NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|446914746|ref|WP_000992002|]
View 

MULTISPECIES: phosphonate ABC transporter substrate-binding protein [Enterobacteriaceae]

Protein Classification

phosphonate ABC transporter substrate-binding protein( domain architecture ID 10194387)

phosphonate ABC transporter substrate-binding protein is a phosphonate binding protein that is part of the phosphonate uptake system; functions as the initial receptor of the ABC-type transport system

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PBP2_PnhD cd13575
Substrate binding domain of ABC-type phosphonate uptake system; contains the type 2 ...
28-284 5.60e-169

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: 470.41  E-value: 5.60e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746  28 EQEKALNFGIISTESQQNLKPQWTPFLQDMEKKLGVKVNAFFAPDYAGIIQGMRFNKVDIAWYGNLSAMEAVDRANGQVF 107
Cdd:cd13575    1 EDEKALNFGIISTESQQNLRAQWEPFLAAMEKKLGVKVNAFFAPDYAGIIEGMRFNKVQIAWYGNKSAMEAVDRANGEVF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746 108 AQTVAADGSPGYWSVLIVNKDSPINNLNDLLAKRKDLTFGNGDPNSTSGFLVPGYYVFAKNNI-SASDFKRTVNAGHETN 186
Cdd:cd13575   81 AQTVAADGSPGYYSHLIVNKDSPINSLNDVLAKAKDLTFGNGDPNSTSGFLVPGYYVFAKNGIdPKKFFKRTVNANHETN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746 187 ALAVANKQVDVATNNTENLDKLKTSAPEKLKELKVIWKSPLIPGDPIVWRKNLSETTKDKIYDFFMNYGKTPEEKAVL-E 265
Cdd:cd13575  161 ALAVANKQVDVATNNTENLDRLKERAPEKLKQLRIIWTSPLIPGDPLVWRKDLPEAVKKKIADFFFGYGQTAEEKSVLkE 240
                        250
                 ....*....|....*....
gi 446914746 266 RLGWAPFRASSDLQLVPIR 284
Cdd:cd13575  241 RLDWSPFKPSSDGQLVPIR 259
 
Name Accession Description Interval E-value
PBP2_PnhD cd13575
Substrate binding domain of ABC-type phosphonate uptake system; contains the type 2 ...
28-284 5.60e-169

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: 470.41  E-value: 5.60e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746  28 EQEKALNFGIISTESQQNLKPQWTPFLQDMEKKLGVKVNAFFAPDYAGIIQGMRFNKVDIAWYGNLSAMEAVDRANGQVF 107
Cdd:cd13575    1 EDEKALNFGIISTESQQNLRAQWEPFLAAMEKKLGVKVNAFFAPDYAGIIEGMRFNKVQIAWYGNKSAMEAVDRANGEVF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746 108 AQTVAADGSPGYWSVLIVNKDSPINNLNDLLAKRKDLTFGNGDPNSTSGFLVPGYYVFAKNNI-SASDFKRTVNAGHETN 186
Cdd:cd13575   81 AQTVAADGSPGYYSHLIVNKDSPINSLNDVLAKAKDLTFGNGDPNSTSGFLVPGYYVFAKNGIdPKKFFKRTVNANHETN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746 187 ALAVANKQVDVATNNTENLDKLKTSAPEKLKELKVIWKSPLIPGDPIVWRKNLSETTKDKIYDFFMNYGKTPEEKAVL-E 265
Cdd:cd13575  161 ALAVANKQVDVATNNTENLDRLKERAPEKLKQLRIIWTSPLIPGDPLVWRKDLPEAVKKKIADFFFGYGQTAEEKSVLkE 240
                        250
                 ....*....|....*....
gi 446914746 266 RLGWAPFRASSDLQLVPIR 284
Cdd:cd13575  241 RLDWSPFKPSSDGQLVPIR 259
PhnD TIGR03431
phosphonate ABC transporter, periplasmic phosphonate binding protein; This model is a subset ...
1-291 3.09e-146

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: 413.67  E-value: 3.09e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746    1 MNAKIIASLAFTSMFSLStllsPAHAEEQEKALNFGIISTESQQNLKPQWTPFLQDMEKKLGVKVNAFFAPDYAGIIQGM 80
Cdd:TIGR03431   1 MLRRLILSLVAAFMLISS----NAQAEDWPKELNFGIIPTENASDLKQRWEPLADYLSKKLGVKVKLFFATDYAGVIEGM 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746   81 RFNKVDIAWYGNLSAMEAVDRANGQVFAQTVAADGSPGYWSVLIVNKDSPINNLNDLlakrKDLTFGNGDPNSTSGFLVP 160
Cdd:TIGR03431  77 RFGKVDIAWYGPSSYAEAYQKANAEAFAIEVNADGSTGYYSVLIVKKDSPIKSLEDL----KGKTFGFVDPNSTSGFLVP 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746  161 GYYVFAKNNISASD-FKRTVNAG-HETNALAVANKQVDVATNNTENLDKLKT-SAPEKLKELKVIWKSPLIPGDPIVWRK 237
Cdd:TIGR03431 153 SYYLFKKNGIKPKEyFKKVTFSGsHEAAILAVANGTVDAATTNDENLDRMIRkGQPDAMEDLRIIWKSPLIPNGPIVYRK 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 446914746  238 NLSETTKDKIYDFFMNYGKTPEEKAVLERLGW-APFRASSDLQLVPIRQLALFKE 291
Cdd:TIGR03431 233 DLPADLKAKIRKAFLNYHKTDKACFEKIAGGDlKGFVAASDKDYDPIRDLKKAKI 287
Phosphonate-bd pfam12974
ABC transporter, phosphonate, periplasmic substrate-binding protein; This is a family of ...
35-277 2.90e-96

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: 285.31  E-value: 2.90e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746   35 FGIISTESQQNLKPQWTPFLQDMEKKLGVKVNAFFAPDYAGIIQGMRFNKVDIAWYGNLSAMEAVDRANGQVFAQTVAAD 114
Cdd:pfam12974   1 FGVLPDESPDELKARYQPLADYLSEELGVPVELVVATDYAAVVEALRAGQVDIAYFGPLAYVQAVDRAGAEPLATPVEPD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746  115 GSPGYWSVLIVNKDSPINNLNDLlakrKDLTFGNGDPNSTSGFLVPGYYVFAKNNISAS-DFKRTVNAGHETNALAVANK 193
Cdd:pfam12974  81 GSAGYRSVIIVRKDSPIQSLEDL----KGKTVAFGDPSSTSGYLVPLALLFAEAGLDPEdDFKPVFSGSHDAVALAVLNG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746  194 QVDVATNNTENLDKLKTSAPEKLKELKVIWKSPLIPGDPIVWRKNLSETTKDKIYDFFMNYGKTPEEKAVLERLGWAPFR 273
Cdd:pfam12974 157 DADAGAVNSEVLERLVAEGPIDRDQLRVIAESPPIPNDPLVARPDLPPELKEKIRDALLALDETPEGRKVLEALGIDGFV 236

                  ....
gi 446914746  274 ASSD 277
Cdd:pfam12974 237 PADD 240
PhnD COG3221
ABC-type phosphate/phosphonate transport system, periplasmic component [Inorganic ion ...
37-287 1.54e-86

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


Pssm-ID: 442454 [Multi-domain]  Cd Length: 250  Bit Score: 260.62  E-value: 1.54e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746  37 IISTESQQNLKPQWTPFLQDMEKKLGVKVNAFFAPDYAGIIQGMRFNKVDIAWYGNLSAMEAVDRANGQVFAQTVaADGS 116
Cdd:COG3221    1 VLPSESPADLLARWQPLADYLEEELGVPVELVPATDYAALIEALRAGQVDLAFLGPLPYVLARDRAGAEPLATPV-RDGS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746 117 PGYWSVLIVNKDSPINNLNDLlakrKDLTFGNGDPNSTSGFLVPGYYvFAKNNISA-SDFKRTVNAG-HETNALAVANKQ 194
Cdd:COG3221   80 PGYRSVIIVRADSPIKSLEDL----KGKRFAFGDPDSTSGYLVPRAL-LAEAGLDPeRDFSEVVFSGsHDAVILAVANGQ 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746 195 VDVATNNTENLDKLKTSAPEKlKELKVIWKSPLIPGDPIVWRKNLSETTKDKIYDFFMNYGKTPEEKAVLERLGWAPFRA 274
Cdd:COG3221  155 ADAGAVDSGVLERLVEEGPDA-DQLRVIWESPPIPNDPFVARPDLPPELREKIREALLSLDEDPEGKAILEALGLEGFVP 233
                        250
                 ....*....|...
gi 446914746 275 SSDLQLVPIRQLA 287
Cdd:COG3221  234 ADDADYDPIRELL 246
 
Name Accession Description Interval E-value
PBP2_PnhD cd13575
Substrate binding domain of ABC-type phosphonate uptake system; contains the type 2 ...
28-284 5.60e-169

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: 470.41  E-value: 5.60e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746  28 EQEKALNFGIISTESQQNLKPQWTPFLQDMEKKLGVKVNAFFAPDYAGIIQGMRFNKVDIAWYGNLSAMEAVDRANGQVF 107
Cdd:cd13575    1 EDEKALNFGIISTESQQNLRAQWEPFLAAMEKKLGVKVNAFFAPDYAGIIEGMRFNKVQIAWYGNKSAMEAVDRANGEVF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746 108 AQTVAADGSPGYWSVLIVNKDSPINNLNDLLAKRKDLTFGNGDPNSTSGFLVPGYYVFAKNNI-SASDFKRTVNAGHETN 186
Cdd:cd13575   81 AQTVAADGSPGYYSHLIVNKDSPINSLNDVLAKAKDLTFGNGDPNSTSGFLVPGYYVFAKNGIdPKKFFKRTVNANHETN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746 187 ALAVANKQVDVATNNTENLDKLKTSAPEKLKELKVIWKSPLIPGDPIVWRKNLSETTKDKIYDFFMNYGKTPEEKAVL-E 265
Cdd:cd13575  161 ALAVANKQVDVATNNTENLDRLKERAPEKLKQLRIIWTSPLIPGDPLVWRKDLPEAVKKKIADFFFGYGQTAEEKSVLkE 240
                        250
                 ....*....|....*....
gi 446914746 266 RLGWAPFRASSDLQLVPIR 284
Cdd:cd13575  241 RLDWSPFKPSSDGQLVPIR 259
PhnD TIGR03431
phosphonate ABC transporter, periplasmic phosphonate binding protein; This model is a subset ...
1-291 3.09e-146

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: 413.67  E-value: 3.09e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746    1 MNAKIIASLAFTSMFSLStllsPAHAEEQEKALNFGIISTESQQNLKPQWTPFLQDMEKKLGVKVNAFFAPDYAGIIQGM 80
Cdd:TIGR03431   1 MLRRLILSLVAAFMLISS----NAQAEDWPKELNFGIIPTENASDLKQRWEPLADYLSKKLGVKVKLFFATDYAGVIEGM 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746   81 RFNKVDIAWYGNLSAMEAVDRANGQVFAQTVAADGSPGYWSVLIVNKDSPINNLNDLlakrKDLTFGNGDPNSTSGFLVP 160
Cdd:TIGR03431  77 RFGKVDIAWYGPSSYAEAYQKANAEAFAIEVNADGSTGYYSVLIVKKDSPIKSLEDL----KGKTFGFVDPNSTSGFLVP 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746  161 GYYVFAKNNISASD-FKRTVNAG-HETNALAVANKQVDVATNNTENLDKLKT-SAPEKLKELKVIWKSPLIPGDPIVWRK 237
Cdd:TIGR03431 153 SYYLFKKNGIKPKEyFKKVTFSGsHEAAILAVANGTVDAATTNDENLDRMIRkGQPDAMEDLRIIWKSPLIPNGPIVYRK 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 446914746  238 NLSETTKDKIYDFFMNYGKTPEEKAVLERLGW-APFRASSDLQLVPIRQLALFKE 291
Cdd:TIGR03431 233 DLPADLKAKIRKAFLNYHKTDKACFEKIAGGDlKGFVAASDKDYDPIRDLKKAKI 287
3A0109s03R TIGR01098
phosphate/phosphite/phosphonate ABC transporter, periplasmic binding protein; Phosphonates are ...
4-254 1.63e-113

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: 329.69  E-value: 1.63e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746    4 KIIASLAFTSMFSLSTLLSPAHAE--EQEKALNFGIISTESQQNLKPQWTPFLQDMEKKLGVKVNAFFAPDYAGIIQGMR 81
Cdd:TIGR01098   3 RLLALLAALLGASLAAACSKKAAEaaAVPKELNFGILPGENASNLTRRWEPLADYLEKKLGIKVQLFVATDYSAVIEAMR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746   82 FNKVDIAWYGNLSAMEAVDRANGQVFAQT-VAADGSPGYWSVLIVNKDSPINNLNDLlakrKDLTFGNGDPNSTSGFLVP 160
Cdd:TIGR01098  83 FGRVDIAWFGPSSYVLAHYRANAEVFALTaVSTDGSPGYYSVIIVKADSPIKSLKDL----KGKTFAFGDPASTSGYLVP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746  161 GYYVFAKNNISAS-DFKRTVNAG-HETNALAVANKQVDVATNNTENLDKLKTSAPEKLKELKVIWKSPLIPGDPIVWRKN 238
Cdd:TIGR01098 159 RYQLKKEGGLDADgFFSEVVFSGsHDASALAVANGKVDAATNNSSAIGRLKKRGPSDMKKVRVIWKSPLIPNDPIAVRKD 238
                         250
                  ....*....|....*.
gi 446914746  239 LSETTKDKIYDFFMNY 254
Cdd:TIGR01098 239 LPPELKEKIRDAFLTL 254
Phosphonate-bd pfam12974
ABC transporter, phosphonate, periplasmic substrate-binding protein; This is a family of ...
35-277 2.90e-96

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: 285.31  E-value: 2.90e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746   35 FGIISTESQQNLKPQWTPFLQDMEKKLGVKVNAFFAPDYAGIIQGMRFNKVDIAWYGNLSAMEAVDRANGQVFAQTVAAD 114
Cdd:pfam12974   1 FGVLPDESPDELKARYQPLADYLSEELGVPVELVVATDYAAVVEALRAGQVDIAYFGPLAYVQAVDRAGAEPLATPVEPD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746  115 GSPGYWSVLIVNKDSPINNLNDLlakrKDLTFGNGDPNSTSGFLVPGYYVFAKNNISAS-DFKRTVNAGHETNALAVANK 193
Cdd:pfam12974  81 GSAGYRSVIIVRKDSPIQSLEDL----KGKTVAFGDPSSTSGYLVPLALLFAEAGLDPEdDFKPVFSGSHDAVALAVLNG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746  194 QVDVATNNTENLDKLKTSAPEKLKELKVIWKSPLIPGDPIVWRKNLSETTKDKIYDFFMNYGKTPEEKAVLERLGWAPFR 273
Cdd:pfam12974 157 DADAGAVNSEVLERLVAEGPIDRDQLRVIAESPPIPNDPLVARPDLPPELKEKIRDALLALDETPEGRKVLEALGIDGFV 236

                  ....
gi 446914746  274 ASSD 277
Cdd:pfam12974 237 PADD 240
PBP2_PhnD_like cd01071
Substrate binding domain of phosphonate uptake system-like, a member of the type 2 ...
28-284 3.42e-96

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: 285.31  E-value: 3.42e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746  28 EQEKALNFGIISTESQQNLKPQWTPFLQDMEKKLGVKVNAFFAPDYAGIIQGMRFNKVDIAWYGNLSAMEAVDRANGQVF 107
Cdd:cd01071    1 AAPKELRFGLVPAEDADELKKEFEPLADYLEEELGVPVELVVATSYAAVVEAMRNGKVDIAWLGPASYVLAHDRAGAEAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746 108 AqTVAADGSPGYWSVLIVNKDSPINNLNDLLAKRkdltFGNGDPNSTSGFLVPGYYVFAKNNISASDFKRTVNAG-HETN 186
Cdd:cd01071   81 A-TEVRDGSPGYYSVIIVRKDSPIKSLEDLKGKT----VAFVDPSSTSGYLFPRAMLKDAGIDPPDFFFEVVFAGsHDSA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746 187 ALAVANKQVDVATNNTENLDKLKTSAPEKLKELKVIWKSPLIPGDPIVWRKNLSETTKDKIYDFFMNYGKTPEEKAVLER 266
Cdd:cd01071  156 LLAVANGDVDAAATYDSTLERAAAAGPIDPDDLRVIWRSPPIPNDPLVVRKDLPPALKAKIRDALLDLDETDEGQKLLAG 235
                        250
                 ....*....|....*...
gi 446914746 267 LGWAPFRASSDLQLVPIR 284
Cdd:cd01071  236 LGLTGFVPATDDDYDPIR 253
PhnD COG3221
ABC-type phosphate/phosphonate transport system, periplasmic component [Inorganic ion ...
37-287 1.54e-86

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


Pssm-ID: 442454 [Multi-domain]  Cd Length: 250  Bit Score: 260.62  E-value: 1.54e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746  37 IISTESQQNLKPQWTPFLQDMEKKLGVKVNAFFAPDYAGIIQGMRFNKVDIAWYGNLSAMEAVDRANGQVFAQTVaADGS 116
Cdd:COG3221    1 VLPSESPADLLARWQPLADYLEEELGVPVELVPATDYAALIEALRAGQVDLAFLGPLPYVLARDRAGAEPLATPV-RDGS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746 117 PGYWSVLIVNKDSPINNLNDLlakrKDLTFGNGDPNSTSGFLVPGYYvFAKNNISA-SDFKRTVNAG-HETNALAVANKQ 194
Cdd:COG3221   80 PGYRSVIIVRADSPIKSLEDL----KGKRFAFGDPDSTSGYLVPRAL-LAEAGLDPeRDFSEVVFSGsHDAVILAVANGQ 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746 195 VDVATNNTENLDKLKTSAPEKlKELKVIWKSPLIPGDPIVWRKNLSETTKDKIYDFFMNYGKTPEEKAVLERLGWAPFRA 274
Cdd:COG3221  155 ADAGAVDSGVLERLVEEGPDA-DQLRVIWESPPIPNDPFVARPDLPPELREKIREALLSLDEDPEGKAILEALGLEGFVP 233
                        250
                 ....*....|...
gi 446914746 275 SSDLQLVPIRQLA 287
Cdd:COG3221  234 ADDADYDPIRELL 246
PBP2_PnhD_1 cd13571
Substrate binding domain of uncharacterized ABC-type phosphonate-like transporter; contains ...
28-284 3.91e-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: 162.43  E-value: 3.91e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746  28 EQEKALNFGIISTESQQNLKPQWTPFLQDMEKKLGVKVNAFFAPDYAGIIQGMRFNKVDIAWYGNLSAMEAVDRANGQVF 107
Cdd:cd13571    1 ASSPPLRIGLASVLSPRETLALYDPLAEYLERKLGRPVEFVQRRTYAEINELLKNGKVDLAFVCSGAYVQARDKAGLELL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746 108 AQTVAaDGSPGYWSVLIVNKDSPINNLNDLlakrKDLTFGNGDPNSTSGFLVPGYYVfAKNNISA-SDFKRTVNAGHETN 186
Cdd:cd13571   81 AVPEI-NGQPTYRSYIIVPADSPAKSLEDL----KGKRFAFTDPLSNSGFLVPMYLL-AELGLDPeRFFSRVFFTGSHDK 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746 187 AL-AVANKQVDVATNNTENLDKLKTSAPEKLKELKVIWKSPLIPGDPIVWRKNLSETTKDKIYDFFMNYGKTPEEKAVLE 265
Cdd:cd13571  155 SIqAVANGLVDGAAVDSLVYEYAVEKGPELAANVRIIWRSEPIGNPPVVARPGLDPELKAALQEAFLSMHEDPEGRAALE 234
                        250
                 ....*....|....*....
gi 446914746 266 RLGWAPFRASSDLQLVPIR 284
Cdd:cd13571  235 GLGIDRFVPADDSLYDPIR 253
PBP2_PnhD_2 cd13572
Substrate binding domain of uncharacterized ABC-type phosphonate-like transporter; contains ...
29-284 6.89e-48

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: 161.71  E-value: 6.89e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746  29 QEKALNFGIISTESQQNLKPQWTPFLQDMEKKLGVKVNAFFAPDYAGIIQGMRFNKVDIAWYGNLSAMEAVDRANGQVFA 108
Cdd:cd13572    2 APETLKVGAIPDENPTTLIRLNDPLADYLEKELGVEVELVVVTDYAAMVEAMRNGQLDLAYFGGLTYVQARLKPGAEPIA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746 109 QtVAADGSPGYWSVLIVNKDSPINNLNDLlakrKDLTFGNGDPNSTSGFLVPGYYVFAKNNISASDFKRTVNAG-HETNA 187
Cdd:cd13572   82 Q-LLRDGDPTFHSVFIANTDSGINSLADL----KGKRFAFGDPASTSGHLMPRYFLLEAGVLPDGDFYRVGFSGaHDATA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746 188 LAVANKQVDVATNNTENLDKLKTSAPEKLKELKVIWKSPLIPGDPIVWRKNLSETTKDKIYDFFMNYgktpEEKAVLERL 267
Cdd:cd13572  157 LAVANGKVDAGALNEAIWESLVEEGKIDGEKVKVIWRTPPYPDYPWTVRPNLGPELKEKVRNAFLSL----DDPEVLDIF 232
                        250
                 ....*....|....*..
gi 446914746 268 GWAPFRASSDLQLVPIR 284
Cdd:cd13572  233 GASGFIPASDDDYDPIE 249
PBP2_PnhD_4 cd13574
Substrate binding domain of uncharacterized ABC-type phosphonate-like transporter; contains ...
28-275 2.45e-32

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: 120.88  E-value: 2.45e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746  28 EQEKALNFGIISTESQQNLKPQWTPFLQDMEKKLGVKVNAFFAPDYAGIIQGMRFNKVDIAWYGNLSAMEAVDRANG-QV 106
Cdd:cd13574    1 AAEPPLRFGVHPYLSPTELVKRFQPLLDYLEEELGRPVEIKVSKDYQEHVDRLGSGKIDIAYLGPAPYVQAKDRRYGiKP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746 107 FAQTVAADGSPGYWSVLIVNKDSPINNLNDLLAKRkdltFGNGDPNSTSGFLVPGYYVfAKNNISASDFKRTVNAG-HET 185
Cdd:cd13574   81 LLALLETDGKPTYNGVIVVRADSPIKSLADLAGKS----FAFGDPLSTMGHLVPRAML-RQAGITSLDLAGYDYLGrHDN 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746 186 NALAVANKQVDVATnntenldkLKTSAPEKLKE--LKVIWKSPLIPGDPIVWRKNLSETTKDKIYDFFMNYGKTPEEKAV 263
Cdd:cd13574  156 VALAVLAGEFDAGA--------LKEEVYRKYKGrgLRVLATSPPLPGHALVARATLPEELVKALRRALLELDSTGAGLAI 227
                        250
                 ....*....|....*..
gi 446914746 264 L-----ERLGWAPFRAS 275
Cdd:cd13574  228 LtwieeLRHGFVPVTDE 244
ABC_peri_selen TIGR04553
putative selenate ABC transporter periplasmic binding protein; Members of this family ABC ...
33-287 1.83e-27

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: 108.32  E-value: 1.83e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746   33 LNFGIISTESQQNLKPQWTPFLQDMEKKLGVKVNafFAP--DYAGIIQGMRFNKVDIAWYGNLSAMEAVDRANGQV-FAQ 109
Cdd:TIGR04553   2 FVFTAIPDEDPTELQRRFAPLADYLEEELGVEVR--FVPvtDYAAAVEAFRNNQVQLAWFGGLTGVQARVRVPGSVpLAQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746  110 TVAadgSPGYWSVLIVNkDSPINNLNDLLAKRKDLTFGNGDPNSTSGFLVPGYYVFAKNNISASDFKRTVNAG-HETNAL 188
Cdd:TIGR04553  80 RVE---DEAFRSVFIAH-ESTILELADGLPELKGKTFTFGSKSSTSGRLMPRSFLLEAGEAPDDDFKRVGYSGaHDATLA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746  189 AVANKQVDVATNNTENLDKLKTSAPEKLKELKVIWKSP-------LIPGDpivWRKNLSETTKDKIYDFFMNY-GKTPEE 260
Cdd:TIGR04553 156 LVEAGTYDAGALNISVWEKEVADGKVDTDKVRVIWTTPgypdynwTVRGD---VDERFGEGFTDKVTQALLDLdPSTAED 232
                         250       260
                  ....*....|....*....|....*..
gi 446914746  261 KAVLERLGWAPFRASSDLQLVPIRQLA 287
Cdd:TIGR04553 233 KEILELFRASRFIPTSNDNYAGIEAAA 259
PBP2_PnhD_3 cd13573
Substrate binding domain of uncharacterized ABC-type phosphonate-like transporter; contains ...
31-262 5.04e-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: 270291 [Multi-domain]  Cd Length: 253  Bit Score: 98.70  E-value: 5.04e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746  31 KALNFGIISTESQQNLKPQWTPFLQDMEKKLGVKVNAFFAPDYAGIIQGMRFNKVDIAWYGNLSAMEAVDRANGQVFAQT 110
Cdd:cd13573    4 DTLVFAYTPVEDPAVYQEIWAPFIAHISKVTGKDVQFYPVQSNAAQTEAMRSGRLHIAGFSTGPTPFAVNLAGAVPFAVK 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746 111 VAADGSPGYWSVLIVNKDSPINNLNDLLAKRKDLTfgngDPNSTSGFLVPGYYVFAKNNISAS-DFKRTVNAGHETNALA 189
Cdd:cd13573   84 GYEDGSFGYELEVITRIDSGIQKVKDLKGRKVAHT----SPTSNSGHLAPRALFPAQGGIVPDkDYEVTFSGKHDQSILG 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446914746 190 VANKQVDVATNNTENLDKLKTSAPEKLKELKVIWKSPLIPGDPIVWRKNLSETTKDKIYDFFMNYGKTPEEKA 262
Cdd:cd13573  160 VFNGDYDAAPVASDVLERMAERGQVKEEQFRVIYKSFAFPTGPFGYAHNLKPELREKIKEAFFTYDFAGTKLA 232
Periplasmic_Binding_Protein_Type_2 cd00648
Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent ...
33-237 4.26e-15

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: 72.61  E-value: 4.26e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746  33 LNFGIISTESQQnlkPQWTPFLQDMEKKLGVKVNAFFAPDYAGIIQGMRFNKVDIAWYGNLSAMEAVDRANgqVFAQTVA 112
Cdd:cd00648    2 LTVASIGPPPYA---GFAEDAAKQLAKETGIKVELVPGSSIGTLIEALAAGDADVAVGPIAPALEAAADKL--APGGLYI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746 113 ADGSPGYWSVLIVNKDSPINNlNDLLAKRKDLTFGNGDPNSTSGFLvpGYYVFAKNNISASDFKRTVNAGHETNALAVAN 192
Cdd:cd00648   77 VPELYVGGYVLVVRKGSSIKG-LLAVADLDGKRVGVGDPGSTAVRQ--ARLALGAYGLKKKDPEVVPVPGTSGALAAVAN 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 446914746 193 KQVDVATNNTENLdklkTSAPEKLKELKVIWKS--PLIPGDPIVWRK 237
Cdd:cd00648  154 GAVDAAIVWVPAA----ERAQLGNVQLEVLPDDlgPLVTTFGVAVRK 196
TauA COG0715
ABC-type nitrate/sulfonate/bicarbonate transport system, periplasmic component [Inorganic ion ...
9-199 3.69e-12

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


Pssm-ID: 440479 [Multi-domain]  Cd Length: 297  Bit Score: 65.80  E-value: 3.69e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746   9 LAFTSMFSLSTLLSPAHAEEQEKaLNFGIISTesqqnlkPQWTPFLQDMEK----KLGVKVNAFFAPDYAGIIQGMRFNK 84
Cdd:COG0715    1 LAALAALALAACSAAAAAAEKVT-LRLGWLPN-------TDHAPLYVAKEKgyfkKEGLDVELVEFAGGAAALEALAAGQ 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746  85 VDIAWYGNLSAMEAvdRANG---QVFAQTVAADGSpgywsVLIVNKDSPINNLNDLlakrKDLTFGnGDPNSTSGFLVPg 161
Cdd:COG0715   73 ADFGVAGAPPALAA--RAKGapvKAVAALSQSGGN-----ALVVRKDSGIKSLADL----KGKKVA-VPGGSTSHYLLR- 139
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 446914746 162 yYVFAKNNISASDFKrTVNAGHETNALAVANKQVDVAT 199
Cdd:COG0715  140 -ALLAKAGLDPKDVE-IVNLPPPDAVAALLAGQVDAAV 175
PBP2_sulfate_ester_like cd13555
Sulfate ester binding protein-like, the type 2 periplasmic binding protein fold; This ...
53-198 3.59e-06

Sulfate ester binding protein-like, the type 2 periplasmic binding protein fold; This subfamily includes the periplasmic component of putative ABC-type sulfonate transport system similar to SsuA. These domains are found in eubacterial SsuA proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates, while other closest homologs are involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB). After binding the ligand, SsuA 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 SsuA 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: 270273  Cd Length: 268  Bit Score: 47.72  E-value: 3.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746  53 FLQDMEKKLGVKVN-AFFAPDYAGIIQGMRFNKVDIAWYGNLSAMeaVDRANGQvfAQTVAADGSPGYWSVLIVNKDSPI 131
Cdd:cd13555   29 WLEEEFAKDGIKVEwVFFKGAGPAVNEAFANGQIDFAVYGDLPAI--IGRAAGL--DTKLLLSSGSGNNAYLVVPPDSTI 104
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446914746 132 NNLNDLlaKRKDLTFGNGdpnstsgflVPGYYVF----AKNNISASDFKRtVNAGHETNALAVANKQVDVA 198
Cdd:cd13555  105 KSVKDL--KGKKVAVQKG---------TAWQLTFlrilAKNGLSEKDFKI-VNLDAQDAQAALASGDVDAA 163
PBP2_NrtA_SsuA_CpmA_like cd01008
Substrate binding domain of ABC-type nitrate/sulfonate/bicarbonate transporters, a member of ...
53-198 1.12e-05

Substrate binding domain of ABC-type nitrate/sulfonate/bicarbonate transporters, a member of the type 2 periplasmic binding fold superfamily; This family represents the periplasmic binding proteins involved in nitrate, alkanesulfonate, and bicarbonate transport. These domains are found in eubacterial perisplamic-binding proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates. Other closest homologs involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB) are also included in this family. After binding their ligand with high affinity, 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. These binding 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: 270229 [Multi-domain]  Cd Length: 212  Bit Score: 45.74  E-value: 1.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746  53 FLQDMEKKLGVKVNAFFAPdyAGIIQGMRFNKVDIAWYGNLSAMEAvdRANGQVFaQTVAADGSPGYWSVLIVNKDSPIN 132
Cdd:cd01008   23 LFEKEKEGIDVEWVEFTSG--PPALEALAAGSLDFGTGGDTPALLA--AAGGVPV-VLIAALSRSPNGNGIVVRKDSGIT 97
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446914746 133 NLNDLLAKRKDLTFGngdpnSTSGFLVpgYYVFAKNNISASDFKrTVNAGHETNALAVANKQVDVA 198
Cdd:cd01008   98 SLADLKGKKIAVTKG-----TTGHFLL--LKALAKAGLSVDDVE-LVNLGPADAAAALASGDVDAW 155
PBP2_Cystine_like_1 cd13713
Substrate binding domain of putative ABC transporters involved in cystine import; the type 2 ...
59-141 1.80e-04

Substrate binding domain of putative ABC transporters involved in cystine import; the type 2 periplasmic binding protein fold; This group contains uncharacterized periplasmic cystine-binding domain of ATP-binding cassette (ABC) transporters. Cystine is an oxidized dimeric form of cysteine that is required for optimal bacterial growth. In Bacillus subtilis, three ABC transporters, TcyJKLMN (YtmJKLMN), TcyABC (YckKJI), and YxeMNO are involved in uptake of cystine. Likewise, three uptake systems were identified in Salmonella enterica serovar Typhimurium, while in Escherichia coli, two transport systems seem to be involved in cystine uptake. Moreover, L-cystine limitation was shown to prevent virulence of Neisseria gonorrhoeae; thus, its L-cystine solute receptor (Ngo0372) may be suited as target for an antimicrobial vaccine. The cystine receptor belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins 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. 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 receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270431 [Multi-domain]  Cd Length: 218  Bit Score: 42.27  E-value: 1.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746  59 KKLGVKVNaFFAPDYAGIIQGMRFNKVDIawygNLSAM-------EAVDRANgqvfaqtvaadgsPGYWS--VLIVNKDS 129
Cdd:cd13713   35 KRLGVKVE-PVTTAWDGIIAGLWAGRYDI----IIGSMtiteerlKVVDFSN-------------PYYYSgaQIFVRKDS 96
                         90
                 ....*....|..
gi 446914746 130 PINNLNDLLAKR 141
Cdd:cd13713   97 TITSLADLKGKK 108
ModA COG0725
ABC-type molybdate transport system, periplasmic Mo-binding protein ModA [Inorganic ion ...
45-198 2.74e-04

ABC-type molybdate transport system, periplasmic Mo-binding protein ModA [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, periplasmic Mo-binding protein ModA is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440489 [Multi-domain]  Cd Length: 253  Bit Score: 41.78  E-value: 2.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746  45 NLKPQWTPFLQDMEKK-LGVKVNAFFAPD---YAGIIQGMRFnkvDIAWYGNLSAMEAVDRAnGQVFAQTVA--ADGSPg 118
Cdd:COG0725   34 SLKEALEELAAAFEKEhPGVKVELSFGGSgalARQIEQGAPA---DVFISADEKYMDKLAKK-GLILAGSRVvfATNRL- 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746 119 ywsVLIVNKDSP--INNLNDLlaKRKDLTFGNGDPNStsgflVP-GYY---VFAKNNISASDFKRTVNAGHETNALA-VA 191
Cdd:COG0725  109 ---VLAVPKGNPadISSLEDL--AKPGVRIAIGDPKT-----VPyGKYakeALEKAGLWDALKPKLVLGENVRQVLAyVE 178

                 ....*..
gi 446914746 192 NKQVDVA 198
Cdd:COG0725  179 SGEADAG 185
PBP2_Bug_TTT cd07012
Bug (Bordetella uptake gene) protein family of periplasmic solute-binding receptors; contains ...
118-277 8.44e-04

Bug (Bordetella uptake gene) protein family of periplasmic solute-binding receptors; contains the type 2 periplasmic binding fold; The Bug (Bordetella uptake gene) protein family is a large family of periplasmic solute-binding (PBP) proteins present in a number of bacterial species, but mainly in proteobacteria. In eubacteria, at least three families of periplasmic binding-protein dependent transporters are known: the ATP-binding cassette (ABC) transporters, the tripartite ATP-independent periplasmic transporters, and the tripartite tricarboxylate transporters (TTT). Bug proteins are the PBP components of the TTT. Their expansive expansion in proteobacteria indicates a large functional diversity. The best studied examples are Bordetella pertussis BugD, which is an aspartic acid transporter, and BugE, which is glutamate transporter.


Pssm-ID: 270234  Cd Length: 291  Bit Score: 40.53  E-value: 8.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746 118 GYWSVLIVNKDSPINNLNDLLAK-RKD---LTFGNGDPNSTSgflvpgyyvfaknNISASDFKRTvnAGHETN------- 186
Cdd:cd07012   97 TDPLVLVVNADSPYKTLAELVAAaKANpgkLTYGSAGAGSSS-------------HLAGELLAQA--AGIKLThvpykgg 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746 187 --AL-AVANKQVDVATNN-TENLD-----KLK---TSAPEKLKELkviwksPLIP-----GDPIV----WR-----KNLS 240
Cdd:cd07012  162 apALtDLLGGQVDAAFDSlSEALPqikagKLRalaVTSPERLPLL------PDVPtlaeqGLPDFevssWRglfapAGTP 235
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 446914746 241 ETTKDKIYDFFMNYGKTPEEKAVLERLGWAPFRASSD 277
Cdd:cd07012  236 PEVVAKLNAALAKALADPEVRERLAALGLEPVYLTPA 272
Imp COG2358
TRAP-type uncharacterized transport system, periplasmic component [General function prediction ...
123-198 1.25e-03

TRAP-type uncharacterized transport system, periplasmic component [General function prediction only];


Pssm-ID: 441925 [Multi-domain]  Cd Length: 303  Bit Score: 40.21  E-value: 1.25e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446914746 123 LIVNKDSPINNLNDLLAKRkdltFGNGDPNSTSGFLVPgyYVFAKNNISASDFKRtVNAGHETNALAVANKQVDVA 198
Cdd:COG2358  106 LVVRADSGIKSLADLKGKR----VSVGPPGSGTEVTAE--RLLEAAGLTYDDVKV-EYLGYGEAADALKDGQIDAA 174
SBP_bac_3 pfam00497
Bacterial extracellular solute-binding proteins, family 3; This is a sensor domain found in ...
53-219 2.21e-03

Bacterial extracellular solute-binding proteins, family 3; This is a sensor domain found in solute-binding protein family 3 members from Gram-positive bacteria, Gram-negative bacteria and archaea. It can also be found in the N-terminal of the membrane-bound lytic murein transglycosylase F (MltF) protein. This domain recognizes Nicotinate, quidalnate, pyridine-2,5-dicarboxylate and salicylate (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 425719 [Multi-domain]  Cd Length: 221  Bit Score: 38.81  E-value: 2.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746   53 FLQDMEKKLGVKVNaFFAPDYAGIIQGMRFNKVDIAWygnlSAM-------EAVDrangqvFAQTVAADGSpgywsVLIV 125
Cdd:pfam00497  28 LAKAIAKRLGVKVE-FVPVSWDGLIPALQSGKVDLII----AGMtitperaKQVD------FSDPYYYSGQ-----VILV 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746  126 NKDSPINNLNDLlakrKDLtfgngdPNSTSGfLVPGYYVFAKNNISASDFKRTVN-AGHETNALAVANKQVDVATNNTEN 204
Cdd:pfam00497  92 RKKDSSKSIKSL----ADL------KGKTVG-VQKGSTAEELLKNLKLPGAEIVEyDDDAEALQALANGRVDAVVADSPV 160
                         170
                  ....*....|....*
gi 446914746  205 LDKLKTSAPEKLKEL 219
Cdd:pfam00497 161 AAYLIKKNPGLNLVV 175
NMT1 pfam09084
NMT1/THI5 like; This family contains the NMT1 and THI5 proteins. These proteins are proposed ...
59-250 2.86e-03

NMT1/THI5 like; This family contains the NMT1 and THI5 proteins. These proteins are proposed to be required for the biosynthesis of the pyrimidine moiety of thiamine.3]. They are regulated by thiamine. The protein adopts a fold related to the periplasmic binding protein (PBP) family. Both pyridoxal-5'-phosphate (PLP) and an iron atom are bound to the protein suggesting numerous residues of the active site necessary for HMP-P biosynthesis. The yeast protein is a dimer and, although exceptionally using PLP as a substrate, has notable similarities with enzymes dependent on this molecule as a cofactor.


Pssm-ID: 430398 [Multi-domain]  Cd Length: 216  Bit Score: 38.36  E-value: 2.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746   59 KKLGVKVNAFFAPDYAGIIQGMRFNKVDIAWYGNLSAMEAVDR-----ANGQVFAQTVAAdgspgywsvLIVNKDSPINN 133
Cdd:pfam09084  17 KEEGLDVEIVEPADPSDATQLVASGKADFGVSYQESVLLARAKglpvvSVAALIQHPLSG---------VISLKDSGIKS 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746  134 LNDLLAKRkdltFG-NGDPNSTSGFLVpgyyVFAKNNISASDFKrTVNAGHETNALAVANKQVDVATNNTENLDKLktSA 212
Cdd:pfam09084  88 PKDLKGKR----IGySGSPFEEALLKA----LLKKDGGDPDDVT-IVNVGGMNLFPALLTGKVDAAIGGYYNWEGV--EL 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 446914746  213 PEKLKELKVI----WKSPLIPGDPIVWRKNLSETTKDKIYDF 250
Cdd:pfam09084 157 KLEGVELNIFaladYGVPDYYSLVLITNEAFLKENPELVRAF 198
PBP2_TAXI_TRAP cd13520
Substrate binding domain of TAXI proteins of the tripartite ATP-independent periplasmic ...
123-198 4.69e-03

Substrate binding domain of TAXI proteins of the tripartite ATP-independent periplasmic transporters; the type 2 periplasmic binding protein fold; This group includes Thermus thermophilus GluBP (TtGluBP) of TAXI-TRAP family and closely related proteins. TRAP transporters are ubiquitous in prokaryotes, but absent from eukaryotes. They are comprised of an SBP (substrate-binding protein) of the DctP or TAXI families and two unequally sized integral membrane components. Although TtGluBP is predicted to be an L-glutamate and/or an L-glutamine-binding protein, the substrate spectrum of TAXI proteins remains to be defined. A sequence-homology search also shows that TtGluBP shares low sequence homology with putative immunogenic proteins of uncharacterized function. The substrate-binding domain of TAXI proteins belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises 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. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and tworeceptor cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270238 [Multi-domain]  Cd Length: 285  Bit Score: 38.37  E-value: 4.69e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446914746 123 LIVNKDSPINNLNDLLAKRkdltFGNGDPNSTSGFLVPgyYVFAKNNISASDFKRtVNAGHETNALAVANKQVDVA 198
Cdd:cd13520   94 LVVRKDSGIKSIADLKGKR----VAVGPPGSGTELTAR--RLLEAYGLTDDDVKA-EYLGLSDAADALKDGQIDAF 162
PBP2_SsuA_like_1 cd13556
Substrate binding domain of putative sulfonate binding protein, a member of the type 2 ...
54-196 5.12e-03

Substrate binding domain of putative sulfonate binding protein, a member of the type 2 periplasmic binding fold superfamily; This subfamily includes the periplasmic component of putative ABC-type sulfonate transport system similar to SsuA. These domains are found in eubacterial SsuA proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates, while other closest homologs are involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB). After binding the ligand, SsuA 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 SsuA 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: 270274  Cd Length: 265  Bit Score: 38.22  E-value: 5.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746  54 LQDMEKKLGVKVNAFFAPDYAGIIQGMRFNKVDIAWYGNLSAMEAvdRANGQ------VFaqtvaadgSPGYWSVLIVNK 127
Cdd:cd13556   22 LEKEFQKDGVKVTWVLSQGSNKALEFLNSGSVDFGSTAGLAALLA--KANGNpiktvyVY--------SRPEWTALVVRK 91
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446914746 128 DSPINNLNDLLAKRKDLTFGNgDPnstsgflvpgyYVF-----AKNNISASDFkRTVNAGHETNALAVANKQVD 196
Cdd:cd13556   92 DSPIRSVADLKGKKVAVTKGT-DP-----------YIFllralNTAGLSKNDI-EIVNLQHADGRTALEKGDVD 152
PBP2_transferrin cd13529
Transferrin family of the type 2 periplasmic-binding protein superfamily; Transferrins are ...
77-171 6.63e-03

Transferrin family of the type 2 periplasmic-binding protein superfamily; Transferrins are iron-binding blood plasma glycoproteins that regulate the level of free iron in biological fluids. Vertebrate transferrins are made of a single polypeptide chain with a molecular weight of about 80 kDa. The polypeptide is folded into two homologous lobes (the N-lobe and C-lobe), and each lobe is further subdivided into two similar alpha helical and beta sheet domains separated by a deep cleft that forms the binding site for ferric iron. Thus, the transferrin protein contains two homologous metal-binding sites with high affinities for ferric iron. The modern transferrin proteins are thought to be evolved from an ancestral gene coding for a protein of 40 kDa containing a single binding site by means of a gene duplication event. Vertebrate transferrins are found in a variety of bodily fluids, including serum transferrins, ovotransferrins, lactoferrins, and melanotransferrins. Transferrin-like proteins are also found in the circulatory fluid of certain invertebrates. The transferrins have the same structural fold as the type 2 periplasmic-binding proteins, many of which are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor.


Pssm-ID: 270247  Cd Length: 298  Bit Score: 37.77  E-value: 6.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746  77 IQGMRFNKVDIawyGNLSAMEAVdRANGQ-----VFAQTVAADGSPGYWSVLIVNKDSPINNLNDLLAKRKDLTfGNGdp 151
Cdd:cd13529   43 MKAIKNGTADF---VTLDGGDVY-TAGKDynlkpIAAELYGDEGEASYYAVAVVKKSSNITSLKDLRGKKSCHT-GYG-- 115
                         90       100
                 ....*....|....*....|
gi 446914746 152 nSTSGFLVPGYYVFAKNNIS 171
Cdd:cd13529  116 -RTAGWNVPIGYLLENGLIS 134
PBP2_ModA_like cd00993
Substrate binding domain of molybdate-binding proteins, the type 2 periplasmic binding protein ...
122-269 7.86e-03

Substrate binding domain of molybdate-binding proteins, the type 2 periplasmic binding protein fold; Molybdate binding domain ModA. Molybdate transport system is comprised of a periplasmic binding protein, an integral membrane protein, and an energizer protein. These three proteins are coded by modA, modB, and modC genes, respectively. ModA proteins serve as initial receptors in the ABC transport of molybdate mostly in eubacteria and archaea. Bacteria and archaea import molybdenum and tungsten from the environment in the form of the oxyanions molybdate (MoO(4) (2-)) and tungstate (WO(4) (2-)). After binding molybdate with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. In contrast to the structure of the two ModA homologs from Escherichia coli and Azotobacter vinelandii, where the oxygen atoms are tetrahedrally arranged around the metal center, the structure of Pyrococcus furiosus ModA/WtpA (PfModA) has revealed a binding site for molybdate and tungstate where the central metal atom is in a hexacoordinate configuration. This octahedral geometry was rather unexpected. The ModA 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: 270215 [Multi-domain]  Cd Length: 225  Bit Score: 37.32  E-value: 7.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446914746 122 VLIVNKDSPINNLNDL-LAKRKDLTFGNGDPNStsgflVP-GYY---VFAKNNISASDFKRTVNAGHETNALA-VANKQV 195
Cdd:cd00993   83 VLVVPKASPVSGTPLLeLALDEGGRIAVGDPQS-----VPaGRYakqVLEKLGLWDKLPPKLVEAPDVRQVLGlVESGEA 157
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446914746 196 DV----ATNNTenldklktsapeKLKELKVIWKSPLIPGDPIVWRKNLSETTKDK-IYDFFMNYGKTPEEKAVLERLGW 269
Cdd:cd00993  158 DAgfvyASDAL------------AAKKVKVVATLPEDLHEPIVYPVAVLKGSKNKaEAKAFLDFLLSPEGQRIFERYGF 224
NMT1_3 pfam16868
NMT1-like family;
123-199 8.54e-03

NMT1-like family;


Pssm-ID: 435616 [Multi-domain]  Cd Length: 289  Bit Score: 37.61  E-value: 8.54e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446914746  123 LIVNKDSPINNLNDLLAKRkdltFGNGDPNstSGFLVPGYYVFAKNNISASDFKRTVNAGHETNALAVANKQVDVAT 199
Cdd:pfam16868  95 FVVSKDSGIGSIADLKGKR----VSVGPPG--SGTEGSTRAILGALGISYKDLSLLEYLGYGESADALKDGQLDGAF 165
 
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