|DHKC_DICDI » Hybrid signal transduction histidine kinase C »|
|Hydrophobic Thickness||37.2 ± 2.2 Å|
|Tilt Angle||12 ± 7°|
|Links||UniProtKB, Pfam, Interpro, iHOP, STRING|
|TM Segments||4-28 (4-31)|
AA: 531-653, PDBID: 3SL2, Subunit A, Seq Identity:34%, Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
|UniProt annotation for DHKC_DICDI » Hybrid signal transduction histidine kinase C|
|FUNCTION: Acts in a signal transduction pathway that regulates the slug versus culmination choice. Believed to be the first component of a phosphorelay that couples the sensing of ammonia to the modulation of PKA activity and hence activates culmination and spore germination. Ammonium transporters amtA and amtC are thought to respectively activate and inhibit dhkC phosphorelay. This protein probably undergoes an ATP-dependent autophosphorylation at conserved His residue in the kinase core, and a phosphoryl group is then transferred to a conserved aspartate residue in the receiver domain. CATALYTIC ACTIVITY: ATP + protein L-histidine = ADP + protein N- phospho-L-histidine. DEVELOPMENTAL STAGE: Expressed at low levels during growth and development, with a peak during early aggregation (8 h). Mounds display weak expression within the upper regions and very strong expression at the perimeter of basal cells in contact with the substrate. Expression becomes tip-specific during first finger formation.|
|UniProt features for DHKC_DICDI » Hybrid signal transduction histidine kinase C|
CHAIN 1 1225 Hybrid signal transduction histidine kinase C. |
DOMAIN 426 653 Histidine kinase.
DOMAIN 669 784 Response regulatory 1.
DOMAIN 1078 1200 Response regulatory 2.
|Amino Acid Sequence for DHKC_DICDI » Hybrid signal transduction histidine kinase C|
|MIVEVELGFL LSTLFFTIIS IILFYFFINN KNNLIDQCQE VTKLNNKDNK IVNNNNNNYN NNNFNKIEEI NDDKNKEIIK LINNSNNKNL KIKIQEIDSG NNNNNNNNNN NNNNNNLNKN SNEIFRNFKI FSGSLLVIDQ DLNIISSSES VRDIFSNIND INGVNQQVIG SLQNYSFINL VHQKDKDRVS TFLKLKFKNN NNIKHQQFSE DIINEKDELK EIQIEDNKEL IIINNNNNNN NDNVLKFGNN NSNNSSIILF QGVYHLNNTD LSKPFNLQVS ILPFISENYI VLSLKDLSPP PLRLLLNKTS SALSPRSLSS SSSSSPSSSN NNGNTNNSGS LSPRSSNSNG SAVSPRNVSS NSMSPRGQNS DRSISSPRGS SSSSSSSSNE LAISPRNSNG TISSPRTSNL SIESVLNNKS IDMISHLSHE LRTPIHSVIA SIQLFRSTIL TVTQNEYLSI IDTSANTLLE LVSNVLDYKR IRSGKLTLNN VDFNLCHVIE DVCAMVSPQA QAKSLQIASF IFIHCPLSFY GDPIRLRQVL LNLIGNGLKY TNKGQVCISV EPEQVNEHCM YLHFQVKDSG IGIKEENMSK LFAGFSQVNN GGTTQEALGS GLGLAISKDL VELMGGKIWC SSNATQNNGE AGCTFHFVIP LETNPKQLPC PIQNFNGLSV LVVDKNPYIQ TVLCQYLEGW NCQVIKSSDI KEASNKLKDL RREQIEVVMI DIDNIDFRDF IQFKDAFNRL EFGRIGLITM SSDRSMVNEM GFGTSKLTKP FRQSHLVACL LASMPEHSSS TTNCFSNIVG MNSNINNNNN INNNSNNNNN NMQTHNSNSV YGNGNYGNCT PFSNNNNRIH MMSSGDKPSI NNRRMSISLG KIPTFNSGGS NSPRSKKLFE EVLQQQQLQQ QLQQQLQQQQ QLQQQQQQQQ QQQQQQQQQL QQQQQQLNTI DDDSNNYCNT TGTMDSIDEI NKNNYSDSES DELNDDQAPI IAPVQQLSFG RVTRRHSIDI IMFENSRELS ELRNLEDSTR YLSPRSMNNN NGNNDNGING GSGNSLFGSS IKEEIGGTSD TSSLAQSPNS LSPRAPTKIM ILDDNPVSLK LMQRILESRG FECYPFDCSE KAVAQLDQVN PAIIFMDCEM PKMNGFECTQ LIRKREQESL CLLKDRKIII ALTAHINPEI QVKCFDAGMN DFISKPFKPQ CLELILRKWE DCISNNQLNY NNSLINNQTT IQEQV|