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Conserved domains on  [gi|1221639851|ref|WP_089768754|]
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TrkA family potassium uptake protein [Halobellus clavatus]

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 super family cl35844
Trk system potassium transporter TrkA;
7-216 9.60e-36

Trk system potassium transporter TrkA;


The actual alignment was detected with superfamily member PRK09496:

Pssm-ID: 236541 [Multi-domain]  Cd Length: 453  Bit Score: 130.63  E-value: 9.60e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221639851   7 IIIAGGGRVGFQTAEILANRDHDVTIIERNERIVSEIADEWIATVIEGDATNPEIIEQAGIERADTIAALTGETGLNLAV 86
Cdd:PRK09496    3 IIIVGAGQVGYTLAENLSGENNDVTVIDTDEERLRRLQDRLDVRTVVGNGSSPDVLREAGAEDADLLIAVTDSDETNMVA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221639851  87 CLAASELDPGIRTIARIGRAAGTAYTRF-------VDAVLFPERAGARVAANEI---AGSDVQTLADvtGDLDIMLVRVA 156
Cdd:PRK09496   83 CQIAKSLFGAPTTIARVRNPEYAEYDKLfskealgIDLLISPELLVAREIARLIeypGALDVEEFAD--GRVQLVEVKVY 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1221639851 157 EGAPAAGKQLTEVRF---PAGTLVVSDDDGHR--VARPDTTLTPGNRYVVAVEPDVADEVMNLMR 216
Cdd:PRK09496  161 EGSPLVGKPLSDLREhfpDIDVRVVAIFRGGRliIPRGDTVIEAGDEVYFIGAREHIRAVMSEFG 225
 
Name Accession Description Interval E-value
trkA PRK09496
Trk system potassium transporter TrkA;
7-216 9.60e-36

Trk system potassium transporter TrkA;


Pssm-ID: 236541 [Multi-domain]  Cd Length: 453  Bit Score: 130.63  E-value: 9.60e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221639851   7 IIIAGGGRVGFQTAEILANRDHDVTIIERNERIVSEIADEWIATVIEGDATNPEIIEQAGIERADTIAALTGETGLNLAV 86
Cdd:PRK09496    3 IIIVGAGQVGYTLAENLSGENNDVTVIDTDEERLRRLQDRLDVRTVVGNGSSPDVLREAGAEDADLLIAVTDSDETNMVA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221639851  87 CLAASELDPGIRTIARIGRAAGTAYTRF-------VDAVLFPERAGARVAANEI---AGSDVQTLADvtGDLDIMLVRVA 156
Cdd:PRK09496   83 CQIAKSLFGAPTTIARVRNPEYAEYDKLfskealgIDLLISPELLVAREIARLIeypGALDVEEFAD--GRVQLVEVKVY 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1221639851 157 EGAPAAGKQLTEVRF---PAGTLVVSDDDGHR--VARPDTTLTPGNRYVVAVEPDVADEVMNLMR 216
Cdd:PRK09496  161 EGSPLVGKPLSDLREhfpDIDVRVVAIFRGGRliIPRGDTVIEAGDEVYFIGAREHIRAVMSEFG 225
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
 7-196 6.00e-34

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: 122.87  E-value: 6.00e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221639851   7 IIIAGGGRVGFQTAEILANRDHDVTIIERNERIVSEIADEwIATVIEGDATNPEIIEQAGIERADTIAALTGETGLNLAV 86
Cdd:COG0569    98 VIIIGAGRVGRSLARELEEEGHDVVVIDKDPERVERLAEE-DVLVIVGDATDEEVLEEAGIEDADAVIAATGDDEANILA 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221639851  87 CLAASELDPgIRTIARIGRAA-GTAYTRF-VDAVLFPERAGARVAANEIAGSDVQTLADV-TGDLDIMLVRVAEGAPAAG 163
Cdd:COG0569   177 CLLAKELGV-PRIIARANDPEyADLLERLgADVVISPERLAARRIARLLLRPGVLDVLELaDGDAEIVEVTVPEGSPLVG 255

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1221639851 164 KQLTEVRFPA--GTLVVS--DDDGHRVARPDTTLTPG 196
Cdd:COG0569   256 KTLKELDLREryGVTVVAikRGGEVIIPSGDTVLEAG 292
TrkA_N pfam02254
TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include ...
 7-103 8.94e-23

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: 88.74  E-value: 8.94e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221639851   7 IIIAGGGRVGFQTAEILAnRDHDVTIIERNERIVSEIADEWIaTVIEGDATNPEIIEQAGIERADTIAALTGETGLNLAV 86
Cdd:pfam02254   1 IIIIGYGRVGRSLAEELS-EGGDVVVIDKDEERVEELREEGV-PVVVGDATDEEVLEEAGIEEADAVIAATGDDEANILI 78

                          90
                  ....*....|....*..
gi 1221639851  87 CLAASELDPGIRTIARI 103
Cdd:pfam02254  79 VLLARELNPDKKIIARA 95
SDR_a5 cd05243
atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are ...
 7-65 1.54e-03

atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are identified as putative NAD(P)-dependent epimerases, one 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 very similar to the extended SDRs, GXXGXXG, and binds NADP. Generally, this subgroup has poor conservation of the active site tetrad; however, individual sequences do contain matches to the YXXXK active site motif, the upstream Ser, and there is a highly conserved Asp in place of the usual active site Asn throughout the subgroup. 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: 187554 [Multi-domain]  Cd Length: 203  Bit Score: 38.37  E-value: 1.54e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221639851   7 IIIAGG-GRVGFQTAEILANRDHDVTIIERNERIVSEIaDEWIATVIEGDATNPEIIEQA 65
Cdd:cd05243     2 VLVVGAtGKVGRHVVRELLDRGYQVRALVRDPSQAEKL-EAAGAEVVVGDLTDAESLAAA 60
 
Name Accession Description Interval E-value
trkA PRK09496
Trk system potassium transporter TrkA;
7-216 9.60e-36

Trk system potassium transporter TrkA;


Pssm-ID: 236541 [Multi-domain]  Cd Length: 453  Bit Score: 130.63  E-value: 9.60e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221639851   7 IIIAGGGRVGFQTAEILANRDHDVTIIERNERIVSEIADEWIATVIEGDATNPEIIEQAGIERADTIAALTGETGLNLAV 86
Cdd:PRK09496    3 IIIVGAGQVGYTLAENLSGENNDVTVIDTDEERLRRLQDRLDVRTVVGNGSSPDVLREAGAEDADLLIAVTDSDETNMVA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221639851  87 CLAASELDPGIRTIARIGRAAGTAYTRF-------VDAVLFPERAGARVAANEI---AGSDVQTLADvtGDLDIMLVRVA 156
Cdd:PRK09496   83 CQIAKSLFGAPTTIARVRNPEYAEYDKLfskealgIDLLISPELLVAREIARLIeypGALDVEEFAD--GRVQLVEVKVY 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1221639851 157 EGAPAAGKQLTEVRF---PAGTLVVSDDDGHR--VARPDTTLTPGNRYVVAVEPDVADEVMNLMR 216
Cdd:PRK09496  161 EGSPLVGKPLSDLREhfpDIDVRVVAIFRGGRliIPRGDTVIEAGDEVYFIGAREHIRAVMSEFG 225
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
 7-196 6.00e-34

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: 122.87  E-value: 6.00e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221639851   7 IIIAGGGRVGFQTAEILANRDHDVTIIERNERIVSEIADEwIATVIEGDATNPEIIEQAGIERADTIAALTGETGLNLAV 86
Cdd:COG0569    98 VIIIGAGRVGRSLARELEEEGHDVVVIDKDPERVERLAEE-DVLVIVGDATDEEVLEEAGIEDADAVIAATGDDEANILA 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221639851  87 CLAASELDPgIRTIARIGRAA-GTAYTRF-VDAVLFPERAGARVAANEIAGSDVQTLADV-TGDLDIMLVRVAEGAPAAG 163
Cdd:COG0569   177 CLLAKELGV-PRIIARANDPEyADLLERLgADVVISPERLAARRIARLLLRPGVLDVLELaDGDAEIVEVTVPEGSPLVG 255

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1221639851 164 KQLTEVRFPA--GTLVVS--DDDGHRVARPDTTLTPG 196
Cdd:COG0569   256 KTLKELDLREryGVTVVAikRGGEVIIPSGDTVLEAG 292
trkA PRK09496
Trk system potassium transporter TrkA;
7-211 4.82e-27

Trk system potassium transporter TrkA;


Pssm-ID: 236541 [Multi-domain]  Cd Length: 453  Bit Score: 106.75  E-value: 4.82e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221639851   7 IIIAGGGRVGFQTAEILANRDHDVTIIERNERIVSEIADEWI-ATVIEGDATNPEIIEQAGIERADTIAALTGETGLNLA 85
Cdd:PRK09496  234 VMIVGGGNIGYYLAKLLEKEGYSVKLIERDPERAEELAEELPnTLVLHGDGTDQELLEEEGIDEADAFIALTNDDEANIL 313

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221639851  86 VCLAASELdpGI-RTIARIGRaagTAYTRFV-----DAVLFPeragARVAANEI----AGSDVQTLADVT-GDLDIMLVR 154
Cdd:PRK09496  314 SSLLAKRL--GAkKVIALVNR---PAYVDLVeglgiDIAISP----RQATASEIlrhvRRGDIVAVHSLRrGAAEAIEAV 384

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1221639851 155 VAEGAPAAGKQLTEVRFPAGTLV--VSDDDGHRVARPDTTLTPGNRYVVAVEPDVADEV 211
Cdd:PRK09496  385 AHETSKVVGKPLKDLKLPKGVLIgaIVRGGEVIIPTGDTVIEPGDHVIVFVLDKKFVPD 443
TrkA_N pfam02254
TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include ...
 7-103 8.94e-23

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: 88.74  E-value: 8.94e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221639851   7 IIIAGGGRVGFQTAEILAnRDHDVTIIERNERIVSEIADEWIaTVIEGDATNPEIIEQAGIERADTIAALTGETGLNLAV 86
Cdd:pfam02254   1 IIIIGYGRVGRSLAEELS-EGGDVVVIDKDEERVEELREEGV-PVVVGDATDEEVLEEAGIEEADAVIAATGDDEANILI 78

                          90
                  ....*....|....*..
gi 1221639851  87 CLAASELDPGIRTIARI 103
Cdd:pfam02254  79 VLLARELNPDKKIIARA 95
Kch COG1226
Voltage-gated potassium channel Kch [Inorganic ion transport and metabolism];
7-102 2.97e-11

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


Pssm-ID: 440839 [Multi-domain]  Cd Length: 279  Bit Score: 61.28  E-value: 2.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221639851   7 IIIAGGGRVGFQTAEILANRDHDVTIIERNERIVSEIADEWIAtVIEGDATNPEIIEQAGIERADTIAALTGETGLNLAV 86
Cdd:COG1226   127 VIIAGFGRVGQIVARLLRAEGIPFVVIDLDPERVEELRRFGIK-VYYGDATRPDVLEAAGIERARALVVAIDDPEAALRI 205

                          90
                  ....*....|....*.
gi 1221639851  87 CLAASELDPGIRTIAR 102
Cdd:COG1226   206 VELARELNPDLKIIAR 221
PRK10537 PRK10537
voltage-gated potassium channel protein;
7-101 4.02e-08

voltage-gated potassium channel protein;


Pssm-ID: 236711 [Multi-domain]  Cd Length: 393  Bit Score: 52.72  E-value: 4.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221639851   7 IIIAGGGRVGFQTAEILANRDHDVTIIernerIVSEIADEWIAT--VIEGDATNPEIIEQAGIERADTIAALTGETGLNL 84
Cdd:PRK10537  243 FIICGHSPLAINTYLGLRQRGQAVTVI-----VPLGLEHRLPDDadLIPGDSSDSAVLKKAGAARARAILALRDNDADNA 317

                          90
                  ....*....|....*..
gi 1221639851  85 AVCLAASELDPGIRTIA 101
Cdd:PRK10537  318 FVVLAAKEMSSDVKTVA 334
TrkA_C pfam02080
TrkA-C domain; This domain is often found next to the pfam02254 domain. The exact function of ...
 150-215 7.50e-07

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: 45.29  E-value: 7.50e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221639851 150 IMLVRVAEGAPAAGKQLTEVRFPAGT----LVVSDDDGHRVARPDTTLTPGNRYVVAVEPDVADEVMNLM 215
Cdd:pfam02080   1 LVEVTVPENSPLVGKTLKELNLPERFgvriVAIRRGGRLIIPSGDTVLEAGDRLLVIGTPDDLAALRELL 70
YwnB COG2910
Putative NADH-flavin reductase [General function prediction only];
7-115 5.72e-05

Putative NADH-flavin reductase [General function prediction only];


Pssm-ID: 442154 [Multi-domain]  Cd Length: 205  Bit Score: 42.54  E-value: 5.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221639851   7 IIIAGGGRVGFQTAEILANRDHDVTIIERNERIVSEIADEwiATVIEGDATNPEIIEQAgIERADT-IAALTGETGLNLA 85
Cdd:COG2910     3 AVIGATGRVGSLIVREALARGHEVTALVRNPEKLPDEHPG--LTVVVGDVLDPAAVAEA-LAGADAvVSALGAGGGNPTT 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 1221639851  86 VCLAaseldpGIRTIARIGRAAGTayTRFV 115
Cdd:COG2910    80 VLSD------GARALIDAMKAAGV--KRLI 101
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
7-115 7.08e-05

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 42.66  E-value: 7.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221639851   7 IIIAGG-GRVGFQTAEILANRDHDVTIIERNERIVSEIADEWIATVIEGDATNPEIIEQAgIERADTIaaltgetgLNLA 85
Cdd:COG0451     2 ILVTGGaGFIGSHLARRLLARGHEVVGLDRSPPGAANLAALPGVEFVRGDLRDPEALAAA-LAGVDAV--------VHLA 72

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1221639851  86 VCLAASELDP---------GIRTIARIGRAAGTAytRFV 115
Cdd:COG0451    73 APAGVGEEDPdetlevnveGTLNLLEAARAAGVK--RFV 109
NAD_binding_10 pfam13460
NAD(P)H-binding;
13-137 1.27e-04

NAD(P)H-binding;


Pssm-ID: 463885 [Multi-domain]  Cd Length: 183  Bit Score: 41.05  E-value: 1.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221639851  13 GRVGFQTAEILANRDHDVTIIERNERIVSEIADEWIATVIEGDATNPEIIEQAgIERADT-IAALTGETGLNLAV--CLA 89
Cdd:pfam13460   4 GKIGRLLVKQLLARGHEVTALVRNPEKLADLEDHPGVEVVDGDVLDPDDLAEA-LAGQDAvISALGGGGTDETGAknIID 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1221639851  90 ASELDpGIRTI-----ARIGRAAGTAYTRFVDAVLFPERAGARVAANEIAGSD 137
Cdd:pfam13460  83 AAKAA-GVKRFvlvssLGVGDEVPGPFGPWNKEMLGPYLAAKRAAEELLRASG 134
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
 6-64 2.23e-04

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 41.56  E-value: 2.23e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1221639851   6 DIIIAGGGRVGFQTAEILANRDHDVTIIERNERIVSEIADEWIATVIEGdatnpEIIEQ 64
Cdd:PRK09564  151 NIVIIGAGFIGLEAVEAAKHLGKNVRIIQLEDRILPDSFDKEITDVMEE-----ELREN 204
SDR_a5 cd05243
atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are ...
 7-65 1.54e-03

atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are identified as putative NAD(P)-dependent epimerases, one 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 very similar to the extended SDRs, GXXGXXG, and binds NADP. Generally, this subgroup has poor conservation of the active site tetrad; however, individual sequences do contain matches to the YXXXK active site motif, the upstream Ser, and there is a highly conserved Asp in place of the usual active site Asn throughout the subgroup. 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: 187554 [Multi-domain]  Cd Length: 203  Bit Score: 38.37  E-value: 1.54e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221639851   7 IIIAGG-GRVGFQTAEILANRDHDVTIIERNERIVSEIaDEWIATVIEGDATNPEIIEQA 65
Cdd:cd05243     2 VLVVGAtGKVGRHVVRELLDRGYQVRALVRDPSQAEKL-EAAGAEVVVGDLTDAESLAAA 60
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 3-82 1.87e-03

NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism];


Pssm-ID: 440215 [Multi-domain]  Cd Length: 322  Bit Score: 38.25  E-value: 1.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221639851   3 NGLDIIIAGGGRVGFQTAEILANRDHDVTIIERNERIVSeIADEWIATVIEgdatnpEIIEQAGIE--RADTIAALTGET 80
Cdd:COG0446   123 KGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRLLG-VLDPEMAALLE------EELREHGVElrLGETVVAIDGDD 195


                  ..
gi 1221639851  81 GL 82
Cdd:COG0446   196 KV 197
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 7-68 3.20e-03

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 425450 [Multi-domain]  Cd Length: 80  Bit Score: 35.26  E-value: 3.20e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1221639851   7 IIIAGGGRVGFQTAEILANRDHDVTIIERNERIVSeIADEWIATVIEgdatnpEIIEQAGIE 68
Cdd:pfam00070   2 VVVVGGGYIGLELAGALARLGSKVTVVERRDRLLP-GFDPEIAKILQ------EKLEKNGIE 56
 
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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