Lipopolysaccharide kinase (Kdo/WaaP) family; These lipopolysaccharide kinases are related to protein kinases pfam00069. This family includes waaP (rfaP) gene product is required for the addition of phosphate to O-4 of the first heptose residue of the lipopolysaccharide (LPS) inner core region. It has previously been shown that WaaP is necessary for resistance to hydrophobic and polycationic antimicrobials in E. coli and that it is required for virulence in invasive strains of S. enterica.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169379075  30 EYWQSTNKVTGSASGRGTTWFVQLDTMQAALRHYRRGGLFGKLVKDNYLFSGwEQTRCAQEFQLLLTLINAGVHVPRPIA 109
Cdd:pfam06293   1 AWWALQGRVVGEPNGRRTGWFVVARVGNGVLRKYYRGGMWGHLNRDLYRYPL-GRTRAFREFRLIRRLREAGLPVPKPVA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169379075 110 ARAVKSGLTYQADLLSERIPNARDLVSILQEKPLPEG-----MYQKIGQEIAKMHNAGVNHTDLNIHNILID----DKDK 180
Cdd:pfam06293  80 AGEVKVGGGYRADLLTERLEGAQSLADWLADWAVPSGelrraIWEAVGRLIRQMHRAGVQHGDLYAHHILLQqegdEGFE 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1169379075 181 VWIIDFDKCRKQEHGD-WKKQNLERLLRSFKKellkrqIHWKERDFAVLTEA 231
Cdd:pfam06293 160 AWLIDLDKGRLRLPARrWRNKDLARLLRSFLN------IGFTEADWERLLRA 205

C-terminal catalytic domain of the atypical protein serine kinase, RIO2 kinase; RIO2 is present in archaea and eukaryotes. It contains an N-terminal winged helix (wHTH) domain and a C-terminal RIO kinase catalytic domain. The wHTH domain is primarily seen in DNA-binding proteins, although some wHTH domains may be involved in RNA recognition. RIO2 is essential for survival and is necessary for rRNA cleavage during 40S ribosomal subunit maturation. RIO kinases are atypical protein serine kinases containing a kinase catalytic signature, but otherwise show very little sequence similarity to typical PKs. Serine kinases catalyze the transfer of the gamma-phosphoryl group from ATP to serine residues in protein substrates. The RIO catalytic domain is truncated compared to the catalytic domains of typical PKs, with deletions of the loops responsible for substrate binding. The RIO2 kinase catalytic domain family is part of a larger superfamily, that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169379075  90 EFQLLLTLINAGVHVPRPIA-ARAVksgltyqadLLSERIPnARDLVSILQEKPlPEGMYQKIGQEIAKMHNAGVNHTDL 168
Cdd:cd05144    68 EFAALKALYEEGFPVPKPIDwNRHA---------VVMELID-GYPLYQVRLLED-PEEVLDEILELIVKLAKHGLIHGDF 136

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1169379075 169 NIHNILIDDKDKVWIIDFDKCRKQEHGDWK---KQNLERLLRSFKK 211
Cdd:cd05144   137 SEFNILVDEDEKITVIDFPQMVSTSHPNAEeyfDRDVECIIKFFRR 182

Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated with Kae1 (kinase-associated endopeptidase 1) in the Archaea. In many Archaeal genomes, Kae1 and Bud32 are fused. The complex is homologous to the Kae1 and Bud32 subunits of the eukaryotic KEOPS complex, an apparently ancient protein kinase-containing molecular machine. [Unknown function, General]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169379075  83 EQTRcaQEFQLLLTLINAGVHVPRPiaaravksgltYQAD-----LLSERIpNARDLVSILQEKPLpeGMYQKIGQEIAK 157
Cdd:TIGR03724  42 ERTR--REARLLSRARKAGVNTPVI-----------YDVDpdnktIVMEYI-EGKPLKDVIEENGD--ELAREIGRLVGK 105

                          90       100
                  ....*....|....*....|....*....
gi 1169379075 158 MHNAGVNHTDLNIHNILIDDkDKVWIIDF 186
Cdd:TIGR03724 106 LHKAGIVHGDLTTSNIIVRD-DKVYLIDF 133

Lipopolysaccharide kinase (Kdo/WaaP) family; These lipopolysaccharide kinases are related to protein kinases pfam00069. This family includes waaP (rfaP) gene product is required for the addition of phosphate to O-4 of the first heptose residue of the lipopolysaccharide (LPS) inner core region. It has previously been shown that WaaP is necessary for resistance to hydrophobic and polycationic antimicrobials in E. coli and that it is required for virulence in invasive strains of S. enterica.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169379075  30 EYWQSTNKVTGSASGRGTTWFVQLDTMQAALRHYRRGGLFGKLVKDNYLFSGwEQTRCAQEFQLLLTLINAGVHVPRPIA 109
Cdd:pfam06293   1 AWWALQGRVVGEPNGRRTGWFVVARVGNGVLRKYYRGGMWGHLNRDLYRYPL-GRTRAFREFRLIRRLREAGLPVPKPVA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169379075 110 ARAVKSGLTYQADLLSERIPNARDLVSILQEKPLPEG-----MYQKIGQEIAKMHNAGVNHTDLNIHNILID----DKDK 180
Cdd:pfam06293  80 AGEVKVGGGYRADLLTERLEGAQSLADWLADWAVPSGelrraIWEAVGRLIRQMHRAGVQHGDLYAHHILLQqegdEGFE 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1169379075 181 VWIIDFDKCRKQEHGD-WKKQNLERLLRSFKKellkrqIHWKERDFAVLTEA 231
Cdd:pfam06293 160 AWLIDLDKGRLRLPARrWRNKDLARLLRSFLN------IGFTEADWERLLRA 205

tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and biogenesis]; tRNA A-37 threonylcarbamoyl transferase component Bud32 is part of the Pathway/BioSystem: tRNA modification

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169379075  85 TRCAQEFQLLLTLINAGVHVPRPIAARAVKsgltyqADLLSERIPNaRDLVSILQEKPLPEGMYQKIGQEIAKMHNAGVN 164
Cdd:COG3642     1 ERTRREARLLRELREAGVPVPKVLDVDPDD------ADLVMEYIEG-ETLADLLEEGELPPELLRELGRLLARLHRAGIV 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1169379075 165 HTDLNIHNILIDDkDKVWIIDFDKCRKQEHGDWKKQNLERLLRSFKKE 212
Cdd:COG3642    74 HGDLTTSNILVDD-GGVYLIDFGLARYSDPLEDKAVDLAVLKRSLEST 120

RIO-like kinase;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169379075   90 EFQLLLTLINAGVHVPRPIAARavKSGLTyqADLLSERIPNARDLVSILQEKPLPEGMYQKIGQEIAKM-HNAGVNHTDL 168
Cdd:smart00090 100 EFRNLQRLYEAGVPVPKPIAWR--RNVLV--MEFIGGDGLPAPRLKDVEPEEEEEFELYDDILEEMRKLyKEGELVHGDL 175

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1169379075  169 NIHNILIDDkDKVWIIDFDKCRKQEHGDWkKQNLER----LLRSFKK 211
Cdd:smart00090 176 SEYNILVHD-GKVVIIDVSQSVELDHPMA-LEFLERdirnIIRFFRR 220

Catalytic domain of the atypical protein serine kinases, RIO1 and RIO3 kinases and similar proteins; RIO1 is present in archaea, bacteria and eukaryotes. In addition, RIO3 is present in multicellular eukaryotes. Both RIO1 and RIO3 are associated with precursors of 40S ribosomal subunits, just like RIO2. RIO1 is essential for survival and is required for 18S rRNA processing, proper cell cycle progression and chromosome maintenance. Although depletion of either RIO1 and RIO2 results in similar effects, the two kinases are not fully interchangeable. The specific function of RIO3 is unknown. RIO kinases are atypical protein serine kinases containing a kinase catalytic signature, but otherwise show very little sequence similarity to typical PKs. Serine kinases catalyze the transfer of the gamma-phosphoryl group from ATP to serine residues in protein substrates. The RIO catalytic domain is truncated compared to the catalytic domains of typical PKs, with deletions of the loops responsible for substrate binding. The RIO kinase catalytic domain family is part of a larger superfamily, that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169379075  90 EFQLLLTLINAGVHVPRPIAARA---VKSGLTYQ---ADLLSEripnardlVSILQEKplPEGMYQKIGQEIAKM-HNAG 162
Cdd:cd05145    68 EFRNLKRLYEAGVRVPEPIAVYRnvlVMEFIGDDgspAPRLKD--------VELEEED--AEELYEQVVEQMRRMyCKAG 137

                          90       100
                  ....*....|....*....|....
gi 1169379075 163 VNHTDLNIHNILIDDkDKVWIIDF 186
Cdd:cd05145   138 LVHGDLSEYNILYYD-GKPVIIDV 160

Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated with Kae1 (kinase-associated endopeptidase 1) in the Archaea. In many Archaeal genomes, Kae1 and Bud32 are fused. The complex is homologous to the Kae1 and Bud32 subunits of the eukaryotic KEOPS complex, an apparently ancient protein kinase-containing molecular machine. [Unknown function, General]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169379075  83 EQTRcaQEFQLLLTLINAGVHVPRPiaaravksgltYQAD-----LLSERIpNARDLVSILQEKPLpeGMYQKIGQEIAK 157
Cdd:TIGR03724  42 ERTR--REARLLSRARKAGVNTPVI-----------YDVDpdnktIVMEYI-EGKPLKDVIEENGD--ELAREIGRLVGK 105

                          90       100
                  ....*....|....*....|....*....
gi 1169379075 158 MHNAGVNHTDLNIHNILIDDkDKVWIIDF 186
Cdd:TIGR03724 106 LHKAGIVHGDLTTSNIIVRD-DKVYLIDF 133

Kae1-associated kinase Bud32;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169379075  82 WEQTRcaQEFQLLLTLINAGVHVPRPiaaravksgltYQAD-----LLSERIPNARdLVSILQEKPLPEGMYQK-IGQEI 155
Cdd:PRK14879   43 RERTR--REARIMSRARKAGVNVPAV-----------YFVDpenfiIVMEYIEGEP-LKDLINSNGMEELELSReIGRLV 108

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1169379075 156 AKMHNAGVNHTDLNIHNILIDDkDKVWIIDF 186
Cdd:PRK14879  109 GKLHSAGIIHGDLTTSNMILSG-GKIYLIDF 138

Spore coat protein CotI/CotS, protein kinase superfamily [Cell cycle control, cell division, chromosome partitioning];

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1169379075 148 YQKIGQEIAKmhNAGVNHTDLNIHNILIDDKDKVWIIDFDKCR 190
Cdd:COG5881   190 YYKLVKEAKK--EGGFCHHDYAYHNILIDEDGKIYIIDFDYCI 230

Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ChoK, ethanolamine kinase (ETNK), macrolide 2'-phosphotransferase (MPH2'), an unusual homoserine kinase, and uncharacterized proteins with similarity to the N-terminal domain of acyl-CoA dehydrogenase 10 (ACAD10). The members of this family catalyze the transfer of the gamma-phosphoryl group from ATP (or CTP) to small molecule substrates such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine. Phosphorylation of the antibiotics, aminoglycosides and macrolides, leads to their inactivation and to bacterial antibiotic resistance. Phosphorylation of choline, ethanolamine, and homoserine serves as precursors to the synthesis of important biological compounds, such as the major phospholipids, phosphatidylcholine and phosphatidylethanolamine and the amino acids, threonine, methionine, and isoleucine. The APH/ChoK family is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169379075  99 NAGVHVPRPIAARAVKsGLTYqadLLSERIP--NARDLVSILQEKPlPEGMYQKIGQEIAKMHNA---GVNHTDLNIHNI 173
Cdd:cd05120    49 KLSLPVPKVYGFGESD-GWEY---LLMERIEgeTLSEVWPRLSEEE-KEKIADQLAEILAALHRIdssVLTHGDLHPGNI 123

                          90
                  ....*....|....*...
gi 1169379075 174 LIDDKDKV-WIIDFDKCR 190
Cdd:cd05120   124 LVKPDGKLsGIIDWEFAG 141

Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. PKs make up a large family of serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and more than 500 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169379075 123 LLSERIPNaRDLVSILQE--KPLPEGMYQKIGQEIAK----MHNAGVNHTDLNIHNILIDDKDKVWIIDFDKCRKQEHGD 196
Cdd:cd00180    68 LVMEYCEG-GSLKDLLKEnkGPLSEEEALSILRQLLSaleyLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDLDSDD 146

                  ....
gi 1169379075 197 WKKQ 200
Cdd:cd00180   147 SLLK 150

Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of yeast Kin1, Kin2, and similar proteins. Fission yeast Kin1 is a membrane-associated kinase that is involved in regulating cell surface cohesiveness during interphase. It also plays a role during mitosis, linking actomyosin ring assembly with septum synthesis and membrane closure to ensure separation of daughter cells. Budding yeast Kin1 and Kin2 act downstream of the Rab-GTPase Sec4 and are associated with the exocytic apparatus; they play roles in the secretory pathway. The Kin1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1169379075 123 LLSERIPNARDLVSILQEKPLPEGMYQKIGQEIAK----MHNAGVNHTDLNIHNILIDDKDKVWIIDF 186
Cdd:cd14077    90 MLFEYVDGGQLLDYIISHGKLKEKQARKFARQIASaldyLHRNSIVHRDLKIENILISKSGNIKIIDF 157

Serine/threonine protein kinase [Signal transduction mechanisms];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169379075  71 KLVKDNYLFSGWEQTRCAQEFQLLLTLinAGVHVPRPIAArAVKSGLTYqadLLSERIPnARDLVSILQEK-PLPEGMYQ 149
Cdd:COG0515    38 KVLRPELAADPEARERFRREARALARL--NHPNIVRVYDV-GEEDGRPY---LVMEYVE-GESLADLLRRRgPLPPAEAL 110

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1169379075 150 KIGQEIAK----MHNAGVNHTDLNIHNILIDDKDKVWIIDF 186
Cdd:COG0515   111 RILAQLAEalaaAHAAGIVHRDIKPANILLTPDGRVKLIDF 151

Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169379075 132 RDLVSILQE-KPLPEGMYQKIGQEIAK----MHNAGVNHTDLNIHNILIDDKDKVWIIDF 186
Cdd:cd14014    85 GSLADLLRErGPLPPREALRILAQIADalaaAHRAGIVHRDIKPANILLTEDGRVKLTDF 144

Predicted Ser/Thr protein kinase [Signal transduction mechanisms];

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1169379075 157 KMHNAGVNHTDLNI--HNILIDdKDKVWIIDFDKCRKQEhgdwKKQNLERLL-----RSFKKELLKRQIHWKERDF 225
Cdd:COG2112   142 LLDRIGIDHGELSRpgKHVIVD-KGRPYIIDFESASISR----KPSNVTSALsylflGSNIAKRIKKILGLDKEKL 212

Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MELK is a cell cycle dependent protein which functions in cytokinesis, cell cycle, apoptosis, cell proliferation, and mRNA processing. It is found upregulated in many types of cancer cells, playing an indispensable role in cancer cell survival. It makes an attractive target in the design of inhibitors for use in the treatment of a wide range of human cancer. The MELK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1169379075 146 GMYQKIGQEIAKMHNAGVNHTDLNIHNILIDDKDKVWIIDFDKCRKQEHGdwKKQNLE 203
Cdd:cd14078   105 VFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLCAKPKGG--MDHHLE 160

Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic choline kinases, as well as eukaryotic ethanolamine kinase. ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP (or CTP) to its substrate, choline, producing phosphorylcholine (PCho), a precursor to the biosynthesis of two major membrane phospholipids, phosphatidylcholine (PC), and sphingomyelin (SM). Although choline is the preferred substrate, ChoK also shows substantial activity towards ethanolamine and its N-methylated derivatives. Bacterial ChoK is also referred to as licA protein. ETNK catalyzes the transfer of the gamma-phosphoryl group from CTP to ethanolamine (Etn), the first step in the CDP-Etn pathway for the formation of the major phospholipid, phosphatidylethanolamine (PtdEtn). Unlike ChoK, ETNK shows specific activity for its substrate and displays negligible activity towards N-methylated derivatives of Etn. ChoK plays an important role in cell signaling pathways and the regulation of cell growth. The ChoK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169379075 123 LLSERIPNARdlvsILQEKPLPEGMYQKIGQEIAKMHNAGVN-----HTDLNIHNILIDDkDKVWIIDFD 187
Cdd:cd05151    68 KITEFIEGAT----LLTNDFSDPENLERIAALLRKLHSSPLEdlvlcHNDLVPGNFLLDD-DRLYLIDWE 132

Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SBK1, also called BSK146, is predominantly expressed in the brain. Its expression is increased in the developing brain during the late embryonic stage, coinciding with dramatic neuronal proliferation, migration, and maturation. SBK1 may play an important role in regulating brain development. The SBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169379075 131 ARDLVSILQ-EKPLPEGMYQKIGQEIAK----MHNAGVNHTDLNIHNILIDDKD--KVWIIDFDKCRKQ 192
Cdd:cd13987    75 YGDLFSIIPpQVGLPEERVKRCAAQLASaldfMHSKNLVHRDIKPENVLLFDKDcrRVKLCDFGLTRRV 143

Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. It phosphorylates Cre-Responsive Element Binding protein (CREB), facilitating the binding of CREB to the specific cis cAMP responsive element (CRE), which is important in activating genes related to germ cell differentiation. Mutations in the human TSSK4 gene is associated with infertile Chinese men with impaired spermatogenesis. The TSSK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.

                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1169379075 155 IAKMHNAGVNHTDLNIHNILIDDKDKVWIIDFDKCRKQ 192
Cdd:cd14162   113 VEYCHSKGVVHRDLKCENLLLDKNNNLKITDFGFARGV 150

Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. TSSK6, also called SSTK, is expressed at the head of elongated sperm. TSSK1/TSSK2 double knock-out and TSSK6 null mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169379075 137 ILQEKPLPEG----MYQKIGQEIAKMHNAGVNHTDLNIHNILIDDKDKVWIIDFD---KCRKQEHGD 196
Cdd:cd14080    93 IQKRGALSESqariWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFGfarLCPDDDGDV 159

Thiamine kinase or a related kinase [Coenzyme transport and metabolism];

                          10        20
                  ....*....|....*....|....*
gi 1169379075 163 VNHTDLNIHNILIDDKDKVWIIDFD 187
Cdd:COG0510    51 LCHGDLHPGNFLVTDDGRLYLIDWE 75

Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of HAL4, Saccharomyces cerevisiae Ptk2/Stk2, and similar fungal proteins. Proteins in this subfamily are involved in regulating ion transporters. In budding and fission yeast, HAL4 promotes potassium ion uptake, which increases cellular resistance to other cations such as sodium, lithium, and calcium ions. HAL4 stabilizes the major high-affinity K+ transporter Trk1 at the plasma membrane under low K+ conditions, which prevents endocytosis and vacuolar degradation. Budding yeast Ptk2 phosphorylates and regulates the plasma membrane H+ ATPase, Pma1. The HAL4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.

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gi 1169379075 147 MYQKIGQEIAKMHNAGVNHTDLNIHNILIDDKDKVWIIDFDKC 189
Cdd:cd13994   103 FFKQILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGTA 145