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Conserved domains on  [gi|1093455174|ref|WP_070833248|]
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MULTISPECIES: TrkA family potassium uptake protein [Corynebacterium]

Protein Classification

potassium channel family protein( domain architecture ID 11426271)

potassium channel family protein spans the cell membrane to form a conduction pathway or pore, through which selective ions such as potassium, sodium, and calcium translocate across cell membranes, similar to Trk system potassium uptake protein TrkA

CATH:  1.20.5.870|3.30.70.1450|3.40.50.720
Gene Ontology:  GO:0016020|GO:0022857|GO:0030001|GO:0034220
PubMed:  15816170|9525859|11836519|1772658|11178249
SCOP:  4000005|4000027
TCDB:  1.A.1

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
 25-219 7.28e-44

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: 149.06  E-value: 7.28e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455174  25 VVILGMGRFGQALGEELVAGGIEVLCVDHREKVVQELSSTFDHVVTADTTMPEVLKQLGVDEAERVVIAIGSDiEASLLT 104
Cdd:COG0569    98 VIIIGAGRVGRSLARELEEEGHDVVVIDKDPERVERLAEEDVLVIVGDATDEEVLEEAGIEDADAVIAATGDD-EANILA 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455174 105 ASALVDMGVPMIWAKADNQAHAKILGQIGVHHVIRPEADTGRRIAHLI-GGKVQDFLEFDR-DYAVGKVAPPIHC--LDK 180
Cdd:COG0569   177 CLLAKELGVPRIIARANDPEYADLLERLGADVVISPERLAARRIARLLlRPGVLDVLELADgDAEIVEVTVPEGSplVGK 256

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1093455174 181 TVAEINQSAP--ITVVAVQKRGQRFRPaLADDRISAGDLLI 219
Cdd:COG0569   257 TLKELDLRERygVTVVAIKRGGEVIIP-SGDTVLEAGDELI 296
 
Name Accession Description Interval E-value
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
 25-219 7.28e-44

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: 149.06  E-value: 7.28e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455174  25 VVILGMGRFGQALGEELVAGGIEVLCVDHREKVVQELSSTFDHVVTADTTMPEVLKQLGVDEAERVVIAIGSDiEASLLT 104
Cdd:COG0569    98 VIIIGAGRVGRSLARELEEEGHDVVVIDKDPERVERLAEEDVLVIVGDATDEEVLEEAGIEDADAVIAATGDD-EANILA 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455174 105 ASALVDMGVPMIWAKADNQAHAKILGQIGVHHVIRPEADTGRRIAHLI-GGKVQDFLEFDR-DYAVGKVAPPIHC--LDK 180
Cdd:COG0569   177 CLLAKELGVPRIIARANDPEYADLLERLGADVVISPERLAARRIARLLlRPGVLDVLELADgDAEIVEVTVPEGSplVGK 256

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1093455174 181 TVAEINQSAP--ITVVAVQKRGQRFRPaLADDRISAGDLLI 219
Cdd:COG0569   257 TLKELDLRERygVTVVAIKRGGEVIIP-SGDTVLEAGDELI 296
TrkA_N pfam02254
TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include ...
 25-140 5.49e-27

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: 99.91  E-value: 5.49e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455174  25 VVILGMGRFGQALGEELVAGGiEVLCVDHREKVVQELSSTFDHVVTADTTMPEVLKQLGVDEAERVVIAIGSDIEASLLT 104
Cdd:pfam02254   1 IIIIGYGRVGRSLAEELSEGG-DVVVIDKDEERVEELREEGVPVVVGDATDEEVLEEAGIEEADAVIAATGDDEANILIV 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1093455174 105 ASALVDMGVPMIWAKADNQAHAKILGQIGVHHVIRP 140
Cdd:pfam02254  80 LLARELNPDKKIIARANDPEHAELLRRLGADHVISP 115
trkA PRK09496
Trk system potassium transporter TrkA;
25-233 7.67e-14

Trk system potassium transporter TrkA;


Pssm-ID: 236541 [Multi-domain]  Cd Length: 453  Bit Score: 69.77  E-value: 7.67e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455174  25 VVILGMGRFGQALGEELVAGGIEVLCVDHREKVVQELSSTFD-HVVTADTTMPEVLKQLGVDEAErVVIAIGSDIEASLL 103
Cdd:PRK09496    3 IIIVGAGQVGYTLAENLSGENNDVTVIDTDEERLRRLQDRLDvRTVVGNGSSPDVLREAGAEDAD-LLIAVTDSDETNMV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455174 104 ---TASALvdMGVPMIWAKADNQ---AHAKILG--QIGVHHVIRPEADTGRRIAHLI------------GGKVQdFLEFd 163
Cdd:PRK09496   82 acqIAKSL--FGAPTTIARVRNPeyaEYDKLFSkeALGIDLLISPELLVAREIARLIeypgaldveefaDGRVQ-LVEV- 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1093455174 164 rdyavgKVAPPIHCLDKTVAEINQSAP---ITVVAVQKRGQRFRPAlADDRISAGDLLIVSGAIRQLETFAGE 233
Cdd:PRK09496  158 ------KVYEGSPLVGKPLSDLREHFPdidVRVVAIFRGGRLIIPR-GDTVIEAGDEVYFIGAREHIRAVMSE 223
SDR_a4 cd05266
atypical (a) SDRs, subgroup 4; Atypical SDRs in this subgroup are poorly defined, one member ...
 25-76 2.22e-03

atypical (a) SDRs, subgroup 4; Atypical SDRs in this subgroup are poorly defined, one member is identified as a putative NAD-dependent epimerase/dehydratase. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif that is related to, but is different from, the archetypical SDRs, GXGXXG. This subgroup also lacks most of the characteristic active site residues of the SDRs; however, the upstream Ser is present at the usual place, and some potential catalytic residues are present in place of the usual YXXXK active site motif. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, 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.


Pssm-ID: 187576 [Multi-domain]  Cd Length: 251  Bit Score: 38.07  E-value: 2.22e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1093455174  25 VVILGMGRFGQALGEELVAGGIEVLCVDHREKVVQELSSTFDHVVTADTTMP 76
Cdd:cd05266     1 VLILGCGYLGQRLARQLLAQGWQVTGTTRSPEKLAADRPAGVTPLAADLTQP 52
 
Name Accession Description Interval E-value
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
 25-219 7.28e-44

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: 149.06  E-value: 7.28e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455174  25 VVILGMGRFGQALGEELVAGGIEVLCVDHREKVVQELSSTFDHVVTADTTMPEVLKQLGVDEAERVVIAIGSDiEASLLT 104
Cdd:COG0569    98 VIIIGAGRVGRSLARELEEEGHDVVVIDKDPERVERLAEEDVLVIVGDATDEEVLEEAGIEDADAVIAATGDD-EANILA 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455174 105 ASALVDMGVPMIWAKADNQAHAKILGQIGVHHVIRPEADTGRRIAHLI-GGKVQDFLEFDR-DYAVGKVAPPIHC--LDK 180
Cdd:COG0569   177 CLLAKELGVPRIIARANDPEYADLLERLGADVVISPERLAARRIARLLlRPGVLDVLELADgDAEIVEVTVPEGSplVGK 256

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1093455174 181 TVAEINQSAP--ITVVAVQKRGQRFRPaLADDRISAGDLLI 219
Cdd:COG0569   257 TLKELDLRERygVTVVAIKRGGEVIIP-SGDTVLEAGDELI 296
TrkA_N pfam02254
TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include ...
 25-140 5.49e-27

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: 99.91  E-value: 5.49e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455174  25 VVILGMGRFGQALGEELVAGGiEVLCVDHREKVVQELSSTFDHVVTADTTMPEVLKQLGVDEAERVVIAIGSDIEASLLT 104
Cdd:pfam02254   1 IIIIGYGRVGRSLAEELSEGG-DVVVIDKDEERVEELREEGVPVVVGDATDEEVLEEAGIEEADAVIAATGDDEANILIV 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1093455174 105 ASALVDMGVPMIWAKADNQAHAKILGQIGVHHVIRP 140
Cdd:pfam02254  80 LLARELNPDKKIIARANDPEHAELLRRLGADHVISP 115
Kch COG1226
Voltage-gated potassium channel Kch [Inorganic ion transport and metabolism];
22-149 1.20e-17

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


Pssm-ID: 440839 [Multi-domain]  Cd Length: 279  Bit Score: 79.39  E-value: 1.20e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455174  22 SSPVVILGMGRFGQALGEELVAGGIEVLCVDHREKVVQELSSTFDHVVTADTTMPEVLKQLGVDEAERVVIAIgSDIEAS 101
Cdd:COG1226   124 EGHVIIAGFGRVGQIVARLLRAEGIPFVVIDLDPERVEELRRFGIKVYYGDATRPDVLEAAGIERARALVVAI-DDPEAA 202

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1093455174 102 LLTASALVDM--GVPMIwAKADNQAHAKILGQIGVHHVIRPEADTGRRIA 149
Cdd:COG1226   203 LRIVELARELnpDLKII-ARARDREHAEELRQAGADEVVRETFESALQLA 251
trkA PRK09496
Trk system potassium transporter TrkA;
25-233 7.67e-14

Trk system potassium transporter TrkA;


Pssm-ID: 236541 [Multi-domain]  Cd Length: 453  Bit Score: 69.77  E-value: 7.67e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455174  25 VVILGMGRFGQALGEELVAGGIEVLCVDHREKVVQELSSTFD-HVVTADTTMPEVLKQLGVDEAErVVIAIGSDIEASLL 103
Cdd:PRK09496    3 IIIVGAGQVGYTLAENLSGENNDVTVIDTDEERLRRLQDRLDvRTVVGNGSSPDVLREAGAEDAD-LLIAVTDSDETNMV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455174 104 ---TASALvdMGVPMIWAKADNQ---AHAKILG--QIGVHHVIRPEADTGRRIAHLI------------GGKVQdFLEFd 163
Cdd:PRK09496   82 acqIAKSL--FGAPTTIARVRNPeyaEYDKLFSkeALGIDLLISPELLVAREIARLIeypgaldveefaDGRVQ-LVEV- 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1093455174 164 rdyavgKVAPPIHCLDKTVAEINQSAP---ITVVAVQKRGQRFRPAlADDRISAGDLLIVSGAIRQLETFAGE 233
Cdd:PRK09496  158 ------KVYEGSPLVGKPLSDLREHFPdidVRVVAIFRGGRLIIPR-GDTVIEAGDEVYFIGAREHIRAVMSE 223
trkA PRK09496
Trk system potassium transporter TrkA;
25-220 7.53e-11

Trk system potassium transporter TrkA;


Pssm-ID: 236541 [Multi-domain]  Cd Length: 453  Bit Score: 60.91  E-value: 7.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455174  25 VVILGMGRFGQALGEELVAGGIEVLCVDHREKVVQELSSTFDH--VVTADTTMPEVLKQLGVDEAErVVIAIGSDIEASL 102
Cdd:PRK09496  234 VMIVGGGNIGYYLAKLLEKEGYSVKLIERDPERAEELAEELPNtlVLHGDGTDQELLEEEGIDEAD-AFIALTNDDEANI 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455174 103 LTASALVDMGVPMIWAKADNQAHAKILGQIGVHHVIRPEADTGRRIAHLI-GGKVQD--FLEFDRDYAVGKVAPPI-HCL 178
Cdd:PRK09496  313 LSSLLAKRLGAKKVIALVNRPAYVDLVEGLGIDIAISPRQATASEILRHVrRGDIVAvhSLRRGAAEAIEAVAHETsKVV 392

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1093455174 179 DKTVAEINQSAPITVVAVQKRGQRFRPaLADDRISAGDLLIV 220
Cdd:PRK09496  393 GKPLKDLKLPKGVLIGAIVRGGEVIIP-TGDTVIEPGDHVIV 433
PRK03562 PRK03562
glutathione-regulated potassium-efflux system protein KefC; Provisional
 22-139 2.17e-08

glutathione-regulated potassium-efflux system protein KefC; Provisional


Pssm-ID: 235131 [Multi-domain]  Cd Length: 621  Bit Score: 53.84  E-value: 2.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455174  22 SSPVVILGMGRFGQALGEELVAGGIEVLCVDHREKVVqELSSTFDH-VVTADTTMPEVLKQLGVDEAERVVIAIgSDIEA 100
Cdd:PRK03562  400 QPRVIIAGFGRFGQIVGRLLLSSGVKMTVLDHDPDHI-ETLRKFGMkVFYGDATRMDLLESAGAAKAEVLINAI-DDPQT 477

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1093455174 101 SLLTASaLVDMGVP--MIWAKADNQAHAKILGQIGVHHVIR 139
Cdd:PRK03562  478 SLQLVE-LVKEHFPhlQIIARARDVDHYIRLRQAGVEKPER 517
KhtT COG0490
K+/H+ antiporter KhtSTU, c-di-AMP-binding regulatory subunit KhtT, contains RCK_C (TrkA_C) ...
 128-231 8.49e-05

K+/H+ antiporter KhtSTU, c-di-AMP-binding regulatory subunit KhtT, contains RCK_C (TrkA_C) domain [Inorganic ion transport and metabolism, Signal transduction mechanisms];


Pssm-ID: 440256 [Multi-domain]  Cd Length: 140  Bit Score: 41.45  E-value: 8.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093455174 128 ILGQIGVHHVIRPEADTGRRIAHLIGGKVQDFLEFDRDYAVGKVAPPIHCLDKTVAEIN--QSAPITVVAVQKRGQRFRP 205
Cdd:COG0490    32 GLILRGLLLLELALLLLLLGELLRLLTRLLIELVLLLAIEEVKVPPGSPLVGKTLGELNlrQRTGVTVVAIRRGGEVILS 111

                          90       100
                  ....*....|....*....|....*.
gi 1093455174 206 ALADDRISAGDLLIVSGAIRQLETFA 231
Cdd:COG0490   112 PGPDTVLEAGDTLVVVGTREQLERLE 137
TrkA_C pfam02080
TrkA-C domain; This domain is often found next to the pfam02254 domain. The exact function of ...
 170-231 6.94e-04

TrkA-C domain; This domain is often found next to the pfam02254 domain. The exact function of this domain is unknown. It has been suggested that it may bind an unidentified ligand. The domain is predicted to adopt an all beta structure.


Pssm-ID: 460440 [Multi-domain]  Cd Length: 70  Bit Score: 37.20  E-value: 6.94e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1093455174 170 KVAPPIHCLDKTVAEIN--QSAPITVVAVqKRGQRFRPALADDRISAGDLLIVSGAIRQLETFA 231
Cdd:pfam02080   5 TVPENSPLVGKTLKELNlpERFGVRIVAI-RRGGRLIIPSGDTVLEAGDRLLVIGTPDDLAALR 67
PRK03659 PRK03659
glutathione-regulated potassium-efflux system protein KefB; Provisional
 25-93 8.34e-04

glutathione-regulated potassium-efflux system protein KefB; Provisional


Pssm-ID: 179625 [Multi-domain]  Cd Length: 601  Bit Score: 40.01  E-value: 8.34e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1093455174  25 VVILGMGRFGQALGEELVAGGIEVLCVDHREKVVQELSSTFDHVVTADTTMPEVLKQLGVDEAERVVIA 93
Cdd:PRK03659  403 VIIVGFGRFGQVIGRLLMANKMRITVLERDISAVNLMRKYGYKVYYGDATQLELLRAAGAEKAEAIVIT 471
SDR_a4 cd05266
atypical (a) SDRs, subgroup 4; Atypical SDRs in this subgroup are poorly defined, one member ...
 25-76 2.22e-03

atypical (a) SDRs, subgroup 4; Atypical SDRs in this subgroup are poorly defined, one member is identified as a putative NAD-dependent epimerase/dehydratase. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif that is related to, but is different from, the archetypical SDRs, GXGXXG. This subgroup also lacks most of the characteristic active site residues of the SDRs; however, the upstream Ser is present at the usual place, and some potential catalytic residues are present in place of the usual YXXXK active site motif. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, 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.


Pssm-ID: 187576 [Multi-domain]  Cd Length: 251  Bit Score: 38.07  E-value: 2.22e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1093455174  25 VVILGMGRFGQALGEELVAGGIEVLCVDHREKVVQELSSTFDHVVTADTTMP 76
Cdd:cd05266     1 VLILGCGYLGQRLARQLLAQGWQVTGTTRSPEKLAADRPAGVTPLAADLTQP 52
 
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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