NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1034557855|ref|XP_016856555|]
View 

sodium/hydrogen exchanger 11 isoform X1 [Homo sapiens]

Protein Classification

cyclic nucleotide-gated ion channel( domain architecture ID 13055902)

cyclic nucleotide-gated ion channel is a nonselective channel that is opened by the direct binding of cyclic nucleotides, cAMP and cGMP

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Na_H_Exchanger super family cl01133
Sodium/hydrogen exchanger family; Na/H antiporters are key transporters in maintaining the pH ...
 98-380 6.75e-15

Sodium/hydrogen exchanger family; Na/H antiporters are key transporters in maintaining the pH of actively metabolising cells. The molecular mechanisms of antiport are unclear. These antiporters contain 10-12 transmembrane regions (M) at the amino-terminus and a large cytoplasmic region at the carboxyl terminus. The transmembrane regions M3-M12 share identity with other members of the family. The M6 and M7 regions are highly conserved. Thus, this is thought to be the region that is involved in the transport of sodium and hydrogen ions. The cytoplasmic region has little similarity throughout the family.


The actual alignment was detected with superfamily member pfam00999:

Pssm-ID: 470090 [Multi-domain]  Cd Length: 377  Bit Score: 77.68  E-value: 6.75e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557855   98 PLIIFMVALDVEFYTLKKMFWQVLLTGLISFSTASIIIGYVViKFNKDSWDLQSCLLFSITLGIIDPLRSVNSLKTIGI- 176
Cdd:pfam00999   57 PPLLFLAGLELDLRELRKNGGSILLLALLGVLIPFVLIGLLL-YLLGLGIPLLEALLFGAILSATSPVVVLAILKELGRv 135

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557855  177 -SKIYIdLIRGESLI--ICSI--ASIFFGNFRGNRIHFSIFRdlhVGIELSYDILGSIIFGYWCAKIIQCILADVFSNML 251
Cdd:pfam00999  136 pERLGT-LLLGESVLndGVAVvlLAVLLALAQGVGGGSDLGW---LLLIFLVVAVGGLLLGLLIGWLLRLITRFTDDDRE 211

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557855  252 TNIILCFSMVYMTFYIVEFLGMSGTLALAAVGLNLDSLTFKPKIElviTKFLRIFSSVYEHLIYAFFGIVIGCGELshyE 331
Cdd:pfam00999  212 LEVLLVLLLALLAALLAEALGVSGILGAFLAGLVLSEYPFANKLS---EKLEPFGYGLFNPLFFVLVGLSLDLSSL---L 285

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1034557855  332 FHTIPFIFILFTTVNLVRLLTILLVSPILmhsnyEYNWRWGVVITWSGI 380
Cdd:pfam00999  286 LSVWILVLLALVAILLGRFLGVFLLLRLL-----GLSLREALIIGFGGL 329
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 873-980 4.33e-11

effector domain of the CAP family of transcription factors; members include CAP (or cAMP receptor protein (CRP)), which binds cAMP, FNR (fumarate and nitrate reduction), which uses an iron-sulfur cluster to sense oxygen) and CooA, a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. Cyclic nucleotide-binding domain similar to CAP are also present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) and vertebrate cyclic nucleotide-gated ion-channels. Cyclic nucleotide-monophosphate binding domain; proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues; the best studied is the prokaryotic catabolite gene activator, CAP, where such a domain is known to be composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure; three conserved glycine residues are thought to be essential for maintenance of the structural integrity of the beta-barrel; CooA is a homodimeric transcription factor that belongs to CAP family; cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclic nucleotide-binding domain; cAPK's are composed of two different subunits, a catalytic chain and a regulatory chain, which contains both copies of the domain; cGPK's are single chain enzymes that include the two copies of the domain in their N-terminal section; also found in vertebrate cyclic nucleotide-gated ion-channels


:

Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 61.19  E-value: 4.33e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557855  873 DVLIDFFKERAKLACFDSGDTICKGGEMPQGIYLIISGMAILHSLsptfgiesnqrcDRGSRDMFTEFCTTGDIIGELSC 952
Cdd:cd00038      7 DEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKL------------DEDGREQIVGFLGPGDLFGELAL 74

                           90       100
                   ....*....|....*....|....*...
gi 1034557855  953 LLKREIEYTVICETSLQACFISLEDLYE 980
Cdd:cd00038     75 LGNGPRSATVRALTDSELLVLPRSDFRR 102
Ion_trans super family cl37996
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 609-731 1.56e-05

Ion transport protein; This family contains sodium, potassium and calcium ion channels. This family is 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times, whereas in others (e.g. K channels) the protein forms as a tetramer in the membrane.


The actual alignment was detected with superfamily member pfam00520:

Pssm-ID: 459842 [Multi-domain]  Cd Length: 238  Bit Score: 47.65  E-value: 1.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557855  609 FEYTGQIINLIYIYPMIIHLWPMARGLNVSALISINYYFMFLYVLESTLKIII--LKRKYFQQCWNTLEFFILVIGIIDI 686
Cdd:pfam00520    4 FELFILLLILLNTIFLALETYFQPEEPLTTVLEILDYVFTGIFTLEMLLKIIAagFKKRYFRSPWNILDFVVVLPSLISL 83

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1034557855  687 FCVYFVKLRpdNLALIQLTVIMGYLRIIRFLPLFKIIVPILIRIA 731
Cdd:pfam00520   84 VLSSVGSLS--GLRVLRLLRLLRLLRLIRRLEGLRTLVNSLIRSL 126
 
Name Accession Description Interval E-value
Na_H_Exchanger pfam00999
Sodium/hydrogen exchanger family; Na/H antiporters are key transporters in maintaining the pH ...
 98-380 6.75e-15

Sodium/hydrogen exchanger family; Na/H antiporters are key transporters in maintaining the pH of actively metabolising cells. The molecular mechanisms of antiport are unclear. These antiporters contain 10-12 transmembrane regions (M) at the amino-terminus and a large cytoplasmic region at the carboxyl terminus. The transmembrane regions M3-M12 share identity with other members of the family. The M6 and M7 regions are highly conserved. Thus, this is thought to be the region that is involved in the transport of sodium and hydrogen ions. The cytoplasmic region has little similarity throughout the family.


Pssm-ID: 425982 [Multi-domain]  Cd Length: 377  Bit Score: 77.68  E-value: 6.75e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557855   98 PLIIFMVALDVEFYTLKKMFWQVLLTGLISFSTASIIIGYVViKFNKDSWDLQSCLLFSITLGIIDPLRSVNSLKTIGI- 176
Cdd:pfam00999   57 PPLLFLAGLELDLRELRKNGGSILLLALLGVLIPFVLIGLLL-YLLGLGIPLLEALLFGAILSATSPVVVLAILKELGRv 135

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557855  177 -SKIYIdLIRGESLI--ICSI--ASIFFGNFRGNRIHFSIFRdlhVGIELSYDILGSIIFGYWCAKIIQCILADVFSNML 251
Cdd:pfam00999  136 pERLGT-LLLGESVLndGVAVvlLAVLLALAQGVGGGSDLGW---LLLIFLVVAVGGLLLGLLIGWLLRLITRFTDDDRE 211

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557855  252 TNIILCFSMVYMTFYIVEFLGMSGTLALAAVGLNLDSLTFKPKIElviTKFLRIFSSVYEHLIYAFFGIVIGCGELshyE 331
Cdd:pfam00999  212 LEVLLVLLLALLAALLAEALGVSGILGAFLAGLVLSEYPFANKLS---EKLEPFGYGLFNPLFFVLVGLSLDLSSL---L 285

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1034557855  332 FHTIPFIFILFTTVNLVRLLTILLVSPILmhsnyEYNWRWGVVITWSGI 380
Cdd:pfam00999  286 LSVWILVLLALVAILLGRFLGVFLLLRLL-----GLSLREALIIGFGGL 329
NhaP COG0025
NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion transport and metabolism];
98-383 1.16e-14

NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion transport and metabolism];


Pssm-ID: 439796 [Multi-domain]  Cd Length: 506  Bit Score: 78.08  E-value: 1.16e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557855   98 PLIIFMVALDVEFYTLKKMFWQV--LLTGLISFSTASI-IIGYVVIkfnkdSWDLQSCLLFSITLGIIDPLRSVNSLKTI 174
Cdd:COG0025     63 PPLLFEAALNLDLRELRRNGRPIlrLAVVGVLLTTLAVaLAAHWLL-----GLPLAAALLLGAILAPTDPVAVSPILRRL 137

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557855  175 GISKIYIDLIRGESLIICSIASIFFgnfrgnRIHFSI-----FRDLHVGIELSYDILGSIIFGYWCAKIIQCILAdVFSN 249
Cdd:COG0025    138 GVPKRLRTILEGESLLNDATALVLF------VLALAAalgggFSLGEALLDFLLAILGGILVGLLLGWLLGRLLR-RLPD 210

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557855  250 MLTNIILCFSMVYMTFYIVEFLGMSGTLALAAVGL---NLDSLTFKPKIELVITKFLRIFSSVYEHLIYAFFGIVIgcgE 326
Cdd:COG0025    211 PLLEILLTLALPFLAYLLAEALHGSGVLAVVVAGLvlgNAGRRSLSPETRLQLLEFWETLEFLLNSLLFVLLGAQL---P 287

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034557855  327 LSHYEFHTIPFIFILFTTVNLVRLLTILLVSPILMHSnyeYNWRWGVVITWSGIKGV 383
Cdd:COG0025    288 LILLGALGLGGILLVLLALLVVRPLWVFLSLALRGSR---LSWRERLFLSWGGPRGI 341
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 873-980 4.33e-11

effector domain of the CAP family of transcription factors; members include CAP (or cAMP receptor protein (CRP)), which binds cAMP, FNR (fumarate and nitrate reduction), which uses an iron-sulfur cluster to sense oxygen) and CooA, a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. Cyclic nucleotide-binding domain similar to CAP are also present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) and vertebrate cyclic nucleotide-gated ion-channels. Cyclic nucleotide-monophosphate binding domain; proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues; the best studied is the prokaryotic catabolite gene activator, CAP, where such a domain is known to be composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure; three conserved glycine residues are thought to be essential for maintenance of the structural integrity of the beta-barrel; CooA is a homodimeric transcription factor that belongs to CAP family; cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclic nucleotide-binding domain; cAPK's are composed of two different subunits, a catalytic chain and a regulatory chain, which contains both copies of the domain; cGPK's are single chain enzymes that include the two copies of the domain in their N-terminal section; also found in vertebrate cyclic nucleotide-gated ion-channels


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 61.19  E-value: 4.33e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557855  873 DVLIDFFKERAKLACFDSGDTICKGGEMPQGIYLIISGMAILHSLsptfgiesnqrcDRGSRDMFTEFCTTGDIIGELSC 952
Cdd:cd00038      7 DEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKL------------DEDGREQIVGFLGPGDLFGELAL 74

                           90       100
                   ....*....|....*....|....*...
gi 1034557855  953 LLKREIEYTVICETSLQACFISLEDLYE 980
Cdd:cd00038     75 LGNGPRSATVRALTDSELLVLPRSDFRR 102
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 873-998 1.29e-09

cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal transduction mechanisms];


Pssm-ID: 440428 [Multi-domain]  Cd Length: 207  Bit Score: 59.23  E-value: 1.29e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557855  873 DVLIDFFKERAKLACFDSGDTICKGGEMPQGIYLIISGMAILHSLSPtfgiesnqrcdrGSRDMFTEFCTTGDIIGELSC 952
Cdd:COG0664      6 DEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISE------------DGREQILGFLGPGDFFGELSL 73

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1034557855  953 LLKREIEYTVICETSLQACFISLEDLYEGFDAFwPSLEYKIWLKLA 998
Cdd:COG0664     74 LGGEPSPATAEALEDSELLRIPREDLEELLERN-PELARALLRLLA 118
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 888-980 7.27e-08

Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, oxygen and 2-oxoglutarate (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 459637 [Multi-domain]  Cd Length: 89  Bit Score: 51.07  E-value: 7.27e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557855  888 FDSGDTICKGGEMPQGIYLIISGMAILHSLSPTfgiesnqrcdrgSRDMFTEFCTTGDIIGELSCLLKREIEYTVICETS 967
Cdd:pfam00027    4 YKAGEVIFREGDPADSLYIVLSGKVKVYRTLED------------GREQILAVLGPGDFFGELALLGGEPRSATVVALTD 71

                           90
                   ....*....|...
gi 1034557855  968 LQACFISLEDLYE 980
Cdd:pfam00027   72 SELLVIPREDFLE 84
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 609-731 1.56e-05

Ion transport protein; This family contains sodium, potassium and calcium ion channels. This family is 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times, whereas in others (e.g. K channels) the protein forms as a tetramer in the membrane.


Pssm-ID: 459842 [Multi-domain]  Cd Length: 238  Bit Score: 47.65  E-value: 1.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557855  609 FEYTGQIINLIYIYPMIIHLWPMARGLNVSALISINYYFMFLYVLESTLKIII--LKRKYFQQCWNTLEFFILVIGIIDI 686
Cdd:pfam00520    4 FELFILLLILLNTIFLALETYFQPEEPLTTVLEILDYVFTGIFTLEMLLKIIAagFKKRYFRSPWNILDFVVVLPSLISL 83

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1034557855  687 FCVYFVKLRpdNLALIQLTVIMGYLRIIRFLPLFKIIVPILIRIA 731
Cdd:pfam00520   84 VLSSVGSLS--GLRVLRLLRLLRLLRLIRRLEGLRTLVNSLIRSL 126
b_cpa1 TIGR00840
sodium/hydrogen exchanger 3; The Monovalent Cation:Proton Antiporter-1 (CPA1) Family (TC 2.A. ...
 153-417 9.89e-05

sodium/hydrogen exchanger 3; The Monovalent Cation:Proton Antiporter-1 (CPA1) Family (TC 2.A.36)The CPA1 family is a large family of proteins derived from Gram-positive and Gram-negative bacteria, blue green bacteria, yeast, plants and animals.Transporters from eukaryotes have been functionally characterized, and all of these catalyze Na+:H+ exchange. Their primary physiological functions may be in(1) cytoplasmic pH regulation, extruding the H+ generated during metabolism, and (2) salt tolerance (in plants), due to Na+ uptake into vacuoles.This model is specific for the eukaryotic members members of this family. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273294 [Multi-domain]  Cd Length: 559  Bit Score: 46.31  E-value: 9.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557855  153 LLFSITLGIIDPLRSVNSLKTIGISKIYIDLIRGESLIICSIASIFFGNFrgnrIHFSIFRDLHVGIElsyDILGSIIF- 231
Cdd:TIGR00840  135 LLFGSLISAVDPVAVLAVFEEYHVNEKLYIIIFGESLLNDAVTVVLYNTF----IKFHKTADEPVTIV---DVFEGCASf 207

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557855  232 ------GYWCAKIIQCILADVFSNM----LTNIILCFSMVYMTFYIVEFLGMSGTLALAAVGLNLD---SLTFKPKIELV 298
Cdd:TIGR00840  208 fvvtcgGLLVGVVFGFLVAFITRFThhirQIEPLFVFLISYLSYLFAETLHLSGILALIFCGITMKkyvEANMSRRSQTT 287

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557855  299 ITKFLRIFSSVYEHLIYAFFGIvigcgELSHYEfHTIPFIFILFTTV--NLVRLLTILLVSPIL-MHSNYEYNWRWGVVI 375
Cdd:TIGR00840  288 IKYFMKMLSSLSETLIFIFLGV-----SLVTEN-HEWNWAFVVATLSfcVIYRVLGVRTLSWITnEFRPVEIPYKDQLVI 361

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1034557855  376 TWSGIKGV--FNLlwapdVYNLAERKVEVPQMFILYVQVISLLT 417
Cdd:TIGR00840  362 FYAGLRGAvaFAL-----ALLLDEKIFPYKFLFVTTTLVVVFFT 400
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 888-986 5.19e-04

Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a prokaryotic homologue of eukaryotic cNMP-binding domains, present in ion channels, and cNMP-dependent kinases.


Pssm-ID: 197516 [Multi-domain]  Cd Length: 120  Bit Score: 40.85  E-value: 5.19e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557855   888 FDSGDTICKGGEMPQGIYLIISGMAILHSLSPtfgiesnqrcdrGSRDMFTEFCTTGDIIGELSCLLKREIEYTVICETS 967
Cdd:smart00100   22 YPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLE------------DGEEQIVGTLGPGDFFGELALLTNSRRAASAAAVAL 89

                            90       100
                    ....*....|....*....|.
gi 1034557855   968 --LQACFISLEDLYEGFDAFW 986
Cdd:smart00100   90 elATLLRIDFRDFLQLLPELP 110
 
Name Accession Description Interval E-value
Na_H_Exchanger pfam00999
Sodium/hydrogen exchanger family; Na/H antiporters are key transporters in maintaining the pH ...
 98-380 6.75e-15

Sodium/hydrogen exchanger family; Na/H antiporters are key transporters in maintaining the pH of actively metabolising cells. The molecular mechanisms of antiport are unclear. These antiporters contain 10-12 transmembrane regions (M) at the amino-terminus and a large cytoplasmic region at the carboxyl terminus. The transmembrane regions M3-M12 share identity with other members of the family. The M6 and M7 regions are highly conserved. Thus, this is thought to be the region that is involved in the transport of sodium and hydrogen ions. The cytoplasmic region has little similarity throughout the family.


Pssm-ID: 425982 [Multi-domain]  Cd Length: 377  Bit Score: 77.68  E-value: 6.75e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557855   98 PLIIFMVALDVEFYTLKKMFWQVLLTGLISFSTASIIIGYVViKFNKDSWDLQSCLLFSITLGIIDPLRSVNSLKTIGI- 176
Cdd:pfam00999   57 PPLLFLAGLELDLRELRKNGGSILLLALLGVLIPFVLIGLLL-YLLGLGIPLLEALLFGAILSATSPVVVLAILKELGRv 135

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557855  177 -SKIYIdLIRGESLI--ICSI--ASIFFGNFRGNRIHFSIFRdlhVGIELSYDILGSIIFGYWCAKIIQCILADVFSNML 251
Cdd:pfam00999  136 pERLGT-LLLGESVLndGVAVvlLAVLLALAQGVGGGSDLGW---LLLIFLVVAVGGLLLGLLIGWLLRLITRFTDDDRE 211

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557855  252 TNIILCFSMVYMTFYIVEFLGMSGTLALAAVGLNLDSLTFKPKIElviTKFLRIFSSVYEHLIYAFFGIVIGCGELshyE 331
Cdd:pfam00999  212 LEVLLVLLLALLAALLAEALGVSGILGAFLAGLVLSEYPFANKLS---EKLEPFGYGLFNPLFFVLVGLSLDLSSL---L 285

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1034557855  332 FHTIPFIFILFTTVNLVRLLTILLVSPILmhsnyEYNWRWGVVITWSGI 380
Cdd:pfam00999  286 LSVWILVLLALVAILLGRFLGVFLLLRLL-----GLSLREALIIGFGGL 329
NhaP COG0025
NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion transport and metabolism];
98-383 1.16e-14

NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion transport and metabolism];


Pssm-ID: 439796 [Multi-domain]  Cd Length: 506  Bit Score: 78.08  E-value: 1.16e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557855   98 PLIIFMVALDVEFYTLKKMFWQV--LLTGLISFSTASI-IIGYVVIkfnkdSWDLQSCLLFSITLGIIDPLRSVNSLKTI 174
Cdd:COG0025     63 PPLLFEAALNLDLRELRRNGRPIlrLAVVGVLLTTLAVaLAAHWLL-----GLPLAAALLLGAILAPTDPVAVSPILRRL 137

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557855  175 GISKIYIDLIRGESLIICSIASIFFgnfrgnRIHFSI-----FRDLHVGIELSYDILGSIIFGYWCAKIIQCILAdVFSN 249
Cdd:COG0025    138 GVPKRLRTILEGESLLNDATALVLF------VLALAAalgggFSLGEALLDFLLAILGGILVGLLLGWLLGRLLR-RLPD 210

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557855  250 MLTNIILCFSMVYMTFYIVEFLGMSGTLALAAVGL---NLDSLTFKPKIELVITKFLRIFSSVYEHLIYAFFGIVIgcgE 326
Cdd:COG0025    211 PLLEILLTLALPFLAYLLAEALHGSGVLAVVVAGLvlgNAGRRSLSPETRLQLLEFWETLEFLLNSLLFVLLGAQL---P 287

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034557855  327 LSHYEFHTIPFIFILFTTVNLVRLLTILLVSPILMHSnyeYNWRWGVVITWSGIKGV 383
Cdd:COG0025    288 LILLGALGLGGILLVLLALLVVRPLWVFLSLALRGSR---LSWRERLFLSWGGPRGI 341
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 873-980 4.33e-11

effector domain of the CAP family of transcription factors; members include CAP (or cAMP receptor protein (CRP)), which binds cAMP, FNR (fumarate and nitrate reduction), which uses an iron-sulfur cluster to sense oxygen) and CooA, a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. Cyclic nucleotide-binding domain similar to CAP are also present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) and vertebrate cyclic nucleotide-gated ion-channels. Cyclic nucleotide-monophosphate binding domain; proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues; the best studied is the prokaryotic catabolite gene activator, CAP, where such a domain is known to be composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure; three conserved glycine residues are thought to be essential for maintenance of the structural integrity of the beta-barrel; CooA is a homodimeric transcription factor that belongs to CAP family; cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclic nucleotide-binding domain; cAPK's are composed of two different subunits, a catalytic chain and a regulatory chain, which contains both copies of the domain; cGPK's are single chain enzymes that include the two copies of the domain in their N-terminal section; also found in vertebrate cyclic nucleotide-gated ion-channels


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 61.19  E-value: 4.33e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557855  873 DVLIDFFKERAKLACFDSGDTICKGGEMPQGIYLIISGMAILHSLsptfgiesnqrcDRGSRDMFTEFCTTGDIIGELSC 952
Cdd:cd00038      7 DEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKL------------DEDGREQIVGFLGPGDLFGELAL 74

                           90       100
                   ....*....|....*....|....*...
gi 1034557855  953 LLKREIEYTVICETSLQACFISLEDLYE 980
Cdd:cd00038     75 LGNGPRSATVRALTDSELLVLPRSDFRR 102
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 873-998 1.29e-09

cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal transduction mechanisms];


Pssm-ID: 440428 [Multi-domain]  Cd Length: 207  Bit Score: 59.23  E-value: 1.29e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557855  873 DVLIDFFKERAKLACFDSGDTICKGGEMPQGIYLIISGMAILHSLSPtfgiesnqrcdrGSRDMFTEFCTTGDIIGELSC 952
Cdd:COG0664      6 DEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISE------------DGREQILGFLGPGDFFGELSL 73

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1034557855  953 LLKREIEYTVICETSLQACFISLEDLYEGFDAFwPSLEYKIWLKLA 998
Cdd:COG0664     74 LGGEPSPATAEALEDSELLRIPREDLEELLERN-PELARALLRLLA 118
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 888-980 7.27e-08

Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, oxygen and 2-oxoglutarate (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 459637 [Multi-domain]  Cd Length: 89  Bit Score: 51.07  E-value: 7.27e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557855  888 FDSGDTICKGGEMPQGIYLIISGMAILHSLSPTfgiesnqrcdrgSRDMFTEFCTTGDIIGELSCLLKREIEYTVICETS 967
Cdd:pfam00027    4 YKAGEVIFREGDPADSLYIVLSGKVKVYRTLED------------GREQILAVLGPGDFFGELALLGGEPRSATVVALTD 71

                           90
                   ....*....|...
gi 1034557855  968 LQACFISLEDLYE 980
Cdd:pfam00027   72 SELLVIPREDFLE 84
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 609-731 1.56e-05

Ion transport protein; This family contains sodium, potassium and calcium ion channels. This family is 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times, whereas in others (e.g. K channels) the protein forms as a tetramer in the membrane.


Pssm-ID: 459842 [Multi-domain]  Cd Length: 238  Bit Score: 47.65  E-value: 1.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557855  609 FEYTGQIINLIYIYPMIIHLWPMARGLNVSALISINYYFMFLYVLESTLKIII--LKRKYFQQCWNTLEFFILVIGIIDI 686
Cdd:pfam00520    4 FELFILLLILLNTIFLALETYFQPEEPLTTVLEILDYVFTGIFTLEMLLKIIAagFKKRYFRSPWNILDFVVVLPSLISL 83

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1034557855  687 FCVYFVKLRpdNLALIQLTVIMGYLRIIRFLPLFKIIVPILIRIA 731
Cdd:pfam00520   84 VLSSVGSLS--GLRVLRLLRLLRLLRLIRRLEGLRTLVNSLIRSL 126
b_cpa1 TIGR00840
sodium/hydrogen exchanger 3; The Monovalent Cation:Proton Antiporter-1 (CPA1) Family (TC 2.A. ...
 153-417 9.89e-05

sodium/hydrogen exchanger 3; The Monovalent Cation:Proton Antiporter-1 (CPA1) Family (TC 2.A.36)The CPA1 family is a large family of proteins derived from Gram-positive and Gram-negative bacteria, blue green bacteria, yeast, plants and animals.Transporters from eukaryotes have been functionally characterized, and all of these catalyze Na+:H+ exchange. Their primary physiological functions may be in(1) cytoplasmic pH regulation, extruding the H+ generated during metabolism, and (2) salt tolerance (in plants), due to Na+ uptake into vacuoles.This model is specific for the eukaryotic members members of this family. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273294 [Multi-domain]  Cd Length: 559  Bit Score: 46.31  E-value: 9.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557855  153 LLFSITLGIIDPLRSVNSLKTIGISKIYIDLIRGESLIICSIASIFFGNFrgnrIHFSIFRDLHVGIElsyDILGSIIF- 231
Cdd:TIGR00840  135 LLFGSLISAVDPVAVLAVFEEYHVNEKLYIIIFGESLLNDAVTVVLYNTF----IKFHKTADEPVTIV---DVFEGCASf 207

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557855  232 ------GYWCAKIIQCILADVFSNM----LTNIILCFSMVYMTFYIVEFLGMSGTLALAAVGLNLD---SLTFKPKIELV 298
Cdd:TIGR00840  208 fvvtcgGLLVGVVFGFLVAFITRFThhirQIEPLFVFLISYLSYLFAETLHLSGILALIFCGITMKkyvEANMSRRSQTT 287

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557855  299 ITKFLRIFSSVYEHLIYAFFGIvigcgELSHYEfHTIPFIFILFTTV--NLVRLLTILLVSPIL-MHSNYEYNWRWGVVI 375
Cdd:TIGR00840  288 IKYFMKMLSSLSETLIFIFLGV-----SLVTEN-HEWNWAFVVATLSfcVIYRVLGVRTLSWITnEFRPVEIPYKDQLVI 361

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1034557855  376 TWSGIKGV--FNLlwapdVYNLAERKVEVPQMFILYVQVISLLT 417
Cdd:TIGR00840  362 FYAGLRGAvaFAL-----ALLLDEKIFPYKFLFVTTTLVVVFFT 400
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 888-986 5.19e-04

Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a prokaryotic homologue of eukaryotic cNMP-binding domains, present in ion channels, and cNMP-dependent kinases.


Pssm-ID: 197516 [Multi-domain]  Cd Length: 120  Bit Score: 40.85  E-value: 5.19e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034557855   888 FDSGDTICKGGEMPQGIYLIISGMAILHSLSPtfgiesnqrcdrGSRDMFTEFCTTGDIIGELSCLLKREIEYTVICETS 967
Cdd:smart00100   22 YPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLE------------DGEEQIVGTLGPGDFFGELALLTNSRRAASAAAVAL 89

                            90       100
                    ....*....|....*....|.
gi 1034557855   968 --LQACFISLEDLYEGFDAFW 986
Cdd:smart00100   90 elATLLRIDFRDFLQLLPELP 110
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH