|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10918 |
PRK10918 |
phosphate ABC transporter substrate-binding protein PstS; |
1-357 |
0e+00 |
|
phosphate ABC transporter substrate-binding protein PstS;
Pssm-ID: 182837 Cd Length: 346 Bit Score: 681.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511334160 1 MKPMRslvvtkkmvtnKTVAAIVAATCSLTTMSAFAATSLTGAGATFPAPVYAKWADTYQKETGNKVNYQGIGSSGGVKQ 80
Cdd:PRK10918 1 MKVMR-----------TTVATVVAATLSMSAFSAFAAASLTGAGATFPAPVYAKWADTYQKETGNKVNYQGIGSSGGVKQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511334160 81 IIAKTVDFGASDAPLTDDKLAADGLFQFPTVIGGVVLAVNIPGLKSGELTLDGKTLGDIYLGNIKKWNDPAITKLNPGLK 160
Cdd:PRK10918 70 IIANTVDFGASDAPLSDEKLAQEGLFQFPTVIGGVVLAVNIPGLKSGELVLDGKTLGDIYLGKIKKWNDEAIAKLNPGVK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511334160 161 LPDTNIAVVRRADGSGTSYVFTNYLAKVNPDWKSKVGAGSTVNWPTGLGGKGNDGVAAFIQRLPGSIGYVEYAYVKQSKL 240
Cdd:PRK10918 150 LPSQNIAVVRRADGSGTSFVFTSYLAKVNEEWKSKVGAGSTVNWPTGLGGKGNDGIAAFVQRLPGAIGYVEYAYAKQNNL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511334160 241 AYTKLISADGDAVLPTEESFSNAAKGADWSKSFAQDLTNQKGANAWPISSTTFILVHKEQQKPEQGEAVLKFFDWAYKNG 320
Cdd:PRK10918 230 AYTKLISADGKPVSPTEESFSNAAKGADWSKSFAQDLTNQKGDDAWPITSTTFILVHKDQKKPEQGAEVLKFFDWAYKNG 309
|
330 340 350
....*....|....*....|....*....|....*..
gi 511334160 321 GKEASALDYAPLPSSVVEQIRAAWKTNVKDSSGKALY 357
Cdd:PRK10918 310 AKQANDLDYASLPDSVVEQVRAAWKTNIKDSSGKPLY 346
|
|
| 3a0107s03 |
TIGR00975 |
phosphate ABC transporter, phosphate-binding protein; This family represents one type of ... |
40-346 |
2.38e-143 |
|
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: 408.37 E-value: 2.38e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511334160 40 LTGAGATFPAPVYAKWADTYQKET-GNKVNYQGIGSSGGVKQIIAKTVDFGASDAPLTDDKLAA--DGLFQFPTVIGGVV 116
Cdd:TIGR00975 1 LTGAGSTFPAPLYTKWFPDFQKSNpGVTINYQGIGSGAGIAQFAAGTVDFGASDAPLSEADLAAagSGLLNFPTVIGAIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511334160 117 LAVNIPGLKSgELTLDGKTLGDIYLGNIKKWNDPAITKLNPGLKLPDTNIAVVRRADGSGTSYVFTNYLAKVNPDWKSKV 196
Cdd:TIGR00975 81 VTYNLPGVSE-KLKLDGPVLAKIFLGKIKQWNDPAIAALNPGVKLPGTAITVVHRSDGSGTTFNFTNYLSKVSPEWGKKV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511334160 197 GAGSTVNWPTGLGGKGNDGVAAFIQRLPGSIGYVEYAYVKQSKLAYTKLISADGDAVLPTEESFSNAAKGADWS--KSFA 274
Cdd:TIGR00975 160 GAGKTVQWPAGVGGKGNDGVVAGVKQTPGAIGYVEWSFAKQNKLSFAALKNSAGKFVLPDAESIKAAAAGAKIStpKNDA 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 511334160 275 QDLTNQKGANAWPISSTTFILVHKEQQKPEQGEAVLKFFDWAYKNGGKEASALDYAPLPSSVVEQIRAAWKT 346
Cdd:TIGR00975 240 ISMTDPPGPGAYPIVSYTYLIVYKKQKDPAKAKALKAFLTWAITNGQSFLDDLGYIPLPPSVVKRVRTAVNT 311
|
|
| PBP2_PstS |
cd13565 |
Substrate binding domain of ABC-type phosphate transporter, a member of the type 2 ... |
37-328 |
4.65e-121 |
|
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: 349.61 E-value: 4.65e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511334160 37 ATSLTGAGATFPAPVYAKWADTYQKET-GNKVNYQGIGSSGGVKQIIAKTVDFGASDAPLTDDKLAA--DGLFQFPTVIG 113
Cdd:cd13565 1 AVTLTGAGATFPAPLYQKWIDEYKKAHpGVKINYQSIGSGAGIKQFIAGTVDFGASDAPLSDAELAKagGGLLQIPTVIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511334160 114 GVVLAVNIPGLKSGELtLDGKTLGDIYLGNIKKWNDPAITKLNPGLKLPDTNIAVVRRADGSGTSYVFTNYLAKVNPDWK 193
Cdd:cd13565 81 AVVVAYNLPGVKGLLL-LSGEVLADIFLGKITKWNDPAIAALNPGVNLPDTPITVVHRSDGSGTTFIFTDYLSAVSPEWK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511334160 194 SKVGAGSTVNWPTGLGGKGNDGVAAFIQRLPGSIGYVEYAYVKQSKLAYTKLisadgdavlpteesfsnaakgadwsksf 273
Cdd:cd13565 160 DKVGAGKSVAWPVGLGGKGNEGVAAAVKQTPGSIGYVELSYALQNGLPAAAL---------------------------- 211
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 511334160 274 aqdltnqkganaWPISSTTFILVHKEQQKPEQGEAVLKFFDWAYKNGGKEASALD 328
Cdd:cd13565 212 ------------YPIVGFTYILVKKDYKDAEKAKAVKKFLKWALTEGQKFAADLG 254
|
|
| PstS |
COG0226 |
ABC-type phosphate transport system, periplasmic component [Inorganic ion transport and ... |
36-345 |
1.06e-88 |
|
ABC-type phosphate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 439996 [Multi-domain] Cd Length: 275 Bit Score: 267.90 E-value: 1.06e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511334160 36 AATSLTGAGATFPAPVYAKWADTYQKE-TGNKVNYQGIGSSGGVKQIIAKTVDFGASDAPLTDDKLAA-----DGLFQFP 109
Cdd:COG0226 2 ASGTITIAGSSTVYPLAEAWAEAFQKAnPGVTINVQSGGSGGGIKQFIAGTVDIGNSSRPLKDEELEAakengVELVEIP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511334160 110 TVIGGVVLAVNipglKSGELT-LDGKTLGDIYLGNIKKWNDpaitkLNPglKLPDTNIAVVRRADGSGTSYVFTNYLAKV 188
Cdd:COG0226 82 VAIDGIAVVVN----PDNPVKnLTGEQLADIFSGKITNWND-----IGG--KLPDEPITVVGRSDGSGTTDYFTEYLLGV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511334160 189 NPDWkskvgagstvnWPTGLGGKGNDGVAAFIQRLPGSIGYVEYAYVKQSKLAYTKLISADGDAVLPTEESFSnaakgad 268
Cdd:COG0226 151 GAEV-----------REGVEGAEGNEGVVQAVAQTPGAIGYVGLSYAEQNKLKALAIDNKAGKFVEPTAENIA------- 212
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 511334160 269 wsksfaqdltnqkgANAWPISSTTFILVHKEqqKPEQGEAVLKFFDWAYKNGGKE-ASALDYAPLPSSVVEQIRAAWK 345
Cdd:COG0226 213 --------------AGSYPLSRPLYIYVKKE--PDAKAPAVKAFLDFVLSDGGQKiVEKLGYVPLPDAVVEKVRAALK 274
|
|
| PBP_like_2 |
pfam12849 |
PBP superfamily domain; This domain belongs to the periplasmic binding protein superfamily. |
33-317 |
5.82e-39 |
|
PBP superfamily domain; This domain belongs to the periplasmic binding protein superfamily.
Pssm-ID: 432831 [Multi-domain] Cd Length: 267 Bit Score: 139.60 E-value: 5.82e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511334160 33 SAFAATSLTGAGATFPAPVYAKWADTYQKE-TGNKVNYQGIGSSGGVKQIIAKTVDFGASDAPLTDDKLAAD------GL 105
Cdd:pfam12849 5 SAPTVGTILIAGSSTQAPGLLDLAEAFEKKyPGAKVKVTSVGSGEGIKALLNGDVDVALVSRPLTEEEFEAFgangagGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511334160 106 FQFPTVIGGVVLAVNIPGlksGELTLDGKTLGDIYLGNIKKWNDPaitklnpglkLPDTNIAVVRRADGSGTSYVFTNYL 185
Cdd:pfam12849 85 VEVPVAYDGIAIVVNKDN---PANILTVEALKKIFSGKITNWNDG----------GPDGPIKFVSRGDNSGTTELFSTHL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511334160 186 AKVNPdWKSkvgagstvnwpTGLGGKGNDGVAAfIQRLPGSIGYVEYAYVKQSKLAytKLISADGDAVLPTEEsfsnAAK 265
Cdd:pfam12849 152 KEKGP-WGA-----------AGIGAAGSPGVAS-VVAGPGAIGYVEVSYALANLGY--TLADVAGGTYLSFAK----ALK 212
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 511334160 266 GADWSKSFAQDLTNQKG--ANAWPISSTTFILVHKEQQKPEqgEAVLKFFDWAY 317
Cdd:pfam12849 213 VAKINPGAGLVIPLEEAiaDGDYPLSRPYYVIVKNPPKGPA--PLAKAFLDFLL 264
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10918 |
PRK10918 |
phosphate ABC transporter substrate-binding protein PstS; |
1-357 |
0e+00 |
|
phosphate ABC transporter substrate-binding protein PstS;
Pssm-ID: 182837 Cd Length: 346 Bit Score: 681.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511334160 1 MKPMRslvvtkkmvtnKTVAAIVAATCSLTTMSAFAATSLTGAGATFPAPVYAKWADTYQKETGNKVNYQGIGSSGGVKQ 80
Cdd:PRK10918 1 MKVMR-----------TTVATVVAATLSMSAFSAFAAASLTGAGATFPAPVYAKWADTYQKETGNKVNYQGIGSSGGVKQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511334160 81 IIAKTVDFGASDAPLTDDKLAADGLFQFPTVIGGVVLAVNIPGLKSGELTLDGKTLGDIYLGNIKKWNDPAITKLNPGLK 160
Cdd:PRK10918 70 IIANTVDFGASDAPLSDEKLAQEGLFQFPTVIGGVVLAVNIPGLKSGELVLDGKTLGDIYLGKIKKWNDEAIAKLNPGVK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511334160 161 LPDTNIAVVRRADGSGTSYVFTNYLAKVNPDWKSKVGAGSTVNWPTGLGGKGNDGVAAFIQRLPGSIGYVEYAYVKQSKL 240
Cdd:PRK10918 150 LPSQNIAVVRRADGSGTSFVFTSYLAKVNEEWKSKVGAGSTVNWPTGLGGKGNDGIAAFVQRLPGAIGYVEYAYAKQNNL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511334160 241 AYTKLISADGDAVLPTEESFSNAAKGADWSKSFAQDLTNQKGANAWPISSTTFILVHKEQQKPEQGEAVLKFFDWAYKNG 320
Cdd:PRK10918 230 AYTKLISADGKPVSPTEESFSNAAKGADWSKSFAQDLTNQKGDDAWPITSTTFILVHKDQKKPEQGAEVLKFFDWAYKNG 309
|
330 340 350
....*....|....*....|....*....|....*..
gi 511334160 321 GKEASALDYAPLPSSVVEQIRAAWKTNVKDSSGKALY 357
Cdd:PRK10918 310 AKQANDLDYASLPDSVVEQVRAAWKTNIKDSSGKPLY 346
|
|
| 3a0107s03 |
TIGR00975 |
phosphate ABC transporter, phosphate-binding protein; This family represents one type of ... |
40-346 |
2.38e-143 |
|
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: 408.37 E-value: 2.38e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511334160 40 LTGAGATFPAPVYAKWADTYQKET-GNKVNYQGIGSSGGVKQIIAKTVDFGASDAPLTDDKLAA--DGLFQFPTVIGGVV 116
Cdd:TIGR00975 1 LTGAGSTFPAPLYTKWFPDFQKSNpGVTINYQGIGSGAGIAQFAAGTVDFGASDAPLSEADLAAagSGLLNFPTVIGAIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511334160 117 LAVNIPGLKSgELTLDGKTLGDIYLGNIKKWNDPAITKLNPGLKLPDTNIAVVRRADGSGTSYVFTNYLAKVNPDWKSKV 196
Cdd:TIGR00975 81 VTYNLPGVSE-KLKLDGPVLAKIFLGKIKQWNDPAIAALNPGVKLPGTAITVVHRSDGSGTTFNFTNYLSKVSPEWGKKV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511334160 197 GAGSTVNWPTGLGGKGNDGVAAFIQRLPGSIGYVEYAYVKQSKLAYTKLISADGDAVLPTEESFSNAAKGADWS--KSFA 274
Cdd:TIGR00975 160 GAGKTVQWPAGVGGKGNDGVVAGVKQTPGAIGYVEWSFAKQNKLSFAALKNSAGKFVLPDAESIKAAAAGAKIStpKNDA 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 511334160 275 QDLTNQKGANAWPISSTTFILVHKEQQKPEQGEAVLKFFDWAYKNGGKEASALDYAPLPSSVVEQIRAAWKT 346
Cdd:TIGR00975 240 ISMTDPPGPGAYPIVSYTYLIVYKKQKDPAKAKALKAFLTWAITNGQSFLDDLGYIPLPPSVVKRVRTAVNT 311
|
|
| PBP2_PstS |
cd13565 |
Substrate binding domain of ABC-type phosphate transporter, a member of the type 2 ... |
37-328 |
4.65e-121 |
|
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: 349.61 E-value: 4.65e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511334160 37 ATSLTGAGATFPAPVYAKWADTYQKET-GNKVNYQGIGSSGGVKQIIAKTVDFGASDAPLTDDKLAA--DGLFQFPTVIG 113
Cdd:cd13565 1 AVTLTGAGATFPAPLYQKWIDEYKKAHpGVKINYQSIGSGAGIKQFIAGTVDFGASDAPLSDAELAKagGGLLQIPTVIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511334160 114 GVVLAVNIPGLKSGELtLDGKTLGDIYLGNIKKWNDPAITKLNPGLKLPDTNIAVVRRADGSGTSYVFTNYLAKVNPDWK 193
Cdd:cd13565 81 AVVVAYNLPGVKGLLL-LSGEVLADIFLGKITKWNDPAIAALNPGVNLPDTPITVVHRSDGSGTTFIFTDYLSAVSPEWK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511334160 194 SKVGAGSTVNWPTGLGGKGNDGVAAFIQRLPGSIGYVEYAYVKQSKLAYTKLisadgdavlpteesfsnaakgadwsksf 273
Cdd:cd13565 160 DKVGAGKSVAWPVGLGGKGNEGVAAAVKQTPGSIGYVELSYALQNGLPAAAL---------------------------- 211
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 511334160 274 aqdltnqkganaWPISSTTFILVHKEQQKPEQGEAVLKFFDWAYKNGGKEASALD 328
Cdd:cd13565 212 ------------YPIVGFTYILVKKDYKDAEKAKAVKKFLKWALTEGQKFAADLG 254
|
|
| PBP2_phosphate_binding |
cd01006 |
Substrate binding domain of ABC-type phosphate transporter, a member of the type 2 ... |
37-322 |
4.27e-110 |
|
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: 321.52 E-value: 4.27e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511334160 37 ATSLTGAGATFPAPVYAKWADTYQKET-GNKVNYQGIGSSGGVKQIIAKTVDFGASDAPLTDDKLAADGLFQFPTVIGGV 115
Cdd:cd01006 1 ASELTISGSTSVAPI*DVWAEKYNQQHpETYVAVQGVGSTAGISQLKAGTVDIGASDAYLSESEAANKGLHTFTLAIDGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511334160 116 VLAVNIPGLKSGeLTLDGKTLGDIYLGNIKKWNDPAITKLNPGLKLPDTNIAVVRRADGSGTSYVFTNYLAKVNPDWKSK 195
Cdd:cd01006 81 AIVVNQPGPVTN-LTLNGKQLYGIYKGQIKNWDDVGIAALNPGVNLPDQKIAVVTREDGSGTRFSFTSYLGKTKTEKDGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511334160 196 VGAGSTVNWPTGLGGKGNDGVAAFIQRLPGSIGYVEYAYVKQSKLAYTKLisadgdavlpteesfsnaakgadwsksfaq 275
Cdd:cd01006 160 GTTEVSDVAPTALGVNGNSG*KTLVNHNPGAVGYISIGSVDQSSLKAIQL------------------------------ 209
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 511334160 276 dltnqkganaWPISSTTFILVHKEQQKPEQGEAVLKFFDWAYKNGGK 322
Cdd:cd01006 210 ----------YPISRPFLILHYSDQKDAATDEQTKEFIAWAKSEGAA 246
|
|
| PstS |
COG0226 |
ABC-type phosphate transport system, periplasmic component [Inorganic ion transport and ... |
36-345 |
1.06e-88 |
|
ABC-type phosphate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 439996 [Multi-domain] Cd Length: 275 Bit Score: 267.90 E-value: 1.06e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511334160 36 AATSLTGAGATFPAPVYAKWADTYQKE-TGNKVNYQGIGSSGGVKQIIAKTVDFGASDAPLTDDKLAA-----DGLFQFP 109
Cdd:COG0226 2 ASGTITIAGSSTVYPLAEAWAEAFQKAnPGVTINVQSGGSGGGIKQFIAGTVDIGNSSRPLKDEELEAakengVELVEIP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511334160 110 TVIGGVVLAVNipglKSGELT-LDGKTLGDIYLGNIKKWNDpaitkLNPglKLPDTNIAVVRRADGSGTSYVFTNYLAKV 188
Cdd:COG0226 82 VAIDGIAVVVN----PDNPVKnLTGEQLADIFSGKITNWND-----IGG--KLPDEPITVVGRSDGSGTTDYFTEYLLGV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511334160 189 NPDWkskvgagstvnWPTGLGGKGNDGVAAFIQRLPGSIGYVEYAYVKQSKLAYTKLISADGDAVLPTEESFSnaakgad 268
Cdd:COG0226 151 GAEV-----------REGVEGAEGNEGVVQAVAQTPGAIGYVGLSYAEQNKLKALAIDNKAGKFVEPTAENIA------- 212
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 511334160 269 wsksfaqdltnqkgANAWPISSTTFILVHKEqqKPEQGEAVLKFFDWAYKNGGKE-ASALDYAPLPSSVVEQIRAAWK 345
Cdd:COG0226 213 --------------AGSYPLSRPLYIYVKKE--PDAKAPAVKAFLDFVLSDGGQKiVEKLGYVPLPDAVVEKVRAALK 274
|
|
| PBP_like_2 |
pfam12849 |
PBP superfamily domain; This domain belongs to the periplasmic binding protein superfamily. |
33-317 |
5.82e-39 |
|
PBP superfamily domain; This domain belongs to the periplasmic binding protein superfamily.
Pssm-ID: 432831 [Multi-domain] Cd Length: 267 Bit Score: 139.60 E-value: 5.82e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511334160 33 SAFAATSLTGAGATFPAPVYAKWADTYQKE-TGNKVNYQGIGSSGGVKQIIAKTVDFGASDAPLTDDKLAAD------GL 105
Cdd:pfam12849 5 SAPTVGTILIAGSSTQAPGLLDLAEAFEKKyPGAKVKVTSVGSGEGIKALLNGDVDVALVSRPLTEEEFEAFgangagGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511334160 106 FQFPTVIGGVVLAVNIPGlksGELTLDGKTLGDIYLGNIKKWNDPaitklnpglkLPDTNIAVVRRADGSGTSYVFTNYL 185
Cdd:pfam12849 85 VEVPVAYDGIAIVVNKDN---PANILTVEALKKIFSGKITNWNDG----------GPDGPIKFVSRGDNSGTTELFSTHL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511334160 186 AKVNPdWKSkvgagstvnwpTGLGGKGNDGVAAfIQRLPGSIGYVEYAYVKQSKLAytKLISADGDAVLPTEEsfsnAAK 265
Cdd:pfam12849 152 KEKGP-WGA-----------AGIGAAGSPGVAS-VVAGPGAIGYVEVSYALANLGY--TLADVAGGTYLSFAK----ALK 212
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 511334160 266 GADWSKSFAQDLTNQKG--ANAWPISSTTFILVHKEQQKPEqgEAVLKFFDWAY 317
Cdd:pfam12849 213 VAKINPGAGLVIPLEEAiaDGDYPLSRPYYVIVKNPPKGPA--PLAKAFLDFLL 264
|
|
| PBP2_phosphate_like_1 |
cd13653 |
Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 ... |
37-323 |
4.86e-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: 270371 [Multi-domain] Cd Length: 240 Bit Score: 114.97 E-value: 4.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511334160 37 ATSLTGAGATFPAPVYAKWADTYQKETGN-KVNYQGIGSSGGVKQIIAKTVDFGASDAPLTDDKLAADGLFQfPTVIG-- 113
Cdd:cd13653 1 SGTITISGSTTVAPLAEALAEAFMEKHPGvRIEVQGGGSGTGIKALIEGTADIGMASRPLKAEEKAAASGLV-EHVIAld 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511334160 114 GVVLAVNiPGLKSGELTLDgkTLGDIYLGNIKKWNDpaitklnpgLKLPDTNIAVVRRADGSGTSYVFTNYLAKvnpdwK 193
Cdd:cd13653 80 GIAIIVN-PDNPVKNLTLE--QLRDIFSGKITNWKE---------VGGPDGPIVVISREEGSGTRETFEELVLG-----K 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511334160 194 SKVGAGSTVnwptglgGKGNDGVAAFIQRLPGSIGYVEYAYVKQSKLaytKLISADGdaVLPTEEsfsNAAKGadwsksf 273
Cdd:cd13653 143 KDFAKNAVV-------VPSNGAVVQAVAKNPNAIGYVSLGYVDDSKV---KALSVDG--VAPTPE---NIKSG------- 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 511334160 274 aqdltnqkganAWPISSTTFILVHKeqqkpEQGEAVLKFFDWAYKNGGKE 323
Cdd:cd13653 201 -----------KYPLSRPLYLYTKG-----EPSGLVKAFIDFALSPEGQA 234
|
|
| ptsS_2 |
TIGR02136 |
phosphate binding protein; Members of this family are phosphate-binding proteins. Most are ... |
1-332 |
2.61e-27 |
|
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: 108.68 E-value: 2.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511334160 1 MKpmRSLVVTKKMVTNKTVAAIVAATCSLTTMSAFAATSLTGAGATFPAPVYAKWADTYQKETGN-KVNYQGIGSSGGVK 79
Cdd:TIGR02136 1 MK--KRIFLLIGLAAALLAAAGCGGAIDSGIPDAKGSSTITIDGSTTVAPLAEAAAEEFQKIHPGvSVTVQGAGSGTGIK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511334160 80 QIIAKTVDFGASDAPLTDDKLAADG-----LFQFPTVIGGVVLAVNIPGLKSGELTLDgkTLGDIYLGNIKKWNDpaitk 154
Cdd:TIGR02136 79 ALINGTVDIGNSSRPIKDEELQKDKqkgikLIEHKVAVDGLAVVVNKKNVPVDDLTVE--QLKKIYSGEITNWKE----- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511334160 155 LNPglKLPDTNIAVVRRADGSGTSYVFTNylaKVNPDWKSKVGAGSTvnwptglggKGNDGVAAFIQRLPGSIGYVEYAY 234
Cdd:TIGR02136 152 VGG--DLPNKPIVVVGRNAGSGTRDTFEE---EVMGKAKIKPGKNEQ---------ESNGAVVSIVSSNPGAIGYLGLGY 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511334160 235 VKQSKlaytKLISADGdaVLPTEESFSNaakgadwsksfaqdltnqkgaNAWPISSTTFILVHKEQQKPEQGEAVLKFFd 314
Cdd:TIGR02136 218 VDDSV----KTLKVNG--VEPSKENIAN---------------------GSYPLSRPLFMYVNGKPKKPELVAEFIDFV- 269
|
330
....*....|....*...
gi 511334160 315 WAYKNGGKEASALDYAPL 332
Cdd:TIGR02136 270 LSDDGGERIVEELGYVPL 287
|
|
| PBP2_phosphate |
cd13566 |
Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 ... |
37-324 |
2.32e-25 |
|
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: 102.66 E-value: 2.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511334160 37 ATSLTGAGATFPAPVYAKWADTYQKETGN-KVNYQGIGSSGGVKQIIAKTVDFGASDAPLTDDKLAA-----DGLFQFPT 110
Cdd:cd13566 1 SGTITIAGSSTVAPLAEALAEEFMKKHPGvRVTVQGGGSGAGIKALIAGTADIAMASRPLKDEEKAAaeangIELVEFVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511334160 111 VIGGVVLAVNiPGLKSGELTLDgkTLGDIYLGNIKKWNDpaitklnpgLKLPDTNIAVVRRADGSGTSYVFTNYLAKvnp 190
Cdd:cd13566 81 AYDGIAVIVN-PDNPVASLTLE--QLRDIFTGKITNWSE---------VGGPDEPIVVYGRDEGSGTRDYFEELVLG--- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511334160 191 dwKSKVGAGSTVnwptglgGKGNDGVAAFIQRLPGSIGYVEYAYVKQSKLAytKLISADGdaVLPTEEsfsNAAKGadws 270
Cdd:cd13566 146 --KGEFIRNAVV-------APSNGALVQAVAGDPNAIGYVGLGYVDENKKV--KALKVDG--VAPTVE---NIKSG---- 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 511334160 271 ksfaqdltnqkganAWPISSTTFILVHKeqqkpEQGEAVLKFFDWAYKNGGKEA 324
Cdd:cd13566 206 --------------KYPLSRPLFLYTKG-----EPSPAVKAFIDFALSPEGQKI 240
|
|
| SBP_bac_1 |
pfam01547 |
Bacterial extracellular solute-binding protein; This family also includes the bacterial ... |
54-323 |
1.07e-06 |
|
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: 49.72 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511334160 54 KWADTYQKE-TGNKVNYQGIGSSGGVKQIiakTVDFGASDAP-----LTDDKLAADGLFQFPTVIGGVVLAVNIPGL-KS 126
Cdd:pfam01547 12 ALVKEFEKEhPGIKVEVESVGSGSLAQKL---TTAIAAGDGPadvfaSDNDWIAELAKAGLLLPLDDYVANYLVLGVpKL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511334160 127 GELTLDGKTLGDIY---------LGNIKKWNDPAITKLNPGLKLPdtNIAVVRRADGSGTSYVFTNYLAKVNPDWKSKVG 197
Cdd:pfam01547 89 YGVPLAAETLGLIYnkdlfkkagLDPPKTWDELLEAAKKLKEKGK--SPGGAGGGDASGTLGYFTLALLASLGGPLFDKD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511334160 198 AGSTVNWPTGLGGKGNDGVAAFIQRLPGSIGYVeyAYVKQSKLAYTKLISADGDAVLPTEESFsNAAKGADWSKSFAQDL 277
Cdd:pfam01547 167 GGGLDNPEAVDAITYYVDLYAKVLLLKKLKNPG--VAGADGREALALFEQGKAAMGIVGPWAA-LAANKVKLKVAFAAPA 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 511334160 278 TNQKGANAWPI---------SSTTFILVHKEQQKpeqgEAVLKFFDWAYKNGGKE 323
Cdd:pfam01547 244 PDPKGDVGYAPlpagkggkgGGYGLAIPKGSKNK----EAAKKFLDFLTSPEAQA 294
|
|
| PBP2_phosphate_like_2 |
cd13654 |
Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 ... |
49-258 |
1.26e-04 |
|
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: 43.01 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511334160 49 APVYAKWADTYQKETGN-KVNYQGIGSSGGVKQIIAKTVDFGASDAPLTDD--KLAADG---LFQFPTVIGGVVLAVNiP 122
Cdd:cd13654 13 YPITEAVAEEFGKSGPGvTVTVGSSGTGGGFKKFCAGETDISNASRPIKDSeaELCEANgieYIELPVAYDGLTVVVN-P 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511334160 123 GLKS-GELTLDGKTLGDIYLGNIKKWNDpaitkLNPGLklPDTNIAVVRRADGSGTSYVFTnylAKVNPDWKSKVGAGSt 201
Cdd:cd13654 92 ANDWaKCLTELELKSIWAAESPITTWSD-----VRPSW--PDEPIELYGPGTDSGTFDYFT---EAIVGEGGSIREDYT- 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 511334160 202 vnwptglgGKGNDGV-AAFIQRLPGSIGYVEYAYVKQ--SKLaytKLISADGDAVLPTEE 258
Cdd:cd13654 161 --------ASEDDNVlVQGVAGDKNALGFFGYAYYEEngDKL---KAVKIDGGEGTVAPS 209
|
|
| Periplasmic_Binding_Protein_Type_2 |
cd00648 |
Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent ... |
40-143 |
1.55e-04 |
|
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: 42.18 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511334160 40 LTGAGATFP--APVYAKWADTYQKETGNKVNYQGIGSSGGV-KQIIAKTVDFGASDAPLTD----DKLAADGLFQFPTV- 111
Cdd:cd00648 2 LTVASIGPPpyAGFAEDAAKQLAKETGIKVELVPGSSIGTLiEALAAGDADVAVGPIAPALeaaaDKLAPGGLYIVPELy 81
|
90 100 110
....*....|....*....|....*....|....*
gi 511334160 112 IGGVVLAVNIPGLKSGE---LTLDGKTLGDIYLGN 143
Cdd:cd00648 82 VGGYVLVVRKGSSIKGLlavADLDGKRVGVGDPGS 116
|
|
| |
