NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|502613375|ref|WP_012850331|]
View 

phosphate ABC transporter substrate-binding protein PstS [Edwardsiella piscicida]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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: 685.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502613375   1 MKLMRTAVAGIVAATVSLSAMPAFAAESLTGAGATFPAPVYAKWADSYQKETGNKVNYQGIGSSGGVKQIIANTVDFGAS 80
Cdd:PRK10918   1 MKVMRTTVATVVAATLSMSAFSAFAAASLTGAGATFPAPVYAKWADTYQKETGNKVNYQGIGSSGGVKQIIANTVDFGAS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502613375  81 DAPLSEEKLAADGLFQFPTVIGGVVMAVNLPGITSGELTLDGETLGDIYLGKIKKWNDAAIAKLNPGVKLPDQAIAVVRR 160
Cdd:PRK10918  81 DAPLSDEKLAQEGLFQFPTVIGGVVLAVNIPGLKSGELVLDGKTLGDIYLGKIKKWNDEAIAKLNPGVKLPSQNIAVVRR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502613375 161 ADGSGTSFVFTSYLNKVNAQWKSDVGAGSTVNWPTGLGGKGNDGVAAFVQRLPGAIGYVEYAYAKQNKLAYTKLISSEGQ 240
Cdd:PRK10918 161 ADGSGTSFVFTSYLAKVNEEWKSKVGAGSTVNWPTGLGGKGNDGIAAFVQRLPGAIGYVEYAYAKQNNLAYTKLISADGK 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502613375 241 AVSPTEVSFSNAAKGADWSASFAQDLTNQPGDNVWPITSTTFILVHKESSKPKQTAEVLKFFDWAYSKGAKQANDLDYAT 320
Cdd:PRK10918 241 PVSPTEESFSNAAKGADWSKSFAQDLTNQKGDDAWPITSTTFILVHKDQKKPEQGAEVLKFFDWAYKNGAKQANDLDYAS 320

                        330       340
                 ....*....|....*....|....*.
gi 502613375 321 LPASVVEHIRTAWKSSVKDSGGNALY 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: 685.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502613375   1 MKLMRTAVAGIVAATVSLSAMPAFAAESLTGAGATFPAPVYAKWADSYQKETGNKVNYQGIGSSGGVKQIIANTVDFGAS 80
Cdd:PRK10918   1 MKVMRTTVATVVAATLSMSAFSAFAAASLTGAGATFPAPVYAKWADTYQKETGNKVNYQGIGSSGGVKQIIANTVDFGAS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502613375  81 DAPLSEEKLAADGLFQFPTVIGGVVMAVNLPGITSGELTLDGETLGDIYLGKIKKWNDAAIAKLNPGVKLPDQAIAVVRR 160
Cdd:PRK10918  81 DAPLSDEKLAQEGLFQFPTVIGGVVLAVNIPGLKSGELVLDGKTLGDIYLGKIKKWNDEAIAKLNPGVKLPSQNIAVVRR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502613375 161 ADGSGTSFVFTSYLNKVNAQWKSDVGAGSTVNWPTGLGGKGNDGVAAFVQRLPGAIGYVEYAYAKQNKLAYTKLISSEGQ 240
Cdd:PRK10918 161 ADGSGTSFVFTSYLAKVNEEWKSKVGAGSTVNWPTGLGGKGNDGIAAFVQRLPGAIGYVEYAYAKQNNLAYTKLISADGK 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502613375 241 AVSPTEVSFSNAAKGADWSASFAQDLTNQPGDNVWPITSTTFILVHKESSKPKQTAEVLKFFDWAYSKGAKQANDLDYAT 320
Cdd:PRK10918 241 PVSPTEESFSNAAKGADWSKSFAQDLTNQKGDDAWPITSTTFILVHKDQKKPEQGAEVLKFFDWAYKNGAKQANDLDYAS 320

                        330       340
                 ....*....|....*....|....*.
gi 502613375 321 LPASVVEHIRTAWKSSVKDSGGNALY 346
Cdd:PRK10918 321 LPDSVVEQVRAAWKTNIKDSSGKPLY 346
3a0107s03 TIGR00975
phosphate ABC transporter, phosphate-binding protein; This family represents one type of ...
 29-335 5.33e-139

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: 396.81  E-value: 5.33e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502613375   29 LTGAGATFPAPVYAKWADSYQKET-GNKVNYQGIGSSGGVKQIIANTVDFGASDAPLSEEKLAA--DGLFQFPTVIGGVV 105
Cdd:TIGR00975   1 LTGAGSTFPAPLYTKWFPDFQKSNpGVTINYQGIGSGAGIAQFAAGTVDFGASDAPLSEADLAAagSGLLNFPTVIGAIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502613375  106 MAVNLPGITSgELTLDGETLGDIYLGKIKKWNDAAIAKLNPGVKLPDQAIAVVRRADGSGTSFVFTSYLNKVNAQWKSDV 185
Cdd:TIGR00975  81 VTYNLPGVSE-KLKLDGPVLAKIFLGKIKQWNDPAIAALNPGVKLPGTAITVVHRSDGSGTTFNFTNYLSKVSPEWGKKV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502613375  186 GAGSTVNWPTGLGGKGNDGVAAFVQRLPGAIGYVEYAYAKQNKLAYTKLISSEGQAVSPTEVSFSNAAKGADWS--ASFA 263
Cdd:TIGR00975 160 GAGKTVQWPAGVGGKGNDGVVAGVKQTPGAIGYVEWSFAKQNKLSFAALKNSAGKFVLPDAESIKAAAAGAKIStpKNDA 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502613375  264 QDLTNQPGDNVWPITSTTFILVHKESSKPKQTAEVLKFFDWAYSKGAKQANDLDYATLPASVVEHIRTAWKS 335
Cdd:TIGR00975 240 ISMTDPPGPGAYPIVSYTYLIVYKKQKDPAKAKALKAFLTWAITNGQSFLDDLGYIPLPPSVVKRVRTAVNT 311
PBP2_PstS cd13565
Substrate binding domain of ABC-type phosphate transporter, a member of the type 2 ...
 26-317 1.05e-118

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: 343.06  E-value: 1.05e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502613375  26 AESLTGAGATFPAPVYAKWADSYQKET-GNKVNYQGIGSSGGVKQIIANTVDFGASDAPLSEEKLAA--DGLFQFPTVIG 102
Cdd:cd13565    1 AVTLTGAGATFPAPLYQKWIDEYKKAHpGVKINYQSIGSGAGIKQFIAGTVDFGASDAPLSDAELAKagGGLLQIPTVIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502613375 103 GVVMAVNLPGITSGELtLDGETLGDIYLGKIKKWNDAAIAKLNPGVKLPDQAIAVVRRADGSGTSFVFTSYLNKVNAQWK 182
Cdd:cd13565   81 AVVVAYNLPGVKGLLL-LSGEVLADIFLGKITKWNDPAIAALNPGVNLPDTPITVVHRSDGSGTTFIFTDYLSAVSPEWK 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502613375 183 SDVGAGSTVNWPTGLGGKGNDGVAAFVQRLPGAIGYVEYAYAKQNKLAYTKLissegqavsptevsfsnaakgadwsasf 262
Cdd:cd13565  160 DKVGAGKSVAWPVGLGGKGNEGVAAAVKQTPGSIGYVELSYALQNGLPAAAL---------------------------- 211

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 502613375 263 aqdltnqpgdnvWPITSTTFILVHKESSKPKQTAEVLKFFDWAYSKGAKQANDLD 317
Cdd:cd13565  212 ------------YPIVGFTYILVKKDYKDAEKAKAVKKFLKWALTEGQKFAADLG 254
PstS COG0226
ABC-type phosphate transport system, periplasmic component [Inorganic ion transport and ...
 25-335 1.16e-85

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


Pssm-ID: 439996 [Multi-domain]  Cd Length: 275  Bit Score: 259.82  E-value: 1.16e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502613375  25 AAESLTGAGATFPAPVYAKWADSYQKE-TGNKVNYQGIGSSGGVKQIIANTVDFGASDAPLSEEKLAA-----DGLFQFP 98
Cdd:COG0226    2 ASGTITIAGSSTVYPLAEAWAEAFQKAnPGVTINVQSGGSGGGIKQFIAGTVDIGNSSRPLKDEELEAakengVELVEIP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502613375  99 TVIGGVVMAVNlpgiTSGELT-LDGETLGDIYLGKIKKWNDaaiakLNPgvKLPDQAIAVVRRADGSGTSFVFTSYLNKV 177
Cdd:COG0226   82 VAIDGIAVVVN----PDNPVKnLTGEQLADIFSGKITNWND-----IGG--KLPDEPITVVGRSDGSGTTDYFTEYLLGV 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502613375 178 NAQWKSDVgagstvnwptgLGGKGNDGVAAFVQRLPGAIGYVEYAYAKQNKLAYTKLISSEGQAVSPTEvsfSNAAKGAd 257
Cdd:COG0226  151 GAEVREGV-----------EGAEGNEGVVQAVAQTPGAIGYVGLSYAEQNKLKALAIDNKAGKFVEPTA---ENIAAGS- 215

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502613375 258 wsasfaqdltnqpgdnvWPITSTTFILVHKESSkpKQTAEVLKFFDWAYSKGAKQ-ANDLDYATLPASVVEHIRTAWKS 335
Cdd:COG0226  216 -----------------YPLSRPLYIYVKKEPD--AKAPAVKAFLDFVLSDGGQKiVEKLGYVPLPDAVVEKVRAALKA 275
PBP_like_2 pfam12849
PBP superfamily domain; This domain belongs to the periplasmic binding protein superfamily.
 23-307 1.18e-38

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


Pssm-ID: 432831 [Multi-domain]  Cd Length: 267  Bit Score: 138.45  E-value: 1.18e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502613375   23 AFAAESLTGAGATFPAPVYAKWADSYQKE-TGNKVNYQGIGSSGGVKQIIANTVDFGASDAPLSEEKLAAD------GLF 95
Cdd:pfam12849   6 APTVGTILIAGSSTQAPGLLDLAEAFEKKyPGAKVKVTSVGSGEGIKALLNGDVDVALVSRPLTEEEFEAFgangagGLV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502613375   96 QFPTVIGGVVMAVNLPGitsGELTLDGETLGDIYLGKIKKWNDaaiaklnpgvKLPDQAIAVVRRADGSGTSFVFTSYLN 175
Cdd:pfam12849  86 EVPVAYDGIAIVVNKDN---PANILTVEALKKIFSGKITNWND----------GGPDGPIKFVSRGDNSGTTELFSTHLK 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502613375  176 KVnAQWKSdvgagstvnwpTGLGGKGNDGVAAfVQRLPGAIGYVEYAYAKQNKLAYTKLISsegqavSPTEVSFSNAAKG 255
Cdd:pfam12849 153 EK-GPWGA-----------AGIGAAGSPGVAS-VVAGPGAIGYVEVSYALANLGYTLADVA------GGTYLSFAKALKV 213

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 502613375  256 ADWSASFAQD--LTNQPGDNVWPITSTTFILVHKESSKPkqTAEVLKFFDWAYS 307
Cdd:pfam12849 214 AKINPGAGLVipLEEAIADGDYPLSRPYYVIVKNPPKGP--APLAKAFLDFLLS 265
 
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: 685.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502613375   1 MKLMRTAVAGIVAATVSLSAMPAFAAESLTGAGATFPAPVYAKWADSYQKETGNKVNYQGIGSSGGVKQIIANTVDFGAS 80
Cdd:PRK10918   1 MKVMRTTVATVVAATLSMSAFSAFAAASLTGAGATFPAPVYAKWADTYQKETGNKVNYQGIGSSGGVKQIIANTVDFGAS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502613375  81 DAPLSEEKLAADGLFQFPTVIGGVVMAVNLPGITSGELTLDGETLGDIYLGKIKKWNDAAIAKLNPGVKLPDQAIAVVRR 160
Cdd:PRK10918  81 DAPLSDEKLAQEGLFQFPTVIGGVVLAVNIPGLKSGELVLDGKTLGDIYLGKIKKWNDEAIAKLNPGVKLPSQNIAVVRR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502613375 161 ADGSGTSFVFTSYLNKVNAQWKSDVGAGSTVNWPTGLGGKGNDGVAAFVQRLPGAIGYVEYAYAKQNKLAYTKLISSEGQ 240
Cdd:PRK10918 161 ADGSGTSFVFTSYLAKVNEEWKSKVGAGSTVNWPTGLGGKGNDGIAAFVQRLPGAIGYVEYAYAKQNNLAYTKLISADGK 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502613375 241 AVSPTEVSFSNAAKGADWSASFAQDLTNQPGDNVWPITSTTFILVHKESSKPKQTAEVLKFFDWAYSKGAKQANDLDYAT 320
Cdd:PRK10918 241 PVSPTEESFSNAAKGADWSKSFAQDLTNQKGDDAWPITSTTFILVHKDQKKPEQGAEVLKFFDWAYKNGAKQANDLDYAS 320

                        330       340
                 ....*....|....*....|....*.
gi 502613375 321 LPASVVEHIRTAWKSSVKDSGGNALY 346
Cdd:PRK10918 321 LPDSVVEQVRAAWKTNIKDSSGKPLY 346
3a0107s03 TIGR00975
phosphate ABC transporter, phosphate-binding protein; This family represents one type of ...
 29-335 5.33e-139

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: 396.81  E-value: 5.33e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502613375   29 LTGAGATFPAPVYAKWADSYQKET-GNKVNYQGIGSSGGVKQIIANTVDFGASDAPLSEEKLAA--DGLFQFPTVIGGVV 105
Cdd:TIGR00975   1 LTGAGSTFPAPLYTKWFPDFQKSNpGVTINYQGIGSGAGIAQFAAGTVDFGASDAPLSEADLAAagSGLLNFPTVIGAIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502613375  106 MAVNLPGITSgELTLDGETLGDIYLGKIKKWNDAAIAKLNPGVKLPDQAIAVVRRADGSGTSFVFTSYLNKVNAQWKSDV 185
Cdd:TIGR00975  81 VTYNLPGVSE-KLKLDGPVLAKIFLGKIKQWNDPAIAALNPGVKLPGTAITVVHRSDGSGTTFNFTNYLSKVSPEWGKKV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502613375  186 GAGSTVNWPTGLGGKGNDGVAAFVQRLPGAIGYVEYAYAKQNKLAYTKLISSEGQAVSPTEVSFSNAAKGADWS--ASFA 263
Cdd:TIGR00975 160 GAGKTVQWPAGVGGKGNDGVVAGVKQTPGAIGYVEWSFAKQNKLSFAALKNSAGKFVLPDAESIKAAAAGAKIStpKNDA 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502613375  264 QDLTNQPGDNVWPITSTTFILVHKESSKPKQTAEVLKFFDWAYSKGAKQANDLDYATLPASVVEHIRTAWKS 335
Cdd:TIGR00975 240 ISMTDPPGPGAYPIVSYTYLIVYKKQKDPAKAKALKAFLTWAITNGQSFLDDLGYIPLPPSVVKRVRTAVNT 311
PBP2_PstS cd13565
Substrate binding domain of ABC-type phosphate transporter, a member of the type 2 ...
 26-317 1.05e-118

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: 343.06  E-value: 1.05e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502613375  26 AESLTGAGATFPAPVYAKWADSYQKET-GNKVNYQGIGSSGGVKQIIANTVDFGASDAPLSEEKLAA--DGLFQFPTVIG 102
Cdd:cd13565    1 AVTLTGAGATFPAPLYQKWIDEYKKAHpGVKINYQSIGSGAGIKQFIAGTVDFGASDAPLSDAELAKagGGLLQIPTVIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502613375 103 GVVMAVNLPGITSGELtLDGETLGDIYLGKIKKWNDAAIAKLNPGVKLPDQAIAVVRRADGSGTSFVFTSYLNKVNAQWK 182
Cdd:cd13565   81 AVVVAYNLPGVKGLLL-LSGEVLADIFLGKITKWNDPAIAALNPGVNLPDTPITVVHRSDGSGTTFIFTDYLSAVSPEWK 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502613375 183 SDVGAGSTVNWPTGLGGKGNDGVAAFVQRLPGAIGYVEYAYAKQNKLAYTKLissegqavsptevsfsnaakgadwsasf 262
Cdd:cd13565  160 DKVGAGKSVAWPVGLGGKGNEGVAAAVKQTPGSIGYVELSYALQNGLPAAAL---------------------------- 211

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 502613375 263 aqdltnqpgdnvWPITSTTFILVHKESSKPKQTAEVLKFFDWAYSKGAKQANDLD 317
Cdd:cd13565  212 ------------YPIVGFTYILVKKDYKDAEKAKAVKKFLKWALTEGQKFAADLG 254
PBP2_phosphate_binding cd01006
Substrate binding domain of ABC-type phosphate transporter, a member of the type 2 ...
 26-317 2.20e-109

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: 319.59  E-value: 2.20e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502613375  26 AESLTGAGATFPAPVYAKWADSYQKET-GNKVNYQGIGSSGGVKQIIANTVDFGASDAPLSEEKLAADGLFQFPTVIGGV 104
Cdd:cd01006    1 ASELTISGSTSVAPI*DVWAEKYNQQHpETYVAVQGVGSTAGISQLKAGTVDIGASDAYLSESEAANKGLHTFTLAIDGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502613375 105 VMAVNLPGITSGeLTLDGETLGDIYLGKIKKWNDAAIAKLNPGVKLPDQAIAVVRRADGSGTSFVFTSYLNKVNAQWKSD 184
Cdd:cd01006   81 AIVVNQPGPVTN-LTLNGKQLYGIYKGQIKNWDDVGIAALNPGVNLPDQKIAVVTREDGSGTRFSFTSYLGKTKTEKDGK 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502613375 185 VGAGSTVNWPTGLGGKGNDGVAAFVQRLPGAIGYVEYAYAKQNKLAYTKLissegqavsptevsfsnaakgadwsasfaq 264
Cdd:cd01006  160 GTTEVSDVAPTALGVNGNSG*KTLVNHNPGAVGYISIGSVDQSSLKAIQL------------------------------ 209

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 502613375 265 dltnqpgdnvWPITSTTFILVHKESSKPKQTAEVLKFFDWAYSKG-AKQANDLD 317
Cdd:cd01006  210 ----------YPISRPFLILHYSDQKDAATDEQTKEFIAWAKSEGaAKLIVEYG 253
PstS COG0226
ABC-type phosphate transport system, periplasmic component [Inorganic ion transport and ...
 25-335 1.16e-85

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


Pssm-ID: 439996 [Multi-domain]  Cd Length: 275  Bit Score: 259.82  E-value: 1.16e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502613375  25 AAESLTGAGATFPAPVYAKWADSYQKE-TGNKVNYQGIGSSGGVKQIIANTVDFGASDAPLSEEKLAA-----DGLFQFP 98
Cdd:COG0226    2 ASGTITIAGSSTVYPLAEAWAEAFQKAnPGVTINVQSGGSGGGIKQFIAGTVDIGNSSRPLKDEELEAakengVELVEIP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502613375  99 TVIGGVVMAVNlpgiTSGELT-LDGETLGDIYLGKIKKWNDaaiakLNPgvKLPDQAIAVVRRADGSGTSFVFTSYLNKV 177
Cdd:COG0226   82 VAIDGIAVVVN----PDNPVKnLTGEQLADIFSGKITNWND-----IGG--KLPDEPITVVGRSDGSGTTDYFTEYLLGV 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502613375 178 NAQWKSDVgagstvnwptgLGGKGNDGVAAFVQRLPGAIGYVEYAYAKQNKLAYTKLISSEGQAVSPTEvsfSNAAKGAd 257
Cdd:COG0226  151 GAEVREGV-----------EGAEGNEGVVQAVAQTPGAIGYVGLSYAEQNKLKALAIDNKAGKFVEPTA---ENIAAGS- 215

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502613375 258 wsasfaqdltnqpgdnvWPITSTTFILVHKESSkpKQTAEVLKFFDWAYSKGAKQ-ANDLDYATLPASVVEHIRTAWKS 335
Cdd:COG0226  216 -----------------YPLSRPLYIYVKKEPD--AKAPAVKAFLDFVLSDGGQKiVEKLGYVPLPDAVVEKVRAALKA 275
PBP_like_2 pfam12849
PBP superfamily domain; This domain belongs to the periplasmic binding protein superfamily.
 23-307 1.18e-38

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


Pssm-ID: 432831 [Multi-domain]  Cd Length: 267  Bit Score: 138.45  E-value: 1.18e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502613375   23 AFAAESLTGAGATFPAPVYAKWADSYQKE-TGNKVNYQGIGSSGGVKQIIANTVDFGASDAPLSEEKLAAD------GLF 95
Cdd:pfam12849   6 APTVGTILIAGSSTQAPGLLDLAEAFEKKyPGAKVKVTSVGSGEGIKALLNGDVDVALVSRPLTEEEFEAFgangagGLV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502613375   96 QFPTVIGGVVMAVNLPGitsGELTLDGETLGDIYLGKIKKWNDaaiaklnpgvKLPDQAIAVVRRADGSGTSFVFTSYLN 175
Cdd:pfam12849  86 EVPVAYDGIAIVVNKDN---PANILTVEALKKIFSGKITNWND----------GGPDGPIKFVSRGDNSGTTELFSTHLK 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502613375  176 KVnAQWKSdvgagstvnwpTGLGGKGNDGVAAfVQRLPGAIGYVEYAYAKQNKLAYTKLISsegqavSPTEVSFSNAAKG 255
Cdd:pfam12849 153 EK-GPWGA-----------AGIGAAGSPGVAS-VVAGPGAIGYVEVSYALANLGYTLADVA------GGTYLSFAKALKV 213

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 502613375  256 ADWSASFAQD--LTNQPGDNVWPITSTTFILVHKESSKPkqTAEVLKFFDWAYS 307
Cdd:pfam12849 214 AKINPGAGLVipLEEAIADGDYPLSRPYYVIVKNPPKGP--APLAKAFLDFLLS 265
PBP2_phosphate_like_1 cd13653
Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 ...
 26-312 5.85e-32

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: 119.98  E-value: 5.85e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502613375  26 AESLTGAGATFPAPVYAKWADSYQKETGN-KVNYQGIGSSGGVKQIIANTVDFGASDAPLS-EEKLAADGLFQFPTVIGG 103
Cdd:cd13653    1 SGTITISGSTTVAPLAEALAEAFMEKHPGvRIEVQGGGSGTGIKALIEGTADIGMASRPLKaEEKAAASGLVEHVIALDG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502613375 104 VVMAVNlPGITSGELTLdgETLGDIYLGKIKKWNDaaiaklnpgVKLPDQAIAVVRRADGSGTSFVFTSYLNKvnaqwKS 183
Cdd:cd13653   81 IAIIVN-PDNPVKNLTL--EQLRDIFSGKITNWKE---------VGGPDGPIVVISREEGSGTRETFEELVLG-----KK 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502613375 184 DVGAGSTVnwptglgGKGNDGVAAFVQRLPGAIGYVEYAYAKQNKLaytKLISSEGqaVSPTEVsfsNAAKGAdwsasfa 263
Cdd:cd13653  144 DFAKNAVV-------VPSNGAVVQAVAKNPNAIGYVSLGYVDDSKV---KALSVDG--VAPTPE---NIKSGK------- 201

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 502613375 264 qdltnqpgdnvWPITSTTFILVHKESSKpkqtaEVLKFFDWAYSKGAKQ 312
Cdd:cd13653  202 -----------YPLSRPLYLYTKGEPSG-----LVKAFIDFALSPEGQA 234
ptsS_2 TIGR02136
phosphate binding protein; Members of this family are phosphate-binding proteins. Most are ...
 7-301 4.03e-30

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: 116.00  E-value: 4.03e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502613375    7 AVAGIVAATVSLSAmPAFAAESLTGAGATFPAPVYAKWADSYQKETGN-KVNYQGIGSSGGVKQIIANTVDFGASDAPLS 85
Cdd:TIGR02136  17 AAAGCGGAIDSGIP-DAKGSSTITIDGSTTVAPLAEAAAEEFQKIHPGvSVTVQGAGSGTGIKALINGTVDIGNSSRPIK 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502613375   86 EEKLAADG-----LFQFPTVIGGVVMAVNLPGITSGELTLdgETLGDIYLGKIKKWNDAaiaklnpGVKLPDQAIAVVRR 160
Cdd:TIGR02136  96 DEELQKDKqkgikLIEHKVAVDGLAVVVNKKNVPVDDLTV--EQLKKIYSGEITNWKEV-------GGDLPNKPIVVVGR 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502613375  161 ADGSGTSFVFTsylNKVNAQWKSDVGAGSTvnwptglggKGNDGVAAFVQRLPGAIGYVEYAYAKQNKlaytKLISSEGq 240
Cdd:TIGR02136 167 NAGSGTRDTFE---EEVMGKAKIKPGKNEQ---------ESNGAVVSIVSSNPGAIGYLGLGYVDDSV----KTLKVNG- 229

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502613375  241 avspTEVSFSNAAKGAdwsasfaqdltnqpgdnvWPITSTTFILVHKESSKPKQTAEVLKF 301
Cdd:TIGR02136 230 ----VEPSKENIANGS------------------YPLSRPLFMYVNGKPKKPELVAEFIDF 268
PBP2_phosphate cd13566
Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 ...
 26-313 2.31e-28

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: 110.37  E-value: 2.31e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502613375  26 AESLTGAGATFPAPVYAKWADSYQKETGN-KVNYQGIGSSGGVKQIIANTVDFGASDAPL--SEEKLAADGLFQF-PTVI 101
Cdd:cd13566    1 SGTITIAGSSTVAPLAEALAEEFMKKHPGvRVTVQGGGSGAGIKALIAGTADIAMASRPLkdEEKAAAEANGIELvEFVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502613375 102 G--GVVMAVNlPGITSGELTLdgETLGDIYLGKIKKWNDaaiaklnpgVKLPDQAIAVVRRADGSGTSFVFTSYLNKvna 179
Cdd:cd13566   81 AydGIAVIVN-PDNPVASLTL--EQLRDIFTGKITNWSE---------VGGPDEPIVVYGRDEGSGTRDYFEELVLG--- 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502613375 180 qwKSDVGAGSTVnwptglgGKGNDGVAAFVQRLPGAIGYVEYAYAKQNKLAytKLISSEGQAVSPTevsfsNAAKGAdws 259
Cdd:cd13566  146 --KGEFIRNAVV-------APSNGALVQAVAGDPNAIGYVGLGYVDENKKV--KALKVDGVAPTVE-----NIKSGK--- 206

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 502613375 260 asfaqdltnqpgdnvWPITSTTFILVHKESSKpkqtaEVLKFFDWAYSKGAKQA 313
Cdd:cd13566  207 ---------------YPLSRPLFLYTKGEPSP-----AVKAFIDFALSPEGQKI 240
PBP2_phosphate_like_2 cd13654
Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 ...
 38-228 1.54e-07

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: 51.87  E-value: 1.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502613375  38 APVYAKWADSYQKETGN-KVNYQGIGSSGGVKQIIANTVDFGASDAPL--SEEKLAADG---LFQFPTVIGGVVMAVNlP 111
Cdd:cd13654   13 YPITEAVAEEFGKSGPGvTVTVGSSGTGGGFKKFCAGETDISNASRPIkdSEAELCEANgieYIELPVAYDGLTVVVN-P 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502613375 112 GITS-GELTLDGETLGDIYLGKIKKWNDaaiakLNPGvkLPDQAIAVVRRADGSGTSFVFTSYLNKVNAQWKSDVGAGST 190
Cdd:cd13654   92 ANDWaKCLTELELKSIWAAESPITTWSD-----VRPS--WPDEPIELYGPGTDSGTFDYFTEAIVGEGGSIREDYTASED 164

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 502613375 191 VNwptglggkgndGVAAFVQRLPGAIGYVEYAYAKQNK 228
Cdd:cd13654  165 DN-----------VLVQGVAGDKNALGFFGYAYYEENG 191
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 49-312 2.52e-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: 51.65  E-value: 2.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502613375   49 QKETGNKVNYQGIGSSGGVKQIianTVDFGASDAP-----LSEEKLAADGLFQFPTVIGGVVMAVNLPG-ITSGELTLDG 122
Cdd:pfam01547  19 KEHPGIKVEVESVGSGSLAQKL---TTAIAAGDGPadvfaSDNDWIAELAKAGLLLPLDDYVANYLVLGvPKLYGVPLAA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502613375  123 ETLGDIY---------LGKIKKWNDAAIAKLNPGVKLPDqaIAVVRRADGSGTSFVFTSYLNKVNAQ--WKSDVGAGSTV 191
Cdd:pfam01547  96 ETLGLIYnkdlfkkagLDPPKTWDELLEAAKKLKEKGKS--PGGAGGGDASGTLGYFTLALLASLGGplFDKDGGGLDNP 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502613375  192 NWPTGLGGKGNDGVAAFVQRLPGAIGYVEYAYAKQNKLAYTK----LISSEGQAVSPTEVSFSNAAKGADWSASFAQDLT 267
Cdd:pfam01547 174 EAVDAITYYVDLYAKVLLLKKLKNPGVAGADGREALALFEQGkaamGIVGPWAALAANKVKLKVAFAAPAPDPKGDVGYA 253

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 502613375  268 NQPGDNVWPITSTTFILVHKEsskpKQTAEVLKFFDWAYSKGAKQ 312
Cdd:pfam01547 254 PLPAGKGGKGGGYGLAIPKGS----KNKEAAKKFLDFLTSPEAQA 294
Periplasmic_Binding_Protein_Type_2 cd00648
Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent ...
 29-234 8.32e-03

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: 37.17  E-value: 8.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502613375  29 LTGAGATFP--APVYAKWADSYQKETGNKVNYQGIGSSGGV-KQIIANTVDFGASDAPLSEE----KLAADGLFQFPTV- 100
Cdd:cd00648    2 LTVASIGPPpyAGFAEDAAKQLAKETGIKVELVPGSSIGTLiEALAAGDADVAVGPIAPALEaaadKLAPGGLYIVPELy 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502613375 101 IGGVVMAVNlpgitsgeltldgetlgdiylgkiKKWNdaaiaKLNPGVKLPDQAIAVVRRADGSGTSFVFTSYLnkvnaq 180
Cdd:cd00648   82 VGGYVLVVR------------------------KGSS-----IKGLLAVADLDGKRVGVGDPGSTAVRQARLAL------ 126

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 502613375 181 wksdVGAGSTVNWPTGLGGKGNDGVAAFVQRLPGAIGYVEYAYAKQNKLAYTKL 234
Cdd:cd00648  127 ----GAYGLKKKDPEVVPVPGTSGALAAVANGAVDAAIVWVPAAERAQLGNVQL 176
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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