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Conserved domains on  [gi|169245740|gb|ACA50916|]
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ThrB, partial [Agrobacterium fabrum str. C58]

Protein Classification

protein kinase family protein( domain architecture ID 229378)

protein kinase family protein may catalyze the transfer of the gamma-phosphoryl group from ATP to substrates such as serine/threonine and/or tyrosine residues on proteins, or may be a pseudokinase

CATH:  1.10.510.10
PubMed:  16244704
SCOP:  4003661

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
 1-165 7.51e-92

Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the catalytic domains of serine/threonine-specific and tyrosine-specific protein kinases. It also includes RIO kinases, which are atypical serine protein kinases, aminoglycoside phosphotransferases, and choline kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to hydroxyl groups in specific substrates such as serine, threonine, or tyrosine residues of proteins.


The actual alignment was detected with superfamily member PRK05231:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 319  Bit Score: 269.74  E-value: 7.51e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169245740   1 FFLGLMQHLAAKGLSCPLPLPRKDGELLGELSGRPAALISFLEGMWLRKPEAKHCREVGKALAAMHLAGDGFEIKRPNAL 80
Cdd:PRK05231  63 FFLGLMQHLAARGVPVPAPVARRDGAALGELAGKPAAIVTFLEGKWPRAPTAAHCAEVGEMLARMHLAGRDFPLERPNLR 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169245740  81 SVDGWKVLWYKSE-DRADEVEKGLKQEIRPEIDYLA-AHWPKdLPAGVIHADLFQDNVFFLGDELSGLIDFYFACNDLLA 158
Cdd:PRK05231 143 GLAWWRELAPRLLpFLADEQAALLEAELAAQLAFLAsAAWPA-LPRGVIHADLFRDNVLFEGDRLSGFIDFYFACNDKLL 221


                 ....*..
gi 169245740 159 YDVSICL 165
Cdd:PRK05231 222 YDVAITL 228
 
Name Accession Description Interval E-value
PRK05231 PRK05231
homoserine kinase; Provisional
 1-165 7.51e-92

homoserine kinase; Provisional


Pssm-ID: 235369 [Multi-domain]  Cd Length: 319  Bit Score: 269.74  E-value: 7.51e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169245740   1 FFLGLMQHLAAKGLSCPLPLPRKDGELLGELSGRPAALISFLEGMWLRKPEAKHCREVGKALAAMHLAGDGFEIKRPNAL 80
Cdd:PRK05231  63 FFLGLMQHLAARGVPVPAPVARRDGAALGELAGKPAAIVTFLEGKWPRAPTAAHCAEVGEMLARMHLAGRDFPLERPNLR 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169245740  81 SVDGWKVLWYKSE-DRADEVEKGLKQEIRPEIDYLA-AHWPKdLPAGVIHADLFQDNVFFLGDELSGLIDFYFACNDLLA 158
Cdd:PRK05231 143 GLAWWRELAPRLLpFLADEQAALLEAELAAQLAFLAsAAWPA-LPRGVIHADLFRDNVLFEGDRLSGFIDFYFACNDKLL 221


                 ....*..
gi 169245740 159 YDVSICL 165
Cdd:PRK05231 222 YDVAITL 228
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
 1-165 1.93e-72

Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a subset of bacteria, which have a Protein Kinase fold. These proteins do not bear any similarity to the GHMP family homoserine kinases present in most bacteria and eukaryotes. Homoserine kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to L-homoserine producing L-homoserine phosphate, an intermediate in the production of the amino acids threonine, methionine, and isoleucine. The Type II homoserine kinase subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270702 [Multi-domain]  Cd Length: 300  Bit Score: 219.82  E-value: 1.93e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169245740   1 FFLGLMQHLAAKGLSCPLPLPRKDGELLGELSGRPAALISFLEGMWLRKPEAKHCREVGKALAAMHLAGDGFEIKRPNAL 80
Cdd:cd05153   56 FELELLDHLAQAGLPVPRPLADKDGELLGELNGKPAALFPFLPGESLTTPTPEQCRAIGAALARLHLALAGFPPPRPNPR 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169245740  81 SVDGWKVLWYKSEDRADEVEKGLKQEIRPEIDYLAAHWPKDLPAGVIHADLFQDNVFFLGDELSGLIDFYFACNDLLAYD 160
Cdd:cd05153  136 GLAWWKPLAERLKARLDLLAADDRALLEDELARLQALAPSDLPRGVIHADLFRDNVLFDGDRLSGIIDFYDACYDPLLYD 215


                 ....*
gi 169245740 161 VSICL 165
Cdd:cd05153  216 LAIAL 220
thrB_alt TIGR00938
homoserine kinase, Neisseria type; Homoserine kinase is required in the biosynthesis of ...
 1-165 2.30e-63

homoserine kinase, Neisseria type; Homoserine kinase is required in the biosynthesis of threonine from aspartate.The member of this family from Pseudomonas aeruginosa was shown by direct assay and complementation to act specifically as a homoserine kinase. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 273351 [Multi-domain]  Cd Length: 307  Bit Score: 196.95  E-value: 2.30e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169245740    1 FFLGLMQHLAAKGLSCPLPLPRKDGELLGELSGRPAALISFLEGMWLRKPEAKHCREVGKALAAMHLAGDGFEIKRPNAL 80
Cdd:TIGR00938  64 FFLALTTHLAARGLPVPKPVKSRDGRQLSTLAGKPACLVEFLQGLSVGRPTAMHCRPVGEVLAWMHLAGAHFPENRKNSL 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169245740   81 SVDGWKVLWYKSEDRADEVEKGLKQEIRPEIDYLAAHWPKDLPAGVIHADLFQDNVFFLGDELSGLIDFYFACNDLLAYD 160
Cdd:TIGR00938 144 RLEAWHILAEKCFEAAPQLEAHMGAELDKELDYLDKFWPRDLPRGVIHADLFPDNVLFDGDSVKGVIDFYFACTDARAYD 223


                  ....*
gi 169245740  161 VSICL 165
Cdd:TIGR00938 224 LAITV 228
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
 1-165 3.10e-57

Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal transduction mechanisms]; Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist is part of the Pathway/BioSystem: Threonine biosynthesis


Pssm-ID: 441905 [Multi-domain]  Cd Length: 297  Bit Score: 180.89  E-value: 3.10e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169245740   1 FFLGLMQHLAAKGLSCPLPLPRKDGELLGELSGRPAALISFLEGMWLRKPEAKHCREVGKALAAMHLAGDGFEikRPNAL 80
Cdd:COG2334   56 FELALLAHLAAAGLPVPAPVPTRDGETLLELEGRPAALFPFLPGRSPEEPSPEQLEELGRLLARLHRALADFP--RPNAR 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169245740  81 SVDGWKVLWYKSEDrADEVEKGLKQEIRPEIDYLAAHW---PKDLPAGVIHADLFQDNVFFLGDELSGLIDFYFACNDLL 157
Cdd:COG2334  134 DLAWWDELLERLLG-PLLPDPEDRALLEELLDRLEARLaplLGALPRGVIHGDLHPDNVLFDGDGVSGLIDFDDAGYGPR 212


                 ....*...
gi 169245740 158 AYDVSICL 165
Cdd:COG2334  213 LYDLAIAL 220
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
 1-165 5.10e-27

Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance proteins, which confer resistance to various aminoglycosides they include: aminoglycoside 3'-phosphotransferase or kanamycin kinase / neomycin-kanamycin phosphotransferase and streptomycin 3''-kinase or streptomycin 3''-phosphotransferase. The aminoglycoside phosphotransferases inactivate aminoglycoside antibiotics via phosphorylation. This family also includes homoserine kinase. This family is related to fructosamine kinase pfam03881.


Pssm-ID: 426359 [Multi-domain]  Cd Length: 239  Bit Score: 101.42  E-value: 5.10e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169245740    1 FFLGLMQHLAAKGLS-CPLPLprkDGELLGELSGRPAALISFLEGMWLRKPEAKHC-----REVGKALAAMH---LAGDG 71
Cdd:pfam01636  39 RELALLRHLAAAGVPpVPRVL---AGCTDAELLGLPFLLMEYLPGEVLARPLLPEErgallEALGRALARLHavdPAALP 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169245740   72 FEIKRPNALSVDGWKVLWYKsEDRADEVEKGLKQEIRPEIDYLAAHWPKDLPAGVIHADLFQDNVFFL-GDELSGLIDFY 150
Cdd:pfam01636 116 LAGRLARLLELLRQLEAALA-RLLAAELLDRLEELEERLLAALLALLPAELPPVLVHGDLHPGNLLVDpGGRVSGVIDFE 194

                         170
                  ....*....|....*
gi 169245740  151 FACNDLLAYDVSICL 165
Cdd:pfam01636 195 DAGLGDPAYDLAILL 209
 
Name Accession Description Interval E-value
PRK05231 PRK05231
homoserine kinase; Provisional
 1-165 7.51e-92

homoserine kinase; Provisional


Pssm-ID: 235369 [Multi-domain]  Cd Length: 319  Bit Score: 269.74  E-value: 7.51e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169245740   1 FFLGLMQHLAAKGLSCPLPLPRKDGELLGELSGRPAALISFLEGMWLRKPEAKHCREVGKALAAMHLAGDGFEIKRPNAL 80
Cdd:PRK05231  63 FFLGLMQHLAARGVPVPAPVARRDGAALGELAGKPAAIVTFLEGKWPRAPTAAHCAEVGEMLARMHLAGRDFPLERPNLR 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169245740  81 SVDGWKVLWYKSE-DRADEVEKGLKQEIRPEIDYLA-AHWPKdLPAGVIHADLFQDNVFFLGDELSGLIDFYFACNDLLA 158
Cdd:PRK05231 143 GLAWWRELAPRLLpFLADEQAALLEAELAAQLAFLAsAAWPA-LPRGVIHADLFRDNVLFEGDRLSGFIDFYFACNDKLL 221


                 ....*..
gi 169245740 159 YDVSICL 165
Cdd:PRK05231 222 YDVAITL 228
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
 1-165 1.93e-72

Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a subset of bacteria, which have a Protein Kinase fold. These proteins do not bear any similarity to the GHMP family homoserine kinases present in most bacteria and eukaryotes. Homoserine kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to L-homoserine producing L-homoserine phosphate, an intermediate in the production of the amino acids threonine, methionine, and isoleucine. The Type II homoserine kinase subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270702 [Multi-domain]  Cd Length: 300  Bit Score: 219.82  E-value: 1.93e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169245740   1 FFLGLMQHLAAKGLSCPLPLPRKDGELLGELSGRPAALISFLEGMWLRKPEAKHCREVGKALAAMHLAGDGFEIKRPNAL 80
Cdd:cd05153   56 FELELLDHLAQAGLPVPRPLADKDGELLGELNGKPAALFPFLPGESLTTPTPEQCRAIGAALARLHLALAGFPPPRPNPR 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169245740  81 SVDGWKVLWYKSEDRADEVEKGLKQEIRPEIDYLAAHWPKDLPAGVIHADLFQDNVFFLGDELSGLIDFYFACNDLLAYD 160
Cdd:cd05153  136 GLAWWKPLAERLKARLDLLAADDRALLEDELARLQALAPSDLPRGVIHADLFRDNVLFDGDRLSGIIDFYDACYDPLLYD 215


                 ....*
gi 169245740 161 VSICL 165
Cdd:cd05153  216 LAIAL 220
thrB_alt TIGR00938
homoserine kinase, Neisseria type; Homoserine kinase is required in the biosynthesis of ...
 1-165 2.30e-63

homoserine kinase, Neisseria type; Homoserine kinase is required in the biosynthesis of threonine from aspartate.The member of this family from Pseudomonas aeruginosa was shown by direct assay and complementation to act specifically as a homoserine kinase. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 273351 [Multi-domain]  Cd Length: 307  Bit Score: 196.95  E-value: 2.30e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169245740    1 FFLGLMQHLAAKGLSCPLPLPRKDGELLGELSGRPAALISFLEGMWLRKPEAKHCREVGKALAAMHLAGDGFEIKRPNAL 80
Cdd:TIGR00938  64 FFLALTTHLAARGLPVPKPVKSRDGRQLSTLAGKPACLVEFLQGLSVGRPTAMHCRPVGEVLAWMHLAGAHFPENRKNSL 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169245740   81 SVDGWKVLWYKSEDRADEVEKGLKQEIRPEIDYLAAHWPKDLPAGVIHADLFQDNVFFLGDELSGLIDFYFACNDLLAYD 160
Cdd:TIGR00938 144 RLEAWHILAEKCFEAAPQLEAHMGAELDKELDYLDKFWPRDLPRGVIHADLFPDNVLFDGDSVKGVIDFYFACTDARAYD 223


                  ....*
gi 169245740  161 VSICL 165
Cdd:TIGR00938 224 LAITV 228
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
 1-165 3.10e-57

Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal transduction mechanisms]; Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist is part of the Pathway/BioSystem: Threonine biosynthesis


Pssm-ID: 441905 [Multi-domain]  Cd Length: 297  Bit Score: 180.89  E-value: 3.10e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169245740   1 FFLGLMQHLAAKGLSCPLPLPRKDGELLGELSGRPAALISFLEGMWLRKPEAKHCREVGKALAAMHLAGDGFEikRPNAL 80
Cdd:COG2334   56 FELALLAHLAAAGLPVPAPVPTRDGETLLELEGRPAALFPFLPGRSPEEPSPEQLEELGRLLARLHRALADFP--RPNAR 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169245740  81 SVDGWKVLWYKSEDrADEVEKGLKQEIRPEIDYLAAHW---PKDLPAGVIHADLFQDNVFFLGDELSGLIDFYFACNDLL 157
Cdd:COG2334  134 DLAWWDELLERLLG-PLLPDPEDRALLEELLDRLEARLaplLGALPRGVIHGDLHPDNVLFDGDGVSGLIDFDDAGYGPR 212


                 ....*...
gi 169245740 158 AYDVSICL 165
Cdd:COG2334  213 LYDLAIAL 220
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
 1-165 5.10e-27

Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance proteins, which confer resistance to various aminoglycosides they include: aminoglycoside 3'-phosphotransferase or kanamycin kinase / neomycin-kanamycin phosphotransferase and streptomycin 3''-kinase or streptomycin 3''-phosphotransferase. The aminoglycoside phosphotransferases inactivate aminoglycoside antibiotics via phosphorylation. This family also includes homoserine kinase. This family is related to fructosamine kinase pfam03881.


Pssm-ID: 426359 [Multi-domain]  Cd Length: 239  Bit Score: 101.42  E-value: 5.10e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169245740    1 FFLGLMQHLAAKGLS-CPLPLprkDGELLGELSGRPAALISFLEGMWLRKPEAKHC-----REVGKALAAMH---LAGDG 71
Cdd:pfam01636  39 RELALLRHLAAAGVPpVPRVL---AGCTDAELLGLPFLLMEYLPGEVLARPLLPEErgallEALGRALARLHavdPAALP 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169245740   72 FEIKRPNALSVDGWKVLWYKsEDRADEVEKGLKQEIRPEIDYLAAHWPKDLPAGVIHADLFQDNVFFL-GDELSGLIDFY 150
Cdd:pfam01636 116 LAGRLARLLELLRQLEAALA-RLLAAELLDRLEELEERLLAALLALLPAELPPVLVHGDLHPGNLLVDpGGRVSGVIDFE 194

                         170
                  ....*....|....*
gi 169245740  151 FACNDLLAYDVSICL 165
Cdd:pfam01636 195 DAGLGDPAYDLAILL 209
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
 3-165 1.60e-10

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


Pssm-ID: 270690 [Multi-domain]  Cd Length: 158  Bit Score: 56.16  E-value: 1.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169245740   3 LGLMQHLAAK-GLSCPLPLPrkdgelLGELSGRPAALISFLEGMWLRK--------PEAKHCREVGKALAAMHlagdgfe 73
Cdd:cd05120   40 AAMLQLLAGKlSLPVPKVYG------FGESDGWEYLLMERIEGETLSEvwprlseeEKEKIADQLAEILAALH------- 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169245740  74 ikrpnalsvdgwkvlwyksedradevekglkqeirpEIDYLAahwpkdlpagVIHADLFQDNVFFLG-DELSGLIDFYFA 152
Cdd:cd05120  107 ------------------------------------RIDSSV----------LTHGDLHPGNILVKPdGKLSGIIDWEFA 140

                        170
                 ....*....|...
gi 169245740 153 CNDLLAYDVSICL 165
Cdd:cd05120  141 GYGPPAFDYAAAL 153
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
 5-149 6.43e-09

Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction only];


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 53.20  E-value: 6.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169245740   5 LMQHLAAKglsCPLPLPR-----KDGELLGelsgRPAALISFLEG------MWLRKPEAKH--CREVGKALAAMH---LA 68
Cdd:COG3173   66 VLRALAPR---LGVPVPRplalgEDGEVIG----APFYVMEWVEGetledaLPDLSPAERRalARALGEFLAALHavdPA 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169245740  69 GDGFEIKRPNALS--VDGWKVLWYKSEDRADEVEkGLKQEIrpeIDYLAAHWPKDLPAGVIHADLFQDNVFFLGD--ELS 144
Cdd:COG3173  139 AAGLADGRPEGLErqLARWRAQLRRALARTDDLP-ALRERL---AAWLAANLPEWGPPVLVHGDLRPGNLLVDPDdgRLT 214


                 ....*
gi 169245740 145 GLIDF 149
Cdd:COG3173  215 AVIDW 219
ACAD10_11_N-like cd05154
N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This ...
 5-148 9.14e-06

N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This subfamily is composed of the N-terminal domains of vertebrate ACAD10 and ACAD11, and similar uncharacterized bacterial and eukaryotic proteins. ACADs are a family of flavoproteins that are involved in the beta-oxidation of fatty acyl-CoA derivatives. ACAD deficiency can cause metabolic disorders including muscle fatigue, hypoglycemia, and hepatic lipidosis. There are at least 11 distinct ACADs, some of which show distinct substrate specificities to either straight-chain or branched-chain fatty acids. ACAD10 is widely expressed in human tissues and highly expressed in liver, kidney, pancreas, and spleen. ACAD10 and ACAD11 are both significantly expressed in human brain tissues. They contain a long N-terminal domain with similarity to phosphotransferases with a Protein Kinase fold, which is absent in other ACADs. They may exhibit multiple functions in acyl-CoA oxidation pathways. ACAD11 utilizes substrates with carbon chain lengths of 20 to 26, with optimal activity towards C22CoA. ACAD10 may be associated with an increased risk in type II diabetes. The ACAD10/11-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270703 [Multi-domain]  Cd Length: 254  Bit Score: 44.14  E-value: 9.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169245740   5 LMQHLAAKGLscplPLPR-----KDGELLGelsgRPAALISFLEGMWLRKPE----------AKHCREVGKALAAMHL-- 67
Cdd:cd05154   51 VLRALAGTGV----PVPRvlalcEDPSVLG----APFYVMERVDGRVLPDPLprpdlspeerRALARSLVDALAALHSvd 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169245740  68 ---AGDGFEIKRPNALS--VDGWkvlwyksEDRADEVEKGLKQEIRPEIDYLAAHWPKDLPAGVIHADLFQDNVFF-LGD 141
Cdd:cd05154  123 paaLGLADLGRPEGYLErqVDRW-------RRQLEAAATDPPPALEEALRWLRANLPADGRPVLVHGDFRLGNLLFdPDG 195


                 ....*..
gi 169245740 142 ELSGLID 148
Cdd:cd05154  196 RVTAVLD 202
PRK06148 PRK06148
hypothetical protein; Provisional
 5-163 2.15e-04

hypothetical protein; Provisional


Pssm-ID: 180426 [Multi-domain]  Cd Length: 1013  Bit Score: 40.78  E-value: 2.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169245740    5 LMQHLAAKG--LSCPLPLPRKDGELLGELSG-----RPAALISFLEGMWL----RKPEAKHcREVGKALAAMHLAGDGFe 73
Cdd:PRK06148   71 ALDHLAAVApdLPVPRLIPSLSGASLASAQDpdgepRLLRLLSWLPGTPLaeaaPRTEALL-DNLGRALGRLDRALQGF- 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169245740   74 iKRPNALSVDGWKVL---WykSEDRADEVEKGLKQEIRPEI-----DYLAAHWPKdLPAGVIHADLFQDNVFF---LGDE 142
Cdd:PRK06148  149 -MHPGALRDLDWDLRhagR--ARDRLHFIDDPEDRALVERFlarfeRNVAPRLAA-LPAQVIHNDANDYNILVdadDGER 224

                         170       180
                  ....*....|....*....|.
gi 169245740  143 LSGLIDFYFACNDLLAYDVSI 163
Cdd:PRK06148  225 ISGLIDFGDAVHAPRICEVAI 245
CotI COG5881
Spore coat protein CotI/CotS, protein kinase superfamily [Cell cycle control, cell division, ...
 1-108 1.42e-03

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


Pssm-ID: 444583 [Multi-domain]  Cd Length: 331  Bit Score: 37.95  E-value: 1.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169245740   1 FFLGLMQHLAAKGLS-CPLPLPRKDGELLGELSGRPAALISFLEGmwlRKPEAKHCREVGKA---LAAMHLAGDGFEIKR 76
Cdd:COG5881   49 FIYEAQEHLKKNGFNnIPRIVPTKDGKPYVKYGGKLYYLTEWIEG---RECDYKNPEDLKKAaetLAEFHKASKGFEPPP 125

                         90       100       110
                 ....*....|....*....|....*....|...
gi 169245740  77 PNALSVDGWKvlWYKS-EDRADEVEKgLKQEIR 108
Cdd:COG5881  126 GSKGRSHLGK--WPERfEKRLEELEK-FKKIAE 155
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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