NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1270473960|gb|PHS65579.1|]
View 

putative selenate ABC transporter substrate-binding protein [Thalassobium sp.]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
ABC_peri_selen super family cl30138
putative selenate ABC transporter periplasmic binding protein; Members of this family ABC ...
24-286 1.39e-147

putative selenate ABC transporter periplasmic binding protein; Members of this family ABC transporter periplasmic binding proteins and represent one clade within a larger family that includes phosphate, phosphite, and phosphonate transporters. All members of the seed alignment occur near a gene for SelD, the selenium-activating protein needed to make selenocysteine or selenouridine. Context therefore suggests members should be able to transport selenate, although transporting other substrates as well (e.g. phosphonates) is possible. This model has no overlap with TIGR03431, whose members are found regularly with phosphonate catabolism operons.


The actual alignment was detected with superfamily member TIGR04553:

Pssm-ID: 275346 [Multi-domain]  Cd Length: 266  Bit Score: 414.17  E-value: 1.39e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270473960  24 TFVFTAIPDEDESRLQQRFNKVADYLSAQTGAEVKYIPVKSYAAAITAFRNDQVQLAWFGGLSGVQARKLVAGSEAIAQG 103
Cdd:TIGR04553   1 VFVFTAIPDEDPTELQRRFAPLADYLEEELGVEVRFVPVTDYAAAVEAFRNNQVQLAWFGGLTGVQARVRVPGSVPLAQR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270473960 104 YEDQFFKTYFIANKSAGLSAEETLSaALKGKTFTFGSKGSTSGRLMPEFYLREQfNAAPEDIFSRVGFSGDHSRTIAQVQ 183
Cdd:TIGR04553  81 VEDEAFRSVFIAHESTILELADGLP-ELKGKTFTFGSKSSTSGRLMPRSFLLEA-GEAPDDDFKRVGYSGAHDATLALVE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270473960 184 SGAYQVGAVNYTVWDNELAAGNIDPEKIQVIWTTPTYPDYQWTIRGDVDARFGKGFKEKMRKALLEM-----KDKDLLAS 258
Cdd:TIGR04553 159 AGTYDAGALNISVWEKEVADGKVDTDKVRVIWTTPGYPDYNWTVRGDVDERFGEGFTDKVTQALLDLdpstaEDKEILEL 238
                         250       260
                  ....*....|....*....|....*...
gi 1270473960 259 FPRESFVPASNDDYAPIENTARAIGLLE 286
Cdd:TIGR04553 239 FRASRFIPTSNDNYAGIEAAAREAGLLD 266
 
Name Accession Description Interval E-value
ABC_peri_selen TIGR04553
putative selenate ABC transporter periplasmic binding protein; Members of this family ABC ...
24-286 1.39e-147

putative selenate ABC transporter periplasmic binding protein; Members of this family ABC transporter periplasmic binding proteins and represent one clade within a larger family that includes phosphate, phosphite, and phosphonate transporters. All members of the seed alignment occur near a gene for SelD, the selenium-activating protein needed to make selenocysteine or selenouridine. Context therefore suggests members should be able to transport selenate, although transporting other substrates as well (e.g. phosphonates) is possible. This model has no overlap with TIGR03431, whose members are found regularly with phosphonate catabolism operons.


Pssm-ID: 275346 [Multi-domain]  Cd Length: 266  Bit Score: 414.17  E-value: 1.39e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270473960  24 TFVFTAIPDEDESRLQQRFNKVADYLSAQTGAEVKYIPVKSYAAAITAFRNDQVQLAWFGGLSGVQARKLVAGSEAIAQG 103
Cdd:TIGR04553   1 VFVFTAIPDEDPTELQRRFAPLADYLEEELGVEVRFVPVTDYAAAVEAFRNNQVQLAWFGGLTGVQARVRVPGSVPLAQR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270473960 104 YEDQFFKTYFIANKSAGLSAEETLSaALKGKTFTFGSKGSTSGRLMPEFYLREQfNAAPEDIFSRVGFSGDHSRTIAQVQ 183
Cdd:TIGR04553  81 VEDEAFRSVFIAHESTILELADGLP-ELKGKTFTFGSKSSTSGRLMPRSFLLEA-GEAPDDDFKRVGYSGAHDATLALVE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270473960 184 SGAYQVGAVNYTVWDNELAAGNIDPEKIQVIWTTPTYPDYQWTIRGDVDARFGKGFKEKMRKALLEM-----KDKDLLAS 258
Cdd:TIGR04553 159 AGTYDAGALNISVWEKEVADGKVDTDKVRVIWTTPGYPDYNWTVRGDVDERFGEGFTDKVTQALLDLdpstaEDKEILEL 238
                         250       260
                  ....*....|....*....|....*...
gi 1270473960 259 FPRESFVPASNDDYAPIENTARAIGLLE 286
Cdd:TIGR04553 239 FRASRFIPTSNDNYAGIEAAAREAGLLD 266
PBP2_PnhD_2 cd13572
Substrate binding domain of uncharacterized ABC-type phosphonate-like transporter; contains ...
22-276 4.28e-111

Substrate binding domain of uncharacterized ABC-type phosphonate-like transporter; contains the type 2 periplasmic binding fold; This subfamily includes putative periplasmic binding component of an ABC transport system similar to alkylphosphonate binding domain PnhD. These domains are found in PnhD-like proteins that are predicted to function as initial receptors in hypophosphite, phosphonate, or phosphate ABC transport in archaea and eubacteria. They 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: 270290 [Multi-domain]  Cd Length: 249  Bit Score: 321.18  E-value: 4.28e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270473960  22 ADTFVFTAIPDEDESRLQQRFNKVADYLSAQTGAEVKYIPVKSYAAAITAFRNDQVQLAWFGGLSGVQARkLVAGSEAIA 101
Cdd:cd13572     3 PETLKVGAIPDENPTTLIRLNDPLADYLEKELGVEVELVVVTDYAAMVEAMRNGQLDLAYFGGLTYVQAR-LKPGAEPIA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270473960 102 QGY--EDQFFKTYFIANKSAGLSAEETlsaaLKGKTFTFGSKGSTSGRLMPEFYLREQFNaAPEDIFSRVGFSGDHSRTI 179
Cdd:cd13572    82 QLLrdGDPTFHSVFIANTDSGINSLAD----LKGKRFAFGDPASTSGHLMPRYFLLEAGV-LPDGDFYRVGFSGAHDATA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270473960 180 AQVQSGAYQVGAVNYTVWDNELAAGNIDPEKIQVIWTTPTYPDYQWTIRGDvdarFGKGFKEKMRKALLEMKDKDLLASF 259
Cdd:cd13572   157 LAVANGKVDAGALNEAIWESLVEEGKIDGEKVKVIWRTPPYPDYPWTVRPN----LGPELKEKVRNAFLSLDDPEVLDIF 232
                         250
                  ....*....|....*..
gi 1270473960 260 PRESFVPASNDDYAPIE 276
Cdd:cd13572   233 GASGFIPASDDDYDPIE 249
PhnD COG3221
ABC-type phosphate/phosphonate transport system, periplasmic component [Inorganic ion ...
29-283 2.40e-75

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


Pssm-ID: 442454 [Multi-domain]  Cd Length: 250  Bit Score: 230.19  E-value: 2.40e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270473960  29 AIPDEDESRLQQRFNKVADYLSAQTGAEVKYIPVKSYAAAITAFRNDQVQLAWFGGLSGVQARKLvAGSEAIAQGYED-- 106
Cdd:COG3221     1 VLPSESPADLLARWQPLADYLEEELGVPVELVPATDYAALIEALRAGQVDLAFLGPLPYVLARDR-AGAEPLATPVRDgs 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270473960 107 QFFKTYFIANKSAGLsaeETLsAALKGKTFTFGSKGSTSGRLMPEFYLREQfNAAPEDIFSRVGFSGDHSRTIAQVQSGA 186
Cdd:COG3221    80 PGYRSVIIVRADSPI---KSL-EDLKGKRFAFGDPDSTSGYLVPRALLAEA-GLDPERDFSEVVFSGSHDAVILAVANGQ 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270473960 187 YQVGAVNYTVWDNELAAGNiDPEKIQVIWTTPTYPDYQWTIRGDVDARfgkgFKEKMRKALLEM----KDKDLLASFPRE 262
Cdd:COG3221   155 ADAGAVDSGVLERLVEEGP-DADQLRVIWESPPIPNDPFVARPDLPPE----LREKIREALLSLdedpEGKAILEALGLE 229
                         250       260
                  ....*....|....*....|.
gi 1270473960 263 SFVPASNDDYAPIENTARAIG 283
Cdd:COG3221   230 GFVPADDADYDPIRELLKALG 250
Phosphonate-bd pfam12974
ABC transporter, phosphonate, periplasmic substrate-binding protein; This is a family of ...
27-272 2.59e-72

ABC transporter, phosphonate, periplasmic substrate-binding protein; This is a family of periplasmic proteins which are part of the transport system for alkylphosphonate uptake.


Pssm-ID: 432911 [Multi-domain]  Cd Length: 243  Bit Score: 222.52  E-value: 2.59e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270473960  27 FTAIPDEDESRLQQRFNKVADYLSAQTGAEVKYIPVKSYAAAITAFRNDQVQLAWFGGLSGVQARKLvAGSEAIAQGYE- 105
Cdd:pfam12974   1 FGVLPDESPDELKARYQPLADYLSEELGVPVELVVATDYAAVVEALRAGQVDIAYFGPLAYVQAVDR-AGAEPLATPVEp 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270473960 106 --DQFFKTYFIANKSAGLsaeETLsAALKGKTFTFGSKGSTSGRLMPEFYLREQFNAAPEDIFSRVgFSGDHSRTIAQVQ 183
Cdd:pfam12974  80 dgSAGYRSVIIVRKDSPI---QSL-EDLKGKTVAFGDPSSTSGYLVPLALLFAEAGLDPEDDFKPV-FSGSHDAVALAVL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270473960 184 SGAYQVGAVNYTVWDNELAAGNIDPEKIQVIWTTPTYPDYQWTIRGDVDARfgkgFKEKMRKALLEM----KDKDLLASF 259
Cdd:pfam12974 155 NGDADAGAVNSEVLERLVAEGPIDRDQLRVIAESPPIPNDPLVARPDLPPE----LKEKIRDALLALdetpEGRKVLEAL 230
                         250
                  ....*....|...
gi 1270473960 260 PRESFVPASNDDY 272
Cdd:pfam12974 231 GIDGFVPADDSDY 243
 
Name Accession Description Interval E-value
ABC_peri_selen TIGR04553
putative selenate ABC transporter periplasmic binding protein; Members of this family ABC ...
24-286 1.39e-147

putative selenate ABC transporter periplasmic binding protein; Members of this family ABC transporter periplasmic binding proteins and represent one clade within a larger family that includes phosphate, phosphite, and phosphonate transporters. All members of the seed alignment occur near a gene for SelD, the selenium-activating protein needed to make selenocysteine or selenouridine. Context therefore suggests members should be able to transport selenate, although transporting other substrates as well (e.g. phosphonates) is possible. This model has no overlap with TIGR03431, whose members are found regularly with phosphonate catabolism operons.


Pssm-ID: 275346 [Multi-domain]  Cd Length: 266  Bit Score: 414.17  E-value: 1.39e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270473960  24 TFVFTAIPDEDESRLQQRFNKVADYLSAQTGAEVKYIPVKSYAAAITAFRNDQVQLAWFGGLSGVQARKLVAGSEAIAQG 103
Cdd:TIGR04553   1 VFVFTAIPDEDPTELQRRFAPLADYLEEELGVEVRFVPVTDYAAAVEAFRNNQVQLAWFGGLTGVQARVRVPGSVPLAQR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270473960 104 YEDQFFKTYFIANKSAGLSAEETLSaALKGKTFTFGSKGSTSGRLMPEFYLREQfNAAPEDIFSRVGFSGDHSRTIAQVQ 183
Cdd:TIGR04553  81 VEDEAFRSVFIAHESTILELADGLP-ELKGKTFTFGSKSSTSGRLMPRSFLLEA-GEAPDDDFKRVGYSGAHDATLALVE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270473960 184 SGAYQVGAVNYTVWDNELAAGNIDPEKIQVIWTTPTYPDYQWTIRGDVDARFGKGFKEKMRKALLEM-----KDKDLLAS 258
Cdd:TIGR04553 159 AGTYDAGALNISVWEKEVADGKVDTDKVRVIWTTPGYPDYNWTVRGDVDERFGEGFTDKVTQALLDLdpstaEDKEILEL 238
                         250       260
                  ....*....|....*....|....*...
gi 1270473960 259 FPRESFVPASNDDYAPIENTARAIGLLE 286
Cdd:TIGR04553 239 FRASRFIPTSNDNYAGIEAAAREAGLLD 266
PBP2_PnhD_2 cd13572
Substrate binding domain of uncharacterized ABC-type phosphonate-like transporter; contains ...
22-276 4.28e-111

Substrate binding domain of uncharacterized ABC-type phosphonate-like transporter; contains the type 2 periplasmic binding fold; This subfamily includes putative periplasmic binding component of an ABC transport system similar to alkylphosphonate binding domain PnhD. These domains are found in PnhD-like proteins that are predicted to function as initial receptors in hypophosphite, phosphonate, or phosphate ABC transport in archaea and eubacteria. They 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: 270290 [Multi-domain]  Cd Length: 249  Bit Score: 321.18  E-value: 4.28e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270473960  22 ADTFVFTAIPDEDESRLQQRFNKVADYLSAQTGAEVKYIPVKSYAAAITAFRNDQVQLAWFGGLSGVQARkLVAGSEAIA 101
Cdd:cd13572     3 PETLKVGAIPDENPTTLIRLNDPLADYLEKELGVEVELVVVTDYAAMVEAMRNGQLDLAYFGGLTYVQAR-LKPGAEPIA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270473960 102 QGY--EDQFFKTYFIANKSAGLSAEETlsaaLKGKTFTFGSKGSTSGRLMPEFYLREQFNaAPEDIFSRVGFSGDHSRTI 179
Cdd:cd13572    82 QLLrdGDPTFHSVFIANTDSGINSLAD----LKGKRFAFGDPASTSGHLMPRYFLLEAGV-LPDGDFYRVGFSGAHDATA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270473960 180 AQVQSGAYQVGAVNYTVWDNELAAGNIDPEKIQVIWTTPTYPDYQWTIRGDvdarFGKGFKEKMRKALLEMKDKDLLASF 259
Cdd:cd13572   157 LAVANGKVDAGALNEAIWESLVEEGKIDGEKVKVIWRTPPYPDYPWTVRPN----LGPELKEKVRNAFLSLDDPEVLDIF 232
                         250
                  ....*....|....*..
gi 1270473960 260 PRESFVPASNDDYAPIE 276
Cdd:cd13572   233 GASGFIPASDDDYDPIE 249
PhnD COG3221
ABC-type phosphate/phosphonate transport system, periplasmic component [Inorganic ion ...
29-283 2.40e-75

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


Pssm-ID: 442454 [Multi-domain]  Cd Length: 250  Bit Score: 230.19  E-value: 2.40e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270473960  29 AIPDEDESRLQQRFNKVADYLSAQTGAEVKYIPVKSYAAAITAFRNDQVQLAWFGGLSGVQARKLvAGSEAIAQGYED-- 106
Cdd:COG3221     1 VLPSESPADLLARWQPLADYLEEELGVPVELVPATDYAALIEALRAGQVDLAFLGPLPYVLARDR-AGAEPLATPVRDgs 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270473960 107 QFFKTYFIANKSAGLsaeETLsAALKGKTFTFGSKGSTSGRLMPEFYLREQfNAAPEDIFSRVGFSGDHSRTIAQVQSGA 186
Cdd:COG3221    80 PGYRSVIIVRADSPI---KSL-EDLKGKRFAFGDPDSTSGYLVPRALLAEA-GLDPERDFSEVVFSGSHDAVILAVANGQ 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270473960 187 YQVGAVNYTVWDNELAAGNiDPEKIQVIWTTPTYPDYQWTIRGDVDARfgkgFKEKMRKALLEM----KDKDLLASFPRE 262
Cdd:COG3221   155 ADAGAVDSGVLERLVEEGP-DADQLRVIWESPPIPNDPFVARPDLPPE----LREKIREALLSLdedpEGKAILEALGLE 229
                         250       260
                  ....*....|....*....|.
gi 1270473960 263 SFVPASNDDYAPIENTARAIG 283
Cdd:COG3221   230 GFVPADDADYDPIRELLKALG 250
Phosphonate-bd pfam12974
ABC transporter, phosphonate, periplasmic substrate-binding protein; This is a family of ...
27-272 2.59e-72

ABC transporter, phosphonate, periplasmic substrate-binding protein; This is a family of periplasmic proteins which are part of the transport system for alkylphosphonate uptake.


Pssm-ID: 432911 [Multi-domain]  Cd Length: 243  Bit Score: 222.52  E-value: 2.59e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270473960  27 FTAIPDEDESRLQQRFNKVADYLSAQTGAEVKYIPVKSYAAAITAFRNDQVQLAWFGGLSGVQARKLvAGSEAIAQGYE- 105
Cdd:pfam12974   1 FGVLPDESPDELKARYQPLADYLSEELGVPVELVVATDYAAVVEALRAGQVDIAYFGPLAYVQAVDR-AGAEPLATPVEp 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270473960 106 --DQFFKTYFIANKSAGLsaeETLsAALKGKTFTFGSKGSTSGRLMPEFYLREQFNAAPEDIFSRVgFSGDHSRTIAQVQ 183
Cdd:pfam12974  80 dgSAGYRSVIIVRKDSPI---QSL-EDLKGKTVAFGDPSSTSGYLVPLALLFAEAGLDPEDDFKPV-FSGSHDAVALAVL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270473960 184 SGAYQVGAVNYTVWDNELAAGNIDPEKIQVIWTTPTYPDYQWTIRGDVDARfgkgFKEKMRKALLEM----KDKDLLASF 259
Cdd:pfam12974 155 NGDADAGAVNSEVLERLVAEGPIDRDQLRVIAESPPIPNDPLVARPDLPPE----LKEKIRDALLALdetpEGRKVLEAL 230
                         250
                  ....*....|...
gi 1270473960 260 PRESFVPASNDDY 272
Cdd:pfam12974 231 GIDGFVPADDSDY 243
PBP2_PhnD_like cd01071
Substrate binding domain of phosphonate uptake system-like, a member of the type 2 ...
22-276 2.34e-67

Substrate binding domain of phosphonate uptake system-like, a member of the type 2 periplasmic-binding fold superfamily; This family includes alkylphosphonate binding domain PhnD. These domains are found in PhnD-like proteins that are predicted to function as initial receptors in hypophosphite, phosphonate, or phosphate ABC transport in archaea and eubacteria. PhnD is the periplasmic binding component of an ABC-type phosphonate uptake system (PhnCDE) that recognizes and binds phosphonate. PhnD belongs 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. The PBP2 have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270232 [Multi-domain]  Cd Length: 253  Bit Score: 210.20  E-value: 2.34e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270473960  22 ADTFVFTAIPDEDESRLQQRFNKVADYLSAQTGAEVKYIPVKSYAAAITAFRNDQVQLAWFGGLSGVQARKlVAGSEAIA 101
Cdd:cd01071     3 PKELRFGLVPAEDADELKKEFEPLADYLEEELGVPVELVVATSYAAVVEAMRNGKVDIAWLGPASYVLAHD-RAGAEALA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270473960 102 Q--GYEDQFFKTYFIANKSAGLsaeETLsAALKGKTFTFGSKGSTSGRLMPEFYLREQFNaAPEDIFSRVGFSGDHSRTI 179
Cdd:cd01071    82 TevRDGSPGYYSVIIVRKDSPI---KSL-EDLKGKTVAFVDPSSTSGYLFPRAMLKDAGI-DPPDFFFEVVFAGSHDSAL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270473960 180 AQVQSGAYQVGAVNYTVWDNELAAGNIDPEKIQVIWTTPTYPDYQWTIRGDVDArfgkGFKEKMRKALLEMKDKD----L 255
Cdd:cd01071   157 LAVANGDVDAAATYDSTLERAAAAGPIDPDDLRVIWRSPPIPNDPLVVRKDLPP----ALKAKIRDALLDLDETDegqkL 232
                         250       260
                  ....*....|....*....|.
gi 1270473960 256 LASFPRESFVPASNDDYAPIE 276
Cdd:cd01071   233 LAGLGLTGFVPATDDDYDPIR 253
3A0109s03R TIGR01098
phosphate/phosphite/phosphonate ABC transporter, periplasmic binding protein; Phosphonates are ...
23-250 3.49e-53

phosphate/phosphite/phosphonate ABC transporter, periplasmic binding protein; Phosphonates are a varied class of phosphorus-containing organic compound in which a direct C-P bond is found, rather than a C-O-P linkage of the phosphorus through an oxygen atom. They may be toxic but also may be used as sources of phosphorus and energy by various bacteria. Phosphonate utilization systems typically are encoded in 14 or more genes, including a three gene ABC transporter. This family includes the periplasmic binding protein component of ABC transporters for phosphonates as well as other, related binding components for closely related substances such as phosphate and phosphite. A number of members of this family are found in genomic contexts with components of selenium metabolic processes suggestive of a role in selenate or other selenium-compound transport. A subset of this model in which nearly all members exhibit genomic context with elements of phosphonate metabolism, particularly the C-P lyase system (GenProp0232) has been built (TIGR03431) as an equivalog. Nevertheless, there are members of this subfamily (TIGR01098) which show up sporadically on a phylogenetic tree that also show phosphonate context and are most likely competent to transport phosphonates. [Transport and binding proteins, Anions]


Pssm-ID: 273442 [Multi-domain]  Cd Length: 254  Bit Score: 173.69  E-value: 3.49e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270473960  23 DTFVFTAIPDEDESRLQQRFNKVADYLSAQTGAEVKYIPVKSYAAAITAFRNDQVQLAWFGGLSGVQARKLvAGSEAIA- 101
Cdd:TIGR01098  32 KELNFGILPGENASNLTRRWEPLADYLEKKLGIKVQLFVATDYSAVIEAMRFGRVDIAWFGPSSYVLAHYR-ANAEVFAl 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270473960 102 ---QGYEDQFFKTYFIANKSAGLSAEEtlsaALKGKTFTFGSKGSTSGRLMPEFYLREQFNAAPEDIFSRVGFSGDHSRT 178
Cdd:TIGR01098 111 tavSTDGSPGYYSVIIVKADSPIKSLK----DLKGKTFAFGDPASTSGYLVPRYQLKKEGGLDADGFFSEVVFSGSHDAS 186
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1270473960 179 IAQVQSGAYQVGAVNYTVWDNELAAGNIDPEKIQVIWTTPTYPDYQWTIRGDVDarfgKGFKEKMRKALLEM 250
Cdd:TIGR01098 187 ALAVANGKVDAATNNSSAIGRLKKRGPSDMKKVRVIWKSPLIPNDPIAVRKDLP----PELKEKIRDAFLTL 254
PhnD TIGR03431
phosphonate ABC transporter, periplasmic phosphonate binding protein; This model is a subset ...
19-283 1.87e-44

phosphonate ABC transporter, periplasmic phosphonate binding protein; This model is a subset of the broader subfamily of phosphate/phosphonate binding protein ABC transporter components, TIGR01098. In this model all members of the seed have support from genomic context for association with pathways for the metabolims of phosphonates, particularly the C-P lyase system, GenProp0232. This model includes the characterized phnD gene from E. coli. Note that this model does not identify all phnD-subfamily genes with evident phosphonate context, but all sequences above the trusted context may be inferred to bind phosphonate compounds even in the absence of such context. Furthermore, there is ample evidence to suggest that many other members of the TIGR01098 subfamily have a different primary function.


Pssm-ID: 132472 [Multi-domain]  Cd Length: 288  Bit Score: 152.12  E-value: 1.87e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270473960  19 SAFAD----TFVFTAIPDEDESRLQQRFNKVADYLSAQTGAEVKYIPVKSYAAAITAFRNDQVQLAWFGGLSGVQARKlV 94
Cdd:TIGR03431  19 NAQAEdwpkELNFGIIPTENASDLKQRWEPLADYLSKKLGVKVKLFFATDYAGVIEGMRFGKVDIAWYGPSSYAEAYQ-K 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270473960  95 AGSEAIAQG-YEDQFFKTY--FIANKSAGLSAEETLsaalKGKTFTFGSKGSTSGRLMPEFYLREQFNAAPEDIFSRVGF 171
Cdd:TIGR03431  98 ANAEAFAIEvNADGSTGYYsvLIVKKDSPIKSLEDL----KGKTFGFVDPNSTSGFLVPSYYLFKKNGIKPKEYFKKVTF 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270473960 172 SGDHSRTIAQVQSGAYQVGAVNYTVWDNELAAGNID-PEKIQVIWTTPTYPDYQWTIRGDVDARfgkgFKEKMRKALLEM 250
Cdd:TIGR03431 174 SGSHEAAILAVANGTVDAATTNDENLDRMIRKGQPDaMEDLRIIWKSPLIPNGPIVYRKDLPAD----LKAKIRKAFLNY 249
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1270473960 251 KDKD-----LLASFPRESFVPASNDDYAPIENTARAIG 283
Cdd:TIGR03431 250 HKTDkacfeKIAGGDLKGFVAASDKDYDPIRDLKKAKI 287
PBP2_PnhD_1 cd13571
Substrate binding domain of uncharacterized ABC-type phosphonate-like transporter; contains ...
30-275 4.85e-39

Substrate binding domain of uncharacterized ABC-type phosphonate-like transporter; contains the type 2 periplasmic binding fold; This subfamily includes putative periplasmic binding components of an ABC transport system similar to alkylphosphonate binding domain PnhD. These domains are found in PnhD-like proteins that are predicted to function as initial receptors in hypophosphite, phosphonate, or phosphate ABC transport in archaea and eubacteria. They 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: 270289 [Multi-domain]  Cd Length: 253  Bit Score: 137.00  E-value: 4.85e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270473960  30 IPDEDESRLQQRFNKVADYLSAQTGAEVKYIPVKSYAAAITAFRNDQVQLAWFGGLSGVQARKlVAGSEAIA--QGYEDQ 107
Cdd:cd13571    11 ASVLSPRETLALYDPLAEYLERKLGRPVEFVQRRTYAEINELLKNGKVDLAFVCSGAYVQARD-KAGLELLAvpEINGQP 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270473960 108 FFKTYFIANKSAGLSAEEtlsaALKGKTFTFGSKGSTSGRLMPEFYLREQFnAAPEDIFSRVGFSGDHSRTIAQVQSGAY 187
Cdd:cd13571    90 TYRSYIIVPADSPAKSLE----DLKGKRFAFTDPLSNSGFLVPMYLLAELG-LDPERFFSRVFFTGSHDKSIQAVANGLV 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270473960 188 QVGAVNYTVWDNELAAGNIDPEKIQVIWTTPTYPDYQWTIRGDVDarfgKGFKEKMRKALLEM----KDKDLLASFPRES 263
Cdd:cd13571   165 DGAAVDSLVYEYAVEKGPELAANVRIIWRSEPIGNPPVVARPGLD----PELKAALQEAFLSMhedpEGRAALEGLGIDR 240
                         250
                  ....*....|..
gi 1270473960 264 FVPASNDDYAPI 275
Cdd:cd13571   241 FVPADDSLYDPI 252
PBP2_PnhD cd13575
Substrate binding domain of ABC-type phosphonate uptake system; contains the type 2 ...
27-275 6.57e-28

Substrate binding domain of ABC-type phosphonate uptake system; contains the type 2 periplasmic binding fold; This subfamily includes the Escherichia coli PhnD (EcPhnD) which exhibits high affinity for the environmentally abundant 2-aminoethylphosphonate (2-AEP), a precursor in the biosynthesis of phosphonolipids, phosphonoproteins, and phosphonoglycans. The Escherichia coli phn operon encodes 14 genes involved in binding, uptake and metabolism of phosphonate, and is activated under phophophate-limiting conditions. PhnD belongs 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. The PBP2 have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. PhnD is the periplasmic binding component of an ABC-type phosphonate uptake system (PhnCDE) that recognizes and binds phosphonate.


Pssm-ID: 270293 [Multi-domain]  Cd Length: 259  Bit Score: 107.94  E-value: 6.57e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270473960  27 FTAIPDEDESRLQQRFNKVADYLSAQTGAEVKYIPVKSYAAAITAFRNDQVQLAWFGGLSGVQARKLvAGSEAIAQ---- 102
Cdd:cd13575     8 FGIISTESQQNLRAQWEPFLAAMEKKLGVKVNAFFAPDYAGIIEGMRFNKVQIAWYGNKSAMEAVDR-ANGEVFAQtvaa 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270473960 103 ----GYedqffKTYFIANK-SAGLSAEETLSAAlKGKTFTFGSKGSTSGRLMPEFYLREQFNAAPEDIFSRVgFSGDHSR 177
Cdd:cd13575    87 dgspGY-----YSHLIVNKdSPINSLNDVLAKA-KDLTFGNGDPNSTSGFLVPGYYVFAKNGIDPKKFFKRT-VNANHET 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270473960 178 TIAQVQSGAYQVGAVNYTVWDNelaAGNIDPEK---IQVIWTTPTYPDYQWTIRGDVDarfgKGFKEKMRKALLEMKD-- 252
Cdd:cd13575   160 NALAVANKQVDVATNNTENLDR---LKERAPEKlkqLRIIWTSPLIPGDPLVWRKDLP----EAVKKKIADFFFGYGQta 232
                         250       260
                  ....*....|....*....|....*.
gi 1270473960 253 ---KDLLASFPRESFVPASNDDYAPI 275
Cdd:cd13575   233 eekSVLKERLDWSPFKPSSDGQLVPI 258
PBP2_PnhD_3 cd13573
Substrate binding domain of uncharacterized ABC-type phosphonate-like transporter; contains ...
23-275 5.06e-26

Substrate binding domain of uncharacterized ABC-type phosphonate-like transporter; contains the type 2 periplasmic binding fold; This subfamily includes putative periplasmic binding component of an ABC transport system similar to alkylphosphonate binding domain PnhD. These domains are found in PnhD-like proteins that are predicted to function as initial receptors in hypophosphite, phosphonate, or phosphate ABC transport in archaea and eubacteria. They 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: 270291 [Multi-domain]  Cd Length: 253  Bit Score: 102.94  E-value: 5.06e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270473960  23 DTFVFTAIPDEDESRLQQRFNKVADYLSAQTGAEVKYIPVKSYAAAITAFRNDQVQLAWFGglSGVQARKL-VAGSEAIA 101
Cdd:cd13573     4 DTLVFAYTPVEDPAVYQEIWAPFIAHISKVTGKDVQFYPVQSNAAQTEAMRSGRLHIAGFS--TGPTPFAVnLAGAVPFA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270473960 102 -QGYEDQFF--KTYFIANKSAGLsaeETLSaALKGKTFTFGSKGSTSGRLMPEFYLREQFNAAPEDIFsRVGFSGDHSRT 178
Cdd:cd13573    82 vKGYEDGSFgyELEVITRIDSGI---QKVK-DLKGRKVAHTSPTSNSGHLAPRALFPAQGGIVPDKDY-EVTFSGKHDQS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270473960 179 IAQVQSGAYQVGAVNYTVWDNELAAGNIDPEKIQVIWTTPTYPDYQWTIRGDVDARfgkgFKEKMRKALL--EMKDKDLL 256
Cdd:cd13573   157 ILGVFNGDYDAAPVASDVLERMAERGQVKEEQFRVIYKSFAFPTGPFGYAHNLKPE----LREKIKEAFFtyDFAGTKLA 232
                         250       260
                  ....*....|....*....|.
gi 1270473960 257 ASFPR-ESFVPAS-NDDYAPI 275
Cdd:cd13573   233 EIFAGfDRFAPITyKEHWAVI 253
PBP2_PnhD_4 cd13574
Substrate binding domain of uncharacterized ABC-type phosphonate-like transporter; contains ...
26-275 2.76e-24

Substrate binding domain of uncharacterized ABC-type phosphonate-like transporter; contains the type 2 periplasmic binding fold; This subfamily includes putative periplasmic binding component of an ABC transport system similar to alkylphosphonate binding domain PnhD. These domains are found in PnhD-like proteins that are predicted to function as initial receptors in hypophosphite, phosphonate, or phosphate ABC transport in archaea and eubacteria. They 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: 270292 [Multi-domain]  Cd Length: 250  Bit Score: 98.15  E-value: 2.76e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270473960  26 VFTAIPDEDESRLQQRFNKVADYLSAQTGAEVKYIPVKSYAAAITAFRNDQVQLAWFGGLSGVQARKLVAGSEAIAQGYE 105
Cdd:cd13574     7 RFGVHPYLSPTELVKRFQPLLDYLEEELGRPVEIKVSKDYQEHVDRLGSGKIDIAYLGPAPYVQAKDRRYGIKPLLALLE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270473960 106 DQ---FFKTYFIANKSaglSAEETLsAALKGKTFTFGSKGSTSGRLMPEFYLREQfNAAPEDiFSRVGFSGDHSRTIAQV 182
Cdd:cd13574    87 TDgkpTYNGVIVVRAD---SPIKSL-ADLAGKSFAFGDPLSTMGHLVPRAMLRQA-GITSLD-LAGYDYLGRHDNVALAV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270473960 183 QSGAYQVGAVNYTVWDNELAAGnidpekIQVIWTTPTYPDYQWTIRGDVDARfgkgFKEKMRKALLEMKD--KDLLASFP 260
Cdd:cd13574   161 LAGEFDAGALKEEVYRKYKGRG------LRVLATSPPLPGHALVARATLPEE----LVKALRRALLELDStgAGLAILTW 230
                         250
                  ....*....|....*....
gi 1270473960 261 RES----FVPASNDDYAPI 275
Cdd:cd13574   231 IEElrhgFVPVTDEDYDLL 249
 
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