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Conserved domains on  [gi|496843510|ref|WP_009382833|]
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molybdate ABC transporter substrate-binding protein [Staphylococcus massiliensis]

Protein Classification

molybdate ABC transporter substrate-binding protein( domain architecture ID 11432494)

molybdate ABC transporter substrate-binding protein functions as the primary receptor for the active transport of molybdate in an ATP-dependent manner

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ModA COG0725
ABC-type molybdate transport system, periplasmic Mo-binding protein ModA [Inorganic ion ...
8-252 1.14e-76

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: 232.45  E-value: 1.14e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510   8 KRLLGIIMMMVVVLAGCTQSKDSQSsLQISAAASLSDVSKELKTAFNKEHPDIKVDFNYGGSGALRKQIETGAPVDVFMS 87
Cdd:COG0725    2 RLLLLALLLLALLLAGASAAAAAAE-LTVFAAASLKEALEELAAAFEKEHPGVKVELSFGGSGALARQIEQGAPADVFIS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510  88 ANQKDVTALKDKDKV--SKTYNYARNELALITHKD--ADIKQISDLDKDD-RFAIGEVNTVPAGKYAKSYLEEHQLYDRY 162
Cdd:COG0725   81 ADEKYMDKLAKKGLIlaGSRVVFATNRLVLAVPKGnpADISSLEDLAKPGvRIAIGDPKTVPYGKYAKEALEKAGLWDAL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510 163 ESNYVFAKDVRQVLNYVKRGNAQLGIVYETvlyqDGKAIQDVKKLENLP--IKRDIVYQAGIVSD---KTASEKWLTFLK 237
Cdd:COG0725  161 KPKLVLGENVRQVLAYVESGEADAGIVYLS----DALAAKGVLVVVELPaeLYAPIVYPAAVLKGaknPEAAKAFLDFLL 236
                        250
                 ....*....|....*
gi 496843510 238 SDEAKRIFKKYHFNV 252
Cdd:COG0725  237 SPEAQAILEKYGFEP 251
 
Name Accession Description Interval E-value
ModA COG0725
ABC-type molybdate transport system, periplasmic Mo-binding protein ModA [Inorganic ion ...
8-252 1.14e-76

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: 232.45  E-value: 1.14e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510   8 KRLLGIIMMMVVVLAGCTQSKDSQSsLQISAAASLSDVSKELKTAFNKEHPDIKVDFNYGGSGALRKQIETGAPVDVFMS 87
Cdd:COG0725    2 RLLLLALLLLALLLAGASAAAAAAE-LTVFAAASLKEALEELAAAFEKEHPGVKVELSFGGSGALARQIEQGAPADVFIS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510  88 ANQKDVTALKDKDKV--SKTYNYARNELALITHKD--ADIKQISDLDKDD-RFAIGEVNTVPAGKYAKSYLEEHQLYDRY 162
Cdd:COG0725   81 ADEKYMDKLAKKGLIlaGSRVVFATNRLVLAVPKGnpADISSLEDLAKPGvRIAIGDPKTVPYGKYAKEALEKAGLWDAL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510 163 ESNYVFAKDVRQVLNYVKRGNAQLGIVYETvlyqDGKAIQDVKKLENLP--IKRDIVYQAGIVSD---KTASEKWLTFLK 237
Cdd:COG0725  161 KPKLVLGENVRQVLAYVESGEADAGIVYLS----DALAAKGVLVVVELPaeLYAPIVYPAAVLKGaknPEAAKAFLDFLL 236
                        250
                 ....*....|....*
gi 496843510 238 SDEAKRIFKKYHFNV 252
Cdd:COG0725  237 SPEAQAILEKYGFEP 251
PBP2_YvgL_like cd13537
Substrate binding domain of putative molybdate-binding protein YvgL and similar proteins;the ...
34-250 6.16e-75

Substrate binding domain of putative molybdate-binding protein YvgL and similar 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: 270255 [Multi-domain]  Cd Length: 225  Bit Score: 227.17  E-value: 6.16e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510  34 LQISAAASLSDVSKELKTAFNKEHPDIKVDFNYGGSGALRKQIETGAPVDVFMSANQKDVTALKDKDKV--SKTYNYARN 111
Cdd:cd13537    2 LTVSAAASLKDALDEIATEYEKENPGVKITFNFGGSGTLQKQIESGAPADVFFSAAKKQMDALEDKGLIdaSTRKNLLKN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510 112 ELALITHKDADIKQIS-DLDKDD--RFAIGEVNTVPAGKYAKSYLEEHQLYDRYESNYVFAKDVRQVLNYVKRGNAQLGI 188
Cdd:cd13537   82 KLVLIVPKDSDSKISSfDLTKDDvkKIAIGEPETVPAGKYAKEALEKLGLWDEIESKLVYGKDVRQVLTYVETGNADAGF 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496843510 189 VYETvlyqDGKAIQDVKKLENLP--IKRDIVYQAGIVSD---KTASEKWLTFLKSDEAKRIFKKYHF 250
Cdd:cd13537  162 VYKT----DALINKKVKVVEEAPedTHTPIIYPIAVIKNsenKEEAQKFIDFLKSEEAKKIFEKYGF 224
SBP_bac_11 pfam13531
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
35-250 1.96e-48

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


Pssm-ID: 463911 [Multi-domain]  Cd Length: 225  Bit Score: 159.35  E-value: 1.96e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510   35 QISAAASLSDVSKELKTAFnKEHPDIKVDFNYGGSGALRKQIETGAPVDVFMSANQKDVTALKDKDKVSKTYN--YARNE 112
Cdd:pfam13531   1 TVAAAGGLAAALRELAAAF-EAETGVKVVVSYGGSGKLAKQIANGAPADVFISADSAWLDKLAAAGLVVPGSRvpLAYSP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510  113 LALITHKD--ADIKQISDLDKDD-RFAIGEVNTVPAGKYAKSYLEEHQLYDRYESNYV-FAKDVRQVLNYVKRGNAQLGI 188
Cdd:pfam13531  80 LVIAVPKGnpKDISGLADLLKPGvRLAVADPKTAPSGRAALELLEKAGLLKALEKKVVvLGENVRQALTAVASGEADAGI 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496843510  189 VYETVLYQDGKaiqdVKKLENLPIKRD----IVYQAGIVS---DKTASEKWLTFLKSDEAKRIFKKYHF 250
Cdd:pfam13531 160 VYLSEALFPEN----GPGLEVVPLPEDlnlpLDYPAAVLKkaaHPEAARAFLDFLLSPEAQAILRKYGF 224
modA TIGR01256
molybdenum ABC transporter, periplasmic molybdate-binding protein; The model describes the ...
39-248 2.65e-48

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: 158.73  E-value: 2.65e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510   39 AASLSDVSKELKTAFNKEHPDiKVDFNYGGSGALRKQIETGAPVDVFMSANQKDVTALKDKDKVSKTYN--YARNELALI 116
Cdd:TIGR01256   1 AASLTDALKEIAKQFEKRTGN-KVVFSFGSSGTLYTQIENGAPADLFISADNKWPKKLVDKGLVVAGSRftYAGNKLVLI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510  117 THKDADIKQISDLDK---DDRFAIGEVNTVPAGKYAKSYLEEHQLYDRYESNYVFAKDVRQVLNYVKRGNAQLGIVYetv 193
Cdd:TIGR01256  80 SPKNRVVDDLDILKKwvaDKRVAIGDPKHAPYGAAAKEVLQKLGLWETLKKKLVYGEDVRQALQFVETGNAPAGIVA--- 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510  194 lYQDGKAIQDVKKLENLPIK--RDIVYQAGIV---SDKTASEKWLTFLKSDEAKRIFKKY 248
Cdd:TIGR01256 157 -LSDVIPSKKVGSVATFPEDlyKPIRYPAVIVkggKNNAAAKAFIDYLKSPEAKEILRKY 215
modA PRK10677
molybdate transporter periplasmic protein; Provisional
7-250 2.96e-28

molybdate transporter periplasmic protein; Provisional


Pssm-ID: 182641 [Multi-domain]  Cd Length: 257  Bit Score: 107.83  E-value: 2.96e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510   7 MKRLLGIIMMMVVVLAG-CTQSKDSQSSLQISAAASLSDVSKELKTAFNKEHpDIKVDFNYGGSGALRKQIETGAPVDVF 85
Cdd:PRK10677   1 MARKWLRLFAGAVLSFAvAGNALADEGKITVFAAASLTNALQDIAAQYKKEK-GVDVVSSFASSSTLARQIEQGAPADLF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510  86 MSANQKDVTALKDKDKVSKT--YNYARNELALITHKDADIKQIS--------DLDKDDRFAIGEVNTVPAGKYAKSYLEE 155
Cdd:PRK10677  80 ISADQKWMDYAVDKKAIDTAtrYTLLGNSLVVVAPKASEQKDFTidkktdwkSLLNGGRLAVGDPDHVPAGIYAKEALQK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510 156 HQLYDRYESNYVFAKDVRQVLNYVKRGNAQLGIVYETvlyqDGKAIQDVKKLENLP--IKRDIVYQAGIVSDKT--ASEK 231
Cdd:PRK10677 160 LGAWDTLSPKLARAEDVRGALALVERNEAPLGIVYGS----DAVASKKVKVVGTFPedSHKPVEYPMAIVKGHNnaTVKA 235
                        250
                 ....*....|....*....
gi 496843510 232 WLTFLKSDEAKRIFKKYHF 250
Cdd:PRK10677 236 FYDYLKGPQAAAIFKRYGF 254
PBPb smart00062
Bacterial periplasmic substrate-binding proteins; bacterial proteins, eukaryotic ones are in ...
48-248 8.92e-03

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


Pssm-ID: 214497 [Multi-domain]  Cd Length: 219  Bit Score: 36.54  E-value: 8.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510    48 ELKTAFNKEHPdIKVDFNYGGSGALRKQIETGApVDVFMSANqkDVTALKDKdKVSKTYNYARNELALITHKDADIKQIS 127
Cdd:smart00062  28 DLAKAIAKELG-LKVEFVEVSFDSLLTALKSGK-IDVVAAGM--TITPERAK-QVDFSDPYYRSGQVILVRKDSPIKSLE 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510   128 DLDKDDrfaIGEVNTVPAGKYAKSYLeehqlydrYESNYVFAKDVRQVLNYVKRGNAQLGIVYETVLYqDGKAIQDVKKL 207
Cdd:smart00062 103 DLKGKK---VAVVAGTTAEELLKKLY--------PEAKIVSYDSNAEALAALKAGRADAAVADAPLLA-ALVKQHGLPEL 170
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 496843510   208 ENLPIKRDIVYQAGIVSDKTASE------KWLTFLKSD-EAKRIFKKY 248
Cdd:smart00062 171 KIVPDPLDTPEGYAIAVRKGDPElldkinKALKELKADgTLKKISEKW 218
 
Name Accession Description Interval E-value
ModA COG0725
ABC-type molybdate transport system, periplasmic Mo-binding protein ModA [Inorganic ion ...
8-252 1.14e-76

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: 232.45  E-value: 1.14e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510   8 KRLLGIIMMMVVVLAGCTQSKDSQSsLQISAAASLSDVSKELKTAFNKEHPDIKVDFNYGGSGALRKQIETGAPVDVFMS 87
Cdd:COG0725    2 RLLLLALLLLALLLAGASAAAAAAE-LTVFAAASLKEALEELAAAFEKEHPGVKVELSFGGSGALARQIEQGAPADVFIS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510  88 ANQKDVTALKDKDKV--SKTYNYARNELALITHKD--ADIKQISDLDKDD-RFAIGEVNTVPAGKYAKSYLEEHQLYDRY 162
Cdd:COG0725   81 ADEKYMDKLAKKGLIlaGSRVVFATNRLVLAVPKGnpADISSLEDLAKPGvRIAIGDPKTVPYGKYAKEALEKAGLWDAL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510 163 ESNYVFAKDVRQVLNYVKRGNAQLGIVYETvlyqDGKAIQDVKKLENLP--IKRDIVYQAGIVSD---KTASEKWLTFLK 237
Cdd:COG0725  161 KPKLVLGENVRQVLAYVESGEADAGIVYLS----DALAAKGVLVVVELPaeLYAPIVYPAAVLKGaknPEAAKAFLDFLL 236
                        250
                 ....*....|....*
gi 496843510 238 SDEAKRIFKKYHFNV 252
Cdd:COG0725  237 SPEAQAILEKYGFEP 251
PBP2_YvgL_like cd13537
Substrate binding domain of putative molybdate-binding protein YvgL and similar proteins;the ...
34-250 6.16e-75

Substrate binding domain of putative molybdate-binding protein YvgL and similar 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: 270255 [Multi-domain]  Cd Length: 225  Bit Score: 227.17  E-value: 6.16e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510  34 LQISAAASLSDVSKELKTAFNKEHPDIKVDFNYGGSGALRKQIETGAPVDVFMSANQKDVTALKDKDKV--SKTYNYARN 111
Cdd:cd13537    2 LTVSAAASLKDALDEIATEYEKENPGVKITFNFGGSGTLQKQIESGAPADVFFSAAKKQMDALEDKGLIdaSTRKNLLKN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510 112 ELALITHKDADIKQIS-DLDKDD--RFAIGEVNTVPAGKYAKSYLEEHQLYDRYESNYVFAKDVRQVLNYVKRGNAQLGI 188
Cdd:cd13537   82 KLVLIVPKDSDSKISSfDLTKDDvkKIAIGEPETVPAGKYAKEALEKLGLWDEIESKLVYGKDVRQVLTYVETGNADAGF 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496843510 189 VYETvlyqDGKAIQDVKKLENLP--IKRDIVYQAGIVSD---KTASEKWLTFLKSDEAKRIFKKYHF 250
Cdd:cd13537  162 VYKT----DALINKKVKVVEEAPedTHTPIIYPIAVIKNsenKEEAQKFIDFLKSEEAKKIFEKYGF 224
PBP2_ModA_like cd00993
Substrate binding domain of molybdate-binding proteins, the type 2 periplasmic binding protein ...
33-250 3.33e-59

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: 187.16  E-value: 3.33e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510  33 SLQISAAASLSDVSKELKTAFNKEhPDIKVDFNYGGSGALRKQIETGAPVDVFMSANQKDVTALKDKDKV--SKTYNYAR 110
Cdd:cd00993    1 ELTVFAAASLKDALQELAKQFKKA-TGVTVVLNFGSSGALAKQIEQGAPADVFISADQKWMDYLVAAGLIlpASVRPFAG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510 111 NELALITHKDADIKQIS----DLDKDDRFAIGEVNTVPAGKYAKSYLEEHQLYDRYESNYVFAKDVRQVLNYVKRGNAQL 186
Cdd:cd00993   80 NRLVLVVPKASPVSGTPllelALDEGGRIAVGDPQSVPAGRYAKQVLEKLGLWDKLPPKLVEAPDVRQVLGLVESGEADA 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496843510 187 GIVYETvlyqDGKAIQDVKKLENLP--IKRDIVYQAGIVSD---KTASEKWLTFLKSDEAKRIFKKYHF 250
Cdd:cd00993  160 GFVYAS----DALAAKKVKVVATLPedLHEPIVYPVAVLKGsknKAEAKAFLDFLLSPEGQRIFERYGF 224
PBP2_EcModA cd13536
Substrate binding domain of ModA from Escherichia coli and its closest homologs;the type 2 ...
34-250 1.48e-52

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: 169.91  E-value: 1.48e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510  34 LQISAAASLSDVSKELKTAFNKEhPDIKVDFNYGGSGALRKQIETGAPVDVFMSANQKDVTALKDK--DKVSKTYNYARN 111
Cdd:cd13536    2 VTVFAAASLTDAMQEIATAFEKA-TGIDVRVSFASSSALARQIEAGAPADLFLSADRDWMDYLVQKglIDPATRQNLLGN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510 112 ELALITHKDADIKQISD-------LDKDDRFAIGEVNTVPAGKYAKSYLEEHQLYDRYESNYVFAKDVRQVLNYVKRGNA 184
Cdd:cd13536   81 RLVLVAPAASPIQVDPKpgfdlaaLLGGGRLAVGDPAHVPAGKYAKEALEKLGLWSSLEPRLALAEDVRAALALVERGEA 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510 185 QLGIVYETvlyqDGKAIQDVKKLENLPIK--RDIVYQAGIV--SDKTASEKWLTFLKSDEAKRIFKKYHF 250
Cdd:cd13536  161 PLGIVYAT----DAAASKGVRVVATFPEDshKPIEYPVALLkgANNPAARAFLDFLKSPQAQAIFKRYGF 226
SBP_bac_11 pfam13531
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
35-250 1.96e-48

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


Pssm-ID: 463911 [Multi-domain]  Cd Length: 225  Bit Score: 159.35  E-value: 1.96e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510   35 QISAAASLSDVSKELKTAFnKEHPDIKVDFNYGGSGALRKQIETGAPVDVFMSANQKDVTALKDKDKVSKTYN--YARNE 112
Cdd:pfam13531   1 TVAAAGGLAAALRELAAAF-EAETGVKVVVSYGGSGKLAKQIANGAPADVFISADSAWLDKLAAAGLVVPGSRvpLAYSP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510  113 LALITHKD--ADIKQISDLDKDD-RFAIGEVNTVPAGKYAKSYLEEHQLYDRYESNYV-FAKDVRQVLNYVKRGNAQLGI 188
Cdd:pfam13531  80 LVIAVPKGnpKDISGLADLLKPGvRLAVADPKTAPSGRAALELLEKAGLLKALEKKVVvLGENVRQALTAVASGEADAGI 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496843510  189 VYETVLYQDGKaiqdVKKLENLPIKRD----IVYQAGIVS---DKTASEKWLTFLKSDEAKRIFKKYHF 250
Cdd:pfam13531 160 VYLSEALFPEN----GPGLEVVPLPEDlnlpLDYPAAVLKkaaHPEAARAFLDFLLSPEAQAILRKYGF 224
modA TIGR01256
molybdenum ABC transporter, periplasmic molybdate-binding protein; The model describes the ...
39-248 2.65e-48

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: 158.73  E-value: 2.65e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510   39 AASLSDVSKELKTAFNKEHPDiKVDFNYGGSGALRKQIETGAPVDVFMSANQKDVTALKDKDKVSKTYN--YARNELALI 116
Cdd:TIGR01256   1 AASLTDALKEIAKQFEKRTGN-KVVFSFGSSGTLYTQIENGAPADLFISADNKWPKKLVDKGLVVAGSRftYAGNKLVLI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510  117 THKDADIKQISDLDK---DDRFAIGEVNTVPAGKYAKSYLEEHQLYDRYESNYVFAKDVRQVLNYVKRGNAQLGIVYetv 193
Cdd:TIGR01256  80 SPKNRVVDDLDILKKwvaDKRVAIGDPKHAPYGAAAKEVLQKLGLWETLKKKLVYGEDVRQALQFVETGNAPAGIVA--- 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510  194 lYQDGKAIQDVKKLENLPIK--RDIVYQAGIV---SDKTASEKWLTFLKSDEAKRIFKKY 248
Cdd:TIGR01256 157 -LSDVIPSKKVGSVATFPEDlyKPIRYPAVIVkggKNNAAAKAFIDYLKSPEAKEILRKY 215
PBP2_ModA_like_1 cd13538
Substrate binding domain of putative molybdate-binding protein;the type 2 periplasmic binding ...
33-250 3.02e-48

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: 159.00  E-value: 3.02e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510  33 SLQISAAASLSDVSKELKTAFNKEHPDIKVDFNYGGSGALRKQIETGAPVDVFMSANQKDVTALKDKDK-VSKTYNYARN 111
Cdd:cd13538    1 TLTVFAAASLTDAFTEIGEQFEKSNPGVKVTFNFAGSQALVTQIEQGAPADVFASADTANMDALVKAGLlVDTPTIFATN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510 112 ELALITHKD--ADIKQISDLDKDD-RFAIGeVNTVPAGKYAKSYLE------EHQLYDRYESNYVFAK-DVRQVLNYVKR 181
Cdd:cd13538   81 KLVVIVPKDnpAKITSLADLAKPGvKIVIG-APEVPVGTYTRRVLDkagndyAYGYKEAVLANVVSEEtNVRDVVTKVAL 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496843510 182 GNAQLGIVYETvlyqDGKAIQDVKKLENLPIKRDIV--YQAGIVSD---KTASEKWLTFLKSDEAKRIFKKYHF 250
Cdd:cd13538  160 GEADAGFVYVT----DAKAASEKLKVITIPEEYNVTatYPIAVLKAsknPELARAFVDFLLSEEGQAILAEYGF 229
PBP2_AvModA cd13539
Substrate binding domain of ModA/WtpA from Azotobacter vinelandii and its closest homologs;the ...
34-250 4.80e-43

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: 145.40  E-value: 4.80e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510  34 LQISAAASLSDVSKELKTAFNKEHPdIKVDFNYGGSGALRKQIETGAPVDVFMSANQKDVTALKDKDKVSKT--YNYARN 111
Cdd:cd13539    2 LRVAAAANLKYALKEIAAAFEKETG-IKVRVSYGSSGKLYAQIRNGAPFDLFLSADEKYPEKLYKAGLAAAGspFVYAIG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510 112 ELALITHKDADIKQISDLDKDD---RFAIGEVNTVPAGKYAKSYLEEHQLYDRYESNYVFAKDVRQVLNYVKRGNAQLGI 188
Cdd:cd13539   81 KLVLWSPKPSLLDPSGDVLLDPkvkRIAIANPKLAPYGRAAVEALEHAGLYEAVKPKLVYGENVSQAAQFAATGNADVGF 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510 189 VYETVLYQDGKAIQD----VKKLENLPIKrdivyQAGIV----SDKTASEKWLTFLKSDEAKRIFKKYHF 250
Cdd:cd13539  161 VALSLALSPKLKEKGsfwlVPPDLYPPIE-----QGAVIlkrgKDNAAAKAFYDFLLSPEARAILKKYGY 225
PBP2_ModA3_like cd13517
Substrate binding domain of molybdate binding protein-like (ModA3), a member of the type 2 ...
33-250 4.68e-34

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: 122.33  E-value: 4.68e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510  33 SLQISAAASLSDVSKELKTAFNKEHpDIKVDFNYGGSGALRKQIETGAPVDVFMSANQKDVTALKDKDKVSKTYNYARNE 112
Cdd:cd13517    1 TLLVYAGAGLKKPMEEIAKLFEKKT-GIKVEVTYGGSGQLLSQIETSKKGDVFIPGSEDYMEKAKEKGLVETVKIVAYHV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510 113 LALITHKD--ADIKQISDLDKDD-RFAIGEVNTVPAGKYAKSYLEEHQLYDRYESNYV-FAKDVRQVLNYVKRGNAQLGI 188
Cdd:cd13517   80 PVIAVPKGnpKNITSLEDLAKPGvKVALGDPKAAAIGKYAKKILEKNGLWEKVKKNVVvYTATVNQLLTYVLLGQVDAAI 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496843510 189 VYETVLYQDGkaiqdvKKLENLPIKRDIVY----QAGIVS---DKTASEKWLTFLKSDEAKRIFKKYHF 250
Cdd:cd13517  160 VWEDFAYWNP------GKVEVIPIPKEQNRiktiPIAVLKsskNKELAKKFVDFVTSDEGKEIFKKYGF 222
modA PRK10677
molybdate transporter periplasmic protein; Provisional
7-250 2.96e-28

molybdate transporter periplasmic protein; Provisional


Pssm-ID: 182641 [Multi-domain]  Cd Length: 257  Bit Score: 107.83  E-value: 2.96e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510   7 MKRLLGIIMMMVVVLAG-CTQSKDSQSSLQISAAASLSDVSKELKTAFNKEHpDIKVDFNYGGSGALRKQIETGAPVDVF 85
Cdd:PRK10677   1 MARKWLRLFAGAVLSFAvAGNALADEGKITVFAAASLTNALQDIAAQYKKEK-GVDVVSSFASSSTLARQIEQGAPADLF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510  86 MSANQKDVTALKDKDKVSKT--YNYARNELALITHKDADIKQIS--------DLDKDDRFAIGEVNTVPAGKYAKSYLEE 155
Cdd:PRK10677  80 ISADQKWMDYAVDKKAIDTAtrYTLLGNSLVVVAPKASEQKDFTidkktdwkSLLNGGRLAVGDPDHVPAGIYAKEALQK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510 156 HQLYDRYESNYVFAKDVRQVLNYVKRGNAQLGIVYETvlyqDGKAIQDVKKLENLP--IKRDIVYQAGIVSDKT--ASEK 231
Cdd:PRK10677 160 LGAWDTLSPKLARAEDVRGALALVERNEAPLGIVYGS----DAVASKKVKVVGTFPedSHKPVEYPMAIVKGHNnaTVKA 235
                        250
                 ....*....|....*....
gi 496843510 232 WLTFLKSDEAKRIFKKYHF 250
Cdd:PRK10677 236 FYDYLKGPQAAAIFKRYGF 254
PBP2_ModA_like_2 cd13541
Substrate binding domain of molybdate-binding proteins;the type 2 periplasmic binding protein ...
33-164 4.97e-18

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: 80.43  E-value: 4.97e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510  33 SLQISAAASLSDVSKELKTAFNKEHpDIKVDFNYGGSGALRKQIETGAPVDVFMSANQKDVTALKDKDKVSKTYNYARNE 112
Cdd:cd13541    1 PLRLYAAGSLRAALTELAAAYQEQT-GVAIELEFGPAGLLRERIEAGEKADLFASANMEHPQALAAAGRASPVVVFARNR 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 496843510 113 LALITHKDADIKQISDLDK--DDRFAIGEVNTV--PAGKYAKsyleehQLYDRYES 164
Cdd:cd13541   80 LCLIARPGLGLTSDNLLDLllDPRLRLGTSTPGadPGGDYAW------QLFDRAEK 129
PBP2_ModA_WtpA cd13540
Substrate binding domain of ModA/WtpA from Pyrococcus furiosus and its closest homologs;the ...
34-251 8.01e-11

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: 60.39  E-value: 8.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510  34 LQISAAASLSDVSKELKTAFNKEHPDIKVDFNYGGS-GALRKQIETGAPVDVFMSANQKDVTALKDKDKVSKTYNYARNE 112
Cdd:cd13540    2 ITVFHAGSLSAPFKALGPAFEKAHTGVRVQGEASGSvGLARKVTDLGKPADVFISADYSLIPKLMIPKYADWYVPFASNE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510 113 LALI----THKDADIKqiSD------LDKDDRFAIGEVNTVPAG-------KYAKSYLEEHQLYDRYESNYVFAKDVR-- 173
Cdd:cd13540   82 MVIAytnkSKYADEIN--TDnwyeilLRPDVKIGRSDPNLDPCGyrtlmtlKLAEKYYNQPDLYSEKLLGNNKKVAQRpk 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510 174 --QVLNYVKRGNAQLGIVYETVL--------------------YQDGKAIQDVKKLENLPIK-RDIVYQAGIVSD---KT 227
Cdd:cd13540  160 etDLLALLESGQIDYAFIYKSVAkqhglpyielpdeinlsdpsYADFYAKSKYTLGDGGTIHgKPIVYGATIPKNapnPE 239
                        250       260
                 ....*....|....*....|....
gi 496843510 228 ASEKWLTFLKSDEAKRIFKKYHFN 251
Cdd:cd13540  240 AARAFVKFLLSPEGQEILEENGLE 263
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
7-86 2.54e-08

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 53.89  E-value: 2.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510   7 MKRLLGII-MMMVVVLAGCTQSKDSQSSLQ-------ISAAASLSDVSKELKTAFNKEHPDIKVDFNYGGSGALRKQIET 78
Cdd:COG1653    1 MRRLALALaAALALALAACGGGGSGAAAAAgkvtltvWHTGGGEAAALEALIKEFEAEHPGIKVEVESVPYDDYRTKLLT 80
                         90
                 ....*....|..
gi 496843510  79 ----GAPVDVFM 86
Cdd:COG1653   81 alaaGNAPDVVQ 92
PRK04168 PRK04168
tungstate ABC transporter substrate-binding protein WtpA;
7-88 6.91e-08

tungstate ABC transporter substrate-binding protein WtpA;


Pssm-ID: 235236  Cd Length: 334  Bit Score: 52.29  E-value: 6.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510   7 MKRLLGIIMMMVVVLA--GCTQSKDSQS-SLQISAAASLSDVSKELKTAFNKEHPDIKVDFNYGGSGAL-RKQIETGAPV 82
Cdd:PRK04168   4 KVKIILIILLLLLVLAfaGCVTAFAEPKgKLKIFHAGSLSVPFEEYEKEFEAYHPNVDVQREAGGSVKCvRKITELGKKA 83

                 ....*.
gi 496843510  83 DVFMSA 88
Cdd:PRK04168  84 DIMASA 89
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
39-242 2.01e-07

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: 50.88  E-value: 2.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510   39 AASLSDVS--KELKTAFNKEHPDIKVDFNYGGSGAL----RKQIETG-APVDVFMSANQK--------------DVTALK 97
Cdd:pfam01547   1 AASLTEAAalQALVKEFEKEHPGIKVEVESVGSGSLaqklTTAIAAGdGPADVFASDNDWiaelakaglllpldDYVANY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510   98 DKDKVSKTY--NYARNELALITHKDA-------DIKQISDLDKDDRfAIGEVNTVPAGKYAKSYLEEHQLYDRYESNY-- 166
Cdd:pfam01547  81 LVLGVPKLYgvPLAAETLGLIYNKDLfkkagldPPKTWDELLEAAK-KLKEKGKSPGGAGGGDASGTLGYFTLALLASlg 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510  167 ----------------------------------------VFAKDVRQVLNYVKRGNAQLGIVYET---VLYQDGKAIQD 203
Cdd:pfam01547 160 gplfdkdgggldnpeavdaityyvdlyakvlllkklknpgVAGADGREALALFEQGKAAMGIVGPWaalAANKVKLKVAF 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 496843510  204 VKKLENLPIKRD------------IVYQAGIVSD---KTASEKWLTFLKSDEAK 242
Cdd:pfam01547 240 AAPAPDPKGDVGyaplpagkggkgGGYGLAIPKGsknKEAAKKFLDFLTSPEAQ 293
PhnD COG3221
ABC-type phosphate/phosphonate transport system, periplasmic component [Inorganic ion ...
114-207 4.88e-06

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


Pssm-ID: 442454 [Multi-domain]  Cd Length: 250  Bit Score: 46.45  E-value: 4.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510 114 ALITHKDADIKQISDLdKDDRFAIGEVNTVPAGKYAKSYLEEHQL-YDRYESNYVFAKDVRQVLNYVKRGNAQLGIVYET 192
Cdd:COG3221   85 VIIVRADSPIKSLEDL-KGKRFAFGDPDSTSGYLVPRALLAEAGLdPERDFSEVVFSGSHDAVILAVANGQADAGAVDSG 163
                         90
                 ....*....|....*
gi 496843510 193 VLYQDGKAIQDVKKL 207
Cdd:COG3221  164 VLERLVEEGPDADQL 178
PBP_like_2 pfam12849
PBP superfamily domain; This domain belongs to the periplasmic binding protein superfamily.
25-127 8.58e-06

PBP superfamily domain; This domain belongs to the periplasmic binding protein superfamily.


Pssm-ID: 432831 [Multi-domain]  Cd Length: 267  Bit Score: 45.61  E-value: 8.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510   25 TQSKDSQSSLQISAAASLSDVSKELKTAFNKEHPDIKVDFNYGGSGALRKQIETGApVDVFMS----ANQKDVTALKDKD 100
Cdd:pfam12849   3 AASAPTVGTILIAGSSTQAPGLLDLAEAFEKKYPGAKVKVTSVGSGEGIKALLNGD-VDVALVsrplTEEEFEAFGANGA 81
                          90       100
                  ....*....|....*....|....*..
gi 496843510  101 KVSKTYNYARNELALITHKDADIKQIS 127
Cdd:pfam12849  82 GGLVEVPVAYDGIAIVVNKDNPANILT 108
PstS COG0226
ABC-type phosphate transport system, periplasmic component [Inorganic ion transport and ...
30-127 1.21e-05

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


Pssm-ID: 439996 [Multi-domain]  Cd Length: 275  Bit Score: 45.26  E-value: 1.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510  30 SQSSLQISAAASLSDVSKELKTAFNKEHPDIKVDFNYGGSGALRKQIETG----APVDVFMSAnqKDVTALKDKDKVSKT 105
Cdd:COG0226    2 ASGTITIAGSSTVYPLAEAWAEAFQKANPGVTINVQSGGSGGGIKQFIAGtvdiGNSSRPLKD--EELEAAKENGVELVE 79
                         90       100
                 ....*....|....*....|..
gi 496843510 106 YNYARNELALITHKDADIKQIS 127
Cdd:COG0226   80 IPVAIDGIAVVVNPDNPVKNLT 101
ptsS_2 TIGR02136
phosphate binding protein; Members of this family are phosphate-binding proteins. Most are ...
8-142 4.32e-05

phosphate binding protein; Members of this family are phosphate-binding proteins. Most are found in phosphate ABC-transporter operons, but some are found in phosphate regulatory operons. This model separates members of the current family from the phosphate ABC transporter phosphate binding protein described by TIGRFAMs model TIGR00975. [Transport and binding proteins, Anions]


Pssm-ID: 273991 [Multi-domain]  Cd Length: 287  Bit Score: 43.58  E-value: 4.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510    8 KRLLGIIMMMVVVLAGCTQSKDSQ---------SSLQISAAASLSDVSKELKTAFNKEHPDIKVDFNYGGSGALRKQIET 78
Cdd:TIGR02136   3 KRIFLLIGLAAALLAAAGCGGAIDsgipdakgsSTITIDGSTTVAPLAEAAAEEFQKIHPGVSVTVQGAGSGTGIKALIN 82
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496843510   79 GApVDVFMSA---NQKDVTALKDKDKVSKTYNYARNELALITHKDADikQISDLDKDDRFAI--GEVNT 142
Cdd:TIGR02136  83 GT-VDIGNSSrpiKDEELQKDKQKGIKLIEHKVAVDGLAVVVNKKNV--PVDDLTVEQLKKIysGEITN 148
PBP2_Fbp_like_2 cd13547
Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 ...
44-132 1.91e-04

Substrate binding domain of an uncharacterized ferric iron transporter, 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. This periplasmic domain (Fbp) has high affinity for ferric iron and serves as the primary receptor for transport. After binding iron with high affinity, Fbp interacts 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 ferric iron-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: 270265 [Multi-domain]  Cd Length: 259  Bit Score: 41.82  E-value: 1.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510  44 DVSKELKTAFNKEHPDIKVDFNYGGSGALRKQIET----GAP-VDVFMSANQKDVTALKDKDkvsktynyarnelALITH 118
Cdd:cd13547   11 DLANALVEAFEKKYPGVKVEVFRAGTGKLMAKLAAeaeaGNPqADVLWVADPPTAEALKKEG-------------LLLPY 77
                         90
                 ....*....|....
gi 496843510 119 KDADIKQISDLDKD 132
Cdd:cd13547   78 KSPEADAIPAPFYD 91
PBP2_Fe3_thiamine_like cd13518
Substrate binding domain of iron and thiamine transporters-like, a member of the type 2 ...
43-100 3.51e-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: 40.75  E-value: 3.51e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496843510  43 SDVSKELKTAFnKEHPDIKVDFNYGGSGALRKQI--ETGAPV-DVFMSANQKDVTALKDKD 100
Cdd:cd13518   10 RDFAEPVLKAF-EEKTGIKVKAVYDGTGELANRLiaEKNNPQaDVFWGGEIIALEALKEEG 69
AfuA COG1840
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]; ...
49-100 1.43e-03

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


Pssm-ID: 441445 [Multi-domain]  Cd Length: 286  Bit Score: 39.15  E-value: 1.43e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 496843510  49 LKTAFNKEHpDIKVDFNYGGSGALRKQIETGA---PVDVFMSANQKDVTALKDKD 100
Cdd:COG1840    1 LLEAFEKKT-GIKVNVVRGGSGELLARLKAEGgnpPADVVWSGDADALEQLANEG 54
PBP2_TMBP cd14750
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ...
43-86 2.50e-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: 38.43  E-value: 2.50e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 496843510  43 SDVSKELKTAFNKEHPDIKVDFNY--GGSGALRKQIET-----GAPVDVFM 86
Cdd:cd14750   13 GELLKKAIAAFEKKHPDIKVEIEElpASSDDQRQQLVTalaagSSAPDVLG 63
PBP2_phosphate_like_1 cd13653
Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 ...
31-127 3.59e-03

Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 periplasmic binding fold superfamily; This subfamily contains uncharacterized phosphate binding domains found in PstS proteins that serve as initial receptors in the ABC transport of phosphate in eubacteria and archaea. After binding the ligand, PstS 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 PstS 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: 270371 [Multi-domain]  Cd Length: 240  Bit Score: 37.55  E-value: 3.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510  31 QSSLQISAAASLSDVSKELKTAFNKEHPDIKVDFNYGGSGALRKQIETGApVDVFMSAnqKDVTAlKDKDKVSKTYNY-- 108
Cdd:cd13653    1 SGTITISGSTTVAPLAEALAEAFMEKHPGVRIEVQGGGSGTGIKALIEGT-ADIGMAS--RPLKA-EEKAAASGLVEHvi 76
                         90
                 ....*....|....*....
gi 496843510 109 ARNELALITHKDADIKQIS 127
Cdd:cd13653   77 ALDGIAIIVNPDNPVKNLT 95
PBPb smart00062
Bacterial periplasmic substrate-binding proteins; bacterial proteins, eukaryotic ones are in ...
48-248 8.92e-03

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


Pssm-ID: 214497 [Multi-domain]  Cd Length: 219  Bit Score: 36.54  E-value: 8.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510    48 ELKTAFNKEHPdIKVDFNYGGSGALRKQIETGApVDVFMSANqkDVTALKDKdKVSKTYNYARNELALITHKDADIKQIS 127
Cdd:smart00062  28 DLAKAIAKELG-LKVEFVEVSFDSLLTALKSGK-IDVVAAGM--TITPERAK-QVDFSDPYYRSGQVILVRKDSPIKSLE 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496843510   128 DLDKDDrfaIGEVNTVPAGKYAKSYLeehqlydrYESNYVFAKDVRQVLNYVKRGNAQLGIVYETVLYqDGKAIQDVKKL 207
Cdd:smart00062 103 DLKGKK---VAVVAGTTAEELLKKLY--------PEAKIVSYDSNAEALAALKAGRADAAVADAPLLA-ALVKQHGLPEL 170
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 496843510   208 ENLPIKRDIVYQAGIVSDKTASE------KWLTFLKSD-EAKRIFKKY 248
Cdd:smart00062 171 KIVPDPLDTPEGYAIAVRKGDPElldkinKALKELKADgTLKKISEKW 218
PBP2_BitB cd13546
Substrate binding domain of a putative iron transporter BitB, a member of the type 2 ...
52-98 9.03e-03

Substrate binding domain of a putative iron transporter BitB, a member of the type 2 periplasmic binding fold superfamily; The substrate domain of this group shows a high homology to the periplasmic component of ferric iron transporter (Fbp), but its biochemical characterization has not been performed. 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. After binding iron with high affinity, Fbp interacts 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 ferric iron-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: 270264 [Multi-domain]  Cd Length: 258  Bit Score: 36.47  E-value: 9.03e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 496843510  52 AFNKEhPDIKVDFNYGGSGALRKQIETGAPV---DVFMSANQKDVTALKD 98
Cdd:cd13546   19 EFEEK-PGIKVEVVTGGTGELLARIKAEADNpqaDVMWGGGIETLEAYKD 67
 
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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