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Conserved domains on  [gi|29897506|gb|AAP10782|]
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Serine/threonine protein kinase [Bacillus cereus ATCC 14579]

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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 ...
17-203 1.09e-51

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: 178.58  E-value: 1.09e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29897506  17 IGGGGMANVYLAHDDILGRDVAVKILRLDysNNEEFIKRFHREAQSVTTLSHPNIVNMYDVGEEDGIYYLVMEYVPGQTL 96
Cdd:cd00180   1 LGEGGFGTVYLARDKKTGKKVAIKIIKKE--DSSSLLEELLREIEILKKLNHPNIVKLYGVFEDENHLYLVMEYCEGGSL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29897506  97 KQYIIER-GMLPIGEALDIMEQLTSAMAHAHHFEIVHRDIKPHNILI-RADGIIKVTDFGiATATSATTITHTNSVLGSV 174
Cdd:cd00180  79 KDLLKENeGKLSEDEILRILLQILEGLEYLHSNGIIHRDLKPENILLdSDNGKVKLADFG-LSKLLTSDKSLLKTIVGTP 157
                       170       180       190
                ....*....|....*....|....*....|
gi 29897506 175 HYLSPEQARG-GIANKQSDIYSLGIVMFEL 203
Cdd:cd00180 158 AYMAPEVLLGkGYYSEKSDIWSLGVILYEL 187
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
370-431 2.75e-15

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: 71.41  E-value: 2.75e-15
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29897506 370 KVPDVAGMKYTTAVNTLVEKGFEVTEPNIVYTDDVEVGDVIKTDPVAGRVVKENAKITIYQS 431
Cdd:cd06577   1 TVPDVVGMTLDEAKAALEAAGLKVGVVTEEYSDDVPKGTVISQSPAAGTKVKKGSTVTLTVS 62
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
508-565 8.92e-12

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: 61.39  E-value: 8.92e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 29897506 508 DFSGWTENSVTGYLNERKLT-SDIKREYSDTVEKGLVISQFPKPGTPLKEGDKVTIIIS 565
Cdd:cd06577   4 DVVGMTLDEAKAALEAAGLKvGVVTEEYSDDVPKGTVISQSPAAGTKVKKGSTVTLTVS 62
PASTA pfam03793
PASTA domain; This domain is found at the C termini of several Penicillin-binding proteins and ...
438-499 7.35e-07

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: 47.23  E-value: 7.35e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29897506   438 KMANFTGQNFESVKAELEEK-YKQVTVNYIENDKPKGEIVEQIPTPDQMViEAEQELKIWVSK 499
Cdd:pfam03793   2 TVPDVVGLSLEEAKKLLEALgLKVGTVEEYSDDVGEGTVISQSPPAGTKV-KKGSKVTLTVSK 63
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
11-264 4.83e-71

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


:

Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 232.42  E-value: 4.83e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29897506     11 YKLLKMIGGGGMANVYLAHDDILGRDVAVKILRLDysNNEEFIKRFHREAQSVTTLSHPNIVNMYDVGEEDGIYYLVMEY 90
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKK--KIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29897506     91 VPGQTLKQYIIERGMLPIGEALDIMEQLTSAMAHAHHFEIVHRDIKPHNILIRADGIIKVTDFGiaTATSATTITHTNSV 170
Cdd:smart00220  79 CEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFG--LARQLDPGEKLTTF 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29897506    171 LGSVHYLSPEQARGGIANKQSDIYSLGIVMFELLTGRQPFSGESAVAIALKHLQSEIPSPKRWNENIPQSVENIILKATA 250
Cdd:smart00220 157 VGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISPEAKDLIRKLLV 236
                          250
                   ....*....|....
gi 29897506    251 KDPFHRYQSANAMK 264
Cdd:smart00220 237 KDPEKRLTAEEALQ 250
COG2815 COG2815
Uncharacterized protein conserved in bacteria [Function unknown]
341-647 3.29e-47

Uncharacterized protein conserved in bacteria [Function unknown]


:

Pssm-ID: 225372 [Multi-domain]  Cd Length: 303  Bit Score: 168.75  E-value: 3.29e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29897506 341 VLISTFLFLAIGITLAlTVIPglFIPKDVKVPDVAGMKYTTAVNTLVEKGFEVTEPNIvYTDDVEVGDVIKTDPVAGRVV 420
Cdd:COG2815   1 LLSLLVSLVVAGVLLA-TFFP--VSPDKVKVPNVAGLDEEDAKAELQKAGLEVGVRER-ESDKVPEGKVIRTDPKAGTVV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29897506 421 KENAKITIYQSGGKKKSKMANFTGQNFESVKAELEEKYK---QVTVNYIENDKPKGEIVEQIPTPDQmVIEAEQELKIWV 497
Cdd:COG2815  77 KQGSKVTLFVSTGAQYITVPDVVGLTIEEAVAKLKAYGLnlsKITQEEVSDEVPAGTVISQSPSAGT-EVKPGETVKLTV 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29897506 498 SKGPYQIRPGDFSGWTENSVTGYLNERKLTSDIKREYSDTVEKGLVISQFPKPGTPLKEGDKVTIIISDGQKPKVTKTVK 577
Cdd:COG2815 156 SKGPETITVPDLVGMTYDEASSNLKAAGLTVNSKEYVSSDRPEGEVISQSPPAGTTVNVGSKIEIVVSKGAFVAPDLSGM 235
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29897506 578 LdNISIPYEPAVTGEKKPQTIEIykEDMQQKMDRPVETRTITESATISLEFVIQEGSKGHYKIVRDGVTI 647
Cdd:COG2815 236 F-TVEAEPHPREEGDTSQEVIRD--KDADVTASGTDSSVNIQPPPGGTIVLKGSEITSGIYQVVVNDKVI 302
 
Name Accession Description Interval E-value
PKc cd00180
Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze ...
17-203 1.09e-51

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: 178.58  E-value: 1.09e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29897506  17 IGGGGMANVYLAHDDILGRDVAVKILRLDysNNEEFIKRFHREAQSVTTLSHPNIVNMYDVGEEDGIYYLVMEYVPGQTL 96
Cdd:cd00180   1 LGEGGFGTVYLARDKKTGKKVAIKIIKKE--DSSSLLEELLREIEILKKLNHPNIVKLYGVFEDENHLYLVMEYCEGGSL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29897506  97 KQYIIER-GMLPIGEALDIMEQLTSAMAHAHHFEIVHRDIKPHNILI-RADGIIKVTDFGiATATSATTITHTNSVLGSV 174
Cdd:cd00180  79 KDLLKENeGKLSEDEILRILLQILEGLEYLHSNGIIHRDLKPENILLdSDNGKVKLADFG-LSKLLTSDKSLLKTIVGTP 157
                       170       180       190
                ....*....|....*....|....*....|
gi 29897506 175 HYLSPEQARG-GIANKQSDIYSLGIVMFEL 203
Cdd:cd00180 158 AYMAPEVLLGkGYYSEKSDIWSLGVILYEL 187
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
370-431 2.75e-15

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: 71.41  E-value: 2.75e-15
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29897506 370 KVPDVAGMKYTTAVNTLVEKGFEVTEPNIVYTDDVEVGDVIKTDPVAGRVVKENAKITIYQS 431
Cdd:cd06577   1 TVPDVVGMTLDEAKAALEAAGLKVGVVTEEYSDDVPKGTVISQSPAAGTKVKKGSTVTLTVS 62
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
508-565 8.92e-12

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: 61.39  E-value: 8.92e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 29897506 508 DFSGWTENSVTGYLNERKLT-SDIKREYSDTVEKGLVISQFPKPGTPLKEGDKVTIIIS 565
Cdd:cd06577   4 DVVGMTLDEAKAALEAAGLKvGVVTEEYSDDVPKGTVISQSPAAGTKVKKGSTVTLTVS 62
PASTA pfam03793
PASTA domain; This domain is found at the C termini of several Penicillin-binding proteins and ...
508-566 9.34e-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: 64.17  E-value: 9.34e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 29897506   508 DFSGWTENSVTGYLNERKLTSDIKREYSDTVEKGLVISQFPKPGTPLKEGDKVTIIISD 566
Cdd:pfam03793   5 DVVGLSLEEAKKLLEALGLKVGTVEEYSDDVGEGTVISQSPPAGTKVKKGSKVTLTVSK 63
PASTA pfam03793
PASTA domain; This domain is found at the C termini of several Penicillin-binding proteins and ...
369-432 1.51e-11

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: 60.71  E-value: 1.51e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29897506   369 VKVPDVAGMKYTTAVNTLVEKGFEVTEPNiVYTDDVEVGDVIKTDPVAGRVVKENAKITIYQSG 432
Cdd:pfam03793   1 VTVPDVVGLSLEEAKKLLEALGLKVGTVE-EYSDDVGEGTVISQSPPAGTKVKKGSKVTLTVSK 63
PASTA smart00740
PASTA domain;
508-566 7.52e-11

PASTA domain;


Pssm-ID: 197851  Cd Length: 67  Bit Score: 58.86  E-value: 7.52e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 29897506    508 DFSGWTENSVTGYLNERKLTSDIKREYSDTVEKGLVISQFPKPGTPLKEGDKVTIIISD 566
Cdd:smart00740   9 DVIGKSKEEAKKLLKALGLKVEVVEEYSSDGEEGTVISQSPAAGTTVKPGSKVTLTVSK 67
PASTA smart00740
PASTA domain;
366-429 1.00e-10

PASTA domain;


Pssm-ID: 197851  Cd Length: 67  Bit Score: 58.47  E-value: 1.00e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29897506    366 PKDVKVPDVAGMKYTTAVNTLVEKGFEVTEPNiVYTDDVEVGDVIKTDPVAGRVVKENAKITIY 429
Cdd:smart00740   2 PEKVEVPDVIGKSKEEAKKLLKALGLKVEVVE-EYSSDGEEGTVISQSPAAGTTVKPGSKVTLT 64
PRK14879 PRK14879
serine/threonine protein kinase; Provisional
14-154 6.08e-09

serine/threonine protein kinase; Provisional


Pssm-ID: 237847  Cd Length: 211  Bit Score: 55.30  E-value: 6.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29897506   14 LKMIGGGGMANVYLAhdDILGRDVAVK--------ILRLDYSNNEEfikRFHREAQSVTTLsHPNIVN---MYDVGEEDG 82
Cdd:PRK14879   1 MKLIKRGAEAEIYLG--DFLGIKAVIKwripkryrHPELDERIRRE---RTRREARIMSRA-RKAGVNvpaVYFVDPENF 74
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29897506   83 IyyLVMEYVPGQTLKQYIIERGMLPIGEALDIMEQLtsAMAHAHHfeIVHRDIKPHNILIRADGIIkVTDFG 154
Cdd:PRK14879  75 I--IVMEYIEGEPLKDLINSNGMEELELSREIGRLV--GKLHSAG--IIHGDLTTSNMILSGGKIY-LIDFG 139
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
17-154 1.28e-08

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: 54.14  E-value: 1.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29897506    17 IGGGGMANVYLahDDILGRDVAVK--------ILRLDYSNNEEfikRFHREAQsVTTLSHPNIVN---MYDVGEEDGIyy 85
Cdd:TIGR03724   2 IAKGAEAIIYL--GDFLGLKAVIKervpksyrHPELDERIRRE---RTRNEAR-LLSRARKAGVNtpvVYDVDPDNKT-- 73
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29897506    86 LVMEYVPGQTLKQYIIERG---MLPIGEALDIMeqltsamahaHHFEIVHRDIKPHNILIRADGIIkVTDFG 154
Cdd:TIGR03724  74 IVMEYIEGKPLKDVIEEGNdelLREIGRLVGKL----------HKAGIVHGDLTTSNIIVRDDKLY-LIDFG 134
COG3642 COG3642
Mn2+-dependent serine/threonine protein kinase [Signal transduction mechanisms]
14-154 1.76e-08

Mn2+-dependent serine/threonine protein kinase [Signal transduction mechanisms]


Pssm-ID: 226168  Cd Length: 204  Bit Score: 53.83  E-value: 1.76e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29897506  14 LKMIGGGGMANVYLahDDILGRDVAVK--------ILRLDYSNNEEfikRFHREAQsVTTLSHPNIVN---MYDVGEEDG 82
Cdd:COG3642   1 MDLIKQGAEAIIYL--TDFLGLPAVVKeripkryrHPELDEKLRRE---RTRREAR-ILAKAREAGVPvpiVYDVDPDNG 74
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29897506  83 IyyLVMEYVPGQTLKQYIIERgmlpigeALDIMEQLTSAMAHAHHFEIVHRDIKPHNILIRADGIIKVtDFG 154
Cdd:COG3642  75 L--IVMEYIEGELLKDALEEA-------RPDLLREVGRLVGKLHKAGIVHGDLTTSNIILSGGRIYFI-DFG 136
PASTA pfam03793
PASTA domain; This domain is found at the C termini of several Penicillin-binding proteins and ...
438-499 7.35e-07

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: 47.23  E-value: 7.35e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29897506   438 KMANFTGQNFESVKAELEEK-YKQVTVNYIENDKPKGEIVEQIPTPDQMViEAEQELKIWVSK 499
Cdd:pfam03793   2 TVPDVVGLSLEEAKKLLEALgLKVGTVEEYSDDVGEGTVISQSPPAGTKV-KKGSKVTLTVSK 63
PASTA smart00740
PASTA domain;
433-499 1.23e-04

PASTA domain;


Pssm-ID: 197851  Cd Length: 67  Bit Score: 40.75  E-value: 1.23e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29897506    433 GKKKSKMANFTGQNFESVKAELEEK-YKQVTVNYIENDKPKGEIVEQIPTPDQmVIEAEQELKIWVSK 499
Cdd:smart00740   1 GPEKVEVPDVIGKSKEEAKKLLKALgLKVEVVEEYSSDGEEGTVISQSPAAGT-TVKPGSKVTLTVSK 67
YrbL-PhoP_reg pfam10707
PhoP regulatory network protein YrbL; This is a family of proteins that are activated by PhoP. ...
86-143 1.50e-03

PhoP regulatory network protein YrbL; This is a family of proteins that are activated by PhoP. PhoP protein controls the expression of a large number of genes that mediate adaptation to low Mg2+ environments and/or virulence in several bacterial species. YbrL is proposed to be acting in a loop activity with PhoP and PrmA analogous to the multicomponent loop in Salmonella where the PhoP-dependent PmrD protein activates the regulatory protein PmrA, and the activated PmrA then represses transcription from the PmrD promoter which harbours binding sites for both the PhoP and PmrA proteins. Expression of YrbL is induced in low Mg2+ in a PhoP-dependent fashion and repressed by Fe3+ in a PmrA-dependent manner.


Pssm-ID: 151200  Cd Length: 199  Bit Score: 39.16  E-value: 1.50e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29897506    86 LVMEYV------PGQTLKQYIIERGMLPigEALDIMEQLTSAMAHAHhfeIVHRDIKPHNILIR 143
Cdd:pfam10707  94 LVTERIrdadgnISPTLEDLLKNGGLTA--ALREALNEFKRYLLDNH---IVARDLNPHNIVYG 152
PHA02882 PHA02882
putative serine/threonine kinase; Provisional
10-212 8.66e-03

putative serine/threonine kinase; Provisional


Pssm-ID: 165211  Cd Length: 294  Bit Score: 37.24  E-value: 8.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29897506   10 RYKLLKMIGGGGMANVY---LAHDDILGRDVAVKILRLdysNNEEFI------------------KRFHreaqsvtTLSH 68
Cdd:PHA02882  13 EWKIDKLIGCGGFGCVYetqCASDHCINNQAVAKIENL---ENETIVmetlvynniydidkialwKNIH-------NIDH 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29897506   69 PNIVNMYDVG--EEDGIYY--LVMEYVPGQTLKqyIIERgMLPIGEAL--DIMEQLTSAMAHAHHFEIVHRDIKPHNILI 142
Cdd:PHA02882  83 LGIPKYYGCGsfKRCRMYYrfILLEKLVENTKE--IFKR-IKCKNKKLikNIMKDMLTTLEYIHEHGISHGDIKPENIMV 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29897506  143 RADGIIKVTDFGIAT------ATSATTITHTNSVLGSVHYLSPEQARGGIANKQSDIYSLGIVMFELLTGRQPFSG 212
Cdd:PHA02882 160 DGNNRGYIIDYGIAShfiihgKHIEYSKEQKDLHRGTLYYAGLDAHNGACVTRRGDLESLGYCMLKWAGIKLPWKG 235
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
11-264 4.83e-71

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 232.42  E-value: 4.83e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29897506     11 YKLLKMIGGGGMANVYLAHDDILGRDVAVKILRLDysNNEEFIKRFHREAQSVTTLSHPNIVNMYDVGEEDGIYYLVMEY 90
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKK--KIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29897506     91 VPGQTLKQYIIERGMLPIGEALDIMEQLTSAMAHAHHFEIVHRDIKPHNILIRADGIIKVTDFGiaTATSATTITHTNSV 170
Cdd:smart00220  79 CEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFG--LARQLDPGEKLTTF 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29897506    171 LGSVHYLSPEQARGGIANKQSDIYSLGIVMFELLTGRQPFSGESAVAIALKHLQSEIPSPKRWNENIPQSVENIILKATA 250
Cdd:smart00220 157 VGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISPEAKDLIRKLLV 236
                          250
                   ....*....|....
gi 29897506    251 KDPFHRYQSANAMK 264
Cdd:smart00220 237 KDPEKRLTAEEALQ 250
COG2815 COG2815
Uncharacterized protein conserved in bacteria [Function unknown]
341-647 3.29e-47

Uncharacterized protein conserved in bacteria [Function unknown]


Pssm-ID: 225372 [Multi-domain]  Cd Length: 303  Bit Score: 168.75  E-value: 3.29e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29897506 341 VLISTFLFLAIGITLAlTVIPglFIPKDVKVPDVAGMKYTTAVNTLVEKGFEVTEPNIvYTDDVEVGDVIKTDPVAGRVV 420
Cdd:COG2815   1 LLSLLVSLVVAGVLLA-TFFP--VSPDKVKVPNVAGLDEEDAKAELQKAGLEVGVRER-ESDKVPEGKVIRTDPKAGTVV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29897506 421 KENAKITIYQSGGKKKSKMANFTGQNFESVKAELEEKYK---QVTVNYIENDKPKGEIVEQIPTPDQmVIEAEQELKIWV 497
Cdd:COG2815  77 KQGSKVTLFVSTGAQYITVPDVVGLTIEEAVAKLKAYGLnlsKITQEEVSDEVPAGTVISQSPSAGT-EVKPGETVKLTV 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29897506 498 SKGPYQIRPGDFSGWTENSVTGYLNERKLTSDIKREYSDTVEKGLVISQFPKPGTPLKEGDKVTIIISDGQKPKVTKTVK 577
Cdd:COG2815 156 SKGPETITVPDLVGMTYDEASSNLKAAGLTVNSKEYVSSDRPEGEVISQSPPAGTTVNVGSKIEIVVSKGAFVAPDLSGM 235
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29897506 578 LdNISIPYEPAVTGEKKPQTIEIykEDMQQKMDRPVETRTITESATISLEFVIQEGSKGHYKIVRDGVTI 647
Cdd:COG2815 236 F-TVEAEPHPREEGDTSQEVIRD--KDADVTASGTDSSVNIQPPPGGTIVLKGSEITSGIYQVVVNDKVI 302
SPS1 COG0515
Serine/threonine protein kinase [General function prediction only / Signal transduction ...
11-353 7.20e-58

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: 201.51  E-value: 7.20e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29897506  11 YKLLKMIGGGGMANVYLAHDDilgRDVAVKILRLDYSNNEEFIKRFHREAQSVTTLSHP-NIVNMYDVGEEDGIYYLVME 89
Cdd:COG0515   2 YRILRKLGEGSFGEVYLARDR---KLVALKVLAKKLESKSKEVERFLREIQILASLNHPpNIVKLYDFFQDEGSLYLVME 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29897506  90 YVPGQTLKQYI---IERGMLPIGEALDIMEQLTSAMAHAHHFEIVHRDIKPHNILIRADG-IIKVTDFG-----IATATS 160
Cdd:COG0515  79 YVDGGSLEDLLkkiGRKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGrVVKLIDFGlakllPDPGST 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29897506 161 ATTITHTNSVLGSVHYLSPEQARGGI---ANKQSDIYSLGIVMFELLTGRQPFSGES---AVAIALKHLQSE------IP 228
Cdd:COG0515 159 SSIPALPSTSVGTPGYMAPEVLLGLSlayASSSSDIWSLGITLYELLTGLPPFEGEKnssATSQTLKIILELptpslaSP 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29897506 229 SPKRWNENIPQSVENIILKATAKDPFHRYQSANAMKRDIETALYPERINEQPFYIPEDMEATKAIPIIQQEQLFENVSDE 308
Cdd:COG0515 239 LSPSNPELISKAASDLLKKLLAKDPKNRLSSSSDLSHDLLAHLKLKESDLSDLLKPDDSAPLRLSLPPSLEALISSLNSL 318
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 29897506 309 TIVLKGSKVEEPIRAEAAELDKKKKRSNKWLKVLISTFLFLAIGI 353
Cdd:COG0515 319 AISGSDLKLDDSNFSKELAPNGVSSSPHNSSSLLLSTASSKRSSL 363
Pkinase pfam00069
Protein kinase domain;
11-264 1.75e-57

Protein kinase domain;


Pssm-ID: 249558 [Multi-domain]  Cd Length: 260  Bit Score: 196.31  E-value: 1.75e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29897506    11 YKLLKMIGGGGMANVYLAHDDILGRDVAVKILRLDySNNEEFIKRFHREAQSVTTLSHPNIVNMYDVGEEDGIYYLVMEY 90
Cdd:pfam00069   1 YELLRKLGSGSFGTVYKAKHKGTGKIVAVKILKKR-SEKSKKDQTARREIRILRRLSHPNIVRLIDAFEDKDHLYLVMEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29897506    91 VPGQTLKQYIIERGMLPIGEALDIMEQLTSAMAHAHHFEIVHRDIKPHNILIRADGIIKVTDFGiATATSATTITHTNSV 170
Cdd:pfam00069  80 CEGGDLFDYLSRGGPLSEDEAKKIALQILRGLEYLHSNGIIHRDLKPENILLDENGVVKIADFG-LAKKLTKSSSSLTTF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29897506   171 LGSVHYLSPEQARGGI-ANKQSDIYSLGIVMFELLTGRQPFSGESAV---AIALKHLQSEIPSPKRWNENIPQSVENIIL 246
Cdd:pfam00069 159 VGTPEYMAPEVLLGGNgYGPKVDVWSLGVILYELLTGKPPFSGESILdqlQLIRRILGPPLEFDEPKSDSGSEEAKDLIK 238
                         250
                  ....*....|....*...
gi 29897506   247 KATAKDPFHRYQSANAMK 264
Cdd:pfam00069 239 KCLNKDPSKRPTAEEILQ 256
pknD PRK13184
serine/threonine-protein kinase; Reviewed
10-271 1.21e-45

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 173.42  E-value: 1.21e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29897506   10 RYKLLKMIGGGGMANVYLAHDDILGRDVAVKILRLDYSNNEEFIKRFHREAQSVTTLSHPNIVNMYDV-GEEDGIYYlVM 88
Cdd:PRK13184   3 RYDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIREDLSENPLLKKRFLREAKIAADLIHPGIVPVYSIcSDGDPVYY-TM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29897506   89 EYVPGQTLKQY---IIERGMLP--------IGEALDIMEQLTSAMAHAHHFEIVHRDIKPHNILIRADGIIKVTDFGIAT 157
Cdd:PRK13184  82 PYIEGYTLKSLlksVWQKESLSkelaektsVGAFLSIFHKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWGAAI 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29897506  158 ATSATTITHTNS-----------------VLGSVHYLSPEQARGGIANKQSDIYSLGIVMFELLTGRQPFSGESAVAIAL 220
Cdd:PRK13184 162 FKKLEEEDLLDIdvdernicyssmtipgkIVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPYRRKKGRKISY 241
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 29897506  221 KHlqsEIPSPKRW--NENIPQSVENIILKATAKDPFHRYQSANAMKRDIETAL 271
Cdd:PRK13184 242 RD---VILSPIEVapYREIPPFLSQIAMKALAVDPAERYSSVQELKQDLEPHL 291
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
34-263 2.41e-42

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: 163.86  E-value: 2.41e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29897506     34 GRDVAVKILRLDYSNNEEFIKRFHREAQSVTTLSHPNIVNMYDVGE-EDGIYYLVMEYVPGQTLKQYIIERGMLPIGEAL 112
Cdd:TIGR03903    3 GHEVAIKLLRTDAPEEEHQRARFRRETALCARLYHPNIVALLDSGEaPPGLLFAVFEYVPGRTLREVLAADGALPAGETG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29897506    113 DIMEQLTSAMAHAHHFEIVHRDIKPHNILIRADGI---IKVTDFGI------ATATSATTITHTNSVLGSVHYLSPEQAR 183
Cdd:TIGR03903   83 RLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGVrphAKVLDFGIgtllpgVRDADVATLTRTTEVLGTPTYCAPEQLR 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29897506    184 GGIANKQSDIYSLGIVMFELLTGRQPFSGESAVAIALKHLqseipSPKrwNENIPQSVE-----NIILKATAKDPFHRYQ 258
Cdd:TIGR03903  163 GEPVTPNSDLYAWGLIFLECLTGQRVVQGASVAEILYQQL-----SPV--DVSLPPWIAghplgQVLRKALNKDPRQRAA 235

                   ....*
gi 29897506    259 SANAM 263
Cdd:TIGR03903  236 SAPAL 240
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
6-235 5.55e-25

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 105.67  E-value: 5.55e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29897506    6 RLNDrYKLLKMIGGGGMANVYLAHDDILGRDVAVKILRldysnNEEFIK-----RFHREAQSVTTLSHPNIVNMYDVGEE 80
Cdd:PTZ00263  16 KLSD-FEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLK-----KREILKmkqvqHVAQEKSILMELSHPFIVNMMCSFQD 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29897506   81 DGIYYLVMEYVPGQTLKQYIIERGMLPIGEALDIMEQLTSAMAHAHHFEIVHRDIKPHNILIRADGIIKVTDFGIATATS 160
Cdd:PTZ00263  90 ENRVYFLLEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKVP 169
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29897506  161 ATTIthtnSVLGSVHYLSPE--QARGgiANKQSDIYSLGIVMFELLTGRQPFSGESAVAIALKHLQSEIPSPkRWNE 235
Cdd:PTZ00263 170 DRTF----TLCGTPEYLAPEviQSKG--HGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFP-NWFD 239
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
17-210 3.53e-23

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 100.28  E-value: 3.53e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29897506   17 IGGGGMANVYLAHDDILGRDVAVKILrldYSNNEEFIKR-FHREAQSVTTLSHPNIVNMYDVGEEDGIYYLVMEYVPGQT 95
Cdd:PLN00034  82 IGSGAGGTVYKVIHRPTGRLYALKVI---YGNHEDTVRRqICREIEILRDVNHPNVVKCHDMFDHNGEIQVLLEFMDGGS 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29897506   96 LK-QYIIERGMLPigealDIMEQLTSAMAHAHHFEIVHRDIKPHNILIRADGIIKVTDFGiATATSATTITHTNSVLGSV 174
Cdd:PLN00034 159 LEgTHIADEQFLA-----DVARQILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFG-VSRILAQTMDPCNSSVGTI 232
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 29897506  175 HYLSPEQA-----RGGIANKQSDIYSLGIVMFELLTGRQPF 210
Cdd:PLN00034 233 AYMSPERIntdlnHGAYDGYAGDIWSLGVSILEFYLGRFPF 273
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
68-236 4.07e-14

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 71.81  E-value: 4.07e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29897506   68 HPNIVNMYDVGEEDGIYYLVMEYVPGQTLKQYIIERGMLPIGEALDIMEQLTSAMA--HAHHfeIVHRDIKPHNILI-RA 144
Cdd:PHA03390  68 NPNFIKLYYSVTTLKGHVLIMDYIKDGDLFDLLKKEGKLSEAEVKKIIRQLVEALNdlHKHN--IIHNDIKLENVLYdRA 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29897506  145 DGIIKVTDFGIATATSATtithtnSVL-GSVHYLSPEQARGGIANKQSDIYSLGIVMFELLTGRQPFSGESA----VAIA 219
Cdd:PHA03390 146 KDRIYLCDYGLCKIIGTP------SCYdGTLDYFSPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPFKEDEDeeldLESL 219
                        170
                 ....*....|....*..
gi 29897506  220 LKHLQSEIPSPKRWNEN 236
Cdd:PHA03390 220 LKRQQKKLPFIKNVSKN 236
spoVD_pbp TIGR02214
stage V sporulation protein D; This model describes the spoVD subfamily of homologs of the ...
367-429 1.55e-04

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: 43.26  E-value: 1.55e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29897506   367 KDVKVPDVAGMKYTTAVNTLVEKGFEV-TEPNIVYtddvevgdVIKTDPVAGRVVKENAKITIY 429
Cdd:TIGR02214 578 EAVAVPNLRGMKVDDAEKTLLHLGLDVaTEGFGTR--------VVNQTPIPGEKVKEGTKVVLY 633
 
Name Accession Description Interval E-value
PKc cd00180
Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze ...
17-203 1.09e-51

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: 178.58  E-value: 1.09e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29897506  17 IGGGGMANVYLAHDDILGRDVAVKILRLDysNNEEFIKRFHREAQSVTTLSHPNIVNMYDVGEEDGIYYLVMEYVPGQTL 96
Cdd:cd00180   1 LGEGGFGTVYLARDKKTGKKVAIKIIKKE--DSSSLLEELLREIEILKKLNHPNIVKLYGVFEDENHLYLVMEYCEGGSL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29897506  97 KQYIIER-GMLPIGEALDIMEQLTSAMAHAHHFEIVHRDIKPHNILI-RADGIIKVTDFGiATATSATTITHTNSVLGSV 174
Cdd:cd00180  79 KDLLKENeGKLSEDEILRILLQILEGLEYLHSNGIIHRDLKPENILLdSDNGKVKLADFG-LSKLLTSDKSLLKTIVGTP 157
                       170       180       190
                ....*....|....*....|....*....|
gi 29897506 175 HYLSPEQARG-GIANKQSDIYSLGIVMFEL 203
Cdd:cd00180 158 AYMAPEVLLGkGYYSEKSDIWSLGVILYEL 187
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
370-431 2.75e-15

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: 71.41  E-value: 2.75e-15
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29897506 370 KVPDVAGMKYTTAVNTLVEKGFEVTEPNIVYTDDVEVGDVIKTDPVAGRVVKENAKITIYQS 431
Cdd:cd06577   1 TVPDVVGMTLDEAKAALEAAGLKVGVVTEEYSDDVPKGTVISQSPAAGTKVKKGSTVTLTVS 62
PASTA_pknB cd06577
PASTA domain of bacterial serine/threonine kinase pknB-like proteins. PknB is a member of a ...
508-565 8.92e-12

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: 61.39  E-value: 8.92e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 29897506 508 DFSGWTENSVTGYLNERKLT-SDIKREYSDTVEKGLVISQFPKPGTPLKEGDKVTIIIS 565
Cdd:cd06577   4 DVVGMTLDEAKAALEAAGLKvGVVTEEYSDDVPKGTVISQSPAAGTKVKKGSTVTLTVS 62
STKc_MAPKKK cd06606
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein Kinase ...
10-253 5.61e-50

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: 175.44  E-value: 5.61e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29897506  10 RYKLLKMIGGGGMANVYLAHDDILGRDVAVKILRLDySNNEEFIKRFHREAQSVTTLSHPNIVNMY--DVGEEDGIYYLV 87
Cdd:cd06606   1 EWTRGELLGRGSFGSVYLALDKDTGELMAVKSVELS-GDSEEELEALEREIRILSSLQHPNIVRYYgsERDEEKNTLNIF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29897506  88 MEYVPGQTLKQYIIERGMLPIGEALDIMEQLTSAMAHAHHFEIVHRDIKPHNILIRADGIIKVTDFGI-ATATSATTITH 166
Cdd:cd06606  80 LEYVSGGSLSSLLKKFGKLPEPVIRKYTRQILEGLAYLHSNGIVHRDIKGANILVDSDGVVKLADFGCaKRLGDIETGEG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29897506 167 TNSVLGSVHYLSPEQARGGIANKQSDIYSLGIVMFELLTGRQPFSGESAVAIALKHLQS-----EIPspkrwnENIPQSV 241
Cdd:cd06606 160 TGSVRGTPYWMAPEVIRGEEYGRAADIWSLGCTVIEMATGKPPWSELGNPMAALYKIGSsgeppEIP------EHLSEEA 233
                       250
                ....*....|..
gi 29897506 242 ENIILKATAKDP 253
Cdd:cd06606 234 KDFLRKCLRRDP 245
STKc_Nek cd08215
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
10-256 2.85e-46

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: 164.59  E-value: 2.85e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29897506  10 RYKLLKMIGGGGMANVYLAHDDILGRDVAVKILRLDYSNNEEfIKRFHREAQSVTTLSHPNIVNMYDVGEEDGIYYLVME 89
Cdd:cd08215   1 KYEIIKQIGKGSFGKVYLVRRKSDGKLYVLKEIDLSNMSEKE-REDALNEVKILKKLNHPNIIKYYESFEEKGKLCIVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29897506  90 YVPGQTLKQYIIERGM----LPIGEALDIMEQLTSAMAHAHHFEIVHRDIKPHNILIRADGIIKVTDFGiATATSATTIT 165
Cdd:cd08215  80 YADGGDLSQKIKKQKKegkpFPEEQILDWFVQLCLALKYLHSRKILHRDIKPQNIFLTSNGLVKLGDFG-ISKVLSSTVD 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29897506 166 HTNSVLGSVHYLSPEQARGGIANKQSDIYSLGIVMFELLTGRQPFSGESAVAIALKHLQSEI-PSPKRWneniPQSVENI 244
Cdd:cd08215 159 LAKTVVGTPYYLSPELCQNKPYNYKSDIWSLGCVLYELCTLKHPFEGENLLELALKILKGQYpPIPSQY----SSELRNL 234
                       250
                ....*....|..
gi 29897506 245 ILKATAKDPFHR 256
Cdd:cd08215 235 VSSLLQKDPEER 246
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; Protein Kinases (PKs), STE family, catalytic ...
11-256 2.28e-40

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: 147.74  E-value: 2.28e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29897506  11 YKLLKMIGGGGMANVYLAHDDILGRDVAVKILRLDYSNNEEFIkrfHREAQSVTTLSHPNIVNMYDVGEEDGIYYLVMEY 90
Cdd:cd05122   2 FEILEKIGKGGFGEVYKARHKRTGKEVAIKVIKLESKEKKEKI---INEIQILKKCKHPNIVKYYGSYLKKDELWIVMEF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29897506  91 VPGQTLKQyIIERGMLPIGEAL--DIMEQLTSAMAHAHHFEIVHRDIKPHNILIRADGIIKVTDFGiaTATSATTITHTN 168
Cdd:cd05122  79 CSGGSLKD-LLKSTNQTLTESQiaYVCKELLKGLEYLHSNGIIHRDIKAANILLTSDGEVKLIDFG--LSAQLSDTKARN 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29897506 169 SVLGSVHYLSPEQARGGIANKQSDIYSLGIVMFELLTGRQPFSGESAVAiALKHLQSEIPSPKRWNENIPQSVENIILKA 248
Cdd:cd05122 156 TMVGTPYWMAPEVINGKPYDYKADIWSLGITAIELAEGKPPYSELPPMK-ALFKIATNGPPGLRNPEKWSDEFKDFLKKC 234

                ....*...
gi 29897506 249 TAKDPFHR 256
Cdd:cd05122 235 LQKNPEKR 242
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family, catalytic ...
15-256 1.86e-39

Catalytic domain of Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family, catalytic domain. This PTKc family is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. They can be classified into receptor and non-receptor tyr kinases. PTKs play important roles in many cellular processes including, lymphocyte activation, epithelium growth and maintenance, metabolism control, organogenesis regulation, survival, proliferation, differentiation, migration, adhesion, motility, and morphogenesis. Receptor tyr kinases (RTKs) are integral membrane proteins which contain an extracellular ligand-binding region, a transmembrane segment, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain, leading to intracellular signaling. Some RTKs are orphan receptors with no known ligands. Non-receptor (or cytoplasmic) tyr kinases are distributed in different intracellular compartments and are usually multi-domain proteins containing a catalytic tyr kinase domain as well as various regulatory domains such as SH3 and SH2. PTKs are usually autoinhibited and require a mechanism for activation. In many PTKs, the phosphorylation of tyr residues in the activation loop is essential for optimal activity. Aberrant expression of PTKs is associated with many development abnormalities and cancers.


Pssm-ID: 173624  Cd Length: 262  Bit Score: 145.76  E-value: 1.86e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29897506  15 KMIGGGGMANVYLAH-DDILG--RDVAVKILRLDYSNNEefIKRFHREAQSVTTLSHPNIVNMYDVGEEDGIYYLVMEYV 91
Cdd:cd00192   1 KKLGEGAFGEVYKGKlKGKDGktTEVAVKTLKEDASEEE--RKDFLKEARVMKKLGHPNVVRLLGVCTEEEPLYLVLEYM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29897506  92 PGQTLKQYIIER---------GMLPIGEALDIMEQLTSAMAHAHHFEIVHRDIKPHNILIRADGIIKVTDFG--IATATS 160
Cdd:cd00192  79 EGGDLLDYLRKSrpvfpspekSTLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGlsRDVYDD 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29897506 161 ATTITHTNSVLgSVHYLSPEQARGGIANKQSDIYSLGIVMFELLT-GRQPFSGESAVAIaLKHLQS----EIPspkrwnE 235
Cdd:cd00192 159 DYYRKKTGGKL-PIRWMAPESLKDGIFTSKSDVWSFGVLLWEIFTlGATPYPGLSNEEV-LEYLRKgyrlPKP------E 230
                       250       260
                ....*....|....*....|.
gi 29897506 236 NIPQSVENIILKATAKDPFHR 256
Cdd:cd00192 231 YCPDELYELMLSCWQLDPEDR 251
STKc_AGC cd05123
Catalytic domain of AGC family Protein Serine/Threonine Kinases; Serine/Threonine Kinases ...
17-262 2.0