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Conserved domains on  [gi|491319715|ref|WP_005177682|]
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MULTISPECIES: TrkA family potassium uptake protein [Acinetobacter]

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

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 ...
3-200 3.52e-41

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: 141.36  E-value: 3.52e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491319715   3 QFAVIGLGSFGATVATQLVSLKHDVIGIDINKKYVENIAEEITHAVIADATDEHVLQELNIQNCDAVVVAIGEDiEASIL 82
Cdd:COG0569   97 HVIIIGAGRVGRSLARELEEEGHDVVVIDKDPERVERLAEEDVLVIVGDATDEEVLEEAGIEDADAVIAATGDD-EANIL 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491319715  83 CVLHLKNMGLEKIYVKAKSKAHHMILTHLQVSKIIHPEEDMGVRIAQSLSYPMVSRYMALEDDHF-IVKVEVTE--ALNG 159
Cdd:COG0569  176 ACLLAKELGVPRIIARANDPEYADLLERLGADVVISPERLAARRIARLLLRPGVLDVLELADGDAeIVEVTVPEgsPLVG 255
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 491319715 160 TRYHEFIGHAP-EVKTLLHKRGSEIqFSLDPQLIMQQGDILV 200
Cdd:COG0569  256 KTLKELDLRERyGVTVVAIKRGGEV-IIPSGDTVLEAGDELI 296
 
Name Accession Description Interval E-value
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
3-200 3.52e-41

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: 141.36  E-value: 3.52e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491319715   3 QFAVIGLGSFGATVATQLVSLKHDVIGIDINKKYVENIAEEITHAVIADATDEHVLQELNIQNCDAVVVAIGEDiEASIL 82
Cdd:COG0569   97 HVIIIGAGRVGRSLARELEEEGHDVVVIDKDPERVERLAEEDVLVIVGDATDEEVLEEAGIEDADAVIAATGDD-EANIL 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491319715  83 CVLHLKNMGLEKIYVKAKSKAHHMILTHLQVSKIIHPEEDMGVRIAQSLSYPMVSRYMALEDDHF-IVKVEVTE--ALNG 159
Cdd:COG0569  176 ACLLAKELGVPRIIARANDPEYADLLERLGADVVISPERLAARRIARLLLRPGVLDVLELADGDAeIVEVTVPEgsPLVG 255
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 491319715 160 TRYHEFIGHAP-EVKTLLHKRGSEIqFSLDPQLIMQQGDILV 200
Cdd:COG0569  256 KTLKELDLRERyGVTVVAIKRGGEV-IIPSGDTVLEAGDELI 296
TrkA_N pfam02254
TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include ...
4-119 1.68e-28

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: 103.37  E-value: 1.68e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491319715    4 FAVIGLGSFGATVATQLVSlKHDVIGIDINKKYVENIAEEITHAVIADATDEHVLQELNIQNCDAVVVAIGEDiEASILC 83
Cdd:pfam02254   1 IIIIGYGRVGRSLAEELSE-GGDVVVIDKDEERVEELREEGVPVVVGDATDEEVLEEAGIEEADAVIAATGDD-EANILI 78
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 491319715   84 VLHLKNM-GLEKIYVKAKSKAHHMILTHLQVSKIIHP 119
Cdd:pfam02254  79 VLLARELnPDKKIIARANDPEHAELLRRLGADHVISP 115
trkA PRK09496
Trk system potassium transporter TrkA;
6-119 2.75e-08

Trk system potassium transporter TrkA;


Pssm-ID: 236541 [Multi-domain]  Cd Length: 453  Bit Score: 53.20  E-value: 2.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491319715   6 VIGLGSFGATVATQLVSLKHDVIGIDINKKYVENIAEEITHAVI--ADATDEHVLQELNIQNCDaVVVAIGEDIEASILC 83
Cdd:PRK09496 236 IVGGGNIGYYLAKLLEKEGYSVKLIERDPERAEELAEELPNTLVlhGDGTDQELLEEEGIDEAD-AFIALTNDDEANILS 314
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 491319715  84 VLHLKNMGLEKIYVKAKSKAHHMILTHLQVSKIIHP 119
Cdd:PRK09496 315 SLLAKRLGAKKVIALVNRPAYVDLVEGLGIDIAISP 350
NDP-sugDHase TIGR03026
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ...
5-74 3.34e-05

nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent alcohol-to-acid oxidation of nucleotide-linked sugars. Examples include UDP-glucose 6-dehydrogenase (1.1.1.22), GDP-mannose 6-dehydrogenase (1.1.1.132), UDP-N-acetylglucosamine 6-dehydrogenase (1.1.1.136), UDP-N-acetyl-D-galactosaminuronic acid dehydrogenase, and UDP-N-acetyl-D-mannosaminuronic acid dehydrogenase. These enzymes are most often involved in the biosynthesis of polysaccharides and are often found in operons devoted to that purpose. All of these enzymes contain three Pfam domains, pfam03721, pfam00984, and pfam03720 for the N-terminal, central, and C-terminal regions respectively.


Pssm-ID: 274399 [Multi-domain]  Cd Length: 409  Bit Score: 43.75  E-value: 3.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491319715    5 AVIGLGSFGATVATQLVSLKHDVIGIDINKKYVEN-------IAEEITHAVIADATDEHVL-----QELNIQNCDAVVVA 72
Cdd:TIGR03026   4 AVIGLGYVGLPLAALLADLGHDVTGVDIDQEKVDKlnkgkspIYEPGLDELLAKALKAGRLrattdYEEAIRDADVIIIC 83

                  ..
gi 491319715   73 IG 74
Cdd:TIGR03026  84 VP 85
LDH-like_MDH cd01339
L-lactate dehydrogenase-like malate dehydrogenase proteins; Members of this subfamily have an ...
5-74 3.68e-03

L-lactate dehydrogenase-like malate dehydrogenase proteins; Members of this subfamily have an LDH-like structure and an MDH enzymatic activity. Some members, like MJ0490 from Methanococcus jannaschii, exhibit both MDH and LDH activities. Tetrameric MDHs, including those from phototrophic bacteria, are more similar to LDHs than to other MDHs. LDH catalyzes the last step of glycolysis in which pyruvate is converted to L-lactate. MDH is one of the key enzymes in the citric acid cycle, facilitating both the conversion of malate to oxaloacetate and replenishing levels of oxalacetate by reductive carboxylation of pyruvate. The LDH-like MDHs are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others.


Pssm-ID: 133424 [Multi-domain]  Cd Length: 300  Bit Score: 37.45  E-value: 3.68e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491319715   5 AVIGLGSFGATVAtQLVSLKH--DVIGIDINKKYVENIAEEITHAVIADATDEHVLQELN---IQNCDAVVVAIG 74
Cdd:cd01339    2 SIIGAGNVGATLA-QLLALKElgDVVLLDIVEGLPQGKALDISQAAPILGSDTKVTGTNDyedIAGSDVVVITAG 75
 
Name Accession Description Interval E-value
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
3-200 3.52e-41

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: 141.36  E-value: 3.52e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491319715   3 QFAVIGLGSFGATVATQLVSLKHDVIGIDINKKYVENIAEEITHAVIADATDEHVLQELNIQNCDAVVVAIGEDiEASIL 82
Cdd:COG0569   97 HVIIIGAGRVGRSLARELEEEGHDVVVIDKDPERVERLAEEDVLVIVGDATDEEVLEEAGIEDADAVIAATGDD-EANIL 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491319715  83 CVLHLKNMGLEKIYVKAKSKAHHMILTHLQVSKIIHPEEDMGVRIAQSLSYPMVSRYMALEDDHF-IVKVEVTE--ALNG 159
Cdd:COG0569  176 ACLLAKELGVPRIIARANDPEYADLLERLGADVVISPERLAARRIARLLLRPGVLDVLELADGDAeIVEVTVPEgsPLVG 255
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 491319715 160 TRYHEFIGHAP-EVKTLLHKRGSEIqFSLDPQLIMQQGDILV 200
Cdd:COG0569  256 KTLKELDLRERyGVTVVAIKRGGEV-IIPSGDTVLEAGDELI 296
TrkA_N pfam02254
TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include ...
4-119 1.68e-28

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: 103.37  E-value: 1.68e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491319715    4 FAVIGLGSFGATVATQLVSlKHDVIGIDINKKYVENIAEEITHAVIADATDEHVLQELNIQNCDAVVVAIGEDiEASILC 83
Cdd:pfam02254   1 IIIIGYGRVGRSLAEELSE-GGDVVVIDKDEERVEELREEGVPVVVGDATDEEVLEEAGIEEADAVIAATGDD-EANILI 78
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 491319715   84 VLHLKNM-GLEKIYVKAKSKAHHMILTHLQVSKIIHP 119
Cdd:pfam02254  79 VLLARELnPDKKIIARANDPEHAELLRRLGADHVISP 115
Kch COG1226
Voltage-gated potassium channel Kch [Inorganic ion transport and metabolism];
6-131 4.35e-11

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


Pssm-ID: 440839 [Multi-domain]  Cd Length: 279  Bit Score: 60.90  E-value: 4.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491319715   6 VIGLGSFGATVATQLVSLKHDVIGIDINKKYVENIAEEITHAVIADATDEHVLQELNIQNCDAVVVAIGeDIEASILCVL 85
Cdd:COG1226  129 IAGFGRVGQIVARLLRAEGIPFVVIDLDPERVEELRRFGIKVYYGDATRPDVLEAAGIERARALVVAID-DPEAALRIVE 207
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 491319715  86 HLKNM--GLeKIYVKAKSKAHHMILTHLQVSKIIHPEEDMGVRIAQSL 131
Cdd:COG1226  208 LARELnpDL-KIIARARDREHAEELRQAGADEVVRETFESALQLARHA 254
trkA PRK09496
Trk system potassium transporter TrkA;
6-119 2.75e-08

Trk system potassium transporter TrkA;


Pssm-ID: 236541 [Multi-domain]  Cd Length: 453  Bit Score: 53.20  E-value: 2.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491319715   6 VIGLGSFGATVATQLVSLKHDVIGIDINKKYVENIAEEITHAVI--ADATDEHVLQELNIQNCDaVVVAIGEDIEASILC 83
Cdd:PRK09496 236 IVGGGNIGYYLAKLLEKEGYSVKLIERDPERAEELAEELPNTLVlhGDGTDQELLEEEGIDEAD-AFIALTNDDEANILS 314
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 491319715  84 VLHLKNMGLEKIYVKAKSKAHHMILTHLQVSKIIHP 119
Cdd:PRK09496 315 SLLAKRLGAKKVIALVNRPAYVDLVEGLGIDIAISP 350
trkA PRK09496
Trk system potassium transporter TrkA;
6-216 2.67e-07

Trk system potassium transporter TrkA;


Pssm-ID: 236541 [Multi-domain]  Cd Length: 453  Bit Score: 50.12  E-value: 2.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491319715   6 VIGLGSFGATVATQLVSLKHDVIGIDINKKYVENIAEEI-THAVIADATDEHVLQELNIQNCDAVVVAIGEDiEASIL-C 83
Cdd:PRK09496   5 IVGAGQVGYTLAENLSGENNDVTVIDTDEERLRRLQDRLdVRTVVGNGSSPDVLREAGAEDADLLIAVTDSD-ETNMVaC 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491319715  84 VL-HLKNMGLEKI-YVKAKSKAHHMIL---THLQVSKIIHPEEDMGVRIAQSLSYPmvsryMALEDDHF------IVKVE 152
Cdd:PRK09496  84 QIaKSLFGAPTTIaRVRNPEYAEYDKLfskEALGIDLLISPELLVAREIARLIEYP-----GALDVEEFadgrvqLVEVK 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491319715 153 VTEA--LNGTRYHEFIGHAPEVKTLLH--KRGSEIqFSLDPQLIMQQGDILVLEGQVEQLKRLSKHFK 216
Cdd:PRK09496 159 VYEGspLVGKPLSDLREHFPDIDVRVVaiFRGGRL-IIPRGDTVIEAGDEVYFIGAREHIRAVMSEFG 225
WecC COG0677
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis];
5-72 3.90e-06

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


Pssm-ID: 440441 [Multi-domain]  Cd Length: 413  Bit Score: 46.59  E-value: 3.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491319715   5 AVIGLGSFGATVATQLVSLKHDVIGIDINKKYVENIAEEITHavIADATDEHVLQELN------------IQNCDAVVVA 72
Cdd:COG0677    3 AVIGLGYVGLPLAVAFAKAGFRVIGFDINPERVEELNAGEDP--ILEPGDELLAEAVAagrlrattdpeaLAEADVVIIA 80
NDP-sugDHase TIGR03026
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ...
5-74 3.34e-05

nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent alcohol-to-acid oxidation of nucleotide-linked sugars. Examples include UDP-glucose 6-dehydrogenase (1.1.1.22), GDP-mannose 6-dehydrogenase (1.1.1.132), UDP-N-acetylglucosamine 6-dehydrogenase (1.1.1.136), UDP-N-acetyl-D-galactosaminuronic acid dehydrogenase, and UDP-N-acetyl-D-mannosaminuronic acid dehydrogenase. These enzymes are most often involved in the biosynthesis of polysaccharides and are often found in operons devoted to that purpose. All of these enzymes contain three Pfam domains, pfam03721, pfam00984, and pfam03720 for the N-terminal, central, and C-terminal regions respectively.


Pssm-ID: 274399 [Multi-domain]  Cd Length: 409  Bit Score: 43.75  E-value: 3.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491319715    5 AVIGLGSFGATVATQLVSLKHDVIGIDINKKYVEN-------IAEEITHAVIADATDEHVL-----QELNIQNCDAVVVA 72
Cdd:TIGR03026   4 AVIGLGYVGLPLAALLADLGHDVTGVDIDQEKVDKlnkgkspIYEPGLDELLAKALKAGRLrattdYEEAIRDADVIIIC 83

                  ..
gi 491319715   73 IG 74
Cdd:TIGR03026  84 VP 85
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
8-70 2.10e-04

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 41.12  E-value: 2.10e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491319715   8 GLGSFGATVATQLVSLKHDVIGIDINKKYVENIAEEIT-HAVIADATDEHVLQELnIQNCDAVV 70
Cdd:COG0451    7 GAGFIGSHLARRLLARGHEVVGLDRSPPGAANLAALPGvEFVRGDLRDPEALAAA-LAGVDAVV 69
UDPG_MGDP_dh_N pfam03721
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose ...
5-74 7.52e-04

UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose dehydrogenaseses are a small group of enzymes which possesses the ability to catalyze the NAD-dependent 2-fold oxidation of an alcohol to an acid without the release of an aldehyde intermediate.


Pssm-ID: 397677 [Multi-domain]  Cd Length: 186  Bit Score: 39.15  E-value: 7.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491319715    5 AVIGLGSFGATVATQLVSLKHDVIGIDINKKYVENIAE---EITHAVIADATDEHVLQELN--------IQNCDAVVVAI 73
Cdd:pfam03721   4 SVIGLGYVGLPTAACLAEIGHDVIGVDIDEEKVDKLNSgqiPIYEPGLDELVKANVSGRLSfttdystaIEEADVIFIAV 83

                  .
gi 491319715   74 G 74
Cdd:pfam03721  84 G 84
PRK09599 PRK09599
NADP-dependent phosphogluconate dehydrogenase;
3-48 3.00e-03

NADP-dependent phosphogluconate dehydrogenase;


Pssm-ID: 236582 [Multi-domain]  Cd Length: 301  Bit Score: 37.81  E-value: 3.00e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 491319715   3 QFAVIGLGSFGATVATQLVSLKHDVIGIDINKKYVENIAEEITHAV 48
Cdd:PRK09599   2 QLGMIGLGRMGGNMARRLLRGGHEVVGYDRNPEAVEALAEEGATGA 47
LDH-like_MDH cd01339
L-lactate dehydrogenase-like malate dehydrogenase proteins; Members of this subfamily have an ...
5-74 3.68e-03

L-lactate dehydrogenase-like malate dehydrogenase proteins; Members of this subfamily have an LDH-like structure and an MDH enzymatic activity. Some members, like MJ0490 from Methanococcus jannaschii, exhibit both MDH and LDH activities. Tetrameric MDHs, including those from phototrophic bacteria, are more similar to LDHs than to other MDHs. LDH catalyzes the last step of glycolysis in which pyruvate is converted to L-lactate. MDH is one of the key enzymes in the citric acid cycle, facilitating both the conversion of malate to oxaloacetate and replenishing levels of oxalacetate by reductive carboxylation of pyruvate. The LDH-like MDHs are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others.


Pssm-ID: 133424 [Multi-domain]  Cd Length: 300  Bit Score: 37.45  E-value: 3.68e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491319715   5 AVIGLGSFGATVAtQLVSLKH--DVIGIDINKKYVENIAEEITHAVIADATDEHVLQELN---IQNCDAVVVAIG 74
Cdd:cd01339    2 SIIGAGNVGATLA-QLLALKElgDVVLLDIVEGLPQGKALDISQAAPILGSDTKVTGTNDyedIAGSDVVVITAG 75
wecC PRK11064
UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional
5-40 6.66e-03

UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional


Pssm-ID: 182940 [Multi-domain]  Cd Length: 415  Bit Score: 36.88  E-value: 6.66e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 491319715   5 AVIGLGSFGATVATQLVSLKHDVIGIDINKKYVENI 40
Cdd:PRK11064   7 SVIGLGYIGLPTAAAFASRQKQVIGVDINQHAVDTI 42
 
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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