|
Name |
Accession |
Description |
Interval |
E-value |
| PotD |
COG0687 |
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism]; |
1-353 |
6.89e-143 |
|
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
Pssm-ID: 440451 [Multi-domain] Cd Length: 348 Bit Score: 408.53 E-value: 6.89e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 1 MKRFLQLIIGALVVGMLCLTLSHWFKSKEQVHtnqkiyVYNWGEYIDPELIKKFEKETGIQVVYETFDSNEAMEAKIRNG 80
Cdd:COG0687 1 MSRRSLLGLAAAALAAALAGGAPAAAAEGTLN------VYNWGGYIDPDVLEPFEKETGIKVVYDTYDSNEEMLAKLRAG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 81 GTHYDVAFPSEYTVQKLKRDHLLLPIDHNKVPNIKNLDSDYMNMSFDKGNKYSLPYFFGTVGILYNKEKYPNEsFDSWKS 160
Cdd:COG0687 75 GSGYDVVVPSDYFVARLIKAGLLQPLDKSKLPNLANLDPRFKDPPFDPGNVYGVPYTWGTTGIAYNTDKVKEP-PTSWAD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 161 LYNPKFKNQILLVDGAREIIGMSLNKLGYNLNDRNSHHLKEAERDLTKLAPQVRGVVGD--EITMMLQQNEGNIAVVWSG 238
Cdd:COG0687 154 LWDPEYKGKVALLDDPREVLGAALLYLGYDPNSTDPADLDAAFELLIELKPNVRAFWSDgaEYIQLLASGEVDLAVGWSG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 239 VAAPLVQEGDKYNYVIPKEGSNLWFDNMVIPKTAQNKEGAYKFMNFLLDAKNNKQNTEFVGYATPNKAARQLLPKEIKDD 318
Cdd:COG0687 234 DALALRAEGPPIAYVIPKEGALLWFDNMAIPKGAPNPDLAYAFINFMLSPEVAAALAEYVGYAPPNKAARELLPPELAAN 313
|
330 340 350
....*....|....*....|....*....|....*
gi 446742428 319 HRFYPTKKEQERLEVYKDLGPEVLSEYNENFLNFK 353
Cdd:COG0687 314 PAIYPPEEVLDKLEFWNPLPPENRELYTRRWTEIK 348
|
|
| PBP2_PotD_PotF_like |
cd13590 |
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ... |
37-347 |
9.06e-133 |
|
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: 381.58 E-value: 9.06e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 37 IYVYNWGEYIDPELIKKFEKETGIQVVYETFDSNEAMEAKIRNGG-THYDVAFPSEYTVQKLKRDHLLLPIDHNKVPNIK 115
Cdd:cd13590 2 LNIYNWSDYIDPEVLKAFEKETGVKVNYDTYDSNEEMLAKLRAGGgSGYDLVVPSDYMVERLIKQGLLEPLDHSKLPNLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 116 NLDSDYMNMSFDKGNKYSLPYFFGTVGILYNKEKYPNESFDSWKSLYNPKFKNQILLVDGAREIIGMSLNKLGYNLNDRN 195
Cdd:cd13590 82 NLDPQFLNPPYDPGNRYSVPYQWGTTGIAYNKDKVKEPPTSWDLDLWDPALKGRIAMLDDAREVLGAALLALGYSPNTTD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 196 SHHLKEAERDLTKLAPQVRGVVGDEITMMLQQNEGNIAVVWSGVAAPLVQEGDKYNYVIPKEGSNLWFDNMVIPKTAQNK 275
Cdd:cd13590 162 PAELAAAAELLIKQKPNVRAFDSDSYVQDLASGEIWLAQAWSGDALQANRENPNLKFVIPKEGGLLWVDNMAIPKGAPNP 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446742428 276 EGAYKFMNFLLDAKNNKQNTEFVGYATPNKAARQLLPKEIKDDHRFYPTKKEQERLEVYKDLGPEVLSEYNE 347
Cdd:cd13590 242 ELAHAFINFLLDPEVAAKNAEYIGYATPNKAALELLPPELLDNPALYPPIEPLAKLLTFKDVDGEALELYDR 313
|
|
| PBP2_PotD_PotF_like_2 |
cd13663 |
The periplasmic substrate-binding component of an uncharacterized active transport system ... |
36-353 |
8.41e-129 |
|
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: 371.62 E-value: 8.41e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 36 KIYVYNWGEYIDPELIKKFEKETGIQVVYETFDSNEAMEAKIRNGGTHYDVAFPSEYTVQKLKRDHLLLPIDHNKVPNIK 115
Cdd:cd13663 1 TLKVYNWGEYIDPDLIDDFEKETGIKVNYETFDSNEEMYTKIKTGGTSYDVIVPSDYMIEKLIKEDLLQPLDYSKLPNVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 116 ---NLDSDYMNMSFDKGNKYSLPYFFGTVGILYNKEKYPNESFDSWKSLYNPKFKNQILLVDGAREIIGMSLNKLGYNLN 192
Cdd:cd13663 81 kniNIQPDLLNLAFDPINEYSVPYFWGTLGIVYNKTKVSLEELSWWNILWNKKYKGKILMYDSPRDAFMVALKALGYSLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 193 DRNSHHLKEAERDLTKLAPQVRGVVGDEITMMLQQNEGNIAVVWSGVAAPLVQEGDKYNYVIPKEGSNLWFDNMVIPKTA 272
Cdd:cd13663 161 TTNPDEIEEAKDWLIKQKPNVKAFVVDEIKDLMINGNADIAVTYSGDAAYAMEENENLDYVIPKEGSNLWFDNWVIPKNA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 273 QNKEGAYKFMNFLLDAKNNKQNTEFVGYATPNKAARQLLPKE--IKDDHRFYPTKKEQERLEVYKDLGPEVLSEYNENFL 350
Cdd:cd13663 241 KNVDLAYKFINFLLRPDNALKNAEYVGYSTPNAAAEELLPEEesIKDDKIFYPDEDIYKKCEVFKYLGGDAKKEYNDLWL 320
|
...
gi 446742428 351 NFK 353
Cdd:cd13663 321 EVK 323
|
|
| PBP2_PotF |
cd13659 |
The periplasmic substrate-binding component of an ABC putrescine transport system and related ... |
37-347 |
6.61e-96 |
|
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: 288.46 E-value: 6.61e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 37 IYVYNWGEYIDPELIKKFEKETGIQVVYETFDSNEAMEAKIRNGGTHYDVAFPSEYTVQKLKRDHLLLPIDHNKVPNIKN 116
Cdd:cd13659 2 LNVYNWSDYIAPDTLEDFEKETGIKVVYDTYDSNEELEAKLLAGGSGYDLVVPSANFLGRQIKAGALQKLDKSKLPNWKN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 117 LDSDYMNMS--FDKGNKYSLPYFFGTVGILYNKEK----YPNESFDSWKSLYNPKFKNQ-----ILLVDGAREIIGMSLN 185
Cdd:cd13659 82 LDPLLLKLLaaVDPGNRYAVPYMWGTTGIAYNVDKvkaaLGDDLPDSWDLVFDPENLSKlkscgVSVLDSPEEVFPAALN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 186 KLGYNLNDRNSHHLKEAERDLTKLAPQVRGVVGDEITMMLQQNEGNIAVVWSGVA------APLVQEGDKYNYVIPKEGS 259
Cdd:cd13659 162 YLGLDPNSTDPEDIKAAEDLLKKVRPYVRYFHSSKYINDLANGEICVAIGWSGDAvqaaqrAKEAGNGVTLEYVIPKEGA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 260 NLWFDNMVIPKTAQNKEGAYKFMNFLLDAKNNKQNTEFVGYATPNKAARQLLPKEIKDDHRFYPTKKEQERLEVYKDLGP 339
Cdd:cd13659 242 NLWFDMFAIPADAKNPDNAYRFINYLMRPEVIAKISNYVNYANANKAATPLVDEAIKDDPAIYPPEEVLKKLYALPPLSA 321
|
....*...
gi 446742428 340 EVLSEYNE 347
Cdd:cd13659 322 KVQRALTR 329
|
|
| PBP2_PotD |
cd13660 |
The periplasmic substrate-binding component of an active spermidine-preferential transport ... |
37-342 |
5.82e-89 |
|
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: 270.22 E-value: 5.82e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 37 IYVYNWGEYIDPELIKKFEKETGIQVVYETFDSNEAMEAKIRNGGTH-YDVAFPSEYTVQKLKRDHLLLPIDHNKVPNIK 115
Cdd:cd13660 2 LNFYNWSEYVPPELLEQFTKETGIKVILSTYESNETMYAKVKLYKDGaYDLVVPSTYYVDKMRKEGLIQKIDKSKITNFS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 116 NLDSDYMNMSFDKGNKYSLPYFFGTVGILYNKEKYPNESFDSWKSLYNPKFKNQILLVDGAREIIGMSLNKLGYNLNDRN 195
Cdd:cd13660 82 NIDPDFLNQPFDPNNDYSIPYIWGATALAVNGDAVDGKSVTSWADLWKPEYKGKLLLTDDAREVFQMALRKLGYSGNTKD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 196 SHHLKEAERDLTKLAPQVRGVVGDEITMMLQQNEGNIAVVWSGVAAPLVQEGDKYNYVIPKEGSNLWFDNMVIPKTAQNK 275
Cdd:cd13660 162 PEEIEAAFEELKKLMPNVAAFDSDNPANPYMEGEVALGMIWNGSAFVARQANKPIHVVWPKEGGIFWMDSFAIPANAKNK 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446742428 276 EGAYKFMNFLLDAKNNKQNTEFVGYATPNKAARQLLPKEIKDDHRFYPTKKEQERLEVYKDLGPEVL 342
Cdd:cd13660 242 EGALKFINFLLRPDVSKQIAETIGYPTPNLKARKLLSPEVANNKIVYPSAETIKNGEFQNDVGAASL 308
|
|
| potD |
PRK09501 |
spermidine/putrescine ABC transporter periplasmic substrate-binding protein; Reviewed |
1-338 |
3.90e-83 |
|
spermidine/putrescine ABC transporter periplasmic substrate-binding protein; Reviewed
Pssm-ID: 181913 [Multi-domain] Cd Length: 348 Bit Score: 256.38 E-value: 3.90e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 1 MKRFLQLIIGAlvvGMLCLTLShwfksKEQVHTNQKIYVYNWGEYIDPELIKKFEKETGIQVVYETFDSNEAMEAKI--- 77
Cdd:PRK09501 1 MKKWSRHLLAA---GALALGMS-----AAHADDNNTLYFYNWTEYVPPGLLEQFTKETGIKVIYSTYESNETMYAKLkty 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 78 RNGGthYDVAFPSEYTVQKLKRDHLLLPIDHNKVPNIKNLDSDYMNMSFDKGNKYSLPYFFGTVGILYNKEKYPNESFDS 157
Cdd:PRK09501 73 KDGA--YDLVVPSTYYVDKMRKEGMIQKIDKSKLTNFSNLDPDMLNKPFDPNNDYSIPYIWGATAIGVNSDAIDPKSVTS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 158 WKSLYNPKFKNQILLVDGAREIIGMSLNKLGYNLNDRNSHHLKEAERDLTKLAPQVRGVVGDEITMMLQQNEGNIAVVWS 237
Cdd:PRK09501 151 WADLWKPEYKGSLLLTDDAREVFQMALRKLGYSGNTTDPKEIEAAYNELKKLMPNVAAFNSDNPANPYMEGEVNLGMIWN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 238 GVAAPLVQEGDKYNYVIPKEGSNLWFDNMVIPKTAQNKEGAYKFMNFLLDAKNNKQNTEFVGYATPNKAARQLLPKEIKD 317
Cdd:PRK09501 231 GSAFVARQAGTPIDVVWPKEGGIFWMDSLAIPANAKNKEGALKLINFLLRPDVAKQVAETIGYPTPNLAARKLLSPEVAN 310
|
330 340
....*....|....*....|.
gi 446742428 318 DHRFYPTKKEQERLEVYKDLG 338
Cdd:PRK09501 311 DKSLYPDAETIKKGEWQNDVG 331
|
|
| PBP2_PotD_PotF_like_3 |
cd13664 |
TThe periplasmic substrate-binding component of an uncharacterized active transport system ... |
39-346 |
6.23e-66 |
|
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: 211.06 E-value: 6.23e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 39 VYNWGEYIDPELIKKFEKETGIQVVYETFDSNEAMEAKIRNGGTHYDVAFPSEYTVQKLKRDHLLLPIDHNKVPNIKNLD 118
Cdd:cd13664 4 LYNWTDYTSPELLDKFEKETGIKVTLDTYDSNETLLAKLKAGGQGYDVVVPSDSFVPILIKEGLLEPLDKSQLTNYDNID 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 119 SDYMNMSFDKGNKYSLPYFFGTVGILYNKEKYPNESfDSWKSLYNP--KFKNQILLVDGAREIIGMSLNKLGYNLNDRNS 196
Cdd:cd13664 84 PRWRKPDFDPGNEYSIPWQWGTTGFAVDTAVYDGDI-DDYSVIFQPpeELKGKIAMVDSMNEVVNAAIYYLGGPICTTDP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 197 HHLKEAERDLTKLAPQVRGVVGDEITMMLQQNEGNIAVVWSGVAAPLVQEGDKYNYVIPKEGSNLWFDNMVIPKTAQNKE 276
Cdd:cd13664 163 KLMRKVRDLLLEQKPHVKAYDSDGIVERMASGDVAAHVDWNGASLRARRQNPSLAYAYPKEGVLIWSDNLVIPKGAPNYE 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 277 GAYKFMNFLLDAKNNKQNTEFVGYATPNKAARQLLPKEIKDDHRFYPTKKEQERLEVYKDLGPEVLSEYN 346
Cdd:cd13664 243 NARTFLNFIMEPENAALQSNFAGYANAITGAEKFMDDPLKDAPALEIPPPEGSRLKFSTLCPPKAEKLQS 312
|
|
| PRK10682 |
PRK10682 |
putrescine transporter subunit: periplasmic-binding component of ABC superfamily; Provisional |
9-341 |
4.90e-60 |
|
putrescine transporter subunit: periplasmic-binding component of ABC superfamily; Provisional
Pssm-ID: 182645 [Multi-domain] Cd Length: 370 Bit Score: 197.38 E-value: 4.90e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 9 IGALVVGMLcLTLSHWFKSKEQvhtnQKIYVYNWGEYIDPELIKKFEKETGIQVVYETFDSNEAMEAKIRNGGTHYDVAF 88
Cdd:PRK10682 9 LSGLVAGAL-MAVSVGTLAAEQ----KTLHIYNWSDYIAPDTVANFEKETGIKVVYDVFDSNEVLEGKLMAGSTGFDLVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 89 PSEYTVQKLKRDHLLLPIDHNKVPNIKNLDSDYMNM--SFDKGNKYSLPYFFGTVGILYNKEKY-----PNESFDSWKSL 161
Cdd:PRK10682 84 PSASFLERQLTAGVFQPLDKSKLPNWKNLDPELLKLvaKHDPDNKYAMPYMWATTGIGYNVDKVkavlgEDAPVDSWDLV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 162 YNP----KFKN-QILLVDGAREIIGMSLNKLGYNLNDRNSHHLKEAERD-LTKLAPQVRGVVGDEITMMLQQNEGNIAVV 235
Cdd:PRK10682 164 LKPenleKLKScGVSFLDAPEEIFATVLNYLGKDPNSTKADDYTGPATDlLLKLRPNIRYFHSSQYINDLANGDICVAIG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 236 WSG---VAAPLVQE---GDKYNYVIPKEGSNLWFDNMVIPKTAQNKEGAYKFMNFLLDAKNNKQNTEFVGYATPNKAARQ 309
Cdd:PRK10682 244 WAGdvwQASNRAKEaknGVNVSYSIPKEGALAFFDVFAMPADAKNKDEAYQFLNYLLRPDVIAHISDHVFYANANKAATP 323
|
330 340 350
....*....|....*....|....*....|..
gi 446742428 310 LLPKEIKDDHRFYPTKKEQERLEVYKDLGPEV 341
Cdd:PRK10682 324 LVSAEVRDNPGIYPPADVRAKLFTLKVQDPKI 355
|
|
| PBP2_polyamine_1 |
cd13588 |
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ... |
36-307 |
7.41e-60 |
|
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: 194.05 E-value: 7.41e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 36 KIYVYNWGEYIDPELIKKFEKETGIQVVYETFDSNEAMEAKIRNGGTHYDVAFPSEYTVQKLKRDHLLLPIDHNKVPNIK 115
Cdd:cd13588 1 ELNVLTWPGYADPDWVTAFEEATGCKVVVKFFGSEDEMVAKLRSGGGDYDVVTPSGDALLRLIAAGLVQPIDTSKIPNYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 116 NLDSDYMNMSFDKGNK--YSLPYFFGTVGILYNKEKYPNESFDSWKSLYNPKFKNQILLVDGAREIIGMSLNKLGYNLND 193
Cdd:cd13588 81 NIDPRLRNLPWLTVDGkvYGVPYDWGANGLAYNTKKVKTPPTSWLALLWDPKYKGRVAARDDPIDAIADAALYLGQDPPF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 194 RNS-HHLKEAERDLTKLAPQVRGV--VGDEITMMLQQNEGNIAVVWSGVAAPLVQEGDKYNYVIPKEGSNLWFDNMVIPK 270
Cdd:cd13588 161 NLTdEQLDAVKAKLREQRPLVRKYwsDGAELVQLFANGEVVAATAWSGQVNALQKAGKPVAYVIPKEGATGWVDTWMILK 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 446742428 271 TAQNKEGAYKFMNFLLDAKNNKQNTEFVGYATPNKAA 307
Cdd:cd13588 241 DAKNPDCAYKWLNYMLSPKVQAAVAEWTGYAPSNPEA 277
|
|
| PBP2_polyamines |
cd13523 |
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ... |
37-296 |
7.88e-60 |
|
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: 193.81 E-value: 7.88e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 37 IYVYNWGEYIDPELIKKFEKETGIQVVYETFDSNEAMEAKIRNGG-THYDVAFPSEYTVQKLKRDHLLLPIDHNKVPNIK 115
Cdd:cd13523 2 VVIYTWGGYLPQDIIDPFEKETGIKVVVDTAANSERMIKKLSAGGsGGFDLVTPSDSYTSRQLGVGLMQPIDKSLLPSWA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 116 NLDSDYMNMS--FDKGNKYSLPYFFGTVGILYNKEKYPNESFDSWKSLYNPKFKNQILLVDGAREIIGMSLNKLGYNLND 193
Cdd:cd13523 82 TLDPHLTLAAvlTVPGKKYGVPYQWGATGLVYNTDKVKAPPKSYAADLDDPKYKGRVSFSDIPRETFAMALANLGADGNE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 194 RNSH-HLKEAERDLTKLAPQVRGV--VGDEITMMLQQNEGNIAVVWSGVAAPLVQEGDKYNYVIPKEGSNLWFDNMVIPK 270
Cdd:cd13523 162 ELYPdFTDAAAALLKELKPNVKKYwsNASQPANLLLNGEVVLAMAWLGSGFKLKQAGAPIEFVVPKEGAVGWLDTFAVPA 241
|
250 260
....*....|....*....|....*.
gi 446742428 271 TAQNKEGAYKFMNFLLDAKNNKQNTE 296
Cdd:cd13523 242 NAPNKDGAYKLLNALLRPKVAAAVAA 267
|
|
| PBP2_TpPotD_like |
cd13662 |
The periplasmic substrate-binding component of an ABC-type polyamine transport system from ... |
37-314 |
1.20e-55 |
|
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: 184.26 E-value: 1.20e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 37 IYVYNWGEYIDPELIKKFEKETGIQVVYETFDSNEAMEAKIRNGGTHYDVAFPSEYTVQKLKRDHLLLPIDHNKVPNIKN 116
Cdd:cd13662 2 LYIYNWTYYIPDKVIEDFEKETGIRVVYDYYASNEEMYAKLKIGGGGYDIVSPSGDYVSIMKKEGLLEKLDKSKLPNVKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 117 LDSDYMNMS--FDKGNKYSLPYFFGTVGILYNKeKYPNESFDSWKSLYNPKFKNQILLVDGAREIIGMSLNKLGYNLNDR 194
Cdd:cd13662 82 EKDNLMEASkiYDPGLEYSVPYMFGATGIAVNK-KIVKNYFRKWSIFLREDLAGRMTMLDDMREVIGAALAYLGYPVDSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 195 NSHHLKEAERDLTKLAPQVrgVVGDEITMMLQQNEGNIAVVwSGVAAPLVQE-----GDKYNYVIPKE-GSNLWFDNMVI 268
Cdd:cd13662 161 DIEQLEEAKEVILSWKKNL--AKFDSNSYGKGFASGDFWVV-HGYAEDVFYEvpeeeEEKFDFFIPEGaASMMYIDSFVI 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 446742428 269 PKTAQNKEGAYKFMNFLLDAKNNKQNTEFVGYATPNKAARQLLPKE 314
Cdd:cd13662 238 PKGSKHKDNAYKFINFILRPENYAEILDVLGNPSIIKEAEKKSQKK 283
|
|
| PBP2_polyamine_2 |
cd13587 |
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ... |
39-311 |
5.68e-44 |
|
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: 153.36 E-value: 5.68e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 39 VYNWGEYIDPELIKKFEKETGIQVVYETFDSNEAMEAKIR-NGGTHYDVAFPSEYTVQKLKRDHLLLPIDHNKVpNIKNL 117
Cdd:cd13587 4 ILTWAGYAPEDLLEKFENETGIKVQVTTSNNNEEMISKLRaTGGGGFDLAQPSQRIAPNYEEFGLYQPIDESKI-KVAQF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 118 DSDYMNMS----FDKGNKYSLPYFFGTVGILYNKEKYPNESFDSWKSLYNPKFKNQILlVDGAREIIGMSL--NKLGYNL 191
Cdd:cd13587 83 PPSLLESTklgtTINGKRYAVPFDWGTEGLTVNSTKAPDVSGFSYGDLWAPEYAGKVA-YRLKSPLTGLGLyaDATGEDP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 192 NDRNSHHLKEAER-----DLTKLAPQVRGVV------GDEITMMLQQNEGNIAVVWSGVAAPLVQEGDKYNYVIPKEGSN 260
Cdd:cd13587 162 FNRYLDYKDEAKYqkildQVLQFLIERKANVkaywnnADEALAAFRSGGCVIGQTWDSTGLKLNRENPPIDYGAPKEGAL 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 446742428 261 LWFDNMVIPKTAQNKEGAYKFMNFLLDAKNNKQNTEFVGYATPNKAARQLL 311
Cdd:cd13587 242 GWIDTFAIPAKAENVDQAYAFINFMLRPEIAAMFTNATGYNTAAVGAQEFL 292
|
|
| PBP2_polyamine_RpCGA009 |
cd13589 |
The periplasmic-binding component of an uncharacterized ABC transport system from ... |
36-301 |
5.03e-42 |
|
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: 147.37 E-value: 5.03e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 36 KIYVYNWG----EYIDPELIKKFEKETGIQVVYETFDSNEaMEAKIRNGGTH--YDVAFPSEYTVQKLKRDHLLLPIDHN 109
Cdd:cd13589 1 TLVVATWGgsyeDAQRKAVIEPFEKETGIKVVYDTGTSAD-RLAKLQAQAGNpqWDVVDLDDGDAARAIAEGLLEPLDYS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 110 KVPNIKNLDSDYMNMsfdkgNKYSLPYFFGTVGILYNKEKYPNESfDSWkSLYNPKFKNQI----LLVDGAREIIGMSLN 185
Cdd:cd13589 80 KIPNAAKDKAPAALK-----TGYGVGYTLYSTGIAYNTDKFKEPP-TSW-WLADFWDVGKFpgprILNTSGLALLEAALL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 186 KLGYNLNDRNshhLKEAERDLTKLAPQVRGVV--GDEITMMLQQNEGNIAVVWSGVAAPLVQEGDKYNYVIPKEGSNLWF 263
Cdd:cd13589 153 ADGVDPYPLD---VDRAFAKLKELKPNVVTWWtsGAQLAQLLQSGEVDMAPAWNGRAQALIDAGAPVAFVWPKEGAILGP 229
|
250 260 270
....*....|....*....|....*....|....*...
gi 446742428 264 DNMVIPKTAQNKEGAYKFMNFLLDAKNNKQNTEFVGYA 301
Cdd:cd13589 230 DTLAIVKGAPNKELAMKFINFALSPEVQAALAEALGYG 267
|
|
| SBP_bac_8 |
pfam13416 |
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
49-319 |
1.13e-30 |
|
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.
Pssm-ID: 433189 [Multi-domain] Cd Length: 281 Bit Score: 117.89 E-value: 1.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 49 ELIKKFEKETGIQVVYETFDSNEaMEAKIR---NGGTHYD--VAFPSEYTVQKLKRDHLLLPIDHnkVPNIKNLDSDYMN 123
Cdd:pfam13416 1 ALAKAFEKKTGVTVEVEPQASND-LQAKLLaaaAAGNAPDldVVWIAADQLATLAEAGLLADLSD--VDNLDDLPDALDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 124 MSFDkGNKYSLPYFFGTVGIL-YNKEKYPNESFD--SWKSL--YNPKFKNQILLVDGAREIIGMSLNKLGYNLNDRNSHH 198
Cdd:pfam13416 78 AGYD-GKLYGVPYAASTPTVLyYNKDLLKKAGEDpkTWDELlaAAAKLKGKTGLTDPATGWLLWALLADGVDLTDDGKGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 199 --LKEAERDLTKLAPQVRGV-VGDEITMMLQQNEGNIAVVWSGVAAPLVQEGDKYNYVIPKEGSNLWFDNMVIPKTAQNK 275
Cdd:pfam13416 157 eaLDEALAYLKKLKDNGKVYnTGADAVQLFANGEVAMTVNGTWAAAAAKKAGKKLGAVVPKDGSFLGGKGLVVPAGAKDP 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 446742428 276 E-GAYKFMNFLLDAKNNKQNTEFVGYATPNKAArqLLPKEIKDDH 319
Cdd:pfam13416 237 RlAALDFIKFLTSPENQAALAEDTGYIPANKSA--ALSDEVKADP 279
|
|
| AfuA |
COG1840 |
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]; ... |
50-286 |
3.04e-28 |
|
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 441445 [Multi-domain] Cd Length: 286 Bit Score: 111.18 E-value: 3.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 50 LIKKFEKETGIQVVYETFDSNEAMeAKIRN--GGTHYDVAFPSEYTVQ-KLKRDHLLLPIdhnKVPNIKNLDSDYMnmsf 126
Cdd:COG1840 1 LLEAFEKKTGIKVNVVRGGSGELL-ARLKAegGNPPADVVWSGDADALeQLANEGLLQPY---KSPELDAIPAEFR---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 127 DKGNKYsLPYFFGTVGILYNKEKYPNESF-DSWKSLYNPKFKNQILLVDGAREIIGMSLnklgynLNDRNSHHLKE-AER 204
Cdd:COG1840 73 DPDGYW-FGFSVRARVIVYNTDLLKELGVpKSWEDLLDPEYKGKIAMADPSSSGTGYLL------VAALLQAFGEEkGWE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 205 DLTKLAPQVRGVVGDEITM--MLQQNEGNIAVVWSGVAAPLVQEGDKYNYVIPKEGSNLWFDNMVIPKTAQNKEGAYKFM 282
Cdd:COG1840 146 WLKGLAANGARVTGSSSAVakAVASGEVAIGIVNSYYALRAKAKGAPVEVVFPEDGTLVNPSGAAILKGAPNPEAAKLFI 225
|
....
gi 446742428 283 NFLL 286
Cdd:COG1840 226 DFLL 229
|
|
| SBP_bac_6 |
pfam13343 |
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
80-317 |
4.06e-19 |
|
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.
Pssm-ID: 463852 [Multi-domain] Cd Length: 247 Bit Score: 85.49 E-value: 4.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 80 GGTHYDVAFpseytVQKLKRDHLLLPIDHNKVPNIKNlDSDYMNMSFDKGNKYslPYFFGTVGILYNKEKYPNESF-DSW 158
Cdd:pfam13343 11 GDLFFDKRF-----LEKFIEEGLFQPLDSANLPNVPK-DFDDEGLRDPDGYYT--PYGVGPLVIAYNKERLGGRPVpRSW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 159 KSLYNPKFKNQILL----VDGAREIIGMSLNK---------LGYNLndRNSHHLKEAERDLTKLAP--QVRGVVGDEITM 223
Cdd:pfam13343 83 ADLLDPEYKGKVALpgpnVGDLFNALLLALYKdfgedgvrkLARNL--KANLHPAQMVKAAGRLESgePAVYLMPYFFAD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 224 MLQQNEGNIAVVWsgvaaplvqegdkynyviPKEGSNLWFDNMVIPKtaQNKEGAYKFMNFLLDAKNNKQNTEFvGYATP 303
Cdd:pfam13343 161 ILPRKKKNVEVVW------------------PEDGALVSPIFMLVKK--GKKELADPLIDFLLSPEVQAILAKA-GLVFP 219
|
250
....*....|....
gi 446742428 304 NKAARQLLPKEIKD 317
Cdd:pfam13343 220 VVLNPAVDNPLPEG 233
|
|
| UgpB |
COG1653 |
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ... |
1-310 |
6.58e-19 |
|
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 441259 [Multi-domain] Cd Length: 363 Bit Score: 86.64 E-value: 6.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 1 MKRFLQLIIGALVVGM-LCLTLSHWFKSKEQvhtNQKIYVYNWGEYIDP---ELIKKFEKET-GIQVVYETFDSNEAMEa 75
Cdd:COG1653 1 MRRLALALAAALALALaACGGGGSGAAAAAG---KVTLTVWHTGGGEAAaleALIKEFEAEHpGIKVEVESVPYDDYRT- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 76 KIR---NGGTHYDVAFPSEYTVQKLKRDHLLLPIDhNKVPNIKNLDSDYM-----NMSFDkGNKYSLPYFFGTVGILYNK 147
Cdd:COG1653 77 KLLtalAAGNAPDVVQVDSGWLAEFAAAGALVPLD-DLLDDDGLDKDDFLpgaldAGTYD-GKLYGVPFNTDTLGLYYNK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 148 ---EKY---PNESFDSWKSLyNPKFKNQ-----ILLVDGAREIIGMSLNKLGYNLNDR------NSHHLKEAERDLTKLA 210
Cdd:COG1653 155 dlfEKAgldPPKTWDELLAA-AKKLKAKdgvygFALGGKDGAAWLDLLLSAGGDLYDEdgkpafDSPEAVEALEFLKDLV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 211 ------PQVRGVVGDEITMMLQQneGNIAVVWSG--VAAPLVQEGDKYNYVI---------PKEGSNLWFDNMVIPKTAQ 273
Cdd:COG1653 234 kdgyvpPGALGTDWDDARAAFAS--GKAAMMINGswALGALKDAAPDFDVGVaplpggpggKKPASVLGGSGLAIPKGSK 311
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 446742428 274 NKEGAYKFMNFLLDAKNNKQNTEFV----GYATPNKAARQL 310
Cdd:COG1653 312 NPEAAWKFLKFLTSPEAQAKWDALQavllGQKTPEEALDAA 352
|
|
| PBP2_UgpB |
cd14748 |
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ... |
41-318 |
5.11e-17 |
|
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: 81.18 E-value: 5.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 41 NWGEYIDpELIKKFEKE-TGIQVVYETFDSNEAMEAKIRN---GGTHYDVAFPSEYTVQKLKRDHLLLPIDhNKVPNIKN 116
Cdd:cd14748 11 PDGKALE-ELVDEFNKShPDIKVKAVYQGSYDDTLTKLLAalaAGTAPDVAQVDASWVAQLADSGALEPLD-DYIDKDGV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 117 LDSDYM-----NMSFDkGNKYSLPYFFGTVGILYNK---EKY---PNESFDSWKSL--YNPKFKNQillvDGAREIIGMS 183
Cdd:cd14748 89 DDDDFYpaaldAGTYD-GKLYGLPFDTSTPVLYYNKdlfEEAgldPEKPPKTWDELeeAAKKLKDK----GGKTGRYGFA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 184 LNKLGYN--------------LNDR------NSHHLKEA---ERDLTKLAPQVRGVVGDEITMMLQQneGNIAVVWSGVA 240
Cdd:cd14748 164 LPPGDGGwtfqallwqnggdlLDEDggkvtfNSPEGVEAlefLVDLVGKDGVSPLNDWGDAQDAFIS--GKVAMTINGTW 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 241 --APLVQEGDKYNY-VIP-------KEGSNLWFDNMVIPK-TAQNKEGAYKFMNFLLDAKNNKQNTEFVGYATPNKAARQ 309
Cdd:cd14748 242 slAGIRDKGAGFEYgVAPlpagkgkKGATPAGGASLVIPKgSSKKKEAAWEFIKFLTSPENQAKWAKATGYLPVRKSAAE 321
|
....*....
gi 446742428 310 LLPKEIKDD 318
Cdd:cd14748 322 DPEEFLAEN 330
|
|
| PBP2_Fbp_like_1 |
cd13544 |
Substrate binding domain of a putative ferric iron transporter, a member of the type 2 ... |
34-318 |
8.84e-16 |
|
Substrate binding domain of a putative ferric iron transporter, a member of the type 2 periplasmic binding fold superfamily; The substrate domain of this group shows a high homology to the periplasmic component of ferric iron transporter (Fbp), but its biochemical characterization has not been performed. 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. After binding iron with high affinity, Fbp interacts 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 ferric iron-binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.
Pssm-ID: 270262 [Multi-domain] Cd Length: 292 Bit Score: 76.49 E-value: 8.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 34 NQKIYVYNWGEYIDPeLIKKFEKETGIQVVYETFDSNEAMeAKIRNGGTH--YDVAF--PSEYTVQkLKRDHLLLPIdhn 109
Cdd:cd13544 1 ELTVYTSLEEEEAKA-ILEAFKKDTGIKVEFVRLSTGEAL-ARLEAEKGNpqADVWFggTADAHIQ-AKKEGLLEPY--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 110 KVPNIKNLDSDYMnmsfDKGNKYSlPYFFGTVGILYNKE-------KYPnesfDSWKSLYNPKFKNQILLVD------GA 176
Cdd:cd13544 75 KSPNADKIPAKFK----DPDGYWT-GIYLGPLGFGVNTDelkekglPVP----KSWEDLLNPEYKGEIVMPNpassgtAY 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 177 REIIGMsLNKLGYnlndrnshhlKEAERDLTKLAPQVR--GVVGDEITMMLQQNEGNIAVVWSGVAAPLVQEGDKYNYVI 254
Cdd:cd13544 146 TFLASL-IQLMGE----------DEAWEYLKKLNKNVGqyTKSGSAPAKLVASGEAAIGISFLHDALKLKEQGYPIKIIF 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446742428 255 PKEGSNLWFDNMVIPKTAQNKEGAYKFMNFLLDAKNNKQNTEFVGYATPNKAARQLLPKEIKDD 318
Cdd:cd13544 215 PKEGTGYEIEAVAIIKGAKNPEAAKAFIDWALSKEAQELLAKVGSYAIPTNPDAKPPEIAPDLK 278
|
|
| PBP2_TMBP_like |
cd13585 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ... |
49-334 |
1.25e-15 |
|
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: 77.06 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 49 ELIKKFEKE-TGIQVVYETFDsNEAMEAKIRN---GGTHYDVAFPSEYTVQKLKRDHLLLPIDH--NKVPNIKNLDSDYM 122
Cdd:cd13585 18 KLIDAFEKEnPGVKVEVVPVP-YDDYWTKLTTaaaAGTAPDVFYVDGPWVPEFASNGALLDLDDyiEKDGLDDDFPPGLL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 123 NMSFDKGNKYSLPYFFGTVGILYNKE--------KYPNESFDSW----KSLYNPKFKNQILLVDGAREIIGMSLNKL--- 187
Cdd:cd13585 97 DAGTYDGKLYGLPFDADTLVLFYNKDlfdkagpgPKPPWTWDELleaaKKLTDKKGGQYGFALRGGSGGQTQWYPFLwsn 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 188 -GYNLNDRNSHHL------KEA---ERDLTK--LAPQVRGVVGDEITMMLQQneGNIA--VVWSGVAAPLVQEGDKYNY- 252
Cdd:cd13585 177 gGDLLDEDDGKATlnspeaVEAlqfYVDLYKdgVAPSSATTGGDEAVDLFAS--GKVAmmIDGPWALGTLKDSKVKFKWg 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 253 VIP-------KEGSNLWFDNMVIPKTAQNKEGAYKFMNFLLDAKNNKQNTEFVGYATPNKAARQLLPKEIKDDHRFYPTK 325
Cdd:cd13585 255 VAPlpagpggKRASVLGGWGLAISKNSKHPEAAWKFIKFLTSKENQLKLGGAAGPAALAAAAASAAAPDAKPALALAAAA 334
|
....*....
gi 446742428 326 KEQERLEVY 334
Cdd:cd13585 335 DALAAAVPP 343
|
|
| PBP2_Fe3_thiamine_like |
cd13518 |
Substrate binding domain of iron and thiamine transporters-like, a member of the type 2 ... |
36-292 |
2.63e-15 |
|
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: 74.64 E-value: 2.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 36 KIYVYNWGEYID-PELIKKFEKETGIQVVYETFDSNEAMEAKIRNGG-THYDVAFPSEYT-VQKLKRDHLLLPIdhnKVP 112
Cdd:cd13518 1 ELVVYTASDRDFaEPVLKAFEEKTGIKVKAVYDGTGELANRLIAEKNnPQADVFWGGEIIaLEALKEEGLLEPY---TPK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 113 NIKNLdsdymNMSFDKGNKYSLPYFFGTVGILYNKEKYPNESFD-SWKSLYNPKFKNQILLVD----GAREIIGMSLNKL 187
Cdd:cd13518 78 VIEAI-----PADYRDPDGYWVGFAARARVFIYNTDKLKEPDLPkSWDDLLDPKWKGKIVYPTplrsGTGLTHVAALLQL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 188 GYNlndrnshhlKEAERDLTKLAPQVRGVVGD--EITMMLQQNEGNIAVVWSGVAAPLVQEGDKYNYVIPKEGSNLWFDN 265
Cdd:cd13518 153 MGE---------EKGGWYLLKLLANNGKPVAGnsDAYDLVAKGEVAVGLTDTYYAARAAAKGEPVEIVYPDQGALVIPEG 223
|
250 260
....*....|....*....|....*..
gi 446742428 266 MVIPKTAQNKEGAYKFMNFLLDAKNNK 292
Cdd:cd13518 224 VALLKGAPNPEAAKKFIDFLLSPEGQK 250
|
|
| PBP2_PotD_PotF_like_1 |
cd13661 |
The periplasmic substrate-binding component of an uncharacterized active transport system ... |
110-345 |
3.68e-14 |
|
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: 72.45 E-value: 3.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 110 KVPNIKNLDSDYMNMSFDKGNKYSLPYFFGTVGILYNKEKYPNESFD--SWKSLYNPKFKNQILLVDGAREIIGMSLNKL 187
Cdd:cd13661 59 PAADLVTLGDSWLGRAIARGQIWAVPYRWGTTVIAYRKDKLKKLGWDpiDWSDLWRPELAGRIAMVDSPREVIGLVLKKL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 188 GYNLNDRNSHHLKEA-ERDLTKLAPQVRgvvGDEITMMLQQ-NEGN--IAVVWSGVAAPLVQEGDKYNYVIPKEGSNLWF 263
Cdd:cd13661 139 GASYNTAEVPGGREAlEERLAALRRQVK---LYSSNNYLQAlLLGDvwVAVGWSQDIIPLARRYSNLAVVIPRSGTSLWA 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 264 DNMVIPKTAQNKEGA-------YKFMNFLLDAKNNKQNTEFVG-------YATPNKAARQLLPKEIKDDH--RFYPTKKE 327
Cdd:cd13661 216 DLWVIPAGSDFGGRVrgpspllSQWIDFCLQPARATQFAQLSFggaspliLDGPSLTPPEATRKLKLDTNlvLGLPPDEI 295
|
250
....*....|....*...
gi 446742428 328 QERLEVYKDLGPEVLSEY 345
Cdd:cd13661 296 LAKSEFLLPLSEATLAQY 313
|
|
| SBP_bac_1 |
pfam01547 |
Bacterial extracellular solute-binding protein; This family also includes the bacterial ... |
48-292 |
9.56e-14 |
|
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: 70.91 E-value: 9.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 48 PELIKKFEKE-TGIQVVYETFDSNEAME---AKIRNGGTHYDVAFPSEYTVQKLKRDHLLLPIDHNKVPNIKNLDSDYmn 123
Cdd:pfam01547 11 QALVKEFEKEhPGIKVEVESVGSGSLAQkltTAIAAGDGPADVFASDNDWIAELAKAGLLLPLDDYVANYLVLGVPKL-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 124 msfdkgnkYSLPYFFGTVGILYNKEKYPNESFD---SWKSLYNPKFKNQILLVDGAREIIGMSLNKLGY----------- 189
Cdd:pfam01547 89 --------YGVPLAAETLGLIYNKDLFKKAGLDppkTWDELLEAAKKLKEKGKSPGGAGGGDASGTLGYftlallaslgg 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 190 --------NLNDRNSHHLKEAERDLTKLAPQVRGVVGDEITM--------MLQQNEGNIAVVWSGVAAPLVQEGDKYNYV 253
Cdd:pfam01547 161 plfdkdggGLDNPEAVDAITYYVDLYAKVLLLKKLKNPGVAGadgrealaLFEQGKAAMGIVGPWAALAANKVKLKVAFA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 446742428 254 IPKEGSNLWFD---------------NMVIPKTAQNKEGAYKFMNFLLDAKNNK 292
Cdd:pfam01547 241 APAPDPKGDVGyaplpagkggkgggyGLAIPKGSKNKEAAKKFLDFLTSPEAQA 294
|
|
| MalE |
COG2182 |
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism]; |
1-318 |
2.10e-13 |
|
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
Pssm-ID: 441785 [Multi-domain] Cd Length: 410 Bit Score: 70.75 E-value: 2.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 1 MKRFLQLIIGALVVGMLCLTLSHWFKSKEQVHT----NQKIYVYNWGEYIDP--ELIKKFEKETGIQVVYETFDSNEAME 74
Cdd:COG2182 1 MKRRLLAALALALALALALAACGSGSSSSGSSSaagaGGTLTVWVDDDEAEAleEAAAAFEEEPGIKVKVVEVPWDDLRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 75 AKIRNGGTHY--DVA-FPSEYtVQKLKRDHLLLPIDhnkvPNIKNLDsDYM-----NMSFDkGNKYSLPYFFGTVGILYN 146
Cdd:COG2182 81 KLTTAAPAGKgpDVFvGAHDW-LGELAEAGLLAPLD----DDLADKD-DFLpaaldAVTYD-GKLYGVPYAVETLALYYN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 147 KEKYPNESFDSWKSLY-------------------NPKFKNQILLVDGArEIIGMSLNKLG-YNLNDRNShhlKEAERDL 206
Cdd:COG2182 154 KDLVKAEPPKTWDELIaaakkltaagkyglaydagDAYYFYPFLAAFGG-YLFGKDGDDPKdVGLNSPGA---VAALEYL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 207 TKLAPQvrGVVGDEIT--MMLQQ-NEGNIAVVWSGV-AAPLVQEGDKYNY---VIPKE----------GSNLWFdnmvIP 269
Cdd:COG2182 230 KDLIKD--GVLPADADydAADALfAEGKAAMIINGPwAAADLKKALGIDYgvaPLPTLaggkpakpfvGVKGFG----VS 303
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 446742428 270 KTAQNKEGAYKFMNFLLDAKNNKQNTEFVGYATPNKAARQLLpkEIKDD 318
Cdd:COG2182 304 AYSKNKEAAQEFAEYLTSPEAQKALFEATGRIPANKAAAEDA--EVKAD 350
|
|
| PBP2_Fbp_like_2 |
cd13547 |
Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 ... |
36-289 |
1.56e-12 |
|
Substrate binding domain of an uncharacterized ferric iron transporter, 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. This periplasmic domain (Fbp) has high affinity for ferric iron and serves as the primary receptor for transport. After binding iron with high affinity, Fbp interacts 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 ferric iron-binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.
Pssm-ID: 270265 [Multi-domain] Cd Length: 259 Bit Score: 66.86 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 36 KIYVYNWG-EYIDPELIKKFEKE-TGIQVvyETFDSNEA-----MEAKIRNGGTHYDVAFPSE-YTVQKLKRDHLLLPid 107
Cdd:cd13547 1 KLVVYTSMpEDLANALVEAFEKKyPGVKV--EVFRAGTGklmakLAAEAEAGNPQADVLWVADpPTAEALKKEGLLLP-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 108 hNKVPNIKNLDSDYMnmsfDKgNKYSLPYFFGTVGILYNKEKYPNESFDSWKSLYNPKFKNQILLVD-----GAREIIGM 182
Cdd:cd13547 77 -YKSPEADAIPAPFY----DK-DGYYYGTRLSAMGIAYNTDKVPEEAPKSWADLTKPKYKGQIVMPDplysgAALDLVAA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 183 SLNKLGYnlndrnshhlkeAERDLTKLA------PQVRGVVGDEITmmlqQNEGNIAVVWSGVAAPLVQEGDKYNYVIPK 256
Cdd:cd13547 151 LADKYGL------------GWEYFEKLKengvkvEGGNGQVLDAVA----SGERPAGVGVDYNALRAKEKGSPLEVIYPE 214
|
250 260 270
....*....|....*....|....*....|...
gi 446742428 257 EGSNLWFDNMVIPKTAQNKEGAYKFMNFLLDAK 289
Cdd:cd13547 215 EGTVVIPSPIAILKGSKNPEAAKAFVDFLLSPE 247
|
|
| PBP2_BitB |
cd13546 |
Substrate binding domain of a putative iron transporter BitB, a member of the type 2 ... |
37-286 |
4.91e-12 |
|
Substrate binding domain of a putative iron transporter BitB, a member of the type 2 periplasmic binding fold superfamily; The substrate domain of this group shows a high homology to the periplasmic component of ferric iron transporter (Fbp), but its biochemical characterization has not been performed. 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. After binding iron with high affinity, Fbp interacts 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 ferric iron-binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.
Pssm-ID: 270264 [Multi-domain] Cd Length: 258 Bit Score: 65.36 E-value: 4.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 37 IYVYNWGEYIDPeLIKKFEKETGIQVVYETFDSNEAMEaKIRNG-GTHY-DVAFPSEYTVQKLKRDHLllpiDHNKVPNI 114
Cdd:cd13546 4 VYSPNSEEIIEP-IIKEFEEKPGIKVEVVTGGTGELLA-RIKAEaDNPQaDVMWGGGIETLEAYKDLF----EPYESPEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 115 KNLDSDYMNMsfdkgNKYSLPYFFGTVGILYNKEKYPNES-FDSWKSLYNPKFKNQILLVDGAREiiGMSLNKLG--YNL 191
Cdd:cd13546 78 AAIPDAYKSP-----EGLWTGFSVLPVVLMVNTDLVKNIGaPKGWKDLLDPKWKGKIAFADPNKS--GSAYTILYtiLKL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 192 NDrnshhlkEAERDLTKLAPQVrGVVGDEITMMLQ---QNEGNIAVVWSGVAAPLVQEGDKYNYVIPKEGSNLWFDNMVI 268
Cdd:cd13546 151 YG-------GAWEYIEKLLDNL-GVILSSSSAVYKavaDGEYAVGLTYEDAAYKYVAGGAPVKIVYPKEGTTAVPDGVAI 222
|
250
....*....|....*...
gi 446742428 269 PKTAQNKEGAYKFMNFLL 286
Cdd:cd13546 223 VKGAKNPENAKKFIDFLL 240
|
|
| PBP2_TbpA |
cd13545 |
Substrate binding domain of thiamin transporter, a member of the type 2 periplasmic binding ... |
36-286 |
6.04e-11 |
|
Substrate binding domain of thiamin transporter, a member of the type 2 periplasmic binding fold superfamily; Thiamin-binding protein TbpA is the periplasmic component of ABC-type transporter in E. coli, while the transmembrane permease and ATPase are ThiP and ThiQ, respectively. Thiamin (vitamin B1) is an essential confactor in all living systems that most prokaryotes, plants, and fungi can synthesized thiamin. However, in vertebrates, thiamine cannot be synthesized and must therefore be obtained through dietary absorption. In addition to thiamin biosynthesis, most organisms can import thiamin using specific transporters. After binding thiamine with high affinity, TbpA interacts 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 thiamine-binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.
Pssm-ID: 270263 [Multi-domain] Cd Length: 269 Bit Score: 62.32 E-value: 6.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 36 KIYVY-----NWGeyIDPELIKKFEKETGIQVVYETFDSNEAMEAKIRNGG--THYDVAFP-SEYTVQKLKRDHLLLPID 107
Cdd:cd13545 3 TVYTYdsfvgEWG--PGPEVKAEFEKETGCKVEFVKPGDAGELLNRLILEKnnPRADVVLGlDNNLLSRALKEGLFEPYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 108 hnkvpnIKNLDsDYMNMSFDKGNKYSLPYFFGTVGILYNKEKYPNESfDSWKSLYNPKFKNQILLVDGAREIIGmslnkL 187
Cdd:cd13545 81 ------SPALD-VVPEVPVFDPEDRLIPYDYGYLAFNYDKKKFKEPP-LSLEDLTAPEYKGLIVVQDPRTSSPG-----L 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 188 GYNLNDRNSHHLKEAERDLTKLAPQVRGVVGDEITMMLQQNEGNIAVVWSGVAAPL--VQEGDKYNY--VIPKEGSNLWF 263
Cdd:cd13545 148 GFLLWTIAVFGEEGYLEYWKKLKANGVTVTPGWSEAYGLFTTGEAPMVVSYATSPAyhVYYEKDLRYtaVIFPEGHYRQV 227
|
250 260
....*....|....*....|...
gi 446742428 264 DNMVIPKTAQNKEGAYKFMNFLL 286
Cdd:cd13545 228 EGAGILKGAKNPELAKKFVDFLL 250
|
|
| PBP2_Maltose_binding_like |
cd13586 |
The periplasmic-binding component of ABC transport systems specific for maltose and related ... |
36-318 |
1.53e-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: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 36 KIYVYNW----GEYIDpELIKKFEKETGIQVVYETFDSNEAMEAKIRNGGTHY--DVAFPSEYTVQKLKRDHLLLPIDHN 109
Cdd:cd13586 1 TITVWTDedgeLEYLK-ELAEEFEKKYGIKVEVVYVDSGDTREKFITAGPAGKgpDVFFGPHDWLGELAAAGLLAPIPEY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 110 KVPNIKNLDSDYMNMSFDkGNKYSLPYFFGTVGILYNKEKYPN--ESFDSWKSL---YNPKFKNQILLV----------- 173
Cdd:cd13586 80 LAVKIKNLPVALAAVTYN-GKLYGVPVSVETIALFYNKDLVPEppKTWEELIALakkFNDKAGGKYGFAydqtnpyfsyp 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 174 ----DGAR-------EIIGMSLN----KLGYNLNdrnsHHLKEAErdlTKLAPQVRGVVGDEitmmlQQNEGNIAVVWSG 238
Cdd:cd13586 159 flaaFGGYvfgenggDPTDIGLNnegaVKGLKFI----KDLKKKY---KVLPPDLDYDIADA-----LFKEGKAAMIING 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 239 --VAAPLVQEGDkyNY---VIPKEGSNLW---F---DNMVIPKTAQNKEGAYKFMNFLLDAKNNKQNTEFVGYATPNKAA 307
Cdd:cd13586 227 pwDLADYKDAGI--NFgvaPLPTLPGGKQaapFvgvQGAFVSAYSKNKEAAVEFAEYLTSDEAQLLLFEKTGRIPALKDA 304
|
330
....*....|.
gi 446742428 308 RQllPKEIKDD 318
Cdd:cd13586 305 LN--DAAVKND 313
|
|
| SBP_bac_11 |
pfam13531 |
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
49-289 |
1.84e-10 |
|
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.
Pssm-ID: 463911 [Multi-domain] Cd Length: 225 Bit Score: 59.97 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 49 ELIKKFEKETGIQVVYETFDSNEAMEAkIRNGgTHYDVAFP-SEYTVQKLKRDHLLLPIDHNkvpniknldsdymnmsfd 127
Cdd:pfam13531 14 ELAAAFEAETGVKVVVSYGGSGKLAKQ-IANG-APADVFISaDSAWLDKLAAAGLVVPGSRV------------------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 128 kgnkyslPYFFGTVGILYNKEKYPNesFDSWKSLYNPKFKnqILLVDGAREIIG----MSLNKLGynlndrnshHLKEAE 203
Cdd:pfam13531 74 -------PLAYSPLVIAVPKGNPKD--ISGLADLLKPGVR--LAVADPKTAPSGraalELLEKAG---------LLKALE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 204 RDLTKLAPQVRGVVgdeitMMLQQNEGNIAVVWSGVAAPLvQEGDKYNYVIPKEGSNLWFD-NMVIPKTAQNKEGAYKFM 282
Cdd:pfam13531 134 KKVVVLGENVRQAL-----TAVASGEADAGIVYLSEALFP-ENGPGLEVVPLPEDLNLPLDyPAAVLKKAAHPEAARAFL 207
|
....*..
gi 446742428 283 NFLLDAK 289
Cdd:pfam13531 208 DFLLSPE 214
|
|
| TbpA |
COG4143 |
ABC-type thiamine transport system, periplasmic component TbpA [Coenzyme transport and ... |
1-286 |
2.39e-09 |
|
ABC-type thiamine transport system, periplasmic component TbpA [Coenzyme transport and metabolism];
Pssm-ID: 443315 [Multi-domain] Cd Length: 343 Bit Score: 57.93 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 1 MKRFLQLIIGALVVGML---CLTLSHWFKSKEQVHTNQkIYVYNWGeyIDPELIKKFEKETGIQVVYETFDSNEAMEAKI 77
Cdd:COG4143 1 MKRRTFLLAAALALALAlagCSGAAAAAKPTLTVYTYD-SFASEWG--PGPWLKAAFEAECGCTLEFVAPGDGGELLNRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 78 RNGG--THYDVAF---PSEytVQKLKRDHLLLPidhNKVPNIKNLDSDYmnmSFDkGNKYSLPYFFGTVGILYNKEKYPN 152
Cdd:COG4143 78 RLEGanPKADVVLgldNNL--LARALDTGLFAP---HGVDALDALALPL---AWD-PDDRFVPYDYGYFAFVYDKTKLLN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 153 --ESFDswkSLYNPKFKNQILLVDGAREIIGMSLnkLgynlndrnshhlkeaerdltkLApqVRGVVGDEITM-MLQQNE 229
Cdd:COG4143 149 ppESLE---DLVDPEYKDKLVVQDPRTSTPGLAF--L---------------------LW--TIAAYGEDGALdYWQKLA 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 230 GNIAVV---WSGV-------AAPLV------------QEGDKYNY--VIPKEGSNLWFDNMVIPKTAQNKEGAYKFMNFL 285
Cdd:COG4143 201 DNGVTVtkgWSEAyglflkgEAPMVlsystspayhviAEGDKDRYaaALFDEGHYRQVEGAGVLAGAKNPELARKFLDFL 280
|
.
gi 446742428 286 L 286
Cdd:COG4143 281 L 281
|
|
| PBP2_CMBP |
cd13658 |
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ... |
44-318 |
4.08e-07 |
|
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; possess the type 2 periplasmic binding fold; This group includes the periplasmic cyclo/maltodextrin-binding protein of Thermoactinomyces vulgaris ATP-binding cassette transporter and related proteins. Cyclodextrins are a family of compounds composed of glucose units connected by 1, 4 glycosidic linkages to form a series of oligosaccharide rings, and their cavity is hydrophibic which allows cyclodextrins to accomodate hydrophobic molecules/moieties in the cavity. 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: 270376 [Multi-domain] Cd Length: 372 Bit Score: 51.33 E-value: 4.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 44 EYIDpELIKKFEKETGIQVVYETFDSNEAMEAKIRNG--GTHYDVAFPSEYTVQKLKRDHLLLPIDHNKVpNIKNLDSDY 121
Cdd:cd13658 13 AFIK-KIAKQYTKKTGVKVKLVEVDQLDQLEKLSLDGpaGKGPDVMVAPHDRIGSAVLQGLLSPIKLSKD-KKKGFTDQA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 122 MNMSFDKGNKYSLPYFFGTVGILYNKE--KYPNESFDSW----KSLYNPKFKNQILLVD--------GAreIIGM----- 182
Cdd:cd13658 91 LKALTYDGKLYGLPAAVETLALYYNKDlvKNAPKTFDELealaKDLTKEKGKQYGFLADatnfyysyGL--LAGNggyif 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 183 SLNKLGYNLND--RNSHHLKEAERDLTK-----LAPQvrGVVGDEITMMLQqnEGNIAVV----WS-----------GVA 240
Cdd:cd13658 169 KKNGSDLDINDigLNSPGAVKAVKFLKKwytegYLPK--GMTGDVIQGLFK--EGKAAAVidgpWAiqeyqeagvnyGVA 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446742428 241 A-PLVQEGDKYNYVIPKEGsnlWfdnmVIPKTAQNKEGAYKFMNFLLDAKNNKQNTEFVGYATPNKAARQLlpKEIKDD 318
Cdd:cd13658 245 PlPTLPNGKPMAPFLGVKG---W----YLSAYSKHKEWAQKFMEFLTSKENLKKRYDETNEIPPRKDVRSD--PEIKNN 314
|
|
| Periplasmic_Binding_Protein_Type_2 |
cd00648 |
Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent ... |
36-270 |
4.52e-07 |
|
Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent the ligand-binding domains found in solute binding proteins that serve as initial receptors in the transport, signal transduction and channel gating. The PBP2 proteins share the same architecture as periplasmic binding proteins type 1 (PBP1), but have a different topology. They are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The origin of PBP module can be traced across the distant phyla, including eukaryotes, archebacteria, and prokaryotes. The majority of PBP2 proteins are involved in the uptake of a variety of soluble substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the family includes ionotropic glutamate receptors and unorthodox sensor proteins involved in signal transduction. The substrate binding domain of the LysR transcriptional regulators and the oligopeptide-like transport systems also contain the type 2 periplasmic binding fold and thus they are significantly homologous to that of the PBP2; however, these two families are grouped into a separate hierarchy of the PBP2 superfamily due to the large number of protein sequences.
Pssm-ID: 270214 [Multi-domain] Cd Length: 196 Bit Score: 49.88 E-value: 4.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 36 KIYVYNWGEY----IDPELIKKFEKETGIQVVYETFDSNEAMEAKIRNGGthYDVAFPSeytvqklkrdhlllpidhnkv 111
Cdd:cd00648 1 TLTVASIGPPpyagFAEDAAKQLAKETGIKVELVPGSSIGTLIEALAAGD--ADVAVGP--------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 112 pnIKNLDSDYMNMSFDKGNKYSLPYFFGTVGILYNKeKYPNESFDSWKSLYNPKFknqILLVDGAREIIGMSLNKLGYNL 191
Cdd:cd00648 58 --IAPALEAAADKLAPGGLYIVPELYVGGYVLVVRK-GSSIKGLLAVADLDGKRV---GVGDPGSTAVRQARLALGAYGL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 192 NDRNshhlkeaerdltklaPQVRGV-VGDEITMMLQQNEGNIAVVWSGVAAPLVQEGDKYNYVIPKEGSNLWFDNMVIPK 270
Cdd:cd00648 132 KKKD---------------PEVVPVpGTSGALAAVANGAVDAAIVWVPAAERAQLGNVQLEVLPDDLGPLVTTFGVAVRK 196
|
|
| PBP2_FutA1_ilke |
cd13542 |
Substrate binding domain of ferric iron-binding protein, a member of the type 2 periplasmic ... |
36-339 |
8.24e-07 |
|
Substrate binding domain of ferric iron-binding protein, a member of the type 2 periplasmic binding fold superfamily; FutA1 is the periplasmic component of an ABC-type iron transporter and serves as the primary receptor in Synerchosystis species. The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria and is critical for survival of these pathogens within the host. After binding iron with high affinity, FutA1 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: 270260 [Multi-domain] Cd Length: 314 Bit Score: 50.03 E-value: 8.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 36 KIYVYNWGEY-IDPELIKKFEKETGIQVVYeTFDSNEAMEAKIRNGGTHYDVAFP---SEYTVQKLKRDHLLLPIDHNKV 111
Cdd:cd13542 1 EVNVYSSRHYnTDKPLYKAFEKETGIKVNV-VFASADELLERLKAEGANSPADVLltvDAGRLWEAKEAGLLQPVTSEKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 112 PniKNLDSDYMNmsfDKGNKYSLPYFFGTvgILYNKEKYPNESFDSWKSLYNPKFKNQILLVDGAREiigmslnklgYN- 190
Cdd:cd13542 80 E--SNVPANLRD---PDGNWFGLTKRARV--IVYNKDKVNPEELSTYEDLADPKWKGKVCMRSSSNS----------YNq 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 191 --LNDRNSHH-LKEAERDLTK----LAPQVRGvvGDE-ITMMLQQNEGNIAVVWSGVAAPLVqEGDKYNYVIPKEGSNLW 262
Cdd:cd13542 143 slVASMIAHDgEKETKEWLQGwvnnLAREPQG--GDRdQAKAIAAGICDVGIANSYYLGRML-NSEDPEEKEVAEPVGVF 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 263 FDN------------MVIPKTAQNKEGAYKFMNFLLDAKNNKqntefvGYATPNKAarqllpkeikddhrfYPTKKEQER 330
Cdd:cd13542 220 FPNqdnrgthvnisgIGVTKYAKNKENAIKFLEFLVSEPAQK------LYAGGNYE---------------YPVNPGVEL 278
|
....*....
gi 446742428 331 LEVYKDLGP 339
Cdd:cd13542 279 SELVKSWGP 287
|
|
| Lipoprotein_8 |
pfam02030 |
Hypothetical lipoprotein (MG045 family); This family includes hypothetical lipoproteins, the ... |
36-296 |
2.06e-06 |
|
Hypothetical lipoprotein (MG045 family); This family includes hypothetical lipoproteins, the amino terminal part of this protein is related to pfam01547, a family of solute binding proteins. This suggests this family also has a solute binding function.
Pssm-ID: 307931 [Multi-domain] Cd Length: 493 Bit Score: 49.18 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 36 KIYVYNWGEYIDPELIKKFEKETgiQVVYETFDSNEAMEAKIRNggTHYDVAFPSEYTVQKLKRDHLLLPID-------- 107
Cdd:pfam02030 27 KFVVANFESYMSPLLLERAKRKR--PLTFLTYPNNEKLINGFAN--NTYDVAVASAYAVSELAKNGLLKPIDwakfnlkk 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 108 ----HNKVPN-----------IKNLDSDYMNMSFDKGNKYSLPYFFGTVGILYNKEKYPN-ESFD-SW----KSLYNPK- 165
Cdd:pfam02030 103 ennqSITVNNiedakklftkqIWAISNAYKDGKNDELLEWMVPYFLQDLVFVYRGEKIPElEKKDvYWsdviKAIVRHKd 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 166 --FKNQILLVDGAREIigMSLNKLGYNLNDRNSHHLKEAERDLTKLAP-----QVRGVVGDEITMMLQQNEGNI------ 232
Cdd:pfam02030 183 rfNKNRLIAIDDARTI--FSLANIVQLENKNNIIDVNPKELKTNYFLNvyesfSYLGLKLNNLSNMFVNSDSNIvinela 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 233 ------AVVWSGVAA--------------PLVQEGDKYNYVIPKEgSNLWFDNMVIPK-TAQNKEGAYKFMNFLLDAKNN 291
Cdd:pfam02030 261 mgrrqgGIVYNGDAVyaalggdlrdeadeNMKPTGDNFHIVQPKD-SPVALDFLIINSqQKQFEQAAHEYINELALAGAD 339
|
....*
gi 446742428 292 KQNTE 296
Cdd:pfam02030 340 QTKEP 344
|
|
| PBP2_TMBP |
cd14750 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ... |
39-324 |
6.88e-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: 47.67 E-value: 6.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 39 VYNWGEYIDpELIKKFEKETG---IQVVYETFDSNEAMEAKIR---NGGTHYDVAF-----PSEytvqkLKRDHLLLPID 107
Cdd:cd14750 9 DGQEGELLK-KAIAAFEKKHPdikVEIEELPASSDDQRQQLVTalaAGSSAPDVLGldviwIPE-----FAEAGWLLPLT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 108 hnkvPNIKNLDSDYM-----NMSFDKGNKYSLPYFfGTVGIL-YNK---EKYPNESFDSWKSLYN----PKFKNQIL--- 171
Cdd:cd14750 83 ----EYLKEEEDDDFlpatvEANTYDGKLYALPWF-TDAGLLyYRKdllEKYGPEPPKTWDELLEaakkRKAGEPGIwgy 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 172 ---------LVDGAREII----GMSLNKLGYN--LNDRNSHHLKEAERDL--TKLAPQVRGVVG-DEITMMLQQNEGNIA 233
Cdd:cd14750 158 vfqgkqyegLVCNFLELLwsngGDIFDDDSGKvtVDSPEALEALQFLRDLigEGISPKGVLTYGeEEARAAFQAGKAAFM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 234 VVWSGVAAPLVQEGDKYNYVI---------PKEGSNL---WfdNMVIPKTAQNKEGAYKFMNFLLDAKNNKQNTEFVGYA 301
Cdd:cd14750 238 RNWPYAYALLQGPESAVAGKVgvaplpagpGGGSASTlggW--NLAISANSKHKEAAWEFVKFLTSPEVQKRRAINGGLP 315
|
330 340
....*....|....*....|...
gi 446742428 302 TPNKAARQllPKEIKDDHRFYPT 324
Cdd:cd14750 316 PTRRALYD--DPEVLEAYPFLPA 336
|
|
| PBP2_ABC_oligosaccharides |
cd13522 |
The periplasmic-binding component of ABC transport systems specific for maltose and related ... |
36-316 |
9.90e-06 |
|
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: 47.02 E-value: 9.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 36 KIYVYNWGEYID----PELIKKFEKETG---IQVVYETFDSNEAMEAKIRNGGTHYDVAFPSEYTVQKLKRDHLLLPIDH 108
Cdd:cd13522 1 TITVWHQYDTGEnqavNELIAKFEKAYPgitVEVTYQDTEARRQFFSTAAAGGKGPDVVFGPSDSLGPFAAAGLLAPLDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 109 NKVPNIKNLDSDYMNMSFDkGNKYSLPYFFGTVGILYNKEKYPNESFDSWKSLYNpkfknqILLVDGAREIIGMSLN-KL 187
Cdd:cd13522 81 YVSKSGKYAPNTIAAMKLN-GKLYGVPVSVGAHLMYYNKKLVPKNPPKTWQELIA------LAQGLKAKNVWGLVYNqNE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 188 GYNL---------------NDRNSHHLKEAE--------RDLtKLAPQVRGVVGDEITMMLQQNEGNIAVVWSG-VAAPL 243
Cdd:cd13522 154 PYFFaawiggfggqvfkanNGKNNPTLDTPGavealqflVDL-KSKYKIMPPETDYSIADALFKAGKAAMIINGpWDLGD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 244 VQEGDKYNY---VIPKEGSNLWFDNMV------IPKTAQNKEGAYKFMNFLLDAKNNKQNTEFVGYATPNKAARQLLPKE 314
Cdd:cd13522 233 YRQALKINLgvaPLPTFSGTKHAAPFVggkgfgINKESQNKAAAVEFVKYLTSYQAQLVLFDDAGDIPANLQAYESPAVQ 312
|
..
gi 446742428 315 IK 316
Cdd:cd13522 313 NK 314
|
|
| PBP2_Fbp_like_6 |
cd13552 |
Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 ... |
51-288 |
1.81e-04 |
|
Substrate binding domain of an uncharacterized ferric iron transporter, 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. This periplasmic domain (Fbp) has high affinity for ferric iron and serves as the primary receptor for transport. After binding iron with high affinity, Fbp interacts 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 ferric iron-binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.
Pssm-ID: 270270 [Multi-domain] Cd Length: 266 Bit Score: 42.44 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 51 IKKFEKETGIQVVYETFDSNEAMEaKIR--NGGTHYDVAF--PSEyTVQKLKRDHLLLPIDhnkvPNIKNldsdymnmSF 126
Cdd:cd13552 17 EDAFEEKTGVEVEWLNMGSQELLD-RVRaeKENPQADVWWggPSQ-LFMQLKEEGLLEPTE----PSWAE--------KV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 127 DKGNKYSLPYFFGT----VGILYNKEKY-PNESFDSWKSLYNPKFKNQIL----LVDGAREIIGMSLNKLGYnlndRNSH 197
Cdd:cd13552 83 AAEFKDADGYWYGTiqtpEVIMYNTELLsEEEAPKDWDDLLDPKWKDKIIirnpLASGTMRTIFAALIQREL----KGTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446742428 198 HLKEAERDLTKLAPQVRGVVGDEITMMLQQNEGNIAV-VWSGVAAPLVQEGDKY--NYVIPKEGSNLWFDNMVIPKTAQN 274
Cdd:cd13552 159 SLDAGYAWLKKLDANTKEYAASPTMLYLKIGRGEAAIsLWNLNDVLDQRENNKMpfGFIDPASGAPVITDGIALIKGAPH 238
|
250
....*....|....
gi 446742428 275 KEGAYKFMNFLLDA 288
Cdd:cd13552 239 PEAAKAFYEFVGSA 252
|
|
| |
