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Conserved domains on  [gi|21361699|ref|NP_064511|]
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sphingosine kinase 2 isoform a [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02958 super family cl29912
diacylglycerol kinase/D-erythro-sphingosine kinase
 187-381 1.64e-40

diacylglycerol kinase/D-erythro-sphingosine kinase


The actual alignment was detected with superfamily member PLN02958:

Pssm-ID: 215517 [Multi-domain]  Cd Length: 481  Bit Score: 154.63  E-value: 1.64e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361699  187 VNPFGGRGLAWQWCKNHVLPMISEAGLSFNLIQTERQNHARELVQGLSLSEWDGIVTVSGDGLLHEVLNGLLDRPDWEEA 266
Cdd:PLN02958 118 VNPFGGKKSASKIFFDVVKPLLEDADIQLTIQETKYQLHAKEVVRTMDLSKYDGIVCVSGDGILVEVVNGLLEREDWKTA 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361699  267 VKMPVGILPCGSGNALAGAVnqhggFEPALGLDLLLNCSLLLCRGGGHPLDLLSVtLASGSRCFSFLSVAWGFVSDVDIQ 346
Cdd:PLN02958 198 IKLPIGMVPAGTGNGMAKSL-----LDSVGEPCSATNAVLAIIRGHKCSLDVATI-LQGETKFFSVLMLAWGLVADIDIE 271

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 21361699  347 SERFRALGSARFTLGTVLGLATLHTYRGRLSYLPA 381
Cdd:PLN02958 272 SEKYRWMGSARLDFYGLQRILCLRQYNGRISFVPA 306
YegS_C super family cl29908
YegS C-terminal NAD kinase beta sandwich-like domain; This entry represents the C-terminal ...
 556-644 5.90e-04

YegS C-terminal NAD kinase beta sandwich-like domain; This entry represents the C-terminal domain found in the YegS protein. It is related to the beta sandwich domain of NAD kinases. The structure of YegS reveals a two-domain protein with the active site crevice found between the two domains. The C-terminal domain contains 13 beta-strands and two alpha-helices. The likely substrate for YegS is phosphatidylglycerol.


The actual alignment was detected with superfamily member pfam19279:

Pssm-ID: 453080  Cd Length: 158  Bit Score: 41.03  E-value: 5.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361699   556 APHARFDDGLVHLCWVRsGISRAALLRLFLAMERGSHFSLgcPQLGYAAARAFRLEplTPRGV-LTVDGEQVEYGPLQAQ 634
Cdd:pfam19279  74 APDARVDDGLLDVVVIE-AASRRTLLRLLPKVYDGRHVRL--PQVEVLRGREVRIE--ADRPLpAGADGEVLGPLPVRVE 148

                          90
                  ....*....|
gi 21361699   635 MHPGIGTLLT 644
Cdd:pfam19279 149 VLPGALRVLA 158
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 355-516 2.04e-03

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 2.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361699   355 SARFTLGTVLGLATLHTYRGRLSYLPATVEPASPTPAHSLPRAKSELTLTPDPAPPmahSPLHRSVSDLPLPLPQPALAS 434
Cdd:PHA03247 2687 AARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPP---AVPAGPATPGGPARPARPPTT 2763

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361699   435 PGSPEPLPILSLNGGGPELAGDWGGAGDAPLSPDPLLSSPPGSPKAALHSPVSEGAPVIPPSSGLPLPTPDARVGASTCG 514
Cdd:PHA03247 2764 AGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPP 2843


                  ..
gi 21361699   515 PP 516
Cdd:PHA03247 2844 GP 2845
 
Name Accession Description Interval E-value
PLN02958 PLN02958
diacylglycerol kinase/D-erythro-sphingosine kinase
 187-381 1.64e-40

diacylglycerol kinase/D-erythro-sphingosine kinase


Pssm-ID: 215517 [Multi-domain]  Cd Length: 481  Bit Score: 154.63  E-value: 1.64e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361699  187 VNPFGGRGLAWQWCKNHVLPMISEAGLSFNLIQTERQNHARELVQGLSLSEWDGIVTVSGDGLLHEVLNGLLDRPDWEEA 266
Cdd:PLN02958 118 VNPFGGKKSASKIFFDVVKPLLEDADIQLTIQETKYQLHAKEVVRTMDLSKYDGIVCVSGDGILVEVVNGLLEREDWKTA 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361699  267 VKMPVGILPCGSGNALAGAVnqhggFEPALGLDLLLNCSLLLCRGGGHPLDLLSVtLASGSRCFSFLSVAWGFVSDVDIQ 346
Cdd:PLN02958 198 IKLPIGMVPAGTGNGMAKSL-----LDSVGEPCSATNAVLAIIRGHKCSLDVATI-LQGETKFFSVLMLAWGLVADIDIE 271

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 21361699  347 SERFRALGSARFTLGTVLGLATLHTYRGRLSYLPA 381
Cdd:PLN02958 272 SEKYRWMGSARLDFYGLQRILCLRQYNGRISFVPA 306
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 187-321 1.04e-27

Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. The catalytic domain is assumed from the finding of bacterial homologs. YegS is the Escherichia coli protein in this family whose crystal structure reveals an active site in the inter-domain cleft formed by four conserved sequence motifs, revealing a novel metal-binding site. The residues of this site are conserved across the family.


Pssm-ID: 425868 [Multi-domain]  Cd Length: 125  Bit Score: 108.06  E-value: 1.04e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361699   187 VNPFGGRGLAWQWCKnHVLPMISEAGLSFNLIQTERQNHARELVQGLSLSEWDGIVTVSGDGLLHEVLNGLLdrpdwEEA 266
Cdd:pfam00781   6 VNPKSGGGKGKKLLR-KVRPLLNKAGVEVELVLTEGPGDALELAREAAEDGYDRIVVAGGDGTVNEVLNGLA-----GLA 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 21361699   267 VKMPVGILPCGSGNALAGAVNQHGGFEPALgldlllncsLLLCRGGGHPLDLLSV 321
Cdd:pfam00781  80 TRPPLGIIPLGTGNDFARALGIPGDPEEAL---------EAILKGQTRPVDVGKV 125
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 187-378 9.55e-15

Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, General function prediction only];


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 75.27  E-value: 9.55e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361699 187 VNPFGGRGLAWQWCKnHVLPMISEAGLSFNLIQTERQNHARELVQGLSLSEWDGIVTVSGDGLLHEVLNGLLDRpdweea 266
Cdd:COG1597   9 VNPASGRGRAARLLE-RLVAALRAAGLEVEVLETESPGDATELAREAAAEGADLVVAAGGDGTVNEVANGLAGT------ 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361699 267 vKMPVGILPCGSGNALAGAVNQHGGFEPALGldlllncslLLCRGGGHPLDLLSVtlasGSRCFsFLSVAWGFVSDV--D 344
Cdd:COG1597  82 -GPPLGILPLGTGNDFARALGIPLDPEAALE---------ALLTGRTRRIDLGRV----NGRYF-LNVAGIGFDAEVveR 146

                       170       180       190
                ....*....|....*....|....*....|....
gi 21361699 345 IQSERFRALGSARFTLGTVLGLATLHTYRGRLSY 378
Cdd:COG1597 147 ANRALKRRLGKLAYVLAALRALLRYRPFRLRIEL 180
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 239-293 7.71e-08

Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. DAG can be produced from the hydrolysis of phosphatidylinositol 4,5-bisphosphate (PIP2) by a phosphoinositide-specific phospholipase C and by the degradation of phosphatidylcholine (PC) by a phospholipase C or the concerted actions of phospholipase D and phosphatidate phosphohydrolase. This domain is presumed to be the catalytic domain. Bacterial homologues areknown.


Pssm-ID: 214487 [Multi-domain]  Cd Length: 124  Bit Score: 51.14  E-value: 7.71e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 21361699    239 DGIVTVSGDGLLHEVLNGLLDRPDweEAVKMPVGILPCGSGNALAGAVNQHGGFE 293
Cdd:smart00046  51 NRVLVCGGDGTVGWVLNALDKREL--PLPEPPVAVLPLGTGNDLARSLGWGGGYD 103
TIGR00147 TIGR00147
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ...
 204-286 5.61e-04

lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been purified and shown to have phosphatidylglycerol kinase activity. The member from M. tuberculosis, Rv2252, has diacylglycerol kinase activity. BmrU from B. subtilis is in an operon with multidrug efflux transporter Bmr, but is uncharacterized. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 161732 [Multi-domain]  Cd Length: 293  Bit Score: 42.49  E-value: 5.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361699   204 VLPMISEAGLSFNLIQTERQNHARELVQGLSLSEWDGIVTVSGDGLLHEVLNGLLDRPDweeavKMPVGILPCGSGNALA 283
Cdd:TIGR00147  24 VIMLLREEGMEIHVRVTWEKGDAARYVEEARKFGVDTVIAGGGDGTINEVVNALIQLDD-----IPALGILPLGTANDFA 98


                  ...
gi 21361699   284 GAV 286
Cdd:TIGR00147  99 RSL 101
YegS_C pfam19279
YegS C-terminal NAD kinase beta sandwich-like domain; This entry represents the C-terminal ...
 556-644 5.90e-04

YegS C-terminal NAD kinase beta sandwich-like domain; This entry represents the C-terminal domain found in the YegS protein. It is related to the beta sandwich domain of NAD kinases. The structure of YegS reveals a two-domain protein with the active site crevice found between the two domains. The C-terminal domain contains 13 beta-strands and two alpha-helices. The likely substrate for YegS is phosphatidylglycerol.


Pssm-ID: 437111  Cd Length: 158  Bit Score: 41.03  E-value: 5.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361699   556 APHARFDDGLVHLCWVRsGISRAALLRLFLAMERGSHFSLgcPQLGYAAARAFRLEplTPRGV-LTVDGEQVEYGPLQAQ 634
Cdd:pfam19279  74 APDARVDDGLLDVVVIE-AASRRTLLRLLPKVYDGRHVRL--PQVEVLRGREVRIE--ADRPLpAGADGEVLGPLPVRVE 148

                          90
                  ....*....|
gi 21361699   635 MHPGIGTLLT 644
Cdd:pfam19279 149 VLPGALRVLA 158
PHA03247 PHA03247
large tegument protein UL36; Provisional
 355-516 2.04e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 2.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361699   355 SARFTLGTVLGLATLHTYRGRLSYLPATVEPASPTPAHSLPRAKSELTLTPDPAPPmahSPLHRSVSDLPLPLPQPALAS 434
Cdd:PHA03247 2687 AARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPP---AVPAGPATPGGPARPARPPTT 2763

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361699   435 PGSPEPLPILSLNGGGPELAGDWGGAGDAPLSPDPLLSSPPGSPKAALHSPVSEGAPVIPPSSGLPLPTPDARVGASTCG 514
Cdd:PHA03247 2764 AGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPP 2843


                  ..
gi 21361699   515 PP 516
Cdd:PHA03247 2844 GP 2845
KLF9_13_N-like cd21975
Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like ...
 450-515 2.19e-03

Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like transcription factors (KLFs) belong to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved alpha-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the related N-terminal domains of KLF9, KLF13, KLF14, KLF16, and similar proteins.


Pssm-ID: 409240 [Multi-domain]  Cd Length: 163  Bit Score: 39.29  E-value: 2.19e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21361699 450 GPELAGDWGGAGDAPLSPDPLLSSPPGSpkAALHSPVSEGAPVIPPSSGLPLPTPDARVGASTCGP 515
Cdd:cd21975  81 GPSVEGSSLESGDADMGSDSDVAPASGA--AASTSPESSSDAASSPSPLSLLHPGEAGLEPERPRP 144
 
Name Accession Description Interval E-value
PLN02958 PLN02958
diacylglycerol kinase/D-erythro-sphingosine kinase
 187-381 1.64e-40

diacylglycerol kinase/D-erythro-sphingosine kinase


Pssm-ID: 215517 [Multi-domain]  Cd Length: 481  Bit Score: 154.63  E-value: 1.64e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361699  187 VNPFGGRGLAWQWCKNHVLPMISEAGLSFNLIQTERQNHARELVQGLSLSEWDGIVTVSGDGLLHEVLNGLLDRPDWEEA 266
Cdd:PLN02958 118 VNPFGGKKSASKIFFDVVKPLLEDADIQLTIQETKYQLHAKEVVRTMDLSKYDGIVCVSGDGILVEVVNGLLEREDWKTA 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361699  267 VKMPVGILPCGSGNALAGAVnqhggFEPALGLDLLLNCSLLLCRGGGHPLDLLSVtLASGSRCFSFLSVAWGFVSDVDIQ 346
Cdd:PLN02958 198 IKLPIGMVPAGTGNGMAKSL-----LDSVGEPCSATNAVLAIIRGHKCSLDVATI-LQGETKFFSVLMLAWGLVADIDIE 271

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 21361699  347 SERFRALGSARFTLGTVLGLATLHTYRGRLSYLPA 381
Cdd:PLN02958 272 SEKYRWMGSARLDFYGLQRILCLRQYNGRISFVPA 306
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 187-321 1.04e-27

Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. The catalytic domain is assumed from the finding of bacterial homologs. YegS is the Escherichia coli protein in this family whose crystal structure reveals an active site in the inter-domain cleft formed by four conserved sequence motifs, revealing a novel metal-binding site. The residues of this site are conserved across the family.


Pssm-ID: 425868 [Multi-domain]  Cd Length: 125  Bit Score: 108.06  E-value: 1.04e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361699   187 VNPFGGRGLAWQWCKnHVLPMISEAGLSFNLIQTERQNHARELVQGLSLSEWDGIVTVSGDGLLHEVLNGLLdrpdwEEA 266
Cdd:pfam00781   6 VNPKSGGGKGKKLLR-KVRPLLNKAGVEVELVLTEGPGDALELAREAAEDGYDRIVVAGGDGTVNEVLNGLA-----GLA 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 21361699   267 VKMPVGILPCGSGNALAGAVNQHGGFEPALgldlllncsLLLCRGGGHPLDLLSV 321
Cdd:pfam00781  80 TRPPLGIIPLGTGNDFARALGIPGDPEEAL---------EAILKGQTRPVDVGKV 125
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 187-378 9.55e-15

Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, General function prediction only];


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 75.27  E-value: 9.55e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361699 187 VNPFGGRGLAWQWCKnHVLPMISEAGLSFNLIQTERQNHARELVQGLSLSEWDGIVTVSGDGLLHEVLNGLLDRpdweea 266
Cdd:COG1597   9 VNPASGRGRAARLLE-RLVAALRAAGLEVEVLETESPGDATELAREAAAEGADLVVAAGGDGTVNEVANGLAGT------ 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361699 267 vKMPVGILPCGSGNALAGAVNQHGGFEPALGldlllncslLLCRGGGHPLDLLSVtlasGSRCFsFLSVAWGFVSDV--D 344
Cdd:COG1597  82 -GPPLGILPLGTGNDFARALGIPLDPEAALE---------ALLTGRTRRIDLGRV----NGRYF-LNVAGIGFDAEVveR 146

                       170       180       190
                ....*....|....*....|....*....|....
gi 21361699 345 IQSERFRALGSARFTLGTVLGLATLHTYRGRLSY 378
Cdd:COG1597 147 ANRALKRRLGKLAYVLAALRALLRYRPFRLRIEL 180
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 239-293 7.71e-08

Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. DAG can be produced from the hydrolysis of phosphatidylinositol 4,5-bisphosphate (PIP2) by a phosphoinositide-specific phospholipase C and by the degradation of phosphatidylcholine (PC) by a phospholipase C or the concerted actions of phospholipase D and phosphatidate phosphohydrolase. This domain is presumed to be the catalytic domain. Bacterial homologues areknown.


Pssm-ID: 214487 [Multi-domain]  Cd Length: 124  Bit Score: 51.14  E-value: 7.71e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 21361699    239 DGIVTVSGDGLLHEVLNGLLDRPDweEAVKMPVGILPCGSGNALAGAVNQHGGFE 293
Cdd:smart00046  51 NRVLVCGGDGTVGWVLNALDKREL--PLPEPPVAVLPLGTGNDLARSLGWGGGYD 103
PLN02204 PLN02204
diacylglycerol kinase
 187-258 8.58e-07

diacylglycerol kinase


Pssm-ID: 215126 [Multi-domain]  Cd Length: 601  Bit Score: 52.19  E-value: 8.58e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21361699  187 VNPFGGRGLA---WQwcknHVLPMISEAGLSFNLIQTERQNHARELVQGLS---LSEWDGIVTVSGDGLLHEVLNGLL 258
Cdd:PLN02204 166 VHPLSGKGSGsrtWE----TVSPIFIRAKVKTKVIVTERAGHAFDVMASISnkeLKSYDGVIAVGGDGFFNEILNGYL 239
TIGR00147 TIGR00147
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ...
 204-286 5.61e-04

lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been purified and shown to have phosphatidylglycerol kinase activity. The member from M. tuberculosis, Rv2252, has diacylglycerol kinase activity. BmrU from B. subtilis is in an operon with multidrug efflux transporter Bmr, but is uncharacterized. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 161732 [Multi-domain]  Cd Length: 293  Bit Score: 42.49  E-value: 5.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361699   204 VLPMISEAGLSFNLIQTERQNHARELVQGLSLSEWDGIVTVSGDGLLHEVLNGLLDRPDweeavKMPVGILPCGSGNALA 283
Cdd:TIGR00147  24 VIMLLREEGMEIHVRVTWEKGDAARYVEEARKFGVDTVIAGGGDGTINEVVNALIQLDD-----IPALGILPLGTANDFA 98


                  ...
gi 21361699   284 GAV 286
Cdd:TIGR00147  99 RSL 101
YegS_C pfam19279
YegS C-terminal NAD kinase beta sandwich-like domain; This entry represents the C-terminal ...
 556-644 5.90e-04

YegS C-terminal NAD kinase beta sandwich-like domain; This entry represents the C-terminal domain found in the YegS protein. It is related to the beta sandwich domain of NAD kinases. The structure of YegS reveals a two-domain protein with the active site crevice found between the two domains. The C-terminal domain contains 13 beta-strands and two alpha-helices. The likely substrate for YegS is phosphatidylglycerol.


Pssm-ID: 437111  Cd Length: 158  Bit Score: 41.03  E-value: 5.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361699   556 APHARFDDGLVHLCWVRsGISRAALLRLFLAMERGSHFSLgcPQLGYAAARAFRLEplTPRGV-LTVDGEQVEYGPLQAQ 634
Cdd:pfam19279  74 APDARVDDGLLDVVVIE-AASRRTLLRLLPKVYDGRHVRL--PQVEVLRGREVRIE--ADRPLpAGADGEVLGPLPVRVE 148

                          90
                  ....*....|
gi 21361699   635 MHPGIGTLLT 644
Cdd:pfam19279 149 VLPGALRVLA 158
PHA03247 PHA03247
large tegument protein UL36; Provisional
 355-516 2.04e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 2.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361699   355 SARFTLGTVLGLATLHTYRGRLSYLPATVEPASPTPAHSLPRAKSELTLTPDPAPPmahSPLHRSVSDLPLPLPQPALAS 434
Cdd:PHA03247 2687 AARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPP---AVPAGPATPGGPARPARPPTT 2763

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361699   435 PGSPEPLPILSLNGGGPELAGDWGGAGDAPLSPDPLLSSPPGSPKAALHSPVSEGAPVIPPSSGLPLPTPDARVGASTCG 514
Cdd:PHA03247 2764 AGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPP 2843


                  ..
gi 21361699   515 PP 516
Cdd:PHA03247 2844 GP 2845
KLF9_13_N-like cd21975
Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like ...
 450-515 2.19e-03

Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like transcription factors (KLFs) belong to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved alpha-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the related N-terminal domains of KLF9, KLF13, KLF14, KLF16, and similar proteins.


Pssm-ID: 409240 [Multi-domain]  Cd Length: 163  Bit Score: 39.29  E-value: 2.19e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21361699 450 GPELAGDWGGAGDAPLSPDPLLSSPPGSpkAALHSPVSEGAPVIPPSSGLPLPTPDARVGASTCGP 515
Cdd:cd21975  81 GPSVEGSSLESGDADMGSDSDVAPASGA--AASTSPESSSDAASSPSPLSLLHPGEAGLEPERPRP 144
PRK13337 PRK13337
putative lipid kinase; Reviewed
 188-287 9.27e-03

putative lipid kinase; Reviewed


Pssm-ID: 183982 [Multi-domain]  Cd Length: 304  Bit Score: 38.49  E-value: 9.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361699  188 NPFGGRGLAwqwcKNH---VLPMISEAGLSFNLIQTERQNHARELVQGLSLSEWDGIVTVSGDGLLHEVLNGLLDRPdwe 264
Cdd:PRK13337   9 NPTSGRELF----KKNlpdVLQKLEQAGYETSAHATTGPGDATLAAERAVERKFDLVIAAGGDGTLNEVVNGIAEKE--- 81

                         90       100
                 ....*....|....*....|....
gi 21361699  265 eavKMP-VGILPCGSGNALAGAVN 287
Cdd:PRK13337  82 ---NRPkLGIIPVGTTNDFARALH 102
 
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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