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DHKA_DICDI
ID   DHKA_DICDI              Reviewed;        2150 AA.
AC   Q54U87; Q23863;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Hybrid signal transduction histidine kinase A;
DE            EC=2.7.13.3;
GN   Name=dhkA; ORFNames=DDB_G0280961;
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 / MRNA], MUTAGENESIS, CHARACTERIZATION,
RP   AND DEVELOPMENTAL STAGE.
RC   STRAIN=AX4;
RX   PubMed=8670894; DOI=10.1002/j.1460-2075.1996.tb00763.x;
RA   Wang N., Shaulsky G., Escalante R., Loomis W.F.;
RT   "A two-component histidine kinase gene that functions in Dictyostelium
RT   development.";
RL   EMBO J. 15:3890-3898(1996).
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   FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF HIS-1396 AND ASP-2076,
RP   INTERACTION WITH SDF-2, AND SUBCELLULAR LOCATION.
RX   PubMed=10373524; DOI=10.1128/mcb.19.7.4750;
RA   Wang N., Soderbom F., Anjard C., Shaulsky G., Loomis W.F.;
RT   "SDF-2 induction of terminal differentiation in Dictyostelium discoideum is
RT   mediated by the membrane-spanning sensor kinase DhkA.";
RL   Mol. Cell. Biol. 19:4750-4756(1999).
RN   [4]
RP   FUNCTION.
RX   PubMed=15897458; DOI=10.1073/pnas.0501820102;
RA   Anjard C., Loomis W.F.;
RT   "Peptide signaling during terminal differentiation of Dictyostelium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:7607-7611(2005).
CC   -!- FUNCTION: Acts as a receptor histidine kinase for the cytokinin SDF-2
CC       in a signal transduction pathway that regulates prestalk gene
CC       expression and controls terminal differentiation of prespore cells.
CC       Binding of SDF-2 to this protein inhibits phosphorelay and induces
CC       rapid sporulation. This protein undergoes an ATP-dependent
CC       autophosphorylation at a conserved histidine residue in the kinase
CC       core, and a phosphoryl group is then transferred to a conserved
CC       aspartate residue in the receiver domain. {ECO:0000269|PubMed:10373524,
CC       ECO:0000269|PubMed:15897458}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3; Evidence={ECO:0000269|PubMed:10373524};
CC   -!- SUBUNIT: Interacts with SDF-2, an acbA peptide involved in sporulation.
CC       {ECO:0000269|PubMed:10373524}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- DEVELOPMENTAL STAGE: Expressed from 8 hours following initiation of
CC       development, prior to the appearance of mound tips. Subsequently
CC       persists throughout development. {ECO:0000269|PubMed:8670894}.
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DR   EMBL; U42597; AAC47300.1; -; mRNA.
DR   EMBL; AAFI02000040; EAL66777.1; -; Genomic_DNA.
DR   PIR; S71629; S71629.
DR   RefSeq; XP_640889.1; XM_635797.1.
DR   AlphaFoldDB; Q54U87; -.
DR   SMR; Q54U87; -.
DR   STRING; 44689.DDB0215354; -.
DR   PaxDb; Q54U87; -.
DR   PRIDE; Q54U87; -.
DR   EnsemblProtists; EAL66777; EAL66777; DDB_G0280961.
DR   GeneID; 8622946; -.
DR   KEGG; ddi:DDB_G0280961; -.
DR   dictyBase; DDB_G0280961; dhkA.
DR   eggNOG; KOG0519; Eukaryota.
DR   HOGENOM; CLU_231770_0_0_1; -.
DR   InParanoid; Q54U87; -.
DR   OMA; SIMEIEC; -.
DR   PRO; PR:Q54U87; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:dictyBase.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:dictyBase.
DR   GO; GO:0005887; C:integral component of plasma membrane; IDA:dictyBase.
DR   GO; GO:0005524; F:ATP binding; TAS:dictyBase.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IMP:dictyBase.
DR   GO; GO:0009784; F:transmembrane receptor histidine kinase activity; IDA:dictyBase.
DR   GO; GO:0140582; P:adenylate cyclase-activating G protein-coupled cAMP receptor signaling pathway; IMP:dictyBase.
DR   GO; GO:0009736; P:cytokinin-activated signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0051344; P:negative regulation of cyclic-nucleotide phosphodiesterase activity; TAS:dictyBase.
DR   GO; GO:0046777; P:protein autophosphorylation; IMP:dictyBase.
DR   GO; GO:0030587; P:sorocarp development; IMP:dictyBase.
DR   GO; GO:0031288; P:sorocarp morphogenesis; IGI:dictyBase.
DR   GO; GO:0031150; P:sorocarp stalk development; IMP:dictyBase.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IMP:dictyBase.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 3.30.450.350; -; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR006189; CHASE_dom.
DR   InterPro; IPR042240; CHASE_sf.
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; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   Pfam; PF03924; CHASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08447; PAS_3; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM01079; CHASE; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF52172; SSF52172; 1.
DR   SUPFAM; SSF55785; SSF55785; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS50839; CHASE; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell membrane; Coiled coil; Cytokinin signaling pathway;
KW   Developmental protein; Differentiation; Kinase; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome; Sporulation;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..2150
FT                   /note="Hybrid signal transduction histidine kinase A"
FT                   /id="PRO_0000328204"
FT   TRANSMEM        772..792
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1098..1118
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          838..1082
FT                   /note="CHASE"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00049"
FT   DOMAIN          1235..1317
FT                   /note="PAS"
FT   DOMAIN          1321..1376
FT                   /note="PAC"
FT   DOMAIN          1393..1620
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   DOMAIN          2026..2146
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          68..149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          184..267
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          286..323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          339..359
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          415..505
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          520..546
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          560..733
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1209..1228
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1233..1252
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1874..1893
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1933..1952
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1962..2017
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1139..1164
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        16..41
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        184..250
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        562..607
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        615..635
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        656..733
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1876..1893
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1962..2012
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1396
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         2076
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   MUTAGEN         1396
FT                   /note="H->Q: Impaired function. Normal function; when
FT                   associated with N-2076."
FT                   /evidence="ECO:0000269|PubMed:10373524"
FT   MUTAGEN         2076
FT                   /note="D->N: Impaired function. Normal function; when
FT                   associated with Q-1396."
FT                   /evidence="ECO:0000269|PubMed:10373524"
FT   CONFLICT        1319
FT                   /note="S -> A (in Ref. 1; AAC47300)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1509
FT                   /note="L -> R (in Ref. 1; AAC47300)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   2150 AA;  239636 MW;  1FDA618EE9B3DBCA CRC64;
     MELKTFKDLN DDIIGDTSPV INTGDQPNPL RTQQQQLQQQ QQQQQQQQQQ QQQQQQQQQQ
     QQQQQQHHIP QQLYQKQQQQ QHSHSYGNHS FIHNVSPTSP SYDINNNNNN NNNNNNNNNN
     NNNNNNNSNN NNNNNNNNKN NYNNNYYYSP IENSNISKSL EESVLNQFPH NFNLNSSNNN
     YLNNSSSLHN INQSVNSLSN NNNNQTNQQP INNNNNNNNN NNNNNSNNSN NSNNNNNGNN
     NNNITDSPTK SKRHSTYETN IGSHQRRKSI QSLIANSAIH SFSKLKNKPL SSSTPSTVNT
     CGAVNNNSNN NNNNNNNSTG SLGAIPMDRS FDGNINTITE ESTGGNNSPR SNCGSNCGSN
     GGIPLSPRNL SSLNSGVNVS PRNIHLNNLN NNSSNLPPLS PRHINFHINV SNLNNNNNNN
     INPNNNPNNS NNSNNNVSPR NNNHNISPRG SNISPRSNNG GSTTISPRNI SNNNNIINNI
     NNNNILTPPR NSPRLENVNP TNSPRLLATS LNSTLPIVSS LTSSNNNNQS NNNTNPSINN
     NNGRNGHCIQ TISEEILGNK PVVYNNGNNN NNNNTNNSTT SNNNITTNNN NNNNNNINNN
     VLSTPRKRTK GNHSKTNSLQ DFETSSMNGG DDSISGAGSG GSLRRRNKDD NDENDGNSNN
     TNSNNSNNNN NNNNNSSNNN NNNSNNNNNN NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN
     NNNNNNNYHN GATMMMSHNH QSIGMSSSPK KNNFKPFSRN CSLMGMGRRA WAIILGLFIV
     GSSISILATL VLRYSEENSI ADDFARVARD RFTMLRIEFN NRLYITQTLS LLLSVFPSTS
     EDQFVPFSKL WSDNAEGLEG IMWAPRVSNL DRYTWEIEHS VKIREIVTNP NNSSDMRDVP
     AAAASDYYPI LFSEPQSSND HFKGYNIYSD MWRRPSLNKT RDTGEKVSVA SPYINKLANV
     PKNSRSNVLL YIYQAVYTYG KVLSTVEDRR HEVIGFASCR FFISRMVSAS LQRLTEEDSL
     DLYVFDLDST PIGELIYYRA SNAGNDDGSS PTNIMNGKML EDRSDMIYYN TMNVGGRNWM
     IALRPSRKFT NKHYTFYPYA IGGVCMLLSA LVSFWFAVNT KHNIKLSATN EDLHKEIYNR
     KLAEKALAES QERLELAMEG SEDAVWDWKV NTGELHISSR WFQILKAHDT SYQSRTLYEE
     LKSSSTNNLN FKGDSKNGGS NNGTFNLFKN GKVDSSSPQS ITNVNTTNGG GGGELRKSNS
     GYLYNDELFS PIILEEMVSS PNTHQLAIWN MKFLAELIHP DDKQKFISEI KKTITRETSI
     MEIECRMRKK YGGYLYIIMR GKVVSNETSF KDNSLRMAGT LRDMTSRKDM QRLILEKEAA
     EEANKAKSAF VATVSHEVRT PLSGVIGVSD LLLETNLSEE QRDYVQTIQK SSQALLTIIN
     DILDYSKLES RQLKMETLPF SIIETCQAVI HMLSVAANDD VDILLRVPPN VPRIIFGDAM
     RMRQVLLNLL SNAIKFTSRG HVLTDISVDD SIPPTNTEEE IIHLCITIED TGIGIPQSLF
     DSIFEPFSQA DNSTTRKYGG TGLGLSITKR LIEEVMGGTI QVSSIVGQGS KFKCIIPFLL
     PNTSPSDLNL ISPSSLPKPF INRSPKSTYS FTDKKNSVPS TPIPSGDILI NKVCLLICRD
     TVTELVFKEQ LEWLGMIVKQ VPRNVIDSIK NTILNNNNNN NNNNNNNNNN SNNSSSIISP
     SSLDYSDENE HLDLVLIDLE ILTEHLKIPS NVPIIFITPT KFNISKHNGI LNKWITKSPN
     QRVELIRRPA ITDKLIPIIS KCIKSQVQFT SGSSQLQSQQ ANLQQQLLHQ QLCNNGQTLN
     NNYNSGGIGG GGGGGGSNTM NGSSGNLSNN NNFGQTPLSS GLVLLVHTGR TPPLFNNNGN
     SIIPPLELAV DHHGNQQQQL YQQQQQQQNN SSGNFQQFYQ QQNNNSNNSF TPTLPNENSN
     NSIMNNSLNN NNTTPSNVTP TLFTSSPLDL QGRDTPVLQP PAYRKKALIV EDNELNRKVL
     AQLFKKIDWT ISFAENGREA LKEITGERCF DIVFMDCQMP VLDGFQTTKI IRSKERENNW
     KRMNIVALSA GSSSSFVQDC LDSGMDSFMG KPITLATLKD ALAKWGGYNN
 
 
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