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Conserved domains on  [gi|504820154|ref|WP_015007256|]
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spermidine/putrescine ABC transporter substrate-binding protein [Sinorhizobium meliloti]

Protein Classification

spermidine/putrescine ABC transporter substrate-binding protein( domain architecture ID 10194417)

spermidine/putrescine ABC transporter substrate-binding protein serves as a primary receptor for the active transport of polyamines; preferentially binds spermidine, but also binds putrescine

CATH:  3.40.190.10
Gene Ontology:  GO:0140359|GO:0042626|GO:0055052|GO:0019808|GO:0015846
PubMed:  26517916|24638992|25750732
TCDB:  3.A.1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PBP2_PotD_PotF_like cd13590
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ...
 24-339 3.46e-92

The periplasmic-binding component of ABC transporters involved in uptake of polyamines; possess the type 2 periplasmic binding fold; This family represents the periplasmic substrate-binding domain that functions as the primary high-affinity receptors of ABC-type polyamine transport systems. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is 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.


:

Pssm-ID: 270308 [Multi-domain]  Cd Length: 315  Bit Score: 277.96  E-value: 3.46e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154  24 TLNLLIWEDYIDEGLIDRWTEKTGVSIRQINFDSDD-ARDEILADPGRNIDLVIVDENGATLFGRKGIIEPLSETNLPAL 102
Cdd:cd13590    1 ELNIYNWSDYIDPEVLKAFEKETGVKVNYDTYDSNEeMLAKLRAGGGSGYDLVVPSDYMVERLIKQGLLEPLDHSKLPNL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 103 EDYAPEWRKS----CAGYGLPYFWGTVGILYRSDVVTPPPTSWrDMMRPAPALRKHIAMFADHSEIFVPPLMLLGASVNA 178
Cdd:cd13590   81 KNLDPQFLNPpydpGNRYSVPYQWGTTGIAYNKDKVKEPPTSW-DLDLWDPALKGRIAMLDDAREVLGAALLALGYSPNT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 179 DDTPTLKAAFALLKTQAPFVLTYDYvvTSIQDPALAGNIYLALGYSGDQHVLNSKAGKaglWRYSVPKEGTLSWLDCFSV 258
Cdd:cd13590  160 TDPAELAAAAELLIKQKPNVRAFDS--DSYVQDLASGEIWLAQAWSGDALQANRENPN---LKFVIPKEGGLLWVDNMAI 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 259 TAASPRKQRALEFLNFIGSPEAAAANAIALNMPTASNAALKLLPDTMRSDPEIYPPTEIMAKNQHHQELSVRSIEARRRI 338
Cdd:cd13590  235 PKGAPNPELAHAFINFLLDPEVAAKNAEYIGYATPNKAALELLPPELLDNPALYPPIEPLAKLLTFKDVDGEALELYDRI 314


                 .
gi 504820154 339 I 339
Cdd:cd13590  315 W 315
 
Name Accession Description Interval E-value
PBP2_PotD_PotF_like cd13590
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ...
 24-339 3.46e-92

The periplasmic-binding component of ABC transporters involved in uptake of polyamines; possess the type 2 periplasmic binding fold; This family represents the periplasmic substrate-binding domain that functions as the primary high-affinity receptors of ABC-type polyamine transport systems. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is 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.


Pssm-ID: 270308 [Multi-domain]  Cd Length: 315  Bit Score: 277.96  E-value: 3.46e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154  24 TLNLLIWEDYIDEGLIDRWTEKTGVSIRQINFDSDD-ARDEILADPGRNIDLVIVDENGATLFGRKGIIEPLSETNLPAL 102
Cdd:cd13590    1 ELNIYNWSDYIDPEVLKAFEKETGVKVNYDTYDSNEeMLAKLRAGGGSGYDLVVPSDYMVERLIKQGLLEPLDHSKLPNL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 103 EDYAPEWRKS----CAGYGLPYFWGTVGILYRSDVVTPPPTSWrDMMRPAPALRKHIAMFADHSEIFVPPLMLLGASVNA 178
Cdd:cd13590   81 KNLDPQFLNPpydpGNRYSVPYQWGTTGIAYNKDKVKEPPTSW-DLDLWDPALKGRIAMLDDAREVLGAALLALGYSPNT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 179 DDTPTLKAAFALLKTQAPFVLTYDYvvTSIQDPALAGNIYLALGYSGDQHVLNSKAGKaglWRYSVPKEGTLSWLDCFSV 258
Cdd:cd13590  160 TDPAELAAAAELLIKQKPNVRAFDS--DSYVQDLASGEIWLAQAWSGDALQANRENPN---LKFVIPKEGGLLWVDNMAI 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 259 TAASPRKQRALEFLNFIGSPEAAAANAIALNMPTASNAALKLLPDTMRSDPEIYPPTEIMAKNQHHQELSVRSIEARRRI 338
Cdd:cd13590  235 PKGAPNPELAHAFINFLLDPEVAAKNAEYIGYATPNKAALELLPPELLDNPALYPPIEPLAKLLTFKDVDGEALELYDRI 314


                 .
gi 504820154 339 I 339
Cdd:cd13590  315 W 315
PotD COG0687
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
1-342 5.43e-82

Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];


Pssm-ID: 440451 [Multi-domain]  Cd Length: 348  Bit Score: 252.91  E-value: 5.43e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154   1 MKARGVISVFLATLLCA------SASRAETLNLLIWEDYIDEGLIDRWTEKTGVSIRQINFDSDDARDEILADPGRNIDL 74
Cdd:COG0687    1 MSRRSLLGLAAAALAAAlaggapAAAAEGTLNVYNWGGYIDPDVLEPFEKETGIKVVYDTYDSNEEMLAKLRAGGSGYDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154  75 VIVDENGATLFGRKGIIEPLSETNLPALEDYAPEWRKS----CAGYGLPYFWGTVGILYRSDVVTPPPTSWRDMMRPApa 150
Cdd:COG0687   81 VVPSDYFVARLIKAGLLQPLDKSKLPNLANLDPRFKDPpfdpGNVYGVPYTWGTTGIAYNTDKVKEPPTSWADLWDPE-- 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 151 LRKHIAMFADHSEIFVPPLMLLGASVNADDTPTLKAAFALLKTQAPFVLTYDYVVTSIQDPALAGNIYLALGYSGDQHVL 230
Cdd:COG0687  159 YKGKVALLDDPREVLGAALLYLGYDPNSTDPADLDAAFELLIELKPNVRAFWSDGAEYIQLLASGEVDLAVGWSGDALAL 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 231 NSKAGKaglWRYSVPKEGTLSWLDCFSVTAASPRKQRALEFLNFIGSPEAAAANAIALNMPTASNAALKLLPDTMRSDPE 310
Cdd:COG0687  239 RAEGPP---IAYVIPKEGALLWFDNMAIPKGAPNPDLAYAFINFMLSPEVAAALAEYVGYAPPNKAARELLPPELAANPA 315

                        330       340       350
                 ....*....|....*....|....*....|..
gi 504820154 311 IYPPTEIMAKNQHHQELSVRSIEARRRIINTL 342
Cdd:COG0687  316 IYPPEEVLDKLEFWNPLPPENRELYTRRWTEI 347
PRK10682 PRK10682
putrescine transporter subunit: periplasmic-binding component of ABC superfamily; Provisional
 6-320 2.78e-33

putrescine transporter subunit: periplasmic-binding component of ABC superfamily; Provisional


Pssm-ID: 182645 [Multi-domain]  Cd Length: 370  Bit Score: 126.50  E-value: 2.78e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154   6 VISVFLATLLCASASRAETLNLLIWEDYIDEGLIDRWTEKTGVSIRQINFDSDDARDEILADPGRNIDLVIvdeNGATLF 85
Cdd:PRK10682  13 VAGALMAVSVGTLAAEQKTLHIYNWSDYIAPDTVANFEKETGIKVVYDVFDSNEVLEGKLMAGSTGFDLVV---PSASFL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154  86 GRK---GIIEPLSETNLPALEDYAPEWRKSCA------GYGLPYFWGTVGILYRSDVVTP------PPTSWRDMMRPA-- 148
Cdd:PRK10682  90 ERQltaGVFQPLDKSKLPNWKNLDPELLKLVAkhdpdnKYAMPYMWATTGIGYNVDKVKAvlgedaPVDSWDLVLKPEnl 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 149 PALRKHIAMFADH-SEIFVPPLMLLGASVNADDTPTL-KAAFALLKTQAPFVLtYDYVVTSIQDPAlAGNIYLALGYSGD 226
Cdd:PRK10682 170 EKLKSCGVSFLDApEEIFATVLNYLGKDPNSTKADDYtGPATDLLLKLRPNIR-YFHSSQYINDLA-NGDICVAIGWAGD 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 227 --QHVLNSKAGKAGL-WRYSVPKEGTLSWLDCFSVTAASPRKQRALEFLNFIGSPEAAAANAIALNMPTASNAALKLLPD 303
Cdd:PRK10682 248 vwQASNRAKEAKNGVnVSYSIPKEGALAFFDVFAMPADAKNKDEAYQFLNYLLRPDVIAHISDHVFYANANKAATPLVSA 327

                        330
                 ....*....|....*..
gi 504820154 304 TMRSDPEIYPPTEIMAK 320
Cdd:PRK10682 328 EVRDNPGIYPPADVRAK 344
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 38-311 5.16e-23

Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 96.71  E-value: 5.16e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154   38 LIDRWTEKTGVSIRQINFDSDDARDEILADP--GRNIDLVIVDENGATL--FGRKGIIEPLSET-NLPALEDYAPEWRKS 112
Cdd:pfam13416   2 LAKAFEKKTGVTVEVEPQASNDLQAKLLAAAaaGNAPDLDVVWIAADQLatLAEAGLLADLSDVdNLDDLPDALDAAGYD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154  113 CAGYGLPYFWGTVGIL-YRSDVVT---PPPTSWRDMMRPAPALRKHIAMFADHSEIFVPPLMLLGASVNADD--TPTLKA 186
Cdd:pfam13416  82 GKLYGVPYAASTPTVLyYNKDLLKkagEDPKTWDELLAAAAKLKGKTGLTDPATGWLLWALLADGVDLTDDGkgVEALDE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154  187 AFALLKTQAPFVLTYDYVVTSIQDPAlAGNIYLALGYSGDQhVLNSKAGKAglWRYSVPKEGTLSWLDCFSVTAASP-RK 265
Cdd:pfam13416 162 ALAYLKKLKDNGKVYNTGADAVQLFA-NGEVAMTVNGTWAA-AAAKKAGKK--LGAVVPKDGSFLGGKGLVVPAGAKdPR 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 504820154  266 QRALEFLNFIGSPEAAAANAIALNMPTASNAAlkLLPDTMRSDPEI 311
Cdd:pfam13416 238 LAALDFIKFLTSPENQAALAEDTGYIPANKSA--ALSDEVKADPAL 281
 
Name Accession Description Interval E-value
PBP2_PotD_PotF_like cd13590
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ...
 24-339 3.46e-92

The periplasmic-binding component of ABC transporters involved in uptake of polyamines; possess the type 2 periplasmic binding fold; This family represents the periplasmic substrate-binding domain that functions as the primary high-affinity receptors of ABC-type polyamine transport systems. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is 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.


Pssm-ID: 270308 [Multi-domain]  Cd Length: 315  Bit Score: 277.96  E-value: 3.46e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154  24 TLNLLIWEDYIDEGLIDRWTEKTGVSIRQINFDSDD-ARDEILADPGRNIDLVIVDENGATLFGRKGIIEPLSETNLPAL 102
Cdd:cd13590    1 ELNIYNWSDYIDPEVLKAFEKETGVKVNYDTYDSNEeMLAKLRAGGGSGYDLVVPSDYMVERLIKQGLLEPLDHSKLPNL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 103 EDYAPEWRKS----CAGYGLPYFWGTVGILYRSDVVTPPPTSWrDMMRPAPALRKHIAMFADHSEIFVPPLMLLGASVNA 178
Cdd:cd13590   81 KNLDPQFLNPpydpGNRYSVPYQWGTTGIAYNKDKVKEPPTSW-DLDLWDPALKGRIAMLDDAREVLGAALLALGYSPNT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 179 DDTPTLKAAFALLKTQAPFVLTYDYvvTSIQDPALAGNIYLALGYSGDQHVLNSKAGKaglWRYSVPKEGTLSWLDCFSV 258
Cdd:cd13590  160 TDPAELAAAAELLIKQKPNVRAFDS--DSYVQDLASGEIWLAQAWSGDALQANRENPN---LKFVIPKEGGLLWVDNMAI 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 259 TAASPRKQRALEFLNFIGSPEAAAANAIALNMPTASNAALKLLPDTMRSDPEIYPPTEIMAKNQHHQELSVRSIEARRRI 338
Cdd:cd13590  235 PKGAPNPELAHAFINFLLDPEVAAKNAEYIGYATPNKAALELLPPELLDNPALYPPIEPLAKLLTFKDVDGEALELYDRI 314


                 .
gi 504820154 339 I 339
Cdd:cd13590  315 W 315
PotD COG0687
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
1-342 5.43e-82

Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];


Pssm-ID: 440451 [Multi-domain]  Cd Length: 348  Bit Score: 252.91  E-value: 5.43e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154   1 MKARGVISVFLATLLCA------SASRAETLNLLIWEDYIDEGLIDRWTEKTGVSIRQINFDSDDARDEILADPGRNIDL 74
Cdd:COG0687    1 MSRRSLLGLAAAALAAAlaggapAAAAEGTLNVYNWGGYIDPDVLEPFEKETGIKVVYDTYDSNEEMLAKLRAGGSGYDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154  75 VIVDENGATLFGRKGIIEPLSETNLPALEDYAPEWRKS----CAGYGLPYFWGTVGILYRSDVVTPPPTSWRDMMRPApa 150
Cdd:COG0687   81 VVPSDYFVARLIKAGLLQPLDKSKLPNLANLDPRFKDPpfdpGNVYGVPYTWGTTGIAYNTDKVKEPPTSWADLWDPE-- 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 151 LRKHIAMFADHSEIFVPPLMLLGASVNADDTPTLKAAFALLKTQAPFVLTYDYVVTSIQDPALAGNIYLALGYSGDQHVL 230
Cdd:COG0687  159 YKGKVALLDDPREVLGAALLYLGYDPNSTDPADLDAAFELLIELKPNVRAFWSDGAEYIQLLASGEVDLAVGWSGDALAL 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 231 NSKAGKaglWRYSVPKEGTLSWLDCFSVTAASPRKQRALEFLNFIGSPEAAAANAIALNMPTASNAALKLLPDTMRSDPE 310
Cdd:COG0687  239 RAEGPP---IAYVIPKEGALLWFDNMAIPKGAPNPDLAYAFINFMLSPEVAAALAEYVGYAPPNKAARELLPPELAANPA 315

                        330       340       350
                 ....*....|....*....|....*....|..
gi 504820154 311 IYPPTEIMAKNQHHQELSVRSIEARRRIINTL 342
Cdd:COG0687  316 IYPPEEVLDKLEFWNPLPPENRELYTRRWTEI 347
PBP2_PotF cd13659
The periplasmic substrate-binding component of an ABC putrescine transport system and related ...
 24-320 2.31e-46

The periplasmic substrate-binding component of an ABC putrescine transport system and related proteins; contains the type 2 periplasmic-binding fold; This group represents the periplasmic substrate-binding domain that serves as the primary polyamine receptor of ABC-type putrescine-preferential transporter from gram-negative bacteria. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is 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.


Pssm-ID: 270377 [Multi-domain]  Cd Length: 331  Bit Score: 160.19  E-value: 2.31e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154  24 TLNLLIWEDYIDEGLIDRWTEKTGVSIRQINFDSDDARDEILADPGRNIDLVIVDENGATLFGRKGIIEPLSETNLPALE 103
Cdd:cd13659    1 TLNVYNWSDYIAPDTLEDFEKETGIKVVYDTYDSNEELEAKLLAGGSGYDLVVPSANFLGRQIKAGALQKLDKSKLPNWK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 104 DYAPEWRKSCAG------YGLPYFWGTVGILYRSDVV-----TPPPTSWRDMMRPAPALRKH---IAMFADHSEIFVPPL 169
Cdd:cd13659   81 NLDPLLLKLLAAvdpgnrYAVPYMWGTTGIAYNVDKVkaalgDDLPDSWDLVFDPENLSKLKscgVSVLDSPEEVFPAAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 170 MLLGASVNADDTPTLKAAFALLKTQAPFVltyDYVVTSIQDPALA-GNIYLALGYSGDQHVLNSKAGKAGL---WRYSVP 245
Cdd:cd13659  161 NYLGLDPNSTDPEDIKAAEDLLKKVRPYV---RYFHSSKYINDLAnGEICVAIGWSGDAVQAAQRAKEAGNgvtLEYVIP 237

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504820154 246 KEGTLSWLDCFSVTAASPRKQRALEFLNFIGSPEAAAANAIALNMPTASNAALKLLPDTMRSDPEIYPPTEIMAK 320
Cdd:cd13659  238 KEGANLWFDMFAIPADAKNPDNAYRFINYLMRPEVIAKISNYVNYANANKAATPLVDEAIKDDPAIYPPEEVLKK 312
PBP2_PotD_PotF_like_3 cd13664
TThe periplasmic substrate-binding component of an uncharacterized active transport system ...
 24-338 9.46e-42

TThe periplasmic substrate-binding component of an uncharacterized active transport system closely related to spermidine and putrescine transporters; contains the type 2 periplasmic binding fold; This family represents the periplasmic substrate-binding domain that functions as the primary high-affinity receptors of ABC-type polyamine transport systems. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is 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.


Pssm-ID: 270382 [Multi-domain]  Cd Length: 315  Bit Score: 147.89  E-value: 9.46e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154  24 TLNLLIWEDYIDEGLIDRWTEKTGVSIRQINFDSDDARDEILADPGRNIDLVIVDENGATLFGRKGIIEPLSETNLPALE 103
Cdd:cd13664    1 ELNLYNWTDYTSPELLDKFEKETGIKVTLDTYDSNETLLAKLKAGGQGYDVVVPSDSFVPILIKEGLLEPLDKSQLTNYD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 104 DYAPEWRKSCAG----YGLPYFWGTVGILYRSDVVTPPPTSWRDMMRPAPALRKHIAMFADHSEIFVPPLMLLGASVNAD 179
Cdd:cd13664   81 NIDPRWRKPDFDpgneYSIPWQWGTTGFAVDTAVYDGDIDDYSVIFQPPEELKGKIAMVDSMNEVVNAAIYYLGGPICTT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 180 DTPTLKAAFALLKTQAPFVLTYDYvvTSIQDPALAGNIYLALGYSGDQHVLNSKagKAGLwRYSVPKEGTLSWLDCFSVT 259
Cdd:cd13664  161 DPKLMRKVRDLLLEQKPHVKAYDS--DGIVERMASGDVAAHVDWNGASLRARRQ--NPSL-AYAYPKEGVLIWSDNLVIP 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 260 AASPRKQRALEFLNFIGSPEaaaanaialNMPTASNAAL---------KLLPDTMRSDPEIYPPTEIMAKNQHHQELSVR 330
Cdd:cd13664  236 KGAPNYENARTFLNFIMEPE---------NAALQSNFAGyanaitgaeKFMDDPLKDAPALEIPPPEGSRLKFSTLCPPK 306


                 ....*...
gi 504820154 331 SIEARRRI 338
Cdd:cd13664  307 AEKLQSRI 314
PBP2_PotD cd13660
The periplasmic substrate-binding component of an active spermidine-preferential transport ...
 24-320 1.45e-37

The periplasmic substrate-binding component of an active spermidine-preferential transport system; contains the type 2 periplasmic binding fold; This group represents the periplasmic binding domain that serves as the primary polyamine receptor of ABC-type spermindine-preferential transport system from gram-negative bacteria. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is 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.


Pssm-ID: 270378 [Multi-domain]  Cd Length: 315  Bit Score: 136.94  E-value: 1.45e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154  24 TLNLLIWEDYIDEGLIDRWTEKTGVsirQINFDSDDARDEILAD----PGRNIDLVIVDENGATLFGRKGIIEPLSETNL 99
Cdd:cd13660    1 TLNFYNWSEYVPPELLEQFTKETGI---KVILSTYESNETMYAKvklyKDGAYDLVVPSTYYVDKMRKEGLIQKIDKSKI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 100 PALEDYAPEWRKSC----AGYGLPYFWGTVGILYRSDVVTPPP-TSWRDMMRPApaLRKHIAMFADHSEIFVPPLMLLGA 174
Cdd:cd13660   78 TNFSNIDPDFLNQPfdpnNDYSIPYIWGATALAVNGDAVDGKSvTSWADLWKPE--YKGKLLLTDDAREVFQMALRKLGY 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 175 SVNADDTPTLKAAFALLKTQAPFVLTYDYvvTSIQDPALAGNIYLALGYSGDQHVLNsKAGKAglWRYSVPKEGTLSWLD 254
Cdd:cd13660  156 SGNTKDPEEIEAAFEELKKLMPNVAAFDS--DNPANPYMEGEVALGMIWNGSAFVAR-QANKP--IHVVWPKEGGIFWMD 230

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504820154 255 CFSVTAASPRKQRALEFLNFIGSPEAAAANAIALNMPTASNAALKLLPDTMRSDPEIYPPTEIMAK 320
Cdd:cd13660  231 SFAIPANAKNKEGALKFINFLLRPDVSKQIAETIGYPTPNLKARKLLSPEVANNKIVYPSAETIKN 296
PBP2_PotD_PotF_like_2 cd13663
The periplasmic substrate-binding component of an uncharacterized active transport system ...
 24-320 2.18e-35

The periplasmic substrate-binding component of an uncharacterized active transport system closely related to spermidine and putrescine transporters; contains the type 2 periplasmic binding fold; This group represents the periplasmic substrate-binding domain that serves as a primary polyamine receptor of an uncharacterized ABC-type transport system from gram-negative bacteria. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, as well as plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is 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.


Pssm-ID: 270381 [Multi-domain]  Cd Length: 323  Bit Score: 131.26  E-value: 2.18e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154  24 TLNLLIWEDYIDEGLIDRWTEKTGVSIRQINFDSDDARDEILADPGRNIDLVIVDENGATLFGRKGIIEPLSETNLPALE 103
Cdd:cd13663    1 TLKVYNWGEYIDPDLIDDFEKETGIKVNYETFDSNEEMYTKIKTGGTSYDVIVPSDYMIEKLIKEDLLQPLDYSKLPNVD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 104 --DYAPEWRKSCAG-----YGLPYFWGTVGILYRSDVVTPPPTSWRDMMrPAPALRKHIAMFADHSEIFVPPLMLLGASV 176
Cdd:cd13663   81 knINIQPDLLNLAFdpineYSVPYFWGTLGIVYNKTKVSLEELSWWNIL-WNKKYKGKILMYDSPRDAFMVALKALGYSL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 177 NADDTPTLKAAFALLKTQAPFVltYDYVVTSIQDPALAGNIYLALGYSGDQHVLNSKAGKaglWRYSVPKEGTLSWLDCF 256
Cdd:cd13663  160 NTTNPDEIEEAKDWLIKQKPNV--KAFVVDEIKDLMINGNADIAVTYSGDAAYAMEENEN---LDYVIPKEGSNLWFDNW 234

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504820154 257 SVTAASPRKQRALEFLNFIGSPEAAAANAIALNMPTASNAALKLLP--DTMRSDPEIYPPTEIMAK 320
Cdd:cd13663  235 VIPKNAKNVDLAYKFINFLLRPDNALKNAEYVGYSTPNAAAEELLPeeESIKDDKIFYPDEDIYKK 300
PBP2_polyamine_1 cd13588
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ...
 24-279 4.39e-34

The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of polyamines; contains the type 2 periplasmic binding fold; This group represents the periplasmic binding domain that functions as the primary high-affinity receptor of an uncharactertized ABC-type polyamine transport system. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is 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.


Pssm-ID: 270306 [Multi-domain]  Cd Length: 279  Bit Score: 126.64  E-value: 4.39e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154  24 TLNLLIWEDYIDEGLIDRWTEKTGVSIRQINFDSDDardEILA---DPGRNIDLVIVDENGATLFGRKGIIEPLSETNLP 100
Cdd:cd13588    1 ELNVLTWPGYADPDWVTAFEEATGCKVVVKFFGSED---EMVAklrSGGGDYDVVTPSGDALLRLIAAGLVQPIDTSKIP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 101 ALEDYAPEWRKSCAG------YGLPYFWGTVGILYRSDVVTPPPTSWRDMMrPAPALRKHIAMFADHSEIFVPPLMLLGA 174
Cdd:cd13588   78 NYANIDPRLRNLPWLtvdgkvYGVPYDWGANGLAYNTKKVKTPPTSWLALL-WDPKYKGRVAARDDPIDAIADAALYLGQ 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 175 SVNADDTPT-LKAAFALLKTQAPFVLTYDYVVTSIQDPALAGNIYLALGYSGDQHVLnSKAGKAGlwRYSVPKEGTLSWL 253
Cdd:cd13588  157 DPPFNLTDEqLDAVKAKLREQRPLVRKYWSDGAELVQLFANGEVVAATAWSGQVNAL-QKAGKPV--AYVIPKEGATGWV 233

                        250       260
                 ....*....|....*....|....*.
gi 504820154 254 DCFSVTAASPRKQRALEFLNFIGSPE 279
Cdd:cd13588  234 DTWMILKDAKNPDCAYKWLNYMLSPK 259
PRK10682 PRK10682
putrescine transporter subunit: periplasmic-binding component of ABC superfamily; Provisional
 6-320 2.78e-33

putrescine transporter subunit: periplasmic-binding component of ABC superfamily; Provisional


Pssm-ID: 182645 [Multi-domain]  Cd Length: 370  Bit Score: 126.50  E-value: 2.78e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154   6 VISVFLATLLCASASRAETLNLLIWEDYIDEGLIDRWTEKTGVSIRQINFDSDDARDEILADPGRNIDLVIvdeNGATLF 85
Cdd:PRK10682  13 VAGALMAVSVGTLAAEQKTLHIYNWSDYIAPDTVANFEKETGIKVVYDVFDSNEVLEGKLMAGSTGFDLVV---PSASFL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154  86 GRK---GIIEPLSETNLPALEDYAPEWRKSCA------GYGLPYFWGTVGILYRSDVVTP------PPTSWRDMMRPA-- 148
Cdd:PRK10682  90 ERQltaGVFQPLDKSKLPNWKNLDPELLKLVAkhdpdnKYAMPYMWATTGIGYNVDKVKAvlgedaPVDSWDLVLKPEnl 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 149 PALRKHIAMFADH-SEIFVPPLMLLGASVNADDTPTL-KAAFALLKTQAPFVLtYDYVVTSIQDPAlAGNIYLALGYSGD 226
Cdd:PRK10682 170 EKLKSCGVSFLDApEEIFATVLNYLGKDPNSTKADDYtGPATDLLLKLRPNIR-YFHSSQYINDLA-NGDICVAIGWAGD 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 227 --QHVLNSKAGKAGL-WRYSVPKEGTLSWLDCFSVTAASPRKQRALEFLNFIGSPEAAAANAIALNMPTASNAALKLLPD 303
Cdd:PRK10682 248 vwQASNRAKEAKNGVnVSYSIPKEGALAFFDVFAMPADAKNKDEAYQFLNYLLRPDVIAHISDHVFYANANKAATPLVSA 327

                        330
                 ....*....|....*..
gi 504820154 304 TMRSDPEIYPPTEIMAK 320
Cdd:PRK10682 328 EVRDNPGIYPPADVRAK 344
PBP2_polyamines cd13523
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ...
 24-279 2.62e-32

The periplasmic-binding component of ABC transporters involved in uptake of polyamines; possess the type 2 periplasmic binding fold; This family represents the periplasmic substrate-binding proteins that function as the primary high-affinity receptors of ABC-type polyamine transport systems. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, as well as plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is 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.


Pssm-ID: 270241 [Multi-domain]  Cd Length: 268  Bit Score: 121.39  E-value: 2.62e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154  24 TLNLLIWEDYIDEGLIDRWTEKTGVSIRQINFDSDDARDEILADPGR-NIDLVIVDENGATLFGRKGIIEPLSETNLPAL 102
Cdd:cd13523    1 TVVIYTWGGYLPQDIIDPFEKETGIKVVVDTAANSERMIKKLSAGGSgGFDLVTPSDSYTSRQLGVGLMQPIDKSLLPSW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 103 EDYAPEWRKSCA------GYGLPYFWGTVGILYRSDVVTPPPTSWRDMMRpAPALRKHIAMFADHSEIFVPPLMLLGASV 176
Cdd:cd13523   81 ATLDPHLTLAAVltvpgkKYGVPYQWGATGLVYNTDKVKAPPKSYAADLD-DPKYKGRVSFSDIPRETFAMALANLGADG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 177 NADDTPT-LKAAFALLKTQAPFVLTYDYVVTSIQDPALAGNIYLALGYSGDQHVLNSKAGKAGLwrySVPKEGTLSWLDC 255
Cdd:cd13523  160 NEELYPDfTDAAAALLKELKPNVKKYWSNASQPANLLLNGEVVLAMAWLGSGFKLKQAGAPIEF---VVPKEGAVGWLDT 236

                        250       260
                 ....*....|....*....|....
gi 504820154 256 FSVTAASPRKQRALEFLNFIGSPE 279
Cdd:cd13523  237 FAVPANAPNKDGAYKLLNALLRPK 260
potD PRK09501
spermidine/putrescine ABC transporter periplasmic substrate-binding protein; Reviewed
 17-322 2.19e-29

spermidine/putrescine ABC transporter periplasmic substrate-binding protein; Reviewed


Pssm-ID: 181913 [Multi-domain]  Cd Length: 348  Bit Score: 115.40  E-value: 2.19e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154  17 ASASRAETLNLLIWEDYIDEGLIDRWTEKTGVSIRQINFDSDD---ARDEILADPGrnIDLVIVDENGATLFGRKGIIEP 93
Cdd:PRK09501  21 AHADDNNTLYFYNWTEYVPPGLLEQFTKETGIKVIYSTYESNEtmyAKLKTYKDGA--YDLVVPSTYYVDKMRKEGMIQK 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154  94 LSETNLPALEDYAPEW-RKSC---AGYGLPYFWGTVGILYRSDVVTPPP-TSWRDMMRPApaLRKHIAMFADHSEIFVPP 168
Cdd:PRK09501  99 IDKSKLTNFSNLDPDMlNKPFdpnNDYSIPYIWGATAIGVNSDAIDPKSvTSWADLWKPE--YKGSLLLTDDAREVFQMA 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 169 LMLLGASVNADDTPTLKAAFALLKTQAPFVLTYDyvVTSIQDPALAGNIYLALGYSGDQHVlnskAGKAG-----LWrys 243
Cdd:PRK09501 177 LRKLGYSGNTTDPKEIEAAYNELKKLMPNVAAFN--SDNPANPYMEGEVNLGMIWNGSAFV----ARQAGtpidvVW--- 247

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504820154 244 vPKEGTLSWLDCFSVTAASPRKQRALEFLNFIGSPEAAAANAIALNMPTASNAALKLLPDTMRSDPEIYPPTEIMAKNQ 322
Cdd:PRK09501 248 -PKEGGIFWMDSLAIPANAKNKEGALKLINFLLRPDVAKQVAETIGYPTPNLAARKLLSPEVANDKSLYPDAETIKKGE 325
PBP2_polyamine_RpCGA009 cd13589
The periplasmic-binding component of an uncharacterized ABC transport system from ...
 30-279 6.28e-29

The periplasmic-binding component of an uncharacterized ABC transport system from Rhodopseudomonas palustris CGA009 and related proteins; contains the type 2 periplasmic-binding fold; This group represents the periplasmic binding domain that serves as the primary high-affinity receptor of an uncharacterized ABC-type polyamine transporter from Rhodopseudomonas palustris Cga009 and related proteins from other bacteria. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is 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.


Pssm-ID: 270307 [Multi-domain]  Cd Length: 268  Bit Score: 112.32  E-value: 6.28e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154  30 WEDYIDEGLIDRWTEKTGVSIRQINFDSDDARDEILADPGR-NIDLVIVDENGATLFGRKGIIEPLSETNLPALeDYAPE 108
Cdd:cd13589   11 YEDAQRKAVIEPFEKETGIKVVYDTGTSADRLAKLQAQAGNpQWDVVDLDDGDAARAIAEGLLEPLDYSKIPNA-AKDKA 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 109 WRKSCAGYGLPYFWGTVGILYRSDVVTPPPTSWrDMMRPA--------PALRKHIAMFAdhsEIFvppLMLLGASVNADD 180
Cdd:cd13589   90 PAALKTGYGVGYTLYSTGIAYNTDKFKEPPTSW-WLADFWdvgkfpgpRILNTSGLALL---EAA---LLADGVDPYPLD 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 181 tptLKAAFALLKTQAPFVLTYDyvvTSIQDPA---LAGNIYLALGYSGDQHVLNskagKAGL-WRYSVPKEGTLSWLDCF 256
Cdd:cd13589  163 ---VDRAFAKLKELKPNVVTWW---TSGAQLAqllQSGEVDMAPAWNGRAQALI----DAGApVAFVWPKEGAILGPDTL 232

                        250       260
                 ....*....|....*....|...
gi 504820154 257 SVTAASPRKQRALEFLNFIGSPE 279
Cdd:cd13589  233 AIVKGAPNKELAMKFINFALSPE 255
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 38-311 5.16e-23

Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 96.71  E-value: 5.16e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154   38 LIDRWTEKTGVSIRQINFDSDDARDEILADP--GRNIDLVIVDENGATL--FGRKGIIEPLSET-NLPALEDYAPEWRKS 112
Cdd:pfam13416   2 LAKAFEKKTGVTVEVEPQASNDLQAKLLAAAaaGNAPDLDVVWIAADQLatLAEAGLLADLSDVdNLDDLPDALDAAGYD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154  113 CAGYGLPYFWGTVGIL-YRSDVVT---PPPTSWRDMMRPAPALRKHIAMFADHSEIFVPPLMLLGASVNADD--TPTLKA 186
Cdd:pfam13416  82 GKLYGVPYAASTPTVLyYNKDLLKkagEDPKTWDELLAAAAKLKGKTGLTDPATGWLLWALLADGVDLTDDGkgVEALDE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154  187 AFALLKTQAPFVLTYDYVVTSIQDPAlAGNIYLALGYSGDQhVLNSKAGKAglWRYSVPKEGTLSWLDCFSVTAASP-RK 265
Cdd:pfam13416 162 ALAYLKKLKDNGKVYNTGADAVQLFA-NGEVAMTVNGTWAA-AAAKKAGKK--LGAVVPKDGSFLGGKGLVVPAGAKdPR 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 504820154  266 QRALEFLNFIGSPEAAAANAIALNMPTASNAAlkLLPDTMRSDPEI 311
Cdd:pfam13416 238 LAALDFIKFLTSPENQAALAEDTGYIPANKSA--ALSDEVKADPAL 281
PBP2_TpPotD_like cd13662
The periplasmic substrate-binding component of an ABC-type polyamine transport system from ...
 24-312 1.77e-20

The periplasmic substrate-binding component of an ABC-type polyamine transport system from Treponema pallidum and related proteins; contains the type 2 periplasmic binding fold; This group includes the polyamine-binding component of an ABC-type polyamine transport system from Treponema pallidum and closely related proteins, which is homologous to the spermidine-preferring periplasmic substrate-binding protein component (PotD)of ABC transport system. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, as well as plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is 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.


Pssm-ID: 270380  Cd Length: 312  Bit Score: 90.27  E-value: 1.77e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154  24 TLNLLIWEDYIDEGLIDRWTEKTGVsirQINFDSDDARDEILAD---PGRNIDLVIVDENGATLFGRKGIIEPLSETNLP 100
Cdd:cd13662    1 VLYIYNWTYYIPDKVIEDFEKETGI---RVVYDYYASNEEMYAKlkiGGGGYDIVSPSGDYVSIMKKEGLLEKLDKSKLP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 101 -----------ALEDYAPEWRkscagYGLPYFWGTVGILYRSDVVTPPPTSWRDMMRPApaLRKHIAMFADHSEIFVPPL 169
Cdd:cd13662   78 nvkeekdnlmeASKIYDPGLE-----YSVPYMFGATGIAVNKKIVKNYFRKWSIFLRED--LAGRMTMLDDMREVIGAAL 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 170 MLLGASVNADDTPTLKAAFALLKTQAPFVLTYDyvVTSIQDPALAGNIYLALGYSGDQHVLNSKAGKAGLwRYSVPKE-G 248
Cdd:cd13662  151 AYLGYPVDSKDIEQLEEAKEVILSWKKNLAKFD--SNSYGKGFASGDFWVVHGYAEDVFYEVPEEEEEKF-DFFIPEGaA 227

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504820154 249 TLSWLDCFSVTAASPRKQRALEFLNFIGSPEAAAANAIALNMPTASNAALKLlpdtMRSDPEIY 312
Cdd:cd13662  228 SMMYIDSFVIPKGSKHKDNAYKFINFILRPENYAEILDVLGNPSIIKEAEKK----SQKKPIIY 287
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 1-279 1.26e-18

ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 85.87  E-value: 1.26e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154   1 MKARGVISVFLATLLCA-------SASRAETLNLLIW------EDYIDEgLIDRWTEKT-GVSIRQINFDSDDARDEILA 66
Cdd:COG1653    2 RRLALALAAALALALAAcggggsgAAAAAGKVTLTVWhtgggeAAALEA-LIKEFEAEHpGIKVEVESVPYDDYRTKLLT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154  67 D--PGRNIDLVIVDENGATLFGRKGIIEPLSE---TNLPALEDYAPEWRKSCA--G--YGLPYFWGTVGILYRSDVVT-- 135
Cdd:COG1653   81 AlaAGNAPDVVQVDSGWLAEFAAAGALVPLDDlldDDGLDKDDFLPGALDAGTydGklYGVPFNTDTLGLYYNKDLFEka 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 136 --PPPTSWRDMMRPAPALRKH-----IAMFADHSEIFVPPLMLLGASV-NAD-----DTPTLKAAFALLKTQA------P 196
Cdd:COG1653  161 glDPPKTWDELLAAAKKLKAKdgvygFALGGKDGAAWLDLLLSAGGDLyDEDgkpafDSPEAVEALEFLKDLVkdgyvpP 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 197 FVLTYDYvvTSIQDPALAGNIYLALGYSGDQHVLNSKAGKAGLWRYSVP------KEGTLSWLDCFSVTAASPRKQRALE 270
Cdd:COG1653  241 GALGTDW--DDARAAFASGKAAMMINGSWALGALKDAAPDFDVGVAPLPggpggkKPASVLGGSGLAIPKGSKNPEAAWK 318


                 ....*....
gi 504820154 271 FLNFIGSPE 279
Cdd:COG1653  319 FLKFLTSPE 327
PBP2_PotD_PotF_like_1 cd13661
The periplasmic substrate-binding component of an uncharacterized active transport system ...
 116-341 2.94e-15

The periplasmic substrate-binding component of an uncharacterized active transport system closely related to spermidine and putrescine transporters; contains the type 2 periplasmic binding fold; This group represents the periplasmic binding domain that serves as a primary polyamine receptor of an uncharacterized ABC-type transport system from plants and plant-symbiotic cyanobacteria. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, as well as plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is 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.


Pssm-ID: 270379 [Multi-domain]  Cd Length: 319  Bit Score: 75.53  E-value: 2.94e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 116 YGLPYFWGTVGILYRSDVVTPP---PTSWRDMMRpaPALRKHIAMFADHSEIFVPPLMLLGASVNADDTP----TLKAAF 188
Cdd:cd13661   81 WAVPYRWGTTVIAYRKDKLKKLgwdPIDWSDLWR--PELAGRIAMVDSPREVIGLVLKKLGASYNTAEVPggreALEERL 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 189 ALLKTQAPFVLTYDYVvtsiqDPALAGNIYLALGYSGDqhVLnskagkAGLWRYS-----VPKEGTLSWLDCFSVTAASP 263
Cdd:cd13661  159 AALRRQVKLYSSNNYL-----QALLLGDVWVAVGWSQD--II------PLARRYSnlavvIPRSGTSLWADLWVIPAGSD 225

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 264 RKQRAL-------EFLNFIGSPEaAAANAIALNMPTAS----NAALKLLPDTMRSD------PEIYPPTEIMAKNQHHQE 326
Cdd:cd13661  226 FGGRVRgpspllsQWIDFCLQPA-RATQFAQLSFGGASplilDGPSLTPPEATRKLkldtnlVLGLPPDEILAKSEFLLP 304

                        250
                 ....*....|....*
gi 504820154 327 LSVRSIEARRRIINT 341
Cdd:cd13661  305 LSEATLAQYRALWQT 319
AfuA COG1840
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]; ...
 38-279 8.12e-14

ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 441445 [Multi-domain]  Cd Length: 286  Bit Score: 70.73  E-value: 8.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154  38 LIDRWTEKTGVSIRQINFDSDDARDEILADPGR-NIDLVIVdeNGATLFGR---KGIIEPLSETNLPALedyaPEWRKSC 113
Cdd:COG1840    1 LLEAFEKKTGIKVNVVRGGSGELLARLKAEGGNpPADVVWS--GDADALEQlanEGLLQPYKSPELDAI----PAEFRDP 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 114 AGYGLPYFWGTVGILYRSDVVTP--PPTSWRDMMRPApaLRKHIAMfADHSEIFVPPLMLLGASVNADDTPTlKAAFALL 191
Cdd:COG1840   75 DGYWFGFSVRARVIVYNTDLLKElgVPKSWEDLLDPE--YKGKIAM-ADPSSSGTGYLLVAALLQAFGEEKG-WEWLKGL 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 192 KTQAPFVLTYDyvvTSIQDPALAGNIylALGYSGDQHVLNSKAGKAGLwRYSVPKEGTLSWLDCFSVTAASPRKQRALEF 271
Cdd:COG1840  151 AANGARVTGSS---SAVAKAVASGEV--AIGIVNSYYALRAKAKGAPV-EVVFPEDGTLVNPSGAAILKGAPNPEAAKLF 224


                 ....*...
gi 504820154 272 LNFIGSPE 279
Cdd:COG1840  225 IDFLLSDE 232
PBP2_polyamine_2 cd13587
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ...
 24-301 1.08e-13

The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of polyamines; contains the type 2 periplasmic binding fold; This family represents the periplasmic binding domain that functions as the primary polyamine receptor of an uncharacterized ABC-type transport system. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is 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.


Pssm-ID: 270305 [Multi-domain]  Cd Length: 292  Bit Score: 70.54  E-value: 1.08e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154  24 TLNLLIWEDYIDEGLIDRWTEKTGVSIRQINFDSDD-ARDEILADPGRNIDLVIVDENGATLFGRKGIIEPLSETNLpAL 102
Cdd:cd13587    1 TLRILTWAGYAPEDLLEKFENETGIKVQVTTSNNNEeMISKLRATGGGGFDLAQPSQRIAPNYEEFGLYQPIDESKI-KV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 103 EDYAPEWRKSCAG--------YGLPYFWGTVGILYRSDvVTPPPTS------WRDMMRPAPALRKH-----IAMFADHSE 163
Cdd:cd13587   80 AQFPPSLLESTKLgttingkrYAVPFDWGTEGLTVNST-KAPDVSGfsygdlWAPEYAGKVAYRLKspltgLGLYADATG 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 164 IFVPPLMLLGASvNADDTPTLKAAFALLKTQAPFVLTYDYVVTSIQDPALAGNIYLALGYsgDQHVLNSKAGKAGlWRYS 243
Cdd:cd13587  159 EDPFNRYLDYKD-EAKYQKILDQVLQFLIERKANVKAYWNNADEALAAFRSGGCVIGQTW--DSTGLKLNRENPP-IDYG 234

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 504820154 244 VPKEGTLSWLDCFSVTAASPRKQRALEFLNFIGSPEAAAANAIALNMPTASNAALKLL 301
Cdd:cd13587  235 APKEGALGWIDTFAIPAKAENVDQAYAFINFMLRPEIAAMFTNATGYNTAAVGAQEFL 292
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 24-320 1.28e-13

The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and similar oligosaccharides; possess type 2 periplasmic binding fold; This family includes the periplasmic trehalose/maltose-binding component of an ABC transport system and related proteins from archaea and bacteria. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is 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.


Pssm-ID: 270303 [Multi-domain]  Cd Length: 383  Bit Score: 71.28  E-value: 1.28e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154  24 TLNLLIWEDYID----EGLIDRWTEK-TGVSIRQINFDSDDARDEILAD--PGRNIDLVIVDENGATLFGRKGIIEPLSE 96
Cdd:cd13585    1 TLTFWDWGQPAEtaalKKLIDAFEKEnPGVKVEVVPVPYDDYWTKLTTAaaAGTAPDVFYVDGPWVPEFASNGALLDLDD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154  97 --TNLPALEDYAPEWRKSCAG----YGLPYFWGTVGILYRSDV------VTPPPTSWRDMMRPAPALRK--------HIA 156
Cdd:cd13585   81 yiEKDGLDDDFPPGLLDAGTYdgklYGLPFDADTLVLFYNKDLfdkagpGPKPPWTWDELLEAAKKLTDkkggqygfALR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 157 MFADHSEIFVPPLMLLGASV-NAD------DTPTLKAAFALLKT-----QAPFVLTYDYvvTSIQDPALAGNIylALGYS 224
Cdd:cd13585  161 GGSGGQTQWYPFLWSNGGDLlDEDdgkatlNSPEAVEALQFYVDlykdgVAPSSATTGG--DEAVDLFASGKV--AMMID 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 225 GDQHVLNSKAGKAGL-WRYSV------PKEGTLSWLDCFSVTAASPRKQRALEFLNFIGSPEAAAANAIALNMPTASNAA 297
Cdd:cd13585  237 GPWALGTLKDSKVKFkWGVAPlpagpgGKRASVLGGWGLAISKNSKHPEAAWKFIKFLTSKENQLKLGGAAGPAALAAAA 316

                        330       340
                 ....*....|....*....|...
gi 504820154 298 LKLLPDTMRSDPEIYPPTEIMAK 320
Cdd:cd13585  317 ASAAAPDAKPALALAAAADALAA 339
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
1-299 3.34e-13

Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 69.98  E-value: 3.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154   1 MKARGVISVFLATLL------CAS--------ASRAETLNLLIWED-----YIDEgLIDRWTEKTGVSIRQINFDSDDAR 61
Cdd:COG2182    1 MKRRLLAALALALALalalaaCGSgssssgssSAAGAGGTLTVWVDddeaeALEE-AAAAFEEEPGIKVKVVEVPWDDLR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154  62 DEIL--ADPGRNIDLVIVDENGATLFGRKGIIEPLSETnLPALEDYAPEWRKSCA--G--YGLPYFWGTVGILYRSDVVT 135
Cdd:COG2182   80 EKLTtaAPAGKGPDVFVGAHDWLGELAEAGLLAPLDDD-LADKDDFLPAALDAVTydGklYGVPYAVETLALYYNKDLVK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 136 P-PPTSWRDMMRPAPALRK--HIAMFADHSEI-FVPPLM------LLGASVNADDTPTL-----KAAFALLKTQAPfvlt 200
Cdd:COG2182  159 AePPKTWDELIAAAKKLTAagKYGLAYDAGDAyYFYPFLaafggyLFGKDGDDPKDVGLnspgaVAALEYLKDLIK---- 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 201 ydyvvTSIQDPALAGNIYLALgysgdqhvlnSKAGKA-----GLWRYS--------------VPK----EGTLSWL--DC 255
Cdd:COG2182  235 -----DGVLPADADYDAADAL----------FAEGKAamiinGPWAAAdlkkalgidygvapLPTlaggKPAKPFVgvKG 299

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 504820154 256 FSVTAASPRKQRALEFLNFIGSPEAAAANAIALNMPTASNAALK 299
Cdd:COG2182  300 FGVSAYSKNKEAAQEFAEYLTSPEAQKALFEATGRIPANKAAAE 343
SBP_bac_6 pfam13343
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 88-279 2.41e-12

Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.


Pssm-ID: 463852 [Multi-domain]  Cd Length: 247  Bit Score: 65.84  E-value: 2.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154   88 KGIIEPLSETNLPAL-EDYAPEWRKSCAGYGLPYFWGTVGILYRSDVV--TPPPTSWRDMMRpaPALRKHIAMFADHSEI 164
Cdd:pfam13343  26 EGLFQPLDSANLPNVpKDFDDEGLRDPDGYYTPYGVGPLVIAYNKERLggRPVPRSWADLLD--PEYKGKVALPGPNVGD 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154  165 FVPPLmLLGASVNADDTPTLKAAFALLKTQAPFvltydYVVTSIQDPAL-AGNIYLALGYSGDQHVLNSKAgkaglWRYS 243
Cdd:pfam13343 104 LFNAL-LLALYKDFGEDGVRKLARNLKANLHPA-----QMVKAAGRLESgEPAVYLMPYFFADILPRKKKN-----VEVV 172

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 504820154  244 VPKEGTLSWLDCFSVTAAspRKQRALEFLNFIGSPE 279
Cdd:pfam13343 173 WPEDGALVSPIFMLVKKG--KKELADPLIDFLLSPE 206
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 31-279 5.24e-11

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


Pssm-ID: 460248 [Multi-domain]  Cd Length: 294  Bit Score: 62.43  E-value: 5.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154   31 EDYIDEGLIDRWT-EKTGVSIRQINFDSDDARDEILAD---PGRNIDLVIVDENGATLFGRKGIIEPLSETNLPALEDYA 106
Cdd:pfam01547   6 EAAALQALVKEFEkEHPGIKVEVESVGSGSLAQKLTTAiaaGDGPADVFASDNDWIAELAKAGLLLPLDDYVANYLVLGV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154  107 PEWrkscagYGLPYFWGTVGILYRSDVV----TPPPTSWRDMMRPAPALRKH-----IAMFADHSE---IFVPPLML--- 171
Cdd:pfam01547  86 PKL------YGVPLAAETLGLIYNKDLFkkagLDPPKTWDELLEAAKKLKEKgkspgGAGGGDASGtlgYFTLALLAslg 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154  172 ------------LGASVNADDTPTLKAAFALLKTQAPFVLTYDYVVTSIQDPALAGNIYLALGYSGDQHVLNSKAGKAGL 239
Cdd:pfam01547 160 gplfdkdgggldNPEAVDAITYYVDLYAKVLLLKKLKNPGVAGADGREALALFEQGKAAMGIVGPWAALAANKVKLKVAF 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 504820154  240 ----------WRYSVPKEGT--LSWLDCFSVTAASPRKQRALEFLNFIGSPE 279
Cdd:pfam01547 240 aapapdpkgdVGYAPLPAGKggKGGGYGLAIPKGSKNKEAAKKFLDFLTSPE 291
PBP2_Maltose_binding_like cd13586
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 27-319 1.23e-10

The periplasmic-binding component of ABC transport systems specific for maltose and related polysaccharides; possess type 2 periplasmic binding fold; This subfamily represents the periplasmic binding component of ABC transport systems involved in uptake of polysaccharides including maltose, maltodextrin, and cyclodextrin. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is 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.


Pssm-ID: 270304 [Multi-domain]  Cd Length: 367  Bit Score: 61.93  E-value: 1.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154  27 LLIWEDYIDE-----GLIDRWTEKTGVSIRQINFDSDDARDEILAD--PGRNIDLVIV--DENGAtlFGRKGIIEPLSET 97
Cdd:cd13586    2 ITVWTDEDGEleylkELAEEFEKKYGIKVEVVYVDSGDTREKFITAgpAGKGPDVFFGphDWLGE--LAAAGLLAPIPEY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154  98 NLPALEDYAPEWRKSCAG---YGLPYFWGTVGILYRSDVVTPPPTSWRDMmrpaPALRKHIAMFADHSEIFV-------- 166
Cdd:cd13586   80 LAVKIKNLPVALAAVTYNgklYGVPVSVETIALFYNKDLVPEPPKTWEEL----IALAKKFNDKAGGKYGFAydqtnpyf 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 167 --PPLMLLGASV---NADDTPTL-------KAAFALLKTQapfVLTYDYVVTSIqDPALAGNIYlalgysgdqhvlnsKA 234
Cdd:cd13586  156 syPFLAAFGGYVfgeNGGDPTDIglnnegaVKGLKFIKDL---KKKYKVLPPDL-DYDIADALF--------------KE 217

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 235 GKA-----GLW----------RYSV---PK-EGTLsWLDCFS------VTAASPRKQRALEFLNFIGSPEAAAANAIALN 289
Cdd:cd13586  218 GKAamiinGPWdladykdagiNFGVaplPTlPGGK-QAAPFVgvqgafVSAYSKNKEAAVEFAEYLTSDEAQLLLFEKTG 296

                        330       340       350
                 ....*....|....*....|....*....|
gi 504820154 290 MPTASNAALKLLPDTmrSDPEIYPPTEIMA 319
Cdd:cd13586  297 RIPALKDALNDAAVK--NDPLVKAFAEQAQ 324
PBP2_TMBP cd14750
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ...
 29-279 4.19e-06

The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; possesses type 2 periplasmic binding fold; This group represents the periplasmic trehalose/maltose-binding component of an ABC transport system and related proteins from archaea and bacteria. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are 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.


Pssm-ID: 270453 [Multi-domain]  Cd Length: 385  Bit Score: 48.06  E-value: 4.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154  29 IWEDYIDEgLIDRWTEKTG---VSIRQINFDSDDARDEILADPGRN---IDLVIVDENGATLFGRKGIIEPLSETNLPA- 101
Cdd:cd14750   11 QEGELLKK-AIAAFEKKHPdikVEIEELPASSDDQRQQLVTALAAGssaPDVLGLDVIWIPEFAEAGWLLPLTEYLKEEe 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 102 LEDYAPEWRKSCA--G--YGLPYFwGTVGIL-YRSDVV----TPPPTSWRDMMRPAPALRKH-------IAMFADHSEIF 165
Cdd:cd14750   90 DDDFLPATVEANTydGklYALPWF-TDAGLLyYRKDLLekygPEPPKTWDELLEAAKKRKAGepgiwgyVFQGKQYEGLV 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 166 VPPLMLL----GASVNAD------DTPTLKAAFALLKTQA------PFVLTYDyvvtsiQDPAL----AGNIYLALGYSG 225
Cdd:cd14750  169 CNFLELLwsngGDIFDDDsgkvtvDSPEALEALQFLRDLIgegispKGVLTYG------EEEARaafqAGKAAFMRNWPY 242

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504820154 226 DQHVLNSK----AGKAGLWRY-SVPKEGTLS----WLdcFSVTAASPRKQRALEFLNFIGSPE 279
Cdd:cd14750  243 AYALLQGPesavAGKVGVAPLpAGPGGGSAStlggWN--LAISANSKHKEAAWEFVKFLTSPE 303
PBP2_Maltodextrin cd13657
The periplasmic binding component of ABC transport system specific for maltodextrin; This ...
 29-312 4.99e-06

The periplasmic binding component of ABC transport system specific for maltodextrin; This group includes the periplasmic maltodextrin-binding protein of a binding protein-dependent ATP-binding cassette transporter. Maltodextrin is a polysaccharide that is used as a food addtive and can be enzymatically produced from any starch . Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is 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.


Pssm-ID: 270375 [Multi-domain]  Cd Length: 368  Bit Score: 47.76  E-value: 4.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154  29 IWEDY------IDEGLIDRWTEKTGVSIRQINFDSDDARDEIL--ADP-GRNIDLVIVDENGATLFGRKGIIEPLSETNL 99
Cdd:cd13657    4 IWHALtgaeedALQQIIDEFEAKYPVPNVKVPFEKKPDLQNKLltAIPaGEGPDLFIWAHDWIGQFAEAGLLVPISDYLS 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 100 P-ALEDYAP------EWRKscAGYGLPYFWGTVGILYRSDVVTPPPTSWRDMMRPAPALRKHIA-MFA---DHSE-IFVP 167
Cdd:cd13657   84 EdDFENYLPtaveavTYKG--KVYGLPEAYETVALIYNKALVDQPPETTDELLAIMKDHTDPAAgSYGlayQVSDaYFVS 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 168 PLML-LGASV---NAD----DTPTLKAAFALLKT-QAPFV---LTYDYVVT---------SIQDPALAGNIYLALgysgd 226
Cdd:cd13657  162 AWIFgFGGYYfddETDkpglDTPETIKGIQFLKDfSWPYMpsdPSYNTQTSlfnegkaamIINGPWFIGGIKAAG----- 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 227 qhvlnSKAGKAGLwrysvPKEGTLSWLDCF--------SVTAASPRKQRALEFLNFIGSPEAAAANAIALNMPTASNAAL 298
Cdd:cd13657  237 -----IDLGVAPL-----PTVDGTNPPRPYsgvegiyvTKYAERKNKEAALDFAKFFTTAEASKILADENGYVPAATNAY 306

                        330
                 ....*....|....
gi 504820154 299 KLlpDTMRSDPEIY 312
Cdd:cd13657  307 DD--AEVAADPVIA 318
PBP2_ABC_oligosaccharides cd13522
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 24-279 3.71e-04

The periplasmic-binding component of ABC transport systems specific for maltose and related oligosaccharides; possess type 2 periplasmic binding fold; This family represents the periplasmic binding component of ABC transport systems involved in uptake of oligosaccharides including maltose, trehalose, maltodextrin, and cyclodextrin. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is 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.


Pssm-ID: 270240 [Multi-domain]  Cd Length: 368  Bit Score: 42.01  E-value: 3.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154  24 TLNLLIWEDYIDE----GLIDRWTEKT-GVSIRQINFDSDDARDEI--LADPGRNIDLVI--VDENGAtlFGRKGIIEPL 94
Cdd:cd13522    1 TITVWHQYDTGENqavnELIAKFEKAYpGITVEVTYQDTEARRQFFstAAAGGKGPDVVFgpSDSLGP--FAAAGLLAPL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154  95 SETnLPALEDYAPE----WRKSCAGYGLPYFWGTVGILYR-SDVVTPPPTSWRDMMRPAPALR-KHIAMFA-DHSEI--F 165
Cdd:cd13522   79 DEY-VSKSGKYAPNtiaaMKLNGKLYGVPVSVGAHLMYYNkKLVPKNPPKTWQELIALAQGLKaKNVWGLVyNQNEPyfF 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 166 VPPLMLLGASVNAD---------DTPTLKAAFALLKTqapfvLTYDY-VVTSIQDPALAGNIYL----ALGYSGD----- 226
Cdd:cd13522  158 AAWIGGFGGQVFKAnngknnptlDTPGAVEALQFLVD-----LKSKYkIMPPETDYSIADALFKagkaAMIINGPwdlgd 232

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 504820154 227 -QHVLNSKAGKAGL-----WRYSVPKEGTLSWldcfSVTAASPRKQRALEFLNFIGSPE 279
Cdd:cd13522  233 yRQALKINLGVAPLptfsgTKHAAPFVGGKGF----GINKESQNKAAAVEFVKYLTSYQ 287
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
 36-320 8.56e-04

The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; possesses type 2 periplasmic binding fold; This group includes the periplasmic component of an ABC transport system specific for sn-glycerol-3-phosphate (G3P) and closely related proteins from archaea and bacteria. Under phophate starvation conditions, Escherichia coli can utilize G3P as phosphate source when exclusively imported by an ATP-binding cassette (ABC) transporter composed of the periplasmic binding protein, UgpB, the transmembrane subunits, UgpA and UgpE, and a homodimer of the nucleotide binding subunit, UgpC. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are 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.


Pssm-ID: 270451 [Multi-domain]  Cd Length: 385  Bit Score: 40.74  E-value: 8.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154  36 EGLIDRWTEK-TGVSIRQINFDS-DDARDEILAD------PgrniDLVIVDENGATLFGRKGIIEPLSE---TNLPALED 104
Cdd:cd14748   17 EELVDEFNKShPDIKVKAVYQGSyDDTLTKLLAAlaagtaP----DVAQVDASWVAQLADSGALEPLDDyidKDGVDDDD 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 105 YAPEWRKSCAG----YGLPYFWGTVGILYRSDV-----VTP--PPTSWRDMMRPAPAL--------RKHIAMFADHSEIF 165
Cdd:cd14748   93 FYPAALDAGTYdgklYGLPFDTSTPVLYYNKDLfeeagLDPekPPKTWDELEEAAKKLkdkggktgRYGFALPPGDGGWT 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 166 VPPLMLL--GASVNAD------DTPTLKAAFALLK---TQAPFVLTYDYvvTSIQDPALAGNIYLALGYSGDQHVLNSKA 234
Cdd:cd14748  173 FQALLWQngGDLLDEDggkvtfNSPEGVEALEFLVdlvGKDGVSPLNDW--GDAQDAFISGKVAMTINGTWSLAGIRDKG 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154 235 GK-----AGLWRYSVPKEGTLSWLDCFSVTAASPRKQR-ALEFLNFIGSPEAAAANAIALNMPTASNAALKLLPDTMRSD 308
Cdd:cd14748  251 AGfeygvAPLPAGKGKKGATPAGGASLVIPKGSSKKKEaAWEFIKFLTSPENQAKWAKATGYLPVRKSAAEDPEEFLAEN 330

                        330
                 ....*....|..
gi 504820154 309 PEIYPPTEIMAK 320
Cdd:cd14748  331 PNYKVAVDQLDY 342
TbpA COG4143
ABC-type thiamine transport system, periplasmic component TbpA [Coenzyme transport and ...
 6-152 3.50e-03

ABC-type thiamine transport system, periplasmic component TbpA [Coenzyme transport and metabolism];


Pssm-ID: 443315 [Multi-domain]  Cd Length: 343  Bit Score: 38.67  E-value: 3.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154   6 VISVFLATLLCASASRAETLNLLIWEDYIDE-----GLIDRWTEKTGVSIRQINFDsdDA----------RDEILADpgr 70
Cdd:COG4143   13 ALALALAGCSGAAAAAKPTLTVYTYDSFASEwgpgpWLKAAFEAECGCTLEFVAPG--DGgellnrlrleGANPKAD--- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504820154  71 nidLVI-VDengATLFGR---KGIIEPLsetNLPALEDYAPEWRKSCAGYGLPYFWGTVGILYRSDVVTPPPTSWRDMMR 146
Cdd:COG4143   88 ---VVLgLD---NNLLARaldTGLFAPH---GVDALDALALPLAWDPDDRFVPYDYGYFAFVYDKTKLLNPPESLEDLVD 158


                 ....*.
gi 504820154 147 PAPALR 152
Cdd:COG4143  159 PEYKDK 164
 
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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