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Conserved domains on  [gi|28572930|ref|NP_789710|]
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serine/threonine-protein kinase [Tropheryma whipplei TW08/27]

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List of domain hits

Name Accession Description Interval E-value
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
349-408 1.75e-11

PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a group of related transmembrane sensor kinases present in many gram positive bacteria, which has been shown to regulate cell shape in Mycobacterium tubercolosis. PknB is a receptor-like transmembrane protein with an extracellular signal sensor domain (containing multiple PASTA domains) and an intracellular, eukaryotic serine/threonine kinase-like domain. The PASTA domain is found at the C-termini of several Penicillin-binding proteins (PBPs) and bacterial serine/threonine kinases. The name PASTA is derived from PBP and Serine/Threonine kinase Associated domain.


:

Pssm-ID: 119328  Cd Length: 62  Bit Score: 60.24  E-value: 1.75e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28572930 349 MPNLIGIDKEQAIKKLNDLGVKF-RINTEHSATMPVGYVTGTSPKSGAVVDSDTEVSISLS 408
Cdd:cd06577   2 VPDVVGMTLDEAKAALEAAGLKVgVVTEEYSDDVPKGTVISQSPAAGTKVKKGSTVTLTVS 62
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
413-464 3.42e-03

PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a group of related transmembrane sensor kinases present in many gram positive bacteria, which has been shown to regulate cell shape in Mycobacterium tubercolosis. PknB is a receptor-like transmembrane protein with an extracellular signal sensor domain (containing multiple PASTA domains) and an intracellular, eukaryotic serine/threonine kinase-like domain. The PASTA domain is found at the C-termini of several Penicillin-binding proteins (PBPs) and bacterial serine/threonine kinases. The name PASTA is derived from PBP and Serine/Threonine kinase Associated domain.


:

Pssm-ID: 119328  Cd Length: 62  Bit Score: 35.97  E-value: 3.42e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 28572930 413 ELPNFVGARFEAARRGLAELRLEVKKI----CSG---DTVNAQKPAGGSIVPQEIEITL 464
Cdd:cd06577   1 TVPDVVGMTLDEAKAALEAAGLKVGVVteeySDDvpkGTVISQSPAAGTKVKKGSTVTL 59
PKc cd00180
Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze ...
53-258 2.34e-10

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: 59.17  E-value: 2.34e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572930  53 KEFSLALDTRVRQAV--------KLDSPHIATIFDggedYFSDSIRQFIASEstHHEEKSLEGCFITISK--SIRLIAEV 122
Cdd:cd00180  24 KIIKKEDSSSLLEELlreieilkKLNHPNIVKLYG----VFEDENHLYLVME--YCEGGSLKDLLKENEGklSEDEILRI 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572930 123 IDGVALALEAGRQGNLPHGSISPQNI--TCHDGSLKVINFAIATSVNDAALPLEDGK---AFFAPELLVDRslnaykaep 197
Cdd:cd00180  98 LLQILEGLEYLHSNGIIHRDLKPENIllDSDNGKVKLADFGLSKLLTSDKSLLKTIVgtpAYMAPEVLLGK--------- 168
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28572930 198 RQITYRSDVYSLGGLLYWLltgttyitgeqvcttryrsdtnEAIDCVLRKALAIEPTSRFS 258
Cdd:cd00180 169 GYYSEKSDIWSLGVILYEL----------------------PELKDLIRKMLQKDPEKRPS 207
SPS1 COG0515
Serine/threonine protein kinase [General function prediction only / Signal transduction ...
14-375 2.04e-13

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: 70.54  E-value: 2.04e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572930  14 YELVKCLRVARYYKMYQGYDRRLkrnVNVVLFDTEVSDKKEFSLALDTRVRQAVKLDSP-HIATIFDggedYFSDSIRQF 92
Cdd:COG0515   2 YRILRKLGEGSFGEVYLARDRKL---VALKVLAKKLESKSKEVERFLREIQILASLNHPpNIVKLYD----FFQDEGSLY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572930  93 IASESTHHEE--KSLEGCFITISKSIRLIAEVIDGVALALEAGRQGNLPHGSISPQNI--TCHDGSLKVINFAIATSVND 168
Cdd:COG0515  75 LVMEYVDGGSleDLLKKIGRKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENIllDRDGRVVKLIDFGLAKLLPD 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572930 169 AALPLEDGK---------AFFAPELLVDRSLNAYkaeprqiTYRSDVYSLGGLLYWLLTGTTYITGEQV----------- 228
Cdd:COG0515 155 PGSTSSIPAlpstsvgtpGYMAPEVLLGLSLAYA-------SSSSDIWSLGITLYELLTGLPPFEGEKNssatsqtlkii 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572930 229 -----------CTTRYRSDTNEAIDCVLRKALAIEPTSRFSSAVEMSDALRKaiEPKKKIDPLSIKDEILAQVNLPHKSS 297
Cdd:COG0515 228 lelptpslaspLSPSNPELISKAASDLLKKLLAKDPKNRLSSSSDLSHDLLA--HLKLKESDLSDLLKPDDSAPLRLSLP 305
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28572930 298 HPKRKHSNAVAFIALAICAVAAVITVSAALITTNLPDNKQAQVGAPLSNLSMPNLIGIDKEQAIKKLNDLGVKFRINT 375
Cdd:COG0515 306 PSLEALISSLNSLAISGSDLKLDDSNFSKELAPNGVSSSPHNSSSLLLSTASSKRSSLPKISARSSPSSLSSSSRQQA 383
 
Name Accession Description Interval E-value
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
349-408 1.75e-11

PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a group of related transmembrane sensor kinases present in many gram positive bacteria, which has been shown to regulate cell shape in Mycobacterium tubercolosis. PknB is a receptor-like transmembrane protein with an extracellular signal sensor domain (containing multiple PASTA domains) and an intracellular, eukaryotic serine/threonine kinase-like domain. The PASTA domain is found at the C-termini of several Penicillin-binding proteins (PBPs) and bacterial serine/threonine kinases. The name PASTA is derived from PBP and Serine/Threonine kinase Associated domain.


Pssm-ID: 119328  Cd Length: 62  Bit Score: 60.24  E-value: 1.75e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28572930 349 MPNLIGIDKEQAIKKLNDLGVKF-RINTEHSATMPVGYVTGTSPKSGAVVDSDTEVSISLS 408
Cdd:cd06577   2 VPDVVGMTLDEAKAALEAAGLKVgVVTEEYSDDVPKGTVISQSPAAGTKVKKGSTVTLTVS 62
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
413-464 3.42e-03

PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a group of related transmembrane sensor kinases present in many gram positive bacteria, which has been shown to regulate cell shape in Mycobacterium tubercolosis. PknB is a receptor-like transmembrane protein with an extracellular signal sensor domain (containing multiple PASTA domains) and an intracellular, eukaryotic serine/threonine kinase-like domain. The PASTA domain is found at the C-termini of several Penicillin-binding proteins (PBPs) and bacterial serine/threonine kinases. The name PASTA is derived from PBP and Serine/Threonine kinase Associated domain.


Pssm-ID: 119328  Cd Length: 62  Bit Score: 35.97  E-value: 3.42e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 28572930 413 ELPNFVGARFEAARRGLAELRLEVKKI----CSG---DTVNAQKPAGGSIVPQEIEITL 464
Cdd:cd06577   1 TVPDVVGMTLDEAKAALEAAGLKVGVVteeySDDvpkGTVISQSPAAGTKVKKGSTVTL 59
PASTA pfam03793
PASTA domain; This domain is found at the C termini of several Penicillin-binding proteins and ...
349-409 2.01e-13

PASTA domain; This domain is found at the C termini of several Penicillin-binding proteins and bacterial serine/threonine kinases. It binds the beta-lactam stem, which implicates it in sensing D-alanyl-D-alanine - the PBP transpeptidase substrate. It is a small globular fold consisting of 3 beta-sheets and an alpha-helix. The name PASTA is derived from PBP and Serine/Threonine kinase Associated domain.


Pssm-ID: 252166  Cd Length: 63  Bit Score: 65.71  E-value: 2.01e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28572930   349 MPNLIGIDKEQAIKKLNDLGVKFRINTEHSATMPVGYVTGTSPKSGAVVDSDTEVSISLSD 409
Cdd:pfam03793   3 VPDVVGLSLEEAKKLLEALGLKVGTVEEYSDDVGEGTVISQSPPAGTKVKKGSKVTLTVSK 63
PKc cd00180
Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze ...
53-258 2.34e-10

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: 59.17  E-value: 2.34e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572930  53 KEFSLALDTRVRQAV--------KLDSPHIATIFDggedYFSDSIRQFIASEstHHEEKSLEGCFITISK--SIRLIAEV 122
Cdd:cd00180  24 KIIKKEDSSSLLEELlreieilkKLNHPNIVKLYG----VFEDENHLYLVME--YCEGGSLKDLLKENEGklSEDEILRI 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572930 123 IDGVALALEAGRQGNLPHGSISPQNI--TCHDGSLKVINFAIATSVNDAALPLEDGK---AFFAPELLVDRslnaykaep 197
Cdd:cd00180  98 LLQILEGLEYLHSNGIIHRDLKPENIllDSDNGKVKLADFGLSKLLTSDKSLLKTIVgtpAYMAPEVLLGK--------- 168
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28572930 198 RQITYRSDVYSLGGLLYWLltgttyitgeqvcttryrsdtnEAIDCVLRKALAIEPTSRFS 258
Cdd:cd00180 169 GYYSEKSDIWSLGVILYEL----------------------PELKDLIRKMLQKDPEKRPS 207
PASTA smart00740
PASTA domain;
349-409 3.14e-10

PASTA domain;


Pssm-ID: 197851  Cd Length: 67  Bit Score: 56.54  E-value: 3.14e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28572930    349 MPNLIGIDKEQAIKKLNDLGVKFRINTEHSATMPVGYVTGTSPKSGAVVDSDTEVSISLSD 409
Cdd:smart00740   7 VPDVIGKSKEEAKKLLKALGLKVEVVEEYSSDGEEGTVISQSPAAGTTVKPGSKVTLTVSK 67
SPS1 COG0515
Serine/threonine protein kinase [General function prediction only / Signal transduction ...
14-375 2.04e-13

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: 70.54  E-value: 2.04e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572930  14 YELVKCLRVARYYKMYQGYDRRLkrnVNVVLFDTEVSDKKEFSLALDTRVRQAVKLDSP-HIATIFDggedYFSDSIRQF 92
Cdd:COG0515   2 YRILRKLGEGSFGEVYLARDRKL---VALKVLAKKLESKSKEVERFLREIQILASLNHPpNIVKLYD----FFQDEGSLY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572930  93 IASESTHHEE--KSLEGCFITISKSIRLIAEVIDGVALALEAGRQGNLPHGSISPQNI--TCHDGSLKVINFAIATSVND 168
Cdd:COG0515  75 LVMEYVDGGSleDLLKKIGRKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENIllDRDGRVVKLIDFGLAKLLPD 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572930 169 AALPLEDGK---------AFFAPELLVDRSLNAYkaeprqiTYRSDVYSLGGLLYWLLTGTTYITGEQV----------- 228
Cdd:COG0515 155 PGSTSSIPAlpstsvgtpGYMAPEVLLGLSLAYA-------SSSSDIWSLGITLYELLTGLPPFEGEKNssatsqtlkii 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572930 229 -----------CTTRYRSDTNEAIDCVLRKALAIEPTSRFSSAVEMSDALRKaiEPKKKIDPLSIKDEILAQVNLPHKSS 297
Cdd:COG0515 228 lelptpslaspLSPSNPELISKAASDLLKKLLAKDPKNRLSSSSDLSHDLLA--HLKLKESDLSDLLKPDDSAPLRLSLP 305
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28572930 298 HPKRKHSNAVAFIALAICAVAAVITVSAALITTNLPDNKQAQVGAPLSNLSMPNLIGIDKEQAIKKLNDLGVKFRINT 375
Cdd:COG0515 306 PSLEALISSLNSLAISGSDLKLDDSNFSKELAPNGVSSSPHNSSSLLLSTASSKRSSLPKISARSSPSSLSSSSRQQA 383
COG2815 COG2815
Uncharacterized protein conserved in bacteria [Function unknown]
349-466 6.34e-12

Uncharacterized protein conserved in bacteria [Function unknown]


Pssm-ID: 225372 [Multi-domain]  Cd Length: 303  Bit Score: 65.13  E-value: 6.34e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572930 349 MPNLIGIDKEQAIKKLNDLGVKFRINTEHSATMPVGYVTGTSPKSGAVVDSDTEVSISLSDGMLELPNFVGA---RFEAA 425
Cdd:COG2815 164 VPDLVGMTYDEASSNLKAAGLTVNSKEYVSSDRPEGEVISQSPPAGTTVNVGSKIEIVVSKGAFVAPDLSGMftvEAEPH 243
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 28572930 426 RRGLAELRLEVKKICSGD--------TVNAQKPAGGSIVPQEIEITLET 466
Cdd:COG2815 244 PREEGDTSQEVIRDKDADvtasgtdsSVNIQPPPGGTIVLKGSEITSGI 292
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
68-268 3.06e-05

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: 45.61  E-value: 3.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572930     68 KLDSPHIATIFDGGE--DYFSDSIRQFIASEsTHHEEKSLEGCFITISkSIRLIAEVIDGVALALEAGrqgnLPHGSISP 145
Cdd:TIGR03903   34 RLYHPNIVALLDSGEapPGLLFAVFEYVPGR-TLREVLAADGALPAGE-TGRLMLQVLDALACAHNQG----IVHRDLKP 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572930    146 QNI--TCHDGS--LKVINFAIATSVNDAALPLE----------DGKAFFAPELLvdrslnayKAEPrqITYRSDVYSLGG 211
Cdd:TIGR03903  108 QNImvSQTGVRphAKVLDFGIGTLLPGVRDADVatltrttevlGTPTYCAPEQL--------RGEP--VTPNSDLYAWGL 177
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28572930    212 LLYWLLTGTTYITGEQVCTTRYR--SDTNEAIDC---------VLRKALAIEPTSRFSSAVEMSDALR 268
Cdd:TIGR03903  178 IFLECLTGQRVVQGASVAEILYQqlSPVDVSLPPwiaghplgqVLRKALNKDPRQRAASAPALAERFR 245
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
143-260 1.44e-04

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 42.52  E-value: 1.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572930    143 ISPQNITC-HDGSLKVINFAIATSVNDaalpleDGKA--------FFAPELLVDRSlnaYkaeprqiTYRSDVYSLGGLL 213
Cdd:smart00220 123 LKPENILLdEDGHVKLADFGLARQLDP------GEKLttfvgtpeYMAPEVLLGKG---Y-------GKAVDIWSLGVIL 186
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28572930    214 YWLLTG--------TTYITGEQVCTTRYRSD------TNEAIDcVLRKALAIEPTSRFSSA 260
Cdd:smart00220 187 YELLTGkppfpgddQLLELFKKIGKPKPPFPppewdiSPEAKD-LIRKLLVKDPEKRLTAE 246
Pkinase pfam00069
Protein kinase domain;
68-258 2.61e-04

Protein kinase domain;


Pssm-ID: 249558 [Multi-domain]  Cd Length: 260  Bit Score: 41.46  E-value: 2.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572930    68 KLDSPHIATIFDggedYFSDSIRQFIASEstHHEEKSL-----EGCFITISKSIRLIAEVIDGVALALEAGrqgnLPHGS 142
Cdd:pfam00069  54 RLSHPNIVRLID----AFEDKDHLYLVME--YCEGGDLfdylsRGGPLSEDEAKKIALQILRGLEYLHSNG----IIHRD 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572930   143 ISPQNITC-HDGSLKVINFAIATSVNDAALPLED--GKAFF-APELLVDRslnaykaepRQITYRSDVYSLGGLLYWLLT 218
Cdd:pfam00069 124 LKPENILLdENGVVKIADFGLAKKLTKSSSSLTTfvGTPEYmAPEVLLGG---------NGYGPKVDVWSLGVILYELLT 194
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 28572930   219 GTTYITGEQVCTTRYR-----------------SDTNEAIDcVLRKALAIEPTSRFS 258
Cdd:pfam00069 195 GKPPFSGESILDQLQLirrilgpplefdepksdSGSEEAKD-LIKKCLNKDPSKRPT 250
spoVD_pbp TIGR02214
stage V sporulation protein D; This model describes the spoVD subfamily of homologs of the ...
349-409 1.09e-03

stage V sporulation protein D; This model describes the spoVD subfamily of homologs of the cell division protein FtsI, a penicillin binding protein. This subfamily is restricted to Bacillus subtilis and related Gram-positive species with known or suspected endospore formation capability. In these species, the functional equivalent of FtsI is desginated PBP-2B, a paralog of spoVD [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Cellular processes, Sporulation and germination].


Pssm-ID: 131269 [Multi-domain]  Cd Length: 636  Bit Score: 40.18  E-value: 1.09e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28572930   349 MPNLIGIDKEQAIKKLNDLGVKfrINTEHSATmpvgYVTGTSPKSGAVVDSDTEVSISLSD 409
Cdd:TIGR02214 582 VPNLRGMKVDDAEKTLLHLGLD--VATEGFGT----RVVNQTPIPGEKVKEGTKVVLYLGE 636
 
Name Accession Description Interval E-value
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
349-408 1.75e-11

PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a group of related transmembrane sensor kinases present in many gram positive bacteria, which has been shown to regulate cell shape in Mycobacterium tubercolosis. PknB is a receptor-like transmembrane protein with an extracellular signal sensor domain (containing multiple PASTA domains) and an intracellular, eukaryotic serine/threonine kinase-like domain. The PASTA domain is found at the C-termini of several Penicillin-binding proteins (PBPs) and bacterial serine/threonine kinases. The name PASTA is derived from PBP and Serine/Threonine kinase Associated domain.


Pssm-ID: 119328  Cd Length: 62  Bit Score: 60.24  E-value: 1.75e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28572930 349 MPNLIGIDKEQAIKKLNDLGVKF-RINTEHSATMPVGYVTGTSPKSGAVVDSDTEVSISLS 408
Cdd:cd06577   2 VPDVVGMTLDEAKAALEAAGLKVgVVTEEYSDDVPKGTVISQSPAAGTKVKKGSTVTLTVS 62
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
413-464 3.42e-03

PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a group of related transmembrane sensor kinases present in many gram positive bacteria, which has been shown to regulate cell shape in Mycobacterium tubercolosis. PknB is a receptor-like transmembrane protein with an extracellular signal sensor domain (containing multiple PASTA domains) and an intracellular, eukaryotic serine/threonine kinase-like domain. The PASTA domain is found at the C-termini of several Penicillin-binding proteins (PBPs) and bacterial serine/threonine kinases. The name PASTA is derived from PBP and Serine/Threonine kinase Associated domain.


Pssm-ID: 119328  Cd Length: 62  Bit Score: 35.97  E-value: 3.42e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 28572930 413 ELPNFVGARFEAARRGLAELRLEVKKI----CSG---DTVNAQKPAGGSIVPQEIEITL 464
Cdd:cd06577   1 TVPDVVGMTLDEAKAALEAAGLKVGVVteeySDDvpkGTVISQSPAAGTKVKKGSTVTL 59
PASTA pfam03793
PASTA domain; This domain is found at the C termini of several Penicillin-binding proteins and ...
349-409 2.01e-13

PASTA domain; This domain is found at the C termini of several Penicillin-binding proteins and bacterial serine/threonine kinases. It binds the beta-lactam stem, which implicates it in sensing D-alanyl-D-alanine - the PBP transpeptidase substrate. It is a small globular fold consisting of 3 beta-sheets and an alpha-helix. The name PASTA is derived from PBP and Serine/Threonine kinase Associated domain.


Pssm-ID: 252166  Cd Length: 63  Bit Score: 65.71  E-value: 2.01e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28572930   349 MPNLIGIDKEQAIKKLNDLGVKFRINTEHSATMPVGYVTGTSPKSGAVVDSDTEVSISLSD 409
Cdd:pfam03793   3 VPDVVGLSLEEAKKLLEALGLKVGTVEEYSDDVGEGTVISQSPPAGTKVKKGSKVTLTVSK 63
PKc cd00180
Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze ...
53-258 2.34e-10

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: 59.17  E-value: 2.34e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572930  53 KEFSLALDTRVRQAV--------KLDSPHIATIFDggedYFSDSIRQFIASEstHHEEKSLEGCFITISK--SIRLIAEV 122
Cdd:cd00180  24 KIIKKEDSSSLLEELlreieilkKLNHPNIVKLYG----VFEDENHLYLVME--YCEGGSLKDLLKENEGklSEDEILRI 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572930 123 IDGVALALEAGRQGNLPHGSISPQNI--TCHDGSLKVINFAIATSVNDAALPLEDGK---AFFAPELLVDRslnaykaep 197
Cdd:cd00180  98 LLQILEGLEYLHSNGIIHRDLKPENIllDSDNGKVKLADFGLSKLLTSDKSLLKTIVgtpAYMAPEVLLGK--------- 168
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28572930 198 RQITYRSDVYSLGGLLYWLltgttyitgeqvcttryrsdtnEAIDCVLRKALAIEPTSRFS 258
Cdd:cd00180 169 GYYSEKSDIWSLGVILYEL----------------------PELKDLIRKMLQKDPEKRPS 207
PASTA smart00740
PASTA domain;
349-409 3.14e-10

PASTA domain;


Pssm-ID: 197851  Cd Length: 67  Bit Score: 56.54  E-value: 3.14e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28572930    349 MPNLIGIDKEQAIKKLNDLGVKFRINTEHSATMPVGYVTGTSPKSGAVVDSDTEVSISLSD 409
Cdd:smart00740   7 VPDVIGKSKEEAKKLLKALGLKVEVVEEYSSDGEEGTVISQSPAAGTTVKPGSKVTLTVSK 67
PASTA_Pbp2x-like_2 cd06575
PASTA domain of PBP2x-like proteins, second repeat. Penicillin-binding proteins (PBPs) are the ...
349-408 2.38e-06

PASTA domain of PBP2x-like proteins, second repeat. Penicillin-binding proteins (PBPs) are the major targets for beta-lactam antibiotics, like penicillins and cephalosporins. Beta-lactam antibiotics specifically inhibit transpeptidase activity by acylating the active site serine. PBPs catalyze key steps in the synthesis of the peptidoglycan, such as the interconnecting of glycan chains (polymers of N-glucosamine and N-acetylmuramic acid residues) and the cross-linking (transpeptidation) of short stem peptides, which are attached to glycan chains. Peptidoglycan is essential in cell division and protects bacteria from osmotic shock and lysis. PBP2x is one of the two monofunctional high molecular mass PBPs in Streptococcus pneumoniae and has been seen as the primary PBP target in beta-lactam-resistant strains. The PASTA domain is found at the C-termini of several PBPs and bacterial serine/threonine kinases. The name PASTA is derived from PBP and Serine/Threonine kinase Associated domain.


Pssm-ID: 119326  Cd Length: 54  Bit Score: 45.14  E-value: 2.38e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572930 349 MPNLIGIDKEQAIKKLNDLGVKFRINTEhsatmpvGYVTGTSPKSGAVVDSDTEVSISLS 408
Cdd:cd06575   2 MPDLTGWSKRDALKLLELLGLKVKFSGS-------GYVVSQSIAPGTKVKKGTTITVTLK 54
STKc_Yank1 cd05578
Catalytic domain of the Protein Serine/Threonine Kinase, Yank1; Serine/Threonine Kinases (STKs) ...
126-276 5.14e-05

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: 43.84  E-value: 5.14e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572930 126 VALALEAGRQGNLPHGSISPQNITC-HDGSLKVINFAIATSVNDAALPLEDG--KAFFAPELLVDRSLNaykaeprqitY 202
Cdd:cd05578 109 IVLALEYLHSKGIIHRDIKPDNILLdEQGHVHITDFNIATKVTPDTLTTSTSgtPGYMAPEVLCRQGYS----------V 178
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28572930 203 RSDVYSLGGLLYWLLTGttyitgeqvcTTRYRSDTNEAIDCVLRKALAIEPTSRFSSAVEMSDALRKAIEPKKK 276
Cdd:cd05578 179 AVDWWSLGVTAYECLRG----------KRPYRGHSRTIRDQIRAKQETADVLYPATWSTEAIDAINKLLERDPQ 242
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine kinase-like proteins; Serine ...
119-256 4.65e-04

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: 40.69  E-value: 4.65e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572930 119 IAEVIdgvaLALEAGRQGNLPHGSISPQNITCH-DGSLKVINF------AIATSVNDAALPLEDGKAF-----FAPELLV 186
Cdd:cd05579  99 IAEIV----LALEYLHSNGIIHRDLKPDNILIDsNGHLKLTDFglskvgLVRRQINLNDDEKEDKRIVgtpdyIAPEVIL 174
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572930 187 DRSLNaykaeprqitYRSDVYSLGGLLYWLLTG-------TTYITGEQVCTTRYR-----SDTNEAIDCVlRKALAIEPT 254
Cdd:cd05579 175 GQGHS----------KTVDWWSLGCILYEFLVGippfhgeTPEEIFQNILNGKIEwpedvEVSDEAIDLI-SKLLVPDPE 243

                ..
gi 28572930 255 SR 256
Cdd:cd05579 244 KR 245
STKc_PDK1 cd05581
Catalytic domain of the Protein Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; ...
119-269 7.46e-04

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: 40.25  E-value: 7.46e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572930 119 IAEVIDgvalALEAGRQGNLPHGSISPQNITC-HDGSLKVINFAIATSVNDAALPLED---------------------- 175
Cdd:cd05581 108 AAEILL----ALEYLHSKGIIHRDLKPENILLdKDMHIKITDFGTAKVLDPNSSPESNkgdatnidsqieknrrrfasfv 183
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572930 176 GKAFF-APELLVDRSlnaykaeprqITYRSDVYSLGGLLYWLLTGTT-------YITGEQV--CTTRYRSDTNEAIDCVL 245
Cdd:cd05581 184 GTAEYvSPELLNEKP----------AGKSSDLWALGCIIYQMLTGKPpfrgsneYLTFQKIlkLEYSFPPNFPPDAKDLI 253
                       170       180
                ....*....|....*....|....
gi 28572930 246 RKALAIEPTSRFSSaVEMSDALRK 269
Cdd:cd05581 254 EKLLVLDPQDRLGV-NEGYDELKA 276
PASTA_Pbp2x-like_1 cd06576
PASTA domain of PBP2x-like proteins, first repeat. Penicillin-binding proteins (PBPs) are the ...
349-403 1.40e-03

PASTA domain of PBP2x-like proteins, first repeat. Penicillin-binding proteins (PBPs) are the major targets for beta-lactam antibiotics, like penicillins and cephalosporins. Beta-lactam antibiotics specifically inhibit transpeptidase activity by acylating the active site serine. PBPs catalyze key steps in the synthesis of the peptidoglycan, such as the interconnecting of glycan chains (polymers of N-glucosamine and N-acetylmuramic acid residues) and the cross-linking (transpeptidation) of short stem peptides, which are connected to glycan chains. Peptidoglycan is essential in cell division and protects bacteria from osmotic shock and lysis. PBP2x is one of the two monofunctional high molecular mass PBPs in Streptococcus pneumoniae and has been seen as the primary PBP target in beta-lactam-resistant strains. The PASTA domain is found at the C-termini of several PBPs and bacterial serine/threonine kinases. The name PASTA is derived from PBP and Serine/Threonine kinase Associated domain.


Pssm-ID: 119327  Cd Length: 55  Bit Score: 37.10  E-value: 1.40e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 28572930 349 MPNLIGIDKEQAIKKLNDLGVKFRIntehsatmpVG---YVTGTSPKSGAVVDSDTEV 403
Cdd:cd06576   2 VPDVTGKSVEEAKKELKEAGLQPVV---------IGngkKVKKQSPKPGEKVLEGSKV 50
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; Protein Tyrosine Kinase (PTK) family; ...
89-218 1.97e-03

Catalytic domain of the Protein Tyrosine Kinase, Lyn; Protein Tyrosine Kinase (PTK) family; Lyn kinase; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lyn is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) tyr kinases. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. Lyn is expressed in B lymphocytes and myeloid cells. It exhibits both positive and negative regulatory roles in B cell receptor (BCR) signaling. Lyn, as well as Fyn and Blk, promotes B cell activation by phosphorylating ITAMs (immunoreceptor tyr activation motifs) in CD19 and in Ig components of BCR. It negatively regulates signaling by its unique ability to phosphorylate ITIMs (immunoreceptor tyr inhibition motifs) in cell surface receptors like CD22 and CD5. Lyn also plays an important role in G-CSF receptor signaling by phosphorylating a variety of adaptor molecules.


Pssm-ID: 173641 [Multi-domain]  Cd Length: 261  Bit Score: 38.85  E-value: 1.97e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572930  89 IRQFIASESTHHEEKSLEGCFITISKSIRLIAEVIDGVALAleagRQGNLPHGSISPQNITCHDGSL-KVINFAIATSVN 167
Cdd:cd05072  79 ITEYMAKGSLLDFLKSDEGGKVLLPKLIDFSAQIAEGMAYI----ERKNYIHRDLRAANVLVSESLMcKIADFGLARVIE 154
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 28572930 168 DAALPLEDGKAF----FAPELLVDRSLnaykaeprqiTYRSDVYSLGGLLYWLLT 218
Cdd:cd05072 155 DNEYTAREGAKFpikwTAPEAINFGSF----------TIKSDVWSFGILLYEIVT 199
STKc_CNK2-like cd08530
Catalytic domain of the Protein Serine/Threonine Kinase, Chlamydomonas reinhardtii CNK2, and ...
126-256 3.91e-03

Catalytic domain of the Protein Serine/Threonine Kinase, Chlamydomonas reinhardtii CNK2, and similar domains; Serine/Threonine Kinases (STKs), Chlamydomonas reinhardtii Never In Mitosis gene A (NIMA)-related kinase 1 (CNK2)-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Chlamydomonas reinhardtii CNK2-like subfamily belongs to the (NIMA)-related kinase (Nek) family. The Nek family includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily includes CNK1, and -2. 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. Chlamydomonas reinhardtii CNK2 has both cilliary and cell cycle functions. It influences flagellar length through promoting flagellar disassembly, and it regulates cell size, through influencing the size threshold at which cells commit to mitosis.


Pssm-ID: 173772 [Multi-domain]  Cd Length: 256  Bit Score: 37.81  E-value: 3.91e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572930 126 VALALEAGRQGNLPHGSISPQNI-TCHDGSLKVINFAIATSVNDAALPLEDGKAFF-APELLVDRslnAYkaeprqiTYR 203
Cdd:cd08530 112 LLRGLQALHEQKILHRDLKSANIlLVANDLVKIGDLGISKVLKKNMAKTQIGTPHYmAPEVWKGR---PY-------SYK 181
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28572930 204 SDVYSLGGLLYWLLTGTTYITGE-------QVCTTRY---RSDTNEAIDCVLRKALAIEPTSR 256
Cdd:cd08530 182 SDIWSLGCLLYEMATFAPPFEARsmqdlryKVQRGKYppiPPIYSQDLQNFIRSMLQVKPKLR 244
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; Protein Kinases (PKs), STE family, catalytic ...
119-210 4.95e-03

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: 37.57  E-value: 4.95e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572930 119 IAEVIDGVALALEAGRQGNLPHGSISPQNI--TcHDGSLKVINFAIATSVNDAalPLED---GKAFF-APELLVDrslNA 192
Cdd:cd05122 100 IAYVCKELLKGLEYLHSNGIIHRDIKAANIllT-SDGEVKLIDFGLSAQLSDT--KARNtmvGTPYWmAPEVING---KP 173
                        90
                ....*....|....*...
gi 28572930 193 YkaeprqiTYRSDVYSLG 210
Cdd:cd05122 174 Y-------DYKADIWSLG 184
STKc_MAPKKK cd06606
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein Kinase ...
140-219 5.34e-03

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: 37.54  E-value: 5.34e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572930 140 HGSISPQNI-TCHDGSLKVINFAIATSVNDAALPLEDGK-----AFFAPELLVDrslNAYkaeprqiTYRSDVYSLGGLL 213
Cdd:cd06606 124 HRDIKGANIlVDSDGVVKLADFGCAKRLGDIETGEGTGSvrgtpYWMAPEVIRG---EEY-------GRAADIWSLGCTV 193

                ....*.
gi 28572930 214 YWLLTG 219
Cdd:cd06606 194 IEMATG 199
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, MAP kinase kinase 4; Protein kinases ...
140-219 7.93e-03

Catalytic domain of the dual-specificity Protein Kinase, MAP kinase kinase 4; Protein kinases (PKs), MAP kinase kinase 4 (MKK4) subfamily, catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. The MKK4 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). MKK4 is a dual-specificity PK that phosphorylates and activates the downstream targets, c-Jun N-terminal kinase (JNK) and p38 MAPK, on specific threonine and tyrosine residues. 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. Their activation is associated with the induction of cell death. Mice deficient in MKK4 die during embryogenesis and display anemia, severe liver hemorrhage, and abnormal hepatogenesis. MKK4 may also play roles in the immune system and in cardiac hypertrophy. It plays a major role in cancer as a tumor and metastasis suppressor. Under certain conditions, MKK4 is pro-oncogenic.


Pssm-ID: 132947 [Multi-domain]  Cd Length: 288  Bit Score: 36.96  E-value: 7.93e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572930 140 HGSISPQNITCHD-GSLKVINFAIATS-VNDAALPLEDG-KAFFAPELLVDRSLNAYKAeprqityRSDVYSLGGLLYWL 216
Cdd:cd06616 131 HRDVKPSNILLDRnGNIKLCDFGISGQlVDSIAKTRDAGcRPYMAPERIDPSARDGYDV-------RSDVWSLGITLYEV 203

                ...
gi 28572930 217 LTG 219
Cdd:cd06616 204 ATG 206
SPS1 COG0515
Serine/threonine protein kinase [General function prediction only / Signal transduction ...
14-375 2.04e-13

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: 70.54  E-value: 2.04e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572930  14 YELVKCLRVARYYKMYQGYDRRLkrnVNVVLFDTEVSDKKEFSLALDTRVRQAVKLDSP-HIATIFDggedYFSDSIRQF 92
Cdd:COG0515   2 YRILRKLGEGSFGEVYLARDRKL---VALKVLAKKLESKSKEVERFLREIQILASLNHPpNIVKLYD----FFQDEGSLY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572930  93 IASESTHHEE--KSLEGCFITISKSIRLIAEVIDGVALALEAGRQGNLPHGSISPQNI--TCHDGSLKVINFAIATSVND 168
Cdd:COG0515  75 LVMEYVDGGSleDLLKKIGRKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENIllDRDGRVVKLIDFGLAKLLPD 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572930 169 AALPLEDGK---------AFFAPELLVDRSLNAYkaeprqiTYRSDVYSLGGLLYWLLTGTTYITGEQV----------- 228
Cdd:COG0515 155 PGSTSSIPAlpstsvgtpGYMAPEVLLGLSLAYA-------SSSSDIWSLGITLYELLTGLPPFEGEKNssatsqtlkii 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572930 229 -----------CTTRYRSDTNEAIDCVLRKALAIEPTSRFSSAVEMSDALRKaiEPKKKIDPLSIKDEILAQVNLPHKSS 297
Cdd:COG0515 228 lelptpslaspLSPSNPELISKAASDLLKKLLAKDPKNRLSSSSDLSHDLLA--HLKLKESDLSDLLKPDDSAPLRLSLP 305
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28572930 298 HPKRKHSNAVAFIALAICAVAAVITVSAALITTNLPDNKQAQVGAPLSNLSMPNLIGIDKEQAIKKLNDLGVKFRINT 375
Cdd:COG0515 306 PSLEALISSLNSLAISGSDLKLDDSNFSKELAPNGVSSSPHNSSSLLLSTASSKRSSLPKISARSSPSSLSSSSRQQA 383
COG2815 COG2815
Uncharacterized protein conserved in bacteria [Function unknown]
349-466 6.34e-12

Uncharacterized protein conserved in bacteria [Function unknown]


Pssm-ID: 225372 [Multi-domain]  Cd Length: 303  Bit Score: 65.13  E-value: 6.34e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572930 349 MPNLIGIDKEQAIKKLNDLGVKFRINTEHSATMPVGYVTGTSPKSGAVVDSDTEVSISLSDGMLELPNFVGA---RFEAA 425
Cdd:COG2815 164 VPDLVGMTYDEASSNLKAAGLTVNSKEYVSSDRPEGEVISQSPPAGTTVNVGSKIEIVVSKGAFVAPDLSGMftvEAEPH 243
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 28572930 426 RRGLAELRLEVKKICSGD--------TVNAQKPAGGSIVPQEIEITLET 466
Cdd:COG2815 244 PREEGDTSQEVIRDKDADvtasgtdsSVNIQPPPGGTIVLKGSEITSGI 292
COG2815 COG2815
Uncharacterized protein conserved in bacteria [Function unknown]
312-472 1.02e-09

Uncharacterized protein conserved in bacteria [Function unknown]


Pssm-ID: 225372 [Multi-domain]  Cd Length: 303  Bit Score: 58.58  E-value: 1.02e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572930 312 LAICAVAAVITVSAALITTNLPDNKQaqvgaplsnlsMPNLIGIDKEQAIKKLNDLGVKFRINTEHSATMPVGYVTGTSP 391
Cdd:COG2815   2 LSLLVSLVVAGVLLATFFPVSPDKVK-----------VPNVAGLDEEDAKAELQKAGLEVGVRERESDKVPEGKVIRTDP 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572930 392 KSGAVVDSDTEVSISLSDG--MLELPNFVGARFEAARRGLAELRLEVKKIC--------SGDTVNAQKPAGGSIVPQEIE 461
Cdd:COG2815  71 KAGTVVKQGSKVTLFVSTGaqYITVPDVVGLTIEEAVAKLKAYGLNLSKITqeevsdevPAGTVISQSPSAGTEVKPGET 150
                       170
                ....*....|.
gi 28572930 462 ITLETCSGAST 472
Cdd:COG2815 151 VKLTVSKGPET 161
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
68-268 3.06e-05

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: 45.61  E-value: 3.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572930     68 KLDSPHIATIFDGGE--DYFSDSIRQFIASEsTHHEEKSLEGCFITISkSIRLIAEVIDGVALALEAGrqgnLPHGSISP 145
Cdd:TIGR03903   34 RLYHPNIVALLDSGEapPGLLFAVFEYVPGR-TLREVLAADGALPAGE-TGRLMLQVLDALACAHNQG----IVHRDLKP 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572930    146 QNI--TCHDGS--LKVINFAIATSVNDAALPLE----------DGKAFFAPELLvdrslnayKAEPrqITYRSDVYSLGG 211
Cdd:TIGR03903  108 QNImvSQTGVRphAKVLDFGIGTLLPGVRDADVatltrttevlGTPTYCAPEQL--------RGEP--VTPNSDLYAWGL 177
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28572930    212 LLYWLLTGTTYITGEQVCTTRYR--SDTNEAIDC---------VLRKALAIEPTSRFSSAVEMSDALR 268
Cdd:TIGR03903  178 IFLECLTGQRVVQGASVAEILYQqlSPVDVSLPPwiaghplgqVLRKALNKDPRQRAASAPALAERFR 245
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
143-260 1.44e-04

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 42.52  E-value: 1.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572930    143 ISPQNITC-HDGSLKVINFAIATSVNDaalpleDGKA--------FFAPELLVDRSlnaYkaeprqiTYRSDVYSLGGLL 213
Cdd:smart00220 123 LKPENILLdEDGHVKLADFGLARQLDP------GEKLttfvgtpeYMAPEVLLGKG---Y-------GKAVDIWSLGVIL 186
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28572930    214 YWLLTG--------TTYITGEQVCTTRYRSD------TNEAIDcVLRKALAIEPTSRFSSA 260
Cdd:smart00220 187 YELLTGkppfpgddQLLELFKKIGKPKPPFPppewdiSPEAKD-LIRKLLVKDPEKRLTAE 246
Pkinase pfam00069
Protein kinase domain;
68-258 2.61e-04

Protein kinase domain;


Pssm-ID: 249558 [Multi-domain]  Cd Length: 260  Bit Score: 41.46  E-value: 2.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572930    68 KLDSPHIATIFDggedYFSDSIRQFIASEstHHEEKSL-----EGCFITISKSIRLIAEVIDGVALALEAGrqgnLPHGS 142
Cdd:pfam00069  54 RLSHPNIVRLID----AFEDKDHLYLVME--YCEGGDLfdylsRGGPLSEDEAKKIALQILRGLEYLHSNG----IIHRD 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572930   143 ISPQNITC-HDGSLKVINFAIATSVNDAALPLED--GKAFF-APELLVDRslnaykaepRQITYRSDVYSLGGLLYWLLT 218
Cdd:pfam00069 124 LKPENILLdENGVVKIADFGLAKKLTKSSSSLTTfvGTPEYmAPEVLLGG---------NGYGPKVDVWSLGVILYELLT 194
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 28572930   219 GTTYITGEQVCTTRYR-----------------SDTNEAIDcVLRKALAIEPTSRFS 258
Cdd:pfam00069 195 GKPPFSGESILDQLQLirrilgpplefdepksdSGSEEAKD-LIKKCLNKDPSKRPT 250
spoVD_pbp TIGR02214
stage V sporulation protein D; This model describes the spoVD subfamily of homologs of the ...
349-409 1.09e-03

stage V sporulation protein D; This model describes the spoVD subfamily of homologs of the cell division protein FtsI, a penicillin binding protein. This subfamily is restricted to Bacillus subtilis and related Gram-positive species with known or suspected endospore formation capability. In these species, the functional equivalent of FtsI is desginated PBP-2B, a paralog of spoVD [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Cellular processes, Sporulation and germination].


Pssm-ID: 131269 [Multi-domain]  Cd Length: 636  Bit Score: 40.18  E-value: 1.09e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28572930   349 MPNLIGIDKEQAIKKLNDLGVKfrINTEHSATmpvgYVTGTSPKSGAVVDSDTEVSISLSD 409
Cdd:TIGR02214 582 VPNLRGMKVDDAEKTLLHLGLD--VATEGFGT----RVVNQTPIPGEKVKEGTKVVLYLGE 636
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.11
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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