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Conserved domains on  [gi|582714723|gb|EWA03344|]
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NitT/TauT family transporter substrate-binding protein [Staphylococcus aureus H57823]

Protein Classification

ABC transporter substrate-binding protein( domain architecture ID 10194283)

ABC transporter substrate-binding protein functions as the initial receptor in the ABC transport of one of a variety of substrates, including ions such as bicarbonate and nitrate; belongs to the type 2 periplasmic binding protein (PBP2) family

CATH:  3.40.190.10
Gene Ontology:  GO:0140359|GO:0042626|GO:0055052
TCDB:  3.A.1

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PBP2_NrtA_CpmA_like cd13553
Substrate binding domain of ABC-type nitrate/bicarbonate transporters, a member of the type 2 ...
36-246 3.04e-52

Substrate binding domain of ABC-type nitrate/bicarbonate transporters, a member of the type 2 periplasmic binding fold superfamily; This subfamily includes nitrate (NrtA) and bicarbonate (CmpA) receptors. These domains are found in eubacterial perisplamic-binding proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates, while other closest homologs are involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB). After binding their ligand with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. These binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


:

Pssm-ID: 270271 [Multi-domain]  Cd Length: 212  Bit Score: 171.22  E-value: 3.04e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582714723  36 VIKIGYLPITHSANLMMTKKLLSqYNHPKYKLELVKFNNWPDLMDALNSGRIDGASTLIELAMKSKQ-KGSNIKAVALGH 114
Cdd:cd13553    1 TLRIGYLPITDHAPLLVAKEKGF-FEKEGLDVELVKFPSWADLRDALAAGELDAAHVLAPMPAAATYgKGAPIKVVAGLH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582714723 115 HEGNVIMGQKGMHLNEFNNGDDYHFGIPHRYSTHYLLLEELRKQLKIKPGH-FSYHEMSPAEMPAALSEHRITGYSVAEP 193
Cdd:cd13553   80 RNGSAIVVSKDSGIKSVADLKGKTIAVPFPGSTHDVLLRYWLAAAGLDPGKdVEIVVLPPPDMVAALAAGQIDAYCVGEP 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 582714723 194 FGALGEKLGKGKTLKHGDDVIPDAYCCVLVLRGELLDQHKDVAQAFVQDYKKS 246
Cdd:cd13553  160 WNARAVAEGVGRVLADSGDIWPGHPCCVLVVREDFLEENPEAVQALLKALVEA 212
 
Name Accession Description Interval E-value
PBP2_NrtA_CpmA_like cd13553
Substrate binding domain of ABC-type nitrate/bicarbonate transporters, a member of the type 2 ...
36-246 3.04e-52

Substrate binding domain of ABC-type nitrate/bicarbonate transporters, a member of the type 2 periplasmic binding fold superfamily; This subfamily includes nitrate (NrtA) and bicarbonate (CmpA) receptors. These domains are found in eubacterial perisplamic-binding proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates, while other closest homologs are involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB). After binding their ligand with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. These binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270271 [Multi-domain]  Cd Length: 212  Bit Score: 171.22  E-value: 3.04e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582714723  36 VIKIGYLPITHSANLMMTKKLLSqYNHPKYKLELVKFNNWPDLMDALNSGRIDGASTLIELAMKSKQ-KGSNIKAVALGH 114
Cdd:cd13553    1 TLRIGYLPITDHAPLLVAKEKGF-FEKEGLDVELVKFPSWADLRDALAAGELDAAHVLAPMPAAATYgKGAPIKVVAGLH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582714723 115 HEGNVIMGQKGMHLNEFNNGDDYHFGIPHRYSTHYLLLEELRKQLKIKPGH-FSYHEMSPAEMPAALSEHRITGYSVAEP 193
Cdd:cd13553   80 RNGSAIVVSKDSGIKSVADLKGKTIAVPFPGSTHDVLLRYWLAAAGLDPGKdVEIVVLPPPDMVAALAAGQIDAYCVGEP 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 582714723 194 FGALGEKLGKGKTLKHGDDVIPDAYCCVLVLRGELLDQHKDVAQAFVQDYKKS 246
Cdd:cd13553  160 WNARAVAEGVGRVLADSGDIWPGHPCCVLVVREDFLEENPEAVQALLKALVEA 212
TauA COG0715
ABC-type nitrate/sulfonate/bicarbonate transport system, periplasmic component [Inorganic ion ...
27-307 1.04e-43

ABC-type nitrate/sulfonate/bicarbonate transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 440479 [Multi-domain]  Cd Length: 297  Bit Score: 151.70  E-value: 1.04e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582714723  27 PSKNAQNQQVIKIGYLPITHSANLMMTKK--LLSQYNhpkYKLELVKFNNWPDLMDALNSGRIDGASTLIELAMKSKQKG 104
Cdd:COG0715   14 AAAAAAEKVTLRLGWLPNTDHAPLYVAKEkgYFKKEG---LDVELVEFAGGAAALEALAAGQADFGVAGAPPALAARAKG 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582714723 105 SNIKAVA-LGHHEGNVIMGQKGMHLNEFnngDDY---HFGIPhRYSTHYLLLEELRKQLKIKPGHFSYHEMSPAEMPAAL 180
Cdd:COG0715   91 APVKAVAaLSQSGGNALVVRKDSGIKSL---ADLkgkKVAVP-GGSTSHYLLRALLAKAGLDPKDVEIVNLPPPDAVAAL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582714723 181 SEHRITGYSVAEPFGALGEKLGKGKTLKHGDDVIPDAYCCVLVLRGELLDQHKDVAQAFVQDYKKSG-FKMNDRKQSVDI 259
Cdd:COG0715  167 LAGQVDAAVVWEPFESQAEKKGGGRVLADSADLVPGYPGDVLVASEDFLEENPEAVKAFLRALLKAWaWAAANPDEAAAI 246
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 582714723 260 MTHHFKQSRDVLTQSAAWT---SYGDLTIKPSGYQEITTLVKQHHLFNPPA 307
Cdd:COG0715  247 LAKATGLDPEVLAAALEGDlrlDPPLGAPDPARLQRVADFLVELGLLPKDV 297
SsuA_fam TIGR01728
ABC transporter, substrate-binding protein, aliphatic sulfonates family; Members of this ...
37-318 1.18e-22

ABC transporter, substrate-binding protein, aliphatic sulfonates family; Members of this family are substrate-binding periplasmic proteins of ABC transporters. This subfamily includes SsuA, a member of a transporter operon needed to obtain sulfur from aliphatic sulfonates. Related proteins outside the scope of this model include taurine (NH2-CH2-CH2-S03H) binding proteins, the probable sulfate ester binding protein AtsR, and the probable aromatic sulfonate binding protein AsfC. All these families make sulfur available when Cys and sulfate levels are low. Please note that phylogenetic analysis by neighbor-joining suggests that a number of sequences belonging to this family have been excluded because of scoring lower than taurine-binding proteins. [Transport and binding proteins, Other]


Pssm-ID: 130789 [Multi-domain]  Cd Length: 288  Bit Score: 95.51  E-value: 1.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582714723   37 IKIGYLPITHSANLM-MTKKLLSQyNHPKYKLELVKFNNWPDLMDALNSGRIDGASTLIELAMKSKQKGSNIKAVALGH- 114
Cdd:TIGR01728   1 VRIGYQKNGHSALALaKEKGLLEK-ELGKTKVEWVEFPAGPPALEALGAGSLDFGYIGPGPALFAYAAGADIKAVGLVSd 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582714723  115 HEGNVIMGQKGMHLNEFNNGDDYHFGIPHRYSTHYLLLEELRKQ-LKIKPGHFSYheMSPAEMPAALSEHRITGYSVAEP 193
Cdd:TIGR01728  80 NKATAIVVIKGSPIRTVADLKGKRIAVPKGGSGHDLLLRALLKAgLSGDDVTILY--LGPSDARAAFAAGQVDAWAIWEP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582714723  194 FGALGEKLGKGKTLKHGDDVIPDAYCCVLVLRGELLDQHKDVAQAFVQDYKKS-GFKMNDRKQSVDIMTHHFKQSRDVLT 272
Cdd:TIGR01728 158 WGSALVEEGGARVLANGEGIGLPGQPGFLVVRREFAEAHPEQVQRVLKVLVKArKWAEENPEESAKILAKELGLSQAVVE 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 582714723  273 QSAAWTSygDLTIKPSGYQEITTL-------VKQHHLFNPPAYDDFVEPSLYK 318
Cdd:TIGR01728 238 ETVLNRR--FLRVEVISDAVVDALqamadffYAAGLLKKKPDLKDAVDRSFLK 288
NMT1_2 pfam13379
NMT1-like family; This family is closely related to the pfam09084 family.
37-241 4.74e-19

NMT1-like family; This family is closely related to the pfam09084 family.


Pssm-ID: 463863  Cd Length: 254  Bit Score: 84.70  E-value: 4.74e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582714723   37 IKIGYLPITHSANLMM--TKKLLSQYNHPkykLELVKFNNWPDLMDALNSGRIDGASTLIELA----MKSKQKGSNIKAV 110
Cdd:pfam13379   8 LKLGFIPLTDAAPLIVaaEKGFFAKYGLT---VELSKQASWAETRDALVAGELDAAHVLTPMPylitLGIGGAKVPMIVL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582714723  111 ALGHHEGNVIM--------------GQKGMHLNEFNNGDDYHFGIPHRYSTHYLLLEELRKQLKIKPGhfSYHEMS---P 173
Cdd:pfam13379  85 ASLNLNGQAITlankyadkgvrdaaALKDLVGAYKASGKPFKFAVTFPGSTHDLWLRYWLAAGGLDPD--ADVKLVvvpP 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 582714723  174 AEMPAALSEHRITGYSVAEPFGALGEKLGKGKTLKHGDDVIPDAYCCVLVLRGELLDQHKDVAQAFVQ 241
Cdd:pfam13379 163 PQMVANLRAGNIDGFCVGEPWNARAVAEGIGVTAATTGELWKDHPEKVLGVRADWVDKNPNAARALVK 230
PBPb smart00062
Bacterial periplasmic substrate-binding proteins; bacterial proteins, eukaryotic ones are in ...
65-248 1.35e-03

Bacterial periplasmic substrate-binding proteins; bacterial proteins, eukaryotic ones are in PBPe


Pssm-ID: 214497 [Multi-domain]  Cd Length: 219  Bit Score: 39.23  E-value: 1.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582714723    65 YKLELVKFNnWPDLMDALNSGRID----GASTLIELA---------MKSKQ-----KGSNIKAVAlgHHEGNVIMGQKGm 126
Cdd:smart00062  39 LKVEFVEVS-FDSLLTALKSGKIDvvaaGMTITPERAkqvdfsdpyYRSGQvilvrKDSPIKSLE--DLKGKKVAVVAG- 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582714723   127 hlnefnngddyhfgiphrySTHYLLLEELRKQLKIKPghfsyhEMSPAEMPAALSEHRITGYSVAEPFGALGEKLGKGKT 206
Cdd:smart00062 115 -------------------TTAEELLKKLYPEAKIVS------YDSNAEALAALKAGRADAAVADAPLLAALVKQHGLPE 169
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 582714723   207 LK-HGDDVIPDAYCCVLVLRGEllDQHKDVAQAFVQDYKKSGF 248
Cdd:smart00062 170 LKiVPDPLDTPEGYAIAVRKGD--PELLDKINKALKELKADGT 210
 
Name Accession Description Interval E-value
PBP2_NrtA_CpmA_like cd13553
Substrate binding domain of ABC-type nitrate/bicarbonate transporters, a member of the type 2 ...
36-246 3.04e-52

Substrate binding domain of ABC-type nitrate/bicarbonate transporters, a member of the type 2 periplasmic binding fold superfamily; This subfamily includes nitrate (NrtA) and bicarbonate (CmpA) receptors. These domains are found in eubacterial perisplamic-binding proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates, while other closest homologs are involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB). After binding their ligand with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. These binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270271 [Multi-domain]  Cd Length: 212  Bit Score: 171.22  E-value: 3.04e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582714723  36 VIKIGYLPITHSANLMMTKKLLSqYNHPKYKLELVKFNNWPDLMDALNSGRIDGASTLIELAMKSKQ-KGSNIKAVALGH 114
Cdd:cd13553    1 TLRIGYLPITDHAPLLVAKEKGF-FEKEGLDVELVKFPSWADLRDALAAGELDAAHVLAPMPAAATYgKGAPIKVVAGLH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582714723 115 HEGNVIMGQKGMHLNEFNNGDDYHFGIPHRYSTHYLLLEELRKQLKIKPGH-FSYHEMSPAEMPAALSEHRITGYSVAEP 193
Cdd:cd13553   80 RNGSAIVVSKDSGIKSVADLKGKTIAVPFPGSTHDVLLRYWLAAAGLDPGKdVEIVVLPPPDMVAALAAGQIDAYCVGEP 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 582714723 194 FGALGEKLGKGKTLKHGDDVIPDAYCCVLVLRGELLDQHKDVAQAFVQDYKKS 246
Cdd:cd13553  160 WNARAVAEGVGRVLADSGDIWPGHPCCVLVVREDFLEENPEAVQALLKALVEA 212
TauA COG0715
ABC-type nitrate/sulfonate/bicarbonate transport system, periplasmic component [Inorganic ion ...
27-307 1.04e-43

ABC-type nitrate/sulfonate/bicarbonate transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 440479 [Multi-domain]  Cd Length: 297  Bit Score: 151.70  E-value: 1.04e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582714723  27 PSKNAQNQQVIKIGYLPITHSANLMMTKK--LLSQYNhpkYKLELVKFNNWPDLMDALNSGRIDGASTLIELAMKSKQKG 104
Cdd:COG0715   14 AAAAAAEKVTLRLGWLPNTDHAPLYVAKEkgYFKKEG---LDVELVEFAGGAAALEALAAGQADFGVAGAPPALAARAKG 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582714723 105 SNIKAVA-LGHHEGNVIMGQKGMHLNEFnngDDY---HFGIPhRYSTHYLLLEELRKQLKIKPGHFSYHEMSPAEMPAAL 180
Cdd:COG0715   91 APVKAVAaLSQSGGNALVVRKDSGIKSL---ADLkgkKVAVP-GGSTSHYLLRALLAKAGLDPKDVEIVNLPPPDAVAAL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582714723 181 SEHRITGYSVAEPFGALGEKLGKGKTLKHGDDVIPDAYCCVLVLRGELLDQHKDVAQAFVQDYKKSG-FKMNDRKQSVDI 259
Cdd:COG0715  167 LAGQVDAAVVWEPFESQAEKKGGGRVLADSADLVPGYPGDVLVASEDFLEENPEAVKAFLRALLKAWaWAAANPDEAAAI 246
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 582714723 260 MTHHFKQSRDVLTQSAAWT---SYGDLTIKPSGYQEITTLVKQHHLFNPPA 307
Cdd:COG0715  247 LAKATGLDPEVLAAALEGDlrlDPPLGAPDPARLQRVADFLVELGLLPKDV 297
SsuA_fam TIGR01728
ABC transporter, substrate-binding protein, aliphatic sulfonates family; Members of this ...
37-318 1.18e-22

ABC transporter, substrate-binding protein, aliphatic sulfonates family; Members of this family are substrate-binding periplasmic proteins of ABC transporters. This subfamily includes SsuA, a member of a transporter operon needed to obtain sulfur from aliphatic sulfonates. Related proteins outside the scope of this model include taurine (NH2-CH2-CH2-S03H) binding proteins, the probable sulfate ester binding protein AtsR, and the probable aromatic sulfonate binding protein AsfC. All these families make sulfur available when Cys and sulfate levels are low. Please note that phylogenetic analysis by neighbor-joining suggests that a number of sequences belonging to this family have been excluded because of scoring lower than taurine-binding proteins. [Transport and binding proteins, Other]


Pssm-ID: 130789 [Multi-domain]  Cd Length: 288  Bit Score: 95.51  E-value: 1.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582714723   37 IKIGYLPITHSANLM-MTKKLLSQyNHPKYKLELVKFNNWPDLMDALNSGRIDGASTLIELAMKSKQKGSNIKAVALGH- 114
Cdd:TIGR01728   1 VRIGYQKNGHSALALaKEKGLLEK-ELGKTKVEWVEFPAGPPALEALGAGSLDFGYIGPGPALFAYAAGADIKAVGLVSd 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582714723  115 HEGNVIMGQKGMHLNEFNNGDDYHFGIPHRYSTHYLLLEELRKQ-LKIKPGHFSYheMSPAEMPAALSEHRITGYSVAEP 193
Cdd:TIGR01728  80 NKATAIVVIKGSPIRTVADLKGKRIAVPKGGSGHDLLLRALLKAgLSGDDVTILY--LGPSDARAAFAAGQVDAWAIWEP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582714723  194 FGALGEKLGKGKTLKHGDDVIPDAYCCVLVLRGELLDQHKDVAQAFVQDYKKS-GFKMNDRKQSVDIMTHHFKQSRDVLT 272
Cdd:TIGR01728 158 WGSALVEEGGARVLANGEGIGLPGQPGFLVVRREFAEAHPEQVQRVLKVLVKArKWAEENPEESAKILAKELGLSQAVVE 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 582714723  273 QSAAWTSygDLTIKPSGYQEITTL-------VKQHHLFNPPAYDDFVEPSLYK 318
Cdd:TIGR01728 238 ETVLNRR--FLRVEVISDAVVDALqamadffYAAGLLKKKPDLKDAVDRSFLK 288
NMT1_2 pfam13379
NMT1-like family; This family is closely related to the pfam09084 family.
37-241 4.74e-19

NMT1-like family; This family is closely related to the pfam09084 family.


Pssm-ID: 463863  Cd Length: 254  Bit Score: 84.70  E-value: 4.74e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582714723   37 IKIGYLPITHSANLMM--TKKLLSQYNHPkykLELVKFNNWPDLMDALNSGRIDGASTLIELA----MKSKQKGSNIKAV 110
Cdd:pfam13379   8 LKLGFIPLTDAAPLIVaaEKGFFAKYGLT---VELSKQASWAETRDALVAGELDAAHVLTPMPylitLGIGGAKVPMIVL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582714723  111 ALGHHEGNVIM--------------GQKGMHLNEFNNGDDYHFGIPHRYSTHYLLLEELRKQLKIKPGhfSYHEMS---P 173
Cdd:pfam13379  85 ASLNLNGQAITlankyadkgvrdaaALKDLVGAYKASGKPFKFAVTFPGSTHDLWLRYWLAAGGLDPD--ADVKLVvvpP 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 582714723  174 AEMPAALSEHRITGYSVAEPFGALGEKLGKGKTLKHGDDVIPDAYCCVLVLRGELLDQHKDVAQAFVQ 241
Cdd:pfam13379 163 PQMVANLRAGNIDGFCVGEPWNARAVAEGIGVTAATTGELWKDHPEKVLGVRADWVDKNPNAARALVK 230
PBP2_NrtA_SsuA_CpmA_like cd01008
Substrate binding domain of ABC-type nitrate/sulfonate/bicarbonate transporters, a member of ...
36-246 8.19e-17

Substrate binding domain of ABC-type nitrate/sulfonate/bicarbonate transporters, a member of the type 2 periplasmic binding fold superfamily; This family represents the periplasmic binding proteins involved in nitrate, alkanesulfonate, and bicarbonate transport. These domains are found in eubacterial perisplamic-binding proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates. Other closest homologs involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB) are also included in this family. After binding their ligand with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. These binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270229 [Multi-domain]  Cd Length: 212  Bit Score: 77.71  E-value: 8.19e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582714723  36 VIKIGYLPITHSANLMMT--KKLLSQYNHpKYKLELVKFNNWPDLMDALNSGRIDGASTLIELAMKSKQKGSNIKAVAL- 112
Cdd:cd01008    1 TVRIGYQAGPLAGPLIVAkeKGLFEKEKE-GIDVEWVEFTSGPPALEALAAGSLDFGTGGDTPALLAAAGGVPVVLIAAl 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582714723 113 -GHHEGNVIMGQKGmhlNEFNNGDD-------YHFGIphrySTHYLLLEELRKQlKIKPGHFSYHEMSPAEMPAALSEHR 184
Cdd:cd01008   80 sRSPNGNGIVVRKD---SGITSLADlkgkkiaVTKGT----TGHFLLLKALAKA-GLSVDDVELVNLGPADAAAALASGD 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 582714723 185 ITGYSVAEPFGALGEKLGKGKTLkHGDDVIPDAYCCVLVLRGELLDQHKDVAQAFVQDYKKS 246
Cdd:cd01008  152 VDAWVTWEPFLSLAEKGGDARII-VDGGGLPYTDPSVLVARRDFVEENPEAVKALLKALVEA 212
PBP2_SsuA_like_6 cd13563
Putative substrate binding domain of sulfonate binding protein-like, a member of the type 2 ...
66-245 1.55e-12

Putative substrate binding domain of sulfonate binding protein-like, a member of the type 2 periplasmic binding protein fold; This subfamily includes the periplasmic component of putative ABC-type sulfonate transport system similar to SsuA. These domains are found in eubacterial SsuA proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates, while other closest homologs are involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB). After binding the ligand, SsuA interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The SsuA proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270281 [Multi-domain]  Cd Length: 208  Bit Score: 65.72  E-value: 1.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582714723  66 KLELVKFNNWPDLMDALNSGRIDGASTLIELAMKSKQKGSNIKAVAlghhegnvimgqkgmhLNEFNNGDDyhfGIPHR- 144
Cdd:cd13563   30 DVELVWFESYSDSMAALASGQIDAAATTLDDALAMAAKGVPVKIVL----------------VLDNSNGAD---GIVAKp 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582714723 145 -----------------YSTHYLLLEELRKQLKIKPGHFSYHEMSPAEMPAALSEHRITGYSVAEPFGALGEKLGKGKTL 207
Cdd:cd13563   91 giksiadlkgktvaveeGSVSHFLLLNALEKAGLTEKDVKIVNMTAGDAGAAFIAGQVDAAVTWEPWLSNALKRGKGKVL 170
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 582714723 208 KHGDD---VIPDayccVLVLRGELLDQHKDVAQAFVQDYKK 245
Cdd:cd13563  171 VSSADtpgLIPD----VLVVREDFIKKNPEAVKAVVKAWFD 207
PBP2_SsuA cd13557
Substrate binding domain of sulfonate binding protein, a member of the type 2 periplasmic ...
36-303 5.91e-10

Substrate binding domain of sulfonate binding protein, a member of the type 2 periplasmic binding fold superfamily; This subfamily includes the sulfonate binding domains SsuA found in eubacterial SsuA proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates, while other closest homologs are involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB). After binding the ligand, SsuA interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The SsuA proteins belong to the PBPII superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270275  Cd Length: 275  Bit Score: 58.84  E-value: 5.91e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582714723  36 VIKIGYLPITHSANLMMTKKLLSQYNHPKYKLELVKFNNWPDLMDALNSGRIDGAST--------------LIELA-MKS 100
Cdd:cd13557    1 TLRIGYQKGGTLVLLKARGELEKRLKPLGVKVTWSEFPAGPQLLEALNVGSIDFGSTgdtppifaqaagapLVYVAvEPP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582714723 101 KQKG--------SNIKAVA-LghhEGNVIMGQKGMhlnefnngddyhfgiphrySTHYLLLEELRK---QLK-IKPGHfs 167
Cdd:cd13557   81 TPKGeailvpkdSPIKTVAdL---KGKKIAFQKGS-------------------SAHYLLVKALEKaglTLDdIEPVY-- 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582714723 168 yheMSPAEMPAALSEHRITGYSVAEPFGALGEKLGKGKTLKHGDDVIPDaYCCVLVLRgELLDQHKDVAQAFVQDYKKSG 247
Cdd:cd13557  137 ---LSPADARAAFEQGQVDAWAIWDPYLAAAELTGGARVLADGEGLVNN-RSFYLAAR-DFAKDNPEAIQIVLEELNKAG 211
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 582714723 248 -FKMNDRKQSVDIMTHHFKQSRDVLTQSAAWTSYGdltIKPSGYQEITTLVKQHHLF 303
Cdd:cd13557  212 eWANTNRDEAAKLLAESLGIDAVVLELAVARRTYG---IIPIDDEIIAAQQAIADTF 265
PBP2_SsuA_like_2 cd13558
Putative substrate binding domain of sulfonate binding protein, the type 2 periplasmic binding ...
65-243 2.64e-06

Putative substrate binding domain of sulfonate binding protein, the type 2 periplasmic binding protein fold; This subfamily includes the periplasmic component of putative ABC-type sulfonate transport system similar to SsuA. These domains are found in eubacterial SsuA proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates, while other closest homologs are involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB). After binding the ligand, SsuA interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The SsuA proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270276  Cd Length: 267  Bit Score: 48.05  E-value: 2.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582714723  65 YKLELVKFNNWPDLMDALNSGRID-----GASTLIELAmkskqKGSNIKAVALGHHEGN--VIMGQKGMHLNEFNNGDDY 137
Cdd:cd13558   26 YKIEWAEFQGGAPLLEALRAGALDiggagDTPPLFAAA-----AGAPIKIVAALRGDVNgqALLVPKDSPIRSVADLKGK 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582714723 138 HFGIPHRYSTHYLLLEELRKQlKIKPGHFSYHEMSPAEMPAALSEHRITGYSVAEPFGALGEKLGKGKTLKHGDDVIPdA 217
Cdd:cd13558  101 RVAYVRGSISHYLLLKALEKA-GLSPSDVELVFLTPADALAAFASGQVDAWATWGPYVARAERRGGARVLVTGEGLIL-G 178
                        170       180
                 ....*....|....*....|....*.
gi 582714723 218 YCCVLVLRGELLDQHKDVAqafVQDY 243
Cdd:cd13558  179 LSFVVAARPALLDPAKRAA---IADF 201
PBP2_ThiY_THI5_like_1 cd13652
Putative substrate binding domain of an ABC-type transporter similar to ThiY/THI5; the type 2 ...
34-246 6.17e-06

Putative substrate binding domain of an ABC-type transporter similar to ThiY/THI5; the type 2 periplasmic binding protein fold; This subfamily is phylogenetically similar to ThiY, which is the periplasmic N-formyl-4-amino-5-(aminomethyl)-2-methylpyrimidine (FAMP) binding component of the ABC transport system (ThiXYZ). FAMP is imported into cell by the transporter, where it is then incorporated into the thiamin biosynthetic pathway. The closest structural homologs of ThiY are THI5, which is responsible for the synthesis of 4-amino-5-(hydroxymethyl)-2-methylpyrimidine phosphate (HMP-P) in the thiamin biosynthetic pathway of eukaryotes, and periplasmic binding proteins involved in alkanesulfonate/nitrate and bicarbonate transport. After binding the ligand, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ThiY/THI5 proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270370 [Multi-domain]  Cd Length: 217  Bit Score: 46.61  E-value: 6.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582714723  34 QQVIKIGYLPITHSANLM--MTKKLLSQYNhpkYKLELVKFNNWPDLMDALNSGRIDGASTLIELA-MKSKQKGSNIKAV 110
Cdd:cd13652    1 TGKVKFGQIPISDFAPVYiaAEKGYFKEEG---LDVEITRFASGAEILAALASGQVDVAGSSPGASlLGALARGADLKIV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582714723 111 ALG-----HHEGNVIMGQKGMHLNEFNNGDDYHFGIPHRYSTHYLLLEELRKQLKIKPGHFSYHEMSPAEMPAALSEHRI 185
Cdd:cd13652   78 AEGlgttpGYGPFAIVVRADSGITSPADLVGKKIAVSTLTNILEYTTNAYLKKNGLDPDKVEFVEVAFPQMVPALENGNV 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 582714723 186 TGYSVAEPFGALGEKLGKGKTLKHGDDVIPDaYCCVLVLRGELLDQHKDVAQAFVQDYKKS 246
Cdd:cd13652  158 DAAVLAEPFLSRARSSGAKVVASDYADPDPH-SQATMVFSADFARENPEVVKKFLRAYLEA 217
COG3888 COG3888
Predicted transcriptional regulator [Transcription];
36-246 1.88e-04

Predicted transcriptional regulator [Transcription];


Pssm-ID: 443096 [Multi-domain]  Cd Length: 328  Bit Score: 42.70  E-value: 1.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582714723  36 VIKIG------YLPIthsanLMMTKKLLSQYnhpkYKLELVKFNNWPDLMDALNSGRID-GAS---TLIELAMKSKqkgs 105
Cdd:COG3888   74 VLRIGilraseYPFL-----LSFVKKLKEKG----IDVEVKVYDNALSLTRDLAEGKIDlALSpliTQLIFSILYR---- 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582714723 106 NIKAVALGHHEGNVIMGQkgmhlnefNNGDDYHFGipHRYSTHYLLLEELRKQLKIKPGHFSYhemSPAEMPAALSEHRI 185
Cdd:COG3888  141 NIKIVGGGASGGSGIVGN--------PSGNGIVGS--SELSSMELWRREFIKRLGLIEIIYFK---SPEELIKSLESGEV 207
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 582714723 186 TGYSVAEPFGALGEKLGKGKTLKHGDDVIPdayCCVLVLRGELldqHKDVAQAFVQDYKKS 246
Cdd:COG3888  208 GYIAIWEPYYSILERNGYKVVFSDLFELEP---CCTLAVNNSL---NSEDLEKIKKIYREA 262
PBP2_ThiY_THI5_like cd13564
Substrate binding domain of ABC-type transporter for thiamin biosynthetic pathway ...
66-246 2.00e-04

Substrate binding domain of ABC-type transporter for thiamin biosynthetic pathway intermediates and similar proteins; the type 2 periplasmic binding protein fold; ThiY is the periplasmic N-formyl-4-amino-5-(aminomethyl)-2-methylpyrimidine (FAMP) binding component of the ABC transport system (ThiXYZ). FAMP is imported into cell by the transporter, where it is then incorporated into the thiamin biosynthetic pathway. The closest structural homologs of ThiY are THI5, which is responsible for the synthesis of 4-amino-5-(hydroxymethyl)-2-methylpyrimidine phosphate (HMP-P) in the thiamin biosynthetic pathway of eukaryotes, and periplasmic binding proteins involved in alkanesulfonate/nitrate and bicarbonate transport. After binding the ligand, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ThiY/THI5 proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270282 [Multi-domain]  Cd Length: 214  Bit Score: 41.72  E-value: 2.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582714723  66 KLELVKFNNWPDLMDALNSGRIDGASTLIELAMKSKQKGSNIKAVA-LGHHEGNVIMGQKGMHLNEFNNGDDYHFGIPHR 144
Cdd:cd13564   32 DVEITTPTGGSDIVQLVASGQFDFGLSAVTHTLVAQSKGVPVKAVAsAIRKPFSGVTVLKDSPIKSPADLKGKKVGYNGL 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582714723 145 YSTHYLLLEELRKQLKIKPGHFSYHEMSPAEMPAALSEHRITGYSVAEPFGALGEKLGKGKTLKHGDDVIPDAYCCVLVL 224
Cdd:cd13564  112 KNINETAVRASVRKAGGDPEDVKFVEVGFDQMPAALDSGQIDAAQGTEPALATLKSQGGDIIASPLVDVAPGDLTVAMLI 191
                        170       180
                 ....*....|....*....|...
gi 582714723 225 RGE-LLDQHKDVAQAFVQDYKKS 246
Cdd:cd13564  192 TNTaYVQQNPEVVKAFQAAIAKA 214
PBPb smart00062
Bacterial periplasmic substrate-binding proteins; bacterial proteins, eukaryotic ones are in ...
65-248 1.35e-03

Bacterial periplasmic substrate-binding proteins; bacterial proteins, eukaryotic ones are in PBPe


Pssm-ID: 214497 [Multi-domain]  Cd Length: 219  Bit Score: 39.23  E-value: 1.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582714723    65 YKLELVKFNnWPDLMDALNSGRID----GASTLIELA---------MKSKQ-----KGSNIKAVAlgHHEGNVIMGQKGm 126
Cdd:smart00062  39 LKVEFVEVS-FDSLLTALKSGKIDvvaaGMTITPERAkqvdfsdpyYRSGQvilvrKDSPIKSLE--DLKGKKVAVVAG- 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582714723   127 hlnefnngddyhfgiphrySTHYLLLEELRKQLKIKPghfsyhEMSPAEMPAALSEHRITGYSVAEPFGALGEKLGKGKT 206
Cdd:smart00062 115 -------------------TTAEELLKKLYPEAKIVS------YDSNAEALAALKAGRADAAVADAPLLAALVKQHGLPE 169
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 582714723   207 LK-HGDDVIPDAYCCVLVLRGEllDQHKDVAQAFVQDYKKSGF 248
Cdd:smart00062 170 LKiVPDPLDTPEGYAIAVRKGD--PELLDKINKALKELKADGT 210
PBP2_SsuA_like_3 cd13559
Putative substrate binding domain of sulfonate binding protein-like, the type 2 periplasmic ...
146-241 1.72e-03

Putative substrate binding domain of sulfonate binding protein-like, the type 2 periplasmic binding protein fold; This subfamily includes the periplasmic component of putative ABC-type sulfonate transport system similar to SsuA. These domains are found in eubacterial SsuA proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates, while other closest homologs are involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB). After binding the ligand, SsuA interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The SsuA proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270277  Cd Length: 258  Bit Score: 39.33  E-value: 1.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582714723 146 STHYLLLEELRKQLKIKPGHFSYHEMSPAEMPAALSEHRITGYSVAEPFGALGEKLGKGKTLKHGDDVIPDAYCCVLVlR 225
Cdd:cd13559  131 SAHGMLLRALDRAGLNPDTDVTIINQAPEVGGSALQANKIDAHADFVPFPELFPHRGIARKLYDGSQTKVPTFHGIVV-D 209
                         90
                 ....*....|....*.
gi 582714723 226 GELLDQHKDVAQAFVQ 241
Cdd:cd13559  210 RDFAEKHPEVVVAYLR 225
Lipoprotein_9 pfam03180
NlpA lipoprotein; This entry represents bacterial lipoproteins that belong to the NlpA family. ...
37-114 3.80e-03

NlpA lipoprotein; This entry represents bacterial lipoproteins that belong to the NlpA family. It contains several antigenic members, that may be involved in bacterial virulence. This entry includes the D-methionine binding lipoprotein MetQ, which is the substrate-binding component of a D-methionine permease, a binding protein-dependent, ATP-driven transport system. Other members of this family, such as NlpA, have been identified as putative substrate-binding components of ABC transporters. NlpA, is an inner-membrane-anchored lipoprotein that has been shown to have a minor role in methionine import.


Pssm-ID: 427184  Cd Length: 236  Bit Score: 38.01  E-value: 3.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582714723   37 IKIGYLPITHSANLMMTKKLLS-QYnhpkYKLELVKFNNWPDLMDALNSGRIDgAS---TLIELAMKSKQKGSNIKAVAL 112
Cdd:pfam03180   1 LKVGATPGPHAEILEVAKPLLKkKG----LDLEIVEFTDYVQPNTALADGEID-ANyfqHLPYLDQFNKEKGLDLVAVGN 75

                  ..
gi 582714723  113 GH 114
Cdd:pfam03180  76 VH 77
 
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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