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Conserved domains on  [gi|550796614|ref|WP_022652104|]
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MULTISPECIES: phosphate ABC transporter substrate-binding protein PstS [Enterobacter]

Protein Classification

phosphate ABC transporter substrate-binding protein PstS( domain architecture ID 10793503)

phosphate ABC transporter substrate-binding protein PstS is part of the ABC transporter complex PstSACB involved in phosphate import and it functions as the initial receptor for phosphate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10918 PRK10918
phosphate ABC transporter substrate-binding protein PstS;
1-346 0e+00

phosphate ABC transporter substrate-binding protein PstS;


:

Pssm-ID: 182837  Cd Length: 346  Bit Score: 688.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550796614   1 MKVMRTTVATVVAATLSMSAFSAFAAASLTGAGATFPAPVYAKWADTYQKETGNKVNYQGIGSSGGVKQITANTVDFGAS 80
Cdd:PRK10918   1 MKVMRTTVATVVAATLSMSAFSAFAAASLTGAGATFPAPVYAKWADTYQKETGNKVNYQGIGSSGGVKQIIANTVDFGAS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550796614  81 DAPLSDEKLNQEGLFQFPTVIGGVVLAVNIPGLKSGELVLDGKTLGDIYLGKIKKWDDEAITKLNPGVKLPSQNIAVVRR 160
Cdd:PRK10918  81 DAPLSDEKLAQEGLFQFPTVIGGVVLAVNIPGLKSGELVLDGKTLGDIYLGKIKKWNDEAIAKLNPGVKLPSQNIAVVRR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550796614 161 ADGSGTSFVFTSYLAKVNEEWKSKVGSGSTVNWPTGLGGKGNDGIAAFVQRLPGSIGYVEYAYAKQNNLAYTKLVSADGK 240
Cdd:PRK10918 161 ADGSGTSFVFTSYLAKVNEEWKSKVGAGSTVNWPTGLGGKGNDGIAAFVQRLPGAIGYVEYAYAKQNNLAYTKLISADGK 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550796614 241 PVSPTEENFANAAKGADWSKSFAQDLTNQKGEDAWPITSTTFILVHKEQKKPEQGAEVLKFFDWAYKNGGKQANDLDYAS 320
Cdd:PRK10918 241 PVSPTEESFSNAAKGADWSKSFAQDLTNQKGDDAWPITSTTFILVHKDQKKPEQGAEVLKFFDWAYKNGAKQANDLDYAS 320

                        330       340
                 ....*....|....*....|....*.
gi 550796614 321 LPDSVVEQIRAAWKTNVKDSSGKALY 346
Cdd:PRK10918 321 LPDSVVEQVRAAWKTNIKDSSGKPLY 346
 
Name Accession Description Interval E-value
PRK10918 PRK10918
phosphate ABC transporter substrate-binding protein PstS;
1-346 0e+00

phosphate ABC transporter substrate-binding protein PstS;


Pssm-ID: 182837  Cd Length: 346  Bit Score: 688.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550796614   1 MKVMRTTVATVVAATLSMSAFSAFAAASLTGAGATFPAPVYAKWADTYQKETGNKVNYQGIGSSGGVKQITANTVDFGAS 80
Cdd:PRK10918   1 MKVMRTTVATVVAATLSMSAFSAFAAASLTGAGATFPAPVYAKWADTYQKETGNKVNYQGIGSSGGVKQIIANTVDFGAS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550796614  81 DAPLSDEKLNQEGLFQFPTVIGGVVLAVNIPGLKSGELVLDGKTLGDIYLGKIKKWDDEAITKLNPGVKLPSQNIAVVRR 160
Cdd:PRK10918  81 DAPLSDEKLAQEGLFQFPTVIGGVVLAVNIPGLKSGELVLDGKTLGDIYLGKIKKWNDEAIAKLNPGVKLPSQNIAVVRR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550796614 161 ADGSGTSFVFTSYLAKVNEEWKSKVGSGSTVNWPTGLGGKGNDGIAAFVQRLPGSIGYVEYAYAKQNNLAYTKLVSADGK 240
Cdd:PRK10918 161 ADGSGTSFVFTSYLAKVNEEWKSKVGAGSTVNWPTGLGGKGNDGIAAFVQRLPGAIGYVEYAYAKQNNLAYTKLISADGK 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550796614 241 PVSPTEENFANAAKGADWSKSFAQDLTNQKGEDAWPITSTTFILVHKEQKKPEQGAEVLKFFDWAYKNGGKQANDLDYAS 320
Cdd:PRK10918 241 PVSPTEESFSNAAKGADWSKSFAQDLTNQKGDDAWPITSTTFILVHKDQKKPEQGAEVLKFFDWAYKNGAKQANDLDYAS 320

                        330       340
                 ....*....|....*....|....*.
gi 550796614 321 LPDSVVEQIRAAWKTNVKDSSGKALY 346
Cdd:PRK10918 321 LPDSVVEQVRAAWKTNIKDSSGKPLY 346
3a0107s03 TIGR00975
phosphate ABC transporter, phosphate-binding protein; This family represents one type of ...
 29-335 3.80e-144

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: 409.91  E-value: 3.80e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550796614   29 LTGAGATFPAPVYAKWADTYQKET-GNKVNYQGIGSSGGVKQITANTVDFGASDAPLSDEKL--NQEGLFQFPTVIGGVV 105
Cdd:TIGR00975   1 LTGAGSTFPAPLYTKWFPDFQKSNpGVTINYQGIGSGAGIAQFAAGTVDFGASDAPLSEADLaaAGSGLLNFPTVIGAIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550796614  106 LAVNIPGLKSgELVLDGKTLGDIYLGKIKKWDDEAITKLNPGVKLPSQNIAVVRRADGSGTSFVFTSYLAKVNEEWKSKV 185
Cdd:TIGR00975  81 VTYNLPGVSE-KLKLDGPVLAKIFLGKIKQWNDPAIAALNPGVKLPGTAITVVHRSDGSGTTFNFTNYLSKVSPEWGKKV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550796614  186 GSGSTVNWPTGLGGKGNDGIAAFVQRLPGSIGYVEYAYAKQNNLAYTKLVSADGKPVSPTEENFANAAKGADWS--KSFA 263
Cdd:TIGR00975 160 GAGKTVQWPAGVGGKGNDGVVAGVKQTPGAIGYVEWSFAKQNKLSFAALKNSAGKFVLPDAESIKAAAAGAKIStpKNDA 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 550796614  264 QDLTNQKGEDAWPITSTTFILVHKEQKKPEQGAEVLKFFDWAYKNGGKQANDLDYASLPDSVVEQIRAAWKT 335
Cdd:TIGR00975 240 ISMTDPPGPGAYPIVSYTYLIVYKKQKDPAKAKALKAFLTWAITNGQSFLDDLGYIPLPPSVVKRVRTAVNT 311
PBP2_PstS cd13565
Substrate binding domain of ABC-type phosphate transporter, a member of the type 2 ...
 29-317 5.99e-122

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: 351.15  E-value: 5.99e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550796614  29 LTGAGATFPAPVYAKWADTYQKET-GNKVNYQGIGSSGGVKQITANTVDFGASDAPLSDEKLNQE--GLFQFPTVIGGVV 105
Cdd:cd13565    4 LTGAGATFPAPLYQKWIDEYKKAHpGVKINYQSIGSGAGIKQFIAGTVDFGASDAPLSDAELAKAggGLLQIPTVIGAVV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550796614 106 LAVNIPGLKSGELvLDGKTLGDIYLGKIKKWDDEAITKLNPGVKLPSQNIAVVRRADGSGTSFVFTSYLAKVNEEWKSKV 185
Cdd:cd13565   84 VAYNLPGVKGLLL-LSGEVLADIFLGKITKWNDPAIAALNPGVNLPDTPITVVHRSDGSGTTFIFTDYLSAVSPEWKDKV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550796614 186 GSGSTVNWPTGLGGKGNDGIAAFVQRLPGSIGYVEYAYAKQNNLAYTKLvsadgkpvspteenfanaakgadwsksfaqd 265
Cdd:cd13565  163 GAGKSVAWPVGLGGKGNEGVAAAVKQTPGSIGYVELSYALQNGLPAAAL------------------------------- 211

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 550796614 266 ltnqkgedaWPITSTTFILVHKEQKKPEQGAEVLKFFDWAYKNGGKQANDLD 317
Cdd:cd13565  212 ---------YPIVGFTYILVKKDYKDAEKAKAVKKFLKWALTEGQKFAADLG 254
PstS COG0226
ABC-type phosphate transport system, periplasmic component [Inorganic ion transport and ...
 29-334 1.34e-87

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


Pssm-ID: 439996 [Multi-domain]  Cd Length: 275  Bit Score: 264.82  E-value: 1.34e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550796614  29 LTGAGATFPAPVYAKWADTYQKE-TGNKVNYQGIGSSGGVKQITANTVDFGASDAPLSDEKL-----NQEGLFQFPTVIG 102
Cdd:COG0226    6 ITIAGSSTVYPLAEAWAEAFQKAnPGVTINVQSGGSGGGIKQFIAGTVDIGNSSRPLKDEELeaakeNGVELVEIPVAID 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550796614 103 GVVLAVNipglKSGEL-VLDGKTLGDIYLGKIKKWDDeaitkLNPgvKLPSQNIAVVRRADGSGTSFVFTSYLAKVNEEW 181
Cdd:COG0226   86 GIAVVVN----PDNPVkNLTGEQLADIFSGKITNWND-----IGG--KLPDEPITVVGRSDGSGTTDYFTEYLLGVGAEV 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550796614 182 kskvgsgstvnWPTGLGGKGNDGIAAFVQRLPGSIGYVEYAYAKQNNLAYTKLVSADGKPVSPTEENFANaakgadwsks 261
Cdd:COG0226  155 -----------REGVEGAEGNEGVVQAVAQTPGAIGYVGLSYAEQNKLKALAIDNKAGKFVEPTAENIAA---------- 213

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 550796614 262 faqdltnqkgeDAWPITSTTFILVHKeqKKPEQGAEVLKFFDWAYKNGGKQ-ANDLDYASLPDSVVEQIRAAWK 334
Cdd:COG0226  214 -----------GSYPLSRPLYIYVKK--EPDAKAPAVKAFLDFVLSDGGQKiVEKLGYVPLPDAVVEKVRAALK 274
PBP_like_2 pfam12849
PBP superfamily domain; This domain belongs to the periplasmic binding protein superfamily.
 29-306 4.00e-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: 4.00e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550796614   29 LTGAGATFPAPVYAKWADTYQKE-TGNKVNYQGIGSSGGVKQITANTVDFGASDAPLSDEKLNQE------GLFQFPTVI 101
Cdd:pfam12849  12 ILIAGSSTQAPGLLDLAEAFEKKyPGAKVKVTSVGSGEGIKALLNGDVDVALVSRPLTEEEFEAFgangagGLVEVPVAY 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550796614  102 GGVVLAVNIPGlksGELVLDGKTLGDIYLGKIKKWDDeaitklnpgvKLPSQNIAVVRRADGSGTSFVFTSYLakvNEEW 181
Cdd:pfam12849  92 DGIAIVVNKDN---PANILTVEALKKIFSGKITNWND----------GGPDGPIKFVSRGDNSGTTELFSTHL---KEKG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550796614  182 KSKVGsgstvnwptGLGGKGNDGIAAfVQRLPGSIGYVEYAYAKQNNLAytKLVSADGKPVSPteenFANAAKGADWSKS 261
Cdd:pfam12849 156 PWGAA---------GIGAAGSPGVAS-VVAGPGAIGYVEVSYALANLGY--TLADVAGGTYLS----FAKALKVAKINPG 219

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 550796614  262 FAQDLTNQKG--EDAWPITSTTFILVHKEQKKPEQGAEvlKFFDWAY 306
Cdd:pfam12849 220 AGLVIPLEEAiaDGDYPLSRPYYVIVKNPPKGPAPLAK--AFLDFLL 264
 
Name Accession Description Interval E-value
PRK10918 PRK10918
phosphate ABC transporter substrate-binding protein PstS;
1-346 0e+00

phosphate ABC transporter substrate-binding protein PstS;


Pssm-ID: 182837  Cd Length: 346  Bit Score: 688.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550796614   1 MKVMRTTVATVVAATLSMSAFSAFAAASLTGAGATFPAPVYAKWADTYQKETGNKVNYQGIGSSGGVKQITANTVDFGAS 80
Cdd:PRK10918   1 MKVMRTTVATVVAATLSMSAFSAFAAASLTGAGATFPAPVYAKWADTYQKETGNKVNYQGIGSSGGVKQIIANTVDFGAS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550796614  81 DAPLSDEKLNQEGLFQFPTVIGGVVLAVNIPGLKSGELVLDGKTLGDIYLGKIKKWDDEAITKLNPGVKLPSQNIAVVRR 160
Cdd:PRK10918  81 DAPLSDEKLAQEGLFQFPTVIGGVVLAVNIPGLKSGELVLDGKTLGDIYLGKIKKWNDEAIAKLNPGVKLPSQNIAVVRR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550796614 161 ADGSGTSFVFTSYLAKVNEEWKSKVGSGSTVNWPTGLGGKGNDGIAAFVQRLPGSIGYVEYAYAKQNNLAYTKLVSADGK 240
Cdd:PRK10918 161 ADGSGTSFVFTSYLAKVNEEWKSKVGAGSTVNWPTGLGGKGNDGIAAFVQRLPGAIGYVEYAYAKQNNLAYTKLISADGK 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550796614 241 PVSPTEENFANAAKGADWSKSFAQDLTNQKGEDAWPITSTTFILVHKEQKKPEQGAEVLKFFDWAYKNGGKQANDLDYAS 320
Cdd:PRK10918 241 PVSPTEESFSNAAKGADWSKSFAQDLTNQKGDDAWPITSTTFILVHKDQKKPEQGAEVLKFFDWAYKNGAKQANDLDYAS 320

                        330       340
                 ....*....|....*....|....*.
gi 550796614 321 LPDSVVEQIRAAWKTNVKDSSGKALY 346
Cdd:PRK10918 321 LPDSVVEQVRAAWKTNIKDSSGKPLY 346
3a0107s03 TIGR00975
phosphate ABC transporter, phosphate-binding protein; This family represents one type of ...
 29-335 3.80e-144

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: 409.91  E-value: 3.80e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550796614   29 LTGAGATFPAPVYAKWADTYQKET-GNKVNYQGIGSSGGVKQITANTVDFGASDAPLSDEKL--NQEGLFQFPTVIGGVV 105
Cdd:TIGR00975   1 LTGAGSTFPAPLYTKWFPDFQKSNpGVTINYQGIGSGAGIAQFAAGTVDFGASDAPLSEADLaaAGSGLLNFPTVIGAIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550796614  106 LAVNIPGLKSgELVLDGKTLGDIYLGKIKKWDDEAITKLNPGVKLPSQNIAVVRRADGSGTSFVFTSYLAKVNEEWKSKV 185
Cdd:TIGR00975  81 VTYNLPGVSE-KLKLDGPVLAKIFLGKIKQWNDPAIAALNPGVKLPGTAITVVHRSDGSGTTFNFTNYLSKVSPEWGKKV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550796614  186 GSGSTVNWPTGLGGKGNDGIAAFVQRLPGSIGYVEYAYAKQNNLAYTKLVSADGKPVSPTEENFANAAKGADWS--KSFA 263
Cdd:TIGR00975 160 GAGKTVQWPAGVGGKGNDGVVAGVKQTPGAIGYVEWSFAKQNKLSFAALKNSAGKFVLPDAESIKAAAAGAKIStpKNDA 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 550796614  264 QDLTNQKGEDAWPITSTTFILVHKEQKKPEQGAEVLKFFDWAYKNGGKQANDLDYASLPDSVVEQIRAAWKT 335
Cdd:TIGR00975 240 ISMTDPPGPGAYPIVSYTYLIVYKKQKDPAKAKALKAFLTWAITNGQSFLDDLGYIPLPPSVVKRVRTAVNT 311
PBP2_PstS cd13565
Substrate binding domain of ABC-type phosphate transporter, a member of the type 2 ...
 29-317 5.99e-122

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: 351.15  E-value: 5.99e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550796614  29 LTGAGATFPAPVYAKWADTYQKET-GNKVNYQGIGSSGGVKQITANTVDFGASDAPLSDEKLNQE--GLFQFPTVIGGVV 105
Cdd:cd13565    4 LTGAGATFPAPLYQKWIDEYKKAHpGVKINYQSIGSGAGIKQFIAGTVDFGASDAPLSDAELAKAggGLLQIPTVIGAVV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550796614 106 LAVNIPGLKSGELvLDGKTLGDIYLGKIKKWDDEAITKLNPGVKLPSQNIAVVRRADGSGTSFVFTSYLAKVNEEWKSKV 185
Cdd:cd13565   84 VAYNLPGVKGLLL-LSGEVLADIFLGKITKWNDPAIAALNPGVNLPDTPITVVHRSDGSGTTFIFTDYLSAVSPEWKDKV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550796614 186 GSGSTVNWPTGLGGKGNDGIAAFVQRLPGSIGYVEYAYAKQNNLAYTKLvsadgkpvspteenfanaakgadwsksfaqd 265
Cdd:cd13565  163 GAGKSVAWPVGLGGKGNEGVAAAVKQTPGSIGYVELSYALQNGLPAAAL------------------------------- 211

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 550796614 266 ltnqkgedaWPITSTTFILVHKEQKKPEQGAEVLKFFDWAYKNGGKQANDLD 317
Cdd:cd13565  212 ---------YPIVGFTYILVKKDYKDAEKAKAVKKFLKWALTEGQKFAADLG 254
PBP2_phosphate_binding cd01006
Substrate binding domain of ABC-type phosphate transporter, a member of the type 2 ...
 29-317 1.46e-116

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: 337.70  E-value: 1.46e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550796614  29 LTGAGATFPAPVYAKWADTYQKET-GNKVNYQGIGSSGGVKQITANTVDFGASDAPLSDEKLNQEGLFQFPTVIGGVVLA 107
Cdd:cd01006    4 LTISGSTSVAPI*DVWAEKYNQQHpETYVAVQGVGSTAGISQLKAGTVDIGASDAYLSESEAANKGLHTFTLAIDGLAIV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550796614 108 VNIPGLKSGELVlDGKTLGDIYLGKIKKWDDEAITKLNPGVKLPSQNIAVVRRADGSGTSFVFTSYLAKVNEEWKSKVGS 187
Cdd:cd01006   84 VNQPGPVTNLTL-NGKQLYGIYKGQIKNWDDVGIAALNPGVNLPDQKIAVVTREDGSGTRFSFTSYLGKTKTEKDGKGTT 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550796614 188 GSTVNWPTGLGGKGNDGIAAFVQRLPGSIGYVEYAYAKQNNLAYTKLvsadgkpvspteenfanaakgadwsksfaqdlt 267
Cdd:cd01006  163 EVSDVAPTALGVNGNSG*KTLVNHNPGAVGYISIGSVDQSSLKAIQL--------------------------------- 209

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 550796614 268 nqkgedaWPITSTTFILVHKEQKKPEQGAEVLKFFDWAYKNGG-KQANDLD 317
Cdd:cd01006  210 -------YPISRPFLILHYSDQKDAATDEQTKEFIAWAKSEGAaKLIVEYG 253
PstS COG0226
ABC-type phosphate transport system, periplasmic component [Inorganic ion transport and ...
 29-334 1.34e-87

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


Pssm-ID: 439996 [Multi-domain]  Cd Length: 275  Bit Score: 264.82  E-value: 1.34e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550796614  29 LTGAGATFPAPVYAKWADTYQKE-TGNKVNYQGIGSSGGVKQITANTVDFGASDAPLSDEKL-----NQEGLFQFPTVIG 102
Cdd:COG0226    6 ITIAGSSTVYPLAEAWAEAFQKAnPGVTINVQSGGSGGGIKQFIAGTVDIGNSSRPLKDEELeaakeNGVELVEIPVAID 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550796614 103 GVVLAVNipglKSGEL-VLDGKTLGDIYLGKIKKWDDeaitkLNPgvKLPSQNIAVVRRADGSGTSFVFTSYLAKVNEEW 181
Cdd:COG0226   86 GIAVVVN----PDNPVkNLTGEQLADIFSGKITNWND-----IGG--KLPDEPITVVGRSDGSGTTDYFTEYLLGVGAEV 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550796614 182 kskvgsgstvnWPTGLGGKGNDGIAAFVQRLPGSIGYVEYAYAKQNNLAYTKLVSADGKPVSPTEENFANaakgadwsks 261
Cdd:COG0226  155 -----------REGVEGAEGNEGVVQAVAQTPGAIGYVGLSYAEQNKLKALAIDNKAGKFVEPTAENIAA---------- 213

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 550796614 262 faqdltnqkgeDAWPITSTTFILVHKeqKKPEQGAEVLKFFDWAYKNGGKQ-ANDLDYASLPDSVVEQIRAAWK 334
Cdd:COG0226  214 -----------GSYPLSRPLYIYVKK--EPDAKAPAVKAFLDFVLSDGGQKiVEKLGYVPLPDAVVEKVRAALK 274
PBP_like_2 pfam12849
PBP superfamily domain; This domain belongs to the periplasmic binding protein superfamily.
 29-306 4.00e-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: 4.00e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550796614   29 LTGAGATFPAPVYAKWADTYQKE-TGNKVNYQGIGSSGGVKQITANTVDFGASDAPLSDEKLNQE------GLFQFPTVI 101
Cdd:pfam12849  12 ILIAGSSTQAPGLLDLAEAFEKKyPGAKVKVTSVGSGEGIKALLNGDVDVALVSRPLTEEEFEAFgangagGLVEVPVAY 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550796614  102 GGVVLAVNIPGlksGELVLDGKTLGDIYLGKIKKWDDeaitklnpgvKLPSQNIAVVRRADGSGTSFVFTSYLakvNEEW 181
Cdd:pfam12849  92 DGIAIVVNKDN---PANILTVEALKKIFSGKITNWND----------GGPDGPIKFVSRGDNSGTTELFSTHL---KEKG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550796614  182 KSKVGsgstvnwptGLGGKGNDGIAAfVQRLPGSIGYVEYAYAKQNNLAytKLVSADGKPVSPteenFANAAKGADWSKS 261
Cdd:pfam12849 156 PWGAA---------GIGAAGSPGVAS-VVAGPGAIGYVEVSYALANLGY--TLADVAGGTYLS----FAKALKVAKINPG 219

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 550796614  262 FAQDLTNQKG--EDAWPITSTTFILVHKEQKKPEQGAEvlKFFDWAY 306
Cdd:pfam12849 220 AGLVIPLEEAiaDGDYPLSRPYYVIVKNPPKGPAPLAK--AFLDFLL 264
PBP2_phosphate_like_1 cd13653
Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 ...
 29-312 1.24e-26

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: 105.73  E-value: 1.24e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550796614  29 LTGAGATFPAPVYAKWADTYQKETGN-KVNYQGIGSSGGVKQITANTVDFGASDAPLSDEKLNQEGLFQfPTVIG--GVV 105
Cdd:cd13653    4 ITISGSTTVAPLAEALAEAFMEKHPGvRIEVQGGGSGTGIKALIEGTADIGMASRPLKAEEKAAASGLV-EHVIAldGIA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550796614 106 LAVNiPGLKSGELVLDgkTLGDIYLGKIKKWDDeaitklnpgVKLPSQNIAVVRRADGSGTSFVFTSYLAKvneewKSKV 185
Cdd:cd13653   83 IIVN-PDNPVKNLTLE--QLRDIFSGKITNWKE---------VGGPDGPIVVISREEGSGTRETFEELVLG-----KKDF 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550796614 186 GSGSTVnwptglgGKGNDGIAAFVQRLPGSIGYVEYAYAKQNNLaytKLVSADGkpVSPTEENFANAakgadwsksfaqd 265
Cdd:cd13653  146 AKNAVV-------VPSNGAVVQAVAKNPNAIGYVSLGYVDDSKV---KALSVDG--VAPTPENIKSG------------- 200

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 550796614 266 ltnqkgedAWPITSTTFILVHKEQKKpeqgaEVLKFFDWAYKNGGKQ 312
Cdd:cd13653  201 --------KYPLSRPLYLYTKGEPSG-----LVKAFIDFALSPEGQA 234
ptsS_2 TIGR02136
phosphate binding protein; Members of this family are phosphate-binding proteins. Most are ...
 29-301 1.40e-25

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: 104.06  E-value: 1.40e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550796614   29 LTGAGATFPAPVYAKWADTYQKETGN-KVNYQGIGSSGGVKQITANTVDFGASDAPLSDE---KLNQEG--LFQFPTVIG 102
Cdd:TIGR02136  38 ITIDGSTTVAPLAEAAAEEFQKIHPGvSVTVQGAGSGTGIKALINGTVDIGNSSRPIKDEelqKDKQKGikLIEHKVAVD 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550796614  103 GVVLAVNIPGLKSGELVLDgkTLGDIYLGKIKKWDDeaitkLNPgvKLPSQNIAVVRRADGSGTSFVFTSylaKVNEEWK 182
Cdd:TIGR02136 118 GLAVVVNKKNVPVDDLTVE--QLKKIYSGEITNWKE-----VGG--DLPNKPIVVVGRNAGSGTRDTFEE---EVMGKAK 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550796614  183 SKVGSGSTvnwptglggKGNDGIAAFVQRLPGSIGYVEYAYAKQNnlayTKLVSADGkpVSPTEENFANAakgadwsksf 262
Cdd:TIGR02136 186 IKPGKNEQ---------ESNGAVVSIVSSNPGAIGYLGLGYVDDS----VKTLKVNG--VEPSKENIANG---------- 240

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 550796614  263 aqdltnqkgedAWPITSTTFILVHKEQKKPEQGAEVLKF 301
Cdd:TIGR02136 241 -----------SYPLSRPLFMYVNGKPKKPELVAEFIDF 268
PBP2_phosphate cd13566
Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 ...
 29-313 2.64e-24

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: 99.58  E-value: 2.64e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550796614  29 LTGAGATFPAPVYAKWADTYQKETGN-KVNYQGIGSSGGVKQITANTVDFGASDAPLSDE-----KLNQEGLFQFPTVIG 102
Cdd:cd13566    4 ITIAGSSTVAPLAEALAEEFMKKHPGvRVTVQGGGSGAGIKALIAGTADIAMASRPLKDEekaaaEANGIELVEFVIAYD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550796614 103 GVVLAVNiPGLKSGELVLDgkTLGDIYLGKIKKWDDeaitklnpgVKLPSQNIAVVRRADGSGTSFVFTSYLAKvneewK 182
Cdd:cd13566   84 GIAVIVN-PDNPVASLTLE--QLRDIFTGKITNWSE---------VGGPDEPIVVYGRDEGSGTRDYFEELVLG-----K 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550796614 183 SKVGSGSTVnwptglgGKGNDGIAAFVQRLPGSIGYVEYAYAKQNNLAytKLVSADGkpVSPTEENFANaakgadwsksf 262
Cdd:cd13566  147 GEFIRNAVV-------APSNGALVQAVAGDPNAIGYVGLGYVDENKKV--KALKVDG--VAPTVENIKS----------- 204

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 550796614 263 aqdltnqkgeDAWPITSTTFILVHKEQKKpeqgaEVLKFFDWAYKNGGKQA 313
Cdd:cd13566  205 ----------GKYPLSRPLFLYTKGEPSP-----AVKAFIDFALSPEGQKI 240
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 43-312 5.55e-07

Bacterial extracellular solute-binding protein; This family also includes the bacterial extracellular solute-binding protein family POTD/POTF.


Pssm-ID: 460248 [Multi-domain]  Cd Length: 294  Bit Score: 50.49  E-value: 5.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550796614   43 KWADTYQKE-TGNKVNYQGIGSSGGVKQITAntvDFGASDAP-----LSDEKLNQEGLFQFPTVIGGVVLAVNIPGL-KS 115
Cdd:pfam01547  12 ALVKEFEKEhPGIKVEVESVGSGSLAQKLTT---AIAAGDGPadvfaSDNDWIAELAKAGLLLPLDDYVANYLVLGVpKL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550796614  116 GELVLDGKTLGDIY---------LGKIKKWDDEAITKLNPGVKLPSqnIAVVRRADGSGTSFVFTSYLAKV-NEEWKSKV 185
Cdd:pfam01547  89 YGVPLAAETLGLIYnkdlfkkagLDPPKTWDELLEAAKKLKEKGKS--PGGAGGGDASGTLGYFTLALLASlGGPLFDKD 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550796614  186 GSGstVNWPTGLGGKGNDGIAAFVQRLPGSIGYVEYAYAKQNNLAytKLVSADGKPVSPTEENFANAAKGADWSKSFAQD 265
Cdd:pfam01547 167 GGG--LDNPEAVDAITYYVDLYAKVLLLKKLKNPGVAGADGREAL--ALFEQGKAAMGIVGPWAALAANKVKLKVAFAAP 242

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 550796614  266 LTNQKGEDAWPI---------TSTTFILVHKEQKKpeqgAEVLKFFDWAYKNGGKQ 312
Cdd:pfam01547 243 APDPKGDVGYAPlpagkggkgGGYGLAIPKGSKNK----EAAKKFLDFLTSPEAQA 294
Periplasmic_Binding_Protein_Type_2 cd00648
Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent ...
 29-234 2.41e-05

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: 44.49  E-value: 2.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550796614  29 LTGAGATFP--APVYAKWADTYQKETGNKVNYQGIGSSGGV-KQITANTVDFGASDAPLSDE----KLNQEGLFQFPTV- 100
Cdd:cd00648    2 LTVASIGPPpyAGFAEDAAKQLAKETGIKVELVPGSSIGTLiEALAAGDADVAVGPIAPALEaaadKLAPGGLYIVPELy 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550796614 101 IGGVVLAVNIPGLKSGelvldgktlgdiylgkikkwddeaitklnPGVKLPSQNIAVVRRADGSGTSFVFTSYLAKVNEE 180
Cdd:cd00648   82 VGGYVLVVRKGSSIKG-----------------------------LLAVADLDGKRVGVGDPGSTAVRQARLALGAYGLK 132

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 550796614 181 WKskvgsgstvnWPTGLGGKGNDGIAAFVQRLPGSIGYVEYAYAKQNNLAYTKL 234
Cdd:cd00648  133 KK----------DPEVVPVPGTSGALAAVANGAVDAAIVWVPAAERAQLGNVQL 176
PBP2_phosphate_like_2 cd13654
Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 ...
 38-248 2.46e-05

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: 45.32  E-value: 2.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550796614  38 APVYAKWADTYQKETGN-KVNYQGIGSSGGVKQITANTVDFGASDAPLSDE-----KLNQEGLFQFPTVIGGVVLAVNIP 111
Cdd:cd13654   13 YPITEAVAEEFGKSGPGvTVTVGSSGTGGGFKKFCAGETDISNASRPIKDSeaelcEANGIEYIELPVAYDGLTVVVNPA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550796614 112 GLKSGELVLDGKTLGDIYLGKIKKWDDeaitkLNPGvkLPSQNIAVVRRADGSGTSFVFTSylaKVNEEWKSKVGSGStv 191
Cdd:cd13654   93 NDWAKCLTELELKSIWAAESPITTWSD-----VRPS--WPDEPIELYGPGTDSGTFDYFTE---AIVGEGGSIREDYT-- 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 550796614 192 nwptglgGKGNDG-IAAFVQRLPGSIGYVEYAYAKQNNlAYTKLVSADG--KPVSPTEEN 248
Cdd:cd13654  161 -------ASEDDNvLVQGVAGDKNALGFFGYAYYEENG-DKLKAVKIDGgeGTVAPSAET 212
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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