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Conserved domains on  [gi|2320292123|ref|WP_263664328|]
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MULTISPECIES: TrkA family potassium uptake protein [unclassified Campylobacter]

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

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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 ...
 8-199 3.40e-40

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: 139.05  E-value: 3.40e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320292123   8 IIGLGRFGSVLAKELIDQGKRVIVSDIDEEAVKELQDHADFAYILDSTHTIALKEAGYANADVVILSIGeNLESSILTFM 87
Cdd:COG0569   100 IIGAGRVGRSLARELEEEGHDVVVIDKDPERVERLAEEDVLVIVGDATDEEVLEEAGIEDADAVIAATG-DDEANILACL 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320292123  88 ALKEIGVKNIIAKANSSTHGQILSKLGVNKVIYPEKESAKRLAKILITNPNFEIIDLSANTIKVAKLLVDEN--LAGKTL 165
Cdd:COG0569   179 LAKELGVPRIIARANDPEYADLLERLGADVVISPERLAARRIARLLLRPGVLDVLELADGDAEIVEVTVPEGspLVGKTL 258

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2320292123 166 QSIGQ----NLKVIAHKQHDTWsIMPNLETTAYLNDIL 199
Cdd:COG0569   259 KELDLreryGVTVVAIKRGGEV-IIPSGDTVLEAGDEL 295
 
Name Accession Description Interval E-value
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
 8-199 3.40e-40

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: 139.05  E-value: 3.40e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320292123   8 IIGLGRFGSVLAKELIDQGKRVIVSDIDEEAVKELQDHADFAYILDSTHTIALKEAGYANADVVILSIGeNLESSILTFM 87
Cdd:COG0569   100 IIGAGRVGRSLARELEEEGHDVVVIDKDPERVERLAEEDVLVIVGDATDEEVLEEAGIEDADAVIAATG-DDEANILACL 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320292123  88 ALKEIGVKNIIAKANSSTHGQILSKLGVNKVIYPEKESAKRLAKILITNPNFEIIDLSANTIKVAKLLVDEN--LAGKTL 165
Cdd:COG0569   179 LAKELGVPRIIARANDPEYADLLERLGADVVISPERLAARRIARLLLRPGVLDVLELADGDAEIVEVTVPEGspLVGKTL 258

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2320292123 166 QSIGQ----NLKVIAHKQHDTWsIMPNLETTAYLNDIL 199
Cdd:COG0569   259 KELDLreryGVTVVAIKRGGEV-IIPSGDTVLEAGDEL 295
TrkA_N pfam02254
TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include ...
 8-121 4.07e-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: 97.21  E-value: 4.07e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320292123   8 IIGLGRFGSVLAKELIdQGKRVIVSDIDEEAVKELQDHADFAYILDSTHTIALKEAGYANADVVILSIGENlESSILTFM 87
Cdd:pfam02254   3 IIGYGRVGRSLAEELS-EGGDVVVIDKDEERVEELREEGVPVVVGDATDEEVLEEAGIEEADAVIAATGDD-EANILIVL 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2320292123  88 ALKEI-GVKNIIAKANSSTHGQILSKLGVNKVIYP 121
Cdd:pfam02254  81 LARELnPDKKIIARANDPEHAELLRRLGADHVISP 115
trkA PRK09496
Trk system potassium transporter TrkA;
8-208 2.26e-13

Trk system potassium transporter TrkA;


Pssm-ID: 236541 [Multi-domain]  Cd Length: 453  Bit Score: 67.84  E-value: 2.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320292123   8 IIGLGRFGSVLAKELIDQGKRVIVSDIDEEAVKELQDHADFAYIL-DSTHTIALKEAGYANADVVIlSIGENLESSILTF 86
Cdd:PRK09496    5 IVGAGQVGYTLAENLSGENNDVTVIDTDEERLRRLQDRLDVRTVVgNGSSPDVLREAGAEDADLLI-AVTDSDETNMVAC 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320292123  87 MALKEI-GVKNIIAKANSS---THGQILSK--LGVNKVIYPEKESAKRLAKiLITNPN-FEIIDLSANTIKVAKLLVDEN 159
Cdd:PRK09496   84 QIAKSLfGAPTTIARVRNPeyaEYDKLFSKeaLGIDLLISPELLVAREIAR-LIEYPGaLDVEEFADGRVQLVEVKVYEG 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2320292123 160 --LAGKTLQSIGQ-----NLKVIAHKQHDTwSIMPNLETTAYLNDILMLLGTQEEL 208
Cdd:PRK09496  163 spLVGKPLSDLREhfpdiDVRVVAIFRGGR-LIIPRGDTVIEAGDEVYFIGAREHI 217
NAD_bind_Leu_Phe_Val_DH cd01075
NAD(P) binding domain of leucine dehydrogenase, phenylalanine dehydrogenase, and valine ...
 5-45 3.82e-05

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: 42.96  E-value: 3.82e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2320292123   5 TYGIIGLGRFGSVLAKELIDQGKRVIVSDIDEEAVKELQDH 45
Cdd:cd01075    30 TVAVQGLGKVGYKLAEHLLEEGAKLIVADINEEAVARAAEL 70
 
Name Accession Description Interval E-value
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
 8-199 3.40e-40

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: 139.05  E-value: 3.40e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320292123   8 IIGLGRFGSVLAKELIDQGKRVIVSDIDEEAVKELQDHADFAYILDSTHTIALKEAGYANADVVILSIGeNLESSILTFM 87
Cdd:COG0569   100 IIGAGRVGRSLARELEEEGHDVVVIDKDPERVERLAEEDVLVIVGDATDEEVLEEAGIEDADAVIAATG-DDEANILACL 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320292123  88 ALKEIGVKNIIAKANSSTHGQILSKLGVNKVIYPEKESAKRLAKILITNPNFEIIDLSANTIKVAKLLVDEN--LAGKTL 165
Cdd:COG0569   179 LAKELGVPRIIARANDPEYADLLERLGADVVISPERLAARRIARLLLRPGVLDVLELADGDAEIVEVTVPEGspLVGKTL 258

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2320292123 166 QSIGQ----NLKVIAHKQHDTWsIMPNLETTAYLNDIL 199
Cdd:COG0569   259 KELDLreryGVTVVAIKRGGEV-IIPSGDTVLEAGDEL 295
TrkA_N pfam02254
TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include ...
 8-121 4.07e-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: 97.21  E-value: 4.07e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320292123   8 IIGLGRFGSVLAKELIdQGKRVIVSDIDEEAVKELQDHADFAYILDSTHTIALKEAGYANADVVILSIGENlESSILTFM 87
Cdd:pfam02254   3 IIGYGRVGRSLAEELS-EGGDVVVIDKDEERVEELREEGVPVVVGDATDEEVLEEAGIEEADAVIAATGDD-EANILIVL 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2320292123  88 ALKEI-GVKNIIAKANSSTHGQILSKLGVNKVIYP 121
Cdd:pfam02254  81 LARELnPDKKIIARANDPEHAELLRRLGADHVISP 115
Kch COG1226
Voltage-gated potassium channel Kch [Inorganic ion transport and metabolism];
8-130 1.10e-15

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


Pssm-ID: 440839 [Multi-domain]  Cd Length: 279  Bit Score: 73.61  E-value: 1.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320292123   8 IIGLGRFGSVLAKELIDQGKRVIVSDIDEEAVKELQDhADFAYIL-DSTHTIALKEAGYANADVVILSIGeNLESSILTF 86
Cdd:COG1226   129 IAGFGRVGQIVARLLRAEGIPFVVIDLDPERVEELRR-FGIKVYYgDATRPDVLEAAGIERARALVVAID-DPEAALRIV 206

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2320292123  87 MALKEI--GVKnIIAKANSSTHGQILSKLGVNKVIYPEKESAKRLA 130
Cdd:COG1226   207 ELARELnpDLK-IIARARDREHAEELRQAGADEVVRETFESALQLA 251
trkA PRK09496
Trk system potassium transporter TrkA;
8-208 2.26e-13

Trk system potassium transporter TrkA;


Pssm-ID: 236541 [Multi-domain]  Cd Length: 453  Bit Score: 67.84  E-value: 2.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320292123   8 IIGLGRFGSVLAKELIDQGKRVIVSDIDEEAVKELQDHADFAYIL-DSTHTIALKEAGYANADVVIlSIGENLESSILTF 86
Cdd:PRK09496    5 IVGAGQVGYTLAENLSGENNDVTVIDTDEERLRRLQDRLDVRTVVgNGSSPDVLREAGAEDADLLI-AVTDSDETNMVAC 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320292123  87 MALKEI-GVKNIIAKANSS---THGQILSK--LGVNKVIYPEKESAKRLAKiLITNPN-FEIIDLSANTIKVAKLLVDEN 159
Cdd:PRK09496   84 QIAKSLfGAPTTIARVRNPeyaEYDKLFSKeaLGIDLLISPELLVAREIAR-LIEYPGaLDVEEFADGRVQLVEVKVYEG 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2320292123 160 --LAGKTLQSIGQ-----NLKVIAHKQHDTwSIMPNLETTAYLNDILMLLGTQEEL 208
Cdd:PRK09496  163 spLVGKPLSDLREhfpdiDVRVVAIFRGGR-LIIPRGDTVIEAGDEVYFIGAREHI 217
trkA PRK09496
Trk system potassium transporter TrkA;
8-121 1.12e-06

Trk system potassium transporter TrkA;


Pssm-ID: 236541 [Multi-domain]  Cd Length: 453  Bit Score: 48.19  E-value: 1.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320292123   8 IIGLGRFGSVLAKELIDQGKRVIVSDIDEEAVKELQDHADFAYIL--DSTHTIALKEAGYANADVVIlSIGENLESSILT 85
Cdd:PRK09496  236 IVGGGNIGYYLAKLLEKEGYSVKLIERDPERAEELAEELPNTLVLhgDGTDQELLEEEGIDEADAFI-ALTNDDEANILS 314

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2320292123  86 FMALKEIGVKNIIAKANSSTHGQILSKLGVNKVIYP 121
Cdd:PRK09496  315 SLLAKRLGAKKVIALVNRPAYVDLVEGLGIDIAISP 350
PRK09599 PRK09599
NADP-dependent phosphogluconate dehydrogenase;
7-45 7.03e-06

NADP-dependent phosphogluconate dehydrogenase;


Pssm-ID: 236582 [Multi-domain]  Cd Length: 301  Bit Score: 45.51  E-value: 7.03e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2320292123   7 GIIGLGRFGSVLAKELIDQGKRVIVSDIDEEAVKELQDH 45
Cdd:PRK09599    4 GMIGLGRMGGNMARRLLRGGHEVVGYDRNPEAVEALAEE 42
PRK03562 PRK03562
glutathione-regulated potassium-efflux system protein KefC; Provisional
 8-131 1.99e-05

glutathione-regulated potassium-efflux system protein KefC; Provisional


Pssm-ID: 235131 [Multi-domain]  Cd Length: 621  Bit Score: 44.60  E-value: 1.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320292123   8 IIGLGRFGSVLAKELIDQGKRVIVSDIDEEAVKELQDHADFAYILDSTHTIALKEAGYANADVVILSIGENLESSILTFM 87
Cdd:PRK03562  405 IAGFGRFGQIVGRLLLSSGVKMTVLDHDPDHIETLRKFGMKVFYGDATRMDLLESAGAAKAEVLINAIDDPQTSLQLVEL 484

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2320292123  88 ALKEIGVKNIIAKANSSTHGQILSKLGVNKVIYPEKESAKRLAK 131
Cdd:PRK03562  485 VKEHFPHLQIIARARDVDHYIRLRQAGVEKPERETFEGALKSGR 528
NAD_bind_Leu_Phe_Val_DH cd01075
NAD(P) binding domain of leucine dehydrogenase, phenylalanine dehydrogenase, and valine ...
 5-45 3.82e-05

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: 42.96  E-value: 3.82e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2320292123   5 TYGIIGLGRFGSVLAKELIDQGKRVIVSDIDEEAVKELQDH 45
Cdd:cd01075    30 TVAVQGLGKVGYKLAEHLLEEGAKLIVADINEEAVARAAEL 70
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 7-75 1.02e-04

Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; Pyrroline-5-carboxylate reductase is part of the Pathway/BioSystem: Proline biosynthesis


Pssm-ID: 440114 [Multi-domain]  Cd Length: 267  Bit Score: 41.97  E-value: 1.02e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2320292123   7 GIIGLGRFGSVLAKELIDQG---KRVIVSDIDEEAVKELQDHADFAYILDSTHTIalkeagyANADVVILSI 75
Cdd:COG0345     6 GFIGAGNMGSAIIKGLLKSGvppEDIIVSDRSPERLEALAERYGVRVTTDNAEAA-------AQADVVVLAV 70
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 5-76 1.10e-04

NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of 6-phosphogluconate dehydrogenase adopts a Rossmann fold.


Pssm-ID: 427298 [Multi-domain]  Cd Length: 159  Bit Score: 40.92  E-value: 1.10e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2320292123   5 TYGIIGLGRFGSVLAKELIDQGKRVIVSDIDEEAVKELQdhADFAYILDSthtiaLKEAgYANADVVILSIG 76
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELV--AAGAIAAAS-----PAEF-VAGLDVVITMVP 64
COG2085 COG2085
Predicted dinucleotide-binding enzyme [General function prediction only];
6-75 1.85e-04

Predicted dinucleotide-binding enzyme [General function prediction only];


Pssm-ID: 441688 [Multi-domain]  Cd Length: 205  Bit Score: 40.92  E-value: 1.85e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2320292123   6 YGIIGLGRFGSVLAKELIDQGKRVIVSDIDEEAVKELqdhadfAYILDSTHTIA-LKEAGyANADVVILSI 75
Cdd:COG2085     1 IGIIGTGNIGSALARRLAAAGHEVVIGSRDPEKAAAL------AAELGPGARAGtNAEAA-AAADVVVLAV 64
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 3-74 2.40e-04

3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism];


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 40.87  E-value: 2.40e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2320292123   3 KETYGIIGLGRFGSVLAKELIDQGKRVIVSDIDEEAVKELQDHAdfAYILDSthtiaLKEAGyANADVVILS 74
Cdd:COG2084     1 MMKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAG--ARVAAS-----PAEAA-AAADVVITM 64
PLN02256 PLN02256
arogenate dehydrogenase
 7-88 7.04e-04

arogenate dehydrogenase


Pssm-ID: 215144 [Multi-domain]  Cd Length: 304  Bit Score: 39.65  E-value: 7.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320292123   7 GIIGLGRFGSVLAKELIDQGKRVIV---SDIDEEA----VKELQDHADFAyildsthtialkeagYANADVVILSigenl 79
Cdd:PLN02256   40 GIVGFGNFGQFLAKTFVKQGHTVLAtsrSDYSDIAaelgVSFFRDPDDFC---------------EEHPDVVLLC----- 99


                  ....*....
gi 2320292123  80 eSSILTFMA 88
Cdd:PLN02256  100 -TSILSTEA 107
PRK10669 PRK10669
putative cation:proton antiport protein; Provisional
 8-137 9.61e-04

putative cation:proton antiport protein; Provisional


Pssm-ID: 182633 [Multi-domain]  Cd Length: 558  Bit Score: 39.70  E-value: 9.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320292123   8 IIGLGRFGSVLAKELIDQGKRVIVSDIDEEAVKELQDHADFAYILDSTHTIALKEAGYANADVVILSIGENLESSILTFM 87
Cdd:PRK10669  422 LVGYGRVGSLLGEKLLAAGIPLVVIETSRTRVDELRERGIRAVLGNAANEEIMQLAHLDCARWLLLTIPNGYEAGEIVAS 501

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2320292123  88 ALKEIGVKNIIAKANSSTHGQILSKLGVNKVIYPEKESAKRLAKILITNP 137
Cdd:PRK10669  502 AREKRPDIEIIARAHYDDEVAYITERGANQVVMGEREIARTMLELLETPP 551
WecC COG0677
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis];
7-73 1.04e-03

UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440441 [Multi-domain]  Cd Length: 413  Bit Score: 39.27  E-value: 1.04e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2320292123   7 GIIGLGRFGSVLAKELIDQGKRVIVSDIDEEAVKELQDHADfaYILDSTHTI---ALKEAGY---------ANADVVIL 73
Cdd:COG0677     3 AVIGLGYVGLPLAVAFAKAGFRVIGFDINPERVEELNAGED--PILEPGDELlaeAVAAGRLrattdpealAEADVVII 79
PRK08293 PRK08293
3-hydroxyacyl-CoA dehydrogenase;
1-105 1.34e-03

3-hydroxyacyl-CoA dehydrogenase;


Pssm-ID: 181359 [Multi-domain]  Cd Length: 287  Bit Score: 38.77  E-value: 1.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320292123   1 MKKETygIIGLGRFGSVLAKELIDQGKRVIVSDIDEEAVK-----------------ELQDHADFAYILDS-THTIALKE 62
Cdd:PRK08293    3 IKNVT--VAGAGVLGSQIAFQTAFHGFDVTIYDISDEALEkakeriakladryvrdlEATKEAPAEAALNRiTLTTDLAE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2320292123  63 AGyANADVVILSIGENLESSILTFMALKEIGVKNIIAKANSST 105
Cdd:PRK08293   81 AV-KDADLVIEAVPEDPEIKGDFYEELAKVAPEKTIFATNSST 122
garR PRK11559
tartronate semialdehyde reductase; Provisional
 7-72 1.96e-03

tartronate semialdehyde reductase; Provisional


Pssm-ID: 183197 [Multi-domain]  Cd Length: 296  Bit Score: 38.11  E-value: 1.96e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2320292123   7 GIIGLGRFGSVLAKELIDQGKRVIVSDIDEEAVKELQDHAdfayildSTHTIALKEAGyANADVVI 72
Cdd:PRK11559    6 GFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAG-------AETASTAKAVA-EQCDVII 63
PRK09186 PRK09186
flagellin modification protein A; Provisional
 10-45 2.10e-03

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 38.05  E-value: 2.10e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2320292123  10 GLGRFGSVLAKELIDQGKRVIVSDIDEEAVKELQDH 45
Cdd:PRK09186   12 AGGLIGSALVKAILEAGGIVIAADIDKEALNELLES 47
PRK05808 PRK05808
3-hydroxybutyryl-CoA dehydrogenase; Validated
 1-105 3.92e-03

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 180269 [Multi-domain]  Cd Length: 282  Bit Score: 37.25  E-value: 3.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320292123   1 MKKETYGIIGLGRFGSVLAKELIDQGKRVIVSDIDEEAV----------------KELQDHADFAYILDSTH-TIALKEA 63
Cdd:PRK05808    1 MGIQKIGVIGAGTMGNGIAQVCAVAGYDVVMVDISDAAVdrglatitksldrlvkKGKMTEADKEAALARITgTTDLDDL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2320292123  64 gyANADVVILSIGENLESSILTFMALKEIGVKNIIAKANSST 105
Cdd:PRK05808   81 --KDADLVIEAATENMDLKKKIFAQLDEIAKPEAILATNTSS 120
SDR_a4 cd05266
atypical (a) SDRs, subgroup 4; Atypical SDRs in this subgroup are poorly defined, one member ...
 7-75 6.00e-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: 36.53  E-value: 6.00e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2320292123   7 GIIGLGRFGSVLAKELIDQGKRVIVSDIDEEAVKELQDHADFAYILDSTHTIALkeagyANADVVILSI 75
Cdd:cd05266     2 LILGCGYLGQRLARQLLAQGWQVTGTTRSPEKLAADRPAGVTPLAADLTQPGLL-----ADVDHLVISL 65
MurD COG0771
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ...
 1-74 8.12e-03

UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramoylalanine-D-glutamate ligase is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440534 [Multi-domain]  Cd Length: 445  Bit Score: 36.60  E-value: 8.12e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2320292123   1 MKKETYGIIGLGRFGSVLAKELIDQGKRVIVSD---IDEEAVKELQDhADFAYILDSTHTIALkeagyANADVVILS 74
Cdd:COG0771     2 LKGKKVLVLGLGKSGLAAARLLAKLGAEVTVSDdrpAPELAAAELEA-PGVEVVLGEHPEELL-----DGADLVVKS 72
 
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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