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Conserved domains on  [gi|504275011|ref|WP_014462113|]
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MULTISPECIES: hypothetical protein [Bacillaceae]

Protein Classification

COG2112 superfamily protein( domain architecture ID 1904195)

COG2112 superfamily protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG2112 super family cl42500
Predicted Ser/Thr protein kinase [Signal transduction mechanisms];
67-209 1.49e-08

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


The actual alignment was detected with superfamily member COG2112:

Pssm-ID: 441715 [Multi-domain]  Cd Length: 225  Bit Score: 53.49  E-value: 1.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504275011  67 IGEKENELMNFKRYKVVGQGKDGVIYQLTDNR---CVKVF---FKEEVYKKELEAIKVGQSSFIIPHLYDYGPNYIVMEY 140
Cdd:COG2112   32 ITSIYSGGTLIGGLRLLGKGYRGVVFLGKLGGkkvALKIRrtdSPRPSLKKEAEILKKANGAGVGPKLYDYGRDFLVMEY 111

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504275011 141 IKGISLAKHLKK-NQYIEKALVVQLISLFNELKKLSFRRQD--TELRHVLITeQGNLKIIDLKRAFSSKRPT 209
Cdd:COG2112  112 IEGEPLKDWLENlDKEELRKVIRELLEAAYLLDRIGIDHGElsRPGKHVIVD-KGRPYIIDFESASISRKPS 182
 
Name Accession Description Interval E-value
COG2112 COG2112
Predicted Ser/Thr protein kinase [Signal transduction mechanisms];
67-209 1.49e-08

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


Pssm-ID: 441715 [Multi-domain]  Cd Length: 225  Bit Score: 53.49  E-value: 1.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504275011  67 IGEKENELMNFKRYKVVGQGKDGVIYQLTDNR---CVKVF---FKEEVYKKELEAIKVGQSSFIIPHLYDYGPNYIVMEY 140
Cdd:COG2112   32 ITSIYSGGTLIGGLRLLGKGYRGVVFLGKLGGkkvALKIRrtdSPRPSLKKEAEILKKANGAGVGPKLYDYGRDFLVMEY 111

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504275011 141 IKGISLAKHLKK-NQYIEKALVVQLISLFNELKKLSFRRQD--TELRHVLITeQGNLKIIDLKRAFSSKRPT 209
Cdd:COG2112  112 IEGEPLKDWLENlDKEELRKVIRELLEAAYLLDRIGIDHGElsRPGKHVIVD-KGRPYIIDFESASISRKPS 182
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
 79-199 3.07e-06

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.


Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 46.81  E-value: 3.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504275011  79 RYKVV---GQGKDGVIYQLTDNRC-----VKVFFKEEVYKKEL------EAIKVGQ-SSFIIPHLYDYG----PNYIVME 139
Cdd:cd14014    1 RYRLVrllGRGGMGEVYRARDTLLgrpvaIKVLRPELAEDEEFrerflrEARALARlSHPNIVRVYDVGeddgRPYIVME 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504275011 140 YIKGISLAKHLKKNQYIEKALVVQLIslfnelkklsfrRQDTE-LRH---------------VLITEQGNLKIIDL 199
Cdd:cd14014   81 YVEGGSLADLLRERGPLPPREALRIL------------AQIADaLAAahragivhrdikpanILLTEDGRVKLTDF 144
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
 77-198 8.32e-06

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 45.60  E-value: 8.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504275011    77 FKRYKVVGQGKDGVIYQLTDNRC-----VKVFFKEEVYKK------ELEAIKVGQSSFIIpHLYDYGPN----YIVMEYI 141
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTgklvaIKVIKKKKIKKDrerilrEIKILKKLKHPNIV-RLYDVFEDedklYLVMEYC 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504275011   142 KGISLAKHLKKNQYIE----KALVVQLISLFNELKKLSFRRQDTELRHVLITEQGNLKIID 198
Cdd:smart00220  80 EGGDLFDLLKKRGRLSedeaRFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLAD 140
Pkinase pfam00069
Protein kinase domain;
77-157 1.98e-04

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 41.46  E-value: 1.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504275011   77 FKRYKVVGQGKDGVIYQLTDNR-----CVKVFFKEEVYKK-------ELEAIKVGQSSFIIpHLYDY---GPN-YIVMEY 140
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDtgkivAIKKIKKEKIKKKkdknilrEIKILKKLNHPNIV-RLYDAfedKDNlYLVLEY 79

                          90
                  ....*....|....*..
gi 504275011  141 IKGISLAKHLKKNQYIE 157
Cdd:pfam00069  80 VEGGSLFDLLSEKGAFS 96
 
Name Accession Description Interval E-value
COG2112 COG2112
Predicted Ser/Thr protein kinase [Signal transduction mechanisms];
67-209 1.49e-08

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


Pssm-ID: 441715 [Multi-domain]  Cd Length: 225  Bit Score: 53.49  E-value: 1.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504275011  67 IGEKENELMNFKRYKVVGQGKDGVIYQLTDNR---CVKVF---FKEEVYKKELEAIKVGQSSFIIPHLYDYGPNYIVMEY 140
Cdd:COG2112   32 ITSIYSGGTLIGGLRLLGKGYRGVVFLGKLGGkkvALKIRrtdSPRPSLKKEAEILKKANGAGVGPKLYDYGRDFLVMEY 111

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504275011 141 IKGISLAKHLKK-NQYIEKALVVQLISLFNELKKLSFRRQD--TELRHVLITeQGNLKIIDLKRAFSSKRPT 209
Cdd:COG2112  112 IEGEPLKDWLENlDKEELRKVIRELLEAAYLLDRIGIDHGElsRPGKHVIVD-KGRPYIIDFESASISRKPS 182
RIO2 COG0478
RIO-like serine/threonine protein kinase fused to N-terminal HTH domain [Signal transduction ...
 125-220 8.63e-07

RIO-like serine/threonine protein kinase fused to N-terminal HTH domain [Signal transduction mechanisms];


Pssm-ID: 440246 [Multi-domain]  Cd Length: 183  Bit Score: 47.98  E-value: 8.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504275011 125 IPHLYDYGPNYIVMEYIKGISLAKHLKKNqyiEKALVVQLISlfnELKKLsFRRQ----DTELRHVLITEQGNLKIIDLK 200
Cdd:COG0478   63 VPRPIAANRHAIVMERIEGVELARLKLED---PEEVLDKILE---EIRRA-HDAGivhaDLSEYNILVDDDGGVWIIDWP 135

                         90       100
                 ....*....|....*....|.
gi 504275011 201 RAFSSKRPTPIKLLK-DLKGL 220
Cdd:COG0478  136 QAVPRDHPNAEELLErDLENL 156
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
79-198 2.61e-06

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 47.70  E-value: 2.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504275011  79 RYKVV---GQGKDGVIY---QLTDNRCV--KVFFKE--------EVYKKELEAIKVGQSSFIiPHLYDYGPN----YIVM 138
Cdd:COG0515    8 RYRILrllGRGGMGVVYlarDLRLGRPValKVLRPElaadpearERFRREARALARLNHPNI-VRVYDVGEEdgrpYLVM 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504275011 139 EYIKGISLAKHLKKNQYIEKALVVQLI-SLfneLKKLSF--RRQdteLRH-------VLITEQGNLKIID 198
Cdd:COG0515   87 EYVEGESLADLLRRRGPLPPAEALRILaQL---AEALAAahAAG---IVHrdikpanILLTPDGRVKLID 150
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
 79-199 3.07e-06

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.


Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 46.81  E-value: 3.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504275011  79 RYKVV---GQGKDGVIYQLTDNRC-----VKVFFKEEVYKKEL------EAIKVGQ-SSFIIPHLYDYG----PNYIVME 139
Cdd:cd14014    1 RYRLVrllGRGGMGEVYRARDTLLgrpvaIKVLRPELAEDEEFrerflrEARALARlSHPNIVRVYDVGeddgRPYIVME 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504275011 140 YIKGISLAKHLKKNQYIEKALVVQLIslfnelkklsfrRQDTE-LRH---------------VLITEQGNLKIIDL 199
Cdd:cd14014   81 YVEGGSLADLLRERGPLPPREALRIL------------AQIADaLAAahragivhrdikpanILLTEDGRVKLTDF 144
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
 77-198 8.32e-06

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 45.60  E-value: 8.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504275011    77 FKRYKVVGQGKDGVIYQLTDNRC-----VKVFFKEEVYKK------ELEAIKVGQSSFIIpHLYDYGPN----YIVMEYI 141
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTgklvaIKVIKKKKIKKDrerilrEIKILKKLKHPNIV-RLYDVFEDedklYLVMEYC 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504275011   142 KGISLAKHLKKNQYIE----KALVVQLISLFNELKKLSFRRQDTELRHVLITEQGNLKIID 198
Cdd:smart00220  80 EGGDLFDLLKKRGRLSedeaRFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLAD 140
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
 79-202 2.84e-05

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).


Pssm-ID: 270690 [Multi-domain]  Cd Length: 158  Bit Score: 43.06  E-value: 2.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504275011  79 RYKVVGQGKDGVIYQLTDNR--CVKVFFKEEV--YKKELEAIKV--GQSSFIIPHLYDYGPN----YIVMEYIKGISLAK 148
Cdd:cd05120    2 SVKLIKEGGDNKVYLLGDPReyVLKIGPPRLKkdLEKEAAMLQLlaGKLSLPVPKVYGFGESdgweYLLMERIEGETLSE 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 504275011 149 HLKKNQYIEKALVVQLI----SLFNELKKLSFRRQDTELRHVLITEQGNL-KIIDLKRA 202
Cdd:cd05120   82 VWPRLSEEEKEKIADQLaeilAALHRIDSSVLTHGDLHPGNILVKPDGKLsGIIDWEFA 140
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
 84-199 3.13e-05

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.


Pssm-ID: 270622 [Multi-domain]  Cd Length: 215  Bit Score: 43.80  E-value: 3.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504275011  84 GQGKDGVIYQLTDN-----RCVKVFFKE------EVYKKELEAIKVGQSSFIIpHLYDY----GPNYIVMEYIKGISLAK 148
Cdd:cd00180    2 GKGSFGKVYKARDKetgkkVAVKVIPKEklkkllEELLREIEILKKLNHPNIV-KLYDVfeteNFLYLVMEYCEGGSLKD 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 504275011 149 HLKKNQY---IEKALVV--QLISLFNELKKLSFRRQDTELRHVLITEQGNLKIIDL 199
Cdd:cd00180   81 LLKENKGplsEEEALSIlrQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADF 136
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
 125-208 7.85e-05

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


Pssm-ID: 442859 [Multi-domain]  Cd Length: 159  Bit Score: 41.87  E-value: 7.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504275011 125 IPHLYDYGPNYIVMEYIKGISLAKHLKKNQYIEKaLVVQLISLFNELKKLSFRRQDTELRHVLITEQGnLKIIDLKRAFS 204
Cdd:COG3642   22 KVLDVDPDDADLVMEYIEGETLADLLEEGELPPE-LLRELGRLLARLHRAGIVHGDLTTSNILVDDGG-VYLIDFGLARY 99


                 ....
gi 504275011 205 SKRP 208
Cdd:COG3642  100 SDPL 103
Pkinase pfam00069
Protein kinase domain;
77-157 1.98e-04

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 41.46  E-value: 1.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504275011   77 FKRYKVVGQGKDGVIYQLTDNR-----CVKVFFKEEVYKK-------ELEAIKVGQSSFIIpHLYDY---GPN-YIVMEY 140
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDtgkivAIKKIKKEKIKKKkdknilrEIKILKKLNHPNIV-RLYDAfedKDNlYLVLEY 79

                          90
                  ....*....|....*..
gi 504275011  141 IKGISLAKHLKKNQYIE 157
Cdd:pfam00069  80 VEGGSLFDLLSEKGAFS 96
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
 77-209 2.29e-04

Catalytic domain of Fungal Nak1-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 Schizosaccharomyces pombe Nak1, Saccharomyces cerevisiae Kic1p (kinase that interacts with Cdc31p) and related proteins. Nak1 (also called N-rich kinase 1), 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. Kic1p is required by budding yeast for cell integrity and morphogenesis. Kic1p interacts with Cdc31p, the yeast homologue of centrin, and phosphorylates substrates in a Cdc31p-dependent manner. The Nak1 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.


Pssm-ID: 270822 [Multi-domain]  Cd Length: 277  Bit Score: 41.31  E-value: 2.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504275011  77 FKRYKVVGQGKDGVIYQ---LTDNRCV--KVF------FKEEVYKKE---LEAIKVGQSSFIIPHLYDY--GPN-YIVME 139
Cdd:cd06917    3 YRRLELVGRGSYGAVYRgyhVKTGRVValKVLnldtddDDVSDIQKEvalLSQLKLGQPKNIIKYYGSYlkGPSlWIIMD 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504275011 140 YIKGISLAKHLKKNQYIEK--ALVVQ--LISLfNELKKLSFRRQDTELRHVLITEQGNLKIIDLKRAF-----SSKRPT 209
Cdd:cd06917   83 YCEGGSIRTLMRAGPIAERyiAVIMRevLVAL-KFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVAAslnqnSSKRST 160
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
 77-199 3.66e-03

Catalytic domain of Mammalian Ste20-like protein kinase 3-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 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. The MST3-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.


Pssm-ID: 270786 [Multi-domain]  Cd Length: 274  Bit Score: 37.61  E-value: 3.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504275011  77 FKRYKVVGQGKDGVIYQLTDNRC-----VKVFFKEEV------YKKELEAIKVGQSSFIIPHLYDYGPNY---IVMEYIK 142
Cdd:cd06609    3 FTLLERIGKGSFGEVYKGIDKRTnqvvaIKVIDLEEAedeiedIQQEIQFLSQCDSPYITKYYGSFLKGSklwIIMEYCG 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 504275011 143 GISLAKHLKKNQYIEKALVVQLISLFNELKKLSFRR---QDTELRHVLITEQGNLKIIDL 199
Cdd:cd06609   83 GGSVLDLLKPGPLDETYIAFILREVLLGLEYLHSEGkihRDIKAANILLSEEGDVKLADF 142
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
 76-198 3.76e-03

Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear Dbf2-Related (NDR)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. 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. The ROCK/NDR-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.


Pssm-ID: 270725 [Multi-domain]  Cd Length: 350  Bit Score: 38.03  E-value: 3.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504275011  76 NFKRYKVVGQGKDGVIYQLTDNRCVKVFFKEEVYKKELeaIKVGQSSFI--------------IPHLY----DYGPNYIV 137
Cdd:cd05573    2 DFEVIKVIGRGAFGEVWLVRDKDTGQVYAMKILRKSDM--LKREQIAHVraerdiladadspwIVRLHyafqDEDHLYLV 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504275011 138 MEYIKGISLAKHL-KKNQYIE---KALVVQLISLFNELKKLSFRRQDTELRHVLITEQGNLKIID 198
Cdd:cd05573   80 MEYMPGGDLMNLLiKYDVFPEetaRFYIAELVLALDSLHKLGFIHRDIKPDNILLDADGHIKLAD 144
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
 77-199 9.98e-03

Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK25 is also called Ste20/oxidant stress response kinase 1 (SOK1) or yeast Sps1/Ste20-related kinase 1 (YSK1). It is localized in the Golgi apparatus through its interaction with the Golgi matrix protein GM130. It may be involved in the regulation of cell migration and polarization. STK25 binds and phosphorylates CCM3 (cerebral cavernous malformation 3), also called PCD10 (programmed cell death 10), and may play a role in apoptosis. Human STK25 is a candidate gene responsible for pseudopseudohypoparathyroidism (PPHP), a disease that shares features with the Albright hereditary osteodystrophy (AHO) phenotype. The STK25 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.


Pssm-ID: 270810 [Multi-domain]  Cd Length: 277  Bit Score: 36.57  E-value: 9.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504275011  77 FKRYKVVGQGKDGVIYQLTDNR-----CVKVFFKEEV------YKKELEAIKVGQSSFIIPHLYDYGPN---YIVMEYIK 142
Cdd:cd06642    6 FTKLERIGKGSFGEVYKGIDNRtkevvAIKIIDLEEAedeiedIQQEITVLSQCDSPYITRYYGSYLKGtklWIIMEYLG 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 504275011 143 GISLAKHLKKNQYIEKALVVQLISLFNELKKLSFRRQ---DTELRHVLITEQGNLKIIDL 199
Cdd:cd06642   86 GGSALDLLKPGPLEETYIATILREILKGLDYLHSERKihrDIKAANVLLSEQGDVKLADF 145
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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