEKEIDL FYLIDKDVPL SLVGDSQKIK
QILLKLITNS IKATYEGEVY IRVSLSSNLG VLKQQPIHHH RHHHRHHHHH HHHHHHHIID
DDDYDDDNDD DNNTEDSSSC CNIDELSDKI KDNQDENLEL KKSNNDKIIE NKENQENNNN
NNNNNNNNNN NNNNNNNNSN NNTNININTN NNNDSNNNNC INNDLKNNNN NSNNNVNNNN
NNINDSNNNN NSNNNNINNN INNNINNNNN IKKKKKKNEF TVYFSVIDSG SGIDPYSTNL
LFQPFSLSSY NVNSTNTDGE FGLGLAICKQ LSNLMNGEIK YETEMEKGSV FELQVPMKCD
SISSITSSMN STTNTTNHYP RIMNNQSSKF FANSKWGEGL KILVIDDNPN IGKVIAMHLE
PFGFKVFQRT TFQSAIYFFN ERNGDFNLIL LDPLIPSLVI DEIKQMKQDS SNIIKNPPLV
IMCTAKLRKS LNVDNVHYLY KPIKREQLTV LSQLLPNTST INPIYSNQNL NNSGSSNGGG
GGGGGGGGGG GGGGSGSSNI DFNKTKLGGS NISTGIGNSG LINSNNIPTP VNTPSNIIPN
LLSCQSLLTS LNNANIPQLT NDIGITNNNI NNNSLMFTTP NSTLSNNGIT GLDNNSNNDT
GSIDNNSNIS TNIDNNNDYF IRNNGIPPQN DMNTYNNYVL NHQQGVLPKS LSVPSTPLSY
NMLPTNLNIN AKRSSLQPLN ENSVLPTNLT PPILSASPQS LLPMGNDINS ILPNTQQSQI
DLQSQIELQP LLQSTIIRND RGGDILPDST LEGQITNLSG NNSTISINPP LPETNNNTTT
TTTTTQPKKS PILTSSNGSD KSEGSTGSNR SKSRISFLNS SNSGLLKNNL GEDIYCKGDQ
SEGIPIPKSE RTSDSSSSSS SSDSHGQDDH SYRLEDFSIS SPSSQSPLLD LSGTSGTSGT
TNLANSGINS GSGSGGGDII NQNQLITSNQ LFQQQLQQQQ QPQQQQPPGT PTISPSSSFP
LLPIPRDIIN SSGASSGIKV KSSTSIPDYV QVSPRRFSGS STGSGSSVAS PQLLSTSNQL
NNNINNLNLN SNNNNNNNNN NNNNNNTNND NNNNNDNNYN VNILLVEDNL VNAKIAMTVL
RKHNFRVELS KNGQLAMERI KQSHSSFDLI LMDIHMPVMD GITCSKLTRK FETEHGLKHL
PIIALTADAT TGHKNLCLEA GCNEFMSKPL DYALLISLLK KLVFNKDQ
