|
Name |
Accession |
Description |
Interval |
E-value |
| ptsS_2 |
TIGR02136 |
phosphate binding protein; Members of this family are phosphate-binding proteins. Most are ... |
1-309 |
1.26e-106 |
|
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: 313.22 E-value: 1.26e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666597 1 MKlKRLMAAMTFVAAGVATANAVAAVDPAIPSYTKTTgvsgNLSSVGSDTLANLMTLWAENYKKEYPNVNIQIQAAGSST 80
Cdd:TIGR02136 1 MK-KRIFLLIGLAAALLAAAGCGGAIDSGIPDAKGSS----TITIDGSTTVAPLAEAAAEEFQKIHPGVSVTVQGAGSGT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666597 81 APPALTEGTANLGPMSRKMKDNELQAFETKyGYKPTAIPVAVDALAVFVHKDN-PIKGLTMAQVDAIFSStrlcgaktDV 159
Cdd:TIGR02136 76 GIKALINGTVDIGNSSRPIKDEELQKDKQK-GIKLIEHKVAVDGLAVVVNKKNvPVDDLTVEQLKKIYSG--------EI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666597 160 KTWGDLGvtGDLANKPLQLFGRNSVSGTYGYFKEEALCKGDFKPNVNEQPGSASVVQSISSSLNGIGYSGIGYKTASVKT 239
Cdd:TIGR02136 147 TNWKEVG--GDLPNKPIVVVGRNAGSGTRDTFEEEVMGKAKIKPGKNEQESNGAVVSIVSSNPGAIGYLGLGYVDDSVKT 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 523666597 240 ValaKKEGgefIEDTEENALNGKYPLSRFLYVYVNKAPNKPlaPLEAEFVKLVLSKQGQE-VVVKDGYIPL 309
Cdd:TIGR02136 225 L---KVNG---VEPSKENIANGSYPLSRPLFMYVNGKPKKP--ELVAEFIDFVLSDDGGErIVEELGYVPL 287
|
|
| PstS |
COG0226 |
ABC-type phosphate transport system, periplasmic component [Inorganic ion transport and ... |
38-321 |
2.95e-102 |
|
ABC-type phosphate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 439996 [Multi-domain] Cd Length: 275 Bit Score: 301.42 E-value: 2.95e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666597 38 GVSGNLSSVGSDTLANLMTLWAENYKKEYPNVNIQIQAAGSSTAPPALTEGTANLGPMSRKMKDNELQAFEtKYGYKPTA 117
Cdd:COG0226 1 AASGTITIAGSSTVYPLAEAWAEAFQKANPGVTINVQSGGSGGGIKQFIAGTVDIGNSSRPLKDEELEAAK-ENGVELVE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666597 118 IPVAVDALAVFVHKDNPIKGLTMAQVDAIFSStrlcgaktDVKTWGDLGvtGDLANKPLQLFGRNSVSGTYGYFKEEAL- 196
Cdd:COG0226 80 IPVAIDGIAVVVNPDNPVKNLTGEQLADIFSG--------KITNWNDIG--GKLPDEPITVVGRSDGSGTTDYFTEYLLg 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666597 197 CKGDFKPNVNEQPGSASVVQSISSSLNGIGYSGIGY-KTASVKTVALAKKEgGEFIEDTEENALNGKYPLSRFLYVYVNK 275
Cdd:COG0226 150 VGAEVREGVEGAEGNEGVVQAVAQTPGAIGYVGLSYaEQNKLKALAIDNKA-GKFVEPTAENIAAGSYPLSRPLYIYVKK 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 523666597 276 APNkPLAPLEAEFVKLVLSKQGQEVVVKDGYIPLPAKVAAKALADL 321
Cdd:COG0226 229 EPD-AKAPAVKAFLDFVLSDGGQKIVEKLGYVPLPDAVVEKVRAAL 273
|
|
| PBP2_phosphate |
cd13566 |
Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 ... |
40-305 |
2.60e-88 |
|
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: 264.83 E-value: 2.60e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666597 40 SGNLSSVGSDTLANLMTLWAENYKKEYPNVNIQIQAAGSSTAPPALTEGTANLGPMSRKMKDNELQAFEtKYGYKPTAIP 119
Cdd:cd13566 1 SGTITIAGSSTVAPLAEALAEEFMKKHPGVRVTVQGGGSGAGIKALIAGTADIAMASRPLKDEEKAAAE-ANGIELVEFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666597 120 VAVDALAVFVHKDNPIKGLTMAQVDAIFSStrlcgaktDVKTWGDLGvtgdLANKPLQLFGRNSVSGTYGYFKEEALCKG 199
Cdd:cd13566 80 IAYDGIAVIVNPDNPVASLTLEQLRDIFTG--------KITNWSEVG----GPDEPIVVYGRDEGSGTRDYFEELVLGKG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666597 200 DFKPNVNEQPGSASVVQSISSSLNGIGYSGIGY--KTASVKTVALAKKEGgefiedTEENALNGKYPLSRFLYVYVNKAP 277
Cdd:cd13566 148 EFIRNAVVAPSNGALVQAVAGDPNAIGYVGLGYvdENKKVKALKVDGVAP------TVENIKSGKYPLSRPLFLYTKGEP 221
|
250 260
....*....|....*....|....*...
gi 523666597 278 NkplaPLEAEFVKLVLSKQGQEVVVKDG 305
Cdd:cd13566 222 S----PAVKAFIDFALSPEGQKIIEEVG 245
|
|
| PBP_like_2 |
pfam12849 |
PBP superfamily domain; This domain belongs to the periplasmic binding protein superfamily. |
36-294 |
8.94e-36 |
|
PBP superfamily domain; This domain belongs to the periplasmic binding protein superfamily.
Pssm-ID: 432831 [Multi-domain] Cd Length: 267 Bit Score: 130.36 E-value: 8.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666597 36 TTGVSGNLSSVGSDTLANLMTLWAENYKKEYPNVNIQIQAAGSSTAPPALTEGTANLGPMSRKMKDNELQAFETKYGYKP 115
Cdd:pfam12849 5 SAPTVGTILIAGSSTQAPGLLDLAEAFEKKYPGAKVKVTSVGSGEGIKALLNGDVDVALVSRPLTEEEFEAFGANGAGGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666597 116 TAIPVAVDALAVFVHKDNPIKGLTMAQVDAIFSSTrlcgaktdVKTWGDLGvtgdlANKPLQLFGRNSVSGTYGYFKEEA 195
Cdd:pfam12849 85 VEVPVAYDGIAIVVNKDNPANILTVEALKKIFSGK--------ITNWNDGG-----PDGPIKFVSRGDNSGTTELFSTHL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666597 196 LCKGDFKpNVNEQPGSASVVQSISSSLNGIGYSGI-------GYKTASVKTV----------ALAKKEGGEFIEDTEENA 258
Cdd:pfam12849 152 KEKGPWG-AAGIGAAGSPGVASVVAGPGAIGYVEVsyalanlGYTLADVAGGtylsfakalkVAKINPGAGLVIPLEEAI 230
|
250 260 270
....*....|....*....|....*....|....*.
gi 523666597 259 LNGKYPLSRFLYVYVNKAPnKPLAPLEAEFVKLVLS 294
Cdd:pfam12849 231 ADGDYPLSRPYYVIVKNPP-KGPAPLAKAFLDFLLS 265
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ptsS_2 |
TIGR02136 |
phosphate binding protein; Members of this family are phosphate-binding proteins. Most are ... |
1-309 |
1.26e-106 |
|
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: 313.22 E-value: 1.26e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666597 1 MKlKRLMAAMTFVAAGVATANAVAAVDPAIPSYTKTTgvsgNLSSVGSDTLANLMTLWAENYKKEYPNVNIQIQAAGSST 80
Cdd:TIGR02136 1 MK-KRIFLLIGLAAALLAAAGCGGAIDSGIPDAKGSS----TITIDGSTTVAPLAEAAAEEFQKIHPGVSVTVQGAGSGT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666597 81 APPALTEGTANLGPMSRKMKDNELQAFETKyGYKPTAIPVAVDALAVFVHKDN-PIKGLTMAQVDAIFSStrlcgaktDV 159
Cdd:TIGR02136 76 GIKALINGTVDIGNSSRPIKDEELQKDKQK-GIKLIEHKVAVDGLAVVVNKKNvPVDDLTVEQLKKIYSG--------EI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666597 160 KTWGDLGvtGDLANKPLQLFGRNSVSGTYGYFKEEALCKGDFKPNVNEQPGSASVVQSISSSLNGIGYSGIGYKTASVKT 239
Cdd:TIGR02136 147 TNWKEVG--GDLPNKPIVVVGRNAGSGTRDTFEEEVMGKAKIKPGKNEQESNGAVVSIVSSNPGAIGYLGLGYVDDSVKT 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 523666597 240 ValaKKEGgefIEDTEENALNGKYPLSRFLYVYVNKAPNKPlaPLEAEFVKLVLSKQGQE-VVVKDGYIPL 309
Cdd:TIGR02136 225 L---KVNG---VEPSKENIANGSYPLSRPLFMYVNGKPKKP--ELVAEFIDFVLSDDGGErIVEELGYVPL 287
|
|
| PstS |
COG0226 |
ABC-type phosphate transport system, periplasmic component [Inorganic ion transport and ... |
38-321 |
2.95e-102 |
|
ABC-type phosphate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 439996 [Multi-domain] Cd Length: 275 Bit Score: 301.42 E-value: 2.95e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666597 38 GVSGNLSSVGSDTLANLMTLWAENYKKEYPNVNIQIQAAGSSTAPPALTEGTANLGPMSRKMKDNELQAFEtKYGYKPTA 117
Cdd:COG0226 1 AASGTITIAGSSTVYPLAEAWAEAFQKANPGVTINVQSGGSGGGIKQFIAGTVDIGNSSRPLKDEELEAAK-ENGVELVE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666597 118 IPVAVDALAVFVHKDNPIKGLTMAQVDAIFSStrlcgaktDVKTWGDLGvtGDLANKPLQLFGRNSVSGTYGYFKEEAL- 196
Cdd:COG0226 80 IPVAIDGIAVVVNPDNPVKNLTGEQLADIFSG--------KITNWNDIG--GKLPDEPITVVGRSDGSGTTDYFTEYLLg 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666597 197 CKGDFKPNVNEQPGSASVVQSISSSLNGIGYSGIGY-KTASVKTVALAKKEgGEFIEDTEENALNGKYPLSRFLYVYVNK 275
Cdd:COG0226 150 VGAEVREGVEGAEGNEGVVQAVAQTPGAIGYVGLSYaEQNKLKALAIDNKA-GKFVEPTAENIAAGSYPLSRPLYIYVKK 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 523666597 276 APNkPLAPLEAEFVKLVLSKQGQEVVVKDGYIPLPAKVAAKALADL 321
Cdd:COG0226 229 EPD-AKAPAVKAFLDFVLSDGGQKIVEKLGYVPLPDAVVEKVRAAL 273
|
|
| PBP2_phosphate |
cd13566 |
Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 ... |
40-305 |
2.60e-88 |
|
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: 264.83 E-value: 2.60e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666597 40 SGNLSSVGSDTLANLMTLWAENYKKEYPNVNIQIQAAGSSTAPPALTEGTANLGPMSRKMKDNELQAFEtKYGYKPTAIP 119
Cdd:cd13566 1 SGTITIAGSSTVAPLAEALAEEFMKKHPGVRVTVQGGGSGAGIKALIAGTADIAMASRPLKDEEKAAAE-ANGIELVEFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666597 120 VAVDALAVFVHKDNPIKGLTMAQVDAIFSStrlcgaktDVKTWGDLGvtgdLANKPLQLFGRNSVSGTYGYFKEEALCKG 199
Cdd:cd13566 80 IAYDGIAVIVNPDNPVASLTLEQLRDIFTG--------KITNWSEVG----GPDEPIVVYGRDEGSGTRDYFEELVLGKG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666597 200 DFKPNVNEQPGSASVVQSISSSLNGIGYSGIGY--KTASVKTVALAKKEGgefiedTEENALNGKYPLSRFLYVYVNKAP 277
Cdd:cd13566 148 EFIRNAVVAPSNGALVQAVAGDPNAIGYVGLGYvdENKKVKALKVDGVAP------TVENIKSGKYPLSRPLFLYTKGEP 221
|
250 260
....*....|....*....|....*...
gi 523666597 278 NkplaPLEAEFVKLVLSKQGQEVVVKDG 305
Cdd:cd13566 222 S----PAVKAFIDFALSPEGQKIIEEVG 245
|
|
| PBP2_phosphate_like_1 |
cd13653 |
Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 ... |
40-305 |
6.61e-88 |
|
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: 263.66 E-value: 6.61e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666597 40 SGNLSSVGSDTLANLMTLWAENYKKEYPNVNIQIQAAGSSTAPPALTEGTANLGPMSRKMKDNELQAFetkygYKPTAIP 119
Cdd:cd13653 1 SGTITISGSTTVAPLAEALAEAFMEKHPGVRIEVQGGGSGTGIKALIEGTADIGMASRPLKAEEKAAA-----SGLVEHV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666597 120 VAVDALAVFVHKDNPIKGLTMAQVDAIFSStrlcgaktDVKTWGDLGvtgdLANKPLQLFGRNSVSGTYGYFKEEALCKG 199
Cdd:cd13653 76 IALDGIAIIVNPDNPVKNLTLEQLRDIFSG--------KITNWKEVG----GPDGPIVVISREEGSGTRETFEELVLGKK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666597 200 DFKPNVNEQPGSASVVQSISSSLNGIGYSGIGYKTAS-VKTVALAKKEGgefiedTEENALNGKYPLSRFLYVYVNKAPN 278
Cdd:cd13653 144 DFAKNAVVVPSNGAVVQAVAKNPNAIGYVSLGYVDDSkVKALSVDGVAP------TPENIKSGKYPLSRPLYLYTKGEPS 217
|
250 260
....*....|....*....|....*..
gi 523666597 279 kplaPLEAEFVKLVLSKQGQEVVVKDG 305
Cdd:cd13653 218 ----GLVKAFIDFALSPEGQAIVEKLG 240
|
|
| PBP2_phosphate_like_2 |
cd13654 |
Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 ... |
40-305 |
9.74e-40 |
|
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: 140.47 E-value: 9.74e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666597 40 SGNLSSVGSDTLANLMTLWAENYKKEYPNVNIQIQAAGSSTAPPALTEGTANLGPMSRKMKDNELQAFETKyGYKPTAIP 119
Cdd:cd13654 1 RGQIRIDGSSTVYPITEAVAEEFGKSGPGVTVTVGSSGTGGGFKKFCAGETDISNASRPIKDSEAELCEAN-GIEYIELP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666597 120 VAVDALAVFVHKDNP-IKGLTMAQVDAIFSstrlcgAKTDVKTWGDlgVTGDLANKPLQLFGRNSVSGTYGYFKEEALCK 198
Cdd:cd13654 80 VAYDGLTVVVNPANDwAKCLTELELKSIWA------AESPITTWSD--VRPSWPDEPIELYGPGTDSGTFDYFTEAIVGE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666597 199 G-----DFKPNVNEQpgsaSVVQSISSSLNGIGYSGIGY---KTASVKTVALAKKEGGEFIEdTEENALNGKYPLSRFLY 270
Cdd:cd13654 152 GgsireDYTASEDDN----VLVQGVAGDKNALGFFGYAYyeeNGDKLKAVKIDGGEGTVAPS-AETTISGGYYPLSRPLF 226
|
250 260 270
....*....|....*....|....*....|....*
gi 523666597 271 VYVNKApNKPLAPLEAEFVKLVLSkQGQEVVVKDG 305
Cdd:cd13654 227 IYVKKA-SLAEKPAVAAFVKFYLE-NAQEAAGEVG 259
|
|
| PBP_like_2 |
pfam12849 |
PBP superfamily domain; This domain belongs to the periplasmic binding protein superfamily. |
36-294 |
8.94e-36 |
|
PBP superfamily domain; This domain belongs to the periplasmic binding protein superfamily.
Pssm-ID: 432831 [Multi-domain] Cd Length: 267 Bit Score: 130.36 E-value: 8.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666597 36 TTGVSGNLSSVGSDTLANLMTLWAENYKKEYPNVNIQIQAAGSSTAPPALTEGTANLGPMSRKMKDNELQAFETKYGYKP 115
Cdd:pfam12849 5 SAPTVGTILIAGSSTQAPGLLDLAEAFEKKYPGAKVKVTSVGSGEGIKALLNGDVDVALVSRPLTEEEFEAFGANGAGGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666597 116 TAIPVAVDALAVFVHKDNPIKGLTMAQVDAIFSSTrlcgaktdVKTWGDLGvtgdlANKPLQLFGRNSVSGTYGYFKEEA 195
Cdd:pfam12849 85 VEVPVAYDGIAIVVNKDNPANILTVEALKKIFSGK--------ITNWNDGG-----PDGPIKFVSRGDNSGTTELFSTHL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666597 196 LCKGDFKpNVNEQPGSASVVQSISSSLNGIGYSGI-------GYKTASVKTV----------ALAKKEGGEFIEDTEENA 258
Cdd:pfam12849 152 KEKGPWG-AAGIGAAGSPGVASVVAGPGAIGYVEVsyalanlGYTLADVAGGtylsfakalkVAKINPGAGLVIPLEEAI 230
|
250 260 270
....*....|....*....|....*....|....*.
gi 523666597 259 LNGKYPLSRFLYVYVNKAPnKPLAPLEAEFVKLVLS 294
Cdd:pfam12849 231 ADGDYPLSRPYYVIVKNPP-KGPAPLAKAFLDFLLS 265
|
|
| PBP2_PstS |
cd13565 |
Substrate binding domain of ABC-type phosphate transporter, a member of the type 2 ... |
40-300 |
5.19e-14 |
|
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: 70.72 E-value: 5.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666597 40 SGNLSSVGSDTLANLMTLWAENYKKEYPNVNIQIQAAGSSTAPPALTEGTANLGPMSRKMKDNELQAFETKYGYkptaIP 119
Cdd:cd13565 1 AVTLTGAGATFPAPLYQKWIDEYKKAHPGVKINYQSIGSGAGIKQFIAGTVDFGASDAPLSDAELAKAGGGLLQ----IP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666597 120 VAVDALAVFVHKDNpIKG---LTMAQVDAIFSstrlcGAKTdvkTWGDL-------GVTgdLANKPLQLFGRNSVSGTYG 189
Cdd:cd13565 77 TVIGAVVVAYNLPG-VKGlllLSGEVLADIFL-----GKIT---KWNDPaiaalnpGVN--LPDTPITVVHRSDGSGTTF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666597 190 YFKEE-ALCKGDFKPNVNEQP-----------GSASVVQSISSSLNGIGYSGIGY-KTASVKTVALakkeggefiedtee 256
Cdd:cd13565 146 IFTDYlSAVSPEWKDKVGAGKsvawpvglggkGNEGVAAAVKQTPGSIGYVELSYaLQNGLPAAAL-------------- 211
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 523666597 257 nalngkYPLSRFLYVYVNK-APNKPLAPLEAEFVKLVLSKQGQEV 300
Cdd:cd13565 212 ------YPIVGFTYILVKKdYKDAEKAKAVKKFLKWALTEGQKFA 250
|
|
| PBP2_phosphate_binding |
cd01006 |
Substrate binding domain of ABC-type phosphate transporter, a member of the type 2 ... |
43-280 |
2.85e-11 |
|
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: 62.66 E-value: 2.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666597 43 LSSVGSDTLANLMTLWAENYKKEYPNVNIQIQAAGSSTAPPALTEGTANLGPMSRKMKDNELQAfETKYgykptAIPVAV 122
Cdd:cd01006 4 LTISGSTSVAPI*DVWAEKYNQQHPETYVAVQGVGSTAGISQLKAGTVDIGASDAYLSESEAAN-KGLH-----TFTLAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666597 123 DALAVFVHKDNPIKGLTMA--QVDAIFSSTrlcgaktdVKTWGDLGVTG-----DLANKPLQLFGRNSVSGTYGYF---- 191
Cdd:cd01006 78 DGLAIVVNQPGPVTNLTLNgkQLYGIYKGQ--------IKNWDDVGIAAlnpgvNLPDQKIAVVTREDGSGTRFSFtsyl 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666597 192 ---KEEALCKG-----DFKPN---VNEQPGSASVVQSISSSlngIGYSGIGY-KTASVKTVALakkeggefiedteenal 259
Cdd:cd01006 150 gktKTEKDGKGttevsDVAPTalgVNGNSG*KTLVNHNPGA---VGYISIGSvDQSSLKAIQL----------------- 209
|
250 260
....*....|....*....|.
gi 523666597 260 ngkYPLSRFLYVYVNKAPNKP 280
Cdd:cd01006 210 ---YPISRPFLILHYSDQKDA 227
|
|
| 3a0107s03 |
TIGR00975 |
phosphate ABC transporter, phosphate-binding protein; This family represents one type of ... |
43-319 |
1.52e-10 |
|
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: 61.31 E-value: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666597 43 LSSVGSDTLANLMTLWAENYKKEYPNVNIQIQAAGSSTAPPALTEGTANLGPMSRKMKDNELQafetKYGYKPTAIPVAV 122
Cdd:TIGR00975 1 LTGAGSTFPAPLYTKWFPDFQKSNPGVTINYQGIGSGAGIAQFAAGTVDFGASDAPLSEADLA----AAGSGLLNFPTVI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666597 123 DALAVFVHKDNPIKGLTM--AQVDAIFSSTrlcgaktdVKTWGD-------LGVTgdLANKPLQLFGRNSVSGTYGYFKE 193
Cdd:TIGR00975 77 GAIVVTYNLPGVSEKLKLdgPVLAKIFLGK--------IKQWNDpaiaalnPGVK--LPGTAITVVHRSDGSGTTFNFTN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666597 194 E-ALCKGDFKPNVNE--------------QPGSASVVQSISSSlngIGYSGIGYKTASVKTVALAKKEGGEFIEDTEENA 258
Cdd:TIGR00975 147 YlSKVSPEWGKKVGAgktvqwpagvggkgNDGVVAGVKQTPGA---IGYVEWSFAKQNKLSFAALKNSAGKFVLPDAESI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666597 259 LN-----------------------GKYPLSRFLYVYVNKAPNKPLAPLEA-EFVKLVLSKqGQEVVVKDGYIPLPAKVA 314
Cdd:TIGR00975 224 KAaaagakistpkndaismtdppgpGAYPIVSYTYLIVYKKQKDPAKAKALkAFLTWAITN-GQSFLDDLGYIPLPPSVV 302
|
....*
gi 523666597 315 AKALA 319
Cdd:TIGR00975 303 KRVRT 307
|
|
| SBP_bac_11 |
pfam13531 |
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
46-306 |
2.76e-04 |
|
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.
Pssm-ID: 463911 [Multi-domain] Cd Length: 225 Bit Score: 41.48 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666597 46 VGSDTLANLMTLWAENYKKEyPNVNIQIQAAGSSTAPPALTEG-------TANLGPMSrkmkdnelQAFETKYGYKPTAI 118
Cdd:pfam13531 3 AAAGGLAAALRELAAAFEAE-TGVKVVVSYGGSGKLAKQIANGapadvfiSADSAWLD--------KLAAAGLVVPGSRV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666597 119 PVAVDALAVFVHKDNPIKGLTMAQVdaifsstrlcgAKTDVKtwgdLGVTgdlankplqlfgrNSVSGTYGYFKEEALCK 198
Cdd:pfam13531 74 PLAYSPLVIAVPKGNPKDISGLADL-----------LKPGVR----LAVA-------------DPKTAPSGRAALELLEK 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666597 199 ----GDFKPN-VNEQPGSASVVQSISSSLNGIGysgIGYKTAsvkTVALAKKEGGEFIEDTEEnalngKYPLSRFLYVYV 273
Cdd:pfam13531 126 agllKALEKKvVVLGENVRQALTAVASGEADAG---IVYLSE---ALFPENGPGLEVVPLPED-----LNLPLDYPAAVL 194
|
250 260 270
....*....|....*....|....*....|...
gi 523666597 274 NKAPNKPLApleAEFVKLVLSKQGQEVVVKDGY 306
Cdd:pfam13531 195 KKAAHPEAA---RAFLDFLLSPEAQAILRKYGF 224
|
|
| ModA |
COG0725 |
ABC-type molybdate transport system, periplasmic Mo-binding protein ModA [Inorganic ion ... |
51-310 |
8.74e-04 |
|
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: 40.24 E-value: 8.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666597 51 LANLMTLWAENYKKEYPNVNIQIQAAGSSTAPPALTEG-------TANLGPMSRKMKDNELQAfetkygykPTAIPVAVD 123
Cdd:COG0725 35 LKEALEELAAAFEKEHPGVKVELSFGGSGALARQIEQGapadvfiSADEKYMDKLAKKGLILA--------GSRVVFATN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666597 124 ALAVFVHKDNP--IKGLT-MAQVDAIFSstrLCGAKTD------VKTWGDLGVTGDLANKplqLFGRNSVSGTYGYFKEe 194
Cdd:COG0725 107 RLVLAVPKGNPadISSLEdLAKPGVRIA---IGDPKTVpygkyaKEALEKAGLWDALKPK---LVLGENVRQVLAYVES- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666597 195 alckgdfkpnvneqpGSASVvqsissslnGIGYsgigyktasvKTVALAKKEGGEFIEDTEENALNGKYPLsrflyVYVN 274
Cdd:COG0725 180 ---------------GEADA---------GIVY----------LSDALAAKGVLVVVELPAELYAPIVYPA-----AVLK 220
|
250 260 270
....*....|....*....|....*....|....*.
gi 523666597 275 KAPNKPLApleAEFVKLVLSKQGQEVVVKDGYIPLP 310
Cdd:COG0725 221 GAKNPEAA---KAFLDFLLSPEAQAILEKYGFEPPK 253
|
|
| PBP2_ModA_like_1 |
cd13538 |
Substrate binding domain of putative molybdate-binding protein;the type 2 periplasmic binding ... |
50-307 |
1.32e-03 |
|
Substrate binding domain of putative molybdate-binding protein;the type 2 periplasmic binding protein fold; This subfamily contains domains found in ModA proteins of putative ABC-type transporter. Molybdate transport system is comprised of a periplasmic binding protein, an integral membrane protein, and an energizer protein. These three proteins are coded by modA, modB, and modC genes, respectively. ModA proteins serve as initial receptors in the ABC transport of molybdate mostly in eubacteria and archaea. After binding molybdate with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ModA proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.
Pssm-ID: 270256 [Multi-domain] Cd Length: 230 Bit Score: 39.59 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666597 50 TLANLMTLWAENYKKEYPNVNIQIQAAGSSTAPPALTEG----------TANLGPMSRKMKDNElqafetkygyKPTAIp 119
Cdd:cd13538 9 SLTDAFTEIGEQFEKSNPGVKVTFNFAGSQALVTQIEQGapadvfasadTANMDALVKAGLLVD----------TPTIF- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666597 120 vAVDALAVFVHKDNPIKGLTMAqvDAIFSSTRLCGAKTDVKtwgdlgvTGDLAnkpLQLFGRNSVSGTYGYFkeealcKG 199
Cdd:cd13538 78 -ATNKLVVIVPKDNPAKITSLA--DLAKPGVKIVIGAPEVP-------VGTYT---RRVLDKAGNDYAYGYK------EA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523666597 200 DFKPNVNEQPGSASVVQSISSslnGIGYSGIGYKTaSVKTVALAKKeggeFIEDTEENALNGKYPlsrflYVYVNKAPNK 279
Cdd:cd13538 139 VLANVVSEETNVRDVVTKVAL---GEADAGFVYVT-DAKAASEKLK----VITIPEEYNVTATYP-----IAVLKASKNP 205
|
250 260
....*....|....*....|....*...
gi 523666597 280 PLApleAEFVKLVLSKQGQEVVVKDGYI 307
Cdd:cd13538 206 ELA---RAFVDFLLSEEGQAILAEYGFG 230
|
|
| |
