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Conserved domains on  [gi|152026874|gb|ABS24642|]
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aliphatic sulfonates family ABC transporter, periplsmic ligand-binding protein [Anaeromyxobacter sp. Fw109-5]

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 ...
27-241 3.52e-58

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: 186.63  E-value: 3.52e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874  27 PLRLGYFPNVTHAQALVGVDDGTFARALSgRLETRMFNAGPAAMEALLAGDLDASYVG-PGPAAIAFLRthGEALRVVAG 105
Cdd:cd13553    1 TLRIGYLPITDHAPLLVAKEKGFFEKEGL-DVELVKFPSWADLRDALAAGELDAAHVLaPMPAAATYGK--GAPIKVVAG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874 106 AASGGAALVVK---DARAPKDLAGKRVASPQLGNTQDVALRMWLRQQGLQDARGqgpVEVTPLANPDILALFARGDLAGA 182
Cdd:cd13553   78 LHRNGSAIVVSkdsGIKSVADLKGKTIAVPFPGSTHDVLLRYWLAAAGLDPGKD---VEIVVLPPPDMVAALAAGQIDAY 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 152026874 183 WVPEPWAARLVAEAGGRILVDERSLWPegRFPITVLVVSARALERRRADVIALVRAHLE 241
Cdd:cd13553  155 CVGEPWNARAVAEGVGRVLADSGDIWP--GHPCCVLVVREDFLEENPEAVQALLKALVE 211
 
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 ...
27-241 3.52e-58

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: 186.63  E-value: 3.52e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874  27 PLRLGYFPNVTHAQALVGVDDGTFARALSgRLETRMFNAGPAAMEALLAGDLDASYVG-PGPAAIAFLRthGEALRVVAG 105
Cdd:cd13553    1 TLRIGYLPITDHAPLLVAKEKGFFEKEGL-DVELVKFPSWADLRDALAAGELDAAHVLaPMPAAATYGK--GAPIKVVAG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874 106 AASGGAALVVK---DARAPKDLAGKRVASPQLGNTQDVALRMWLRQQGLQDARGqgpVEVTPLANPDILALFARGDLAGA 182
Cdd:cd13553   78 LHRNGSAIVVSkdsGIKSVADLKGKTIAVPFPGSTHDVLLRYWLAAAGLDPGKD---VEIVVLPPPDMVAALAAGQIDAY 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 152026874 183 WVPEPWAARLVAEAGGRILVDERSLWPegRFPITVLVVSARALERRRADVIALVRAHLE 241
Cdd:cd13553  155 CVGEPWNARAVAEGVGRVLADSGDIWP--GHPCCVLVVREDFLEENPEAVQALLKALVE 211
NMT1_2 pfam13379
NMT1-like family; This family is closely related to the pfam09084 family.
21-249 4.29e-50

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


Pssm-ID: 463863  Cd Length: 254  Bit Score: 167.13  E-value: 4.29e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874   21 AKGPDAPLRLGYFPNVTHAQALVGVDDGTFARalSGR-LETRMFNAGPAAMEALLAGDLDASYVgPGPAAIAFLRTHG-- 97
Cdd:pfam13379   1 GAPEKTSLKLGFIPLTDAAPLIVAAEKGFFAK--YGLtVELSKQASWAETRDALVAGELDAAHV-LTPMPYLITLGIGga 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874   98 -EALRVVAGA---------ASGGAALVVKDARAPKDLAGK--------RVASPQLGNTQDVALRMWLRQQGLQDARgqgP 159
Cdd:pfam13379  78 kVPMIVLASLnlngqaitlANKYADKGVRDAAALKDLVGAykasgkpfKFAVTFPGSTHDLWLRYWLAAGGLDPDA---D 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874  160 VEVTPLANPDILALFARGDLAGAWVPEPWAARLVAEAGGRILVDERSLWPEgrFPITVLVVSARALERRRADVIALVRAH 239
Cdd:pfam13379 155 VKLVVVPPPQMVANLRAGNIDGFCVGEPWNARAVAEGIGVTAATTGELWKD--HPEKVLGVRADWVDKNPNAARALVKAL 232
                         250
                  ....*....|
gi 152026874  240 LELTRRWEAD 249
Cdd:pfam13379 233 IEATRWLDAK 242
SsuA_fam TIGR01728
ABC transporter, substrate-binding protein, aliphatic sulfonates family; Members of this ...
28-319 4.01e-41

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: 144.81  E-value: 4.01e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874   28 LRLGYFPNvTHAQALVGVDDGTFARALSG-RLETRMFNAGPAAMEALLAGDLDASYVGPGPAaiAFLRTHGEALRVVAGA 106
Cdd:TIGR01728   1 VRIGYQKN-GHSALALAKEKGLLEKELGKtKVEWVEFPAGPPALEALGAGSLDFGYIGPGPA--LFAYAAGADIKAVGLV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874  107 ASGGAALVVKDARAP----KDLAGKRVASPQLGNTQDVALRMwLRQQGLqdarGQGPVEVTPLANPDILALFARGDLAGA 182
Cdd:TIGR01728  78 SDNKATAIVVIKGSPirtvADLKGKRIAVPKGGSGHDLLLRA-LLKAGL----SGDDVTILYLGPSDARAAFAAGQVDAW 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874  183 WVPEPWAARLVAEAGGRILVDERSLWpeGRFPITVLVVSARALERRRADVIALVRAHLELTRRWEADRaafaRLANAAYG 262
Cdd:TIGR01728 153 AIWEPWGSALVEEGGARVLANGEGIG--LPGQPGFLVVRREFAEAHPEQVQRVLKVLVKARKWAEENP----EESAKILA 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 152026874  263 KRAG---KALPDAVLLDALSRVEPVSDPLPRQLERMARDAQELGFAPKG-DPSGIVDATML 319
Cdd:TIGR01728 227 KELGlsqAVVEETVLNRRFLRVEVISDAVVDALQAMADFFYAAGLLKKKpDLKDAVDRSFL 287
TauA COG0715
ABC-type nitrate/sulfonate/bicarbonate transport system, periplasmic component [Inorganic ion ...
17-307 4.37e-41

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


Pssm-ID: 440479 [Multi-domain]  Cd Length: 297  Bit Score: 144.76  E-value: 4.37e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874  17 GCSRAKGPDAP--LRLGYFPNVTHAQALVGVDDGTFARAlsG-RLETRMFNAGPAAMEALLAGDLDASYVGPGPAAIAfl 93
Cdd:COG0715   11 ACSAAAAAAEKvtLRLGWLPNTDHAPLYVAKEKGYFKKE--GlDVELVEFAGGAAALEALAAGQADFGVAGAPPALAA-- 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874  94 RTHGEALRVV-AGAASGGAALVVKDA---RAPKDLAGKRVASPQlGNTQDVALRMWLRQQGLQDARgqgpVEVTPLANPD 169
Cdd:COG0715   87 RAKGAPVKAVaALSQSGGNALVVRKDsgiKSLADLKGKKVAVPG-GSTSHYLLRALLAKAGLDPKD----VEIVNLPPPD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874 170 ILALFARGDLAGAWVPEPWAARLVAEAGGRILVDERSLWPegRFPITVLVVSARALERRRADVIALVRAHLELTRRWEAD 249
Cdd:COG0715  162 AVAALLAGQVDAAVVWEPFESQAEKKGGGRVLADSADLVP--GYPGDVLVASEDFLEENPEAVKAFLRALLKAWAWAAAN 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 152026874 250 RAAFARLANAAYGkragkaLPDAVLLDALSR----VEPVSDPLPRQLERMARDAQELGFAPK 307
Cdd:COG0715  240 PDEAAAILAKATG------LDPEVLAAALEGdlrlDPPLGAPDPARLQRVADFLVELGLLPK 295
tauA PRK11480
taurine transporter substrate binding subunit; Provisional
41-241 6.16e-13

taurine transporter substrate binding subunit; Provisional


Pssm-ID: 183158  Cd Length: 320  Bit Score: 68.48  E-value: 6.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874  41 ALVGVDDGTFARALSGRLETRMFNAGPAAMEALLAGDLDASYVGPGPAAIAFLRTHGEALRVVAGAASGGAALVV-KDAR 119
Cdd:PRK11480  36 AKVAQADNTFAKESGATVDWRKFDSGASIVRALASGDVQIGNLGSSPLAVAASQQVPIEVFLLASKLGNSEALVVkKTIS 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874 120 APKDLAGKRVASPQLGNTQdVALRMWLRQQGLQdargQGPVEVTPLANPDILALFARGDLAGAWVPEPWAARLvaEAGGR 199
Cdd:PRK11480 116 KPEDLIGKRIAVPFISTTH-YSLLAALKHWGIK----PGQVEIVNLQPPAIIAAWQRGDIDGAYVWAPAVNAL--EKDGK 188
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 152026874 200 ILVDERSLWPEGRFPITVLVVSARALERRRADVIALVRAHLE 241
Cdd:PRK11480 189 VLTDSEQVGQWGAPTLDVWVVRKDFAEKHPEVVKAFAKSAID 230
 
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 ...
27-241 3.52e-58

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: 186.63  E-value: 3.52e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874  27 PLRLGYFPNVTHAQALVGVDDGTFARALSgRLETRMFNAGPAAMEALLAGDLDASYVG-PGPAAIAFLRthGEALRVVAG 105
Cdd:cd13553    1 TLRIGYLPITDHAPLLVAKEKGFFEKEGL-DVELVKFPSWADLRDALAAGELDAAHVLaPMPAAATYGK--GAPIKVVAG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874 106 AASGGAALVVK---DARAPKDLAGKRVASPQLGNTQDVALRMWLRQQGLQDARGqgpVEVTPLANPDILALFARGDLAGA 182
Cdd:cd13553   78 LHRNGSAIVVSkdsGIKSVADLKGKTIAVPFPGSTHDVLLRYWLAAAGLDPGKD---VEIVVLPPPDMVAALAAGQIDAY 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 152026874 183 WVPEPWAARLVAEAGGRILVDERSLWPegRFPITVLVVSARALERRRADVIALVRAHLE 241
Cdd:cd13553  155 CVGEPWNARAVAEGVGRVLADSGDIWP--GHPCCVLVVREDFLEENPEAVQALLKALVE 211
NMT1_2 pfam13379
NMT1-like family; This family is closely related to the pfam09084 family.
21-249 4.29e-50

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


Pssm-ID: 463863  Cd Length: 254  Bit Score: 167.13  E-value: 4.29e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874   21 AKGPDAPLRLGYFPNVTHAQALVGVDDGTFARalSGR-LETRMFNAGPAAMEALLAGDLDASYVgPGPAAIAFLRTHG-- 97
Cdd:pfam13379   1 GAPEKTSLKLGFIPLTDAAPLIVAAEKGFFAK--YGLtVELSKQASWAETRDALVAGELDAAHV-LTPMPYLITLGIGga 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874   98 -EALRVVAGA---------ASGGAALVVKDARAPKDLAGK--------RVASPQLGNTQDVALRMWLRQQGLQDARgqgP 159
Cdd:pfam13379  78 kVPMIVLASLnlngqaitlANKYADKGVRDAAALKDLVGAykasgkpfKFAVTFPGSTHDLWLRYWLAAGGLDPDA---D 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874  160 VEVTPLANPDILALFARGDLAGAWVPEPWAARLVAEAGGRILVDERSLWPEgrFPITVLVVSARALERRRADVIALVRAH 239
Cdd:pfam13379 155 VKLVVVPPPQMVANLRAGNIDGFCVGEPWNARAVAEGIGVTAATTGELWKD--HPEKVLGVRADWVDKNPNAARALVKAL 232
                         250
                  ....*....|
gi 152026874  240 LELTRRWEAD 249
Cdd:pfam13379 233 IEATRWLDAK 242
SsuA_fam TIGR01728
ABC transporter, substrate-binding protein, aliphatic sulfonates family; Members of this ...
28-319 4.01e-41

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: 144.81  E-value: 4.01e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874   28 LRLGYFPNvTHAQALVGVDDGTFARALSG-RLETRMFNAGPAAMEALLAGDLDASYVGPGPAaiAFLRTHGEALRVVAGA 106
Cdd:TIGR01728   1 VRIGYQKN-GHSALALAKEKGLLEKELGKtKVEWVEFPAGPPALEALGAGSLDFGYIGPGPA--LFAYAAGADIKAVGLV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874  107 ASGGAALVVKDARAP----KDLAGKRVASPQLGNTQDVALRMwLRQQGLqdarGQGPVEVTPLANPDILALFARGDLAGA 182
Cdd:TIGR01728  78 SDNKATAIVVIKGSPirtvADLKGKRIAVPKGGSGHDLLLRA-LLKAGL----SGDDVTILYLGPSDARAAFAAGQVDAW 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874  183 WVPEPWAARLVAEAGGRILVDERSLWpeGRFPITVLVVSARALERRRADVIALVRAHLELTRRWEADRaafaRLANAAYG 262
Cdd:TIGR01728 153 AIWEPWGSALVEEGGARVLANGEGIG--LPGQPGFLVVRREFAEAHPEQVQRVLKVLVKARKWAEENP----EESAKILA 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 152026874  263 KRAG---KALPDAVLLDALSRVEPVSDPLPRQLERMARDAQELGFAPKG-DPSGIVDATML 319
Cdd:TIGR01728 227 KELGlsqAVVEETVLNRRFLRVEVISDAVVDALQAMADFFYAAGLLKKKpDLKDAVDRSFL 287
TauA COG0715
ABC-type nitrate/sulfonate/bicarbonate transport system, periplasmic component [Inorganic ion ...
17-307 4.37e-41

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


Pssm-ID: 440479 [Multi-domain]  Cd Length: 297  Bit Score: 144.76  E-value: 4.37e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874  17 GCSRAKGPDAP--LRLGYFPNVTHAQALVGVDDGTFARAlsG-RLETRMFNAGPAAMEALLAGDLDASYVGPGPAAIAfl 93
Cdd:COG0715   11 ACSAAAAAAEKvtLRLGWLPNTDHAPLYVAKEKGYFKKE--GlDVELVEFAGGAAALEALAAGQADFGVAGAPPALAA-- 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874  94 RTHGEALRVV-AGAASGGAALVVKDA---RAPKDLAGKRVASPQlGNTQDVALRMWLRQQGLQDARgqgpVEVTPLANPD 169
Cdd:COG0715   87 RAKGAPVKAVaALSQSGGNALVVRKDsgiKSLADLKGKKVAVPG-GSTSHYLLRALLAKAGLDPKD----VEIVNLPPPD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874 170 ILALFARGDLAGAWVPEPWAARLVAEAGGRILVDERSLWPegRFPITVLVVSARALERRRADVIALVRAHLELTRRWEAD 249
Cdd:COG0715  162 AVAALLAGQVDAAVVWEPFESQAEKKGGGRVLADSADLVP--GYPGDVLVASEDFLEENPEAVKAFLRALLKAWAWAAAN 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 152026874 250 RAAFARLANAAYGkragkaLPDAVLLDALSR----VEPVSDPLPRQLERMARDAQELGFAPK 307
Cdd:COG0715  240 PDEAAAILAKATG------LDPEVLAAALEGdlrlDPPLGAPDPARLQRVADFLVELGLLPK 295
PBP2_NrtA_SsuA_CpmA_like cd01008
Substrate binding domain of ABC-type nitrate/sulfonate/bicarbonate transporters, a member of ...
27-241 3.16e-23

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: 95.43  E-value: 3.16e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874  27 PLRLGYFPNVTHAQALVGVDDGTFARALSG-RLETRMFNAGPAAMEALLAGDLDASYVGPGPAAIAflRTHGEALRVVAG 105
Cdd:cd01008    1 TVRIGYQAGPLAGPLIVAKEKGLFEKEKEGiDVEWVEFTSGPPALEALAAGSLDFGTGGDTPALLA--AAGGVPVVLIAA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874 106 AASGGAA--LVVKDA---RAPKDLAGKRVASPQlGNTQDVALRMWLRQQGLQDargqGPVEVTPLANPDILALFARGDLA 180
Cdd:cd01008   79 LSRSPNGngIVVRKDsgiTSLADLKGKKIAVTK-GTTGHFLLLKALAKAGLSV----DDVELVNLGPADAAAALASGDVD 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 152026874 181 GAWVPEPWAARLVAEAGGRILVDERSLWPEgrfPITVLVVSARALERRRADVIALVRAHLE 241
Cdd:cd01008  154 AWVTWEPFLSLAEKGGDARIIVDGGGLPYT---DPSVLVARRDFVEENPEAVKALLKALVE 211
PBP2_taurine cd13560
Taurine-binding periplasmic protein; the type 2 periplasmic binding protein fold; This ...
27-207 2.16e-22

Taurine-binding periplasmic 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: 270278 [Multi-domain]  Cd Length: 218  Bit Score: 93.14  E-value: 2.16e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874  27 PLRLGYF--PNVthaqALVGVDDGTFARALSGRLETRMFNAGPAAMEALLAGDLDASYVGPGPAAIAFLRthGEALRV-- 102
Cdd:cd13560    1 EIRIGYQtvPNP----QLVAKADGLLEKALGVKVNWRKFDSGADVNAAMASGSIDIGLLGSPPAAVAIAA--GLPIEViw 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874 103 VAGAASGGAALVVKDA---RAPKDLAGKRVASPqLGNTQDVALRMWLRQQGLQdargQGPVEVTPLANPDILALFARGDL 179
Cdd:cd13560   75 IADVIGDAEALVVRKGsgiKSLKDLAGKKVAVP-FGSTAHYSLLAALKHAGVD----PGKVKILDMQPPEIVAAWQRGDI 149
                        170       180
                 ....*....|....*....|....*...
gi 152026874 180 AGAWVPEPWAARLVAEagGRILVDERSL 207
Cdd:cd13560  150 DAAYVWEPALSQLKKN--GKVLLSSKDL 175
TauA COG4521
ABC-type taurine transport system, periplasmic component [Inorganic ion transport and ...
17-249 1.57e-20

ABC-type taurine transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 443595 [Multi-domain]  Cd Length: 332  Bit Score: 90.32  E-value: 1.57e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874  17 GCSRAKGPDA---PLRLGY--FPNVthaqALVGVDDGTFARALSGRLETRMFNAGPAAMEALLAGDLDASYVGPGPAAIA 91
Cdd:COG4521   16 GCALAAAAAAaakEVTIGYqtIPNP----ELVAKADGALEKALGAKVNWRKFDSGADVITALASGDVDIGSIGSSPFAAA 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874  92 FlrTHGEALRVVAGAASGGA--ALVVKDAR---APKDLAGKRVASPqLGNTQDVALRMWLRQQGLQDARgqgpVEVTPLA 166
Cdd:COG4521   92 L--SRGLPIEVIWIADVIGDaeALVVRNGSgitSPKDLKGKKIAVP-FGSTSHYSLLAALKHAGIDPSD----VTILNMQ 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874 167 NPDILALFARGDLAGAWVPEPWAARLVAEagGRILVDERSLWPEGRFPITVLVVSARALERRRADVIALVRAHLELTRRW 246
Cdd:COG4521  165 PPEIAAAWQRGDIDAAYVWDPALSELKKS--GKVLITSAELAKWGAPTFDVWVVRKDFAEENPDFVAAFLKVLADAVADY 242

                 ...
gi 152026874 247 EAD 249
Cdd:COG4521  243 RAD 245
PBP2_ThiY_THI5_like_1 cd13652
Putative substrate binding domain of an ABC-type transporter similar to ThiY/THI5; the type 2 ...
27-241 2.19e-17

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: 79.35  E-value: 2.19e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874  27 PLRLGYFPNVTHAQALVGVDDGtFARALSGRLETRMFNAGPAAMEALLAGDLDASYVGPGPAAIAfLRTHGEALRVVAGA 106
Cdd:cd13652    3 KVKFGQIPISDFAPVYIAAEKG-YFKEEGLDVEITRFASGAEILAALASGQVDVAGSSPGASLLG-ALARGADLKIVAEG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874 107 ASGGAA------LVVKDA--RAPKDLAGKRVASPQLGNTQDVALRMWLRQQGLQDARgqgpVEVTPLANPDILALFARGD 178
Cdd:cd13652   81 LGTTPGygpfaiVVRADSgiTSPADLVGKKIAVSTLTNILEYTTNAYLKKNGLDPDK----VEFVEVAFPQMVPALENGN 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 152026874 179 LAGAWVPEPWAARLVAEAGGRILVDERSLWPEgrfPITVLVVSARALERRRADVIALVRAHLE 241
Cdd:cd13652  157 VDAAVLAEPFLSRARSSGAKVVASDYADPDPH---SQATMVFSADFARENPEVVKKFLRAYLE 216
PBP2_SsuA_like_4 cd13561
Putative substrate binding domain of sulfonate binding protein-like, the type 2 periplasmic ...
27-241 9.86e-15

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: 270279 [Multi-domain]  Cd Length: 212  Bit Score: 72.02  E-value: 9.86e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874  27 PLRLGYFPNV-THAQALVGVDDGTFArALSGRLETRMFNAGPAAMEALLAGDLDASYVGPGPAAIAfLRTHGEALRVVAG 105
Cdd:cd13561    1 PIRIGYLPALaVAGPIFIAKEKGLFA-KHGLDPDFIEFTSGPPLVAALGSGSLDVGYTGPVAFNLP-ASGQAKVVLINNL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874 106 AASGGAALVVKDA--RAPKDLAGKRVASPQlGNTQDVALRMWLRQQGLQdargQGPVEVTPLANPDILALFARG--DLAG 181
Cdd:cd13561   79 ENATASLIVRADSgiASIADLKGKKIGTPS-GTTADVALDLALRKAGLS----EKDVQIVNMDPAEIVTAFTSGsvDAAA 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874 182 AWVPEPWAARLVAEaGGRILVDERSLWPEGRFPITvLVVSARALERRRADVIALVRAHLE 241
Cdd:cd13561  154 LWAPNTATIKEKVP-GAVELADNSDFGPDAAVPGA-WVARNKYAEENPEELKKFLAALAE 211
tauA PRK11480
taurine transporter substrate binding subunit; Provisional
41-241 6.16e-13

taurine transporter substrate binding subunit; Provisional


Pssm-ID: 183158  Cd Length: 320  Bit Score: 68.48  E-value: 6.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874  41 ALVGVDDGTFARALSGRLETRMFNAGPAAMEALLAGDLDASYVGPGPAAIAFLRTHGEALRVVAGAASGGAALVV-KDAR 119
Cdd:PRK11480  36 AKVAQADNTFAKESGATVDWRKFDSGASIVRALASGDVQIGNLGSSPLAVAASQQVPIEVFLLASKLGNSEALVVkKTIS 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874 120 APKDLAGKRVASPQLGNTQdVALRMWLRQQGLQdargQGPVEVTPLANPDILALFARGDLAGAWVPEPWAARLvaEAGGR 199
Cdd:PRK11480 116 KPEDLIGKRIAVPFISTTH-YSLLAALKHWGIK----PGQVEIVNLQPPAIIAAWQRGDIDGAYVWAPAVNAL--EKDGK 188
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 152026874 200 ILVDERSLWPEGRFPITVLVVSARALERRRADVIALVRAHLE 241
Cdd:PRK11480 189 VLTDSEQVGQWGAPTLDVWVVRKDFAEKHPEVVKAFAKSAID 230
PBP2_SsuA_like_2 cd13558
Putative substrate binding domain of sulfonate binding protein, the type 2 periplasmic binding ...
57-303 4.18e-12

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: 65.38  E-value: 4.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874  57 RLETRMFNAGPAAMEALLAGDLDASYVGPGPAaiAFLRTHGEALRVVAGAASGGAA---LVVKDA--RAPKDLAGKRVAS 131
Cdd:cd13558   27 KIEWAEFQGGAPLLEALRAGALDIGGAGDTPP--LFAAAAGAPIKIVAALRGDVNGqalLVPKDSpiRSVADLKGKRVAY 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874 132 PQLGNTQDVALRMwLRQQGLqdarGQGPVEVTPLANPDILALFARGDLAGAWVPEPWAARLVAEAGGRILVDERSLWPeg 211
Cdd:cd13558  105 VRGSISHYLLLKA-LEKAGL----SPSDVELVFLTPADALAAFASGQVDAWATWGPYVARAERRGGARVLVTGEGLIL-- 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874 212 rfPITVLVVSARALE-RRRADVIALVRAHLELTRRW-EADRAAFARLANAAYGKRAGKALpdAVLLDALSRVEPVSDPLP 289
Cdd:cd13558  178 --GLSFVVAARPALLdPAKRAAIADFLARLARAQAWaNAHPDEWAKAYAAETGLPPEVAA--AIFARRSAPVVPIDAQVI 253
                        250
                 ....*....|....
gi 152026874 290 RQLERMARDAQELG 303
Cdd:cd13558  254 ASQQQTADTFHEAG 267
PBP2_SsuA_like_6 cd13563
Putative substrate binding domain of sulfonate binding protein-like, a member of the type 2 ...
27-241 1.61e-11

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: 62.64  E-value: 1.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874  27 PLRLGYFPNVTHAQALVGVDDGTFARALSgRLETRMFNAGPAAMEALLAGDLDAsyvgpgpAAIaflrTHGEALRVVAGA 106
Cdd:cd13563    1 PLKIGISTWPGYGPWYLADEKGFFKKEGL-DVELVWFESYSDSMAALASGQIDA-------AAT----TLDDALAMAAKG 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874 107 ASGGAALVV------------KDARAPKDLAGKRVASpQLGNTQDVALRMWLRQQGLQDARgqgpVEVTPLANPDILALF 174
Cdd:cd13563   69 VPVKIVLVLdnsngadgivakPGIKSIADLKGKTVAV-EEGSVSHFLLLNALEKAGLTEKD----VKIVNMTAGDAGAAF 143
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 152026874 175 ARGDL--AGAWvpEPWAARLVAEAGGRILVDERSlwpegrFP--IT-VLVVSARALERRRADVIALVRAHLE 241
Cdd:cd13563  144 IAGQVdaAVTW--EPWLSNALKRGKGKVLVSSAD------TPglIPdVLVVREDFIKKNPEAVKAVVKAWFD 207
PBP2_SsuA cd13557
Substrate binding domain of sulfonate binding protein, a member of the type 2 periplasmic ...
56-307 2.21e-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: 60.38  E-value: 2.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874  56 GRLETRM-----------FNAGPAAMEALLAGDLDASYVGPGPAaiAFLRTHGEALRVVAGAASGGAA---LVVKDA--R 119
Cdd:cd13557   19 GELEKRLkplgvkvtwseFPAGPQLLEALNVGSIDFGSTGDTPP--IFAQAAGAPLVYVAVEPPTPKGeaiLVPKDSpiK 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874 120 APKDLAGKRVASPQLGNTQDVALRMwLRQQGLQdargQGPVEVTPLANPDILALFARGDLaGAWVP-EPWAARLVAEAGG 198
Cdd:cd13557   97 TVADLKGKKIAFQKGSSAHYLLVKA-LEKAGLT----LDDIEPVYLSPADARAAFEQGQV-DAWAIwDPYLAAAELTGGA 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874 199 RILVDERSLWPEGRFpitvlVVSARALERRRADVIALVRAHLELTRRW-EADRAAFARLANAAYGkragkaLPDAVLLDA 277
Cdd:cd13557  171 RVLADGEGLVNNRSF-----YLAARDFAKDNPEAIQIVLEELNKAGEWaNTNRDEAAKLLAESLG------IDAVVLELA 239
                        250       260       270
                 ....*....|....*....|....*....|....
gi 152026874 278 LSR----VEPVSDPLPRQLERMARDAQELGFAPK 307
Cdd:cd13557  240 VARrtygIIPIDDEIIAAQQAIADTFYDLGLIPK 273
PBP2_DszB cd13554
Substrate binding domain of 2'-hydroxybiphenyl-2-sulfinate desulfinase, a member of the type 2 ...
28-250 7.97e-09

Substrate binding domain of 2'-hydroxybiphenyl-2-sulfinate desulfinase, a member of the type 2 periplasmic binding fold superfamily; This subfamily includes DszB, which converts 2'-hydroxybiphenyl-2-sulfinate to 2-hydroxybiphenyl and sulfinate at the rate-limiting step of the microbial dibenzothiophene desulfurization pathway. The overall fold of DszB is highly similar to those of periplasmic substrate-binding proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates. 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. The DszB protein belongs 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: 270272 [Multi-domain]  Cd Length: 246  Bit Score: 55.21  E-value: 7.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874  28 LRLGYFPNVthaQALVGVDDGTFARALSGRLETRMFN-AGPAAMEALLAGDLDASYVGPGPAAIAFLRTHGEALRV--VA 104
Cdd:cd13554    3 LRYSNCPVP---NALLTAEESGYLDAAGIDLEVVAGTpTGTVDFTYDQGIPADVVFSGAIPPLLAEGLRAPGRTRLigIT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874 105 GAASGGAALVVKD---ARAPKDLAGKRVASPQLGntqdvALRMWLRQQGLQ-DARGQGPVEVTPLANP--DILALFARGD 178
Cdd:cd13554   80 PLDLGRQGLFVRAdspITSAADLEGKRIGMSAGA-----IRGSWLARALLHnLEIGGLDVEIVPIDSPgrGQAAALDSGD 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 152026874 179 LAGAWVPEPWAARLVAEAGGRILVDERSLwpEGRFPITVLVVSARALERRRADVIALVRAHLELTRRWEADR 250
Cdd:cd13554  155 IDALASWLPWATTLQATGGARPLVDLGLV--EGNSYYSTWTVRSDFIEQNPEAVKALVEALVRAGDWIQAHP 224
PBP2_SsuA_like_5 cd13562
Putative substrate binding domain of sulfonate binding protein-like, the type 2 periplasmic ...
28-203 8.13e-08

Putative substrate binding domain of sulfonate binding protein-like, the type 2 periplasmic binding protein fold; This subfamily includes sulfonate binding domains 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: 270280 [Multi-domain]  Cd Length: 215  Bit Score: 52.12  E-value: 8.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874  28 LRLGYFPNVTHAQALVGVDDGTFARALSGRL-----ETRMFNAGPAAMEALLAGDLDASYVGPGPAAIAflRTHGEALRV 102
Cdd:cd13562    2 IRIGFQPIPPYAPILVAKQKGWLEEELKKAGadvgvKWSQFSAGPPVNEAFAAGELDVGLLGDTPAIIG--RAAGQDTRI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874 103 VAGAASGGAAL---VVKDA--RAPKDLAGKRVASPQLGNTQDVaLRMWLRQQGLQdargQGPVEVTPLANPDILALFARG 177
Cdd:cd13562   80 VGLASTGPKALalvVRKDSaiKSVKDLKGKKVATTKGSYVHHL-LVLVLQEAGLT----IDDVEFINMQQADMNTALTNG 154
                        170       180
                 ....*....|....*....|....*.
gi 152026874 178 DLAGAWVPEPWAARLVAEAGGRILVD 203
Cdd:cd13562  155 DIDAAVIWEPLITKLLSDGVVRVLRD 180
PhnD COG3221
ABC-type phosphate/phosphonate transport system, periplasmic component [Inorganic ion ...
67-234 2.95e-06

ABC-type phosphate/phosphonate transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 442454 [Multi-domain]  Cd Length: 250  Bit Score: 47.61  E-value: 2.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874  67 PAAMEALLAGDLDASYVGPGPAAIAFLRTHGEAL--RVVAGAASGGAALVVK---DARAPKDLAGKRVASPQLGNTQ-DV 140
Cdd:COG3221   38 AALIEALRAGQVDLAFLGPLPYVLARDRAGAEPLatPVRDGSPGYRSVIIVRadsPIKSLEDLKGKRFAFGDPDSTSgYL 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874 141 ALRMWLRQQGLQDARgqGPVEVTPLANPD--ILALfARGDLAGAWVPEPWAARLVAEagGRILVDERSLWPEGRFPITVL 218
Cdd:COG3221  118 VPRALLAEAGLDPER--DFSEVVFSGSHDavILAV-ANGQADAGAVDSGVLERLVEE--GPDADQLRVIWESPPIPNDPF 192
                        170
                 ....*....|....*.
gi 152026874 219 VVSARALERRRADVIA 234
Cdd:COG3221  193 VARPDLPPELREKIRE 208
PBP2_sulfate_ester_like cd13555
Sulfate ester binding protein-like, the type 2 periplasmic binding protein fold; This ...
64-249 1.20e-04

Sulfate ester 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: 270273  Cd Length: 268  Bit Score: 43.09  E-value: 1.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874  64 NAGPAAMEALLAGDLDASYVGPGPAAIafLRTHGEALRVVAGAASGG-AALVVK---DARAPKDLAGKRVASPQLGNTQD 139
Cdd:cd13555   48 GAGPAVNEAFANGQIDFAVYGDLPAII--GRAAGLDTKLLLSSGSGNnAYLVVPpdsTIKSVKDLKGKKVAVQKGTAWQL 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874 140 VALRMwLRQQGLQDARgqgpVEVTPLANPDILALFARGDLAGAWVPEPWAArLVAEAGGRILVDERSLwPEGRFPITVLV 219
Cdd:cd13555  126 TFLRI-LAKNGLSEKD----FKIVNLDAQDAQAALASGDVDAAFTGYEALK-LEDQGAGKIIWSTKDK-PEDWTTQSGVW 198
                        170       180       190
                 ....*....|....*....|....*....|
gi 152026874 220 VSArALERRRADVIALVRAHLELTRRWEAD 249
Cdd:cd13555  199 ART-DFIKENPDVVQRIVTALVKAARWVSQ 227
PBP2_peptides_like cd13530
Peptide-binding protein and related homologs; type 2 periplasmic binding protein fold; This ...
43-103 4.48e-04

Peptide-binding protein and related homologs; type 2 periplasmic binding protein fold; This domain is found in solute binding proteins that serve as initial receptors in the ABC transport, signal transduction and channel gating. The PBP2 proteins share the same architecture as periplasmic binding proteins type 1, but have a different topology. They are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can 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. Besides transport proteins, the family includes ionotropic glutamate receptors and unorthodox sensor proteins involved in signal transduction.


Pssm-ID: 270248 [Multi-domain]  Cd Length: 217  Bit Score: 40.70  E-value: 4.48e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 152026874  43 VGVDDGT----FARALSGRLETRMFNAGPAAMEALLAGDLDAsYVGPGPAAIAFLRTHGEALRVV 103
Cdd:cd13530  110 VGVQAGTtgedYAKKNLPNAEVVTYDNYPEALQALKAGRIDA-VITDAPVAKYYVKKNGPDLKVV 173
Periplasmic_Binding_Protein_Type_2 cd00648
Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent ...
71-217 9.43e-04

Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent the ligand-binding domains found in solute binding proteins that serve as initial receptors in the transport, signal transduction and channel gating. The PBP2 proteins share the same architecture as periplasmic binding proteins type 1 (PBP1), but have a different topology. They are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The origin of PBP module can be traced across the distant phyla, including eukaryotes, archebacteria, and prokaryotes. The majority of PBP2 proteins are involved in the uptake of a variety of soluble substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. After binding their specific ligand with high affinity, they can 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. Besides transport proteins, the family includes ionotropic glutamate receptors and unorthodox sensor proteins involved in signal transduction. The substrate binding domain of the LysR transcriptional regulators and the oligopeptide-like transport systems also contain the type 2 periplasmic binding fold and thus they are significantly homologous to that of the PBP2; however, these two families are grouped into a separate hierarchy of the PBP2 superfamily due to the large number of protein sequences.


Pssm-ID: 270214 [Multi-domain]  Cd Length: 196  Bit Score: 39.86  E-value: 9.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874  71 EALLAGDLDASYVGPGPA-AIAFLRTHGEALRVVAGAASGGAALVV------KDARAPKDLAGKRVASPQLGNTQDVALR 143
Cdd:cd00648   44 EALAAGDADVAVGPIAPAlEAAADKLAPGGLYIVPELYVGGYVLVVrkgssiKGLLAVADLDGKRVGVGDPGSTAVRQAR 123
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 152026874 144 MWLRQQGLQDARgqgpVEVTPLANPD-ILALFARGDLAGAWVPEPWAARLVAEAGGRILVDERSLWPEGRFPITV 217
Cdd:cd00648  124 LALGAYGLKKKD----PEVVPVPGTSgALAAVANGAVDAAIVWVPAAERAQLGNVQLEVLPDDLGPLVTTFGVAV 194
Phosphonate-bd pfam12974
ABC transporter, phosphonate, periplasmic substrate-binding protein; This is a family of ...
30-223 1.21e-03

ABC transporter, phosphonate, periplasmic substrate-binding protein; This is a family of periplasmic proteins which are part of the transport system for alkylphosphonate uptake.


Pssm-ID: 432911 [Multi-domain]  Cd Length: 243  Bit Score: 39.94  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874   30 LGYFPNVTHAQALVGVDDgtFARALSGRL----ETRMFNAGPAAMEALLAGDLDASYVGPGPAAIAFLRTHGEALRVVAG 105
Cdd:pfam12974   1 FGVLPDESPDELKARYQP--LADYLSEELgvpvELVVATDYAAVVEALRAGQVDIAYFGPLAYVQAVDRAGAEPLATPVE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874  106 AASGGA---ALVVK---DARAPKDLAGKRVASPQLGNTQD--VALRMWLRQQGLQDARGQGPVEVtplANPD--ILALfA 175
Cdd:pfam12974  79 PDGSAGyrsVIIVRkdsPIQSLEDLKGKTVAFGDPSSTSGylVPLALLFAEAGLDPEDDFKPVFS---GSHDavALAV-L 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 152026874  176 RGDLAGAWVPEPWAARLVAEagGRILVDE-RSLWPEGRFPITVLVVSAR 223
Cdd:pfam12974 155 NGDADAGAVNSEVLERLVAE--GPIDRDQlRVIAESPPIPNDPLVARPD 201
Imp COG2358
TRAP-type uncharacterized transport system, periplasmic component [General function prediction ...
65-201 2.73e-03

TRAP-type uncharacterized transport system, periplasmic component [General function prediction only];


Pssm-ID: 441925 [Multi-domain]  Cd Length: 303  Bit Score: 39.06  E-value: 2.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152026874  65 AGPAAMEALLAGDLDASYVGPGPAAIAFlrtHGEA---------LRVVAGAASGGAALVV-KDA--RAPKDLAGKRVASP 132
Cdd:COG2358   52 GSVENLRLLRAGEADLAIVQSDVAYDAY---NGTGpfeggpldnLRALASLYPEPVHLVVrADSgiKSLADLKGKRVSVG 128
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 152026874 133 QLGNTQDVALRMWLRQQGLqdarGQGPVEVTPLANPDILALFARGDLAGAW----VPEPWAARLVAEAGGRIL 201
Cdd:COG2358  129 PPGSGTEVTAERLLEAAGL----TYDDVKVEYLGYGEAADALKDGQIDAAFfvagLPTGAVTELAATTDIRLL 197
 
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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