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Conserved domains on  [gi|17232770|ref|NP_489318|]
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serine/threonine kinase [Nostoc sp. PCC 7120]

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List of domain hits

Name Accession Description Interval E-value
PKc cd00180
Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze ...
40-289 6.65e-45

Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. 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. PKs make up a large family of serine/threonine kinases, protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation, about 95%, 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 550 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.


:

Pssm-ID: 173623 [Multi-domain]  Cd Length: 215  Bit Score: 155.47  E-value: 6.65e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770  40 IGQGGFGRTFLAvdEDKPSKPRCVIKQFYPQAQGTNtvqkaVELFTQEAVQLDELgKHPQIPELLAYFTQDDRQYLVQEF 119
Cdd:cd00180   1 LGEGGFGTVYLA--RDKKTGKKVAIKIIKKEDSSSL-----LEELLREIEILKKL-NHPNIVKLYGVFEDENHLYLVMEY 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770 120 IDGLNLAQELAHK-GVFQETHIIQLLNDLLPVLQFCHNRQVIHRDIKPENIILRNSDNKLVVVDFGASKSATNTaLNHTG 198
Cdd:cd00180  73 CEGGSLKDLLKENeGKLSEDEILRILLQILEGLEYLHSNGIIHRDLKPENILLDSDNGKVKLADFGLSKLLTSD-KSLLK 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770 199 TSIGSPEYVAPEQMRGRAI--FASDIYSLGVTCINLltgrspfdsydtnndtwiwqqylkppvsNHLHKIINKMTASVPA 276
Cdd:cd00180 152 TIVGTPAYMAPEVLLGKGYysEKSDIWSLGVILYEL----------------------------PELKDLIRKMLQKDPE 203
                       250
                ....*....|...
gi 17232770 277 RRYqNVEEVLKDL 289
Cdd:cd00180 204 KRP-SAKEILEHL 215
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
34-288 3.60e-51

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


:

Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 173.10  E-value: 3.60e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770     34 YRAIKPIGQGGFGRTFLAVDedKPSKPRCVIKQFYPQAQgtntvQKAVELFTQEAVQLDELgKHPQIPELLAYFTQDDRQ 113
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARD--KKTGKLVAIKVIKKKKI-----KKDRERILREIKILKKL-KHPNIVRLYDVFEDEDKL 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770    114 YLVQEFIDGLNLAQELAHKGVFQETHIIQLLNDLLPVLQFCHNRQVIHRDIKPENIILrNSDNKLVVVDFGASKSATNTa 193
Cdd:smart00220  73 YLVMEYCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILL-DEDGHVKLADFGLARQLDPG- 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770    194 lNHTGTSIGSPEYVAPEQMRGRAI-FASDIYSLGVTCINLLTGRSPFdsYDTNNDTWIWQQYLKPP---------VSNHL 263
Cdd:smart00220 151 -EKLTTFVGTPEYMAPEVLLGKGYgKAVDIWSLGVILYELLTGKPPF--PGDDQLLELFKKIGKPKppfpppewdISPEA 227
                          250       260
                   ....*....|....*....|....*
gi 17232770    264 HKIINKMTASVPARRYqNVEEVLKD 288
Cdd:smart00220 228 KDLIRKLLVKDPEKRL-TAEEALQH 251
 
Name Accession Description Interval E-value
PKc cd00180
Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze ...
40-289 6.65e-45

Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. 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. PKs make up a large family of serine/threonine kinases, protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation, about 95%, 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 550 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.


Pssm-ID: 173623 [Multi-domain]  Cd Length: 215  Bit Score: 155.47  E-value: 6.65e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770  40 IGQGGFGRTFLAvdEDKPSKPRCVIKQFYPQAQGTNtvqkaVELFTQEAVQLDELgKHPQIPELLAYFTQDDRQYLVQEF 119
Cdd:cd00180   1 LGEGGFGTVYLA--RDKKTGKKVAIKIIKKEDSSSL-----LEELLREIEILKKL-NHPNIVKLYGVFEDENHLYLVMEY 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770 120 IDGLNLAQELAHK-GVFQETHIIQLLNDLLPVLQFCHNRQVIHRDIKPENIILRNSDNKLVVVDFGASKSATNTaLNHTG 198
Cdd:cd00180  73 CEGGSLKDLLKENeGKLSEDEILRILLQILEGLEYLHSNGIIHRDLKPENILLDSDNGKVKLADFGLSKLLTSD-KSLLK 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770 199 TSIGSPEYVAPEQMRGRAI--FASDIYSLGVTCINLltgrspfdsydtnndtwiwqqylkppvsNHLHKIINKMTASVPA 276
Cdd:cd00180 152 TIVGTPAYMAPEVLLGKGYysEKSDIWSLGVILYEL----------------------------PELKDLIRKMLQKDPE 203
                       250
                ....*....|...
gi 17232770 277 RRYqNVEEVLKDL 289
Cdd:cd00180 204 KRP-SAKEILEHL 215
KIND smart00750
kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to ...
151-286 1.45e-06

kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to the C-terminal protein kinase catalytic fold (C lobe). Its presence at the N terminus of signalling proteins and the absence of the active-site residues in the catalytic and activation loops suggest that it folds independently and is likely to be non-catalytic. The occurrence of KIND only in metazoa implies that it has evolved from the catalytic protein kinase domain into an interaction domain possibly by keeping the substrate-binding features


Pssm-ID: 214801  Cd Length: 176  Bit Score: 46.62  E-value: 1.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770    151 LQFCHNRQVIHRDIKPENIILRNSdnkLVVVDFGASKSATNTalnhtgTSIGSPEYVAPEQMRGRAI-FASDIYSLGVTC 229
Cdd:smart00750  24 LQCLGALRELHRQAKSGNILLTWD---GLLKLDGSVAFKTPE------QSRPDPYFMAPEVIQGQSYtEKADIYSLGITL 94
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 17232770    230 INLLTGRSPfdsydtnndtwiwqQYLKPPVSNHLHKIINKMTASVPARRyQNVEEVL 286
Cdd:smart00750  95 YEALDYELP--------------YNEERELSAILEILLNGMPADDPRDR-SNLEGVS 136
Choline_kinase pfam01633
Choline/ethanolamine kinase; Choline kinase catalyses the committed step in the synthesis of ...
142-183 2.39e-04

Choline/ethanolamine kinase; Choline kinase catalyses the committed step in the synthesis of phosphatidylcholine by the CDP-choline pathway. This alignment covers the protein kinase portion of the protein. The divergence of this family makes it very difficult to create a model that specifically predicts choline/ethanolamine kinases only.


Pssm-ID: 250759  Cd Length: 208  Bit Score: 40.72  E-value: 2.39e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 17232770   142 QLLNDLLPVLQFCHNrqvihrDIKPENIILRNSDNKLVVVDF 183
Cdd:pfam01633 132 KLLENLESPIVFCHN------DLQPGNILLLESTNRLVLIDF 167
PRK14879 PRK14879
serine/threonine protein kinase; Provisional
115-187 1.08e-03

serine/threonine protein kinase; Provisional


Pssm-ID: 237847  Cd Length: 211  Bit Score: 38.73  E-value: 1.08e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17232770  115 LVQEFIDGLNLAQELAHKGVFQEtHIIQLLNDLLPVLqfcHNRQVIHRDIKPENIILrnSDNKLVVVDFGASK 187
Cdd:PRK14879  76 IVMEYIEGEPLKDLINSNGMEEL-ELSREIGRLVGKL---HSAGIIHGDLTTSNMIL--SGGKIYLIDFGLAE 142
AarF COG0661
Predicted unusual protein kinase [General function prediction only]
82-186 1.60e-03

Predicted unusual protein kinase [General function prediction only]


Pssm-ID: 223733  Cd Length: 517  Bit Score: 38.83  E-value: 1.60e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770  82 EL-FTQEAVQLDELGKH----PQ--IPELLAYFTQddRQYLVQEFIDGLNLAQELAHK-GVFQETHIIQLLNDLLpvlqf 153
Cdd:COG0661 205 ELdYRREAANAERFRENfkddPDvyVPKVYWEYTT--RRVLTMEWIDGIKISDIAALKsAGIDRKELAELLVRAF----- 277
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 17232770 154 chNRQVI-----HRDIKPENIILRnSDNKLVVVDFGAS 186
Cdd:COG0661 278 --LRQLLrdgffHADPHPGNILVR-SDGRIVLLDFGIV 312
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
106-187 1.82e-03

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].


Pssm-ID: 234331  Cd Length: 199  Bit Score: 37.97  E-value: 1.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770   106 YFTQDDRQYLVQEFIDGLNLAQELahkgvfqETHIIQLLNDLLPVLQFCHNRQVIHRDIKPENIILRnsDNKLVVVDFGA 185
Cdd:TIGR03724  65 YDVDPDNKTIVMEYIEGKPLKDVI-------EEGNDELLREIGRLVGKLHKAGIVHGDLTTSNIIVR--DDKLYLIDFGL 135

                  ..
gi 17232770   186 SK 187
Cdd:TIGR03724 136 GK 137
PHA02882 PHA02882
putative serine/threonine kinase; Provisional
140-184 3.65e-03

putative serine/threonine kinase; Provisional


Pssm-ID: 165211  Cd Length: 294  Bit Score: 37.62  E-value: 3.65e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 17232770  140 IIQLLNDLLPVLQFCHNRQVIHRDIKPENIILrNSDNKLVVVDFG 184
Cdd:PHA02882 128 IKNIMKDMLTTLEYIHEHGISHGDIKPENIMV-DGNNRGYIIDYG 171
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
34-288 3.60e-51

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 173.10  E-value: 3.60e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770     34 YRAIKPIGQGGFGRTFLAVDedKPSKPRCVIKQFYPQAQgtntvQKAVELFTQEAVQLDELgKHPQIPELLAYFTQDDRQ 113
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARD--KKTGKLVAIKVIKKKKI-----KKDRERILREIKILKKL-KHPNIVRLYDVFEDEDKL 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770    114 YLVQEFIDGLNLAQELAHKGVFQETHIIQLLNDLLPVLQFCHNRQVIHRDIKPENIILrNSDNKLVVVDFGASKSATNTa 193
Cdd:smart00220  73 YLVMEYCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILL-DEDGHVKLADFGLARQLDPG- 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770    194 lNHTGTSIGSPEYVAPEQMRGRAI-FASDIYSLGVTCINLLTGRSPFdsYDTNNDTWIWQQYLKPP---------VSNHL 263
Cdd:smart00220 151 -EKLTTFVGTPEYMAPEVLLGKGYgKAVDIWSLGVILYELLTGKPPF--PGDDQLLELFKKIGKPKppfpppewdISPEA 227
                          250       260
                   ....*....|....*....|....*
gi 17232770    264 HKIINKMTASVPARRYqNVEEVLKD 288
Cdd:smart00220 228 KDLIRKLLVKDPEKRL-TAEEALQH 251
SPS1 COG0515
Serine/threonine protein kinase [General function prediction only / Signal transduction ...
34-359 7.34e-52

Serine/threonine protein kinase [General function prediction only / Signal transduction mechanisms / Transcription / DNA replication, recombination, and repair]


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 178.78  E-value: 7.34e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770  34 YRAIKPIGQGGFGRTFLAVDedkpsKPRCVIKQFYPQAQGTNtvqKAVELFTQEAVQLDELGKHPQIPELLAYFTQDDRQ 113
Cdd:COG0515   2 YRILRKLGEGSFGEVYLARD-----RKLVALKVLAKKLESKS---KEVERFLREIQILASLNHPPNIVKLYDFFQDEGSL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770 114 YLVQEFIDGLNLAQELAH---KGVFQETHIIQLLNDLLPVLQFCHNRQVIHRDIKPENIILRNSDNKLVVVDFGASKSAT 190
Cdd:COG0515  74 YLVMEYVDGGSLEDLLKKigrKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGRVVKLIDFGLAKLLP 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770 191 N-----TALNHTGTSIGSPEYVAPEQMRG----RAIFASDIYSLGVTCINLLTGRSPFDSYD----------------TN 245
Cdd:COG0515 154 DpgstsSIPALPSTSVGTPGYMAPEVLLGlslaYASSSSDIWSLGITLYELLTGLPPFEGEKnssatsqtlkiilelpTP 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770 246 NDTWIWQQYLKPPVSNHLHKIINKMTASVPARRYQNVEEVLKDLNQYSPVVNTPAKSSHQPPQIPSPQPVSKSQSQIDLE 325
Cdd:COG0515 234 SLASPLSPSNPELISKAASDLLKKLLAKDPKNRLSSSSDLSHDLLAHLKLKESDLSDLLKPDDSAPLRLSLPPSLEALIS 313
                       330       340       350
                ....*....|....*....|....*....|....
gi 17232770 326 LEELKTQFLPGGKSKPQNIQPQPATNNNAAKSEI 359
Cdd:COG0515 314 SLNSLAISGSDLKLDDSNFSKELAPNGVSSSPHN 347
Pkinase pfam00069
Protein kinase domain;
34-288 4.09e-43

Protein kinase domain;


Pssm-ID: 249558 [Multi-domain]  Cd Length: 260  Bit Score: 152.02  E-value: 4.09e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770    34 YRAIKPIGQGGFGRTFLAVDEDKPSkpRCVIKQFYPQAQGTNTVQKAVelftQEAVQLDELgKHPQIPELLAYFTQDDRQ 113
Cdd:pfam00069   1 YELLRKLGSGSFGTVYKAKHKGTGK--IVAVKILKKRSEKSKKDQTAR----REIRILRRL-SHPNIVRLIDAFEDKDHL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770   114 YLVQEFIDGLNLAQELAHKGVFQETHIIQLLNDLLPVLQFCHNRQVIHRDIKPENIILrNSDNKLVVVDFGASKSATNTA 193
Cdd:pfam00069  74 YLVMEYCEGGDLFDYLSRGGPLSEDEAKKIALQILRGLEYLHSNGIIHRDLKPENILL-DENGVVKIADFGLAKKLTKSS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770   194 LNHTgTSIGSPEYVAPEQMRGR--AIFASDIYSLGVTCINLLTGRSPFDSYDTNNDTWIWQQYLKPPVSNH--------- 262
Cdd:pfam00069 153 SSLT-TFVGTPEYMAPEVLLGGngYGPKVDVWSLGVILYELLTGKPPFSGESILDQLQLIRRILGPPLEFDepksdsgse 231
                         250       260
                  ....*....|....*....|....*..
gi 17232770   263 -LHKIINKMTASVPARRYqNVEEVLKD 288
Cdd:pfam00069 232 eAKDLIKKCLNKDPSKRP-TAEEILQH 257
pknD PRK13184
serine/threonine-protein kinase; Reviewed
32-292 4.87e-23

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 99.84  E-value: 4.87e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770   32 ERYRAIKPIGQGGFGRTFLAvdEDKPSKPRCVIKQFYPQAQGTNTVQKAvelFTQEAVQLDELgKHPQIPELLAYFTQDD 111
Cdd:PRK13184   2 QRYDIIRLIGKGGMGEVYLA--YDPVCSRRVALKKIREDLSENPLLKKR---FLREAKIAADL-IHPGIVPVYSICSDGD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770  112 RQYLVQEFIDGLNLAQELahKGVFQ------ETHIIQLLNDLLPV-------LQFCHNRQVIHRDIKPENIILrNSDNKL 178
Cdd:PRK13184  76 PVYYTMPYIEGYTLKSLL--KSVWQkeslskELAEKTSVGAFLSIfhkicatIEYVHSKGVLHRDLKPDNILL-GLFGEV 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770  179 VVVDFGASKS-----------------ATNTALNHTGTSIGSPEYVAPEQMRGR-AIFASDIYSLGVTCINLLTGRSPFD 240
Cdd:PRK13184 153 VILDWGAAIFkkleeedlldidvdernICYSSMTIPGKIVGTPDYMAPERLLGVpASESTDIYALGVILYQMLTLSFPYR 232
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770  241 SYDTNNdtWIWQQYLKPP--VSNH------LHKIINKMTASVPARRYQNVEEVLKDLNQY 292
Cdd:PRK13184 233 RKKGRK--ISYRDVILSPieVAPYreippfLSQIAMKALAVDPAERYSSVQELKQDLEPH 290
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
97-260 2.76e-22

TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, in multiple species of Burkholderia, in Acidovorax avenae subsp. citrulli AAC00-1 and Delftia acidovorans SPH-1, and in multiple copies in Sorangium cellulosum, in genomic neighborhoods that include a cyclodehydratase/docking scaffold fusion protein (TIGR03882) and a member of the thiazole/oxazole modified metabolite (TOMM) precursor family TIGR03795. It has a kinase domain in the N-terminal 300 amino acids, followed by a cyclase homology domain, followed by regions without named domain definitions. It is a probable bacteriocin-like metabolite biosynthesis protein [Cellular processes, Toxin production and resistance].


Pssm-ID: 234389 [Multi-domain]  Cd Length: 1266  Bit Score: 97.61  E-value: 2.76e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770     97 HPQIPELL-AYFTQDDRQYLVQEFIDGLNLAQELAHKGVFQETHIIQLLNDLLPVLQFCHNRQVIHRDIKPENIILRNSD 175
Cdd:TIGR03903   37 HPNIVALLdSGEAPPGLLFAVFEYVPGRTLREVLAADGALPAGETGRLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTG 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770    176 NK--LVVVDFGAS------KSATNTALNHTGTSIGSPEYVAPEQMRGRAIFA-SDIYSLGVTCINLLTGRSPFDSYDTNN 246
Cdd:TIGR03903  117 VRphAKVLDFGIGtllpgvRDADVATLTRTTEVLGTPTYCAPEQLRGEPVTPnSDLYAWGLIFLECLTGQRVVQGASVAE 196
                          170
                   ....*....|....*
gi 17232770    247 dtwIWQQYLKP-PVS 260
Cdd:TIGR03903  197 ---ILYQQLSPvDVS 208
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
40-239 1.23e-19

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 87.18  E-value: 1.23e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770   40 IGQGGFGRTFLAvdEDKPSKPRCVIKQFYPQAQgtnTVQKAVELFTQEAVQLDELgKHPQIPELLAYFTQDDRQYLVQEF 119
Cdd:PTZ00263  26 LGTGSFGRVRIA--KHKGTGEYYAIKCLKKREI---LKMKQVQHVAQEKSILMEL-SHPFIVNMMCSFQDENRVYFLLEF 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770  120 IDGLNLAQELAHKGVFQETHIIQLLNDLLPVLQFCHNRQVIHRDIKPENIILrNSDNKLVVVDFGASKSATntalNHTGT 199
Cdd:PTZ00263 100 VVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLL-DNKGHVKVTDFGFAKKVP----DRTFT 174
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 17232770  200 SIGSPEYVAPE--QMRGRAIfASDIYSLGVTCINLLTGRSPF 239
Cdd:PTZ00263 175 LCGTPEYLAPEviQSKGHGK-AVDWWTMGVLLYEFIAGYPPF 215
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
97-239 1.86e-13

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 69.47  E-value: 1.86e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770   97 HPQIPELLAYFTQDDRQYLVQEFIDGLNLaqELAHkgVFQETHIIQLLNDLLPVLQFCHNRQVIHRDIKPENIILrNSDN 176
Cdd:PLN00034 131 HPNVVKCHDMFDHNGEIQVLLEFMDGGSL--EGTH--IADEQFLADVARQILSGIAYLHRRHIVHRDIKPSNLLI-NSAK 205
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17232770  177 KLVVVDFGASKSATNTaLNHTGTSIGSPEYVAPEQM-----RGRAI-FASDIYSLGVTCINLLTGRSPF 239
Cdd:PLN00034 206 NVKIADFGVSRILAQT-MDPCNSSVGTIAYMSPERIntdlnHGAYDgYAGDIWSLGVSILEFYLGRFPF 273
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
107-271 5.99e-13

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 66.80  E-value: 5.99e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770  107 FTQDDRQYLVQEFIDGLNLAQELAHKGVFQET---HII-QL---LNDLlpvlqfcHNRQVIHRDIKPENIILRNSDNKLV 179
Cdd:PHA03390  78 VTTLKGHVLIMDYIKDGDLFDLLKKEGKLSEAevkKIIrQLveaLNDL-------HKHNIIHNDIKLENVLYDRAKDRIY 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770  180 VVDFGASKSAtNTALNHTGTSigspEYVAPEQMRGRAIFAS-DIYSLGVTCINLLTGRSPFDSYDTNN---DTWIWQQYL 255
Cdd:PHA03390 151 LCDYGLCKII-GTPSCYDGTL----DYFSPEKIKGHNYDVSfDWWAVGVLTYELLTGKHPFKEDEDEEldlESLLKRQQK 225
                        170       180
                 ....*....|....*....|
gi 17232770  256 KPP----VSNHLHKIINKMT 271
Cdd:PHA03390 226 KLPfiknVSKNANDFVQSML 245
 
Name Accession Description Interval E-value
PKc cd00180
Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze ...
40-289 6.65e-45

Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. 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. PKs make up a large family of serine/threonine kinases, protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation, about 95%, 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 550 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.


Pssm-ID: 173623 [Multi-domain]  Cd Length: 215  Bit Score: 155.47  E-value: 6.65e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770  40 IGQGGFGRTFLAvdEDKPSKPRCVIKQFYPQAQGTNtvqkaVELFTQEAVQLDELgKHPQIPELLAYFTQDDRQYLVQEF 119
Cdd:cd00180   1 LGEGGFGTVYLA--RDKKTGKKVAIKIIKKEDSSSL-----LEELLREIEILKKL-NHPNIVKLYGVFEDENHLYLVMEY 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770 120 IDGLNLAQELAHK-GVFQETHIIQLLNDLLPVLQFCHNRQVIHRDIKPENIILRNSDNKLVVVDFGASKSATNTaLNHTG 198
Cdd:cd00180  73 CEGGSLKDLLKENeGKLSEDEILRILLQILEGLEYLHSNGIIHRDLKPENILLDSDNGKVKLADFGLSKLLTSD-KSLLK 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770 199 TSIGSPEYVAPEQMRGRAI--FASDIYSLGVTCINLltgrspfdsydtnndtwiwqqylkppvsNHLHKIINKMTASVPA 276
Cdd:cd00180 152 TIVGTPAYMAPEVLLGKGYysEKSDIWSLGVILYEL----------------------------PELKDLIRKMLQKDPE 203
                       250
                ....*....|...
gi 17232770 277 RRYqNVEEVLKDL 289
Cdd:cd00180 204 KRP-SAKEILEHL 215
STKc_Nek cd08215
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
33-287 1.85e-38

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related kinase; Serine/Threonine Kinases (STKs), Never In Mitosis gene A (NIMA)-related kinase (Nek) family, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek family 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. The Nek family is composed of 11 different mammalian members (Nek1-11) with similarity to the catalytic domain of Aspergillus nidulans NIMA kinase, the founding member of the Nek family which was identified in a screen for cell cycle mutants that were prevented from entering mitosis. Neks contain a conserved N-terminal catalytic domain and a more divergent C-terminal regulatory region of various sizes and structures. They are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis.


Pssm-ID: 173755 [Multi-domain]  Cd Length: 258  Bit Score: 139.56  E-value: 1.85e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770  33 RYRAIKPIGQGGFGRTFLAvdEDKPSKPRCVIKQFYPQAQGTNTVQKAVelftQEAVQLDELgKHPQIPELLAYFTQDDR 112
Cdd:cd08215   1 KYEIIKQIGKGSFGKVYLV--RRKSDGKLYVLKEIDLSNMSEKEREDAL----NEVKILKKL-NHPNIIKYYESFEEKGK 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770 113 QYLVQEFIDGLNLAQEL---AHKGV-FQETHIIQLLNDLLPVLQFCHNRQVIHRDIKPENIILrNSDNKLVVVDFGASKS 188
Cdd:cd08215  74 LCIVMEYADGGDLSQKIkkqKKEGKpFPEEQILDWFVQLCLALKYLHSRKILHRDIKPQNIFL-TSNGLVKLGDFGISKV 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770 189 ATNTaLNHTGTSIGSPEYVAPEQMRGRAI-FASDIYSLGVTCINLLTGRSPFDSYDTNN--DTWIWQQYlkPPVSNH--- 262
Cdd:cd08215 153 LSST-VDLAKTVVGTPYYLSPELCQNKPYnYKSDIWSLGCVLYELCTLKHPFEGENLLElaLKILKGQY--PPIPSQyss 229
                       250       260
                ....*....|....*....|....*.
gi 17232770 263 -LHKIINKMTASVPARRYqNVEEVLK 287
Cdd:cd08215 230 eLRNLVSSLLQKDPEERP-SIAQILQ 254
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; Protein Kinases (PKs), STE family, catalytic ...
34-239 2.94e-35

Catalytic domain of STE family Protein Kinases; Protein Kinases (PKs), STE family, catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. The STE family is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K). This family is composed of STKs, and some dual-specificity PKs that phosphorylate both threonine and tyrosine residues of target proteins. Most members are kinases involved in mitogen-activated protein kinase (MAPK) signaling cascades, acting as MAPK kinases (MAPKKs), MAPK kinase kinases (MAPKKKs), or MAPK kinase kinase kinases (MAP4Ks). The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPKK, which itself is phosphorylated and activated by a MAPKKK. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAPKKK to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Other STE family members include p21-activated kinases (PAKs) and class III myosins, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain, which can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, as well as autophosphorylate the C-terminal motor domain. They play an important role in maintaining the structural integrity of photoreceptor cell microvilli.


Pssm-ID: 173659 [Multi-domain]  Cd Length: 253  Bit Score: 130.41  E-value: 2.94e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770  34 YRAIKPIGQGGFGRTFLAvdEDKPSKPRCVIKQFYPQaqgtntVQKAVELFTQEaVQLDELGKHPQIPELLAYFTQDDRQ 113
Cdd:cd05122   2 FEILEKIGKGGFGEVYKA--RHKRTGKEVAIKVIKLE------SKEKKEKIINE-IQILKKCKHPNIVKYYGSYLKKDEL 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770 114 YLVQEFIDGLNLAQELAHK-GVFQETHIIQLLNDLLPVLQFCHNRQVIHRDIKPENIILrNSDNKLVVVDFGASKSATNT 192
Cdd:cd05122  73 WIVMEFCSGGSLKDLLKSTnQTLTESQIAYVCKELLKGLEYLHSNGIIHRDIKAANILL-TSDGEVKLIDFGLSAQLSDT 151
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 17232770 193 ALNHtgTSIGSPEYVAPEQMRGRAI-FASDIYSLGVTCINLLTGRSPF 239
Cdd:cd05122 152 KARN--TMVGTPYWMAPEVINGKPYdYKADIWSLGITAIELAEGKPPY 197
STKc_MAPKKK cd06606
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein Kinase ...
38-243 1.83e-33

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase Kinase; Serine/threonine kinases (STKs), mitogen-activated protein kinase (MAPK) kinase kinase (MAPKKK) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MAPKKK 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. MAPKKKs (MKKKs or MAP3Ks) are also called MAP/ERK kinase kinases (MEKKs) in some cases. They phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. This subfamily is composed of the Apoptosis Signal-regulating Kinases ASK1 (or MAPKKK5) and ASK2 (or MAPKKK6), MEKK1, MEKK2, MEKK3, MEKK4, as well as plant and fungal MAPKKKs. Also included in this subfamily are the cell division control proteins Schizosaccharomyces pombe Cdc7 and Saccharomyces cerevisiae Cdc15.


Pssm-ID: 173724 [Multi-domain]  Cd Length: 260  Bit Score: 125.75  E-value: 1.83e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770  38 KPIGQGGFGRTFLAVDEDkpSKPRCVIKQfypqAQGTNTVQKAVELFTQEAVQLDELgKHPQIpelLAYF----TQDDRQ 113
Cdd:cd06606   6 ELLGRGSFGSVYLALDKD--TGELMAVKS----VELSGDSEEELEALEREIRILSSL-QHPNI---VRYYgserDEEKNT 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770 114 Y-LVQEFIDGLNLAQELAHKGVFQETHIIQLLNDLLPVLQFCHNRQVIHRDIKPENIILRNSDN-KLvvVDFGASKS-AT 190
Cdd:cd06606  76 LnIFLEYVSGGSLSSLLKKFGKLPEPVIRKYTRQILEGLAYLHSNGIVHRDIKGANILVDSDGVvKL--ADFGCAKRlGD 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 17232770 191 NTALNHTGTSIGSPEYVAPEQMRG-RAIFASDIYSLGVTCINLLTGRSPFDSYD 243
Cdd:cd06606 154 IETGEGTGSVRGTPYWMAPEVIRGeEYGRAADIWSLGCTVIEMATGKPPWSELG 207
STKc_AGC cd05123
Catalytic domain of AGC family Protein Serine/Threonine Kinases; Serine/Threonine Kinases ...
40-285 6.83e-31

Catalytic domain of AGC family Protein Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), AGC (Protein Kinases A, G and C) family, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The AGC family 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 (PI3K). Members of this family include cAMP-dependent Protein Kinase (PKA), cGMP-dependent Protein Kinase (PKG), Protein Kinase C (PKC), Protein Kinase B (PKB), G protein-coupled Receptor Kinase (GRK), Serum- and Glucocorticoid-induced Kinase (SGK), and 70 kDa ribosomal Protein S6 Kinase (p70S6K or S6K), among others. AGC kinases share an activation mechanism based on the phosphorylation of up to three sites: the activation loop (A-loop), the hydrophobic motif (HM) and the turn motif. Phosphorylation at the A-loop is required of most AGC kinases, which results in a disorder-to-order transition of the A-loop. The ordered conformation results in the access of substrates and ATP to the active site. A subset of AGC kinases with C-terminal extensions containing the HM also requires phosphorylation at this site. Phosphorylation at the HM allows the C-terminal extension to form an ordered structure that packs into the hydrophobic pocket of the catalytic domain, which then reconfigures the kinase into an active bi-lobed state. In addition, growth factor-activated AGC kinases such as PKB, p70S6K, RSK, MSK, PKC, and SGK, require phosphorylation at the turn motif (also called tail or zipper site), located N-terminal to the HM at the C-terminal extension. AGC kinases regulate many cellular processes including division, growth, survival, metabolism, motility, and differentiation. Many are implicated in the development of various human diseases.


Pssm-ID: 173660 [Multi-domain]  Cd Length: 250  Bit Score: 118.39  E-value: 6.83e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770  40 IGQGGFGRTFLAVDEDkpskprcvIKQFYPQAQ--GTNTVQKAVELFTQEAVQLDELGKHPQIPELLAYFTQDDRQYLVQ 117
Cdd:cd05123   1 LGKGSFGKVLLVRKKD--------TGKLYAMKVlkKKKIIKRKEVEHTLTERNILSRINHPFIVKLHYAFQTEEKLYLVL 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770 118 EFIDGLNLAQELAHKGVFQETHIIQLLNDLLPVLQFCHNRQVIHRDIKPENIILrNSDNKLVVVDFGASKSATNTAlNHT 197
Cdd:cd05123  73 EYAPGGELFSHLSKEGRFSEERARFYAAEIVLALEYLHSLGIIYRDLKPENILL-DADGHIKLTDFGLAKELSSEG-SRT 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770 198 GTSIGSPEYVAPEQMRGRAI-FASDIYSLGVTCINLLTGRSPFDSYDTNNdtwIWQQYLK------PPVSNHLHKIINKM 270
Cdd:cd05123 151 NTFCGTPEYLAPEVLLGKGYgKAVDWWSLGVLLYEMLTGKPPFYAEDRKE---IYEKILKdplrfpEFLSPEARDLISGL 227
                       250
                ....*....|....*..
gi 17232770 271 TASVPARRYQN--VEEV 285
Cdd:cd05123 228 LQKDPTKRLGSggAEEI 244
STKc_Sid2p_Dbf2p cd05600
Catalytic domain of Fungal Sid2p- and Dbf2p-like Protein Serine/Threonine Kinases; Serine ...
37-287 5.13e-30

Catalytic domain of Fungal Sid2p- and Dbf2p-like Protein Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), ROCK- and NDR-like subfamily, fungal Sid2p- and Dbf2p-like proteins, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Sid2p- and Dbf2p-like group 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. This group contains fungal kinases including Schizosaccharomyces pombe Sid2p and Saccharomyces cerevisiae Dbf2p. Group members show similarity to NDR kinases in that they contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Sid2p plays a crucial role in the septum initiation network (SIN) and in the initiation of cytokinesis. Dbf2p is important in regulating the mitotic exit network (MEN) and in cytokinesis.


Pssm-ID: 173691 [Multi-domain]  Cd Length: 333  Bit Score: 117.51  E-value: 5.13e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770  37 IKPIGQGGFGRTFLAVDEDkpSKPRCVIKQFYPQaqgtnTVQKAVE---LFTQEAVQLDelGKHPQIPELLAYFTQDDRQ 113
Cdd:cd05600   6 LTQVGQGGYGQVFLAKKKD--TGEIVALKRMKKS-----LLFKLNEvrhVLTERDILTT--TKSEWLVKLLYAFQDDEYL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770 114 YLVQEFIDGLNLAQELAHKGVFQETHIIQLLNDLLPVLQFCHNRQVIHRDIKPENIILrNSDNKLVVVDFGASKSATNTA 193
Cdd:cd05600  77 YLAMEYVPGGDFRTLLNNLGVLSEDHARFYMAEMFEAVDALHELGYIHRDLKPENFLI-DASGHIKLTDFGLSKGIVTYA 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770 194 lnhtGTSIGSPEYVAPEQMRGRAI-FASDIYSLGVTCINLLTGRSPFDSyDTNNDTWI----WQQYLKPPV--------S 260
Cdd:cd05600 156 ----NSVVGSPDYMAPEVLRGKGYdFTVDYWSLGCMLYEFLCGFPPFSG-STPNETWEnlkyWKETLQRPVyddprfnlS 230
                       250       260
                ....*....|....*....|....*..
gi 17232770 261 NHLHKIINKMTASvPARRYQNVEEVLK 287
Cdd:cd05600 231 DEAWDLITKLIND-PSRRFGSLEDIKN 256
STKc_Nek5 cd08225
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
33-287 5.04e-29

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related kinase 5; Serine/Threonine Kinases (STKs), Never In Mitosis gene A (NIMA)-related kinase 5 (Nek5) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek5 subfamily is one of a family of 11 different Neks (Nek1-11). The Nek family 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. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The specific function of Nek5 is unknown.


Pssm-ID: 173765 [Multi-domain]  Cd Length: 257  Bit Score: 113.13  E-value: 5.04e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770  33 RYRAIKPIGQGGFGRTFLAvdEDKPSKPRCVIKQFypqaQGTNTVQKAVELFTQEAVQLDELgKHPQIPELLAYFTQDDR 112
Cdd:cd08225   1 RYEIIKKIGEGSFGKIYLA--KAKSDSEHCVIKEI----DLTKMPVKEKEASKKEVILLAKM-KHPNIVTFFASFQENGR 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770 113 QYLVQEFIDGLNLAQEL-AHKGV-FQETHIIQLLNDLLPVLQFCHNRQVIHRDIKPENIILrnSDNKLV--VVDFGASKS 188
Cdd:cd08225  74 LFIVMEYCDGGDLMKRInRQRGVlFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFL--SKNGMVakLGDFGIARQ 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770 189 ATNTaLNHTGTSIGSPEYVAPEQMRGRAI-FASDIYSLGVTCINLLTGRSPFDSYDTNNDTW-IWQQY---LKPPVSNHL 263
Cdd:cd08225 152 LNDS-MELAYTCVGTPYYLSPEICQNRPYnNKTDIWSLGCVLYELCTLKHPFEGNNLHQLVLkICQGYfapISPNFSRDL 230
                       250       260
                ....*....|....*....|....
gi 17232770 264 HKIINKMTASVPARRyQNVEEVLK 287
Cdd:cd08225 231 RSLISQLFKVSPRDR-PSITSILK 253
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Protein Serine/Threonine Kinases; ...
40-245 8.64e-28

Catalytic domain of Cell division control protein 7-like Protein Serine/Threonine Kinases; Serine/threonine kinases (STKs), (Cdc7)-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Cdc7-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. Members of this subfamily include Schizosaccharomyces pombe Cdc7, Saccharomyces cerevisiae Cdc15, Arabidopsis thaliana mitogen-activated protein kinase (MAPK) kinase kinase (MAPKKK) epsilon, and related proteins. MAPKKKs phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Cdc7 is essential for cell division by playing a key role in the initiation of septum formation and cytokinesis. Budding yeast Cdc15 functions to coordinate mitotic exit with cytokinesis. Arabidopsis MAPKKK epsilon is required for pollen development in the plasma membrane.


Pssm-ID: 173731 [Multi-domain]  Cd Length: 254  Bit Score: 109.64  E-value: 8.64e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770  40 IGQGGFGRTFLAVDEDkpSKPRCVIKQFYPqaqgTNTVQKAVELFTQEAVQLDELgKHPQIPELLAYFTQDDRQYLVQEF 119
Cdd:cd06627   8 IGRGAFGVVYKGLNLE--TGDFVAIKQISL----EKIKEEALKSIMQEIDLLKNL-KHPNIVKYIGSIETSDSLYIILEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770 120 IDGLNLAQELAHKGVFQETHIIQLLNDLLPVLQFCHNRQVIHRDIKPENiILRNSDNKLVVVDFG-ASKSATNTALNHtg 198
Cdd:cd06627  81 AENGSLRQIIKKFGPFPESLVAVYVYQVLQGLAYLHEQGVIHRDIKAAN-ILTTKDGVVKLADFGvATKLNDVSKDDA-- 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 17232770 199 TSIGSPEYVAPE--QMRGRAIfASDIYSLGVTCINLLTGRSPFdsYDTN 245
Cdd:cd06627 158 SVVGTPYWMAPEviEMSGAST-ASDIWSLGCTVIELLTGNPPY--YDLN 203
STKc_PDK1 cd05581
Catalytic domain of the Protein Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; ...
34-240 1.02e-27

Catalytic domain of the Protein Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; Serine/Threonine Kinases (STKs), Phosphoinositide-dependent kinase 1 (PDK1) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PDK1 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 (PI3K). PDK1 carries an N-terminal catalytic domain and a C-terminal pleckstrin homology (PH) domain that binds phosphoinositides. It phosphorylates the activation loop of AGC kinases that are regulated by PI3K such as PKB, SGK, and PKC, among others, and is crucial for their activation. Thus, it contributes in regulating many processes including metabolism, growth, proliferation, and survival. PDK1 also has the ability to autophosphorylate and is constitutively active in mammalian cells. PDK1 is essential for normal embryo development and is important in regulating cell volume.


Pssm-ID: 173672 [Multi-domain]  Cd Length: 280  Bit Score: 109.98  E-value: 1.02e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770  34 YRAIKPIGQGGFGRTFLAVDEdKPSKP--------RCVIKQfypqaqgtntvqKAVELFTQEAVQLDELGKHPQIPELLA 105
Cdd:cd05581   3 FKFGKIIGEGSFSTVVLAKEK-ETNKEyaikildkRQLIKE------------KKVKYVKIEKEVLTRLNGHPGIIKLYY 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770 106 YFTQDDRQYLVQEFIDGLNLAQELAHKGVFQETHIIQLLNDLLPVLQFCHNRQVIHRDIKPENIILrNSDNKLVVVDFGA 185
Cdd:cd05581  70 TFQDEENLYFVLEYAPNGELLQYIRKYGSLDEKCTRFYAAEILLALEYLHSKGIIHRDLKPENILL-DKDMHIKITDFGT 148
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17232770 186 SKSATNTALNHTGTS-------------------IGSPEYVAPEQMRGRAI-FASDIYSLGVTCINLLTGRSPFD 240
Cdd:cd05581 149 AKVLDPNSSPESNKGdatnidsqieknrrrfasfVGTAEYVSPELLNEKPAgKSSDLWALGCIIYQMLTGKPPFR 223
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine kinase-like proteins; Serine ...
40-285 7.77e-27

Catalytic domain of Microtubule-associated serine/threonine kinase-like proteins; Serine/Threonine Kinases (STKs), Microtubule-associated serine/threonine (MAST) kinase subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MAST kinase 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. The MAST kinase subfamily includes MAST kinases, MAST-like (MASTL) kinases, and fungal kinases with similarity to Saccharomyces cerevisiae Rim15 and Schizosaccharomyces pombe cek1. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. MASTL kinases carry only a catalytic domain which contains a long insert relative to other kinases. The fungal kinases in this subfamily harbor other domains in addition to a central catalytic domain, which also contains an insert relative to MAST kinases like MASTL. Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. The fungal proteins Rim15 and cek1 are involved in the regulation of meiosis and mitosis, respectively.


Pssm-ID: 173670 [Multi-domain]  Cd Length: 265  Bit Score: 106.95  E-value: 7.77e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770  40 IGQGGFGRTFLAvdEDKPSKPRCVIKQF-YPQAQGTNTVQkavELFTQEAVQLDElgKHPQIPELLAYFTQDDRQYLVQE 118
Cdd:cd05579   1 ISKGAYGRVFLA--KKKSTGDIYAIKVIkKADMIRKNQVD---QVLTERDILSQA--QSPYVVKLYYSFQGKKNLYLVME 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770 119 FIDGLNLAQELAHKGVFQETHIIQLLNDLLPVLQFCHNRQVIHRDIKPENIILrNSDNKLVVVDFGASK-------SATN 191
Cdd:cd05579  74 YLPGGDLASLLENVGSLDEDVARIYIAEIVLALEYLHSNGIIHRDLKPDNILI-DSNGHLKLTDFGLSKvglvrrqINLN 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770 192 TALNHTGTSIGSPEYVAPEQMRGRAI-FASDIYSLGVTCINLLTGRSPFdsydtNNDT--WIWQQYLK--------PPVS 260
Cdd:cd05579 153 DDEKEDKRIVGTPDYIAPEVILGQGHsKTVDWWSLGCILYEFLVGIPPF-----HGETpeEIFQNILNgkiewpedVEVS 227
                       250       260
                ....*....|....*....|....*..
gi 17232770 261 NHLHKIINKMTASVPARR--YQNVEEV 285
Cdd:cd05579 228 DEAIDLISKLLVPDPEKRlgAKSIEEI 254
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, MAP/ERK kinase kinase 4; Serine ...
40-245 1.71e-26

Catalytic domain of the Protein Serine/Threonine Kinase, MAP/ERK kinase kinase 4; Serine/threonine kinases (STKs), MAP/ERK kinase kinase 4 (MEKK4) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MEKK4 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. MEKK4 is a mitogen-activated protein kinase (MAPK) kinase kinase (MAPKKK or MKKK or MAP3K), that phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MEKK4 activates the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. MEKK4 also plays roles in the re-polarization of the actin cytoskeleton in response to osmotic stress, in the proper closure of the neural tube, in cardiovascular development, and in immune responses.


Pssm-ID: 132957 [Multi-domain]  Cd Length: 264  Bit Score: 105.88  E-value: 1.71e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770  40 IGQGGFGRTFLAVDEDkpskprcvikqfypqaqgTNTVQKAVELFTQEAVQL------DELG-----KHPQIPELLAYFT 108
Cdd:cd06626   8 IGGGTFGKVYTAVNLD------------------TGELMAVKEIRIQDNDPKtikeiaDEMKvlellKHPNLVKYYGVEV 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770 109 QDDRQYLVQEFIDGLNLAQELAHKGVFQETHIIQLLNDLLPVLQFCHNRQVIHRDIKPENIIL-RNSDNKLvvVDFGASK 187
Cdd:cd06626  70 HREKVYIFMEYCSGGTLEELLEHGRILDEHVIRVYTLQLLEGLAYLHSHGIVHRDIKPANIFLdHNGVIKL--GDFGCAV 147
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17232770 188 -SATNTALNHTG--TSIGSPEYVAPEQM-------RGRAIfasDIYSLGVTCINLLTGRSPFDSYDTN 245
Cdd:cd06626 148 kLKNNTTTMGEEvqSLAGTPAYMAPEVItggkgkgHGRAA---DIWSLGCVVLEMATGKRPWSELDNE 212
STKc_MEKK1_plant cd06632
Catalytic domain of the Protein Serine/Threonine Kinase, Plant MAP/ERK kinase kinase 1; Serine ...
33-263 4.56e-26

Catalytic domain of the Protein Serine/Threonine Kinase, Plant MAP/ERK kinase kinase 1; Serine/threonine kinases (STKs), plant MAP/ERK kinase kinase 1 (MEKK1)-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The plant MEKK1 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. This subfamily is composed of plant mitogen-activated protein kinase (MAPK) kinase kinases (MAPKKKs or MKKKs or MAP3Ks) including Arabidopsis thaliana MEKK1 and MAPKKK3. MEKK1 is a MAPKKK that phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Arabidopsis thaliana MEKK1 activates MPK4, a MAPK that regulates systemic acquired resistance. MEKK1 also participates in the regulation of temperature-sensitive and tissue-specific cell death.


Pssm-ID: 132963 [Multi-domain]  Cd Length: 258  Bit Score: 104.81  E-value: 4.56e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770  33 RYRAIKPIGQGGFGRTFLAVDEDKPSkpRCVIKQFyPQAQGTNTVQKAVELFTQEAVQLDELgKHPQIPELLAYFTQDDR 112
Cdd:cd06632   1 RWRKGELLGSGSFGSVYEGLNLDDGD--FFAVKEV-SLADDGQTGQEAVKQLEQEIALLSKL-QHPNIVQYLGTEREEDN 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770 113 QYLVQEFIDGLNLAQELAHKGVFQETHIIQLLNDLLPVLQFCHNRQVIHRDIKPENIILrnsDNKLVV--VDFGASKSAt 190
Cdd:cd06632  77 LYIFLELVPGGSLAKLLKKYGSFPEPVIRLYTRQILLGLEYLHDRNTVHRDIKGANILV---DTNGVVklADFGMAKQV- 152
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17232770 191 nTALNHTGTSIGSPEYVAPEQMR--GRAIFASDIYSLGVTCINLLTGRSPFDSYDTNNDTW-IWQQYLKPPVSNHL 263
Cdd:cd06632 153 -VEFSFAKSFKGSPYWMAPEVIAqqGGYGLAADIWSLGCTVLEMATGKPPWSQLEGVAAVFkIGRSKELPPIPDHL 227
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity MAP kinase kinases and similar proteins; Protein ...
37-241 9.74e-25

Catalytic domain of Plant dual-specificity MAP kinase kinases and similar proteins; Protein kinases (PKs), MAP kinase kinase (MAPKK) subfamily, Plant MAPKKs and similar proteins, catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. The mitogen-activated protein (MAP) kinase signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAP kinase (MAPK), which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK), which itself is phosphorylated and activated by a MAPK kinase kinase (MAPKKK or MKKK). Members of this group include MAPKKs from plants, kinetoplastids, alveolates, and mycetozoa. The MAPKK, LmxPK4, from Leishmania mexicana, is important in differentiation and virulence. Dictyostelium discoideum MEK1 is required for proper chemotaxis. MEK1 null mutants display severe defects in cell polarization and directional movement. Plants contain multiple MAPKKs like other eukaryotes. The Arabidopsis genome encodes for 10 MAPKKs while poplar and rice contain 13 MAPKKs each. The functions of these proteins have not been fully elucidated. There is evidence to suggest that MAPK cascades are involved in plant stress responses. In Arabidopsis, MKK3 plays a role in pathogen signaling, MKK2 is involved in cold and salt stress signaling, MKK4/MKK5 participates in innate immunity, and MKK7 regulates basal and systemic acquired resistance.


Pssm-ID: 132954 [Multi-domain]  Cd Length: 264  Bit Score: 100.74  E-value: 9.74e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770  37 IKPIGQGGFGRTFLAVDedKPSKPRCVIKQFYPQAQGTNTVQKAVELftqEAVQLdelGKHPQIPELLAYFTQDDRQYLV 116
Cdd:cd06623   6 VKVLGQGSSGVVYKVRH--KPTGKIYALKKIHVDGDEEFRKQLLREL---KTLRS---CESPYVVKCYGAFYKEGEISIV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770 117 QEFIDGLNLAQELAHKGVFQETHIIQLLNDLLPVLQFCHN-RQVIHRDIKPENIILrNSDNKLVVVDFGASKSATNTALN 195
Cdd:cd06623  78 LEYMDGGSLADLLKKVGKIPEPVLAYIARQILKGLDYLHTkRHIIHRDIKPSNLLI-NSKGEVKIADFGISKVLENTLDQ 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 17232770 196 HTgTSIGSPEYVAPEQMRGRAI-FASDIYSLGVTCINLLTGRSPFDS 241
Cdd:cd06623 157 CN-TFVGTVTYMSPERIQGESYsYAADIWSLGLTLLECALGKFPFLP 202
STKc_Yank1 cd05578
Catalytic domain of the Protein Serine/Threonine Kinase, Yank1; Serine/Threonine Kinases (STKs) ...
34-250 2.24e-24

Catalytic domain of the Protein Serine/Threonine Kinase, Yank1; Serine/Threonine Kinases (STKs), Yank1 or STK32A subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Yank1 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. This subfamily contains uncharacterized STKs with similarity to the human protein designated Yank1 or STK32A.


Pssm-ID: 173669 [Multi-domain]  Cd Length: 258  Bit Score: 99.70  E-value: 2.24e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770  34 YRAIKPIGQGGFGRTFLaVDEDKP---------SKPRCVIKQfypqaqgtntvqkAVELFTQEAVQLDELgKHPQIPELL 104
Cdd:cd05578   2 FELLRVIGKGAFGKVCI-VQKRDTkkmfamkymNKQKCVEKG-------------SVRNVLNERRILQEL-NHPFLVNLW 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770 105 AYFTQDDRQYLVQEFIDGLNLAQELAHKGVFQETHIIQLLNDLLPVLQFCHNRQVIHRDIKPENIILrnsDNK--LVVVD 182
Cdd:cd05578  67 YSFQDEENMYLVVDLLLGGDLRYHLSQKVKFSEEQVKFWICEIVLALEYLHSKGIIHRDIKPDNILL---DEQghVHITD 143
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770 183 FG-ASKSATNTalNHTGTSiGSPEYVAPEQMRGRAI-FASDIYSLGVTCINLLTGRSPFDSYDTNNDTWI 250
Cdd:cd05578 144 FNiATKVTPDT--LTTSTS-GTPGYMAPEVLCRQGYsVAVDWWSLGVTAYECLRGKRPYRGHSRTIRDQI 210
STKc_PKA cd05580
Catalytic domain of the Protein Serine/Threonine Kinase, cAMP-dependent protein kinase; Serine ...
34-281 2.27e-24

Catalytic domain of the Protein Serine/Threonine Kinase, cAMP-dependent protein kinase; Serine/Threonine Kinases (STKs), cAMP-dependent protein kinase (PKA) subfamily, catalytic (c) subunit. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKA 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 (PI3K). This subfamily is composed of the cAMP-dependent proteins kinases, PKA and PRKX. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic (C) subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active C subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis.


Pssm-ID: 173671 [Multi-domain]  Cd Length: 290  Bit Score: 100.31  E-value: 2.27e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770  34 YRAIKPIGQGGFGRTFLAvdEDKPSKPRCVIKQFypqaqgtnTVQKAVELfTQEAVQLDE---LG--KHPQIPELLAYFt 108
Cdd:cd05580   3 FEFIKTLGTGSFGRVMLV--RHKGSGKYYALKIL--------SKAKIVKL-KQVEHVLNEkriLQsiRHPFLVNLYGSF- 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770 109 QDDRQ-YLVQEFIDGLNLAQELAHKGVFQETHIIQLLNDLLPVLQFCHNRQVIHRDIKPENIILRnSDNKLVVVDFGASK 187
Cdd:cd05580  71 QDDSNlYLVMEYVPGGELFSHLRKSGRFPEPVARFYAAQVVLALEYLHSLDIVYRDLKPENLLLD-SDGYIKITDFGFAK 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770 188 SATntalNHTGTSIGSPEYVAPEQMRGRAI-FASDIYSLGVTCINLLTGRSPFdsYDtNNDTWIWQQYLK------PPVS 260
Cdd:cd05580 150 RVK----GRTYTLCGTPEYLAPEIILSKGYgKAVDWWALGILIYEMLAGYPPF--FD-DNPIQIYEKILEgkvrfpSFFS 222
                       250       260
                ....*....|....*....|.
gi 17232770 261 NHLHKIINKMTASVPARRYQN 281
Cdd:cd05580 223 PDAKDLIRNLLQVDLTKRLGN 243
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Protein Serine/Threonine ...
32-243 4.08e-24

Catalytic domain of Mammalian Ste20-like protein kinase 3-like Protein Serine/Threonine Kinases; Serine/threonine kinases (STKs), mammalian Ste20-like protein kinase 3 (MST3)-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MST3-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. This subfamily is composed of MST3, MST4, STK25, Schizosaccharomyces pombe Nak1 and Sid1, Saccharomyces cerevisiae sporulation-specific protein 1 (SPS1), and related proteins. Nak1 is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Sid1 is a component in the septation initiation network (SIN) signaling pathway, and plays a role in cytokinesis. SPS1 plays a role in regulating proteins required for spore wall formation. MST4 plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. STK25 may play a role in the regulation of cell migration and polarization.


Pssm-ID: 132940 [Multi-domain]  Cd Length: 274  Bit Score: 99.23  E-value: 4.08e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770  32 ERYRAIKPIGQGGFGRTFLAVDedKPSKPRCVIKQFypqaqgtnTVQKA---VELFTQEAVQLDELgKHPQIPELLAYFT 108
Cdd:cd06609   1 ELFTLLECIGKGSFGEVYKAID--KRTNQVVAIKVI--------DLEEAedeIEDIQQEIQFLSQC-RSPYITKYYGSFL 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770 109 QDDRQYLVQEFIDGLNLAqELAHKGVFQETHIIQLLNDLLPVLQFCHNRQVIHRDIKPENIILRNS-DNKLvvVDFGASK 187
Cdd:cd06609  70 KGSKLWIIMEYCGGGSCL-DLLKPGKLDETYIAFILREVLLGLEYLHEEGKIHRDIKAANILLSEEgDVKL--ADFGVSG 146
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 17232770 188 SATNTALNHTgTSIGSPEYVAPEQMRGRAI-FASDIYSLGVTCINLLTGRSPFDSYD 243
Cdd:cd06609 147 QLTSTMSKRN-TFVGTPFWMAPEVIKQSGYdEKADIWSLGITAIELAKGEPPLSDLH 202
STKc_cGK_PKG cd05572
Catalytic domain of the Protein Serine/Threonine Kinase, cGMP-dependent protein kinase; Serine ...
40-244 4.26e-24

Catalytic domain of the Protein Serine/Threonine Kinase, cGMP-dependent protein kinase; Serine/Threonine Kinases (STKs), cGMP-dependent protein kinase (cGK or PKG) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The cGK 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. Mammals have two cGK isoforms from different genes, cGKI and cGKII. cGKI exists as two splice variants, cGKI-alpha and cGKI-beta. cGK consists of an N-terminal regulatory domain containing a dimerization and an autoinhibitory pseudosubstrate region, two cGMP-binding domains, and a C-terminal catalytic domain. Binding of cGMP to both binding sites releases the inhibition of the catalytic center by the pseudosubstrate region, allowing autophosphorylation and activation of the kinase. cGKI is a soluble protein expressed in all smooth muscles, platelets, cerebellum, and kidney. It is also expressed at lower concentrations in other tissues. cGKII is a membrane-bound protein that is most abundantly expressed in the intestine. It is also present in the brain nuclei, adrenal cortex, kidney, lung, and prostate. cGKI is involved in the regulation of smooth muscle tone, smooth cell proliferation, and platelet activation. cGKII plays a role in the regulation of secretion, such as renin secretion by the kidney and aldosterone secretion by the adrenal. It also regulates bone growth and the circadian rhythm.


Pssm-ID: 173663 [Multi-domain]  Cd Length: 262  Bit Score: 98.85  E-value: 4.26e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770  40 IGQGGFGRTFLAvdEDKPSKPRCVIKQfypqaqgtntVQKA--VELFTQEAVQLD----ELGKHPQIPELLAYFtQDDRQ 113
Cdd:cd05572   1 LGVGGFGRVELV--KVKSKNRTFALKC----------VKKRhiVETGQQEHIFSEkeilEECNHPFIVKLYRTF-KDKKY 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770 114 -YLVQEFIDGLNLAQELAHKGVFQETHIIQLLNDLLPVLQFCHNRQVIHRDIKPENIILrNSDNKLVVVDFGASKSATNT 192
Cdd:cd05572  68 iYMLMEYCLGGELWTILRDRGLFDEYTARFYIACVVLAFEYLHNRGIIYRDLKPENLLL-DSNGYVKLVDFGFAKKLKSG 146
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 17232770 193 alNHTGTSIGSPEYVAPEQMRGRAI-FASDIYSLGVTCINLLTGRSPFDSYDT 244
Cdd:cd05572 147 --QKTWTFCGTPEYVAPEIILNKGYdFSVDYWSLGILLYELLTGRPPFGEDDE 197
STKc_Nek2 cd08217
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
34-288 4.57e-24

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related kinase 2; Serine/Threonine Kinases (STKs), Never In Mitosis gene A (NIMA)-related kinase 2 (Nek2) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek2 subfamily is one of a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family 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. The Nek2 subfamily includes Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants prevented from entering mitosis. NIMA is essential for mitotic entry and progression through mitosis, and its degradation is essential for mitotic exit. NIMA is involved in nuclear membrane fission. Vertebrate Nek2 is a cell cycle-regulated STK, localized in centrosomes and kinetochores, that regulates centrosome splitting at the G2/M phase. It also interacts with other mitotic kinases such as Polo-like kinase 1 and may play a role in spindle checkpoint. An increase in the expression of the human NEK2 gene is strongly associated with the progression of non-Hodgkin lymphoma.


Pssm-ID: 173757 [Multi-domain]  Cd Length: 265  Bit Score: 98.86  E-value: 4.57e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770  34 YRAIKPIGQGGFGRTFLAvdEDKPSKPRCVIKQF-YpqaqGTNTvQKAVELFTQEAVQLDELgKHPQIpelLAYFTQD-D 111
Cdd:cd08217   2 YEVLETIGKGSFGTVRKV--RRKSDGKILVWKEIdY----GNMT-EKEKQQLVSEVNILREL-KHPNI---VRYYDRIiD 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770 112 RQ----YLVQEFIDGLNLAQELAH----KGVFQETHIIQLLNDLLPVLQFCHNRQ-----VIHRDIKPENIILRNSDN-K 177
Cdd:cd08217  71 RSnqtlYIVMEYCEGGDLAQLIQKckkeRKYIEEEFIWRILTQLLLALYECHNRSdpgntVLHRDLKPANIFLDANNNvK 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770 178 LvvVDFGASKSATNTAlNHTGTSIGSPEYVAPEQMRGRAI-FASDIYSLGVTCINLLTGRSPFDSYdtNNDTwiWQQYLK 256
Cdd:cd08217 151 L--GDFGLAKILGHDS-SFAKTYVGTPYYMSPEQLNHMSYdEKSDIWSLGCLIYELCALSPPFTAR--NQLQ--LASKIK 223
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 17232770 257 ----PPV----SNHLHKIINKMTASVPARRyQNVEEVLKD 288
Cdd:cd08217 224 egkfRRIpyrySSELNEVIKSMLNVDPDKR-PSTEELLQL 262
STKc_ROCK_NDR_like cd05573
Catalytic domain of ROCK- and NDR kinase-like Protein Serine/Threonine Kinases; Serine ...
32-304 1.77e-23

Catalytic domain of ROCK- and NDR kinase-like Protein Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), Rho-associated coiled-coil containing protein kinase (ROCK) and Nuclear Dbf2-Related (NDR)-like kinase subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ROCK- and NDR-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. Members of this subfamily include ROCK and ROCK-like proteins such as DMPK, MRCK, and CRIK, as well as NDR and NDR-like proteins such as LATS, CBK1 and Sid2p. ROCK and CRIK are effectors of the small GTPase Rho, while MRCK is an effector of the small GTPase Cdc42. NDR and NDR-like kinases contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Proteins in this subfamily are involved in regulating many cellular functions including contraction, motility, division, proliferation, apoptosis, morphogenesis, and cytokinesis.


Pssm-ID: 173664 [Multi-domain]  Cd Length: 350  Bit Score: 98.52  E-value: 1.77e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770  32 ERYRAIKPIGQGGFGRTFLAVDEDKpskprcviKQFYpqaqGTNTVQKAVeLFTQEAVQLDEL-------GKHPQIPELL 104
Cdd:cd05573   1 DDFEVIKVIGRGAFGEVWLVRDKDT--------GQVY----AMKVLRKSD-MIKRNQIAHVRAerdiladADSPWIVKLY 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770 105 AYFTQDDRQYLVQEFIDGLNLAQELAHKGVFQETHIIQLLNDLLPVLQFCHNRQVIHRDIKPENIILrNSDNKLVVVDFG 184
Cdd:cd05573  68 YSFQDEEHLYLVMEYMPGGDLMNLLIRKDVFPEETARFYIAELVLALDSVHKLGFIHRDIKPDNILI-DADGHIKLADFG 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770 185 ASK------------SATNTALNHTG----------------TSIGSPEYVAPEQMRGRAI-FASDIYSLGVTCINLLTG 235
Cdd:cd05573 147 LCKkmnkakdreyylNDSHNLLFRDNvlvrrrdhkqrrvranSTVGTPDYIAPEVLRGTPYgLECDWWSLGVILYEMLYG 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770 236 RSPFDSyDTNNDTWI----WQQYL----KPPVSNHLHKIINKMTASvPARRYQNVEEVLK----------DLNQYS---- 293
Cdd:cd05573 227 FPPFYS-DTLQETYNkiinWKESLrfppDPPVSPEAIDLICRLLCD-PEDRLGSFEEIKShpffkgidweNLRETKppfv 304
                       330
                ....*....|.
gi 17232770 294 PVVNTPAKSSH 304
Cdd:cd05573 305 PELSSPLDTSN 315
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
33-278 5.43e-23

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related kinase 3; Serine/Threonine Kinases (STKs), Never In Mitosis gene A (NIMA)-related kinase 3 (Nek3) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek3 subfamily is one of a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family 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. Nek3 is primarily localized in the cytoplasm and shows no cell cycle-dependent changes in its activity. It is present in the axons of neurons and affects morphogenesis and polarity through its regulation of microtubule acetylation. Nek3 modulates the signaling of the prolactin receptor through its activation of Vav2 and contributes to prolactin-mediated motility of breast cancer cells.


Pssm-ID: 173759 [Multi-domain]  Cd Length: 255  Bit Score: 95.81  E-value: 5.43e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770  33 RYRAIKPIGQGGFGRTFLAvdEDKPSKPRCVIKQF-YPQAQgtntvqKAVELFTQEAVQLDELgKHPQIPELLAYFTQDD 111
Cdd:cd08219   1 QYNVLRVVGEGSFGRALLV--QHVNSDQKYAMKEIrLPKSS------SAVEDSRKEAVLLAKM-KHPNIVAFKESFEADG 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770 112 RQYLVQEFIDGLNLAQELA-HKG-VFQETHIIQLLNDLLPVLQFCHNRQVIHRDIKPENIILrNSDNKLVVVDFGASKSA 189
Cdd:cd08219  72 HLYIVMEYCDGGDLMQKIKlQRGkLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFL-TQNGKVKLGDFGSARLL 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770 190 TNtALNHTGTSIGSPEYVAPEQMRGRAI-FASDIYSLGVTCINLLTGRSPFDSydtnnDTW------IWQQYLKPPVSNH 262
Cdd:cd08219 151 TS-PGAYACTYVGTPYYVPPEIWENMPYnNKSDIWSLGCILYELCTLKHPFQA-----NSWknlilkVCQGSYKPLPSHY 224
                       250
                ....*....|....*....
gi 17232770 263 ---LHKIINKMTASVPARR 278
Cdd:cd08219 225 syeLRSLIKQMFKRNPRSR 243
STKc_OSR1_SPAK cd06610
Catalytic domain of the Protein Serine/Threonine Kinases, Oxidative stress response kinase and ...
34-242 2.95e-22

Catalytic domain of the Protein Serine/Threonine Kinases, Oxidative stress response kinase and Ste20-related proline alanine-rich kinase; Serine/threonine kinases (STKs), oxidative stress response kinase (OSR1) and Ste20-related proline alanine-rich kinase (SPAK) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The OSR1 and SPAK 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. SPAK is also referred to as STK39 or PASK (proline-alanine-rich STE20-related kinase). OSR1 and SPAK regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. They are also implicated in cytoskeletal rearrangement, cell differentiation, transformation and proliferation. OSR1 and SPAK contain a conserved C-terminal (CCT) domain, which recognizes a unique motif ([RK]FX[VI]) present in their activating kinases (WNK1/WNK4) and their substrates.


Pssm-ID: 173726 [Multi-domain]  Cd Length: 267  Bit Score: 93.58  E-value: 2.95e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17232770  34 YRAIKPIGQGGFGRTFLAvdEDKPSKPRCVIKQFYPQAQGTNtvqkaVELFTQEaVQLDELGKHPQIPELLAYFTQDDRQ 113
Cdd:cd06610   3 YELIEVIGVGATAVVYAA--ICLPNNEKVAIKRIDLEKCQTS-----VDELRKE-VQ