NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|880808994|ref|WP_048661151|]
View 

phosphate ABC transporter substrate-binding protein [Vibrio crassostreae]

Protein Classification

phosphate ABC transporter substrate-binding protein( domain architecture ID 10194586)

phosphate ABC transporter substrate-binding protein similar to Bacillus subtilis phosphate-binding protein PstS, part of the ABC transporter complex PstSACB that is involved in phosphate import

CATH:  3.40.190.10
Gene Ontology:  GO:0140359|GO:0042626|GO:0055052|GO:0006817
PubMed:  26517916|24638992|25750732
TCDB:  3.A.1

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PBP2_phosphate_like_1 cd13653
Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 ...
 21-266 1.98e-89

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: 265.20  E-value: 1.98e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994  21 AQETTISGSTSVSRVMDVLAEEYNKTHPDNYIAVQGIGSTAGITMVNKGVSDIGMSSRYLTDRE--QNDKLKVFPIAFDG 98
Cdd:cd13653    1 SGTITISGSTTVAPLAEALAEAFMEKHPGVRIEVQGGGSGTGIKALIEGTADIGMASRPLKAEEkaAASGLVEHVIALDG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994  99 LAVVTNRSNGVSNVTREQLFDIYKGKITNWKAIGGADQPIAVVTREASSGSRYSFESLLGLTKiindrlvsDINPNNLVV 178
Cdd:cd13653   81 IAIIVNPDNPVKNLTLEQLRDIFSGKITNWKEVGGPDGPIVVISREEGSGTRETFEELVLGKK--------DFAKNAVVV 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994 179 NSNSMVKTIVNHNPHAIGFISVGSID-RSIKAITFEGVEPTSKNIANHSYELARPFLLLHKTDSvSDESKDFIKFVKSKQ 257
Cdd:cd13653  153 PSNGAVVQAVAKNPNAIGYVSLGYVDdSKVKALSVDGVAPTPENIKSGKYPLSRPLYLYTKGEP-SGLVKAFIDFALSPE 231


                 ....*....
gi 880808994 258 GQDLIEEYG 266
Cdd:cd13653  232 GQAIVEKLG 240
 
Name Accession Description Interval E-value
PBP2_phosphate_like_1 cd13653
Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 ...
 21-266 1.98e-89

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: 265.20  E-value: 1.98e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994  21 AQETTISGSTSVSRVMDVLAEEYNKTHPDNYIAVQGIGSTAGITMVNKGVSDIGMSSRYLTDRE--QNDKLKVFPIAFDG 98
Cdd:cd13653    1 SGTITISGSTTVAPLAEALAEAFMEKHPGVRIEVQGGGSGTGIKALIEGTADIGMASRPLKAEEkaAASGLVEHVIALDG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994  99 LAVVTNRSNGVSNVTREQLFDIYKGKITNWKAIGGADQPIAVVTREASSGSRYSFESLLGLTKiindrlvsDINPNNLVV 178
Cdd:cd13653   81 IAIIVNPDNPVKNLTLEQLRDIFSGKITNWKEVGGPDGPIVVISREEGSGTRETFEELVLGKK--------DFAKNAVVV 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994 179 NSNSMVKTIVNHNPHAIGFISVGSID-RSIKAITFEGVEPTSKNIANHSYELARPFLLLHKTDSvSDESKDFIKFVKSKQ 257
Cdd:cd13653  153 PSNGAVVQAVAKNPNAIGYVSLGYVDdSKVKALSVDGVAPTPENIKSGKYPLSRPLYLYTKGEP-SGLVKAFIDFALSPE 231


                 ....*....
gi 880808994 258 GQDLIEEYG 266
Cdd:cd13653  232 GQAIVEKLG 240
PstS COG0226
ABC-type phosphate transport system, periplasmic component [Inorganic ion transport and ...
 25-267 4.18e-75

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


Pssm-ID: 439996 [Multi-domain]  Cd Length: 275  Bit Score: 229.77  E-value: 4.18e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994  25 TISGSTSVSRVMDVLAEEYNKTHPDNYIAVQGIGSTAGITMVNKGVSDIGMSSRYLTDREQ------NDKLKVFPIAFDG 98
Cdd:COG0226    7 TIAGSSTVYPLAEAWAEAFQKANPGVTINVQSGGSGGGIKQFIAGTVDIGNSSRPLKDEELeaakenGVELVEIPVAIDG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994  99 LAVVTNRSNGVSNVTREQLFDIYKGKITNWKAIGGA--DQPIAVVTREASSGSRYSFESLLGLTKiindrlvSDINPNNL 176
Cdd:COG0226   87 IAVVVNPDNPVKNLTGEQLADIFSGKITNWNDIGGKlpDEPITVVGRSDGSGTTDYFTEYLLGVG-------AEVREGVE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994 177 VVNSNSMVKTIVNHNPHAIGFISVGSID-RSIKAITFE-----GVEPTSKNIANHSYELARP-FLLLHKT-DSVSDESKD 248
Cdd:COG0226  160 GAEGNEGVVQAVAQTPGAIGYVGLSYAEqNKLKALAIDnkagkFVEPTAENIAAGSYPLSRPlYIYVKKEpDAKAPAVKA 239

                        250
                 ....*....|....*....
gi 880808994 249 FIKFVKSKQGQDLIEEYGY 267
Cdd:COG0226  240 FLDFVLSDGGQKIVEKLGY 258
ptsS_2 TIGR02136
phosphate binding protein; Members of this family are phosphate-binding proteins. Most are ...
 25-267 1.47e-69

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: 216.15  E-value: 1.47e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994   25 TISGSTSVSRVMDVLAEEYNKTHPDNYIAVQGIGSTAGITMVNKGVSDIGMSSRYLTDREQ------NDKLKVFPIAFDG 98
Cdd:TIGR02136  39 TIDGSTTVAPLAEAAAEEFQKIHPGVSVTVQGAGSGTGIKALINGTVDIGNSSRPIKDEELqkdkqkGIKLIEHKVAVDG 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994   99 LAVVTNRSN-GVSNVTREQLFDIYKGKITNWKAIGGA--DQPIAVVTREASSGSRYSFEsllglTKIINDRlvsDINPNN 175
Cdd:TIGR02136 119 LAVVVNKKNvPVDDLTVEQLKKIYSGEITNWKEVGGDlpNKPIVVVGRNAGSGTRDTFE-----EEVMGKA---KIKPGK 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994  176 LVVNSNSMVKTIVNHNPHAIGFISVGSIDRSIKAITFEGVEPTSKNIANHSYELARP-FLLLHKTDSVSDESKDFIKFVK 254
Cdd:TIGR02136 191 NEQESNGAVVSIVSSNPGAIGYLGLGYVDDSVKTLKVNGVEPSKENIANGSYPLSRPlFMYVNGKPKKPELVAEFIDFVL 270

                         250
                  ....*....|....
gi 880808994  255 SKQGQD-LIEEYGY 267
Cdd:TIGR02136 271 SDDGGErIVEELGY 284
PBP_like pfam12727
PBP superfamily domain; This family belongs to the periplasmic binding domain superfamily. It ...
 40-253 4.27e-36

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


Pssm-ID: 463683 [Multi-domain]  Cd Length: 192  Bit Score: 127.31  E-value: 4.27e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994   40 AEEYNKTHPDNYIAVQGIGSTAGITMVNKGVSDIGMSSRYLTD-REQNdkLKVFPIAFDGLAVVTnrsngVSNVTREQLF 118
Cdd:pfam12727   1 AEELARKHPGVRLAVAYVGSLGGLAALRRGEAHIAGIHLLDPEtGEYN--LPFLRRLLPGIPVVL-----INLAYREQGL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994  119 DIYKG---KITNWKAIggADQPIAVVTREASSGSRYSFESLLGLTKIINdrlvSDINPNNLVVNSNSMVKTIVNHNPHAI 195
Cdd:pfam12727  74 VVAPGnpkGITGWEDL--ARPGLRFVNRQRGSGTRVLLDELLRKAGIDP----SDINGYDREERSHLAVAAAVASGRADA 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 880808994  196 GFiSVGSIDRSIKAITFegvEPTSKnianhsyelARPFLLLHKTDSVSDESKDFIKFV 253
Cdd:pfam12727 148 GL-GIEAAARALGGLDF---IPLAR---------ERYDLVIPKEALDDPAVQALLEVL 192
PRK10918 PRK10918
phosphate ABC transporter substrate-binding protein PstS;
21-261 4.35e-10

phosphate ABC transporter substrate-binding protein PstS;


Pssm-ID: 182837  Cd Length: 346  Bit Score: 59.46  E-value: 4.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994  21 AQETTISGSTSVSRVMDVLAEEYNKtHPDNYIAVQGIGSTAGITMVNKGVSDIGMSSRYLTDRE-QNDKLKVFPIAFDGL 99
Cdd:PRK10918  26 AASLTGAGATFPAPVYAKWADTYQK-ETGNKVNYQGIGSSGGVKQIIANTVDFGASDAPLSDEKlAQEGLFQFPTVIGGV 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994 100 AVVTNRS---NGVSNVTREQLFDIYKGKITNWK--AIGG-------ADQPIAVVTREASSGSRYSFESLLGLtkiINDRL 167
Cdd:PRK10918 105 VLAVNIPglkSGELVLDGKTLGDIYLGKIKKWNdeAIAKlnpgvklPSQNIAVVRRADGSGTSFVFTSYLAK---VNEEW 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994 168 VSDIN-------PNNLVVNSNSMVKTIVNHNPHAIGFISVGSIDRS----IKAITFEG--VEPTSKNIA----------- 223
Cdd:PRK10918 182 KSKVGagstvnwPTGLGGKGNDGIAAFVQRLPGAIGYVEYAYAKQNnlayTKLISADGkpVSPTEESFSnaakgadwsks 261

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 880808994 224 ------NHSYELARP-----FLLLHKTDSVSDESKDFIKFVK------SKQGQDL 261
Cdd:PRK10918 262 faqdltNQKGDDAWPitsttFILVHKDQKKPEQGAEVLKFFDwaykngAKQANDL 316
 
Name Accession Description Interval E-value
PBP2_phosphate_like_1 cd13653
Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 ...
 21-266 1.98e-89

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: 265.20  E-value: 1.98e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994  21 AQETTISGSTSVSRVMDVLAEEYNKTHPDNYIAVQGIGSTAGITMVNKGVSDIGMSSRYLTDRE--QNDKLKVFPIAFDG 98
Cdd:cd13653    1 SGTITISGSTTVAPLAEALAEAFMEKHPGVRIEVQGGGSGTGIKALIEGTADIGMASRPLKAEEkaAASGLVEHVIALDG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994  99 LAVVTNRSNGVSNVTREQLFDIYKGKITNWKAIGGADQPIAVVTREASSGSRYSFESLLGLTKiindrlvsDINPNNLVV 178
Cdd:cd13653   81 IAIIVNPDNPVKNLTLEQLRDIFSGKITNWKEVGGPDGPIVVISREEGSGTRETFEELVLGKK--------DFAKNAVVV 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994 179 NSNSMVKTIVNHNPHAIGFISVGSID-RSIKAITFEGVEPTSKNIANHSYELARPFLLLHKTDSvSDESKDFIKFVKSKQ 257
Cdd:cd13653  153 PSNGAVVQAVAKNPNAIGYVSLGYVDdSKVKALSVDGVAPTPENIKSGKYPLSRPLYLYTKGEP-SGLVKAFIDFALSPE 231


                 ....*....
gi 880808994 258 GQDLIEEYG 266
Cdd:cd13653  232 GQAIVEKLG 240
PBP2_phosphate cd13566
Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 ...
 21-266 5.73e-82

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 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: 270284 [Multi-domain]  Cd Length: 245  Bit Score: 246.34  E-value: 5.73e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994  21 AQETTISGSTSVSRVMDVLAEEYNKTHPDNYIAVQGIGSTAGITMVNKGVSDIGMSSRYLTDREQ------NDKLKVFPI 94
Cdd:cd13566    1 SGTITIAGSSTVAPLAEALAEEFMKKHPGVRVTVQGGGSGAGIKALIAGTADIAMASRPLKDEEKaaaeanGIELVEFVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994  95 AFDGLAVVTNRSNGVSNVTREQLFDIYKGKITNWKAIGGADQPIAVVTREASSGSRYSFESLLGLTKiindrlvsDINPN 174
Cdd:cd13566   81 AYDGIAVIVNPDNPVASLTLEQLRDIFTGKITNWSEVGGPDEPIVVYGRDEGSGTRDYFEELVLGKG--------EFIRN 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994 175 NLVVNSNSMVKTIVNHNPHAIGFISVGSIDRS--IKAITFEGVEPTSKNIANHSYELARPFLLLHKTDSvSDESKDFIKF 252
Cdd:cd13566  153 AVVAPSNGALVQAVAGDPNAIGYVGLGYVDENkkVKALKVDGVAPTVENIKSGKYPLSRPLFLYTKGEP-SPAVKAFIDF 231

                        250
                 ....*....|....
gi 880808994 253 VKSKQGQDLIEEYG 266
Cdd:cd13566  232 ALSPEGQKIIEEVG 245
PstS COG0226
ABC-type phosphate transport system, periplasmic component [Inorganic ion transport and ...
 25-267 4.18e-75

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


Pssm-ID: 439996 [Multi-domain]  Cd Length: 275  Bit Score: 229.77  E-value: 4.18e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994  25 TISGSTSVSRVMDVLAEEYNKTHPDNYIAVQGIGSTAGITMVNKGVSDIGMSSRYLTDREQ------NDKLKVFPIAFDG 98
Cdd:COG0226    7 TIAGSSTVYPLAEAWAEAFQKANPGVTINVQSGGSGGGIKQFIAGTVDIGNSSRPLKDEELeaakenGVELVEIPVAIDG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994  99 LAVVTNRSNGVSNVTREQLFDIYKGKITNWKAIGGA--DQPIAVVTREASSGSRYSFESLLGLTKiindrlvSDINPNNL 176
Cdd:COG0226   87 IAVVVNPDNPVKNLTGEQLADIFSGKITNWNDIGGKlpDEPITVVGRSDGSGTTDYFTEYLLGVG-------AEVREGVE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994 177 VVNSNSMVKTIVNHNPHAIGFISVGSID-RSIKAITFE-----GVEPTSKNIANHSYELARP-FLLLHKT-DSVSDESKD 248
Cdd:COG0226  160 GAEGNEGVVQAVAQTPGAIGYVGLSYAEqNKLKALAIDnkagkFVEPTAENIAAGSYPLSRPlYIYVKKEpDAKAPAVKA 239

                        250
                 ....*....|....*....
gi 880808994 249 FIKFVKSKQGQDLIEEYGY 267
Cdd:COG0226  240 FLDFVLSDGGQKIVEKLGY 258
PBP2_phosphate_binding cd01006
Substrate binding domain of ABC-type phosphate transporter, a member of the type 2 ...
 21-266 1.94e-70

Substrate binding domain of ABC-type phosphate transporter, a member of the type 2 periplasmic-binding fold superfamily; This phosphate-binding domain shows significant homology to the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. 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: 270227 [Multi-domain]  Cd Length: 253  Bit Score: 217.51  E-value: 1.94e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994  21 AQETTISGSTSVSRVMDVLAEEYNKTHPDNYIAVQGIGSTAGITMVNKGVSDIGMSSRYLTDRE-QNDKLKVFPIAFDGL 99
Cdd:cd01006    1 ASELTISGSTSVAPI*DVWAEKYNQQHPETYVAVQGVGSTAGISQLKAGTVDIGASDAYLSESEaANKGLHTFTLAIDGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994 100 AVVTNRSNGVSNVT--REQLFDIYKGKITNWKAIGGA---------DQPIAVVTREASSGSRYSFESLLGLTKIIND--- 165
Cdd:cd01006   81 AIVVNQPGPVTNLTlnGKQLYGIYKGQIKNWDDVGIAalnpgvnlpDQKIAVVTREDGSGTRFSFTSYLGKTKTEKDgkg 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994 166 -RLVSDINPNNLVVNSNSMVKTIVNHNPHAIGFISVGSIDRS-IKAITFegveptsknianhsYELARPFLLLHKTD--- 240
Cdd:cd01006  161 tTEVSDVAPTALGVNGNSG*KTLVNHNPGAVGYISIGSVDQSsLKAIQL--------------YPISRPFLILHYSDqkd 226

                        250       260
                 ....*....|....*....|....*..
gi 880808994 241 -SVSDESKDFIKFVKSKQGQDLIEEYG 266
Cdd:cd01006  227 aATDEQTKEFIAWAKSEGAAKLIVEYG 253
ptsS_2 TIGR02136
phosphate binding protein; Members of this family are phosphate-binding proteins. Most are ...
 25-267 1.47e-69

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: 216.15  E-value: 1.47e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994   25 TISGSTSVSRVMDVLAEEYNKTHPDNYIAVQGIGSTAGITMVNKGVSDIGMSSRYLTDREQ------NDKLKVFPIAFDG 98
Cdd:TIGR02136  39 TIDGSTTVAPLAEAAAEEFQKIHPGVSVTVQGAGSGTGIKALINGTVDIGNSSRPIKDEELqkdkqkGIKLIEHKVAVDG 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994   99 LAVVTNRSN-GVSNVTREQLFDIYKGKITNWKAIGGA--DQPIAVVTREASSGSRYSFEsllglTKIINDRlvsDINPNN 175
Cdd:TIGR02136 119 LAVVVNKKNvPVDDLTVEQLKKIYSGEITNWKEVGGDlpNKPIVVVGRNAGSGTRDTFE-----EEVMGKA---KIKPGK 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994  176 LVVNSNSMVKTIVNHNPHAIGFISVGSIDRSIKAITFEGVEPTSKNIANHSYELARP-FLLLHKTDSVSDESKDFIKFVK 254
Cdd:TIGR02136 191 NEQESNGAVVSIVSSNPGAIGYLGLGYVDDSVKTLKVNGVEPSKENIANGSYPLSRPlFMYVNGKPKKPELVAEFIDFVL 270

                         250
                  ....*....|....
gi 880808994  255 SKQGQD-LIEEYGY 267
Cdd:TIGR02136 271 SDDGGErIVEELGY 284
PBP_like pfam12727
PBP superfamily domain; This family belongs to the periplasmic binding domain superfamily. It ...
 40-253 4.27e-36

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


Pssm-ID: 463683 [Multi-domain]  Cd Length: 192  Bit Score: 127.31  E-value: 4.27e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994   40 AEEYNKTHPDNYIAVQGIGSTAGITMVNKGVSDIGMSSRYLTD-REQNdkLKVFPIAFDGLAVVTnrsngVSNVTREQLF 118
Cdd:pfam12727   1 AEELARKHPGVRLAVAYVGSLGGLAALRRGEAHIAGIHLLDPEtGEYN--LPFLRRLLPGIPVVL-----INLAYREQGL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994  119 DIYKG---KITNWKAIggADQPIAVVTREASSGSRYSFESLLGLTKIINdrlvSDINPNNLVVNSNSMVKTIVNHNPHAI 195
Cdd:pfam12727  74 VVAPGnpkGITGWEDL--ARPGLRFVNRQRGSGTRVLLDELLRKAGIDP----SDINGYDREERSHLAVAAAVASGRADA 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 880808994  196 GFiSVGSIDRSIKAITFegvEPTSKnianhsyelARPFLLLHKTDSVSDESKDFIKFV 253
Cdd:pfam12727 148 GL-GIEAAARALGGLDF---IPLAR---------ERYDLVIPKEALDDPAVQALLEVL 192
PBP_like_2 pfam12849
PBP superfamily domain; This domain belongs to the periplasmic binding protein superfamily.
 21-255 4.68e-35

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


Pssm-ID: 432831 [Multi-domain]  Cd Length: 267  Bit Score: 126.89  E-value: 4.68e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994   21 AQETTISGSTSVSRVMDVLAEEYNKTHPDNYIAVQGIGSTAGITMVNKGVSDIGMSSRYLTDRE-------QNDKLKVFP 93
Cdd:pfam12849   9 VGTILIAGSSTQAPGLLDLAEAFEKKYPGAKVKVTSVGSGEGIKALLNGDVDVALVSRPLTEEEfeafganGAGGLVEVP 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994   94 IAFDGLAVVTNRSNGVSNVTREQLFDIYKGKITNWKAiGGADQPIAVVTREASSGSRYSFESLLGLTKIINDRLVSDINP 173
Cdd:pfam12849  89 VAYDGIAIVVNKDNPANILTVEALKKIFSGKITNWND-GGPDGPIKFVSRGDNSGTTELFSTHLKEKGPWGAAGIGAAGS 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994  174 NnlvvnsnsMVKTIVNhNPHAIGFISVG-------------------SIDRSIKAITFEG----VEPTSKNIANHSYELA 230
Cdd:pfam12849 168 P--------GVASVVA-GPGAIGYVEVSyalanlgytladvaggtylSFAKALKVAKINPgaglVIPLEEAIADGDYPLS 238

                         250       260
                  ....*....|....*....|....*..
gi 880808994  231 RP-FLLLHKTDS-VSDESKDFIKFVKS 255
Cdd:pfam12849 239 RPyYVIVKNPPKgPAPLAKAFLDFLLS 265
PBP2_PstS cd13565
Substrate binding domain of ABC-type phosphate transporter, a member of the type 2 ...
 25-263 3.99e-30

Substrate binding domain of ABC-type phosphate transporter, a member of the type 2 periplasmic-binding fold superfamily; This subfamily contians phosphate binding domain 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 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: 270283 [Multi-domain]  Cd Length: 254  Bit Score: 113.48  E-value: 3.99e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994  25 TISGSTSVSRVMDVLAEEYNKTHPDNYIAVQGIGSTAGITMVNKGVSDIGMSSRYLTDREQ---NDKLKVFPIAFDGLAV 101
Cdd:cd13565    5 TGAGATFPAPLYQKWIDEYKKAHPGVKINYQSIGSGAGIKQFIAGTVDFGASDAPLSDAELakaGGGLLQIPTVIGAVVV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994 102 VTNRsNGVS---NVTREQLFDIYKGKITNW--KAIGGA-------DQPIAVVTREASSGSRYSFESLLGL------TKII 163
Cdd:cd13565   85 AYNL-PGVKgllLLSGEVLADIFLGKITKWndPAIAALnpgvnlpDTPITVVHRSDGSGTTFIFTDYLSAvspewkDKVG 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994 164 NDRLVSdiNPNNLVVNSNSMVKTIVNHNPHAIGFISVGSIDrsIKAITFEGVEPtsknIANHSYelarpfLLLHKT---D 240
Cdd:cd13565  164 AGKSVA--WPVGLGGKGNEGVAAAVKQTPGSIGYVELSYAL--QNGLPAAALYP----IVGFTY------ILVKKDykdA 229

                        250       260
                 ....*....|....*....|...
gi 880808994 241 SVSDESKDFIKFVKSKQGQDLIE 263
Cdd:cd13565  230 EKAKAVKKFLKWALTEGQKFAAD 252
PBP2_phosphate_like_2 cd13654
Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 ...
 26-266 5.14e-30

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: 270372  Cd Length: 259  Bit Score: 113.12  E-value: 5.14e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994  26 ISGSTSVSRVMDVLAEEYNKTHPDNYIAVQGIGSTAGITMVNKGVSDIGMSSRYLTDREQ------NDKLKVFPIAFDGL 99
Cdd:cd13654    6 IDGSSTVYPITEAVAEEFGKSGPGVTVTVGSSGTGGGFKKFCAGETDISNASRPIKDSEAelceanGIEYIELPVAYDGL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994 100 AVVTNRSNG-VSNVTREQLFDI--YKGKITNWKAIGGA--DQPIAVVTREASSGSRYSF-ESLLGLTKIIndrlVSDINP 173
Cdd:cd13654   86 TVVVNPANDwAKCLTELELKSIwaAESPITTWSDVRPSwpDEPIELYGPGTDSGTFDYFtEAIVGEGGSI----REDYTA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994 174 NNlvvNSNSMVKTIVNhNPHAIGFISVG---SIDRSIKAITFEGVEPT-----SKNIANHSYELARPFLLLHKTDSVSDE 245
Cdd:cd13654  162 SE---DDNVLVQGVAG-DKNALGFFGYAyyeENGDKLKAVKIDGGEGTvapsaETTISGGYYPLSRPLFIYVKKASLAEK 237

                        250       260
                 ....*....|....*....|...
gi 880808994 246 S--KDFIKFVKSkQGQDLIEEYG 266
Cdd:cd13654  238 PavAAFVKFYLE-NAQEAAGEVG 259
3a0107s03 TIGR00975
phosphate ABC transporter, phosphate-binding protein; This family represents one type of ...
 25-198 4.88e-17

phosphate ABC transporter, phosphate-binding protein; This family represents one type of (periplasmic, in Gram-negative bacteria) phosphate-binding protein found in phosphate ABC (ATP-binding cassette) transporters. This protein is accompanied, generally in the same operon, by an ATP binding protein and (usually) two permease proteins. [Transport and binding proteins, Anions]


Pssm-ID: 273374 [Multi-domain]  Cd Length: 313  Bit Score: 79.02  E-value: 4.88e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994   25 TISGSTSVSRVMDVLAEEYNKTHPDNYIAVQGIGSTAGITMVNKGVSDIGMSSRYLTDRE---QNDKLKVFPIAFDGLAV 101
Cdd:TIGR00975   2 TGAGSTFPAPLYTKWFPDFQKSNPGVTINYQGIGSGAGIAQFAAGTVDFGASDAPLSEADlaaAGSGLLNFPTVIGAIVV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994  102 VTNrSNGVS---NVTREQLFDIYKGKITNWK--AIGGA-------DQPIAVVTREASSGSRYSFESLLGLtkiINDRLVS 169
Cdd:TIGR00975  82 TYN-LPGVSeklKLDGPVLAKIFLGKIKQWNdpAIAALnpgvklpGTAITVVHRSDGSGTTFNFTNYLSK---VSPEWGK 157

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 880808994  170 DINPNNLV-------VNSNSMVKTIVNHNPHAIGFI 198
Cdd:TIGR00975 158 KVGAGKTVqwpagvgGKGNDGVVAGVKQTPGAIGYV 193
PRK10918 PRK10918
phosphate ABC transporter substrate-binding protein PstS;
21-261 4.35e-10

phosphate ABC transporter substrate-binding protein PstS;


Pssm-ID: 182837  Cd Length: 346  Bit Score: 59.46  E-value: 4.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994  21 AQETTISGSTSVSRVMDVLAEEYNKtHPDNYIAVQGIGSTAGITMVNKGVSDIGMSSRYLTDRE-QNDKLKVFPIAFDGL 99
Cdd:PRK10918  26 AASLTGAGATFPAPVYAKWADTYQK-ETGNKVNYQGIGSSGGVKQIIANTVDFGASDAPLSDEKlAQEGLFQFPTVIGGV 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994 100 AVVTNRS---NGVSNVTREQLFDIYKGKITNWK--AIGG-------ADQPIAVVTREASSGSRYSFESLLGLtkiINDRL 167
Cdd:PRK10918 105 VLAVNIPglkSGELVLDGKTLGDIYLGKIKKWNdeAIAKlnpgvklPSQNIAVVRRADGSGTSFVFTSYLAK---VNEEW 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994 168 VSDIN-------PNNLVVNSNSMVKTIVNHNPHAIGFISVGSIDRS----IKAITFEG--VEPTSKNIA----------- 223
Cdd:PRK10918 182 KSKVGagstvnwPTGLGGKGNDGIAAFVQRLPGAIGYVEYAYAKQNnlayTKLISADGkpVSPTEESFSnaakgadwsks 261

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 880808994 224 ------NHSYELARP-----FLLLHKTDSVSDESKDFIKFVK------SKQGQDL 261
Cdd:PRK10918 262 faqdltNQKGDDAWPitsttFILVHKDQKKPEQGAEVLKFFDwaykngAKQANDL 316
PBP2_CysL_like cd08420
C-terminal substrate binding domain of LysR-type transcriptional regulator CysL, which ...
 37-253 4.08e-07

C-terminal substrate binding domain of LysR-type transcriptional regulator CysL, which activates the transcription of the cysJI operon encoding sulfite reductase, contains the type 2 periplasmic binding fold; CysL, also known as YwfK, is a regular of sulfur metabolism in Bacillus subtilis. Sulfur is required for the synthesis of proteins and essential cofactors in all living organism. Sulfur can be assimilated either from inorganic sources (sulfate and thiosulfate), or from organic sources (sulfate esters, sulfamates, and sulfonates). CysL activates the transcription of the cysJI operon encoding sulfite reductase, which reduces sulfite to sulfide. Both cysL mutant and cysJI mutant are unable to grow using sulfate or sulfite as the sulfur source. Like other LysR-type regulators, CysL also negatively regulates its own transcription. In Escherichia coli, three LysR-type activators are involved in the regulation of sulfur metabolism: CysB, Cbl and MetR. The topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. 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: 176112 [Multi-domain]  Cd Length: 201  Bit Score: 49.41  E-value: 4.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994  37 DVLAEeYNKTHPDnyIAVQ-GIGSTAGIT-MVNKGVSDIGmssryLTD-REQNDKLKVFPIAFDGLAVVTNRSN---GVS 110
Cdd:cd08420   17 RLLAR-FRKRYPE--VRVSlTIGNTEEIAeRVLDGEIDLG-----LVEgPVDHPDLIVEPFAEDELVLVVPPDHplaGRK 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994 111 NVTREQLfdiykgkitnwkaiggADQPIavVTREASSGSRYSFESLLgltkiindrLVSDINPNNL----VVNSNSMVKT 186
Cdd:cd08420   89 EVTAEEL----------------AAEPW--ILREPGSGTREVFERAL---------AEAGLDGLDLnivmELGSTEAIKE 141

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 880808994 187 IVNHNpHAIGFISVGSIDR-----SIKAITFEGVEPTsknianhsyelaRPF-LLLHKTDSVSDESKDFIKFV 253
Cdd:cd08420  142 AVEAG-LGISILSRLAVRKelelgRLVALPVEGLRLT------------RPFsLIYHKDKYLSPAAEAFLEFL 201
SBP_bac_11 pfam13531
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 25-268 8.56e-07

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


Pssm-ID: 463911 [Multi-domain]  Cd Length: 225  Bit Score: 48.80  E-value: 8.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994   25 TISGSTSVSRVMDVLAEEYnKTHPDNYIAVQGIGSTAGITMVNKGVS-D--IGMSSRYLTDREQNDKL---KVFPIAFDG 98
Cdd:pfam13531   1 TVAAAGGLAAALRELAAAF-EAETGVKVVVSYGGSGKLAKQIANGAPaDvfISADSAWLDKLAAAGLVvpgSRVPLAYSP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994   99 LAVVTNRSNgvsnvtreqlfdiyKGKITNWKAIGGADQPIAVVTREASSGSRYSFESL--LGLTKIINDRLVsdinpnNL 176
Cdd:pfam13531  80 LVIAVPKGN--------------PKDISGLADLLKPGVRLAVADPKTAPSGRAALELLekAGLLKALEKKVV------VL 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994  177 VVNSNSMVKTIVNhnphaiGFISVGSIDRSIkAITFEGVEPTSK-NIANHSY-ELARPFLLLHKTDSvSDESKDFIKFVK 254
Cdd:pfam13531 140 GENVRQALTAVAS------GEADAGIVYLSE-ALFPENGPGLEVvPLPEDLNlPLDYPAAVLKKAAH-PEAARAFLDFLL 211

                         250
                  ....*....|....
gi 880808994  255 SKQGQDLIEEYGYT 268
Cdd:pfam13531 212 SPEAQAILRKYGFR 225
ModA COG0725
ABC-type molybdate transport system, periplasmic Mo-binding protein ModA [Inorganic ion ...
 20-271 4.20e-06

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: 46.79  E-value: 4.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994  20 FAQETTISGSTSVSRVMDVLAEEYNKTHPDNYIAVQGIGSTAGITMVNKGVS-DIGMSS-----RYLTDREQNDKLKVFP 93
Cdd:COG0725   23 AAAELTVFAAASLKEALEELAAAFEKEHPGVKVELSFGGSGALARQIEQGAPaDVFISAdekymDKLAKKGLILAGSRVV 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994  94 IAFDGLAVVTNRSNgvsnvtreqlfdiyKGKITNWKAIGGADQPIAVVTREASSGSRYSFESL--LGLTKIINDRLVsdi 171
Cdd:COG0725  103 FATNRLVLAVPKGN--------------PADISSLEDLAKPGVRIAIGDPKTVPYGKYAKEALekAGLWDALKPKLV--- 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994 172 npnnlvvnsnsMVKTIvnhnPHAIGFISVGSID-----RSIkAITFEGVEPTSKnIANHSYELAR-PFLLLHKTDSvSDE 245
Cdd:COG0725  166 -----------LGENV----RQVLAYVESGEADagivyLSD-ALAAKGVLVVVE-LPAELYAPIVyPAAVLKGAKN-PEA 227

                        250       260
                 ....*....|....*....|....*.
gi 880808994 246 SKDFIKFVKSKQGQDLIEEYGYTRIK 271
Cdd:COG0725  228 AKAFLDFLLSPEAQAILEKYGFEPPK 253
PBP2_YvgL_like cd13537
Substrate binding domain of putative molybdate-binding protein YvgL and similar proteins;the ...
 23-268 8.64e-04

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: 39.58  E-value: 8.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994  23 ETTISGSTSVSRVMDVLAEEYNKTHPDNYIAVQGIGSTAGITMVNKGVS-DIGMSSryltDREQNDKLKVfpiafDGLAV 101
Cdd:cd13537    1 TLTVSAAASLKDALDEIATEYEKENPGVKITFNFGGSGTLQKQIESGAPaDVFFSA----AKKQMDALED-----KGLID 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994 102 VTNRSNGVSNvtreQLFDI----YKGKITNWKAIGGADQPIAVVTREASSGSRYSFESL--LGLTKIINDRLVsdinPNN 175
Cdd:cd13537   72 ASTRKNLLKN----KLVLIvpkdSDSKISSFDLTKDDVKKIAIGEPETVPAGKYAKEALekLGLWDEIESKLV----YGK 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808994 176 LVVNsnsmVKTIVNHNPHAIGFI----SVGSIDRSIKAitfEGVEPTSKNIAnhsYELARPflllhKTDSVSDESKDFIK 251
Cdd:cd13537  144 DVRQ----VLTYVETGNADAGFVyktdALINKKVKVVE---EAPEDTHTPII---YPIAVI-----KNSENKEEAQKFID 208

                        250
                 ....*....|....*..
gi 880808994 252 FVKSKQGQDLIEEYGYT 268
Cdd:cd13537  209 FLKSEEAKKIFEKYGFE 225
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH