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Conserved domains on  [gi|1621110282]
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Chain A, Probable phosphite transport system-binding protein HtxB

Protein Classification

phosphate/phosphite/phosphonate ABC transporter substrate-binding protein( domain architecture ID 10099495)

phosphate/phosphite/phosphonate ABC transporter substrate-binding protein functions as the initial receptor in the ABC transport of phosphate, phosphite, and/or phosphonate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PBP2_PhnD_like cd01071
Substrate binding domain of phosphonate uptake system-like, a member of the type 2 ...
10-257 9.40e-89

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: 264.12  E-value: 9.40e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621110282  10 HLRFAIAPMRPtPSQTIKEFEPIFKYLADQLGATYEIVSPESWAAISVAMTNGHVDVGWLGPWGYVLSNKKAGTEVLATV 89
Cdd:cd01071     5 ELRFGLVPAED-ADELKKEFEPLADYLEEELGVPVELVVATSYAAVVEAMRNGKVDIAWLGPASYVLAHDRAGAEALATE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621110282  90 KYRGEPFYKALIVGRADLPIkKWPEDAKGLKLSLSDQGNTSGWLIPMAYFKSIGIDPASYF-EYREGATFGQNESQIQHG 168
Cdd:cd01071    84 VRDGSPGYYSVIIVRKDSPI-KSLEDLKGKTVAFVDPSSTSGYLFPRAMLKDAGIDPPDFFfEVVFAGSHDSALLAVANG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621110282 169 LIDLGSDMDRGRNGMIEAGQIDPSKSKIVWESSKLPNDAISVPKDFDPALKARITEILTSLSEEKAQSLM--GSGYNGFV 246
Cdd:cd01071   163 DVDAAATYDSTLERAAAAGPIDPDDLRVIWRSPPIPNDPLVVRKDLPPALKAKIRDALLDLDETDEGQKLlaGLGLTGFV 242
                         250
                  ....*....|.
gi 1621110282 247 KAKHSDYKVIE 257
Cdd:cd01071   243 PATDDDYDPIR 253
 
Name Accession Description Interval E-value
PBP2_PhnD_like cd01071
Substrate binding domain of phosphonate uptake system-like, a member of the type 2 ...
10-257 9.40e-89

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: 264.12  E-value: 9.40e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621110282  10 HLRFAIAPMRPtPSQTIKEFEPIFKYLADQLGATYEIVSPESWAAISVAMTNGHVDVGWLGPWGYVLSNKKAGTEVLATV 89
Cdd:cd01071     5 ELRFGLVPAED-ADELKKEFEPLADYLEEELGVPVELVVATSYAAVVEAMRNGKVDIAWLGPASYVLAHDRAGAEALATE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621110282  90 KYRGEPFYKALIVGRADLPIkKWPEDAKGLKLSLSDQGNTSGWLIPMAYFKSIGIDPASYF-EYREGATFGQNESQIQHG 168
Cdd:cd01071    84 VRDGSPGYYSVIIVRKDSPI-KSLEDLKGKTVAFVDPSSTSGYLFPRAMLKDAGIDPPDFFfEVVFAGSHDSALLAVANG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621110282 169 LIDLGSDMDRGRNGMIEAGQIDPSKSKIVWESSKLPNDAISVPKDFDPALKARITEILTSLSEEKAQSLM--GSGYNGFV 246
Cdd:cd01071   163 DVDAAATYDSTLERAAAAGPIDPDDLRVIWRSPPIPNDPLVVRKDLPPALKAKIRDALLDLDETDEGQKLlaGLGLTGFV 242
                         250
                  ....*....|.
gi 1621110282 247 KAKHSDYKVIE 257
Cdd:cd01071   243 PATDDDYDPIR 253
PhnD COG3221
ABC-type phosphate/phosphonate transport system, periplasmic component [Inorganic ion ...
21-264 4.69e-58

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


Pssm-ID: 442454 [Multi-domain]  Cd Length: 250  Bit Score: 185.51  E-value: 4.69e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621110282  21 TPSQTIKEFEPIFKYLADQLGATYEIVSPESWAAISVAMTNGHVDVGWLGPWGYVLSNKKAGTEVLATVKYRGEPFYKAL 100
Cdd:COG3221     6 SPADLLARWQPLADYLEEELGVPVELVPATDYAALIEALRAGQVDLAFLGPLPYVLARDRAGAEPLATPVRDGSPGYRSV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621110282 101 IVGRADLPIKKwPEDAKGLKLSLSDQGNTSGWLIPMAYFKSIGIDPASYF-EYREGATFGQNESQIQHGLIDLGSDMDRG 179
Cdd:COG3221    86 IIVRADSPIKS-LEDLKGKRFAFGDPDSTSGYLVPRALLAEAGLDPERDFsEVVFSGSHDAVILAVANGQADAGAVDSGV 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621110282 180 RNGMIEAGQiDPSKSKIVWESSKLPNDAISVPKDFDPALKARITEILTSLSEEKAQS--LMGSGYNGFVKAKHSDYKVIE 257
Cdd:COG3221   165 LERLVEEGP-DADQLRVIWESPPIPNDPFVARPDLPPELREKIREALLSLDEDPEGKaiLEALGLEGFVPADDADYDPIR 243

                  ....*..
gi 1621110282 258 DAGRILG 264
Cdd:COG3221   244 ELLKALG 250
Phosphonate-bd pfam12974
ABC transporter, phosphonate, periplasmic substrate-binding protein; This is a family of ...
13-253 4.80e-50

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: 164.74  E-value: 4.80e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621110282  13 FAIAPMRpTPSQTIKEFEPIFKYLADQLGATYEIVSPESWAAISVAMTNGHVDVGWLGPWGYVLSNKKAGTEVLAT-VKY 91
Cdd:pfam12974   1 FGVLPDE-SPDELKARYQPLADYLSEELGVPVELVVATDYAAVVEALRAGQVDIAYFGPLAYVQAVDRAGAEPLATpVEP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621110282  92 RGEPFYKALIVGRADLPIKKWpEDAKGLKLSLSDQGNTSGWLIPMAY-FKSIGIDPASYFEYREGATFGQNESQIQHGLI 170
Cdd:pfam12974  80 DGSAGYRSVIIVRKDSPIQSL-EDLKGKTVAFGDPSSTSGYLVPLALlFAEAGLDPEDDFKPVFSGSHDAVALAVLNGDA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621110282 171 DLGSDMDRGRNGMIEAGQIDPSKSKIVWESSKLPNDAISVPKDFDPALKARITEILTSLSEEKAQSLM--GSGYNGFVKA 248
Cdd:pfam12974 159 DAGAVNSEVLERLVAEGPIDRDQLRVIAESPPIPNDPLVARPDLPPELKEKIRDALLALDETPEGRKVleALGIDGFVPA 238

                  ....*
gi 1621110282 249 KHSDY 253
Cdd:pfam12974 239 DDSDY 243
PhnD TIGR03431
phosphonate ABC transporter, periplasmic phosphonate binding protein; This model is a subset ...
11-265 6.82e-40

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: 139.80  E-value: 6.82e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621110282  11 LRFAIAPMRpTPSQTIKEFEPIFKYLADQLGATYEIVSPESWAAISVAMTNGHVDVGWLGPWGYVLSNKKAGTEVLATVK 90
Cdd:TIGR03431  29 LNFGIIPTE-NASDLKQRWEPLADYLSKKLGVKVKLFFATDYAGVIEGMRFGKVDIAWYGPSSYAEAYQKANAEAFAIEV 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621110282  91 Y-RGEPFYKALIVGRADLPIKKWpEDAKGLKLSLSDQGNTSGWLIPMAYF-KSIGIDPASYF-EYREGATFGQNESQIQH 167
Cdd:TIGR03431 108 NaDGSTGYYSVLIVKKDSPIKSL-EDLKGKTFGFVDPNSTSGFLVPSYYLfKKNGIKPKEYFkKVTFSGSHEAAILAVAN 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621110282 168 GLIDLGSDMDRGRNGMIEAGQIDPSKS-KIVWESSKLPNDAISVPKDFDPALKARITEILTSLSEEKAQSLMGSGY---N 243
Cdd:TIGR03431 187 GTVDAATTNDENLDRMIRKGQPDAMEDlRIIWKSPLIPNGPIVYRKDLPADLKAKIRKAFLNYHKTDKACFEKIAGgdlK 266
                         250       260
                  ....*....|....*....|..
gi 1621110282 244 GFVKAKHSDYKVIEDAGRILGK 265
Cdd:TIGR03431 267 GFVAASDKDYDPIRDLKKAKIK 288
 
Name Accession Description Interval E-value
PBP2_PhnD_like cd01071
Substrate binding domain of phosphonate uptake system-like, a member of the type 2 ...
10-257 9.40e-89

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: 264.12  E-value: 9.40e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621110282  10 HLRFAIAPMRPtPSQTIKEFEPIFKYLADQLGATYEIVSPESWAAISVAMTNGHVDVGWLGPWGYVLSNKKAGTEVLATV 89
Cdd:cd01071     5 ELRFGLVPAED-ADELKKEFEPLADYLEEELGVPVELVVATSYAAVVEAMRNGKVDIAWLGPASYVLAHDRAGAEALATE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621110282  90 KYRGEPFYKALIVGRADLPIkKWPEDAKGLKLSLSDQGNTSGWLIPMAYFKSIGIDPASYF-EYREGATFGQNESQIQHG 168
Cdd:cd01071    84 VRDGSPGYYSVIIVRKDSPI-KSLEDLKGKTVAFVDPSSTSGYLFPRAMLKDAGIDPPDFFfEVVFAGSHDSALLAVANG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621110282 169 LIDLGSDMDRGRNGMIEAGQIDPSKSKIVWESSKLPNDAISVPKDFDPALKARITEILTSLSEEKAQSLM--GSGYNGFV 246
Cdd:cd01071   163 DVDAAATYDSTLERAAAAGPIDPDDLRVIWRSPPIPNDPLVVRKDLPPALKAKIRDALLDLDETDEGQKLlaGLGLTGFV 242
                         250
                  ....*....|.
gi 1621110282 247 KAKHSDYKVIE 257
Cdd:cd01071   243 PATDDDYDPIR 253
PhnD COG3221
ABC-type phosphate/phosphonate transport system, periplasmic component [Inorganic ion ...
21-264 4.69e-58

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


Pssm-ID: 442454 [Multi-domain]  Cd Length: 250  Bit Score: 185.51  E-value: 4.69e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621110282  21 TPSQTIKEFEPIFKYLADQLGATYEIVSPESWAAISVAMTNGHVDVGWLGPWGYVLSNKKAGTEVLATVKYRGEPFYKAL 100
Cdd:COG3221     6 SPADLLARWQPLADYLEEELGVPVELVPATDYAALIEALRAGQVDLAFLGPLPYVLARDRAGAEPLATPVRDGSPGYRSV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621110282 101 IVGRADLPIKKwPEDAKGLKLSLSDQGNTSGWLIPMAYFKSIGIDPASYF-EYREGATFGQNESQIQHGLIDLGSDMDRG 179
Cdd:COG3221    86 IIVRADSPIKS-LEDLKGKRFAFGDPDSTSGYLVPRALLAEAGLDPERDFsEVVFSGSHDAVILAVANGQADAGAVDSGV 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621110282 180 RNGMIEAGQiDPSKSKIVWESSKLPNDAISVPKDFDPALKARITEILTSLSEEKAQS--LMGSGYNGFVKAKHSDYKVIE 257
Cdd:COG3221   165 LERLVEEGP-DADQLRVIWESPPIPNDPFVARPDLPPELREKIREALLSLDEDPEGKaiLEALGLEGFVPADDADYDPIR 243

                  ....*..
gi 1621110282 258 DAGRILG 264
Cdd:COG3221   244 ELLKALG 250
Phosphonate-bd pfam12974
ABC transporter, phosphonate, periplasmic substrate-binding protein; This is a family of ...
13-253 4.80e-50

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: 164.74  E-value: 4.80e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621110282  13 FAIAPMRpTPSQTIKEFEPIFKYLADQLGATYEIVSPESWAAISVAMTNGHVDVGWLGPWGYVLSNKKAGTEVLAT-VKY 91
Cdd:pfam12974   1 FGVLPDE-SPDELKARYQPLADYLSEELGVPVELVVATDYAAVVEALRAGQVDIAYFGPLAYVQAVDRAGAEPLATpVEP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621110282  92 RGEPFYKALIVGRADLPIKKWpEDAKGLKLSLSDQGNTSGWLIPMAY-FKSIGIDPASYFEYREGATFGQNESQIQHGLI 170
Cdd:pfam12974  80 DGSAGYRSVIIVRKDSPIQSL-EDLKGKTVAFGDPSSTSGYLVPLALlFAEAGLDPEDDFKPVFSGSHDAVALAVLNGDA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621110282 171 DLGSDMDRGRNGMIEAGQIDPSKSKIVWESSKLPNDAISVPKDFDPALKARITEILTSLSEEKAQSLM--GSGYNGFVKA 248
Cdd:pfam12974 159 DAGAVNSEVLERLVAEGPIDRDQLRVIAESPPIPNDPLVARPDLPPELKEKIRDALLALDETPEGRKVleALGIDGFVPA 238

                  ....*
gi 1621110282 249 KHSDY 253
Cdd:pfam12974 239 DDSDY 243
PBP2_PnhD_1 cd13571
Substrate binding domain of uncharacterized ABC-type phosphonate-like transporter; contains ...
11-253 3.37e-48

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: 160.50  E-value: 3.37e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621110282  11 LRFAIAPMrPTPSQTIKEFEPIFKYLADQLGATYEIVSPESWAAISVAMTNGHVDVGWLGPWGYVLSNKKAGTEVLATVK 90
Cdd:cd13571     6 LRIGLASV-LSPRETLALYDPLAEYLERKLGRPVEFVQRRTYAEINELLKNGKVDLAFVCSGAYVQARDKAGLELLAVPE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621110282  91 YRGEPFYKALIVGRADLPIKKWpEDAKGLKLSLSDQGNTSGWLIPMAYFKSIGIDPASYFEYregATFGQN-ESQIQ--- 166
Cdd:cd13571    85 INGQPTYRSYIIVPADSPAKSL-EDLKGKRFAFTDPLSNSGFLVPMYLLAELGLDPERFFSR---VFFTGShDKSIQava 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621110282 167 HGLIDLGSDMDRGRNGMIEAGQIDPSKSKIVWESSKLPNDAISVPKDFDPALKARITEILTSL--SEEKAQSLMGSGYNG 244
Cdd:cd13571   161 NGLVDGAAVDSLVYEYAVEKGPELAANVRIIWRSEPIGNPPVVARPGLDPELKAALQEAFLSMheDPEGRAALEGLGIDR 240

                  ....*....
gi 1621110282 245 FVKAKHSDY 253
Cdd:cd13571   241 FVPADDSLY 249
PBP2_PnhD_2 cd13572
Substrate binding domain of uncharacterized ABC-type phosphonate-like transporter; contains ...
11-257 7.42e-41

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: 141.30  E-value: 7.42e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621110282  11 LRFAIAPMRpTPSQTIKEFEPIFKYLADQLGATYEIVSPESWAAISVAMTNGHVDVGWLGPWGYVLSNKKAGTEVLATVK 90
Cdd:cd13572     6 LKVGAIPDE-NPTTLIRLNDPLADYLEKELGVEVELVVVTDYAAMVEAMRNGQLDLAYFGGLTYVQARLKPGAEPIAQLL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621110282  91 YRGEPFYKALIVGRADLPIKKwPEDAKGLKLSLSDQGNTSGWLIPMAYFKSIGIDPASYFeYREGATfGQNESQI---QH 167
Cdd:cd13572    85 RDGDPTFHSVFIANTDSGINS-LADLKGKRFAFGDPASTSGHLMPRYFLLEAGVLPDGDF-YRVGFS-GAHDATAlavAN 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621110282 168 GLIDLGSDMDRGRNGMIEAGQIDPSKSKIVWESSKLPNDAISVPKDFDPALKARITEILTSLSEEKAQSLMGSgyNGFVK 247
Cdd:cd13572   162 GKVDAGALNEAIWESLVEEGKIDGEKVKVIWRTPPYPDYPWTVRPNLGPELKEKVRNAFLSLDDPEVLDIFGA--SGFIP 239
                         250
                  ....*....|
gi 1621110282 248 AKHSDYKVIE 257
Cdd:cd13572   240 ASDDDYDPIE 249
PhnD TIGR03431
phosphonate ABC transporter, periplasmic phosphonate binding protein; This model is a subset ...
11-265 6.82e-40

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: 139.80  E-value: 6.82e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621110282  11 LRFAIAPMRpTPSQTIKEFEPIFKYLADQLGATYEIVSPESWAAISVAMTNGHVDVGWLGPWGYVLSNKKAGTEVLATVK 90
Cdd:TIGR03431  29 LNFGIIPTE-NASDLKQRWEPLADYLSKKLGVKVKLFFATDYAGVIEGMRFGKVDIAWYGPSSYAEAYQKANAEAFAIEV 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621110282  91 Y-RGEPFYKALIVGRADLPIKKWpEDAKGLKLSLSDQGNTSGWLIPMAYF-KSIGIDPASYF-EYREGATFGQNESQIQH 167
Cdd:TIGR03431 108 NaDGSTGYYSVLIVKKDSPIKSL-EDLKGKTFGFVDPNSTSGFLVPSYYLfKKNGIKPKEYFkKVTFSGSHEAAILAVAN 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621110282 168 GLIDLGSDMDRGRNGMIEAGQIDPSKS-KIVWESSKLPNDAISVPKDFDPALKARITEILTSLSEEKAQSLMGSGY---N 243
Cdd:TIGR03431 187 GTVDAATTNDENLDRMIRKGQPDAMEDlRIIWKSPLIPNGPIVYRKDLPADLKAKIRKAFLNYHKTDKACFEKIAGgdlK 266
                         250       260
                  ....*....|....*....|..
gi 1621110282 244 GFVKAKHSDYKVIEDAGRILGK 265
Cdd:TIGR03431 267 GFVAASDKDYDPIRDLKKAKIK 288
3A0109s03R TIGR01098
phosphate/phosphite/phosphonate ABC transporter, periplasmic binding protein; Phosphonates are ...
11-229 4.11e-39

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: 137.10  E-value: 4.11e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621110282  11 LRFAIAPMRpTPSQTIKEFEPIFKYLADQLGATYEIVSPESWAAISVAMTNGHVDVGWLGPWGYVLSNKKAGTEVLA--T 88
Cdd:TIGR01098  34 LNFGILPGE-NASNLTRRWEPLADYLEKKLGIKVQLFVATDYSAVIEAMRFGRVDIAWFGPSSYVLAHYRANAEVFAltA 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621110282  89 VKYRGEPFYKALIVGRADLPIKKWpEDAKGLKLSLSDQGNTSGWLIPMAYFKSIGIDPASYFEYREGATfGQNESQI--- 165
Cdd:TIGR01098 113 VSTDGSPGYYSVIIVKADSPIKSL-KDLKGKTFAFGDPASTSGYLVPRYQLKKEGGLDADGFFSEVVFS-GSHDASAlav 190
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1621110282 166 QHGLIDLGSDMDRGRNGMIEAGQIDPSKSKIVWESSKLPNDAISVPKDFDPALKARITEILTSL 229
Cdd:TIGR01098 191 ANGKVDAATNNSSAIGRLKKRGPSDMKKVRVIWKSPLIPNDPIAVRKDLPPELKEKIRDAFLTL 254
PBP2_PnhD_4 cd13574
Substrate binding domain of uncharacterized ABC-type phosphonate-like transporter; contains ...
11-253 1.66e-21

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: 90.45  E-value: 1.66e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621110282  11 LRFAIAPMRPtPSQTIKEFEPIFKYLADQLGATYEIVSPESWAAISVAMTNGHVDVGWLGPWGYV-LSNKKAGTEVLATV 89
Cdd:cd13574     6 LRFGVHPYLS-PTELVKRFQPLLDYLEEELGRPVEIKVSKDYQEHVDRLGSGKIDIAYLGPAPYVqAKDRRYGIKPLLAL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621110282  90 KYR-GEPFYKALIVGRADLPIKKwPEDAKGLKLSLSDQGNTSGWLIPMAYFKSIGIDPASYFEYregATFGQNES---QI 165
Cdd:cd13574    85 LETdGKPTYNGVIVVRADSPIKS-LADLAGKSFAFGDPLSTMGHLVPRAMLRQAGITSLDLAGY---DYLGRHDNvalAV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621110282 166 QHGLIDLGsdmdrgrnGMIE--AGQIDPSKSKIVWESSKLPNDAISVPKDFDPALKARITEILTSLSEEKAQSLMGSGY- 242
Cdd:cd13574   161 LAGEFDAG--------ALKEevYRKYKGRGLRVLATSPPLPGHALVARATLPEELVKALRRALLELDSTGAGLAILTWIe 232
                         250
                  ....*....|....
gi 1621110282 243 ---NGFVKAKHSDY 253
Cdd:cd13574   233 elrHGFVPVTDEDY 246
PBP2_PnhD cd13575
Substrate binding domain of ABC-type phosphonate uptake system; contains the type 2 ...
11-248 1.84e-17

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: 79.44  E-value: 1.84e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621110282  11 LRFAIapMRPTPSQTIK-EFEPIFKYLADQLGATYEIVSPESWAAISVAMTNGHVDVGWLGPWGYVLSNKKAGTEVLA-T 88
Cdd:cd13575     6 LNFGI--ISTESQQNLRaQWEPFLAAMEKKLGVKVNAFFAPDYAGIIEGMRFNKVQIAWYGNKSAMEAVDRANGEVFAqT 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621110282  89 VKYRGEPFYKALIVGRADLPIKKWPE---DAKGLKLSLSDQGNTSGWLIPMAY-FKSIGIDPASYFEYREGATFGQNESQ 164
Cdd:cd13575    84 VAADGSPGYYSHLIVNKDSPINSLNDvlaKAKDLTFGNGDPNSTSGFLVPGYYvFAKNGIDPKKFFKRTVNANHETNALA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621110282 165 IQHGLIDLGS----DMDRgrngmieAGQIDPSKS---KIVWESSKLPNDAISVPKDFDPALKARITEILTSL---SEEKA 234
Cdd:cd13575   164 VANKQVDVATnnteNLDR-------LKERAPEKLkqlRIIWTSPLIPGDPLVWRKDLPEAVKKKIADFFFGYgqtAEEKS 236
                         250
                  ....*....|....
gi 1621110282 235 QSLMGSGYNGFVKA 248
Cdd:cd13575   237 VLKERLDWSPFKPS 250
PBP2_PnhD_3 cd13573
Substrate binding domain of uncharacterized ABC-type phosphonate-like transporter; contains ...
29-224 2.73e-10

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: 59.41  E-value: 2.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621110282  29 FEPIFKYLADQLGATYEIVSPESWAAISVAMTNGHVDVGWL--GPWGYVLSnkKAGTEVLATVKYRGEPF-YKALIVGRA 105
Cdd:cd13573    23 WAPFIAHISKVTGKDVQFYPVQSNAAQTEAMRSGRLHIAGFstGPTPFAVN--LAGAVPFAVKGYEDGSFgYELEVITRI 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621110282 106 DLPIKKwPEDAKGLKLSLSDQGNTSGWLIPMAYFKSI-GIDPASYFEyregATFGQNESQIQHGlIDLGsDMDRGR---- 180
Cdd:cd13573   101 DSGIQK-VKDLKGRKVAHTSPTSNSGHLAPRALFPAQgGIVPDKDYE----VTFSGKHDQSILG-VFNG-DYDAAPvasd 173
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1621110282 181 --NGMIEAGQIDPSKSKIVWESSKLPNDAISVPKDFDPALKARITE 224
Cdd:cd13573   174 vlERMAERGQVKEEQFRVIYKSFAFPTGPFGYAHNLKPELREKIKE 219
TauA COG0715
ABC-type nitrate/sulfonate/bicarbonate transport system, periplasmic component [Inorganic ion ...
35-147 2.26e-06

ABC-type nitrate/sulfonate/bicarbonate transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 440479 [Multi-domain]  Cd Length: 297  Bit Score: 48.08  E-value: 2.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621110282  35 YLADQlGATYEIVSPESWAAISVAMTNGHVDVGWLG-PWGYVLSNKKAGTEVLATVkYRGEPFYkalIVGRADLPIKKwP 113
Cdd:COG0715    45 YFKKE-GLDVELVEFAGGAAALEALAAGQADFGVAGaPPALAARAKGAPVKAVAAL-SQSGGNA---LVVRKDSGIKS-L 118
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1621110282 114 EDAKGLKLSLSdQGNTSGWLIPmAYFKSIGIDPA 147
Cdd:COG0715   119 ADLKGKKVAVP-GGSTSHYLLR-ALLAKAGLDPK 150
Periplasmic_Binding_Protein_Type_2 cd00648
Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent ...
11-173 6.11e-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: 42.95  E-value: 6.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621110282  11 LRFAIapmrPTPSQTIKEFEPIFKYLADQLGATYEIVSPESWAAISVAMTNGHVDVGWLG--PWGYVLSNKKAGTEVLAT 88
Cdd:cd00648     2 LTVAS----IGPPPYAGFAEDAAKQLAKETGIKVELVPGSSIGTLIEALAAGDADVAVGPiaPALEAAADKLAPGGLYIV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621110282  89 VKYrgePFYKALIVGRADLPIKK--WPEDAKGLKLsLSDQGNTSGWLIpMAYFKSIGIDPASYFEYREGATFGQNESQIQ 166
Cdd:cd00648    78 PEL---YVGGYVLVVRKGSSIKGllAVADLDGKRV-GVGDPGSTAVRQ-ARLALGAYGLKKKDPEVVPVPGTSGALAAVA 152

                  ....*..
gi 1621110282 167 HGLIDLG 173
Cdd:cd00648   153 NGAVDAA 159
PBP2_ThiY_THI5_like_1 cd13652
Putative substrate binding domain of an ABC-type transporter similar to ThiY/THI5; the type 2 ...
41-147 2.92e-04

Putative substrate binding domain of an ABC-type transporter similar to ThiY/THI5; the type 2 periplasmic binding protein fold; This subfamily is phylogenetically similar to ThiY, which is the periplasmic N-formyl-4-amino-5-(aminomethyl)-2-methylpyrimidine (FAMP) binding component of the ABC transport system (ThiXYZ). FAMP is imported into cell by the transporter, where it is then incorporated into the thiamin biosynthetic pathway. The closest structural homologs of ThiY are THI5, which is responsible for the synthesis of 4-amino-5-(hydroxymethyl)-2-methylpyrimidine phosphate (HMP-P) in the thiamin biosynthetic pathway of eukaryotes, and periplasmic binding proteins involved in alkanesulfonate/nitrate and bicarbonate transport. After binding the ligand, they 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. The ThiY/THI5 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: 270370 [Multi-domain]  Cd Length: 217  Bit Score: 41.22  E-value: 2.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621110282  41 GATYEIVSPESWAAISVAMTNGHVDVGWLGPWGYVLSNKKAGTEV-LATVKYRGEPFY-KALIVGRADLPIKKwPEDAKG 118
Cdd:cd13652    30 GLDVEITRFASGAEILAALASGQVDVAGSSPGASLLGALARGADLkIVAEGLGTTPGYgPFAIVVRADSGITS-PADLVG 108
                          90       100
                  ....*....|....*....|....*....
gi 1621110282 119 LKLSLSDQGNTSGWLIPmAYFKSIGIDPA 147
Cdd:cd13652   109 KKIAVSTLTNILEYTTN-AYLKKNGLDPD 136
PBP2_peptides_like cd13530
Peptide-binding protein and related homologs; type 2 periplasmic binding protein fold; This ...
32-226 2.75e-03

Peptide-binding protein and related homologs; type 2 periplasmic binding protein fold; This domain is found in solute binding proteins that serve as initial receptors in the ABC transport, signal transduction and channel gating. The PBP2 proteins share the same architecture as periplasmic binding proteins type 1, 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 majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. 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.


Pssm-ID: 270248 [Multi-domain]  Cd Length: 217  Bit Score: 38.00  E-value: 2.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621110282  32 IFKYLADQLGATYEIVsPESWAAISVAMTNGHVDVGWlGPWGYVLSNKKagtEVLATvkyrgEPFYKA--LIVGRADLPI 109
Cdd:cd13530    29 LANAIAKRLGVKVEFV-DTDFDGLIPALQSGKIDVAI-SGMTITPERAK---VVDFS-----DPYYYTgqVLVVKKDSKI 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621110282 110 KKWPEDAKGLKLSLsdQGNTSGwlipMAYFKSIGIDpasyFEYREGATFGQNESQIQHGLID-------LGSDMDRGRNG 182
Cdd:cd13530    99 TKTVADLKGKKVGV--QAGTTG----EDYAKKNLPN----AEVVTYDNYPEALQALKAGRIDavitdapVAKYYVKKNGP 168
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1621110282 183 MIEAGQIDPSKSKIvwessklpndAISVPKDfDPALKARITEIL 226
Cdd:cd13530   169 DLKVVGEPLTPEPY----------GIAVRKG-NPELLDAINKAL 201
 
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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