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Conserved domains on  [gi|1468437435|ref|WP_117341654|]
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MULTISPECIES: molybdate ABC transporter substrate-binding protein [Citrobacter]

Protein Classification

molybdate ABC transporter substrate-binding protein( domain architecture ID 10793440)

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 PRK10677
molybdate transporter periplasmic protein; Provisional
1-257 0e+00

molybdate transporter periplasmic protein; Provisional


:

Pssm-ID: 182641 [Multi-domain]  Cd Length: 257  Bit Score: 531.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468437435   1 MARTWLRLFAGATLSLSVAGHALADEGKITVFAAASLTNAMQDIAAQYKKEKNVDVVSSFASSSTLARQIEAGAPADLFI 80
Cdd:PRK10677    1 MARKWLRLFAGAVLSFAVAGNALADEGKITVFAAASLTNALQDIAAQYKKEKGVDVVSSFASSSTLARQIEQGAPADLFI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468437435  81 SADQKWMDYAVDKKSIDTASRKTLLGNSLVVVAPKASEQKAFTIDSKTNWTNLLNGGRLAVGDPEHVPAGIYAKEALQKL 160
Cdd:PRK10677   81 SADQKWMDYAVDKKAIDTATRYTLLGNSLVVVAPKASEQKDFTIDKKTDWKSLLNGGRLAVGDPDHVPAGIYAKEALQKL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468437435 161 GAWDTLAPKLAPAEDVRGALALVERNEAPLGIVYGSDAVASKGVKVVATFPEDSHKKVEYPIAIVDGHSNATVSAFYDYL 240
Cdd:PRK10677  161 GAWDTLSPKLARAEDVRGALALVERNEAPLGIVYGSDAVASKKVKVVGTFPEDSHKPVEYPMAIVKGHNNATVKAFYDYL 240
                         250
                  ....*....|....*..
gi 1468437435 241 KGPQAADIFKRYGFTTK 257
Cdd:PRK10677  241 KGPQAAAIFKRYGFTTK 257
 
Name Accession Description Interval E-value
modA PRK10677
molybdate transporter periplasmic protein; Provisional
1-257 0e+00

molybdate transporter periplasmic protein; Provisional


Pssm-ID: 182641 [Multi-domain]  Cd Length: 257  Bit Score: 531.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468437435   1 MARTWLRLFAGATLSLSVAGHALADEGKITVFAAASLTNAMQDIAAQYKKEKNVDVVSSFASSSTLARQIEAGAPADLFI 80
Cdd:PRK10677    1 MARKWLRLFAGAVLSFAVAGNALADEGKITVFAAASLTNALQDIAAQYKKEKGVDVVSSFASSSTLARQIEQGAPADLFI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468437435  81 SADQKWMDYAVDKKSIDTASRKTLLGNSLVVVAPKASEQKAFTIDSKTNWTNLLNGGRLAVGDPEHVPAGIYAKEALQKL 160
Cdd:PRK10677   81 SADQKWMDYAVDKKAIDTATRYTLLGNSLVVVAPKASEQKDFTIDKKTDWKSLLNGGRLAVGDPDHVPAGIYAKEALQKL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468437435 161 GAWDTLAPKLAPAEDVRGALALVERNEAPLGIVYGSDAVASKGVKVVATFPEDSHKKVEYPIAIVDGHSNATVSAFYDYL 240
Cdd:PRK10677  161 GAWDTLSPKLARAEDVRGALALVERNEAPLGIVYGSDAVASKKVKVVGTFPEDSHKPVEYPMAIVKGHNNATVKAFYDYL 240
                         250
                  ....*....|....*..
gi 1468437435 241 KGPQAADIFKRYGFTTK 257
Cdd:PRK10677  241 KGPQAAAIFKRYGFTTK 257
PBP2_EcModA cd13536
Substrate binding domain of ModA from Escherichia coli and its closest homologs;the type 2 ...
28-255 3.95e-115

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: 329.38  E-value: 3.95e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468437435  28 KITVFAAASLTNAMQDIAAQYKKEKNVDVVSSFASSSTLARQIEAGAPADLFISADQKWMDYAVDKKSIDTASRKTLLGN 107
Cdd:cd13536     1 TVTVFAAASLTDAMQEIATAFEKATGIDVRVSFASSSALARQIEAGAPADLFLSADRDWMDYLVQKGLIDPATRQNLLGN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468437435 108 SLVVVAPKASEQKAFTIDSkTNWTNLLNGGRLAVGDPEHVPAGIYAKEALQKLGAWDTLAPKLAPAEDVRGALALVERNE 187
Cdd:cd13536    81 RLVLVAPAASPIQVDPKPG-FDLAALLGGGRLAVGDPAHVPAGKYAKEALEKLGLWSSLEPRLALAEDVRAALALVERGE 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1468437435 188 APLGIVYGSDAVASKGVKVVATFPEDSHKKVEYPIAIVDGHSNATVSAFYDYLKGPQAADIFKRYGFT 255
Cdd:cd13536   160 APLGIVYATDAAASKGVRVVATFPEDSHKPIEYPVALLKGANNPAARAFLDFLKSPQAQAIFKRYGFT 227
modA TIGR01256
molybdenum ABC transporter, periplasmic molybdate-binding protein; The model describes the ...
34-253 7.74e-94

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: 275.06  E-value: 7.74e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468437435  34 AASLTNAMQDIAAQYKKEKNVDVVSSFASSSTLARQIEAGAPADLFISADQKWMDYAVDKKSIDTASRKTLLGNSLVVVA 113
Cdd:TIGR01256   1 AASLTDALKEIAKQFEKRTGNKVVFSFGSSGTLYTQIENGAPADLFISADNKWPKKLVDKGLVVAGSRFTYAGNKLVLIS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468437435 114 PKASEQKAFTIDSKTnwtnlLNGGRLAVGDPEHVPAGIYAKEALQKLGAWDTLAPKLAPAEDVRGALALVERNEAPLGIV 193
Cdd:TIGR01256  81 PKNRVVDDLDILKKW-----VADKRVAIGDPKHAPYGAAAKEVLQKLGLWETLKKKLVYGEDVRQALQFVETGNAPAGIV 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1468437435 194 YGSDAVASKGVKVVATFPEDSHKKVEYPIAIVDGHSN-ATVSAFYDYLKGPQAADIFKRYG 253
Cdd:TIGR01256 156 ALSDVIPSKKVGSVATFPEDLYKPIRYPAVIVKGGKNnAAAKAFIDYLKSPEAKEILRKYG 216
ModA COG0725
ABC-type molybdate transport system, periplasmic Mo-binding protein ModA [Inorganic ion ...
3-255 1.51e-90

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: 267.89  E-value: 1.51e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468437435   3 RTWLRLFAGATLSLSVAGHALADEGKITVFAAASLTNAMQDIAAQYKKE-KNVDVVSSFASSSTLARQIEAGAPADLFIS 81
Cdd:COG0725     1 RRLLLLALLLLALLLAGASAAAAAAELTVFAAASLKEALEELAAAFEKEhPGVKVELSFGGSGALARQIEQGAPADVFIS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468437435  82 ADQKWMDYAVDKKSIDTASRKTLLGNSLVVVAPKASeqkAFTIDSKTNWTNllNGGRLAVGDPEHVPAGIYAKEALQKLG 161
Cdd:COG0725    81 ADEKYMDKLAKKGLILAGSRVVFATNRLVLAVPKGN---PADISSLEDLAK--PGVRIAIGDPKTVPYGKYAKEALEKAG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468437435 162 AWDTLAPKLAPAEDVRGALALVERNEAPLGIVYGSDAVASKGVKVVATFPEDSHKKVEYPIAIVDGHSNATVS-AFYDYL 240
Cdd:COG0725   156 LWDALKPKLVLGENVRQVLAYVESGEADAGIVYLSDALAAKGVLVVVELPAELYAPIVYPAAVLKGAKNPEAAkAFLDFL 235
                         250
                  ....*....|....*
gi 1468437435 241 KGPQAADIFKRYGFT 255
Cdd:COG0725   236 LSPEAQAILEKYGFE 250
SBP_bac_11 pfam13531
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
30-255 1.01e-55

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


Pssm-ID: 463911 [Multi-domain]  Cd Length: 225  Bit Score: 178.23  E-value: 1.01e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468437435  30 TVFAAASLTNAMQDIAAQYKKEKNVDVVSSFASSSTLARQIEAGAPADLFISADQKWMDYAVDKKSIDTASRKTLLGNSL 109
Cdd:pfam13531   1 TVAAAGGLAAALRELAAAFEAETGVKVVVSYGGSGKLAKQIANGAPADVFISADSAWLDKLAAAGLVVPGSRVPLAYSPL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468437435 110 VVVAPKASEQKAftidskTNWTNLLNGG-RLAVGDPEHVPAGIYAKEALQKLGAWDTLAPKLAP-AEDVRGALALVERNE 187
Cdd:pfam13531  81 VIAVPKGNPKDI------SGLADLLKPGvRLAVADPKTAPSGRAALELLEKAGLLKALEKKVVVlGENVRQALTAVASGE 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1468437435 188 APLGIVYGSDAVASKGVK--VVATFPEDSHKKVEYPIAIV-DGHSNATVSAFYDYLKGPQAADIFKRYGFT 255
Cdd:pfam13531 155 ADAGIVYLSEALFPENGPglEVVPLPEDLNLPLDYPAAVLkKAAHPEAARAFLDFLLSPEAQAILRKYGFR 225
 
Name Accession Description Interval E-value
modA PRK10677
molybdate transporter periplasmic protein; Provisional
1-257 0e+00

molybdate transporter periplasmic protein; Provisional


Pssm-ID: 182641 [Multi-domain]  Cd Length: 257  Bit Score: 531.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468437435   1 MARTWLRLFAGATLSLSVAGHALADEGKITVFAAASLTNAMQDIAAQYKKEKNVDVVSSFASSSTLARQIEAGAPADLFI 80
Cdd:PRK10677    1 MARKWLRLFAGAVLSFAVAGNALADEGKITVFAAASLTNALQDIAAQYKKEKGVDVVSSFASSSTLARQIEQGAPADLFI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468437435  81 SADQKWMDYAVDKKSIDTASRKTLLGNSLVVVAPKASEQKAFTIDSKTNWTNLLNGGRLAVGDPEHVPAGIYAKEALQKL 160
Cdd:PRK10677   81 SADQKWMDYAVDKKAIDTATRYTLLGNSLVVVAPKASEQKDFTIDKKTDWKSLLNGGRLAVGDPDHVPAGIYAKEALQKL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468437435 161 GAWDTLAPKLAPAEDVRGALALVERNEAPLGIVYGSDAVASKGVKVVATFPEDSHKKVEYPIAIVDGHSNATVSAFYDYL 240
Cdd:PRK10677  161 GAWDTLSPKLARAEDVRGALALVERNEAPLGIVYGSDAVASKKVKVVGTFPEDSHKPVEYPMAIVKGHNNATVKAFYDYL 240
                         250
                  ....*....|....*..
gi 1468437435 241 KGPQAADIFKRYGFTTK 257
Cdd:PRK10677  241 KGPQAAAIFKRYGFTTK 257
PBP2_EcModA cd13536
Substrate binding domain of ModA from Escherichia coli and its closest homologs;the type 2 ...
28-255 3.95e-115

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: 329.38  E-value: 3.95e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468437435  28 KITVFAAASLTNAMQDIAAQYKKEKNVDVVSSFASSSTLARQIEAGAPADLFISADQKWMDYAVDKKSIDTASRKTLLGN 107
Cdd:cd13536     1 TVTVFAAASLTDAMQEIATAFEKATGIDVRVSFASSSALARQIEAGAPADLFLSADRDWMDYLVQKGLIDPATRQNLLGN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468437435 108 SLVVVAPKASEQKAFTIDSkTNWTNLLNGGRLAVGDPEHVPAGIYAKEALQKLGAWDTLAPKLAPAEDVRGALALVERNE 187
Cdd:cd13536    81 RLVLVAPAASPIQVDPKPG-FDLAALLGGGRLAVGDPAHVPAGKYAKEALEKLGLWSSLEPRLALAEDVRAALALVERGE 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1468437435 188 APLGIVYGSDAVASKGVKVVATFPEDSHKKVEYPIAIVDGHSNATVSAFYDYLKGPQAADIFKRYGFT 255
Cdd:cd13536   160 APLGIVYATDAAASKGVRVVATFPEDSHKPIEYPVALLKGANNPAARAFLDFLKSPQAQAIFKRYGFT 227
PBP2_ModA_like cd00993
Substrate binding domain of molybdate-binding proteins, the type 2 periplasmic binding protein ...
29-255 1.54e-96

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: 281.92  E-value: 1.54e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468437435  29 ITVFAAASLTNAMQDIAAQYKKEKNVDVVSSFASSSTLARQIEAGAPADLFISADQKWMDYAVDKKSIDTASRKTLLGNS 108
Cdd:cd00993     2 LTVFAAASLKDALQELAKQFKKATGVTVVLNFGSSGALAKQIEQGAPADVFISADQKWMDYLVAAGLILPASVRPFAGNR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468437435 109 LVVVAPKASEQKaftiDSKTNWTNLLNGGRLAVGDPEHVPAGIYAKEALQKLGAWDTLAPKLAPAEDVRGALALVERNEA 188
Cdd:cd00993    82 LVLVVPKASPVS----GTPLLELALDEGGRIAVGDPQSVPAGRYAKQVLEKLGLWDKLPPKLVEAPDVRQVLGLVESGEA 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1468437435 189 PLGIVYGSDAVASKGVKVVATFPEDSHKKVEYPIAIVDGHSN-ATVSAFYDYLKGPQAADIFKRYGFT 255
Cdd:cd00993   158 DAGFVYASDALAAKKVKVVATLPEDLHEPIVYPVAVLKGSKNkAEAKAFLDFLLSPEGQRIFERYGFL 225
modA TIGR01256
molybdenum ABC transporter, periplasmic molybdate-binding protein; The model describes the ...
34-253 7.74e-94

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: 275.06  E-value: 7.74e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468437435  34 AASLTNAMQDIAAQYKKEKNVDVVSSFASSSTLARQIEAGAPADLFISADQKWMDYAVDKKSIDTASRKTLLGNSLVVVA 113
Cdd:TIGR01256   1 AASLTDALKEIAKQFEKRTGNKVVFSFGSSGTLYTQIENGAPADLFISADNKWPKKLVDKGLVVAGSRFTYAGNKLVLIS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468437435 114 PKASEQKAFTIDSKTnwtnlLNGGRLAVGDPEHVPAGIYAKEALQKLGAWDTLAPKLAPAEDVRGALALVERNEAPLGIV 193
Cdd:TIGR01256  81 PKNRVVDDLDILKKW-----VADKRVAIGDPKHAPYGAAAKEVLQKLGLWETLKKKLVYGEDVRQALQFVETGNAPAGIV 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1468437435 194 YGSDAVASKGVKVVATFPEDSHKKVEYPIAIVDGHSN-ATVSAFYDYLKGPQAADIFKRYG 253
Cdd:TIGR01256 156 ALSDVIPSKKVGSVATFPEDLYKPIRYPAVIVKGGKNnAAAKAFIDYLKSPEAKEILRKYG 216
ModA COG0725
ABC-type molybdate transport system, periplasmic Mo-binding protein ModA [Inorganic ion ...
3-255 1.51e-90

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: 267.89  E-value: 1.51e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468437435   3 RTWLRLFAGATLSLSVAGHALADEGKITVFAAASLTNAMQDIAAQYKKE-KNVDVVSSFASSSTLARQIEAGAPADLFIS 81
Cdd:COG0725     1 RRLLLLALLLLALLLAGASAAAAAAELTVFAAASLKEALEELAAAFEKEhPGVKVELSFGGSGALARQIEQGAPADVFIS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468437435  82 ADQKWMDYAVDKKSIDTASRKTLLGNSLVVVAPKASeqkAFTIDSKTNWTNllNGGRLAVGDPEHVPAGIYAKEALQKLG 161
Cdd:COG0725    81 ADEKYMDKLAKKGLILAGSRVVFATNRLVLAVPKGN---PADISSLEDLAK--PGVRIAIGDPKTVPYGKYAKEALEKAG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468437435 162 AWDTLAPKLAPAEDVRGALALVERNEAPLGIVYGSDAVASKGVKVVATFPEDSHKKVEYPIAIVDGHSNATVS-AFYDYL 240
Cdd:COG0725   156 LWDALKPKLVLGENVRQVLAYVESGEADAGIVYLSDALAAKGVLVVVELPAELYAPIVYPAAVLKGAKNPEAAkAFLDFL 235
                         250
                  ....*....|....*
gi 1468437435 241 KGPQAADIFKRYGFT 255
Cdd:COG0725   236 LSPEAQAILEKYGFE 250
PBP2_YvgL_like cd13537
Substrate binding domain of putative molybdate-binding protein YvgL and similar proteins;the ...
29-255 5.40e-77

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: 232.56  E-value: 5.40e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468437435  29 ITVFAAASLTNAMQDIAAQYKKEK-NVDVVSSFASSSTLARQIEAGAPADLFISADQKWMDYAVDKKSIDTASRKTLLGN 107
Cdd:cd13537     2 LTVSAAASLKDALDEIATEYEKENpGVKITFNFGGSGTLQKQIESGAPADVFFSAAKKQMDALEDKGLIDASTRKNLLKN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468437435 108 SLVVVAPKASEQKAFTIDSKTNwtnllNGGRLAVGDPEHVPAGIYAKEALQKLGAWDTLAPKLAPAEDVRGALALVERNE 187
Cdd:cd13537    82 KLVLIVPKDSDSKISSFDLTKD-----DVKKIAIGEPETVPAGKYAKEALEKLGLWDEIESKLVYGKDVRQVLTYVETGN 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1468437435 188 APLGIVYGSDAVASKGVKVVATFPEDSHKKVEYPIAIVDGHSNATVSA-FYDYLKGPQAADIFKRYGFT 255
Cdd:cd13537   157 ADAGFVYKTDALINKKVKVVEEAPEDTHTPIIYPIAVIKNSENKEEAQkFIDFLKSEEAKKIFEKYGFE 225
SBP_bac_11 pfam13531
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
30-255 1.01e-55

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


Pssm-ID: 463911 [Multi-domain]  Cd Length: 225  Bit Score: 178.23  E-value: 1.01e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468437435  30 TVFAAASLTNAMQDIAAQYKKEKNVDVVSSFASSSTLARQIEAGAPADLFISADQKWMDYAVDKKSIDTASRKTLLGNSL 109
Cdd:pfam13531   1 TVAAAGGLAAALRELAAAFEAETGVKVVVSYGGSGKLAKQIANGAPADVFISADSAWLDKLAAAGLVVPGSRVPLAYSPL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468437435 110 VVVAPKASEQKAftidskTNWTNLLNGG-RLAVGDPEHVPAGIYAKEALQKLGAWDTLAPKLAP-AEDVRGALALVERNE 187
Cdd:pfam13531  81 VIAVPKGNPKDI------SGLADLLKPGvRLAVADPKTAPSGRAALELLEKAGLLKALEKKVVVlGENVRQALTAVASGE 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1468437435 188 APLGIVYGSDAVASKGVK--VVATFPEDSHKKVEYPIAIV-DGHSNATVSAFYDYLKGPQAADIFKRYGFT 255
Cdd:pfam13531 155 ADAGIVYLSEALFPENGPglEVVPLPEDLNLPLDYPAAVLkKAAHPEAARAFLDFLLSPEAQAILRKYGFR 225
PBP2_ModA_like_1 cd13538
Substrate binding domain of putative molybdate-binding protein;the type 2 periplasmic binding ...
28-254 1.96e-51

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: 167.48  E-value: 1.96e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468437435  28 KITVFAAASLTNAMQDIAAQYKKE-KNVDVVSSFASSSTLARQIEAGAPADLFISADQKWMDYAVDKKsIDTASRKTLLG 106
Cdd:cd13538     1 TLTVFAAASLTDAFTEIGEQFEKSnPGVKVTFNFAGSQALVTQIEQGAPADVFASADTANMDALVKAG-LLVDTPTIFAT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468437435 107 NSLVVVAPKaseqkaftiDSKTNWTNLLN----GGRLAVGDPEhVPAGIYAKEALQKLGAWDTLAPKLA-----PAE--D 175
Cdd:cd13538    80 NKLVVIVPK---------DNPAKITSLADlakpGVKIVIGAPE-VPVGTYTRRVLDKAGNDYAYGYKEAvlanvVSEetN 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468437435 176 VRGALALVERNEAPLGIVYGSDAVASKGVKVVATFPEDSHKKVEYPIAIVDGHSNATVS-AFYDYLKGPQAADIFKRYGF 254
Cdd:cd13538   150 VRDVVTKVALGEADAGFVYVTDAKAASEKLKVITIPEEYNVTATYPIAVLKASKNPELArAFVDFLLSEEGQAILAEYGF 229
PBP2_AvModA cd13539
Substrate binding domain of ModA/WtpA from Azotobacter vinelandii and its closest homologs;the ...
28-255 6.00e-41

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: 140.39  E-value: 6.00e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468437435  28 KITVFAAASLTNAMQDIAAQYKKEKNVDVVSSFASSSTLARQIEAGAPADLFISADQKWMDYAVDKKSIDTASRKTLLGN 107
Cdd:cd13539     1 TLRVAAAANLKYALKEIAAAFEKETGIKVRVSYGSSGKLYAQIRNGAPFDLFLSADEKYPEKLYKAGLAAAGSPFVYAIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468437435 108 SLVVVAPKASEQKAFTIDSKTNWTnllngGRLAVGDPEHVPAGIYAKEALQKLGAWDTLAPKLAPAEDVRGALALVERNE 187
Cdd:cd13539    81 KLVLWSPKPSLLDPSGDVLLDPKV-----KRIAIANPKLAPYGRAAVEALEHAGLYEAVKPKLVYGENVSQAAQFAATGN 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1468437435 188 APLGIVYGSDAVASKGVKVVATF--PEDSHKKVEYPIAIVDGHS-NATVSAFYDYLKGPQAADIFKRYGFT 255
Cdd:cd13539   156 ADVGFVALSLALSPKLKEKGSFWlvPPDLYPPIEQGAVILKRGKdNAAAKAFYDFLLSPEARAILKKYGYV 226
PBP2_ModA3_like cd13517
Substrate binding domain of molybdate binding protein-like (ModA3), a member of the type 2 ...
29-254 1.41e-26

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: 102.69  E-value: 1.41e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468437435  29 ITVFAAASLTNAMQDIAAQYKKEKNVDVVSSFASSSTLARQIEAGAPADLFISADQKWMDYAVDKKSIDTAsrKTLLGNS 108
Cdd:cd13517     2 LLVYAGAGLKKPMEEIAKLFEKKTGIKVEVTYGGSGQLLSQIETSKKGDVFIPGSEDYMEKAKEKGLVETV--KIVAYHV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468437435 109 LVVVAPKASEQKAFTIDSKTNwtnllNGGRLAVGDPEHVPAGIYAKEALQKLGAWDTLAPKL-APAEDVRGALALVERNE 187
Cdd:cd13517    80 PVIAVPKGNPKNITSLEDLAK-----PGVKVALGDPKAAAIGKYAKKILEKNGLWEKVKKNVvVYTATVNQLLTYVLLGQ 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1468437435 188 APLGIVYGSDAVASKGvKVVATFPEDSHKKVEY-PIAIVDGHSNATVS-AFYDYLKGPQAADIFKRYGF 254
Cdd:cd13517   155 VDAAIVWEDFAYWNPG-KVEVIPIPKEQNRIKTiPIAVLKSSKNKELAkKFVDFVTSDEGKEIFKKYGF 222
PBP2_ModA_like_2 cd13541
Substrate binding domain of molybdate-binding proteins;the type 2 periplasmic binding protein ...
28-255 5.67e-16

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: 74.65  E-value: 5.67e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468437435  28 KITVFAAASLTNAMQDIAAQYKKEKNVDVVSSFASSSTLARQIEAGAPADLFISADQKWMDYAVDKKSIDTASRKTllGN 107
Cdd:cd13541     1 PLRLYAAGSLRAALTELAAAYQEQTGVAIELEFGPAGLLRERIEAGEKADLFASANMEHPQALAAAGRASPVVVFA--RN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468437435 108 SLVVVApKASeqKAFTIDsktNWTNLLNGG--RLAVGDPEHVPAGIYAKEALQKL-----GAWDTL---APKL------- 170
Cdd:cd13541    79 RLCLIA-RPG--LGLTSD---NLLDLLLDPrlRLGTSTPGADPGGDYAWQLFDRAeklhpGAGKKLkakALKLvggpdsp 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468437435 171 APAEDVRGALALVERNEAPLGIVYGSDAVASKGV---KVVATfPEDSHKKVEYPIAIVDGHSNATVsAFYDYLKGPQAAD 247
Cdd:cd13541   153 PIPGGRNAAHYLIENGQADLFIGYCSNARLLKQVpdlQVVAL-PDELNIGAEYGLAILSAAHAAAQ-RLALFLLSPEGQA 230

                  ....*...
gi 1468437435 248 IFKRYGFT 255
Cdd:cd13541   231 ILAKYGFL 238
Periplasmic_Binding_Protein_Type_2 cd00648
Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent ...
36-224 3.87e-15

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


Pssm-ID: 270214 [Multi-domain]  Cd Length: 196  Bit Score: 71.84  E-value: 3.87e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468437435  36 SLTNAMQDIAAQYKKEKNVDVVSSFASS-STLARQIEAGaPADLFISADQKWMDYAVDKKSIDT-ASRKTLLGNSLVVVA 113
Cdd:cd00648    11 PYAGFAEDAAKQLAKETGIKVELVPGSSiGTLIEALAAG-DADVAVGPIAPALEAAADKLAPGGlYIVPELYVGGYVLVV 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468437435 114 PKASEQKaftidsKTNWTNLLNGGRLAVGDPEhVPAGIYAKEALQKlGAWDTLAPKLAPAEDVRGALALVERNEAPLGIV 193
Cdd:cd00648    90 RKGSSIK------GLLAVADLDGKRVGVGDPG-STAVRQARLALGA-YGLKKKDPEVVPVPGTSGALAAVANGAVDAAIV 161
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1468437435 194 YGSDAVAS--KGVKVVATFPEDSHKKVEYPIAI 224
Cdd:cd00648   162 WVPAAERAqlGNVQLEVLPDDLGPLVTTFGVAV 194
PBP2_ModA_WtpA cd13540
Substrate binding domain of ModA/WtpA from Pyrococcus furiosus and its closest homologs;the ...
28-255 7.46e-10

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: 57.70  E-value: 7.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468437435  28 KITVFAAASLTNAMQDIAAQY-KKEKNVDVVSSFASSSTLARQI-EAGAPADLFISADQKWMDyaVDKKSIDTASRKTLL 105
Cdd:cd13540     1 TITVFHAGSLSAPFKALGPAFeKAHTGVRVQGEASGSVGLARKVtDLGKPADVFISADYSLIP--KLMIPKYADWYVPFA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468437435 106 GNSLVVVapkASEQKAFTID-SKTNWTNLL--NGGRLAVGDPEHVPAGIYAKEALQK----LGAWDTLAPKLA---PAED 175
Cdd:cd13540    79 SNEMVIA---YTNKSKYADEiNTDNWYEILlrPDVKIGRSDPNLDPCGYRTLMTLKLaekyYNQPDLYSEKLLgnnKKVA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468437435 176 VRGA----LALVERNEAPLGIVYGSDAV----------------------ASKGVKVVATFPEDSH-KKVEYPIAIVDGH 228
Cdd:cd13540   156 QRPKetdlLALLESGQIDYAFIYKSVAKqhglpyielpdeinlsdpsyadFYAKSKYTLGDGGTIHgKPIVYGATIPKNA 235
                         250       260
                  ....*....|....*....|....*...
gi 1468437435 229 SN-ATVSAFYDYLKGPQAADIFKRYGFT 255
Cdd:cd13540   236 PNpEAARAFVKFLLSPEGQEILEENGLE 263
PRK04168 PRK04168
tungstate ABC transporter substrate-binding protein WtpA;
6-83 5.64e-06

tungstate ABC transporter substrate-binding protein WtpA;


Pssm-ID: 235236  Cd Length: 334  Bit Score: 46.52  E-value: 5.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468437435   6 LRLFAGATLSLSVAGHALA---DEGKITVFAAASLTNAMQDIAAQYKKE-KNVDVVSSFASSSTLARQI-EAGAPADLFI 80
Cdd:PRK04168    8 ILIILLLLLVLAFAGCVTAfaePKGKLKIFHAGSLSVPFEEYEKEFEAYhPNVDVQREAGGSVKCVRKItELGKKADIMA 87

                  ...
gi 1468437435  81 SAD 83
Cdd:PRK04168   88 SAD 90
PBP2_PEB3_AcfC cd13519
Ligand-binding domain of a glycoprotein adhesion and an accessory colonization factor, a ...
40-253 8.25e-05

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


Pssm-ID: 270237 [Multi-domain]  Cd Length: 227  Bit Score: 42.68  E-value: 8.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468437435  40 AMQDIAAQYKKEKNVDVVSSFASSSTLARQieAGAPADLFISADQKWMDYAVD--KKSIDTASRKTL-LGNSLVVVapka 116
Cdd:cd13519    13 AMKEAAKKFEKKTGVKVNVTAGPQPTWEDK--AKQDADIIYGGSEQMMTDFISalPKLFDSSDIKPLyLRPSAILV---- 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468437435 117 seqKAFTIDSKTNWTNLLNGGrlavgdpehvpAGIYAKEALQKLGAWDTLAPKLAPAEDVRG------------ALAL-- 182
Cdd:cd13519    87 ---RKGNPKKIKGLKDLLKPG-----------VKILVVNGAGQTGLWEDMAGRTGDIETVRAfrknivvfaknsGAARka 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1468437435 183 -VERNEAPLGIVYGSDAVASKGVKVVATFPEDSHKKVEYPIAIV-DGHSNATVSAFYDYLKGPQAADIFKRYG 253
Cdd:cd13519   153 wKQDPNIDAWITWNIWQKANPDIADFVELEKDYVIYRDMNVALTkKGLQNPEAQEFIDYLSSKEAQAIFKKWG 225
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
40-246 5.56e-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: 37.40  E-value: 5.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468437435  40 AMQDIAAQYKKEK-NVDVVSSFASSSTLAR----QIEAG-APADLFISADQKWMDYA--------------VDKKSIDTA 99
Cdd:pfam01547   9 ALQALVKEFEKEHpGIKVEVESVGSGSLAQklttAIAAGdGPADVFASDNDWIAELAkaglllplddyvanYLVLGVPKL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468437435 100 SRKTLLGNSLVVVAPKASEQKAfTIDSKTNWTNLLNGGRLAVGDPEHvPAGIYAKEALQKLGAW---------------- 163
Cdd:pfam01547  89 YGVPLAAETLGLIYNKDLFKKA-GLDPPKTWDELLEAAKKLKEKGKS-PGGAGGGDASGTLGYFtlallaslggplfdkd 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468437435 164 --------------------------DTLAPKLAPAEDVRGALALVERNEAPLGIVYGSDAVASKGVKVVATFPEDSHKK 217
Cdd:pfam01547 167 gggldnpeavdaityyvdlyakvlllKKLKNPGVAGADGREALALFEQGKAAMGIVGPWAALAANKVKLKVAFAAPAPDP 246
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1468437435 218 VE-----------------YPIAIVDGHSN-ATVSAFYDYLKGPQAA 246
Cdd:pfam01547 247 KGdvgyaplpagkggkgggYGLAIPKGSKNkEAAKKFLDFLTSPEAQ 293
 
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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