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Conserved domains on  [gi|2505195663|ref|WP_282568615|]
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substrate-binding domain-containing protein [Bosea sp. 124]

Protein Classification

AcfC family protein( domain architecture ID 10790690)

AcfC family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AcfC COG4588
Accessory colonization factor AcfC, contains ABC-type periplasmic domain [Cell wall/membrane ...
 2-226 1.18e-120

Accessory colonization factor AcfC, contains ABC-type periplasmic domain [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 443645  Cd Length: 232  Bit Score: 342.34  E-value: 1.18e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505195663   2 RVYGPGGPMPAMKEAAATFGRAQGIEVQVEAGPLPAWKDKATKDADTIFSGFEVMMSDFIEALPD-IDPSTVQPLYLRAS 80
Cdd:COG4588     7 NVYGPGGPAPALKEAAEAFEKKTGVKVEVTAGPTPKWIDKAKKNADIIFGGSEQMMTAFAEAYPGaFDSKDVEPLYLRPA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505195663  81 AILVRPGNPKTIGGAKALLEPGHRILVVNGAGQQGLWEDVAGRLGRIADVKAFRSNIAKVAKNSADARKAWVEDSSLDAW 160
Cdd:COG4588    87 AILVRPGNPKNIKGFEDLLKPGVKIVVVNGAGQTGVWEDIAGRTGDIETVQAFRSNIVAYAPNSGAARKAWTQDPDIDAW 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2505195663 161 LIWTIWQVANPTLADVVEVEPDLRIYRDTGIALTKRGQMRPEAKRLVEFLASAEGQHNFVKWGWMR 226
Cdd:COG4588   167 ITWNIWQKANPDLADLVEIEPDYRIYRDTNVALTKKGKADAEAQAFVDFLKSPEAQAIFKKWGWKR 232
 
Name Accession Description Interval E-value
AcfC COG4588
Accessory colonization factor AcfC, contains ABC-type periplasmic domain [Cell wall/membrane ...
 2-226 1.18e-120

Accessory colonization factor AcfC, contains ABC-type periplasmic domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443645  Cd Length: 232  Bit Score: 342.34  E-value: 1.18e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505195663   2 RVYGPGGPMPAMKEAAATFGRAQGIEVQVEAGPLPAWKDKATKDADTIFSGFEVMMSDFIEALPD-IDPSTVQPLYLRAS 80
Cdd:COG4588     7 NVYGPGGPAPALKEAAEAFEKKTGVKVEVTAGPTPKWIDKAKKNADIIFGGSEQMMTAFAEAYPGaFDSKDVEPLYLRPA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505195663  81 AILVRPGNPKTIGGAKALLEPGHRILVVNGAGQQGLWEDVAGRLGRIADVKAFRSNIAKVAKNSADARKAWVEDSSLDAW 160
Cdd:COG4588    87 AILVRPGNPKNIKGFEDLLKPGVKIVVVNGAGQTGVWEDIAGRTGDIETVQAFRSNIVAYAPNSGAARKAWTQDPDIDAW 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2505195663 161 LIWTIWQVANPTLADVVEVEPDLRIYRDTGIALTKRGQMRPEAKRLVEFLASAEGQHNFVKWGWMR 226
Cdd:COG4588   167 ITWNIWQKANPDLADLVEIEPDYRIYRDTNVALTKKGKADAEAQAFVDFLKSPEAQAIFKKWGWKR 232
PBP2_PEB3_AcfC cd13519
Ligand-binding domain of a glycoprotein adhesion and an accessory colonization factor, a ...
 1-225 6.97e-118

Ligand-binding domain of a glycoprotein adhesion and an accessory colonization factor, a member of the type 2 periplasmic binding fold superfamily; PEB3 is a glycoprotein adhesion from Campylobacter jejuni whose structure suggests a functional role in transport, and resembles PEB1a, an Asp/Glu transporter and an adhesin. The overall structure of PEB3 is a dimer and is similar to that of other type 2 periplasmic transport proteins such as the molybdate/tungstate, sulfate, and ferric iron transporters. PEB3 has high sequence identity to Paa, an Escherichia coli adhesin, and to AcfC, an accessory colonization factor from Vibrio cholera.


Pssm-ID: 270237 [Multi-domain]  Cd Length: 227  Bit Score: 335.05  E-value: 6.97e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505195663   1 MRVYGPGGPMPAMKEAAATFGRAQGIEVQVEAGPLPAWKDKATKDADTIFSGFEVMMSDFIEALPD-IDPSTVQPLYLRA 79
Cdd:cd13519     2 INLYGPGGPAPAMKEAAKKFEKKTGVKVNVTAGPQPTWEDKAKQDADIIYGGSEQMMTDFISALPKlFDSSDIKPLYLRP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505195663  80 SAILVRPGNPKTIGGAKALLEPGHRILVVNGAGQQGLWEDVAGRLGRIADVKAFRSNIAKVAKNSADARKAWVEDSSLDA 159
Cdd:cd13519    82 SAILVRKGNPKKIKGLKDLLKPGVKILVVNGAGQTGLWEDMAGRTGDIETVRAFRKNIVVFAKNSGAARKAWKQDPNIDA 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2505195663 160 WLIWTIWQVANPTLADVVEVEPDLRIYRDTGIALTKRGQMRPEAKRLVEFLASAEGQHNFVKWGWM 225
Cdd:cd13519   162 WITWNIWQKANPDIADFVELEKDYVIYRDMNVALTKKGLQNPEAQEFIDYLSSKEAQAIFKKWGWK 227
SBP_bac_11 pfam13531
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 2-224 1.43e-31

Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.


Pssm-ID: 463911 [Multi-domain]  Cd Length: 225  Bit Score: 115.06  E-value: 1.43e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505195663   2 RVYGPGGPMPAMKEAAATFGRAQGIEVQVEAGPLPAWKD--KATKDADTIFSGFEVMMSDFIEALPdIDPSTVQPLYLRA 79
Cdd:pfam13531   1 TVAAAGGLAAALRELAAAFEAETGVKVVVSYGGSGKLAKqiANGAPADVFISADSAWLDKLAAAGL-VVPGSRVPLAYSP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505195663  80 SAILVRPGNPKTIGGAKALLEPGHRILVVN----GAGQQglWEDVAGRLGRIadvKAFRSNIAKVAKNSADARKAwVEDS 155
Cdd:pfam13531  80 LVIAVPKGNPKDISGLADLLKPGVRLAVADpktaPSGRA--ALELLEKAGLL---KALEKKVVVLGENVRQALTA-VASG 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2505195663 156 SLDAWLIWTIW--QVANPTLADVVEVEPDLRIYRDTGIALTKRGQMRPEAKRLVEFLASAEGQHNFVKWGW 224
Cdd:pfam13531 154 EADAGIVYLSEalFPENGPGLEVVPLPEDLNLPLDYPAAVLKKAAHPEAARAFLDFLLSPEAQAILRKYGF 224
PRK14498 PRK14498
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ...
 60-147 2.53e-03

putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional


Pssm-ID: 237732 [Multi-domain]  Cd Length: 633  Bit Score: 38.66  E-value: 2.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505195663  60 FIEALPDIDPSTVQPLYLRASAILVRPGNPKTIGGAKALLEPGHRIlvVN---GAGQQGLWEDVAGRLG----RIA---- 128
Cdd:PRK14498  481 YIKKYLLGEDAVLVKGYRREQGLVVRKGNPKGIEGIEDLVRKDVRF--VNrqrGSGTRILLDYHLKELAidpeRINgydr 558

                          90
                  ....*....|....*....
gi 2505195663 129 DVKAFRSNIAKVAKNSADA 147
Cdd:PRK14498  559 EEKTHMAVAAAVAQGRADA 577
 
Name Accession Description Interval E-value
AcfC COG4588
Accessory colonization factor AcfC, contains ABC-type periplasmic domain [Cell wall/membrane ...
 2-226 1.18e-120

Accessory colonization factor AcfC, contains ABC-type periplasmic domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443645  Cd Length: 232  Bit Score: 342.34  E-value: 1.18e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505195663   2 RVYGPGGPMPAMKEAAATFGRAQGIEVQVEAGPLPAWKDKATKDADTIFSGFEVMMSDFIEALPD-IDPSTVQPLYLRAS 80
Cdd:COG4588     7 NVYGPGGPAPALKEAAEAFEKKTGVKVEVTAGPTPKWIDKAKKNADIIFGGSEQMMTAFAEAYPGaFDSKDVEPLYLRPA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505195663  81 AILVRPGNPKTIGGAKALLEPGHRILVVNGAGQQGLWEDVAGRLGRIADVKAFRSNIAKVAKNSADARKAWVEDSSLDAW 160
Cdd:COG4588    87 AILVRPGNPKNIKGFEDLLKPGVKIVVVNGAGQTGVWEDIAGRTGDIETVQAFRSNIVAYAPNSGAARKAWTQDPDIDAW 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2505195663 161 LIWTIWQVANPTLADVVEVEPDLRIYRDTGIALTKRGQMRPEAKRLVEFLASAEGQHNFVKWGWMR 226
Cdd:COG4588   167 ITWNIWQKANPDLADLVEIEPDYRIYRDTNVALTKKGKADAEAQAFVDFLKSPEAQAIFKKWGWKR 232
PBP2_PEB3_AcfC cd13519
Ligand-binding domain of a glycoprotein adhesion and an accessory colonization factor, a ...
 1-225 6.97e-118

Ligand-binding domain of a glycoprotein adhesion and an accessory colonization factor, a member of the type 2 periplasmic binding fold superfamily; PEB3 is a glycoprotein adhesion from Campylobacter jejuni whose structure suggests a functional role in transport, and resembles PEB1a, an Asp/Glu transporter and an adhesin. The overall structure of PEB3 is a dimer and is similar to that of other type 2 periplasmic transport proteins such as the molybdate/tungstate, sulfate, and ferric iron transporters. PEB3 has high sequence identity to Paa, an Escherichia coli adhesin, and to AcfC, an accessory colonization factor from Vibrio cholera.


Pssm-ID: 270237 [Multi-domain]  Cd Length: 227  Bit Score: 335.05  E-value: 6.97e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505195663   1 MRVYGPGGPMPAMKEAAATFGRAQGIEVQVEAGPLPAWKDKATKDADTIFSGFEVMMSDFIEALPD-IDPSTVQPLYLRA 79
Cdd:cd13519     2 INLYGPGGPAPAMKEAAKKFEKKTGVKVNVTAGPQPTWEDKAKQDADIIYGGSEQMMTDFISALPKlFDSSDIKPLYLRP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505195663  80 SAILVRPGNPKTIGGAKALLEPGHRILVVNGAGQQGLWEDVAGRLGRIADVKAFRSNIAKVAKNSADARKAWVEDSSLDA 159
Cdd:cd13519    82 SAILVRKGNPKKIKGLKDLLKPGVKILVVNGAGQTGLWEDMAGRTGDIETVRAFRKNIVVFAKNSGAARKAWKQDPNIDA 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2505195663 160 WLIWTIWQVANPTLADVVEVEPDLRIYRDTGIALTKRGQMRPEAKRLVEFLASAEGQHNFVKWGWM 225
Cdd:cd13519   162 WITWNIWQKANPDIADFVELEKDYVIYRDMNVALTKKGLQNPEAQEFIDYLSSKEAQAIFKKWGWK 227
SBP_bac_11 pfam13531
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 2-224 1.43e-31

Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.


Pssm-ID: 463911 [Multi-domain]  Cd Length: 225  Bit Score: 115.06  E-value: 1.43e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505195663   2 RVYGPGGPMPAMKEAAATFGRAQGIEVQVEAGPLPAWKD--KATKDADTIFSGFEVMMSDFIEALPdIDPSTVQPLYLRA 79
Cdd:pfam13531   1 TVAAAGGLAAALRELAAAFEAETGVKVVVSYGGSGKLAKqiANGAPADVFISADSAWLDKLAAAGL-VVPGSRVPLAYSP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505195663  80 SAILVRPGNPKTIGGAKALLEPGHRILVVN----GAGQQglWEDVAGRLGRIadvKAFRSNIAKVAKNSADARKAwVEDS 155
Cdd:pfam13531  80 LVIAVPKGNPKDISGLADLLKPGVRLAVADpktaPSGRA--ALELLEKAGLL---KALEKKVVVLGENVRQALTA-VASG 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2505195663 156 SLDAWLIWTIW--QVANPTLADVVEVEPDLRIYRDTGIALTKRGQMRPEAKRLVEFLASAEGQHNFVKWGW 224
Cdd:pfam13531 154 EADAGIVYLSEalFPENGPGLEVVPLPEDLNLPLDYPAAVLKKAAHPEAARAFLDFLLSPEAQAILRKYGF 224
PBP2_ModA3_like cd13517
Substrate binding domain of molybdate binding protein-like (ModA3), a member of the type 2 ...
 3-223 4.98e-16

Substrate binding domain of molybdate binding protein-like (ModA3), a member of the type 2 periplasmic binding fold superfamily; This subfamily contains molybdate binding protein-like (ModA3) domain of an ABC-type transporter. Molybdate transport system is comprised of a periplasmic binding protein, an integral membrane protein, and an energizer protein. These three proteins are coded by modA, modB, and modC genes, respectively. ModA proteins serve as initial receptors in the ABC transport of molybdate mostly in eubacteria and archaea. ModA transporters import molybdenum and tungsten from the environment in the form of the oxyanions molybdate (MoO(4) (2-)) and tungstate (WO(4) (2-)). After binding molybdate with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. In contrast to the structure of the two ModA homologs from Escherichia coli and Azotobacter vinelandii, where the oxygen atoms are tetrahedrally arrangted around the metal center, the structure of Pyrococcus furiosus ModA/WtpA (PfModA) has shown that a binding site for molybdate and tungstate where the central metal atom is in a hexacoordinate configuration. The ModA 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: 270235 [Multi-domain]  Cd Length: 223  Bit Score: 73.80  E-value: 4.98e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505195663   3 VYGPGGPMPAMKEAAATFGRAQGIEVQVE---AGPLPAwKDKATKDADTIFSGfevmMSDFIEALPDI-DPSTVQPLYLR 78
Cdd:cd13517     4 VYAGAGLKKPMEEIAKLFEKKTGIKVEVTyggSGQLLS-QIETSKKGDVFIPG----SEDYMEKAKEKgLVETVKIVAYH 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505195663  79 ASAILVRPGNPKTIGGAKALLEPGHRILVVN------GAGQQ------GLWEDVAgrlgriADVKAFRSNIAKVAknsad 146
Cdd:cd13517    79 VPVIAVPKGNPKNITSLEDLAKPGVKVALGDpkaaaiGKYAKkileknGLWEKVK------KNVVVYTATVNQLL----- 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2505195663 147 arkAWVEDSSLDAWLIWTIWQVANPTLADVVEVEPDLRIYRDTGIALTKRGQMRPEAKRLVEFLASAEGQHNFVKWG 223
Cdd:cd13517   148 ---TYVLLGQVDAAIVWEDFAYWNPGKVEVIPIPKEQNRIKTIPIAVLKSSKNKELAKKFVDFVTSDEGKEIFKKYG 221
ModA COG0725
ABC-type molybdate transport system, periplasmic Mo-binding protein ModA [Inorganic ion ...
 2-223 2.26e-12

ABC-type molybdate transport system, periplasmic Mo-binding protein ModA [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, periplasmic Mo-binding protein ModA is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440489 [Multi-domain]  Cd Length: 253  Bit Score: 64.51  E-value: 2.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505195663   2 RVYGPGGPMPAMKEAAATFGRAQ-GIEVQVEAGPLPAWKD--KATKDADTIFSGFEVMMsDFIEALPDIDPSTVQPlYLR 78
Cdd:COG0725    28 TVFAAASLKEALEELAAAFEKEHpGVKVELSFGGSGALARqiEQGAPADVFISADEKYM-DKLAKKGLILAGSRVV-FAT 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505195663  79 AS-AILVRPGNPKTIGGAKALLEPGHRILVVN----GAGQQ--------GLWEDVAGRLGRIADVKAFrsnIAKVAKNSA 145
Cdd:COG0725   106 NRlVLAVPKGNPADISSLEDLAKPGVRIAIGDpktvPYGKYakealekaGLWDALKPKLVLGENVRQV---LAYVESGEA 182

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2505195663 146 DArkAWVEDSslDAwliwtiwqVANPTLADVVEVEPDLRIYRDTGIALTKRGQMRPEAKRLVEFLASAEGQHNFVKWG 223
Cdd:COG0725   183 DA--GIVYLS--DA--------LAAKGVLVVVELPAELYAPIVYPAAVLKGAKNPEAAKAFLDFLLSPEAQAILEKYG 248
Periplasmic_Binding_Protein_Type_2 cd00648
Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent ...
 3-195 7.73e-09

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: 53.73  E-value: 7.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505195663   3 VYGPGGPMPAMKEAAATFGRAQGIEVQ-VEAGPLPAWKDK-ATKDADTIFSGFEVMMSDFIEALPDIDPSTVQPLYLRAS 80
Cdd:cd00648     6 SIGPPPYAGFAEDAAKQLAKETGIKVElVPGSSIGTLIEAlAAGDADVAVGPIAPALEAAADKLAPGGLYIVPELYVGGY 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505195663  81 AILVRPGNPKTIGGAKALLePGHRILVvngaGQQGLWEDVAGRLGRIADVKAFRSNIAKVAKNSAdARKAWVEDSSLDAW 160
Cdd:cd00648    86 VLVVRKGSSIKGLLAVADL-DGKRVGV----GDPGSTAVRQARLALGAYGLKKKDPEVVPVPGTS-GALAAVANGAVDAA 159

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2505195663 161 LIWTIWQVANPTLADVVEVEPD--LRIYRDTGIALTK 195
Cdd:cd00648   160 IVWVPAAERAQLGNVQLEVLPDdlGPLVTTFGVAVRK 196
PBP2_ModA_like cd00993
Substrate binding domain of molybdate-binding proteins, the type 2 periplasmic binding protein ...
 2-224 4.49e-08

Substrate binding domain of molybdate-binding proteins, the type 2 periplasmic binding protein fold; Molybdate binding domain ModA. Molybdate transport system is comprised of a periplasmic binding protein, an integral membrane protein, and an energizer protein. These three proteins are coded by modA, modB, and modC genes, respectively. ModA proteins serve as initial receptors in the ABC transport of molybdate mostly in eubacteria and archaea. Bacteria and archaea import molybdenum and tungsten from the environment in the form of the oxyanions molybdate (MoO(4) (2-)) and tungstate (WO(4) (2-)). After binding molybdate with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. In contrast to the structure of the two ModA homologs from Escherichia coli and Azotobacter vinelandii, where the oxygen atoms are tetrahedrally arranged around the metal center, the structure of Pyrococcus furiosus ModA/WtpA (PfModA) has revealed a binding site for molybdate and tungstate where the central metal atom is in a hexacoordinate configuration. This octahedral geometry was rather unexpected. The ModA 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: 270215 [Multi-domain]  Cd Length: 225  Bit Score: 51.95  E-value: 4.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505195663   2 RVYGPGGPMPAMKEAAATFGRAQGIEVQVEAGP--LPAWKDKATKDADTIFSGFEVMMsDFIEALPDIDPSTVQPLyLRA 79
Cdd:cd00993     3 TVFAAASLKDALQELAKQFKKATGVTVVLNFGSsgALAKQIEQGAPADVFISADQKWM-DYLVAAGLILPASVRPF-AGN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505195663  80 SAILVRPGNPK--TIGGAKALLEPGHRILV-------VNGAGQQ-----GLWEDVAGRLgriadvkAFRSNIAKVAknsa 145
Cdd:cd00993    81 RLVLVVPKASPvsGTPLLELALDEGGRIAVgdpqsvpAGRYAKQvleklGLWDKLPPKL-------VEAPDVRQVL---- 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2505195663 146 darkAWVEDSSLDAWLIWTIWQVANPTLADVVEVEPDLRIYRDTGIALTKRGQMRPEAKRLVEFLASAEGQHNFVKWGW 224
Cdd:cd00993   150 ----GLVESGEADAGFVYASDALAAKKVKVVATLPEDLHEPIVYPVAVLKGSKNKAEAKAFLDFLLSPEGQRIFERYGF 224
PBP2_EcModA cd13536
Substrate binding domain of ModA from Escherichia coli and its closest homologs;the type 2 ...
 12-223 1.73e-05

Substrate binding domain of ModA from Escherichia coli and its closest homologs;the type 2 periplasmic binding protein fold; This subfamily contains domains found in ModA proteins that serve as initial receptors in the ABC transport of molybdate in eubacteria and archaea. After binding molybdate with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ModA 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: 270254 [Multi-domain]  Cd Length: 227  Bit Score: 44.33  E-value: 1.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505195663  12 AMKEAAATFGRAQGIEVQVEAGPLPAW--KDKATKDADTIFSGFEVMMsDFIEALPDIDPSTVQPLyLRASAILV----R 85
Cdd:cd13536    13 AMQEIATAFEKATGIDVRVSFASSSALarQIEAGAPADLFLSADRDWM-DYLVQKGLIDPATRQNL-LGNRLVLVapaaS 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505195663  86 PGNPKTIGGAKALLEPGHRILVVNG-----AGQ--------QGLWEDVAGRLGRIADVkafRSNIAKVAKNSADARKAWV 152
Cdd:cd13536    91 PIQVDPKPGFDLAALLGGGRLAVGDpahvpAGKyakealekLGLWSSLEPRLALAEDV---RAALALVERGEAPLGIVYA 167

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2505195663 153 EDSsldawliwtiwqVANPTLADVVEVEPDLRIYRDTGIALTKrGQMRPEAKRLVEFLASAEGQHNFVKWG 223
Cdd:cd13536   168 TDA------------AASKGVRVVATFPEDSHKPIEYPVALLK-GANNPAARAFLDFLKSPQAQAIFKRYG 225
PBP2_ModA_like_1 cd13538
Substrate binding domain of putative molybdate-binding protein;the type 2 periplasmic binding ...
 81-223 2.17e-03

Substrate binding domain of putative molybdate-binding protein;the type 2 periplasmic binding protein fold; This subfamily contains domains found in ModA proteins of putative ABC-type transporter. Molybdate transport system is comprised of a periplasmic binding protein, an integral membrane protein, and an energizer protein. These three proteins are coded by modA, modB, and modC genes, respectively. ModA proteins serve as initial receptors in the ABC transport of molybdate mostly in eubacteria and archaea. After binding molybdate with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ModA 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: 270256 [Multi-domain]  Cd Length: 230  Bit Score: 38.05  E-value: 2.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505195663  81 AILVRPGNPKTIGGAKALLEPGHRILV------VNGAGQQGLweDVAGRLGRIADVKAFRSNI-----------AKVAKN 143
Cdd:cd13538    83 VVIVPKDNPAKITSLADLAKPGVKIVIgapevpVGTYTRRVL--DKAGNDYAYGYKEAVLANVvseetnvrdvvTKVALG 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505195663 144 SADARKAWVEDSSLDAWliwTIWQVANPTLADVVEVEPdlriyrdtgIALTKRGQMRPEAKRLVEFLASAEGQHNFVKWG 223
Cdd:cd13538   161 EADAGFVYVTDAKAASE---KLKVITIPEEYNVTATYP---------IAVLKASKNPELARAFVDFLLSEEGQAILAEYG 228
PRK14498 PRK14498
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ...
 60-147 2.53e-03

putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional


Pssm-ID: 237732 [Multi-domain]  Cd Length: 633  Bit Score: 38.66  E-value: 2.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505195663  60 FIEALPDIDPSTVQPLYLRASAILVRPGNPKTIGGAKALLEPGHRIlvVN---GAGQQGLWEDVAGRLG----RIA---- 128
Cdd:PRK14498  481 YIKKYLLGEDAVLVKGYRREQGLVVRKGNPKGIEGIEDLVRKDVRF--VNrqrGSGTRILLDYHLKELAidpeRINgydr 558

                          90
                  ....*....|....*....
gi 2505195663 129 DVKAFRSNIAKVAKNSADA 147
Cdd:PRK14498  559 EEKTHMAVAAAVAQGRADA 577
PBP_like pfam12727
PBP superfamily domain; This family belongs to the periplasmic binding domain superfamily. It ...
 62-147 6.74e-03

PBP superfamily domain; This family belongs to the periplasmic binding domain superfamily. It is often associated with a helix-turn-helix domain.


Pssm-ID: 463683 [Multi-domain]  Cd Length: 192  Bit Score: 36.40  E-value: 6.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505195663  62 EALPDIDPSTVqPLYLRASAILVRPGNPKTIGGAKALLEPGHRIlvVN---GAGQQGLWEDVAGRLG-RIADVKAF---- 133
Cdd:pfam12727  54 RLLPGIPVVLI-NLAYREQGLVVAPGNPKGITGWEDLARPGLRF--VNrqrGSGTRVLLDELLRKAGiDPSDINGYdree 130

                          90
                  ....*....|....*..
gi 2505195663 134 RSNIA---KVAKNSADA 147
Cdd:pfam12727 131 RSHLAvaaAVASGRADA 147
PBP2_CysP cd01005
Substrate binding domain of an active sulfate transporter, a member of the type 2 periplasmic ...
 81-223 9.01e-03

Substrate binding domain of an active sulfate transporter, a member of the type 2 periplasmic binding fold superfamily; This family contains sulfate binding domain of CysP proteins that serve as initial receptors in the ABC transport of sulfate and thiosulfate in eubacteria. After binding the ligand, CysP 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 CysP 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: 270226  Cd Length: 307  Bit Score: 36.52  E-value: 9.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505195663  81 AILVRPGNPKTIGGAKALLEPGHRILVVN----GAGQ---QGLWEDVAGRLGRIADVKAFrsnIAKVAKNSA----DARK 149
Cdd:cd01005    98 VFLVRKGNPKGIRDWDDLVKPGVSVITPNpktsGGARwnyLAAWGYALKKGGSEAKAKEF---VTSLYKNVPvldsGARE 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505195663 150 A---WVEDSSLDAWLIWT--IWQVANPTLADVVE-VEPDLRIYRDTGIALT-----KRGQmRPEAKRLVEFLASAEGQHN 218
Cdd:cd01005   175 AtttFVKRGIGDVLITWEneAILANKELGGDKFEiVYPSVSILAEPPVAVVdknvdKHGT-REVAEAYLEFLYSPEAQEI 253


                  ....*
gi 2505195663 219 FVKWG 223
Cdd:cd01005   254 AAKNG 258
YvgK COG1910
Periplasmic molybdate-binding protein/domain [Inorganic ion transport and metabolism];
75-125 9.14e-03

Periplasmic molybdate-binding protein/domain [Inorganic ion transport and metabolism];


Pssm-ID: 441514 [Multi-domain]  Cd Length: 328  Bit Score: 36.52  E-value: 9.14e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2505195663  75 LYLRASAILVRPGNPKTIGGAKALLEPGHRIlvVN---GAGQQGLWEDVAGRLG 125
Cdd:COG1910   176 LARREQGLIVAKGNPKGIKGLEDLARPDLRF--VNrqkGSGTRVLLDELLRRLG 227
 
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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