|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11622 |
PRK11622 |
ABC transporter substrate-binding protein; |
32-424 |
0e+00 |
|
ABC transporter substrate-binding protein;
Pssm-ID: 183238 [Multi-domain] Cd Length: 401 Bit Score: 568.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527639138 32 ASTQLQSRWQQIESLGKNQSVYFYAWGGDAQINAYIQWAAQQVKAKYNINLVHVKLSDTSEAVSRVLAEKSANNNDKGSV 111
Cdd:PRK11622 21 ASDAENKDWQQILEEAKGQTVYFYAWGGSPAINRYLDWVAKELKERYGITLKHVKLADIAEAVNRLLAEKQAGRDTGGSV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527639138 112 DLIWINGANFATMSEHSLLLKQWANKLPNFSYTDPSnnPAVNFDFGIPTNGMEAPWGQASLTFYYDSLAIdgtanNTLPT 191
Cdd:PRK11622 101 DLVWINGENFRTLKEAGLLYGPFAETLPNWRYVDTS--LPVREDFGVPTEGLEAPWGGAQLVFIYDSART-----PQPPQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527639138 192 TLNQLLSWSAQNPGRFSYPKPPDFLGMSFLKYALVMLHQQsdetlKAQLNQPATAQNTAQVLNPLWDFLNKLHPTLWRGG 271
Cdd:PRK11622 174 SPAELLEWAKANPGRFTYPRPPDFTGTAFLKQLLYELTGD-----PAALKQPVDKATFARVTAPLWDYLDELHPYLWREG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527639138 272 KHFMQSGAQMRRLVGDTELSIAFTFSAPEVPAAVKRYDLPKSIRSYAMQDGSLSNTHFVAIPYNASHAQSAQLVANFLLS 351
Cdd:PRK11622 249 KTFPASPAELDQLLADGELDLAMTFNPNHAQSKIANGELPASTRSFVFDDGTIGNTHFVAIPFNANAKAGAKVVANFLLS 328
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2527639138 352 PEAQAQKQKAPIWGDKSVLIQSTLAPQQQALFKTTQPHPSALPLNSIKRTLSEPHPSWVNAIVQGWQTRFGVS 424
Cdd:PRK11622 329 PEAQLRKADPAVWGDPSVLDPQKLPEEQRAAFAALDLGAATLQPELLPPALPEPHASWVEALEQEWQRRYGTH 401
|
|
| YnjB |
COG4134 |
ABC-type uncharacterized transport system YnjBCD, periplasmic component [General function ... |
30-422 |
1.78e-174 |
|
ABC-type uncharacterized transport system YnjBCD, periplasmic component [General function prediction only];
Pssm-ID: 443309 [Multi-domain] Cd Length: 401 Bit Score: 493.22 E-value: 1.78e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527639138 30 SLASTQLQSRWQQIESLGKNQSVYFYAWGGDAQINAYIQ-WAAQQVKAKYNINLVHVKLSDTSEAVSRVLAEKSANNNDK 108
Cdd:COG4134 17 ACSAALAAADWQAIEAEARGQTVYFNAWGGDPNINDYIDdWVAPQLKERYGITLEHVKLADTADAVNRVLAEKQAGKDDG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527639138 109 GSVDLIWINGANFATMSEHSLLLKQWANKLPNFSYTDPsNNPAVNFDFGIPTNGMEAPWGQASLTFYYDSLAIDgtannT 188
Cdd:COG4134 97 GSVDLIWINGENFAAMKEAGLLFGPFAEKLPNWAYVDT-EKPTVTTDFGVPVDGYEAPWGMAQLVFIYDSARVP-----N 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527639138 189 LPTTLNQLLSWSAQNPGRFSYPKPPDFLGMSFLKYALVMLHQQSDetlkaQLNQPATAQNTAQVLNPLWDFLNKLHPTLW 268
Cdd:COG4134 171 PPRSLAELLEWAKANPGRFTYPAPPDFTGSTFLKQALYELTGDPD-----ALQQPVDEAKFAKVTAPLWAYLDELHPYLW 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527639138 269 RGGKHFMQSGAQMRRLVGDTELSIAFTFSAPEVPAAVKRYDLPKSIRSYAMQDGSLSNTHFVAIPYNASHAQSAQLVANF 348
Cdd:COG4134 246 RQGKTYPASNAALDQLLADGEIDMAMSFNPAEASSAIANGELPPTVRTFVFDGGTIGNTHFLAIPFNAPNKAGAMVVANF 325
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2527639138 349 LLSPEAQAQKQKAPIWGDKSVLIQSTLAPQQQALFKTTQPHPSALPLNSIKRTLSEPHPSWVNAIVQGWQTRFG 422
Cdd:COG4134 326 LLSPEAQARKADPAVWGDPTVLDLDKLPAEQRAAFDALPLGPATLSPEELGNALPEPHASWVEAIEEEWLKRYG 399
|
|
| SBP_bac_8 |
pfam13416 |
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
69-357 |
2.21e-11 |
|
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.
Pssm-ID: 433189 [Multi-domain] Cd Length: 281 Bit Score: 63.96 E-value: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527639138 69 WAAQQVKAKYNINLVHVKlSDTSEAVSRVLAEKSANNNdkGSVDLIWINGANFATMSEHSLLLKqwANKLPNFSYTDPSN 148
Cdd:pfam13416 1 ALAKAFEKKTGVTVEVEP-QASNDLQAKLLAAAAAGNA--PDLDVVWIAADQLATLAEAGLLAD--LSDVDNLDDLPDAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527639138 149 NpAVNFD---FGIPTNGmeapwgQASLTFYYDSLAIDGTANNtlPTTLNQLLSWSAQNPGRFSYPKPPDFLGMSFLKYAL 225
Cdd:pfam13416 76 D-AAGYDgklYGVPYAA------STPTVLYYNKDLLKKAGED--PKTWDELLAAAAKLKGKTGLTDPATGWLLWALLADG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527639138 226 VMLhqqsDETLKAQLNQPATaqntaqvlnplWDFLNKlhptlWRGGKHFMQSGAQMRRLVGDTElsIAFTFSAPEVPAAV 305
Cdd:pfam13416 147 VDL----TDDGKGVEALDEA-----------LAYLKK-----LKDNGKVYNTGADAVQLFANGE--VAMTVNGTWAAAAA 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2527639138 306 KRYDLPksirsYAM---QDGSLSNTHFVAIPYNASHAQ-SAQLVANFLLSPEAQAQ 357
Cdd:pfam13416 205 KKAGKK-----LGAvvpKDGSFLGGKGLVVPAGAKDPRlAALDFIKFLTSPENQAA 255
|
|
| PBP2_PotD_PotF_like |
cd13590 |
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ... |
52-357 |
7.63e-09 |
|
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: 56.86 E-value: 7.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527639138 52 VYFYAWGGdaqinaYIqwaAQQV----KAKYNINLVHVKLSDTSEAVSRVLAEKsannndKGSVDLIWINGANFATMSEH 127
Cdd:cd13590 2 LNIYNWSD------YI---DPEVlkafEKETGVKVNYDTYDSNEEMLAKLRAGG------GSGYDLVVPSDYMVERLIKQ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527639138 128 SLLLKQWANKLPNFSYTDPSNNPaVNFDfgiPTNGMEAPWGQASLTFYYDSLAIDGtanntlPTTLNQLLSWSAQNPGRF 207
Cdd:cd13590 67 GLLEPLDHSKLPNLKNLDPQFLN-PPYD---PGNRYSVPYQWGTTGIAYNKDKVKE------PPTSWDLDLWDPALKGRI 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527639138 208 S-YPKPPDFLGMsflkyALVMLHQQSDETLKAQLNQpatAQNTAQVLNPLWDFLNklhptlwrggkhfmqsGAQMRRLVG 286
Cdd:cd13590 137 AmLDDAREVLGA-----ALLALGYSPNTTDPAELAA---AAELLIKQKPNVRAFD----------------SDSYVQDLA 192
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2527639138 287 DTELSIAFTFSAPEVPAAVK----RYDLPKsirsyamqDGSLSNTHFVAIPYNASHAQSAQLVANFLLSPEAQAQ 357
Cdd:cd13590 193 SGEIWLAQAWSGDALQANREnpnlKFVIPK--------EGGLLWVDNMAIPKGAPNPELAHAFINFLLDPEVAAK 259
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11622 |
PRK11622 |
ABC transporter substrate-binding protein; |
32-424 |
0e+00 |
|
ABC transporter substrate-binding protein;
Pssm-ID: 183238 [Multi-domain] Cd Length: 401 Bit Score: 568.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527639138 32 ASTQLQSRWQQIESLGKNQSVYFYAWGGDAQINAYIQWAAQQVKAKYNINLVHVKLSDTSEAVSRVLAEKSANNNDKGSV 111
Cdd:PRK11622 21 ASDAENKDWQQILEEAKGQTVYFYAWGGSPAINRYLDWVAKELKERYGITLKHVKLADIAEAVNRLLAEKQAGRDTGGSV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527639138 112 DLIWINGANFATMSEHSLLLKQWANKLPNFSYTDPSnnPAVNFDFGIPTNGMEAPWGQASLTFYYDSLAIdgtanNTLPT 191
Cdd:PRK11622 101 DLVWINGENFRTLKEAGLLYGPFAETLPNWRYVDTS--LPVREDFGVPTEGLEAPWGGAQLVFIYDSART-----PQPPQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527639138 192 TLNQLLSWSAQNPGRFSYPKPPDFLGMSFLKYALVMLHQQsdetlKAQLNQPATAQNTAQVLNPLWDFLNKLHPTLWRGG 271
Cdd:PRK11622 174 SPAELLEWAKANPGRFTYPRPPDFTGTAFLKQLLYELTGD-----PAALKQPVDKATFARVTAPLWDYLDELHPYLWREG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527639138 272 KHFMQSGAQMRRLVGDTELSIAFTFSAPEVPAAVKRYDLPKSIRSYAMQDGSLSNTHFVAIPYNASHAQSAQLVANFLLS 351
Cdd:PRK11622 249 KTFPASPAELDQLLADGELDLAMTFNPNHAQSKIANGELPASTRSFVFDDGTIGNTHFVAIPFNANAKAGAKVVANFLLS 328
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2527639138 352 PEAQAQKQKAPIWGDKSVLIQSTLAPQQQALFKTTQPHPSALPLNSIKRTLSEPHPSWVNAIVQGWQTRFGVS 424
Cdd:PRK11622 329 PEAQLRKADPAVWGDPSVLDPQKLPEEQRAAFAALDLGAATLQPELLPPALPEPHASWVEALEQEWQRRYGTH 401
|
|
| YnjB |
COG4134 |
ABC-type uncharacterized transport system YnjBCD, periplasmic component [General function ... |
30-422 |
1.78e-174 |
|
ABC-type uncharacterized transport system YnjBCD, periplasmic component [General function prediction only];
Pssm-ID: 443309 [Multi-domain] Cd Length: 401 Bit Score: 493.22 E-value: 1.78e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527639138 30 SLASTQLQSRWQQIESLGKNQSVYFYAWGGDAQINAYIQ-WAAQQVKAKYNINLVHVKLSDTSEAVSRVLAEKSANNNDK 108
Cdd:COG4134 17 ACSAALAAADWQAIEAEARGQTVYFNAWGGDPNINDYIDdWVAPQLKERYGITLEHVKLADTADAVNRVLAEKQAGKDDG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527639138 109 GSVDLIWINGANFATMSEHSLLLKQWANKLPNFSYTDPsNNPAVNFDFGIPTNGMEAPWGQASLTFYYDSLAIDgtannT 188
Cdd:COG4134 97 GSVDLIWINGENFAAMKEAGLLFGPFAEKLPNWAYVDT-EKPTVTTDFGVPVDGYEAPWGMAQLVFIYDSARVP-----N 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527639138 189 LPTTLNQLLSWSAQNPGRFSYPKPPDFLGMSFLKYALVMLHQQSDetlkaQLNQPATAQNTAQVLNPLWDFLNKLHPTLW 268
Cdd:COG4134 171 PPRSLAELLEWAKANPGRFTYPAPPDFTGSTFLKQALYELTGDPD-----ALQQPVDEAKFAKVTAPLWAYLDELHPYLW 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527639138 269 RGGKHFMQSGAQMRRLVGDTELSIAFTFSAPEVPAAVKRYDLPKSIRSYAMQDGSLSNTHFVAIPYNASHAQSAQLVANF 348
Cdd:COG4134 246 RQGKTYPASNAALDQLLADGEIDMAMSFNPAEASSAIANGELPPTVRTFVFDGGTIGNTHFLAIPFNAPNKAGAMVVANF 325
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2527639138 349 LLSPEAQAQKQKAPIWGDKSVLIQSTLAPQQQALFKTTQPHPSALPLNSIKRTLSEPHPSWVNAIVQGWQTRFG 422
Cdd:COG4134 326 LLSPEAQARKADPAVWGDPTVLDLDKLPAEQRAAFDALPLGPATLSPEELGNALPEPHASWVEAIEEEWLKRYG 399
|
|
| PotD |
COG0687 |
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism]; |
49-357 |
9.54e-12 |
|
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
Pssm-ID: 440451 [Multi-domain] Cd Length: 348 Bit Score: 65.70 E-value: 9.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527639138 49 NQSVYFYAWGGdaqinaYIQ-WAAQQVKAKYNINLVHVKLSDTSEAVSRVLAEKSannndkgSVDLIWINGANFATMSEH 127
Cdd:COG0687 28 EGTLNVYNWGG------YIDpDVLEPFEKETGIKVVYDTYDSNEEMLAKLRAGGS-------GYDVVVPSDYFVARLIKA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527639138 128 SLLLKQWANKLPNFSYTDPSnnpAVNFDFGiPTNGMEAPWgqaslTFYYDSLAIDGTANNTLPTTLNQLlsWSAQNPGRF 207
Cdd:COG0687 95 GLLQPLDKSKLPNLANLDPR---FKDPPFD-PGNVYGVPY-----TWGTTGIAYNTDKVKEPPTSWADL--WDPEYKGKV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527639138 208 SYPK-PPDFLGMsflkyALVMLHQQSDETLKAQLNQpataqntaqvlnpLWDFLNKLHPtLWRGgkhFMQSGAQMRRLVG 286
Cdd:COG0687 164 ALLDdPREVLGA-----ALLYLGYDPNSTDPADLDA-------------AFELLIELKP-NVRA---FWSDGAEYIQLLA 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2527639138 287 DTELSIAFTFSaPEVPAAVKRYdlpKSIRSYAMQDGSLSNTHFVAIPYNASHAQSAQLVANFLLSPEAQAQ 357
Cdd:COG0687 222 SGEVDLAVGWS-GDALALRAEG---PPIAYVIPKEGALLWFDNMAIPKGAPNPDLAYAFINFMLSPEVAAA 288
|
|
| SBP_bac_8 |
pfam13416 |
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
69-357 |
2.21e-11 |
|
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.
Pssm-ID: 433189 [Multi-domain] Cd Length: 281 Bit Score: 63.96 E-value: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527639138 69 WAAQQVKAKYNINLVHVKlSDTSEAVSRVLAEKSANNNdkGSVDLIWINGANFATMSEHSLLLKqwANKLPNFSYTDPSN 148
Cdd:pfam13416 1 ALAKAFEKKTGVTVEVEP-QASNDLQAKLLAAAAAGNA--PDLDVVWIAADQLATLAEAGLLAD--LSDVDNLDDLPDAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527639138 149 NpAVNFD---FGIPTNGmeapwgQASLTFYYDSLAIDGTANNtlPTTLNQLLSWSAQNPGRFSYPKPPDFLGMSFLKYAL 225
Cdd:pfam13416 76 D-AAGYDgklYGVPYAA------STPTVLYYNKDLLKKAGED--PKTWDELLAAAAKLKGKTGLTDPATGWLLWALLADG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527639138 226 VMLhqqsDETLKAQLNQPATaqntaqvlnplWDFLNKlhptlWRGGKHFMQSGAQMRRLVGDTElsIAFTFSAPEVPAAV 305
Cdd:pfam13416 147 VDL----TDDGKGVEALDEA-----------LAYLKK-----LKDNGKVYNTGADAVQLFANGE--VAMTVNGTWAAAAA 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2527639138 306 KRYDLPksirsYAM---QDGSLSNTHFVAIPYNASHAQ-SAQLVANFLLSPEAQAQ 357
Cdd:pfam13416 205 KKAGKK-----LGAvvpKDGSFLGGKGLVVPAGAKDPRlAALDFIKFLTSPENQAA 255
|
|
| AfuA |
COG1840 |
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]; ... |
71-356 |
9.01e-11 |
|
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 441445 [Multi-domain] Cd Length: 286 Bit Score: 62.26 E-value: 9.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527639138 71 AQQVKAKYNINLVHVKLSdTSEAVSRVLAEKsannnDKGSVDLIWINGA-NFATMSEHSLLLK---QWANKLPNfSYTDP 146
Cdd:COG1840 2 LEAFEKKTGIKVNVVRGG-SGELLARLKAEG-----GNPPADVVWSGDAdALEQLANEGLLQPyksPELDAIPA-EFRDP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527639138 147 SNNPavnfdFGIPTNGMeapwgqaslTFYYDSLAIDGtanNTLPTTLNQLLswsaqNP---GRFSYPKPpdflGMSFLKY 223
Cdd:COG1840 75 DGYW-----FGFSVRAR---------VIVYNTDLLKE---LGVPKSWEDLL-----DPeykGKIAMADP----SSSGTGY 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527639138 224 ALV--MLHQQSDEtlkaqlnqpataqntaqvlnPLWDFLNKLHptlwRGGKHFMQSGAQMRRLVGDTELSIAFTFSApev 301
Cdd:COG1840 129 LLVaaLLQAFGEE--------------------KGWEWLKGLA----ANGARVTGSSSAVAKAVASGEVAIGIVNSY--- 181
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2527639138 302 pAAVKRYDLPKSIRSYAMQDGSLSNTHFVAIPYNASHAQSAQLVANFLLSPEAQA 356
Cdd:COG1840 182 -YALRAKAKGAPVEVVFPEDGTLVNPSGAAILKGAPNPEAAKLFIDFLLSDEGQE 235
|
|
| PBP2_PotD_PotF_like |
cd13590 |
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ... |
52-357 |
7.63e-09 |
|
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: 56.86 E-value: 7.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527639138 52 VYFYAWGGdaqinaYIqwaAQQV----KAKYNINLVHVKLSDTSEAVSRVLAEKsannndKGSVDLIWINGANFATMSEH 127
Cdd:cd13590 2 LNIYNWSD------YI---DPEVlkafEKETGVKVNYDTYDSNEEMLAKLRAGG------GSGYDLVVPSDYMVERLIKQ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527639138 128 SLLLKQWANKLPNFSYTDPSNNPaVNFDfgiPTNGMEAPWGQASLTFYYDSLAIDGtanntlPTTLNQLLSWSAQNPGRF 207
Cdd:cd13590 67 GLLEPLDHSKLPNLKNLDPQFLN-PPYD---PGNRYSVPYQWGTTGIAYNKDKVKE------PPTSWDLDLWDPALKGRI 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527639138 208 S-YPKPPDFLGMsflkyALVMLHQQSDETLKAQLNQpatAQNTAQVLNPLWDFLNklhptlwrggkhfmqsGAQMRRLVG 286
Cdd:cd13590 137 AmLDDAREVLGA-----ALLALGYSPNTTDPAELAA---AAELLIKQKPNVRAFD----------------SDSYVQDLA 192
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2527639138 287 DTELSIAFTFSAPEVPAAVK----RYDLPKsirsyamqDGSLSNTHFVAIPYNASHAQSAQLVANFLLSPEAQAQ 357
Cdd:cd13590 193 SGEIWLAQAWSGDALQANREnpnlKFVIPK--------EGGLLWVDNMAIPKGAPNPELAHAFINFLLDPEVAAK 259
|
|
| PBP2_polyamine_RpCGA009 |
cd13589 |
The periplasmic-binding component of an uncharacterized ABC transport system from ... |
51-357 |
1.15e-06 |
|
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: 49.53 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527639138 51 SVYFYAWGG---DAQINAYIQWAAqqvkAKYNINlVHVKLSDTSEAVSRVLAEKsannnDKGSVDLIWINGANFATMSEH 127
Cdd:cd13589 1 TLVVATWGGsyeDAQRKAVIEPFE----KETGIK-VVYDTGTSADRLAKLQAQA-----GNPQWDVVDLDDGDAARAIAE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527639138 128 SLLLKQWANKLPNFSYTDPsNNPAVNfDFGIPTNgmeapwgQASLTFYYDSLAIDGtanntlPTTLNQLlsWSAQNPGRF 207
Cdd:cd13589 71 GLLEPLDYSKIPNAAKDKA-PAALKT-GYGVGYT-------LYSTGIAYNTDKFKE------PPTSWWL--ADFWDVGKF 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527639138 208 SYPKPPDFLGMSFLKYALVMLhqqsdetlkaqlNQPATAQNTAqvlnPLWDFLNKLHP---TLWRggkhfmqSGAQMRRL 284
Cdd:cd13589 134 PGPRILNTSGLALLEAALLAD------------GVDPYPLDVD----RAFAKLKELKPnvvTWWT-------SGAQLAQL 190
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2527639138 285 VGDTELSIAFTFSAPevPAAVKRYDLPksIRSYAMQDGSLSNTHFVAIPYNASHAQSAQLVANFLLSPEAQAQ 357
Cdd:cd13589 191 LQSGEVDMAPAWNGR--AQALIDAGAP--VAFVWPKEGAILGPDTLAIVKGAPNKELAMKFINFALSPEVQAA 259
|
|
| PBP2_Fe3_thiamine_like |
cd13518 |
Substrate binding domain of iron and thiamine transporters-like, a member of the type 2 ... |
75-356 |
2.22e-06 |
|
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: 48.84 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527639138 75 KAKYNINLVHVKLSdTSEAVSRVLAEKSANNNDkgsvdlIWINGANFAT--MSEHSLLlkqwanklpnfSYTDPSNNPAV 152
Cdd:cd13518 21 EEKTGIKVKAVYDG-TGELANRLIAEKNNPQAD------VFWGGEIIALeaLKEEGLL-----------EPYTPKVIEAI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527639138 153 NFDFGIPtNGMEAPWGQASLTFYYDSlaiDGTANNTLPTTLNQLLSwSAQNpGRFSYPKPPDFlGMSFLKYALVMLHQQS 232
Cdd:cd13518 83 PADYRDP-DGYWVGFAARARVFIYNT---DKLKEPDLPKSWDDLLD-PKWK-GKIVYPTPLRS-GTGLTHVAALLQLMGE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527639138 233 DETlkaqlnqpataqntaqvlnplWDFLNKLhptLWRGGKhFMQSGAQMRRLVGDTELSIAFTFSapEVPAAVKRYDLPK 312
Cdd:cd13518 156 EKG---------------------GWYLLKL---LANNGK-PVAGNSDAYDLVAKGEVAVGLTDT--YYAARAAAKGEPV 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2527639138 313 SIrsYAMQDGSLSNTHFVAIPYNASHAQSAQLVANFLLSPEAQA 356
Cdd:cd13518 209 EI--VYPDQGALVIPEGVALLKGAPNPEAAKKFIDFLLSPEGQK 250
|
|
| PBP2_polyamines |
cd13523 |
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ... |
51-357 |
8.38e-06 |
|
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: 47.05 E-value: 8.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527639138 51 SVYFYAWGGDAQINAYIQWAAQQ-VKakyninlVHVKLSDTSEAVSRVLAEKSannndKGSVDLIWINGANFATMSEHSL 129
Cdd:cd13523 1 TVVIYTWGGYLPQDIIDPFEKETgIK-------VVVDTAANSERMIKKLSAGG-----SGGFDLVTPSDSYTSRQLGVGL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527639138 130 LLKQWANKLPNFSYTDPSNNPAVNFDFGIPTNGMEAPWGQASLTfyYDSLAIDGtanntlPTTLNQLLSWSAQNPGRFSY 209
Cdd:cd13523 69 MQPIDKSLLPSWATLDPHLTLAAVLTVPGKKYGVPYQWGATGLV--YNTDKVKA------PPKSYAADLDDPKYKGRVSF 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527639138 210 PKPPDFLGMSFLKYalvmlhqqsdetLKAQLNQPATAQNTAQVLNPLwdFLNKLHPtlwrggKHFMQSGAQMRRLV--GD 287
Cdd:cd13523 141 SDIPRETFAMALAN------------LGADGNEELYPDFTDAAAALL--KELKPNV------KKYWSNASQPANLLlnGE 200
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527639138 288 TELSIAFTFSApevpAAVKRYDLPksIRSYAMQDGSLSNTHFVAIPYNASHAQSAQLVANFLLSPEAQAQ 357
Cdd:cd13523 201 VVLAMAWLGSG----FKLKQAGAP--IEFVVPKEGAVGWLDTFAVPANAPNKDGAYKLLNALLRPKVAAA 264
|
|
| SBP_bac_1 |
pfam01547 |
Bacterial extracellular solute-binding protein; This family also includes the bacterial ... |
65-356 |
3.42e-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: 42.40 E-value: 3.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527639138 65 AYIQWAAQQVKAKYNINlvhVKLSDTSEAVSRVLAEKSANNNDkGSVDLIWINGANFATMSEhslllKQWAnkLPNFSYT 144
Cdd:pfam01547 9 ALQALVKEFEKEHPGIK---VEVESVGSGSLAQKLTTAIAAGD-GPADVFASDNDWIAELAK-----AGLL--LPLDDYV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527639138 145 DPSNNPAVNFDFGIPtngmeapWGQASLTFYYDSLAIDgTANNTLPTTLNQLLSWSAQ---NPGRFSYPKPPDFLGMSFL 221
Cdd:pfam01547 78 ANYLVLGVPKLYGVP-------LAAETLGLIYNKDLFK-KAGLDPPKTWDELLEAAKKlkeKGKSPGGAGGGDASGTLGY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527639138 222 kYALVMLHQQSDETLKAQLNQPATAQNTAQVLNPLWDFLNKLHPTLWRGGKHFMQSGAQMRRLV--GDTELSIAFTFSA- 298
Cdd:pfam01547 150 -FTLALLASLGGPLFDKDGGGLDNPEAVDAITYYVDLYAKVLLLKKLKNPGVAGADGREALALFeqGKAAMGIVGPWAAl 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2527639138 299 ------PEVPAAVKRYDLPKSIRSYAM--QDGSLSNTHFVAIPYNASHAQSAQLVANFLLSPEAQA 356
Cdd:pfam01547 229 aankvkLKVAFAAPAPDPKGDVGYAPLpaGKGGKGGGYGLAIPKGSKNKEAAKKFLDFLTSPEAQA 294
|
|
| SBP_bac_6 |
pfam13343 |
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
253-356 |
8.59e-03 |
|
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.
Pssm-ID: 463852 [Multi-domain] Cd Length: 247 Bit Score: 37.72 E-value: 8.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527639138 253 LNPLWDFLNKLhptlwRGGKHFMQSGAQMRRLV-GDTELSIAFTFSAPEVPAAVKRYDL--PKsirsyamqDGSLSNTHF 329
Cdd:pfam13343 118 EDGVRKLARNL-----KANLHPAQMVKAAGRLEsGEPAVYLMPYFFADILPRKKKNVEVvwPE--------DGALVSPIF 184
|
90 100
....*....|....*....|....*..
gi 2527639138 330 VAIPynASHAQSAQLVANFLLSPEAQA 356
Cdd:pfam13343 185 MLVK--KGKKELADPLIDFLLSPEVQA 209
|
|
| |
