|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11622 |
PRK11622 |
ABC transporter substrate-binding protein; |
19-380 |
0e+00 |
|
ABC transporter substrate-binding protein;
Pssm-ID: 183238 [Multi-domain] Cd Length: 401 Bit Score: 588.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 19 AAVDWQEVEKKAAGQTVYFNAWGGSQEINNYLRWAGKRLQSEYGVTLKHVKVTDISEAVSRLAVEKTAQKNSAGSIDMVW 98
Cdd:PRK11622 25 ENKDWQQILEEAKGQTVYFYAWGGSPAINRYLDWVAKELKERYGITLKHVKLADIAEAVNRLLAEKQAGRDTGGSVDLVW 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 99 INGENFKSMKQHQLLSEAFTTRLPNWKFVDQSLPVSSDFAEPTLGLEAPWGVGQLVFIYDTKRLSTPPDSFNAMLNYAKA 178
Cdd:PRK11622 105 INGENFRTLKEAGLLYGPFAETLPNWRYVDTSLPVREDFGVPTEGLEAPWGGAQLVFIYDSARTPQPPQSPAELLEWAKA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 179 NPQRLSYPKPPSFHGTSFLKAALLELSADSNLLYSPVNENNFQEISAPLWDYLDEFHKSAWRQGKLFPASSSETLQLLDD 258
Cdd:PRK11622 185 NPGRFTYPRPPDFTGTAFLKQLLYELTGDPAALKQPVDKATFARVTAPLWDYLDELHPYLWREGKTFPASPAELDQLLAD 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 259 GQLDLAVTFNPNEVLSAQENGTLSESTKAYALKAGALSNIHFLAIPWNAAAKEGALVAINFLLSPEAQSHKGDLQVWGDP 338
Cdd:PRK11622 265 GELDLAMTFNPNHAQSKIANGELPASTRSFVFDDGTIGNTHFVAIPFNANAKAGAKVVANFLLSPEAQLRKADPAVWGDP 344
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 518445122 339 AVLYPHYIRGSAK--------------DTTLFKSLPEPHPSWQTALETEWQKRYGH 380
Cdd:PRK11622 345 SVLDPQKLPEEQRaafaaldlgaatlqPELLPPALPEPHASWVEALEQEWQRRYGT 400
|
|
| YnjB |
COG4134 |
ABC-type uncharacterized transport system YnjBCD, periplasmic component [General function ... |
19-380 |
2.79e-179 |
|
ABC-type uncharacterized transport system YnjBCD, periplasmic component [General function prediction only];
Pssm-ID: 443309 [Multi-domain] Cd Length: 401 Bit Score: 503.62 E-value: 2.79e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 19 AAVDWQEVEKKAAGQTVYFNAWGGSQEINNYL-RWAGKRLQSEYGVTLKHVKVTDISEAVSRLAVEKTAQKNSAGSIDMV 97
Cdd:COG4134 23 AAADWQAIEAEARGQTVYFNAWGGDPNINDYIdDWVAPQLKERYGITLEHVKLADTADAVNRVLAEKQAGKDDGGSVDLI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 98 WINGENFKSMKQHQLLSEAFTTRLPNWKFVD-QSLPVSSDFAEPTLGLEAPWGVGQLVFIYDTKRLSTPPDSFNAMLNYA 176
Cdd:COG4134 103 WINGENFAAMKEAGLLFGPFAEKLPNWAYVDtEKPTVTTDFGVPVDGYEAPWGMAQLVFIYDSARVPNPPRSLAELLEWA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 177 KANPQRLSYPKPPSFHGTSFLKAALLELSADSNLLYSPVNENNFQEISAPLWDYLDEFHKSAWRQGKLFPASSSETLQLL 256
Cdd:COG4134 183 KANPGRFTYPAPPDFTGSTFLKQALYELTGDPDALQQPVDEAKFAKVTAPLWAYLDELHPYLWRQGKTYPASNAALDQLL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 257 DDGQLDLAVTFNPNEVLSAQENGTLSESTKAYALKAGALSNIHFLAIPWNAAAKEGALVAINFLLSPEAQSHKGDLQVWG 336
Cdd:COG4134 263 ADGEIDMAMSFNPAEASSAIANGELPPTVRTFVFDGGTIGNTHFLAIPFNAPNKAGAMVVANFLLSPEAQARKADPAVWG 342
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 337 DPAVLYPHyiRGSAKDTTLFKS----------------LPEPHPSWQTALETEWQKRYGH 380
Cdd:COG4134 343 DPTVLDLD--KLPAEQRAAFDAlplgpatlspeelgnaLPEPHASWVEAIEEEWLKRYGA 400
|
|
| SBP_bac_8 |
pfam13416 |
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
52-326 |
5.83e-15 |
|
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.
Pssm-ID: 433189 [Multi-domain] Cd Length: 281 Bit Score: 74.36 E-value: 5.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 52 WAGKRLQSEYGVTLKHVKVtDISEAVSRLAVEktAQKNSAGSIDMVWINGENFKSMKQHQLLSEafTTRLPNWKFVDQSL 131
Cdd:pfam13416 1 ALAKAFEKKTGVTVEVEPQ-ASNDLQAKLLAA--AAAGNAPDLDVVWIAADQLATLAEAGLLAD--LSDVDNLDDLPDAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 132 PvSSDFAEPTLGLeaPWGVG-QLVFIYDTKRLS---TPPDSFNAMLNYAKANPQRLSYPKPPSFHGTSFLKAALLELSAD 207
Cdd:pfam13416 76 D-AAGYDGKLYGV--PYAAStPTVLYYNKDLLKkagEDPKTWDELLAAAAKLKGKTGLTDPATGWLLWALLADGVDLTDD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 208 snllyspvNENNFQEISAplWDYLDEFHKSawrqgKLFPASSSETLQLLDDGQLDLAVTFnPNEVLSAQENGtlsESTKA 287
Cdd:pfam13416 153 --------GKGVEALDEA--LAYLKKLKDN-----GKVYNTGADAVQLFANGEVAMTVNG-TWAAAAAKKAG---KKLGA 213
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 518445122 288 YALKAGALSNIHFLAIPWNAAAKE-GALVAINFLLSPEAQ 326
Cdd:pfam13416 214 VVPKDGSFLGGKGLVVPAGAKDPRlAALDFIKFLTSPENQ 253
|
|
| PBP2_polyamines |
cd13523 |
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ... |
34-328 |
3.39e-13 |
|
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: 69.00 E-value: 3.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 34 TVYFNAWGGsqeinnYLR--WAGKrLQSEYGVtlkhvKVTDISEAVSRLAVEKTAQKNSaGSIDMVWINGENFKSMKQHQ 111
Cdd:cd13523 1 TVVIYTWGG------YLPqdIIDP-FEKETGI-----KVVVDTAANSERMIKKLSAGGS-GGFDLVTPSDSYTSRQLGVG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 112 LLSEAFTTRLPNWKFVD---QSLPVSSDFAEPtlgLEAPWGVGQLVFIYDTKRLSTPPDSFNAmLNYAKANPQRLSYPKP 188
Cdd:cd13523 68 LMQPIDKSLLPSWATLDphlTLAAVLTVPGKK---YGVPYQWGATGLVYNTDKVKAPPKSYAA-DLDDPKYKGRVSFSDI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 189 PSFhgtsFLKAALLELSADsnllyspVNENNFQEISAPLWDYLDEFHKSAwrqgKLFPASSSETLQLLDDGQLDLAVTFN 268
Cdd:cd13523 144 PRE----TFAMALANLGAD-------GNEELYPDFTDAAAALLKELKPNV----KKYWSNASQPANLLLNGEVVLAMAWL 208
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 269 PNEVLSAQENGTLSEStkayALKAGALSNIHFLAIPWNAAAKEGALVAINFLLSPEAQSH 328
Cdd:cd13523 209 GSGFKLKQAGAPIEFV----VPKEGAVGWLDTFAVPANAPNKDGAYKLLNALLRPKVAAA 264
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11622 |
PRK11622 |
ABC transporter substrate-binding protein; |
19-380 |
0e+00 |
|
ABC transporter substrate-binding protein;
Pssm-ID: 183238 [Multi-domain] Cd Length: 401 Bit Score: 588.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 19 AAVDWQEVEKKAAGQTVYFNAWGGSQEINNYLRWAGKRLQSEYGVTLKHVKVTDISEAVSRLAVEKTAQKNSAGSIDMVW 98
Cdd:PRK11622 25 ENKDWQQILEEAKGQTVYFYAWGGSPAINRYLDWVAKELKERYGITLKHVKLADIAEAVNRLLAEKQAGRDTGGSVDLVW 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 99 INGENFKSMKQHQLLSEAFTTRLPNWKFVDQSLPVSSDFAEPTLGLEAPWGVGQLVFIYDTKRLSTPPDSFNAMLNYAKA 178
Cdd:PRK11622 105 INGENFRTLKEAGLLYGPFAETLPNWRYVDTSLPVREDFGVPTEGLEAPWGGAQLVFIYDSARTPQPPQSPAELLEWAKA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 179 NPQRLSYPKPPSFHGTSFLKAALLELSADSNLLYSPVNENNFQEISAPLWDYLDEFHKSAWRQGKLFPASSSETLQLLDD 258
Cdd:PRK11622 185 NPGRFTYPRPPDFTGTAFLKQLLYELTGDPAALKQPVDKATFARVTAPLWDYLDELHPYLWREGKTFPASPAELDQLLAD 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 259 GQLDLAVTFNPNEVLSAQENGTLSESTKAYALKAGALSNIHFLAIPWNAAAKEGALVAINFLLSPEAQSHKGDLQVWGDP 338
Cdd:PRK11622 265 GELDLAMTFNPNHAQSKIANGELPASTRSFVFDDGTIGNTHFVAIPFNANAKAGAKVVANFLLSPEAQLRKADPAVWGDP 344
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 518445122 339 AVLYPHYIRGSAK--------------DTTLFKSLPEPHPSWQTALETEWQKRYGH 380
Cdd:PRK11622 345 SVLDPQKLPEEQRaafaaldlgaatlqPELLPPALPEPHASWVEALEQEWQRRYGT 400
|
|
| YnjB |
COG4134 |
ABC-type uncharacterized transport system YnjBCD, periplasmic component [General function ... |
19-380 |
2.79e-179 |
|
ABC-type uncharacterized transport system YnjBCD, periplasmic component [General function prediction only];
Pssm-ID: 443309 [Multi-domain] Cd Length: 401 Bit Score: 503.62 E-value: 2.79e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 19 AAVDWQEVEKKAAGQTVYFNAWGGSQEINNYL-RWAGKRLQSEYGVTLKHVKVTDISEAVSRLAVEKTAQKNSAGSIDMV 97
Cdd:COG4134 23 AAADWQAIEAEARGQTVYFNAWGGDPNINDYIdDWVAPQLKERYGITLEHVKLADTADAVNRVLAEKQAGKDDGGSVDLI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 98 WINGENFKSMKQHQLLSEAFTTRLPNWKFVD-QSLPVSSDFAEPTLGLEAPWGVGQLVFIYDTKRLSTPPDSFNAMLNYA 176
Cdd:COG4134 103 WINGENFAAMKEAGLLFGPFAEKLPNWAYVDtEKPTVTTDFGVPVDGYEAPWGMAQLVFIYDSARVPNPPRSLAELLEWA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 177 KANPQRLSYPKPPSFHGTSFLKAALLELSADSNLLYSPVNENNFQEISAPLWDYLDEFHKSAWRQGKLFPASSSETLQLL 256
Cdd:COG4134 183 KANPGRFTYPAPPDFTGSTFLKQALYELTGDPDALQQPVDEAKFAKVTAPLWAYLDELHPYLWRQGKTYPASNAALDQLL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 257 DDGQLDLAVTFNPNEVLSAQENGTLSESTKAYALKAGALSNIHFLAIPWNAAAKEGALVAINFLLSPEAQSHKGDLQVWG 336
Cdd:COG4134 263 ADGEIDMAMSFNPAEASSAIANGELPPTVRTFVFDGGTIGNTHFLAIPFNAPNKAGAMVVANFLLSPEAQARKADPAVWG 342
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 337 DPAVLYPHyiRGSAKDTTLFKS----------------LPEPHPSWQTALETEWQKRYGH 380
Cdd:COG4134 343 DPTVLDLD--KLPAEQRAAFDAlplgpatlspeelgnaLPEPHASWVEAIEEEWLKRYGA 400
|
|
| PotD |
COG0687 |
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism]; |
30-326 |
3.64e-19 |
|
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
Pssm-ID: 440451 [Multi-domain] Cd Length: 348 Bit Score: 87.66 E-value: 3.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 30 AAGQTVYFNAWGGSqeINNYLRwagKRLQSEYGVTLKHVKVTDISEAVSRLavektaqKNSAGSIDMVWINGENFKSMKQ 109
Cdd:COG0687 26 AAEGTLNVYNWGGY--IDPDVL---EPFEKETGIKVVYDTYDSNEEMLAKL-------RAGGSGYDVVVPSDYFVARLIK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 110 HQLLSEAFTTRLPNWKFVDQSL-PVSSDFAEPTLgleAPWGVGQLVFIYDTKRLSTPPDSFNAMLNyaKANPQRLSYPKP 188
Cdd:COG0687 94 AGLLQPLDKSKLPNLANLDPRFkDPPFDPGNVYG---VPYTWGTTGIAYNTDKVKEPPTSWADLWD--PEYKGKVALLDD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 189 PSfhgtSFLKAALLELSadsnllYSPvNENNFQEIsAPLWDYLDEFHKSAwrqgKLFPASSSETLQLLDDGQLDLAVTFN 268
Cdd:COG0687 169 PR----EVLGAALLYLG------YDP-NSTDPADL-DAAFELLIELKPNV----RAFWSDGAEYIQLLASGEVDLAVGWS 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 518445122 269 PnEVLSAQENGtlsESTKAYALKAGALSNIHFLAIPWNAAAKEGALVAINFLLSPEAQ 326
Cdd:COG0687 233 G-DALALRAEG---PPIAYVIPKEGALLWFDNMAIPKGAPNPDLAYAFINFMLSPEVA 286
|
|
| SBP_bac_8 |
pfam13416 |
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
52-326 |
5.83e-15 |
|
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.
Pssm-ID: 433189 [Multi-domain] Cd Length: 281 Bit Score: 74.36 E-value: 5.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 52 WAGKRLQSEYGVTLKHVKVtDISEAVSRLAVEktAQKNSAGSIDMVWINGENFKSMKQHQLLSEafTTRLPNWKFVDQSL 131
Cdd:pfam13416 1 ALAKAFEKKTGVTVEVEPQ-ASNDLQAKLLAA--AAAGNAPDLDVVWIAADQLATLAEAGLLAD--LSDVDNLDDLPDAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 132 PvSSDFAEPTLGLeaPWGVG-QLVFIYDTKRLS---TPPDSFNAMLNYAKANPQRLSYPKPPSFHGTSFLKAALLELSAD 207
Cdd:pfam13416 76 D-AAGYDGKLYGV--PYAAStPTVLYYNKDLLKkagEDPKTWDELLAAAAKLKGKTGLTDPATGWLLWALLADGVDLTDD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 208 snllyspvNENNFQEISAplWDYLDEFHKSawrqgKLFPASSSETLQLLDDGQLDLAVTFnPNEVLSAQENGtlsESTKA 287
Cdd:pfam13416 153 --------GKGVEALDEA--LAYLKKLKDN-----GKVYNTGADAVQLFANGEVAMTVNG-TWAAAAAKKAG---KKLGA 213
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 518445122 288 YALKAGALSNIHFLAIPWNAAAKE-GALVAINFLLSPEAQ 326
Cdd:pfam13416 214 VVPKDGSFLGGKGLVVPAGAKDPRlAALDFIKFLTSPENQ 253
|
|
| PBP2_polyamines |
cd13523 |
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ... |
34-328 |
3.39e-13 |
|
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: 69.00 E-value: 3.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 34 TVYFNAWGGsqeinnYLR--WAGKrLQSEYGVtlkhvKVTDISEAVSRLAVEKTAQKNSaGSIDMVWINGENFKSMKQHQ 111
Cdd:cd13523 1 TVVIYTWGG------YLPqdIIDP-FEKETGI-----KVVVDTAANSERMIKKLSAGGS-GGFDLVTPSDSYTSRQLGVG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 112 LLSEAFTTRLPNWKFVD---QSLPVSSDFAEPtlgLEAPWGVGQLVFIYDTKRLSTPPDSFNAmLNYAKANPQRLSYPKP 188
Cdd:cd13523 68 LMQPIDKSLLPSWATLDphlTLAAVLTVPGKK---YGVPYQWGATGLVYNTDKVKAPPKSYAA-DLDDPKYKGRVSFSDI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 189 PSFhgtsFLKAALLELSADsnllyspVNENNFQEISAPLWDYLDEFHKSAwrqgKLFPASSSETLQLLDDGQLDLAVTFN 268
Cdd:cd13523 144 PRE----TFAMALANLGAD-------GNEELYPDFTDAAAALLKELKPNV----KKYWSNASQPANLLLNGEVVLAMAWL 208
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 269 PNEVLSAQENGTLSEStkayALKAGALSNIHFLAIPWNAAAKEGALVAINFLLSPEAQSH 328
Cdd:cd13523 209 GSGFKLKQAGAPIEFV----VPKEGAVGWLDTFAVPANAPNKDGAYKLLNALLRPKVAAA 264
|
|
| PBP2_PotD_PotF_like |
cd13590 |
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ... |
48-326 |
7.16e-11 |
|
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: 62.64 E-value: 7.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 48 NYLRWAG-------KRLQSEYGVtlkHVKVTDIS---EAVSRLavektaQKNSAGSIDMVWINGENFKSMKQHQLLSEAF 117
Cdd:cd13590 3 NIYNWSDyidpevlKAFEKETGV---KVNYDTYDsneEMLAKL------RAGGGSGYDLVVPSDYMVERLIKQGLLEPLD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 118 TTRLPNWKFVD-QSLPVSSDfaePTLGLEAPWGVGQLVFIYDTKRLSTPPDSFNAMLNyakanpqrlsypkPPSFHGTSF 196
Cdd:cd13590 74 HSKLPNLKNLDpQFLNPPYD---PGNRYSVPYQWGTTGIAYNKDKVKEPPTSWDLDLW-------------DPALKGRIA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 197 --------LKAALLELSADSNllyspvnennfqEISAPLWDYLDEFHKSAWRQGKLFpaSSSETLQLLDDGQLDLAVTFN 268
Cdd:cd13590 138 mlddarevLGAALLALGYSPN------------TTDPAELAAAAELLIKQKPNVRAF--DSDSYVQDLASGEIWLAQAWS 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 518445122 269 PNEVLSAQENGTLsestkAYAL-KAGALSNIHFLAIPWNAAAKEGALVAINFLLSPEAQ 326
Cdd:cd13590 204 GDALQANRENPNL-----KFVIpKEGGLLWVDNMAIPKGAPNPELAHAFINFLLDPEVA 257
|
|
| PBP2_polyamine_RpCGA009 |
cd13589 |
The periplasmic-binding component of an uncharacterized ABC transport system from ... |
34-326 |
2.33e-10 |
|
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: 60.70 E-value: 2.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 34 TVYFNAWGGSQEiNNYLRWAGKRLQSEYGVTLKHVKVTDiSEAVSRLAVEKTAQknsagSIDMVWINGENFKSMKQHQLL 113
Cdd:cd13589 1 TLVVATWGGSYE-DAQRKAVIEPFEKETGIKVVYDTGTS-ADRLAKLQAQAGNP-----QWDVVDLDDGDAARAIAEGLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 114 SEafttrlpnwkfVDQSLPVSSDFAEPTLGLEAPWGVG----QLVFIYDTKRLSTPPDSFN-AMLNYAKanpqRLSYPKP 188
Cdd:cd13589 74 EP-----------LDYSKIPNAAKDKAPAALKTGYGVGytlySTGIAYNTDKFKEPPTSWWlADFWDVG----KFPGPRI 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 189 PSFHGTSFLKAALLelsADSnllySPVNENNFqeisAPLWDYLDEFHKSAwrqgKLFPASSSETLQLLDDGQLDLAVTFN 268
Cdd:cd13589 139 LNTSGLALLEAALL---ADG----VDPYPLDV----DRAFAKLKELKPNV----VTWWTSGAQLAQLLQSGEVDMAPAWN 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 518445122 269 pNEVLSAQENGtlseSTKAYAL-KAGALSNIHFLAIPWNAAAKEGALVAINFLLSPEAQ 326
Cdd:cd13589 204 -GRAQALIDAG----APVAFVWpKEGAILGPDTLAIVKGAPNKELAMKFINFALSPEVQ 257
|
|
| AfuA |
COG1840 |
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]; ... |
55-378 |
2.76e-09 |
|
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 441445 [Multi-domain] Cd Length: 286 Bit Score: 57.64 E-value: 2.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 55 KRLQSEYGVTLKHVKVTDiSEAVSRLAVEKtaqKNSAGsiDMVWI-NGENFKSMKQHQLLsEAFTTrlPNWKFVDqslpv 133
Cdd:COG1840 3 EAFEKKTGIKVNVVRGGS-GELLARLKAEG---GNPPA--DVVWSgDADALEQLANEGLL-QPYKS--PELDAIP----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 134 sSDFAEPTlGLEAPWGVGQLVFIYDTKRLS--TPPDSFNAMLN--YAKanpqRLSYPKPPSfHGT--SFLKAALLELSAD 207
Cdd:COG1840 69 -AEFRDPD-GYWFGFSVRARVIVYNTDLLKelGVPKSWEDLLDpeYKG----KIAMADPSS-SGTgyLLVAALLQAFGEE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 208 snllyspvnennfqeisaPLWDYLDEFHKsawrQGKLFPASSSETLQLLDDGQLDLAVTfNPNEVLSAQENGtlsESTKA 287
Cdd:COG1840 142 ------------------KGWEWLKGLAA----NGARVTGSSSAVAKAVASGEVAIGIV-NSYYALRAKAKG---APVEV 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 288 YALKAGALSNIHFLAIPWNAAAKEGALVAINFLLSPEAQshkgdlQVWGDPAVLYPhyIRGSAKDTTLFKSLPE----PH 363
Cdd:COG1840 196 VFPEDGTLVNPSGAAILKGAPNPEAAKLFIDFLLSDEGQ------ELLAEEGYEYP--VRPDVEPPEGLPPLGElkliDD 267
|
330
....*....|....*
gi 518445122 364 PSWQTALETEWQKRY 378
Cdd:COG1840 268 DDKAAENREELLELW 282
|
|
| PBP2_polyamine_1 |
cd13588 |
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ... |
60-326 |
1.40e-05 |
|
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: 46.14 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 60 EYGVTLKHVKVTDISEAVSRLavektaqKNSAGSIDMVWINGENFKSMKQHQLLSEAFTTRLPNWKFVDQSLPVSSDFA- 138
Cdd:cd13588 22 ATGCKVVVKFFGSEDEMVAKL-------RSGGGDYDVVTPSGDALLRLIAAGLVQPIDTSKIPNYANIDPRLRNLPWLTv 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 139 EPTL-GLeaPWGVGQLVFIYDTKRLSTPPDSFNAMLnYAKANPQRLSYPKPPSfhgTSFLKAALLelsadsnLLYSPVNE 217
Cdd:cd13588 95 DGKVyGV--PYDWGANGLAYNTKKVKTPPTSWLALL-WDPKYKGRVAARDDPI---DAIADAALY-------LGQDPPFN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 218 NNFQEISApLWDYLDEFHKsawrQGKLFPASSSETLQLLDDGQLDLAVTFNPnEVLSAQENGTLSESTKAyalKAGALSN 297
Cdd:cd13588 162 LTDEQLDA-VKAKLREQRP----LVRKYWSDGAELVQLFANGEVVAATAWSG-QVNALQKAGKPVAYVIP---KEGATGW 232
|
250 260
....*....|....*....|....*....
gi 518445122 298 IHFLAIPWNAAAKEGALVAINFLLSPEAQ 326
Cdd:cd13588 233 VDTWMILKDAKNPDCAYKWLNYMLSPKVQ 261
|
|
| PBP2_Fe3_thiamine_like |
cd13518 |
Substrate binding domain of iron and thiamine transporters-like, a member of the type 2 ... |
60-326 |
2.38e-05 |
|
Substrate binding domain of iron and thiamine transporters-like, a member of the type 2 periplasmic binding fold superfamily; The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. On the other hand, thiamin is an essential cofactor in all living systems. Thiamin diphosphate (ThDP)-dependent enzymes play an important role in carbohydrate and branched-chain amino acid metabolism. Most prokaryotes, plants, and fungi can synthesize thiamin, but it is not synthesized in vertebrates. These periplasmic domains have high affinities for their respective substrates and serve as the primary receptor for transport. After binding iron and thiamine 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. The iron- and thiamine-binding proteins belong to the PBPI2 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: 270236 [Multi-domain] Cd Length: 260 Bit Score: 45.37 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 60 EYGVTLKHV-KVTdiSEAVSRLAVEKtaqKNSAGSidmVWINGEN--FKSMKQHQLLsEAFTTrlpnwkfvDQSLPVSSD 136
Cdd:cd13518 23 KTGIKVKAVyDGT--GELANRLIAEK---NNPQAD---VFWGGEIiaLEALKEEGLL-EPYTP--------KVIEAIPAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 137 FAEPTlGLEAPWGVGQLVFIYDTKRLSTPPDSFNaMLNYAKAN-PQRLSYPKPPSFhGTSFLKAALLelsadsnlLYSPV 215
Cdd:cd13518 86 YRDPD-GYWVGFAARARVFIYNTDKLKEPDLPKS-WDDLLDPKwKGKIVYPTPLRS-GTGLTHVAAL--------LQLMG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 216 NENNFqeisaplWDYLDEFHKsawrqGKLFPASSSETLQLLDDGQLDLAVTFNPNEVLSAQENgtlsESTKAYALKAGAL 295
Cdd:cd13518 155 EEKGG-------WYLLKLLAN-----NGKPVAGNSDAYDLVAKGEVAVGLTDTYYAARAAAKG----EPVEIVYPDQGAL 218
|
250 260 270
....*....|....*....|....*....|.
gi 518445122 296 SNIHFLAIPWNAAAKEGALVAINFLLSPEAQ 326
Cdd:cd13518 219 VIPEGVALLKGAPNPEAAKKFIDFLLSPEGQ 249
|
|
| SBP_bac_1 |
pfam01547 |
Bacterial extracellular solute-binding protein; This family also includes the bacterial ... |
67-326 |
5.45e-04 |
|
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: 41.63 E-value: 5.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 67 HVKVTDISEAVSRLAVeKTAQKNSAGSIDMVWINGENFKSMKQHQLLsEAFTTRLPNWKFvdqslpvssDFAEPTLGLea 146
Cdd:pfam01547 25 KVEVESVGSGSLAQKL-TTAIAAGDGPADVFASDNDWIAELAKAGLL-LPLDDYVANYLV---------LGVPKLYGV-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 147 PWGVGQLVFIYDTKRLS----TPPDSFNAMLNYAKANpqRLSYPKPPSFHGTSFLKAALLELSADSNLLYSPVNENNFQE 222
Cdd:pfam01547 92 PLAAETLGLIYNKDLFKkaglDPPKTWDELLEAAKKL--KEKGKSPGGAGGGDASGTLGYFTLALLASLGGPLFDKDGGG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 223 ISAPLWD---------YLDEFHKSAWRQGKLFPASSSETLQLLDDGQLDLAVTFNPNEVLSAQENGTLSESTKAYALK-- 291
Cdd:pfam01547 170 LDNPEAVdaityyvdlYAKVLLLKKLKNPGVAGADGREALALFEQGKAAMGIVGPWAALAANKVKLKVAFAAPAPDPKgd 249
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 518445122 292 ---------AGALSNIHFLAIPWNAAAKEGALVAINFLLSPEAQ 326
Cdd:pfam01547 250 vgyaplpagKGGKGGGYGLAIPKGSKNKEAAKKFLDFLTSPEAQ 293
|
|
| TbpA |
COG4143 |
ABC-type thiamine transport system, periplasmic component TbpA [Coenzyme transport and ... |
58-328 |
3.85e-03 |
|
ABC-type thiamine transport system, periplasmic component TbpA [Coenzyme transport and metabolism];
Pssm-ID: 443315 [Multi-domain] Cd Length: 343 Bit Score: 39.06 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 58 QSEYGVTLKHVKVTDISEAVSRLAVEKtaqKNSAGsiDMVW-INgenfksmkqHQLLSEAFTTRLpnwkFVDQSLPVSSD 136
Cdd:COG4143 55 EAECGCTLEFVAPGDGGELLNRLRLEG---ANPKA--DVVLgLD---------NNLLARALDTGL----FAPHGVDALDA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 137 FAEPtLGLEA-----PWGVGQLVFIYDTKRLSTPPDSFNAMLNYAKANpqRLSYPKPpsfhGTSFLKAALLelsadsnll 211
Cdd:COG4143 117 LALP-LAWDPddrfvPYDYGYFAFVYDKTKLLNPPESLEDLVDPEYKD--KLVVQDP----RTSTPGLAFL--------- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 212 yspvnennfqeisapLW---DYLDEFHKSAWRQ--------GKlfpaSSSETLQLLDDGQLDLavtfnpneVLS------ 274
Cdd:COG4143 181 ---------------LWtiaAYGEDGALDYWQKladngvtvTK----GWSEAYGLFLKGEAPM--------VLSystspa 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 518445122 275 -AQENGTLSESTKAYALKAGALSNIHFLAIPWNAAAKEGALVAINFLLSPEAQSH 328
Cdd:COG4143 234 yHVIAEGDKDRYAAALFDEGHYRQVEGAGVLAGAKNPELARKFLDFLLSPEFQAE 288
|
|
| PBP2_PotD |
cd13660 |
The periplasmic substrate-binding component of an active spermidine-preferential transport ... |
107-324 |
7.89e-03 |
|
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: 37.95 E-value: 7.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 107 MKQHQLLSEAFTTRLPNWKFVDQSLpvSSDFAEPTLGLEAPWGVGQLVFIYDTKRLStpPDSFNAMLNYAKANPQ-RLSY 185
Cdd:cd13660 63 MRKEGLIQKIDKSKITNFSNIDPDF--LNQPFDPNNDYSIPYIWGATALAVNGDAVD--GKSVTSWADLWKPEYKgKLLL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 186 PKPPSfhgtSFLKAALLELSadsnllYSpVNENNFQEISAPLwdyldEFHKSAWRQGKLFpaSSSETLQLLDDGQLDLAV 265
Cdd:cd13660 139 TDDAR----EVFQMALRKLG------YS-GNTKDPEEIEAAF-----EELKKLMPNVAAF--DSDNPANPYMEGEVALGM 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 518445122 266 TFNpNEVLSAQENGTlseSTKAYALKAGALSNIHFLAIPWNAAAKEGALVAINFLLSPE 324
Cdd:cd13660 201 IWN-GSAFVARQANK---PIHVVWPKEGGIFWMDSFAIPANAKNKEGALKFINFLLRPD 255
|
|
| potD |
PRK09501 |
spermidine/putrescine ABC transporter periplasmic substrate-binding protein; Reviewed |
291-380 |
8.25e-03 |
|
spermidine/putrescine ABC transporter periplasmic substrate-binding protein; Reviewed
Pssm-ID: 181913 [Multi-domain] Cd Length: 348 Bit Score: 37.97 E-value: 8.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518445122 291 KAGALSNIHFLAIPWNAAAKEGALVAINFLLSPEAQSHKGDLQVWGDPAV----LYPHYIrgsAKDTTLFkslpephPSW 366
Cdd:PRK09501 249 KEGGIFWMDSLAIPANAKNKEGALKLINFLLRPDVAKQVAETIGYPTPNLaarkLLSPEV---ANDKSLY-------PDA 318
|
90
....*....|....
gi 518445122 367 QTALETEWQKRYGH 380
Cdd:PRK09501 319 ETIKKGEWQNDVGA 332
|
|
| |
