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Conserved domains on  [gi|733373840|gb|KHK48938|]
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molybdenum ABC transporter substrate-binding protein [Ralstonia sp. A12]

Protein Classification

molybdate ABC transporter substrate-binding protein; substrate-binding domain-containing protein( domain architecture ID 12147048)

molybdate ABC transporter substrate-binding protein functions as the primary receptor for the active transport of molybdate in an ATP-dependent manner; substrate-binding domain-containing protein similar to Pseudomonas sp. aconitate isomerase, which is involved in assimilation of trans-aconitic acid

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SBP_bac_11 pfam13531
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
33-259 6.48e-43

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


:

Pssm-ID: 463911 [Multi-domain]  Cd Length: 225  Bit Score: 145.87  E-value: 6.48e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733373840   33 RVMNSGGFTAAYKALAPGYEKATGNTLTTAWGPSMgaspeAIPNRLARGEQADVLIMVGEA-LDGLIQKGLVDPASRVPL 111
Cdd:pfam13531   1 TVAAAGGLAAALRELAAAFEAETGVKVVVSYGGSG-----KLAKQIANGAPADVFISADSAwLDKLAAAGLVVPGSRVPL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733373840  112 AESRIGMVVKAGAPKpDISTEAALRNTLLqakSVAYSD---SASGVYIETtLFKRLGIEDQMRGKARKIEK--IPVGTVV 186
Cdd:pfam13531  76 AYSPLVIAVPKGNPK-DISGLADLLKPGV---RLAVADpktAPSGRAALE-LLEKAGLLKALEKKVVVLGEnvRQALTAV 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 733373840  187 ASGEYAIGFQQVSELL---PVAGVDFVgKIPEPLQKVTVFAAGIPVNAVHPKAARELIRYLASPEAAPAVEKSGME 259
Cdd:pfam13531 151 ASGEADAGIVYLSEALfpeNGPGLEVV-PLPEDLNLPLDYPAAVLKKAAHPEAARAFLDFLLSPEAQAILRKYGFR 225
 
Name Accession Description Interval E-value
SBP_bac_11 pfam13531
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
33-259 6.48e-43

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


Pssm-ID: 463911 [Multi-domain]  Cd Length: 225  Bit Score: 145.87  E-value: 6.48e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733373840   33 RVMNSGGFTAAYKALAPGYEKATGNTLTTAWGPSMgaspeAIPNRLARGEQADVLIMVGEA-LDGLIQKGLVDPASRVPL 111
Cdd:pfam13531   1 TVAAAGGLAAALRELAAAFEAETGVKVVVSYGGSG-----KLAKQIANGAPADVFISADSAwLDKLAAAGLVVPGSRVPL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733373840  112 AESRIGMVVKAGAPKpDISTEAALRNTLLqakSVAYSD---SASGVYIETtLFKRLGIEDQMRGKARKIEK--IPVGTVV 186
Cdd:pfam13531  76 AYSPLVIAVPKGNPK-DISGLADLLKPGV---RLAVADpktAPSGRAALE-LLEKAGLLKALEKKVVVLGEnvRQALTAV 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 733373840  187 ASGEYAIGFQQVSELL---PVAGVDFVgKIPEPLQKVTVFAAGIPVNAVHPKAARELIRYLASPEAAPAVEKSGME 259
Cdd:pfam13531 151 ASGEADAGIVYLSEALfpeNGPGLEVV-PLPEDLNLPLDYPAAVLKKAAHPEAARAFLDFLLSPEAQAILRKYGFR 225
ModA COG0725
ABC-type molybdate transport system, periplasmic Mo-binding protein ModA [Inorganic ion ...
6-260 1.42e-35

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: 127.68  E-value: 1.42e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733373840   6 RLLRHVVFALGALSLGFLSPAASADEVRVMNSGGFTAAYKALAPGYEKAT-GNTLTTAWGPSmgaspEAIPNRLARGEQA 84
Cdd:COG0725    1 RRLLLLALLLLALLLAGASAAAAAAELTVFAAASLKEALEELAAAFEKEHpGVKVELSFGGS-----GALARQIEQGAPA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733373840  85 DVLIMVGEA-LDGLIQKGLVDPASRVPLAESRIGMVVKAGAPKpDISTEAALRNTllqAKSVAYSDSAS---GVYIETTL 160
Cdd:COG0725   76 DVFISADEKyMDKLAKKGLILAGSRVVFATNRLVLAVPKGNPA-DISSLEDLAKP---GVRIAIGDPKTvpyGKYAKEAL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733373840 161 fKRLGIEDQMRGKARKIEKIP-VGTVVASGEYAIGFQQVSELLPVAGVDFVGKIPEPLQKVTVFAAGIPVNAVHPKAARE 239
Cdd:COG0725  152 -EKAGLWDALKPKLVLGENVRqVLAYVESGEADAGIVYLSDALAAKGVLVVVELPAELYAPIVYPAAVLKGAKNPEAAKA 230
                        250       260
                 ....*....|....*....|.
gi 733373840 240 LIRYLASPEAAPAVEKSGMEP 260
Cdd:COG0725  231 FLDFLLSPEAQAILEKYGFEP 251
PBP2_ModA_like cd00993
Substrate binding domain of molybdate-binding proteins, the type 2 periplasmic binding protein ...
31-257 3.72e-20

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: 86.24  E-value: 3.72e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733373840  31 EVRVMNSGGFTAAYKALAPGYEKATGNTLTTAWGPSmgaspEAIPNRLARGEQADVLIMVGEAL-DGLIQKGLVDPASRV 109
Cdd:cd00993    1 ELTVFAAASLKDALQELAKQFKKATGVTVVLNFGSS-----GALAKQIEQGAPADVFISADQKWmDYLVAAGLILPASVR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733373840 110 PLAESRIGMVVKAGAPKPDISTEAALRNTLlqaKSVAYSDSAS---GVYiETTLFKRLGIEDQMRGKARKIEKIP-VGTV 185
Cdd:cd00993   76 PFAGNRLVLVVPKASPVSGTPLLELALDEG---GRIAVGDPQSvpaGRY-AKQVLEKLGLWDKLPPKLVEAPDVRqVLGL 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 733373840 186 VASGEYAIGFQQVSELLPVAGVDFVGKIPEPLQKVTVFAAGIPVNAVHPKAARELIRYLASPEAAPAVEKSG 257
Cdd:cd00993  152 VESGEADAGFVYASDALAAKKVKVVATLPEDLHEPIVYPVAVLKGSKNKAEAKAFLDFLLSPEGQRIFERYG 223
modA TIGR01256
molybdenum ABC transporter, periplasmic molybdate-binding protein; The model describes the ...
40-257 1.11e-10

molybdenum ABC transporter, periplasmic molybdate-binding protein; The model describes the molybdate ABC transporter periplasmic binding protein in bacteria and archae. Several of the periplasmic receptors constitute a diverse class of binding proteins that differ widely in size, sequence and ligand specificity. It has been shown experimentally by radioactive labeling that ModA represent hydrophylioc periplasmic-binding protein in gram-negative organisms and its counterpart in gram-positive organisms is a lipoprotein. The other components of the system include the ModB, an integral membrane protein and ModC the ATP-binding subunit. Invariably almost all of them display a common beta/alpha folding motif and have similar tertiary structures consisting of two globular domains. [Transport and binding proteins, Anions]


Pssm-ID: 273526 [Multi-domain]  Cd Length: 216  Bit Score: 59.73  E-value: 1.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733373840   40 FTAAYKALAPGYEKATGNTLTTAWGPSmgaspEAIPNRLARGEQADVLIMVGEA-LDGLIQKGLVDPASRVPLAESRIGM 118
Cdd:TIGR01256   4 LTDALKEIAKQFEKRTGNKVVFSFGSS-----GTLYTQIENGAPADLFISADNKwPKKLVDKGLVVAGSRFTYAGNKLVL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733373840  119 VvkagAPKPDISTEAALRNTLLQAKSVAYSDSAS---GVYIETTLFKrLGIEDQMRGKARKIEKIP-VGTVVASGEYAIG 194
Cdd:TIGR01256  79 I----SPKNRVVDDLDILKKWVADKRVAIGDPKHapyGAAAKEVLQK-LGLWETLKKKLVYGEDVRqALQFVETGNAPAG 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 733373840  195 FQQVSELLPVAGVDFVGKIPEPLQKVTVFAAGIPVNAVHPKAARELIRYLASPEAAPAVEKSG 257
Cdd:TIGR01256 154 IVALSDVIPSKKVGSVATFPEDLYKPIRYPAVIVKGGKNNAAAKAFIDYLKSPEAKEILRKYG 216
PelF NF038011
GT4 family glycosyltransferase PelF; Proteins of this family are components of the ...
194-241 5.67e-03

GT4 family glycosyltransferase PelF; Proteins of this family are components of the exopolysaccharide Pel transporter. It has been reported that PelF is a soluble glycosyltransferase that uses UDP-glucose as the substrate for the synthesis of exopolysaccharide Pel, whereas PelG is a Wzx-like and PST family exopolysaccharide transporter.


Pssm-ID: 411604 [Multi-domain]  Cd Length: 489  Bit Score: 37.99  E-value: 5.67e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 733373840 194 GFQQVSELLPVAGVDFVGKIPE--PLQKVTVFAAGIPVNAVHPKAARELI 241
Cdd:NF038011 373 GFQKIDDLLPQVGLMVLSSISEalPLVVLEAFAAGVPVVTTDVGSCRQLI 422
 
Name Accession Description Interval E-value
SBP_bac_11 pfam13531
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
33-259 6.48e-43

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


Pssm-ID: 463911 [Multi-domain]  Cd Length: 225  Bit Score: 145.87  E-value: 6.48e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733373840   33 RVMNSGGFTAAYKALAPGYEKATGNTLTTAWGPSMgaspeAIPNRLARGEQADVLIMVGEA-LDGLIQKGLVDPASRVPL 111
Cdd:pfam13531   1 TVAAAGGLAAALRELAAAFEAETGVKVVVSYGGSG-----KLAKQIANGAPADVFISADSAwLDKLAAAGLVVPGSRVPL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733373840  112 AESRIGMVVKAGAPKpDISTEAALRNTLLqakSVAYSD---SASGVYIETtLFKRLGIEDQMRGKARKIEK--IPVGTVV 186
Cdd:pfam13531  76 AYSPLVIAVPKGNPK-DISGLADLLKPGV---RLAVADpktAPSGRAALE-LLEKAGLLKALEKKVVVLGEnvRQALTAV 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 733373840  187 ASGEYAIGFQQVSELL---PVAGVDFVgKIPEPLQKVTVFAAGIPVNAVHPKAARELIRYLASPEAAPAVEKSGME 259
Cdd:pfam13531 151 ASGEADAGIVYLSEALfpeNGPGLEVV-PLPEDLNLPLDYPAAVLKKAAHPEAARAFLDFLLSPEAQAILRKYGFR 225
ModA COG0725
ABC-type molybdate transport system, periplasmic Mo-binding protein ModA [Inorganic ion ...
6-260 1.42e-35

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: 127.68  E-value: 1.42e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733373840   6 RLLRHVVFALGALSLGFLSPAASADEVRVMNSGGFTAAYKALAPGYEKAT-GNTLTTAWGPSmgaspEAIPNRLARGEQA 84
Cdd:COG0725    1 RRLLLLALLLLALLLAGASAAAAAAELTVFAAASLKEALEELAAAFEKEHpGVKVELSFGGS-----GALARQIEQGAPA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733373840  85 DVLIMVGEA-LDGLIQKGLVDPASRVPLAESRIGMVVKAGAPKpDISTEAALRNTllqAKSVAYSDSAS---GVYIETTL 160
Cdd:COG0725   76 DVFISADEKyMDKLAKKGLILAGSRVVFATNRLVLAVPKGNPA-DISSLEDLAKP---GVRIAIGDPKTvpyGKYAKEAL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733373840 161 fKRLGIEDQMRGKARKIEKIP-VGTVVASGEYAIGFQQVSELLPVAGVDFVGKIPEPLQKVTVFAAGIPVNAVHPKAARE 239
Cdd:COG0725  152 -EKAGLWDALKPKLVLGENVRqVLAYVESGEADAGIVYLSDALAAKGVLVVVELPAELYAPIVYPAAVLKGAKNPEAAKA 230
                        250       260
                 ....*....|....*....|.
gi 733373840 240 LIRYLASPEAAPAVEKSGMEP 260
Cdd:COG0725  231 FLDFLLSPEAQAILEKYGFEP 251
PBP2_ModA_like cd00993
Substrate binding domain of molybdate-binding proteins, the type 2 periplasmic binding protein ...
31-257 3.72e-20

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: 86.24  E-value: 3.72e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733373840  31 EVRVMNSGGFTAAYKALAPGYEKATGNTLTTAWGPSmgaspEAIPNRLARGEQADVLIMVGEAL-DGLIQKGLVDPASRV 109
Cdd:cd00993    1 ELTVFAAASLKDALQELAKQFKKATGVTVVLNFGSS-----GALAKQIEQGAPADVFISADQKWmDYLVAAGLILPASVR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733373840 110 PLAESRIGMVVKAGAPKPDISTEAALRNTLlqaKSVAYSDSAS---GVYiETTLFKRLGIEDQMRGKARKIEKIP-VGTV 185
Cdd:cd00993   76 PFAGNRLVLVVPKASPVSGTPLLELALDEG---GRIAVGDPQSvpaGRY-AKQVLEKLGLWDKLPPKLVEAPDVRqVLGL 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 733373840 186 VASGEYAIGFQQVSELLPVAGVDFVGKIPEPLQKVTVFAAGIPVNAVHPKAARELIRYLASPEAAPAVEKSG 257
Cdd:cd00993  152 VESGEADAGFVYASDALAAKKVKVVATLPEDLHEPIVYPVAVLKGSKNKAEAKAFLDFLLSPEGQRIFERYG 223
PBP2_ModA_WtpA cd13540
Substrate binding domain of ModA/WtpA from Pyrococcus furiosus and its closest homologs;the ...
31-259 5.08e-15

Substrate binding domain of ModA/WtpA from Pyrococcus furiosus 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. 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 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: 270258 [Multi-domain]  Cd Length: 263  Bit Score: 72.72  E-value: 5.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733373840  31 EVRVMNSGGFTAAYKALAPGYEKATGNTltTAWGPSMGAspeaipNRLAR-----GEQADVLIMVGEAL-DGLIQKGLVD 104
Cdd:cd13540    1 TITVFHAGSLSAPFKALGPAFEKAHTGV--RVQGEASGS------VGLARkvtdlGKPADVFISADYSLiPKLMIPKYAD 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733373840 105 PAsrVPLAESRIGMVVKAGAP-KPDISTEAALRNTLLQAKSVAYSDSA---SGVYIETTL-----------FKRLGIEDQ 169
Cdd:cd13540   73 WY--VPFASNEMVIAYTNKSKyADEINTDNWYEILLRPDVKIGRSDPNldpCGYRTLMTLklaekyynqpdLYSEKLLGN 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733373840 170 MRGKARKIEKIPVGTVVASGEYAIGFQQVSEL---------LPVAG--------------VDFVGKIPEPLQKVTVFAAG 226
Cdd:cd13540  151 NKKVAQRPKETDLLALLESGQIDYAFIYKSVAkqhglpyieLPDEInlsdpsyadfyaksKYTLGDGGTIHGKPIVYGAT 230
                        250       260       270
                 ....*....|....*....|....*....|...
gi 733373840 227 IPVNAVHPKAARELIRYLASPEAAPAVEKSGME 259
Cdd:cd13540  231 IPKNAPNPEAARAFVKFLLSPEGQEILEENGLE 263
PBP2_EcModA cd13536
Substrate binding domain of ModA from Escherichia coli and its closest homologs;the type 2 ...
32-250 1.87e-11

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: 62.05  E-value: 1.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733373840  32 VRVMNSGGFTAAYKALAPGYEKATGNTLTTAWgpsmgASPEAIPNRLARGEQADVLIMVGEA-LDGLIQKGLVDPASRVP 110
Cdd:cd13536    2 VTVFAAASLTDAMQEIATAFEKATGIDVRVSF-----ASSSALARQIEAGAPADLFLSADRDwMDYLVQKGLIDPATRQN 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733373840 111 LAESRIGMVVKAGAPKPDISTEAALRNTLLQAKSVAYSDSAS---GVYIETTLFKrLGIEDQMRGKARKIEKI-PVGTVV 186
Cdd:cd13536   77 LLGNRLVLVAPAASPIQVDPKPGFDLAALLGGGRLAVGDPAHvpaGKYAKEALEK-LGLWSSLEPRLALAEDVrAALALV 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 733373840 187 ASGEYAIGFQQVSELLPVAGVDFVGKIPEPLQKVTVFAAGIPVNAvHPKAARELIRYLASPEAA 250
Cdd:cd13536  156 ERGEAPLGIVYATDAAASKGVRVVATFPEDSHKPIEYPVALLKGA-NNPAARAFLDFLKSPQAQ 218
PBP2_ModA_like_1 cd13538
Substrate binding domain of putative molybdate-binding protein;the type 2 periplasmic binding ...
31-257 7.68e-11

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: 60.39  E-value: 7.68e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733373840  31 EVRVMNSGGFTAAYKALAPGYEKATGNTLTTawgPSMGASPEAIPnRLARGEQADVLIMVGEA-LDGLIQKGLVDPASRV 109
Cdd:cd13538    1 TLTVFAAASLTDAFTEIGEQFEKSNPGVKVT---FNFAGSQALVT-QIEQGAPADVFASADTAnMDALVKAGLLVDTPTI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733373840 110 pLAESRIGMVVKAGAPKpDISTEAALrntllqAKS-----VAYSDSASGVYIETTLfKRLGIeDQMRGKARKIEKIPV-- 182
Cdd:cd13538   77 -FATNKLVVIVPKDNPA-KITSLADL------AKPgvkivIGAPEVPVGTYTRRVL-DKAGN-DYAYGYKEAVLANVVse 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733373840 183 -GTV------VASGEYAIGFQQVSELLPVAG-VDFVgKIPEPLQKVTVFAAGIPVNAVHPKAARELIRYLASPEAAPAVE 254
Cdd:cd13538  147 eTNVrdvvtkVALGEADAGFVYVTDAKAASEkLKVI-TIPEEYNVTATYPIAVLKASKNPELARAFVDFLLSEEGQAILA 225

                 ...
gi 733373840 255 KSG 257
Cdd:cd13538  226 EYG 228
modA TIGR01256
molybdenum ABC transporter, periplasmic molybdate-binding protein; The model describes the ...
40-257 1.11e-10

molybdenum ABC transporter, periplasmic molybdate-binding protein; The model describes the molybdate ABC transporter periplasmic binding protein in bacteria and archae. Several of the periplasmic receptors constitute a diverse class of binding proteins that differ widely in size, sequence and ligand specificity. It has been shown experimentally by radioactive labeling that ModA represent hydrophylioc periplasmic-binding protein in gram-negative organisms and its counterpart in gram-positive organisms is a lipoprotein. The other components of the system include the ModB, an integral membrane protein and ModC the ATP-binding subunit. Invariably almost all of them display a common beta/alpha folding motif and have similar tertiary structures consisting of two globular domains. [Transport and binding proteins, Anions]


Pssm-ID: 273526 [Multi-domain]  Cd Length: 216  Bit Score: 59.73  E-value: 1.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733373840   40 FTAAYKALAPGYEKATGNTLTTAWGPSmgaspEAIPNRLARGEQADVLIMVGEA-LDGLIQKGLVDPASRVPLAESRIGM 118
Cdd:TIGR01256   4 LTDALKEIAKQFEKRTGNKVVFSFGSS-----GTLYTQIENGAPADLFISADNKwPKKLVDKGLVVAGSRFTYAGNKLVL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733373840  119 VvkagAPKPDISTEAALRNTLLQAKSVAYSDSAS---GVYIETTLFKrLGIEDQMRGKARKIEKIP-VGTVVASGEYAIG 194
Cdd:TIGR01256  79 I----SPKNRVVDDLDILKKWVADKRVAIGDPKHapyGAAAKEVLQK-LGLWETLKKKLVYGEDVRqALQFVETGNAPAG 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 733373840  195 FQQVSELLPVAGVDFVGKIPEPLQKVTVFAAGIPVNAVHPKAARELIRYLASPEAAPAVEKSG 257
Cdd:TIGR01256 154 IVALSDVIPSKKVGSVATFPEDLYKPIRYPAVIVKGGKNNAAAKAFIDYLKSPEAKEILRKYG 216
PotD COG0687
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
6-110 7.98e-06

Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];


Pssm-ID: 440451 [Multi-domain]  Cd Length: 348  Bit Score: 46.44  E-value: 7.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733373840   6 RLLRHVVFALGALSLGFLSPAASADEVRVMNSGGFTAayKALAPGYEKATGNTLTTAwgpSMGASPEAIPNRLARGEQAD 85
Cdd:COG0687    5 SLLGLAAAALAAALAGGAPAAAAEGTLNVYNWGGYID--PDVLEPFEKETGIKVVYD---TYDSNEEMLAKLRAGGSGYD 79
                         90       100
                 ....*....|....*....|....*..
gi 733373840  86 VLIMVGEALDGLIQKGLVDP--ASRVP 110
Cdd:COG0687   80 VVVPSDYFVARLIKAGLLQPldKSKLP 106
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
11-212 8.04e-05

ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 43.49  E-value: 8.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733373840  11 VVFALGALSLGFLSPAASADEVRVM---NSGGFTAAYKALAPGYEKATGN-TLTTAWGPSmGASPEAIPNRLARGEQADV 86
Cdd:COG1653   12 LALALAACGGGGSGAAAAAGKVTLTvwhTGGGEAAALEALIKEFEAEHPGiKVEVESVPY-DDYRTKLLTALAAGNAPDV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733373840  87 LIMVGEALDGLIQKGLVdpasrVPLAEsrigmVVKAGAPKPDISTEAALRNTLLQAK--SVAYSDSASGVYIETTLFKRL 164
Cdd:COG1653   91 VQVDSGWLAEFAAAGAL-----VPLDD-----LLDDDGLDKDDFLPGALDAGTYDGKlyGVPFNTDTLGLYYNKDLFEKA 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 733373840 165 GIE-----DQMRGKARKIEKipvgtvvASGEYAIGFQ-----QVSELLPVAGVDFVGK 212
Cdd:COG1653  161 GLDppktwDELLAAAKKLKA-------KDGVYGFALGgkdgaAWLDLLLSAGGDLYDE 211
AfuA COG1840
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]; ...
186-262 1.93e-04

ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 441445 [Multi-domain]  Cd Length: 286  Bit Score: 41.84  E-value: 1.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733373840 186 VASGEYAIG----FQQVSELLPVAGVDFVgkIPEPLQKVTVFAAGIPVNAVHPKAARELIRYLASPEAAPAVEKSGME-P 260
Cdd:COG1840  168 VASGEVAIGivnsYYALRAKAKGAPVEVV--FPEDGTLVNPSGAAILKGAPNPEAAKLFIDFLLSDEGQELLAEEGYEyP 245

                 ..
gi 733373840 261 SR 262
Cdd:COG1840  246 VR 247
PBP2_Fe3_thiamine_like cd13518
Substrate binding domain of iron and thiamine transporters-like, a member of the type 2 ...
43-249 7.37e-04

Substrate binding domain of iron and thiamine transporters-like, a member of the type 2 periplasmic binding fold superfamily; The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. On the other hand, thiamin is an essential cofactor in all living systems. Thiamin diphosphate (ThDP)-dependent enzymes play an important role in carbohydrate and branched-chain amino acid metabolism. Most prokaryotes, plants, and fungi can synthesize thiamin, but it is not synthesized in vertebrates. These periplasmic domains have high affinities for their respective substrates and serve as the primary receptor for transport. After binding iron and thiamine 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 iron- and thiamine-binding proteins belong to the PBPI2 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: 270236 [Multi-domain]  Cd Length: 260  Bit Score: 39.98  E-value: 7.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733373840  43 AYKALAPGYEKATGNTLTtawgPSMGASPEAIpNRLARgE----QADVLIMVGE-ALDGLIQKGLVDPASR--------- 108
Cdd:cd13518   12 FAEPVLKAFEEKTGIKVK----AVYDGTGELA-NRLIA-EknnpQADVFWGGEIiALEALKEEGLLEPYTPkvieaipad 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733373840 109 --------VPLAESRIGMVV------KAGAPKPdisteaalRNTLLQAK---SVAYSD---SASGVYIETTLFKRLGIED 168
Cdd:cd13518   86 yrdpdgywVGFAARARVFIYntdklkEPDLPKS--------WDDLLDPKwkgKIVYPTplrSGTGLTHVAALLQLMGEEK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733373840 169 ---QMRGKARKIEKIPVGT-----VVASGEYAIGF--QQVSELLPVAGVDfVGKIPePLQKVTVFAAGIPV--NAVHPKA 236
Cdd:cd13518  158 ggwYLLKLLANNGKPVAGNsdaydLVAKGEVAVGLtdTYYAARAAAKGEP-VEIVY-PDQGALVIPEGVALlkGAPNPEA 235
                        250
                 ....*....|...
gi 733373840 237 ARELIRYLASPEA 249
Cdd:cd13518  236 AKKFIDFLLSPEG 248
PBP2_ModA_like_2 cd13541
Substrate binding domain of molybdate-binding proteins;the type 2 periplasmic binding protein ...
31-259 1.40e-03

Substrate binding domain of molybdate-binding proteins;the type 2 periplasmic binding protein fold; This subfamily contains domains found in ModA proteins of putative ABC-type transporter. ModA proteins serve as initial receptors in the ABC transport of molybdate 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 and tungstate 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: 270259 [Multi-domain]  Cd Length: 238  Bit Score: 39.21  E-value: 1.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733373840  31 EVRVMNSGGFTAAYKALAPGYEKATGNTLTTAWGPSmgaspEAIPNRLARGEQADVLI---MVGEAldGLIQKGLVDPAs 107
Cdd:cd13541    1 PLRLYAAGSLRAALTELAAAYQEQTGVAIELEFGPA-----GLLRERIEAGEKADLFAsanMEHPQ--ALAAAGRASPV- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733373840 108 rVPLAESRIGMVVKAGAP-KPDISTEAALRNTLLQAKSVAYSDsASGVY-------IETtlfKRLGIEDQMRGKARKI-- 177
Cdd:cd13541   73 -VVFARNRLCLIARPGLGlTSDNLLDLLLDPRLRLGTSTPGAD-PGGDYawqlfdrAEK---LHPGAGKKLKAKALKLvg 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733373840 178 ---------EKIPVGTVVASGE---------YAIGFQQVSELLPVAgvdfvgkIPEPLQKVTVFAAGIPvNAVHPkAARE 239
Cdd:cd13541  148 gpdsppipgGRNAAHYLIENGQadlfigycsNARLLKQVPDLQVVA-------LPDELNIGAEYGLAIL-SAAHA-AAQR 218
                        250       260
                 ....*....|....*....|
gi 733373840 240 LIRYLASPEAAPAVEKSGME 259
Cdd:cd13541  219 LALFLLSPEGQAILAKYGFL 238
PBP2_AvModA cd13539
Substrate binding domain of ModA/WtpA from Azotobacter vinelandii and its closest homologs;the ...
31-249 2.04e-03

Substrate binding domain of ModA/WtpA from Azotobacter vinelandii 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. 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 shown that a binding site for molybdate and tungstate is 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: 270257 [Multi-domain]  Cd Length: 226  Bit Score: 38.70  E-value: 2.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733373840  31 EVRVMNSGGFTAAYKALAPGYEKATGNTLTTAWGPSmGASPEAIPNrlarGEQADVLIMVGEAL-DGLIQKGLVDPASRV 109
Cdd:cd13539    1 TLRVAAAANLKYALKEIAAAFEKETGIKVRVSYGSS-GKLYAQIRN----GAPFDLFLSADEKYpEKLYKAGLAAAGSPF 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733373840 110 PLAESRIGMVVkagaPKPDISTEAALRNTLLQAKSVAYSDSAS---GVYIETTLfKRLGIEDQMRGKARKIEKI-PVGTV 185
Cdd:cd13539   76 VYAIGKLVLWS----PKPSLLDPSGDVLLDPKVKRIAIANPKLapyGRAAVEAL-EHAGLYEAVKPKLVYGENVsQAAQF 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 733373840 186 VASGEYAIGFQQVSELLP---VAGVDFVgKIPEPLQKVTVFAAGIPVNAVHPKAARELIRYLASPEA 249
Cdd:cd13539  151 AATGNADVGFVALSLALSpklKEKGSFW-LVPPDLYPPIEQGAVILKRGKDNAAAKAFYDFLLSPEA 216
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
42-250 2.99e-03

Bacterial extracellular solute-binding protein; This family also includes the bacterial extracellular solute-binding protein family POTD/POTF.


Pssm-ID: 460248 [Multi-domain]  Cd Length: 294  Bit Score: 38.55  E-value: 2.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733373840   42 AAYKALAPGYEKA-TGNTLTTAWGPSmGASPEAIPNRLARGE-QADVLIMVGEALDGLIQKGLVDP-------------- 105
Cdd:pfam01547   8 AALQALVKEFEKEhPGIKVEVESVGS-GSLAQKLTTAIAAGDgPADVFASDNDWIAELAKAGLLLPlddyvanylvlgvp 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733373840  106 -ASRVPLAESRIGMVV------KAGAPKP---DISTEAALR------------------------NTLLQAKSVAYSDSA 151
Cdd:pfam01547  87 kLYGVPLAAETLGLIYnkdlfkKAGLDPPktwDELLEAAKKlkekgkspggagggdasgtlgyftLALLASLGGPLFDKD 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733373840  152 SGVYIETTLFKRLGIEDQMRGKARKIEKIP-----------VGTVVASGEYAIGF----QQVSELLPVAGVDFVGKIPEP 216
Cdd:pfam01547 167 GGGLDNPEAVDAITYYVDLYAKVLLLKKLKnpgvagadgreALALFEQGKAAMGIvgpwAALAANKVKLKVAFAAPAPDP 246
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 733373840  217 LQKVTVFA-------------AGIPVNAVHPKAARELIRYLASPEAA 250
Cdd:pfam01547 247 KGDVGYAPlpagkggkgggygLAIPKGSKNKEAAKKFLDFLTSPEAQ 293
PBP2_TMBP cd14750
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ...
205-250 4.89e-03

The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; possesses type 2 periplasmic binding fold; This group represents the periplasmic trehalose/maltose-binding component of an ABC transport system and related proteins from archaea and bacteria. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are 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.


Pssm-ID: 270453 [Multi-domain]  Cd Length: 385  Bit Score: 38.04  E-value: 4.89e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 733373840 205 AGVDFVGKIPEPLQKVTVFAA-------GIPVNAVHPKAARELIRYLASPEAA 250
Cdd:cd14750  253 AVAGKVGVAPLPAGPGGGSAStlggwnlAISANSKHKEAAWEFVKFLTSPEVQ 305
PelF NF038011
GT4 family glycosyltransferase PelF; Proteins of this family are components of the ...
194-241 5.67e-03

GT4 family glycosyltransferase PelF; Proteins of this family are components of the exopolysaccharide Pel transporter. It has been reported that PelF is a soluble glycosyltransferase that uses UDP-glucose as the substrate for the synthesis of exopolysaccharide Pel, whereas PelG is a Wzx-like and PST family exopolysaccharide transporter.


Pssm-ID: 411604 [Multi-domain]  Cd Length: 489  Bit Score: 37.99  E-value: 5.67e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 733373840 194 GFQQVSELLPVAGVDFVGKIPE--PLQKVTVFAAGIPVNAVHPKAARELI 241
Cdd:NF038011 373 GFQKIDDLLPQVGLMVLSSISEalPLVVLEAFAAGVPVVTTDVGSCRQLI 422
 
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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