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Conserved domains on  [gi|284011151|gb|ADB57104|]
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TrkA-N domain protein [Archaeoglobus profundus DSM 5631]

Protein Classification

DHH family phosphoesterase( domain architecture ID 12033305)

DHH family phosphoesterase with TrkA-N domain similar to Methanocaldococcus jannaschii uncharacterized protein MJ1633

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NrnA COG0618
nanoRNase/pAp phosphatase, hydrolyzes c-di-AMP and oligoRNAs [Nucleotide transport and ...
 148-449 9.61e-82

nanoRNase/pAp phosphatase, hydrolyzes c-di-AMP and oligoRNAs [Nucleotide transport and metabolism, Signal transduction mechanisms];


:

Pssm-ID: 440383 [Multi-domain]  Cd Length: 312  Bit Score: 255.50  E-value: 9.61e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284011151 148 LAKVIEScRGRLGIFTHDNPDPDAISSALALKEIARYYGVEADILYYGDImHQENRAMVNLLEIEmlKADEVDLSiYDKF 227
Cdd:COG0618    3 LAELLKK-ADRILILTHVNPDGDALGSALALALLLRALGKEVTIVYPGEI-PHELAFLPGADEIV--RLEDVDLE-YDLV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284011151 228 AIVDCSKPGVNNSIP---QNIHISIVIDHHPAEDVMADFVDIRTDVGACATILTEYLKEMRITPSRTLATALFFGIKTET 304
Cdd:COG0618   78 IVVDTSSPDRIGDLAellEKAKPVIVIDHHPSNDDFGDFNDVDPDAGATSEIIYELLKELGIEIDPEIATALYTGIVTDT 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284011151 305 NNFK-KNTRTADFLAAAFLYPF-VDHELIEKMEGPAISTETLDVLATAIKNRQVYS--SFLISFAGYIT------NRDVL 374
Cdd:COG0618  158 GSFRySNTTPRDFRAAAELLEKgADLDLIARILYPSLSLEQLKLLGRALENLEVLEdgKVAYSYLTKEDleefgaTPDDT 237

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 284011151 375 PQAADFLLRLEGISTVLVFGILKDK-VYISARNKDvRINIGEVLKRaFGdvgsAGGHAHSGGAQIPLGIFGEVTDR 449
Cdd:COG0618  238 EGLVDYLLSIEGVEVAVVFGEVEDGeIKVSLRSKG-RVDVGEIARE-FG----GGGHARAAGATIPGLDLEEVVEK 307
TrkA_N pfam02254
TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include ...
 9-124 3.78e-26

TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include potassium channels, phosphoesterases, and various other transporters. This domain binds to NAD.


:

Pssm-ID: 426679 [Multi-domain]  Cd Length: 115  Bit Score: 102.22  E-value: 3.78e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284011151    9 YIVIGCGATGFSVVKELvRKGKKVLAIDISKERVEVLRDENYDAIVGDATDESLYQDIDFSKVSIVMVLTSDTEANKRAV 88
Cdd:pfam02254   1 IIIIGYGRVGRSLAEEL-SEGGDVVVIDKDEERVEELREEGVPVVVGDATDEEVLEEAGIEEADAVIAATGDDEANILIV 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 284011151   89 EIVRSISKDVFIIARSQSSKTKEELEQAGADFVVVP 124
Cdd:pfam02254  80 LLARELNPDKKIIARANDPEHAELLRRLGADHVISP 115
 
Name Accession Description Interval E-value
NrnA COG0618
nanoRNase/pAp phosphatase, hydrolyzes c-di-AMP and oligoRNAs [Nucleotide transport and ...
 148-449 9.61e-82

nanoRNase/pAp phosphatase, hydrolyzes c-di-AMP and oligoRNAs [Nucleotide transport and metabolism, Signal transduction mechanisms];


Pssm-ID: 440383 [Multi-domain]  Cd Length: 312  Bit Score: 255.50  E-value: 9.61e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284011151 148 LAKVIEScRGRLGIFTHDNPDPDAISSALALKEIARYYGVEADILYYGDImHQENRAMVNLLEIEmlKADEVDLSiYDKF 227
Cdd:COG0618    3 LAELLKK-ADRILILTHVNPDGDALGSALALALLLRALGKEVTIVYPGEI-PHELAFLPGADEIV--RLEDVDLE-YDLV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284011151 228 AIVDCSKPGVNNSIP---QNIHISIVIDHHPAEDVMADFVDIRTDVGACATILTEYLKEMRITPSRTLATALFFGIKTET 304
Cdd:COG0618   78 IVVDTSSPDRIGDLAellEKAKPVIVIDHHPSNDDFGDFNDVDPDAGATSEIIYELLKELGIEIDPEIATALYTGIVTDT 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284011151 305 NNFK-KNTRTADFLAAAFLYPF-VDHELIEKMEGPAISTETLDVLATAIKNRQVYS--SFLISFAGYIT------NRDVL 374
Cdd:COG0618  158 GSFRySNTTPRDFRAAAELLEKgADLDLIARILYPSLSLEQLKLLGRALENLEVLEdgKVAYSYLTKEDleefgaTPDDT 237

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 284011151 375 PQAADFLLRLEGISTVLVFGILKDK-VYISARNKDvRINIGEVLKRaFGdvgsAGGHAHSGGAQIPLGIFGEVTDR 449
Cdd:COG0618  238 EGLVDYLLSIEGVEVAVVFGEVEDGeIKVSLRSKG-RVDVGEIARE-FG----GGGHARAAGATIPGLDLEEVVEK 307
TrkA_N pfam02254
TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include ...
 9-124 3.78e-26

TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include potassium channels, phosphoesterases, and various other transporters. This domain binds to NAD.


Pssm-ID: 426679 [Multi-domain]  Cd Length: 115  Bit Score: 102.22  E-value: 3.78e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284011151    9 YIVIGCGATGFSVVKELvRKGKKVLAIDISKERVEVLRDENYDAIVGDATDESLYQDIDFSKVSIVMVLTSDTEANKRAV 88
Cdd:pfam02254   1 IIIIGYGRVGRSLAEEL-SEGGDVVVIDKDEERVEELREEGVPVVVGDATDEEVLEEAGIEEADAVIAATGDDEANILIV 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 284011151   89 EIVRSISKDVFIIARSQSSKTKEELEQAGADFVVVP 124
Cdd:pfam02254  80 LLARELNPDKKIIARANDPEHAELLRRLGADHVISP 115
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
 1-137 2.44e-22

Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and metabolism, Signal transduction mechanisms];


Pssm-ID: 440335 [Multi-domain]  Cd Length: 296  Bit Score: 96.67  E-value: 2.44e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284011151   1 MEEKFSHEYIVIGCGATGFSVVKELVRKGKKVLAIDISKERVEVLRDENYDAIVGDATDESLYQDIDFSKVSIVMVLTSD 80
Cdd:COG0569   90 GIKKLKMHVIIIGAGRVGRSLARELEEEGHDVVVIDKDPERVERLAEEDVLVIVGDATDEEVLEEAGIEDADAVIAATGD 169

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 284011151  81 TEANKRAVEIVRSISKdVFIIARSQSSKTKEELEQAGADFVVVPSEAMKTIVLEVIR 137
Cdd:COG0569  170 DEANILACLLAKELGV-PRIIARANDPEYADLLERLGADVVISPERLAARRIARLLL 225
DHH pfam01368
DHH family; It is predicted that this family of proteins all perform a phosphoesterase ...
 161-300 1.30e-12

DHH family; It is predicted that this family of proteins all perform a phosphoesterase function. It included the single stranded DNA exonuclease RecJ.


Pssm-ID: 460177 [Multi-domain]  Cd Length: 145  Bit Score: 65.29  E-value: 1.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284011151  161 IFTHDNPDPDAISSALALKEIARYYgVEADILYYGDIMHQENRAmVNLLEIEMLKADEvdlsiyDKFAIVDCSKP---GV 237
Cdd:pfam01368   4 IYGHYNPDGDGIGSALGLYRYLKEL-VGPDVEYYIPDRLEEGYG-INPEAIEELIDFD------TLLITVDCGIKsveGI 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 284011151  238 NNSIPQNIHIsIVIDHHPAEDVMADFVDI----RTDVGACATILTE----YLKEMRITPSRTLATALFFGI 300
Cdd:pfam01368  76 ELAKELGIDV-IVIDHHLPNDFLPDADAIinprEPPASSTSEVVFKllqyAYGEEGKEIDKELADLLLLGI 145
PRK05427 PRK05427
putative manganese-dependent inorganic pyrophosphatase; Provisional
 161-322 1.20e-06

putative manganese-dependent inorganic pyrophosphatase; Provisional


Pssm-ID: 235458 [Multi-domain]  Cd Length: 308  Bit Score: 50.21  E-value: 1.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284011151 161 IFTHDNPDPDAISSALALKEIARYYGVEADILYYGDImhqeNRAMVNLLEIEMLKADEV--DLSIYDKFAIVDCSKPGVN 238
Cdd:PRK05427   6 VFGHKNPDTDSICSAIAYAYLKKALGLDAEAVRLGEP----NPETAFVLDYFGVEAPELitSVAGEVQVILVDHNEFQQS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284011151 239 nsiPQNI---HISIVIDHHPAEDVM-ADFVDIRTD-VGACATILTEYLKEMRITPSRTLATALFFGIKTETNNFKKNTRT 313
Cdd:PRK05427  82 ---PDDIdeaTVVGVVDHHRLGNFEtSNPLYYRIEpVGCTATILYKMFKENGVEIPKEIAGLMLSAILSDTLLFKSPTTT 158

                        170
                 ....*....|
gi 284011151 314 -ADFLAAAFL 322
Cdd:PRK05427 159 eQDKAAAEEL 168
trkA PRK09496
Trk system potassium transporter TrkA;
2-84 1.22e-04

Trk system potassium transporter TrkA;


Pssm-ID: 236541 [Multi-domain]  Cd Length: 453  Bit Score: 44.34  E-value: 1.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284011151   2 EEKFSHEYIVIGCGATGFSVVKELVRKGKKVLAIDISKERVEVLRDENYDAIV--GDATDESLYQDIDFSKVSIVMVLTS 79
Cdd:PRK09496 227 LEKPVKRVMIVGGGNIGYYLAKLLEKEGYSVKLIERDPERAEELAEELPNTLVlhGDGTDQELLEEEGIDEADAFIALTN 306


                 ....*
gi 284011151  80 DTEAN 84
Cdd:PRK09496 307 DDEAN 311
sugar_DH cd08236
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol ...
 10-100 1.36e-03

NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol dehydrogenases and other sugar dehydrogenases of the medium-chain dehydrogenase/reductase family (MDR), which includes zinc-dependent alcohol dehydrogenase and related proteins. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose. Sorbitol dehydrogenase is tetrameric and has a single catalytic zinc per subunit. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Related proteins include threonine dehydrogenase, formaldehyde dehydrogenase, and butanediol dehydrogenase. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Horse liver alcohol dehydrogenase is a dimeric enzyme and each subunit has two domains. The NAD binding domain is in a Rossmann fold and the catalytic domain contains a zinc ion to which substrates bind. There is a cleft between the domains that closes upon formation of the ternary complex.


Pssm-ID: 176198 [Multi-domain]  Cd Length: 343  Bit Score: 40.67  E-value: 1.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284011151  10 IVIGCGATGFSVVKELVRKG-KKVLAIDISKERVEVLRDENYDAIVgDATDESLYQDIDF---SKVSIVMVLTSDTEANK 85
Cdd:cd08236  164 VVIGAGTIGLLAIQWLKILGaKRVIAVDIDDEKLAVARELGADDTI-NPKEEDVEKVRELtegRGADLVIEAAGSPATIE 242

                         90
                 ....*....|....*
gi 284011151  86 RAVEIVRSISKDVFI 100
Cdd:cd08236  243 QALALARPGGKVVLV 257
 
Name Accession Description Interval E-value
NrnA COG0618
nanoRNase/pAp phosphatase, hydrolyzes c-di-AMP and oligoRNAs [Nucleotide transport and ...
 148-449 9.61e-82

nanoRNase/pAp phosphatase, hydrolyzes c-di-AMP and oligoRNAs [Nucleotide transport and metabolism, Signal transduction mechanisms];


Pssm-ID: 440383 [Multi-domain]  Cd Length: 312  Bit Score: 255.50  E-value: 9.61e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284011151 148 LAKVIEScRGRLGIFTHDNPDPDAISSALALKEIARYYGVEADILYYGDImHQENRAMVNLLEIEmlKADEVDLSiYDKF 227
Cdd:COG0618    3 LAELLKK-ADRILILTHVNPDGDALGSALALALLLRALGKEVTIVYPGEI-PHELAFLPGADEIV--RLEDVDLE-YDLV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284011151 228 AIVDCSKPGVNNSIP---QNIHISIVIDHHPAEDVMADFVDIRTDVGACATILTEYLKEMRITPSRTLATALFFGIKTET 304
Cdd:COG0618   78 IVVDTSSPDRIGDLAellEKAKPVIVIDHHPSNDDFGDFNDVDPDAGATSEIIYELLKELGIEIDPEIATALYTGIVTDT 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284011151 305 NNFK-KNTRTADFLAAAFLYPF-VDHELIEKMEGPAISTETLDVLATAIKNRQVYS--SFLISFAGYIT------NRDVL 374
Cdd:COG0618  158 GSFRySNTTPRDFRAAAELLEKgADLDLIARILYPSLSLEQLKLLGRALENLEVLEdgKVAYSYLTKEDleefgaTPDDT 237

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 284011151 375 PQAADFLLRLEGISTVLVFGILKDK-VYISARNKDvRINIGEVLKRaFGdvgsAGGHAHSGGAQIPLGIFGEVTDR 449
Cdd:COG0618  238 EGLVDYLLSIEGVEVAVVFGEVEDGeIKVSLRSKG-RVDVGEIARE-FG----GGGHARAAGATIPGLDLEEVVEK 307
TrkA_N pfam02254
TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include ...
 9-124 3.78e-26

TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include potassium channels, phosphoesterases, and various other transporters. This domain binds to NAD.


Pssm-ID: 426679 [Multi-domain]  Cd Length: 115  Bit Score: 102.22  E-value: 3.78e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284011151    9 YIVIGCGATGFSVVKELvRKGKKVLAIDISKERVEVLRDENYDAIVGDATDESLYQDIDFSKVSIVMVLTSDTEANKRAV 88
Cdd:pfam02254   1 IIIIGYGRVGRSLAEEL-SEGGDVVVIDKDEERVEELREEGVPVVVGDATDEEVLEEAGIEEADAVIAATGDDEANILIV 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 284011151   89 EIVRSISKDVFIIARSQSSKTKEELEQAGADFVVVP 124
Cdd:pfam02254  80 LLARELNPDKKIIARANDPEHAELLRRLGADHVISP 115
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
 1-137 2.44e-22

Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and metabolism, Signal transduction mechanisms];


Pssm-ID: 440335 [Multi-domain]  Cd Length: 296  Bit Score: 96.67  E-value: 2.44e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284011151   1 MEEKFSHEYIVIGCGATGFSVVKELVRKGKKVLAIDISKERVEVLRDENYDAIVGDATDESLYQDIDFSKVSIVMVLTSD 80
Cdd:COG0569   90 GIKKLKMHVIIIGAGRVGRSLARELEEEGHDVVVIDKDPERVERLAEEDVLVIVGDATDEEVLEEAGIEDADAVIAATGD 169

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 284011151  81 TEANKRAVEIVRSISKdVFIIARSQSSKTKEELEQAGADFVVVPSEAMKTIVLEVIR 137
Cdd:COG0569  170 DEANILACLLAKELGV-PRIIARANDPEYADLLERLGADVVISPERLAARRIARLLL 225
Kch COG1226
Voltage-gated potassium channel Kch [Inorganic ion transport and metabolism];
1-125 5.95e-20

Voltage-gated potassium channel Kch [Inorganic ion transport and metabolism];


Pssm-ID: 440839 [Multi-domain]  Cd Length: 279  Bit Score: 89.79  E-value: 5.95e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284011151   1 MEEKFSHEYIVIGCGATGFSVVKELVRKGKKVLAIDISKERVEVLRDENYDAIVGDATDESLYQDIDFSKVSIVMVLTSD 80
Cdd:COG1226  119 DAIDLEGHVIIAGFGRVGQIVARLLRAEGIPFVVIDLDPERVEELRRFGIKVYYGDATRPDVLEAAGIERARALVVAIDD 198

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 284011151  81 TEANKRAVEIVRSISKDVFIIARSQSSKTKEELEQAGADFVVVPS 125
Cdd:COG1226  199 PEAALRIVELARELNPDLKIIARARDREHAEELRQAGADEVVRET 243
DHH pfam01368
DHH family; It is predicted that this family of proteins all perform a phosphoesterase ...
 161-300 1.30e-12

DHH family; It is predicted that this family of proteins all perform a phosphoesterase function. It included the single stranded DNA exonuclease RecJ.


Pssm-ID: 460177 [Multi-domain]  Cd Length: 145  Bit Score: 65.29  E-value: 1.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284011151  161 IFTHDNPDPDAISSALALKEIARYYgVEADILYYGDIMHQENRAmVNLLEIEMLKADEvdlsiyDKFAIVDCSKP---GV 237
Cdd:pfam01368   4 IYGHYNPDGDGIGSALGLYRYLKEL-VGPDVEYYIPDRLEEGYG-INPEAIEELIDFD------TLLITVDCGIKsveGI 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 284011151  238 NNSIPQNIHIsIVIDHHPAEDVMADFVDI----RTDVGACATILTE----YLKEMRITPSRTLATALFFGI 300
Cdd:pfam01368  76 ELAKELGIDV-IVIDHHLPNDFLPDADAIinprEPPASSTSEVVFKllqyAYGEEGKEIDKELADLLLLGI 145
DHHA1 pfam02272
DHHA1 domain; This domain is often found adjacent to the DHH domain pfam01368 and is called ...
 328-449 6.55e-10

DHHA1 domain; This domain is often found adjacent to the DHH domain pfam01368 and is called DHHA1 for DHH associated domain. This domain is diagnostic of DHH subfamily 1 members. This domains is also found in alanyl tRNA synthetase, suggesting that this domain may have an RNA binding function. The domain is about 60 residues long and contains a conserved GG motif.


Pssm-ID: 396724 [Multi-domain]  Cd Length: 139  Bit Score: 57.07  E-value: 6.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284011151  328 HELIEKMEGPAISTETLDVLATAIKNRQVysSFLISFAGYITNRDVLPQAADFLL-RLEGISTVLVFGILKDKVYISAR- 405
Cdd:pfam02272  12 EKELEELKEALALLKAKELLEKAEEINGV--KVLVAEVGEGWDAGALGIAADRLKkKLGDPVIVLVAKEDGDKVKVSARs 89

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 284011151  406 NKDVRINIGEVLKRAFGDV-GSAGGHAHSGGAQIPLGIFGEVTDR 449
Cdd:pfam02272  90 SKDKGVDAGELLKEVAAILgGGGGGHDLAAGAGIDAEKLDEALEL 134
PPX1 COG1227
Inorganic pyrophosphatase/exopolyphosphatase [Energy production and conversion];
161-322 4.47e-07

Inorganic pyrophosphatase/exopolyphosphatase [Energy production and conversion];


Pssm-ID: 440840 [Multi-domain]  Cd Length: 307  Bit Score: 51.32  E-value: 4.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284011151 161 IFTHDNPDPDAISSALALKEIARYYGVEADILYYGDImhqeNRAMVNLLEIEMLKADEV--DLSIYDKFAIVDCSKPGvn 238
Cdd:COG1227    6 VFGHKNPDTDSICSAIAYAYLKNQLGEDAEAVRLGEP----NPETAFVLDYFGVEAPELieDVAAGKKVILVDHNELA-- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284011151 239 nSIPQNI---HISIVIDHHPaedvMADF-----VDIRTD-VGACATILTEYLKEMRITPSRTLATALFFGIKTETNNFKK 309
Cdd:COG1227   80 -QSVDGIdeaEILEIIDHHR----IGDFetaapLYIRIEpVGCTATIIAKLYKENGVEIPKEIAGLMLSAILSDTLLFKS 154

                        170
                 ....*....|....
gi 284011151 310 NTRTA-DFLAAAFL 322
Cdd:COG1227  155 PTTTDeDREAAEEL 168
PRK05427 PRK05427
putative manganese-dependent inorganic pyrophosphatase; Provisional
 161-322 1.20e-06

putative manganese-dependent inorganic pyrophosphatase; Provisional


Pssm-ID: 235458 [Multi-domain]  Cd Length: 308  Bit Score: 50.21  E-value: 1.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284011151 161 IFTHDNPDPDAISSALALKEIARYYGVEADILYYGDImhqeNRAMVNLLEIEMLKADEV--DLSIYDKFAIVDCSKPGVN 238
Cdd:PRK05427   6 VFGHKNPDTDSICSAIAYAYLKKALGLDAEAVRLGEP----NPETAFVLDYFGVEAPELitSVAGEVQVILVDHNEFQQS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284011151 239 nsiPQNI---HISIVIDHHPAEDVM-ADFVDIRTD-VGACATILTEYLKEMRITPSRTLATALFFGIKTETNNFKKNTRT 313
Cdd:PRK05427  82 ---PDDIdeaTVVGVVDHHRLGNFEtSNPLYYRIEpVGCTATILYKMFKENGVEIPKEIAGLMLSAILSDTLLFKSPTTT 158

                        170
                 ....*....|
gi 284011151 314 -ADFLAAAFL 322
Cdd:PRK05427 159 eQDKAAAEEL 168
PRK14538 PRK14538
putative bifunctional signaling protein/50S ribosomal protein L9; Provisional
 161-449 9.88e-06

putative bifunctional signaling protein/50S ribosomal protein L9; Provisional


Pssm-ID: 173004 [Multi-domain]  Cd Length: 838  Bit Score: 48.29  E-value: 9.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284011151 161 IFTHDNPDPDAISSALAL--------KEIARYYGVEADIL------YYGDIMHQENRAMVNLLEIEMLKADEVDlsiYDK 226
Cdd:PRK14538 372 IMGHNHTDLDSLGSMIAFykialtihPDNNNYIILDEEKLdksltpVYHQLIKQEHKVTLNIITTQQASKMIKK---NDL 448

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284011151 227 FAIVDCSKPGVNNSiPQNIHIS---IVIDHH--PAEDVMADFVDIRTDVGACATILTEYL----KEMRITPSRtlATALF 297
Cdd:PRK14538 449 IAVLDTQTKDIVNS-PELLSLTnniIVIDHHraTEEIIPSIFSYVDSSASSTVELLVELMgfleKEIHITAFE--ASIMY 525

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284011151 298 FGIKTETNNFKKNTRTADFLAAAFLYPF-------------------VDHELIEKMEgpaistETLDVLATaIKNRQVYS 358
Cdd:PRK14538 526 AGILIDTNAFIYRTSSRTFEVASKLKDLgadaievkswlrkdfdkvlEINKLISKME------IFMDRFAI-IKSEEIYD 598

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284011151 359 sflisfagyitNRDVLPQAADFLLRLEGISTVLVFGILKD-KVYISARNKDvRINIGEVLKRAFGdvgsaGGHAHSGGAQ 437
Cdd:PRK14538 599 -----------NRSFLAQVAESVLNIQNVDAAFMIAKISDnTIAISARSYN-EINVQTIMEQMEG-----GGHLNSAATQ 661

                        330
                 ....*....|..
gi 284011151 438 IPLGIFGEVTDR 449
Cdd:PRK14538 662 IKGTNIKTVTQT 673
trkA PRK09496
Trk system potassium transporter TrkA;
2-84 1.22e-04

Trk system potassium transporter TrkA;


Pssm-ID: 236541 [Multi-domain]  Cd Length: 453  Bit Score: 44.34  E-value: 1.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284011151   2 EEKFSHEYIVIGCGATGFSVVKELVRKGKKVLAIDISKERVEVLRDENYDAIV--GDATDESLYQDIDFSKVSIVMVLTS 79
Cdd:PRK09496 227 LEKPVKRVMIVGGGNIGYYLAKLLEKEGYSVKLIERDPERAEELAEELPNTLVlhGDGTDQELLEEEGIDEADAFIALTN 306


                 ....*
gi 284011151  80 DTEAN 84
Cdd:PRK09496 307 DDEAN 311
trkA PRK09496
Trk system potassium transporter TrkA;
10-137 1.39e-04

Trk system potassium transporter TrkA;


Pssm-ID: 236541 [Multi-domain]  Cd Length: 453  Bit Score: 44.34  E-value: 1.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284011151  10 IVIGCGATGFSVVKELVRKGKKVLAIDISKERVEVLRDEnYD--AIVGDATDESLYQDIDFSKVSIVMVLTSDTEANKRA 87
Cdd:PRK09496   4 IIVGAGQVGYTLAENLSGENNDVTVIDTDEERLRRLQDR-LDvrTVVGNGSSPDVLREAGAEDADLLIAVTDSDETNMVA 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 284011151  88 VEIVRSISKDVFIIAR--SQSSKTKEEL---EQAGADFVVVPSEAMKTIVLEVIR 137
Cdd:PRK09496  83 CQIAKSLFGAPTTIARvrNPEYAEYDKLfskEALGIDLLISPELLVAREIARLIE 137
sugar_DH cd08236
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol ...
 10-100 1.36e-03

NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol dehydrogenases and other sugar dehydrogenases of the medium-chain dehydrogenase/reductase family (MDR), which includes zinc-dependent alcohol dehydrogenase and related proteins. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose. Sorbitol dehydrogenase is tetrameric and has a single catalytic zinc per subunit. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Related proteins include threonine dehydrogenase, formaldehyde dehydrogenase, and butanediol dehydrogenase. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Horse liver alcohol dehydrogenase is a dimeric enzyme and each subunit has two domains. The NAD binding domain is in a Rossmann fold and the catalytic domain contains a zinc ion to which substrates bind. There is a cleft between the domains that closes upon formation of the ternary complex.


Pssm-ID: 176198 [Multi-domain]  Cd Length: 343  Bit Score: 40.67  E-value: 1.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284011151  10 IVIGCGATGFSVVKELVRKG-KKVLAIDISKERVEVLRDENYDAIVgDATDESLYQDIDF---SKVSIVMVLTSDTEANK 85
Cdd:cd08236  164 VVIGAGTIGLLAIQWLKILGaKRVIAVDIDDEKLAVARELGADDTI-NPKEEDVEKVRELtegRGADLVIEAAGSPATIE 242

                         90
                 ....*....|....*
gi 284011151  86 RAVEIVRSISKDVFI 100
Cdd:cd08236  243 QALALARPGGKVVLV 257
PRK10537 PRK10537
voltage-gated potassium channel protein;
7-124 3.21e-03

voltage-gated potassium channel protein;


Pssm-ID: 236711 [Multi-domain]  Cd Length: 393  Bit Score: 39.62  E-value: 3.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284011151   7 HEYIVIGCGATGFSVVKELVRKGKKVLAIdiSKERVEVLRDENYDAIVGDATDESLYQDIDFSKVSIVMVLTSDTEANKR 86
Cdd:PRK10537 241 DHFIICGHSPLAINTYLGLRQRGQAVTVI--VPLGLEHRLPDDADLIPGDSSDSAVLKKAGAARARAILALRDNDADNAF 318

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 284011151  87 AVEIVRSISKDVFIIARSQSSKTKEELEQAGADFVVVP 124
Cdd:PRK10537 319 VVLAAKEMSSDVKTVAAVNDSKNLEKIKRVHPDMIFSP 356
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
 11-114 4.61e-03

Alcohol dehydrogenases of the MDR family; This group contains members identified as related to zinc-dependent alcohol dehydrogenase and other members of the MDR family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group includes various activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176222 [Multi-domain]  Cd Length: 337  Bit Score: 39.09  E-value: 4.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284011151  11 VIGCGATGFSVVKELVRKGKKVLAIDISKERVEVLRDENYDAIV--GDATDESLYQDI-DFSKVSIVMVLTSDTEANKRA 87
Cdd:cd08261  165 VVGAGPIGLGVIQVAKARGARVIVVDIDDERLEFARELGADDTInvGDEDVAARLRELtDGEGADVVIDATGNPASMEEA 244

                         90       100       110
                 ....*....|....*....|....*....|...
gi 284011151  88 VEIVRSISKDVFI------IARSQSSKTKEELE 114
Cdd:cd08261  245 VELVAHGGRVVLVglskgpVTFPDPEFHKKELT 277
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 12-59 6.31e-03

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 36.00  E-value: 6.31e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 284011151   12 IGCGaTGFsVVKELVRK-GKKVLAIDISKERVEVLRDE------NYDAIVGDATD 59
Cdd:pfam13649   4 LGCG-TGR-LTLALARRgGARVTGVDLSPEMLERARERaaeaglNVEFVQGDAED 56
PRK10669 PRK10669
putative cation:proton antiport protein; Provisional
 10-123 7.40e-03

putative cation:proton antiport protein; Provisional


Pssm-ID: 182633 [Multi-domain]  Cd Length: 558  Bit Score: 38.93  E-value: 7.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284011151  10 IVIGCGATGFSVVKELVRKGKKVLAIDISKERVEVLRDENYDAIVGDATDESLyqdIDFSKVSIVMVLTSDTEANKRAVE 89
Cdd:PRK10669 421 LLVGYGRVGSLLGEKLLAAGIPLVVIETSRTRVDELRERGIRAVLGNAANEEI---MQLAHLDCARWLLLTIPNGYEAGE 497

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 284011151  90 IV---RSISKDVFIIARSQSSKTKEELEQAGADFVVV 123
Cdd:PRK10669 498 IVasaREKRPDIEIIARAHYDDEVAYITERGANQVVM 534
NAD_bind_Leu_Phe_Val_DH cd01075
NAD(P) binding domain of leucine dehydrogenase, phenylalanine dehydrogenase, and valine ...
 9-81 7.97e-03

NAD(P) binding domain of leucine dehydrogenase, phenylalanine dehydrogenase, and valine dehydrogenase; Amino acid dehydrogenase (DH) is a widely distributed family of enzymes that catalyzes the oxidative deamination of an amino acid to its keto acid and ammonia with concomitant reduction of NADP+. For example, leucine DH catalyzes the reversible oxidative deamination of L-leucine and several other straight or branched chain amino acids to the corresponding 2-oxoacid derivative. Amino acid DH -like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133444  Cd Length: 200  Bit Score: 37.57  E-value: 7.97e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 284011151   9 YIVIGCGATGFSVVKELVRKGKKVLAIDISKERVEVLRdENYDA-IVgdATDESLYQDID-FSKVSIVMVLTSDT 81
Cdd:cd01075   31 VAVQGLGKVGYKLAEHLLEEGAKLIVADINEEAVARAA-ELFGAtVV--APEEIYSVDADvFAPCALGGVINDDT 102
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 13-100 8.87e-03

cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB) is a classical SDR, it is of particular importance for its role in the degradation of biphenyl/polychlorinated biphenyls(PCBs); PCBs are a significant source of environmental contamination. This subgroup also includes Pseudomonas putida F1 cis-biphenyl-1,2-dihydrodiol-1,2-dehydrogenase (aka cis-benzene glycol dehydrogenase, encoded by the bnzE gene), which participates in benzene metabolism. In addition it includes Pseudomonas sp. C18 putative 1,2-dihydroxy-1,2-dihydronaphthalene dehydrogenase (aka dibenzothiophene dihydrodiol dehydrogenase, encoded by the doxE gene) which participates in an upper naphthalene catabolic pathway. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187606 [Multi-domain]  Cd Length: 257  Bit Score: 37.72  E-value: 8.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284011151  13 GCGATGFSVVKELVRKGKKVLAIDISKERVEVLRDENYDAIVGDATDESLYQDidfskvsivmvltsdteaNKRAV-EIV 91
Cdd:cd05348   12 GGSGLGRALVERFVAEGAKVAVLDRSAEKVAELRADFGDAVVGVEGDVRSLAD------------------NERAVaRCV 73

                         90
                 ....*....|
gi 284011151  92 RSISK-DVFI 100
Cdd:cd05348   74 ERFGKlDCFI 83
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
15-59 9.24e-03

Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 38.04  E-value: 9.24e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 284011151  15 GATGF---SVVKELVRKGKKVLAIDISKERVEVLRD-ENYDAIVGDATD 59
Cdd:COG0451    6 GGAGFigsHLARRLLARGHEVVGLDRSPPGAANLAAlPGVEFVRGDLRD 54
 
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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