|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10682 |
PRK10682 |
putrescine transporter subunit: periplasmic-binding component of ABC superfamily; Provisional |
1-370 |
0e+00 |
|
putrescine transporter subunit: periplasmic-binding component of ABC superfamily; Provisional
Pssm-ID: 182645 [Multi-domain] Cd Length: 370 Bit Score: 792.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 1 MTALGKKWLTGVITGALMAVSAGSLAAEQKTLHVYNWSDYIAPDTVANFEKETGIKVVYDVFDSNEVLEGKLMAGSTGFD 80
Cdd:PRK10682 1 MTALNKKWLSGLVAGALMAVSVGTLAAEQKTLHIYNWSDYIAPDTVANFEKETGIKVVYDVFDSNEVLEGKLMAGSTGFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 81 LVVPSASFLERQLAAGVFQPLDKSKLPNWKNLDPKVLQLVARHDPDNKYAMPYMWATTGIGYNVDKVKAALGKDAPLNSW 160
Cdd:PRK10682 81 LVVPSASFLERQLTAGVFQPLDKSKLPNWKNLDPELLKLVAKHDPDNKYAMPYMWATTGIGYNVDKVKAVLGEDAPVDSW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 161 DLVLKPENLEKLKSCGVSFLDAPEEIFSTVLNYLGKDPNSTKADDYTGPATDLLLKLRPNIRYFHSSQYINDLANGDICV 240
Cdd:PRK10682 161 DLVLKPENLEKLKSCGVSFLDAPEEIFATVLNYLGKDPNSTKADDYTGPATDLLLKLRPNIRYFHSSQYINDLANGDICV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 241 AIGWAGDVWQAANRAKEAKNGVNISYFIPKEGALAFFDVFAMPADAKNKDEAYQFLNYLLRPEVIAHISDHVYYANANKE 320
Cdd:PRK10682 241 AIGWAGDVWQASNRAKEAKNGVNVSYSIPKEGALAFFDVFAMPADAKNKDEAYQFLNYLLRPDVIAHISDHVFYANANKA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 695799972 321 ATPLVSADIRNNPAIYPPEDVFAKLFTLKVQDPKIDRVRTRAWTKVKSGK 370
Cdd:PRK10682 321 ATPLVSAEVRDNPGIYPPADVRAKLFTLKVQDPKIDRVRTRAWTKVKSGK 370
|
|
| PBP2_PotF |
cd13659 |
The periplasmic substrate-binding component of an ABC putrescine transport system and related ... |
31-363 |
0e+00 |
|
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: 562.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 31 TLHVYNWSDYIAPDTVANFEKETGIKVVYDVFDSNEVLEGKLMAGSTGFDLVVPSASFLERQLAAGVFQPLDKSKLPNWK 110
Cdd:cd13659 1 TLNVYNWSDYIAPDTLEDFEKETGIKVVYDTYDSNEELEAKLLAGGSGYDLVVPSANFLGRQIKAGALQKLDKSKLPNWK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 111 NLDPKVLQLVARHDPDNKYAMPYMWATTGIGYNVDKVKAALGKDAPlNSWDLVLKPENLEKLKSCGVSFLDAPEEIFSTV 190
Cdd:cd13659 81 NLDPLLLKLLAAVDPGNRYAVPYMWGTTGIAYNVDKVKAALGDDLP-DSWDLVFDPENLSKLKSCGVSVLDSPEEVFPAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 191 LNYLGKDPNSTKADDYtGPATDLLLKLRPNIRYFHSSQYINDLANGDICVAIGWAGDVWQAANRAKEAKNGVNISYFIPK 270
Cdd:cd13659 160 LNYLGLDPNSTDPEDI-KAAEDLLKKVRPYVRYFHSSKYINDLANGEICVAIGWSGDAVQAAQRAKEAGNGVTLEYVIPK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 271 EGALAFFDVFAMPADAKNKDEAYQFLNYLLRPEVIAHISDHVYYANANKEATPLVSADIRNNPAIYPPEDVFAKLFTLKV 350
Cdd:cd13659 239 EGANLWFDMFAIPADAKNPDNAYRFINYLMRPEVIAKISNYVNYANANKAATPLVDEAIKDDPAIYPPEEVLKKLYALPP 318
|
330
....*....|...
gi 695799972 351 QDPKIDRVRTRAW 363
Cdd:cd13659 319 LSAKVQRALTRAW 331
|
|
| PotD |
COG0687 |
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism]; |
4-367 |
8.76e-149 |
|
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
Pssm-ID: 440451 [Multi-domain] Cd Length: 348 Bit Score: 423.94 E-value: 8.76e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 4 LGKKWLTGVITGALMAVSAG--SLAAEQKTLHVYNWSDYIAPDTVANFEKETGIKVVYDVFDSNEVLEGKLMAGSTGFDL 81
Cdd:COG0687 1 MSRRSLLGLAAAALAAALAGgaPAAAAEGTLNVYNWGGYIDPDVLEPFEKETGIKVVYDTYDSNEEMLAKLRAGGSGYDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 82 VVPSASFLERQLAAGVFQPLDKSKLPNWKNLDPKVLQLVarHDPDNKYAMPYMWATTGIGYNVDKVKaalgkdAPLNSWD 161
Cdd:COG0687 81 VVPSDYFVARLIKAGLLQPLDKSKLPNLANLDPRFKDPP--FDPGNVYGVPYTWGTTGIAYNTDKVK------EPPTSWA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 162 LVLKPENLEKlkscgVSFLDAPEEIFSTVLNYLGKDPNSTKADDYTgPATDLLLKLRPNIRYFHSS--QYINDLANGDIC 239
Cdd:COG0687 153 DLWDPEYKGK-----VALLDDPREVLGAALLYLGYDPNSTDPADLD-AAFELLIELKPNVRAFWSDgaEYIQLLASGEVD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 240 VAIGWAGDVWQAANRakeaknGVNISYFIPKEGALAFFDVFAMPADAKNKDEAYQFLNYLLRPEVIAHISDHVYYANANK 319
Cdd:COG0687 227 LAVGWSGDALALRAE------GPPIAYVIPKEGALLWFDNMAIPKGAPNPDLAYAFINFMLSPEVAAALAEYVGYAPPNK 300
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 695799972 320 EATPLVSADIRNNPAIYPPEDVFAKLFTLKVQDPKIDRVRTRAWTKVK 367
Cdd:COG0687 301 AARELLPPELAANPAIYPPEEVLDKLEFWNPLPPENRELYTRRWTEIK 348
|
|
| PBP2_PotD_PotF_like |
cd13590 |
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ... |
31-363 |
3.11e-126 |
|
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: 365.40 E-value: 3.11e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 31 TLHVYNWSDYIAPDTVANFEKETGIKVVYDVFDSNEVLEGKLMAGS-TGFDLVVPSASFLERQLAAGVFQPLDKSKLPNW 109
Cdd:cd13590 1 ELNIYNWSDYIDPEVLKAFEKETGVKVNYDTYDSNEEMLAKLRAGGgSGYDLVVPSDYMVERLIKQGLLEPLDHSKLPNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 110 KNLDPKVLQLVarHDPDNKYAMPYMWATTGIGYNVDKVKAalgkdaPLNSWDLVLKPENLeklkSCGVSFLDAPEEIFST 189
Cdd:cd13590 81 KNLDPQFLNPP--YDPGNRYSVPYQWGTTGIAYNKDKVKE------PPTSWDLDLWDPAL----KGRIAMLDDAREVLGA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 190 VLNYLGKDPNSTKADDyTGPATDLLLKLRPNIRYFHSSQYINDLANGDICVAIGWAGDVWQAANRAKeakngvNISYFIP 269
Cdd:cd13590 149 ALLALGYSPNTTDPAE-LAAAAELLIKQKPNVRAFDSDSYVQDLASGEIWLAQAWSGDALQANRENP------NLKFVIP 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 270 KEGALAFFDVFAMPADAKNKDEAYQFLNYLLRPEVIAHISDHVYYANANKEATPLVSADIRNNPAIYPPEDVFAKLFTLK 349
Cdd:cd13590 222 KEGGLLWVDNMAIPKGAPNPELAHAFINFLLDPEVAAKNAEYIGYATPNKAALELLPPELLDNPALYPPIEPLAKLLTFK 301
|
330
....*....|....
gi 695799972 350 VQDPKIDRVRTRAW 363
Cdd:cd13590 302 DVDGEALELYDRIW 315
|
|
| PBP2_polyamines |
cd13523 |
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ... |
31-311 |
4.28e-115 |
|
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: 335.56 E-value: 4.28e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 31 TLHVYNWSDYIAPDTVANFEKETGIKVVYDVFDSNEVLEGKLMA-GSTGFDLVVPSASFLERQLAAGVFQPLDKSKLPNW 109
Cdd:cd13523 1 TVVIYTWGGYLPQDIIDPFEKETGIKVVVDTAANSERMIKKLSAgGSGGFDLVTPSDSYTSRQLGVGLMQPIDKSLLPSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 110 KNLDPKVLQLVARHDPDNKYAMPYMWATTGIGYNVDKVKaalgkdAPLNSWdlvlKPENLEKLKSCGVSFLDAPEEIFST 189
Cdd:cd13523 81 ATLDPHLTLAAVLTVPGKKYGVPYQWGATGLVYNTDKVK------APPKSY----AADLDDPKYKGRVSFSDIPRETFAM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 190 VLNYLGKDPNSTKADDYTGPATDLLLKLRPNIRYFHS--SQYINDLANGDICVAIGWAGDVWQAANRakeaknGVNISYF 267
Cdd:cd13523 151 ALANLGADGNEELYPDFTDAAAALLKELKPNVKKYWSnaSQPANLLLNGEVVLAMAWLGSGFKLKQA------GAPIEFV 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 695799972 268 IPKEGALAFFDVFAMPADAKNKDEAYQFLNYLLRPEVIAHISDH 311
Cdd:cd13523 225 VPKEGAVGWLDTFAVPANAPNKDGAYKLLNALLRPKVAAAVAAT 268
|
|
| PBP2_PotD_PotF_like_3 |
cd13664 |
TThe periplasmic substrate-binding component of an uncharacterized active transport system ... |
31-363 |
1.20e-75 |
|
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: 236.49 E-value: 1.20e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 31 TLHVYNWSDYIAPDTVANFEKETGIKVVYDVFDSNEVLEGKLMAGSTGFDLVVPSASFLERQLAAGVFQPLDKSKLPNWK 110
Cdd:cd13664 1 ELNLYNWTDYTSPELLDKFEKETGIKVTLDTYDSNETLLAKLKAGGQGYDVVVPSDSFVPILIKEGLLEPLDKSQLTNYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 111 NLDPKVLQLVArhDPDNKYAMPYMWATTGIGYNVDKVkaalgkDAPLNSWDLVLKPENLEKLKscgVSFLDAPEEIFSTV 190
Cdd:cd13664 81 NIDPRWRKPDF--DPGNEYSIPWQWGTTGFAVDTAVY------DGDIDDYSVIFQPPEELKGK---IAMVDSMNEVVNAA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 191 LNYLGKDPNSTKADDYTgPATDLLLKLRPNIRYFHSSQYINDLANGDICVAIGWAGdvwqAANRAKEAKNgvNISYFIPK 270
Cdd:cd13664 150 IYYLGGPICTTDPKLMR-KVRDLLLEQKPHVKAYDSDGIVERMASGDVAAHVDWNG----ASLRARRQNP--SLAYAYPK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 271 EGALAFFDVFAMPADAKNKDEAYQFLNYLLRPEVIAHISDHVYYANANKEATPLVSADIRNNPAIYPPEDVFAKLFTLKV 350
Cdd:cd13664 223 EGVLIWSDNLVIPKGAPNYENARTFLNFIMEPENAALQSNFAGYANAITGAEKFMDDPLKDAPALEIPPPEGSRLKFSTL 302
|
330
....*....|...
gi 695799972 351 QDPKIDRVRTRAW 363
Cdd:cd13664 303 CPPKAEKLQSRIW 315
|
|
| PBP2_PotD_PotF_like_2 |
cd13663 |
The periplasmic substrate-binding component of an uncharacterized active transport system ... |
31-367 |
6.32e-72 |
|
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: 227.17 E-value: 6.32e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 31 TLHVYNWSDYIAPDTVANFEKETGIKVVYDVFDSNEVLEGKLMAGSTGFDLVVPSASFLERQLAAGVFQPLDKSKLPNWK 110
Cdd:cd13663 1 TLKVYNWGEYIDPDLIDDFEKETGIKVNYETFDSNEEMYTKIKTGGTSYDVIVPSDYMIEKLIKEDLLQPLDYSKLPNVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 111 ---NLDPKVLQLvaRHDPDNKYAMPYMWATTGIGYNVDKVkaalgKDAPLNSWDLVLKPENLEKlkscgVSFLDAPEEIF 187
Cdd:cd13663 81 kniNIQPDLLNL--AFDPINEYSVPYFWGTLGIVYNKTKV-----SLEELSWWNILWNKKYKGK-----ILMYDSPRDAF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 188 STVLNYLGKDPNSTKaDDYTGPATDLLLKLRPNIRYFHSSQYINDLANGDICVAIGWAGDvwqaANRAKEaKNgVNISYF 267
Cdd:cd13663 149 MVALKALGYSLNTTN-PDEIEEAKDWLIKQKPNVKAFVVDEIKDLMINGNADIAVTYSGD----AAYAME-EN-ENLDYV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 268 IPKEGALAFFDVFAMPADAKNKDEAYQFLNYLLRPEVIAHISDHVYYA--NANKEATPLVSADIRNNPAIYPPEDVFAKL 345
Cdd:cd13663 222 IPKEGSNLWFDNWVIPKNAKNVDLAYKFINFLLRPDNALKNAEYVGYStpNAAAEELLPEEESIKDDKIFYPDEDIYKKC 301
|
330 340
....*....|....*....|..
gi 695799972 346 FTLKVQDPKIDRVRTRAWTKVK 367
Cdd:cd13663 302 EVFKYLGGDAKKEYNDLWLEVK 323
|
|
| PBP2_PotD |
cd13660 |
The periplasmic substrate-binding component of an active spermidine-preferential transport ... |
31-340 |
6.11e-69 |
|
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: 219.38 E-value: 6.11e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 31 TLHVYNWSDYIAPDTVANFEKETGIKVVYDVFDSNEVLEGKL-MAGSTGFDLVVPSASFLERQLAAGVFQPLDKSKLPNW 109
Cdd:cd13660 1 TLNFYNWSEYVPPELLEQFTKETGIKVILSTYESNETMYAKVkLYKDGAYDLVVPSTYYVDKMRKEGLIQKIDKSKITNF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 110 KNLDPKVLQlvARHDPDNKYAMPYMWATTGIGYNVDkvkaALGKDApLNSWDLVLKPENLEKLkscgvSFLDAPEEIFST 189
Cdd:cd13660 81 SNIDPDFLN--QPFDPNNDYSIPYIWGATALAVNGD----AVDGKS-VTSWADLWKPEYKGKL-----LLTDDAREVFQM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 190 VLNYLGKDPNSTKADDYTGpATDLLLKLRPNIRYFHSSQYINDLANGDICVAIGWAGDVWQAANRAKeakngvNISYFIP 269
Cdd:cd13660 149 ALRKLGYSGNTKDPEEIEA-AFEELKKLMPNVAAFDSDNPANPYMEGEVALGMIWNGSAFVARQANK------PIHVVWP 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695799972 270 KEGALAFFDVFAMPADAKNKDEAYQFLNYLLRPEVIAHISDHVYYANANKEATPLVSADIRNNPAIYPPED 340
Cdd:cd13660 222 KEGGIFWMDSFAIPANAKNKEGALKFINFLLRPDVSKQIAETIGYPTPNLKARKLLSPEVANNKIVYPSAE 292
|
|
| potD |
PRK09501 |
spermidine/putrescine ABC transporter periplasmic substrate-binding protein; Reviewed |
6-344 |
7.04e-68 |
|
spermidine/putrescine ABC transporter periplasmic substrate-binding protein; Reviewed
Pssm-ID: 181913 [Multi-domain] Cd Length: 348 Bit Score: 217.48 E-value: 7.04e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 6 KKWLTGVITGALMAVSAGSLAA-EQKTLHVYNWSDYIAPDTVANFEKETGIKVVYDVFDSNEVLEGKLMAGSTG-FDLVV 83
Cdd:PRK09501 2 KKWSRHLLAAGALALGMSAAHAdDNNTLYFYNWTEYVPPGLLEQFTKETGIKVIYSTYESNETMYAKLKTYKDGaYDLVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 84 PSASFLERQLAAGVFQPLDKSKLPNWKNLDPKVLQlvARHDPDNKYAMPYMWATTGIGYNVDKVKAAlgkdaPLNSWDLV 163
Cdd:PRK09501 82 PSTYYVDKMRKEGMIQKIDKSKLTNFSNLDPDMLN--KPFDPNNDYSIPYIWGATAIGVNSDAIDPK-----SVTSWADL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 164 LKPENLEKLkscgvSFLDAPEEIFSTVLNYLGKDPNSTKADDYTGpATDLLLKLRPNIRYFHSSQYINDLANGDICVAIG 243
Cdd:PRK09501 155 WKPEYKGSL-----LLTDDAREVFQMALRKLGYSGNTTDPKEIEA-AYNELKKLMPNVAAFNSDNPANPYMEGEVNLGMI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 244 WAGDVWQAanraKEAKNGVNISYfiPKEGALAFFDVFAMPADAKNKDEAYQFLNYLLRPEVIAHISDHVYYANANKEATP 323
Cdd:PRK09501 229 WNGSAFVA----RQAGTPIDVVW--PKEGGIFWMDSLAIPANAKNKEGALKLINFLLRPDVAKQVAETIGYPTPNLAARK 302
|
330 340
....*....|....*....|.
gi 695799972 324 LVSADIRNNPAIYPPEDVFAK 344
Cdd:PRK09501 303 LLSPEVANDKSLYPDAETIKK 323
|
|
| PBP2_polyamine_1 |
cd13588 |
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ... |
31-321 |
8.17e-63 |
|
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: 202.14 E-value: 8.17e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 31 TLHVYNWSDYIAPDTVANFEKETGIKVVYDVFDSNEVLEGKLMAGSTGFDLVVPSASFLERQLAAGVFQPLDKSKLPNWK 110
Cdd:cd13588 1 ELNVLTWPGYADPDWVTAFEEATGCKVVVKFFGSEDEMVAKLRSGGGDYDVVTPSGDALLRLIAAGLVQPIDTSKIPNYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 111 NLDPKvLQLVARHDPDNK-YAMPYMWATTGIGYNVDKVKAalgkdAPLNSWDLVLKPENLEKlkscgVSFLDAPEEIFST 189
Cdd:cd13588 81 NIDPR-LRNLPWLTVDGKvYGVPYDWGANGLAYNTKKVKT-----PPTSWLALLWDPKYKGR-----VAARDDPIDAIAD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 190 VLNYLG-KDPNSTKADDYTGpATDLLLKLRPNIR-YFHSS-QYINDLANGDICVAIGWAGdvwqAANRAKeaKNGVNISY 266
Cdd:cd13588 150 AALYLGqDPPFNLTDEQLDA-VKAKLREQRPLVRkYWSDGaELVQLFANGEVVAATAWSG----QVNALQ--KAGKPVAY 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 695799972 267 FIPKEGALAFFDVFAMPADAKNKDEAYQFLNYLLRPEVIAHISDHVYYANANKEA 321
Cdd:cd13588 223 VIPKEGATGWVDTWMILKDAKNPDCAYKWLNYMLSPKVQAAVAEWTGYAPSNPEA 277
|
|
| PBP2_TpPotD_like |
cd13662 |
The periplasmic substrate-binding component of an ABC-type polyamine transport system from ... |
31-341 |
1.41e-62 |
|
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: 202.75 E-value: 1.41e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 31 TLHVYNWSDYIAPDTVANFEKETGIKVVYDVFDSNEVLEGKLMAGSTGFDLVVPSASFLERQLAAGVFQPLDKSKLPNWK 110
Cdd:cd13662 1 VLYIYNWTYYIPDKVIEDFEKETGIRVVYDYYASNEEMYAKLKIGGGGYDIVSPSGDYVSIMKKEGLLEKLDKSKLPNVK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 111 NLDPKVLQLVARHDPDNKYAMPYMWATTGIGYNvdkvKAALGKDAplNSWDLVLKpenlEKLKScGVSFLDAPEEIFSTV 190
Cdd:cd13662 81 EEKDNLMEASKIYDPGLEYSVPYMFGATGIAVN----KKIVKNYF--RKWSIFLR----EDLAG-RMTMLDDMREVIGAA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 191 LNYLGKdPNSTKADDYTGPATDLLLKLRPNIRYFHSSQYINDLANGDICVAIGWAGDVWQAANRAKEAkngvNISYFIPK 270
Cdd:cd13662 150 LAYLGY-PVDSKDIEQLEEAKEVILSWKKNLAKFDSNSYGKGFASGDFWVVHGYAEDVFYEVPEEEEE----KFDFFIPE 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695799972 271 EGA-LAFFDVFAMPADAKNKDEAYQFLNYLLRPEVIAHISDHVYYANANKEAtplvSADIRNNPAIYPPEDV 341
Cdd:cd13662 225 GAAsMMYIDSFVIPKGSKHKDNAYKFINFILRPENYAEILDVLGNPSIIKEA----EKKSQKKPIIYAEEDL 292
|
|
| PBP2_polyamine_RpCGA009 |
cd13589 |
The periplasmic-binding component of an uncharacterized ABC transport system from ... |
49-315 |
1.01e-37 |
|
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: 136.59 E-value: 1.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 49 FEKETGIKVVYDVFDSNEVLeGKLMA--GSTGFDLVVPSASFLERQLAAGVFQPLDKSKLPNWKNLDPKvlqlvARHDpd 126
Cdd:cd13589 23 FEKETGIKVVYDTGTSADRL-AKLQAqaGNPQWDVVDLDDGDAARAIAEGLLEPLDYSKIPNAAKDKAP-----AALK-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 127 NKYAMPYMWATTGIGYNVDKVKAalgkdaPLNSWDLvLKPENLEKLK------SCGVSFLdapeEIFstvLNYLGKDPNS 200
Cdd:cd13589 95 TGYGVGYTLYSTGIAYNTDKFKE------PPTSWWL-ADFWDVGKFPgprilnTSGLALL----EAA---LLADGVDPYP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 201 TKADdytgPATDLLLKLRPNIRYFHSS--QYINDLANGDICVAIGWAGDVWQAAnrakeaKNGVNISYFIPKEGALAFFD 278
Cdd:cd13589 161 LDVD----RAFAKLKELKPNVVTWWTSgaQLAQLLQSGEVDMAPAWNGRAQALI------DAGAPVAFVWPKEGAILGPD 230
|
250 260 270
....*....|....*....|....*....|....*..
gi 695799972 279 VFAMPADAKNKDEAYQFLNYLLRPEVIAHISDHVYYA 315
Cdd:cd13589 231 TLAIVKGAPNKELAMKFINFALSPEVQAALAEALGYG 267
|
|
| PBP2_polyamine_2 |
cd13587 |
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ... |
31-321 |
9.82e-36 |
|
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: 131.79 E-value: 9.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 31 TLHVYNWSDYIAPDTVANFEKETGIKVVYDVFDSNEVLEGKLMA-GSTGFDLVVPSASFLERQLAAGVFQPLDKSKLpNW 109
Cdd:cd13587 1 TLRILTWAGYAPEDLLEKFENETGIKVQVTTSNNNEEMISKLRAtGGGGFDLAQPSQRIAPNYEEFGLYQPIDESKI-KV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 110 KNLDPKVLQ---LVARHDpDNKYAMPYMWATTGIGYNVDKVKAALGkdapLNSWDLvLKPENLEKlkscgVSFldAPEEI 186
Cdd:cd13587 80 AQFPPSLLEstkLGTTIN-GKRYAVPFDWGTEGLTVNSTKAPDVSG----FSYGDL-WAPEYAGK-----VAY--RLKSP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 187 FSTVLNYL---GKDPnSTKADDYTGPAT---------DLLLKLRPNIRYF--HSSQYINDLANGDICVAIGWAGDVWqaa 252
Cdd:cd13587 147 LTGLGLYAdatGEDP-FNRYLDYKDEAKyqkildqvlQFLIERKANVKAYwnNADEALAAFRSGGCVIGQTWDSTGL--- 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695799972 253 nraKEAKNGVNISYFIPKEGALAFFDVFAMPADAKNKDEAYQFLNYLLRPEVIAHISDHVYYANANKEA 321
Cdd:cd13587 223 ---KLNRENPPIDYGAPKEGALGWIDTFAIPAKAENVDQAYAFINFMLRPEIAAMFTNATGYNTAAVGA 288
|
|
| AfuA |
COG1840 |
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]; ... |
45-323 |
1.58e-24 |
|
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 441445 [Multi-domain] Cd Length: 286 Bit Score: 101.55 E-value: 1.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 45 TVANFEKETGIKVVYDVFDSNEVLEgKLMA--GSTGFDLV-VPSASFLERQLAAGVFQPLdksKLPNWKNLDPKVlqlva 121
Cdd:COG1840 1 LLEAFEKKTGIKVNVVRGGSGELLA-RLKAegGNPPADVVwSGDADALEQLANEGLLQPY---KSPELDAIPAEF----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 122 rHDPDNKYAMPYMWATtGIGYNVDKVKAalgKDAPLNSWDLvLKPENLEKLKSCGVSFLDAPEEIFSTVLNYLGKDPnst 201
Cdd:COG1840 72 -RDPDGYWFGFSVRAR-VIVYNTDLLKE---LGVPKSWEDL-LDPEYKGKIAMADPSSSGTGYLLVAALLQAFGEEK--- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 202 kaddytgpATDLLLKLRPNIRYF--HSSQYINDLANGDICVAIGWAGDVwqaanrAKEAKNGVNISYFIPKEGALAFFDV 279
Cdd:COG1840 143 --------GWEWLKGLAANGARVtgSSSAVAKAVASGEVAIGIVNSYYA------LRAKAKGAPVEVVFPEDGTLVNPSG 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 695799972 280 FAMPADAKNKDEAYQFLNYLLRPEVIAHISDHVYYANANKEATP 323
Cdd:COG1840 209 AAILKGAPNPEAAKLFIDFLLSDEGQELLAEEGYEYPVRPDVEP 252
|
|
| SBP_bac_8 |
pfam13416 |
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
46-335 |
6.77e-23 |
|
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.
Pssm-ID: 433189 [Multi-domain] Cd Length: 281 Bit Score: 96.71 E-value: 6.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 46 VANFEKETGIKVVYDVFDSNEvLEGKLM----AGSTG-FDLVVPSASFLERQLAAGVFQPLDKskLPNWKNLDPkvlqLV 120
Cdd:pfam13416 3 AKAFEKKTGVTVEVEPQASND-LQAKLLaaaaAGNAPdLDVVWIAADQLATLAEAGLLADLSD--VDNLDDLPD----AL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 121 ARHDPDNK-YAMPYMW-ATTGIGYNVDKVKAAlgkDAPLNSWDLVLkpENLEKLKSCgVSFLDAPEEIFSTVLNYLGKDP 198
Cdd:pfam13416 76 DAAGYDGKlYGVPYAAsTPTVLYYNKDLLKKA---GEDPKTWDELL--AAAAKLKGK-TGLTDPATGWLLWALLADGVDL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 199 N-STKADDYTGPATDLLLKLRPNIRYF-HSSQYINDLANGDICVAIGWAGDVwqaanrAKEAKNGVNISYFIPKEGALAF 276
Cdd:pfam13416 150 TdDGKGVEALDEALAYLKKLKDNGKVYnTGADAVQLFANGEVAMTVNGTWAA------AAAKKAGKKLGAVVPKDGSFLG 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 277 FDVFAMPADAKNKDE-AYQFLNYLLRPEVIAHISDHVYYANANKEATPlvSADIRNNPAI 335
Cdd:pfam13416 224 GKGLVVPAGAKDPRLaALDFIKFLTSPENQAALAEDTGYIPANKSAAL--SDEVKADPAL 281
|
|
| UgpB |
COG1653 |
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ... |
6-304 |
1.12e-21 |
|
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 441259 [Multi-domain] Cd Length: 363 Bit Score: 94.73 E-value: 1.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 6 KKWLTGVITGALMAVSA-------GSLAAEQKTLHVYNWSDYIAP---DTVANFEKET-GIKVVYDVFDSNEVLEgKL-- 72
Cdd:COG1653 2 RRLALALAAALALALAAcggggsgAAAAAGKVTLTVWHTGGGEAAaleALIKEFEAEHpGIKVEVESVPYDDYRT-KLlt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 73 -MAGSTGFDLVVPSASFLERQLAAGVFQPLD---KSKLPNWKNLDPKVLQLVArhdPDNK-YAMPYMWATTGIGYNVDKV 147
Cdd:COG1653 81 aLAAGNAPDVVQVDSGWLAEFAAAGALVPLDdllDDDGLDKDDFLPGALDAGT---YDGKlYGVPFNTDTLGLYYNKDLF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 148 KAAlGKDAPLNsWDLVLkpENLEKLKS----CGVSFLDAPEEIFSTVLNYLGKDP-NSTKADDYTGPAT----DLLLKLR 218
Cdd:COG1653 158 EKA-GLDPPKT-WDELL--AAAKKLKAkdgvYGFALGGKDGAAWLDLLLSAGGDLyDEDGKPAFDSPEAvealEFLKDLV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 219 ------PNIRYFHSSQYINDLANGDicVAIGWAGDvWQAANrAKEAKNGVNISYF-IP------KEGALAFFDVFAMPAD 285
Cdd:COG1653 234 kdgyvpPGALGTDWDDARAAFASGK--AAMMINGS-WALGA-LKDAAPDFDVGVApLPggpggkKPASVLGGSGLAIPKG 309
|
330
....*....|....*....
gi 695799972 286 AKNKDEAYQFLNYLLRPEV 304
Cdd:COG1653 310 SKNPEAAWKFLKFLTSPEA 328
|
|
| PBP2_PotD_PotF_like_1 |
cd13661 |
The periplasmic substrate-binding component of an uncharacterized active transport system ... |
129-344 |
1.37e-20 |
|
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: 90.94 E-value: 1.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 129 YAMPYMWATTGIGYNVDKVKAALGKDAplnSWDLVLKPEnlekLKScGVSFLDAPEEIFSTVLNYLGKDPNSTkaddyTG 208
Cdd:cd13661 81 WAVPYRWGTTVIAYRKDKLKKLGWDPI---DWSDLWRPE----LAG-RIAMVDSPREVIGLVLKKLGASYNTA-----EV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 209 PATD-----LLLKLRPNIRYFHSSQYINDLANGDICVAIGWAGDVWQAANRAKeakngvNISYFIPKEGALAFFDVFAMP 283
Cdd:cd13661 148 PGGRealeeRLAALRRQVKLYSSNNYLQALLLGDVWVAVGWSQDIIPLARRYS------NLAVVIPRSGTSLWADLWVIP 221
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695799972 284 ADAKNKDEA-------YQFLNYLLRPEVIAHISDHVY-----YANANKEATP----LVSADIRNNPAIYPPEDVFAK 344
Cdd:cd13661 222 AGSDFGGRVrgpspllSQWIDFCLQPARATQFAQLSFggaspLILDGPSLTPpeatRKLKLDTNLVLGLPPDEILAK 298
|
|
| PBP2_Fbp_like_1 |
cd13544 |
Substrate binding domain of a putative ferric iron transporter, a member of the type 2 ... |
46-339 |
1.88e-15 |
|
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: 75.72 E-value: 1.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 46 VANFEKETGIKVVYdVFDSNEVLEGKLMA--GSTGFDLVV--PSASFLerQLAA-GVFQPLdksKLPNWKNLDPKVlqlv 120
Cdd:cd13544 17 LEAFKKDTGIKVEF-VRLSTGEALARLEAekGNPQADVWFggTADAHI--QAKKeGLLEPY---KSPNADKIPAKF---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 121 arHDPDNKYAMPYMWaTTGIGYNVDKVKAaLGKDAPlNSWDLVLKPEnlekLK---------SCGVSFLdapeeIFSTVL 191
Cdd:cd13544 87 --KDPDGYWTGIYLG-PLGFGVNTDELKE-KGLPVP-KSWEDLLNPE----YKgeivmpnpaSSGTAYT-----FLASLI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 192 NYLGKDpnstKADDYtgpatdlLLKLRPNIRYFHSSQY--INDLANGDICVAIGWAGDVwqaanrAKEAKNGVNISYFIP 269
Cdd:cd13544 153 QLMGED----EAWEY-------LKKLNKNVGQYTKSGSapAKLVASGEAAIGISFLHDA------LKLKEQGYPIKIIFP 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695799972 270 KEGALAFFDVFAMPADAKNKDEAYQFLNYLLRPE---VIAHISDHVYYANANKEATPLVSADIRNNPAIYPPE 339
Cdd:cd13544 216 KEGTGYEIEAVAIIKGAKNPEAAKAFIDWALSKEaqeLLAKVGSYAIPTNPDAKPPEIAPDLKKDKLIKYDFE 288
|
|
| SBP_bac_6 |
pfam13343 |
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
80-340 |
5.93e-15 |
|
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.
Pssm-ID: 463852 [Multi-domain] Cd Length: 247 Bit Score: 73.55 E-value: 5.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 80 DLVVP------SASFLERQLAAGVFQPLDKSKLPNWKNlDPKVLQLVarhDPDNKYAMpYMWATTGIGYNVDKVKaalGK 153
Cdd:pfam13343 5 DIILSagdlffDKRFLEKFIEEGLFQPLDSANLPNVPK-DFDDEGLR---DPDGYYTP-YGVGPLVIAYNKERLG---GR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 154 DAPlNSWDLVLKPEnlekLKSCGVSFLDAPEEIFSTVLNYLGKDPNSTkaddytgPATDLLLKLRPNIRYFHSSQYINDL 233
Cdd:pfam13343 77 PVP-RSWADLLDPE----YKGKVALPGPNVGDLFNALLLALYKDFGED-------GVRKLARNLKANLHPAQMVKAAGRL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 234 ANGD--ICVAIGWAGDVWQAanrakeakNGVNISYFIPKEGALAFFDVFAMPADakNKDEAYQFLNYLLRPEVIAHISDH 311
Cdd:pfam13343 145 ESGEpaVYLMPYFFADILPR--------KKKNVEVVWPEDGALVSPIFMLVKKG--KKELADPLIDFLLSPEVQAILAKA 214
|
250 260 270
....*....|....*....|....*....|.
gi 695799972 312 --VYYANANKEATPlvsADIRNNPAIYPPED 340
Cdd:pfam13343 215 glVFPVVLNPAVDN---PLPEGAPFKWLGWD 242
|
|
| SBP_bac_1 |
pfam01547 |
Bacterial extracellular solute-binding protein; This family also includes the bacterial ... |
46-304 |
4.70e-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: 72.06 E-value: 4.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 46 VANFEKE-TGIKVVYDVFDSNEV---LEGKLMAGSTGFDLVVPSASFLERQLAAGVFQPLDKSKLPNWKNLDPKVlqlva 121
Cdd:pfam01547 14 VKEFEKEhPGIKVEVESVGSGSLaqkLTTAIAAGDGPADVFASDNDWIAELAKAGLLLPLDDYVANYLVLGVPKL----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 122 rhdpdnkYAMPYMWATTGIGYNVDKVKAAlGKDAPLNsWDLVLKPenLEKLKSCGVSFLDAPEEIFSTVLNYL------- 194
Cdd:pfam01547 89 -------YGVPLAAETLGLIYNKDLFKKA-GLDPPKT-WDELLEA--AKKLKEKGKSPGGAGGGDASGTLGYFtlallas 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 195 ---------GKDPNSTKADDYTGPATDLLLKLR-------PNIRYFHSSQYINDLANGDICVAIGWAGDVWQAANRAKEA 258
Cdd:pfam01547 158 lggplfdkdGGGLDNPEAVDAITYYVDLYAKVLllkklknPGVAGADGREALALFEQGKAAMGIVGPWAALAANKVKLKV 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 695799972 259 KNGVNISYFIPKEGALAFF---------DVFAMPADAKNKDEAYQFLNYLLRPEV 304
Cdd:pfam01547 238 AFAAPAPDPKGDVGYAPLPagkggkgggYGLAIPKGSKNKEAAKKFLDFLTSPEA 292
|
|
| MalE |
COG2182 |
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism]; |
9-335 |
3.06e-11 |
|
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
Pssm-ID: 441785 [Multi-domain] Cd Length: 410 Bit Score: 64.20 E-value: 3.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 9 LTGVITGALMAVSAG-------SLAAEQKTLHVYNWSDYIAP--DTVANFEKETGIKVVYDVFDSNEVLEGKLMAGSTGF 79
Cdd:COG2182 11 LALALALALAACGSGssssgssSAAGAGGTLTVWVDDDEAEAleEAAAAFEEEPGIKVKVVEVPWDDLREKLTTAAPAGK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 80 --DLVVPSASFLERQLAAGVFQPLDKSkLPNWKNLDPKVLQLVARhdpDNK-YAMPYMWATTGIGYNVDKVKAalgkDAP 156
Cdd:COG2182 91 gpDVFVGAHDWLGELAEAGLLAPLDDD-LADKDDFLPAALDAVTY---DGKlYGVPYAVETLALYYNKDLVKA----EPP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 157 lNSWDLVLkpENLEKLKSCGVSFL--DAPEEIFSTVL------NYLGKDPNSTKADDYTGPAT----DLLLKLRPNiRYF 224
Cdd:COG2182 163 -KTWDELI--AAAKKLTAAGKYGLayDAGDAYYFYPFlaafggYLFGKDGDDPKDVGLNSPGAvaalEYLKDLIKD-GVL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 225 HSS----QYINDLANGDICVAIGWAgdvWQAANrAKEAKnGVNISYF-IPK----EGALAFFDV--FAMPADAKNKDEAY 293
Cdd:COG2182 239 PADadydAADALFAEGKAAMIINGP---WAAAD-LKKAL-GIDYGVApLPTlaggKPAKPFVGVkgFGVSAYSKNKEAAQ 313
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 695799972 294 QFLNYLLRPEVIAHISDHVYYANANKEAtpLVSADIRNNPAI 335
Cdd:COG2182 314 EFAEYLTSPEAQKALFEATGRIPANKAA--AEDAEVKADPLI 353
|
|
| PBP2_Fbp_like_2 |
cd13547 |
Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 ... |
31-303 |
5.55e-11 |
|
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: 62.24 E-value: 5.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 31 TLHVYNwSDY--IAPDTVANFEKE-TGIKVvyDVFDSNEvleGKLM--------AGSTGFDLV-VPSASFLERQLAAGVF 98
Cdd:cd13547 1 KLVVYT-SMPedLANALVEAFEKKyPGVKV--EVFRAGT---GKLMaklaaeaeAGNPQADVLwVADPPTAEALKKEGLL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 99 QPLdksKLPNWKNLDPKVlqlvarHDPDnKYAMPYMWATTGIGYNVDKVkaalGKDAPLNSWDLvLKPEnleklkscgvs 178
Cdd:cd13547 75 LPY---KSPEADAIPAPF------YDKD-GYYYGTRLSAMGIAYNTDKV----PEEAPKSWADL-TKPK----------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 179 fldapeeifstvlnYLGK----DPNstkaddYTGPATDLL--LKLRPNIR--YFH------------SSQYINDLANGDI 238
Cdd:cd13547 129 --------------YKGQivmpDPL------YSGAALDLVaaLADKYGLGweYFEklkengvkveggNGQVLDAVASGER 188
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695799972 239 CVAIGwaGDVwqAANRAKEAKNGVNISYfiPKEGALAFFDVFAMPADAKNKDEAYQFLNYLLRPE 303
Cdd:cd13547 189 PAGVG--VDY--NALRAKEKGSPLEVIY--PEEGTVVIPSPIAILKGSKNPEAAKAFVDFLLSPE 247
|
|
| PBP2_Fe3_thiamine_like |
cd13518 |
Substrate binding domain of iron and thiamine transporters-like, a member of the type 2 ... |
31-304 |
1.19e-10 |
|
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: 61.16 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 31 TLHVYNWSDYIAPDTVAN-FEKETGIKVVYdVFDSNEVLEGKLMA--GSTGFDLVVPSA-SFLERQLAAGVFQPldkskl 106
Cdd:cd13518 1 ELVVYTASDRDFAEPVLKaFEEKTGIKVKA-VYDGTGELANRLIAekNNPQADVFWGGEiIALEALKEEGLLEP------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 107 PNWKNLDPkvlQLVARHDPDNKYaMPYMWATTGIGYNVDKVKaalGKDAPLNSWDLvLKPENLEKLKSCGVSFLDAPEEI 186
Cdd:cd13518 74 YTPKVIEA---IPADYRDPDGYW-VGFAARARVFIYNTDKLK---EPDLPKSWDDL-LDPKWKGKIVYPTPLRSGTGLTH 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 187 FSTVLNYLGKDpnstKADDYtgpatdLLLKLRPNIRYFHSSQYINDL-ANGDICVAIGWAGDVwqaanrAKEAKNGVNIS 265
Cdd:cd13518 146 VAALLQLMGEE----KGGWY------LLKLLANNGKPVAGNSDAYDLvAKGEVAVGLTDTYYA------ARAAAKGEPVE 209
|
250 260 270
....*....|....*....|....*....|....*....
gi 695799972 266 YFIPKEGALAFFDVFAMPADAKNKDEAYQFLNYLLRPEV 304
Cdd:cd13518 210 IVYPDQGALVIPEGVALLKGAPNPEAAKKFIDFLLSPEG 248
|
|
| PBP2_TMBP_like |
cd13585 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ... |
46-355 |
4.15e-10 |
|
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: 60.50 E-value: 4.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 46 VANFEKE-TGIKVVYDVFDSNEVLEgKLM---AGSTGFDLVVPSASFLERQLAAGVFQPLDkSKLPNWKNLDPKVLQLVA 121
Cdd:cd13585 20 IDAFEKEnPGVKVEVVPVPYDDYWT-KLTtaaAAGTAPDVFYVDGPWVPEFASNGALLDLD-DYIEKDGLDDDFPPGLLD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 122 RHDPDNK-YAMPYMWATTGIGYNVDKVKAALGKDAPLNSWDLVL---KPENLEKLKSCGVSFlDAPEEIFSTVLNYL--- 194
Cdd:cd13585 98 AGTYDGKlYGLPFDADTLVLFYNKDLFDKAGPGPKPPWTWDELLeaaKKLTDKKGGQYGFAL-RGGSGGQTQWYPFLwsn 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 195 -GK--DPNSTKADdYTGPAT--------DLLL-KLRPNIRYFHSSQYINDLANGDicVAIGWAGdVWQAANrAKEAKNGV 262
Cdd:cd13585 177 gGDllDEDDGKAT-LNSPEAvealqfyvDLYKdGVAPSSATTGGDEAVDLFASGK--VAMMIDG-PWALGT-LKDSKVKF 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 263 NISYF-IP-----KEGALAFFDVFAMPADAKNKDEAYQFLNYLLRPEVIAHISDHVYYANANKEATPLVSADIRNNPAIY 336
Cdd:cd13585 252 KWGVApLPagpggKRASVLGGWGLAISKNSKHPEAAWKFIKFLTSKENQLKLGGAAGPAALAAAAASAAAPDAKPALALA 331
|
330
....*....|....*....
gi 695799972 337 PPEDVFAKLFTLKVQDPKI 355
Cdd:cd13585 332 AAADALAAAVPPPVPPPWP 350
|
|
| PBP2_XBP1_like |
cd14749 |
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ... |
46-344 |
3.52e-09 |
|
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; possesses type 2 periplasmic binding fold; This group represents the periplasmic component of an ABC transport system XBP1 that shows preference for xylo-oligosaccharides in the order of xylotriose > xylobiose > xylotetraose. 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: 270452 [Multi-domain] Cd Length: 388 Bit Score: 57.77 E-value: 3.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 46 VANFEKET-GIKVVYDVF---DSNEVLEgKLMAGSTGFDLV-VPSASFLERQLAAGVFQPLDKsKLPNWKNLDPKVLQLV 120
Cdd:cd14749 21 IADFEKENpNIKVKVVVFpydNYKTKLK-TAVAAGEGPDVFnLWPGGWLAEFVKAGLLLPLTD-YLDPNGVDKRFLPGLA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 121 ARHDPDNK-YAMPYMWATTGIGYNVDKVKAALGKDAPlNSWDLVLkpENLEKLKS-----CGVSFLDAPEE---IFSTVL 191
Cdd:cd14749 99 DAVTFNGKvYGIPFAARALALFYNKDLFEEAGGVKPP-KTWDELI--EAAKKDKFkakgqTGFGLLLGAQGghwYFQYLV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 192 NYLGKDPnstKADDYTGPAT--------------DLLLK--LRPNIRYFHSSQYINDLANGDICVAIGwaGDvWQAANrA 255
Cdd:cd14749 176 RQAGGGP---LSDDGSGKATfndpafvqalqklqDLVKAgaFQEGFEGIDYDDAGQAFAQGKAAMNIG--GS-WDLGA-I 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 256 KEAKNGVNISYF-IP--KEGAL-----AFFDVFAMPADAKNKDEAYQFLNYLLRPEVIAhisdhvYYANANKE--ATPLV 325
Cdd:cd14749 249 KAGEPGGKIGVFpFPtvGKGAQtstigGSDWAIAISANGKKKEAAVKFLKYLTSPEVMK------QYLEDVGLlpAKEVV 322
|
330 340
....*....|....*....|
gi 695799972 326 SADIRN-NPAIYPPEDVFAK 344
Cdd:cd14749 323 AKDEDPdPVAILGPFADVLN 342
|
|
| PBP2_UgpB |
cd14748 |
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ... |
46-333 |
4.09e-08 |
|
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: 54.61 E-value: 4.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 46 VANFEKE-TGIKVVYDVFDSNEVLEGKLMA---GSTGFDLVVPSASFLERQLAAGVFQPLDK--SKLPNWKNLDPKVLQL 119
Cdd:cd14748 20 VDEFNKShPDIKVKAVYQGSYDDTLTKLLAalaAGTAPDVAQVDASWVAQLADSGALEPLDDyiDKDGVDDDDFYPAALD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 120 VARHDpDNKYAMPYMWATTGIGYNVDKVKAA-LGKDAPLNSWDLV------LKPENLEKLKSCGVSFLDAPEEIFSTVLN 192
Cdd:cd14748 100 AGTYD-GKLYGLPFDTSTPVLYYNKDLFEEAgLDPEKPPKTWDELeeaakkLKDKGGKTGRYGFALPPGDGGWTFQALLW 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 193 YLGK---DPNSTKAdDYTGPA--------TDLLLKlRPNIRYFHSSQYINDLANGDICVAIGWagdVWQAANrAKEAKNG 261
Cdd:cd14748 179 QNGGdllDEDGGKV-TFNSPEgvealeflVDLVGK-DGVSPLNDWGDAQDAFISGKVAMTING---TWSLAG-IRDKGAG 252
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695799972 262 VNISY-FIP-----KEGALAFFDVFAMPAD-AKNKDEAYQFLNYLLRPEVIAHISDHVYYANANKEATPLVSADIRNNP 333
Cdd:cd14748 253 FEYGVaPLPagkgkKGATPAGGASLVIPKGsSKKKEAAWEFIKFLTSPENQAKWAKATGYLPVRKSAAEDPEEFLAENP 331
|
|
| PBP2_Fbp_like_3 |
cd13549 |
Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 ... |
37-300 |
2.51e-07 |
|
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: 270267 [Multi-domain] Cd Length: 263 Bit Score: 51.30 E-value: 2.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 37 WSDYIApdTVANFEKETGIKVVYDVFDSNEVLeGKLMA--GSTGFDLVVPSASFLERQLAAGVFQPLdksKLPNWKNLdP 114
Cdd:cd13549 11 WADWGT--QLKAFKKRTGIQIPYDNKNSGQAL-AALIAerARPVADVAYYGVAFGIQAVAQGVVQPY---KPAHWDEI-P 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 115 KVLQlvarhDPDNKYAMPYMwATTGIGYNVDKVKaalGKDAPlNSWDLVLKPENLEKlkscgVSFLDAPEEIFSTVLNYL 194
Cdd:cd13549 84 EGLK-----DPDGKWFAIHS-GTLGFIVNVDALG---GKPVP-KSWADLLKPEYKGM-----VGYLDPRSAFVGYVGAVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 195 GKDPNSTKADDYtGPATDLLLKLRPNIRYFHSSQYINDLANGDICVAIGWAGDvwqaANRAKEaKNGVNISYFIPKEGAL 274
Cdd:cd13549 149 VNQAMGGSLDNF-GPGIDYFKKLHKNGPIVPKQTAYARVLSGEIPILIDYDFN----AYRAKY-TDKANVAFVIPKEGSV 222
|
250 260
....*....|....*....|....*.
gi 695799972 275 AFFDVFAMPADAKNKDEAYQFLNYLL 300
Cdd:cd13549 223 VVPYVMSLVKNAPNPNNGKKVLDFIM 248
|
|
| PRK15046 |
PRK15046 |
2-aminoethylphosphonate ABC transporter substrate-binding protein; Provisional |
14-323 |
2.35e-06 |
|
2-aminoethylphosphonate ABC transporter substrate-binding protein; Provisional
Pssm-ID: 237887 [Multi-domain] Cd Length: 349 Bit Score: 48.91 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 14 TGALMAVSAGSLAAEQKTLH----VYNWSDYIAPDtvanFEKETGIKVVYDVFDSNEVLE-GKLMAGSTGFDLVVPSASF 88
Cdd:PRK15046 21 AAAFGGGAAPAWAADAVTVYsadgLEDWYQDVFPA----FTKATGIKVNYVEAGSGEVVNrAAKEKSNPQADVLVTLPPF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 89 LERQLAAGVFQPLDKSklpNWKNLDPkvlqlvARHDPDNKYAmPYMWATTGIGYNVDKVkaalgKDAPlNSWDLVLKPEN 168
Cdd:PRK15046 97 IQQAAAEGLLQPYSSV---NAKAVPA------IAKDADGTYA-PFVNNYLSFIYNPKVL-----KTAP-ATWADLLDPKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 169 LEKLKSC-------GVSFLDAPEEIFstvlnylGKDpnstkaddytgPATDLLLKLRPNIRyFHSSQ--YINDLAN-GDI 238
Cdd:PRK15046 161 KGKLQYStpgqagdGTAVLLLTFHLM-------GKD-----------KAFDYLAKLQANNV-GPSKStgKLTPLVSkGEI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 239 CVAigwAGDVwqAANRAKEAKNGVNISYFIP-----KEGALAFFDVFAMPADAKNKDEAYQFLNYLLRPEVIAHISDHVY 313
Cdd:PRK15046 222 YVA---NGDL--QMNLAQAEHGGPNVKIFFPakdggERSTFALPYVIGLVKGAPNSENGKKLIDFLLSKEAQTKVSDMAW 296
|
330
....*....|
gi 695799972 314 YANANKEATP 323
Cdd:PRK15046 297 GIPVRTDVPP 306
|
|
| PBP2_TbpA |
cd13545 |
Substrate binding domain of thiamin transporter, a member of the type 2 periplasmic binding ... |
31-304 |
3.38e-06 |
|
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: 48.06 E-value: 3.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 31 TLHVY-----NWSDYIAPDTVANFEKETGIKV-VYDVFDSNEVLE-GKLMAGSTGFDLVVP-SASFLERQLAAGVFQPLD 102
Cdd:cd13545 1 TLTVYtydsfVGEWGPGPEVKAEFEKETGCKVeFVKPGDAGELLNrLILEKNNPRADVVLGlDNNLLSRALKEGLFEPYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 103 KsklpnwKNLDPKVLQLVArhDPDNkYAMPYMWATTGIGYNVDKVkaalgKDAPLNSWDLvLKPEnLEKL--------KS 174
Cdd:cd13545 81 S------PALDVVPEVPVF--DPED-RLIPYDYGYLAFNYDKKKF-----KEPPLSLEDL-TAPE-YKGLivvqdprtSS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 175 CGVSFLdapeeiFSTVLNYlgkdpnstKADDYtgpatdlllklrpniryfhsSQYINDLANGDICVAIGWaGDVWQ---- 250
Cdd:cd13545 145 PGLGFL------LWTIAVF--------GEEGY--------------------LEYWKKLKANGVTVTPGW-SEAYGlftt 189
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695799972 251 ---------AANRAKEAKNGVNISY--FIPKEGALAFFDVFAMPADAKNKDEAYQFLNYLLRPEV 304
Cdd:cd13545 190 geapmvvsyATSPAYHVYYEKDLRYtaVIFPEGHYRQVEGAGILKGAKNPELAKKFVDFLLSPEF 254
|
|
| PBP2_Maltose_binding_like |
cd13586 |
The periplasmic-binding component of ABC transport systems specific for maltose and related ... |
37-355 |
3.23e-05 |
|
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: 45.36 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 37 WSDYIAPDTVAN-----FEKETGIKVVYdVFDSNEVLEGKLMA---GSTGFDLVVPSASFLERQLAAGVFQPLDKSKLPN 108
Cdd:cd13586 5 WTDEDGELEYLKelaeeFEKKYGIKVEV-VYVDSGDTREKFITagpAGKGPDVFFGPHDWLGELAAAGLLAPIPEYLAVK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 109 WKNLDPKVLQLVArhdpDNK-YAMPYMWATTGIGYNVDKVkaalgKDAPlNSWDLVL---KPENLEKLKSCGVSFlDAPE 184
Cdd:cd13586 84 IKNLPVALAAVTY----NGKlYGVPVSVETIALFYNKDLV-----PEPP-KTWEELIalaKKFNDKAGGKYGFAY-DQTN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 185 EIFSTVL------NYLGKDPNSTKADDYTGPAT----DLLLKLRPNIRYFHSSqyindlANGDICVAIGWAGDV------ 248
Cdd:cd13586 153 PYFSYPFlaafggYVFGENGGDPTDIGLNNEGAvkglKFIKDLKKKYKVLPPD------LDYDIADALFKEGKAamiing 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 249 -WQAANrAKEAknGVN-----ISYFIPKEGALAFFDV--FAMPADAKNKDEAYQFLNYLLRPEVIAHISDHVYYANANKE 320
Cdd:cd13586 227 pWDLAD-YKDA--GINfgvapLPTLPGGKQAAPFVGVqgAFVSAYSKNKEAAVEFAEYLTSDEAQLLLFEKTGRIPALKD 303
|
330 340 350
....*....|....*....|....*....|....*
gi 695799972 321 AtpLVSADIRNNPAIYPpedvFAKLFTLKVQDPKI 355
Cdd:cd13586 304 A--LNDAAVKNDPLVKA----FAEQAQYGVPMPNI 332
|
|
| Lipoprotein_8 |
pfam02030 |
Hypothetical lipoprotein (MG045 family); This family includes hypothetical lipoproteins, the ... |
16-331 |
5.56e-05 |
|
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: 44.95 E-value: 5.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 16 ALMAVSAGSLAAEQKTLHVYNWSDYIAPdtVANFEKETGIKVVYDVFDSNEVLEgKLMAGSTgFDLVVPSASFLERQLAA 95
Cdd:pfam02030 12 AGITFSPILTACSSSKFVVANFESYMSP--LLLERAKRKRPLTFLTYPNNEKLI-NGFANNT-YDVAVASAYAVSELAKN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 96 GVFQPLDKSKL---------------PNWKNLDPKVLQLVARHDPDNK------YAMPYMWATTGIGYNVDKVKAALGKD 154
Cdd:pfam02030 88 GLLKPIDWAKFnlkkennqsitvnniEDAKKLFTKQIWAISNAYKDGKndelleWMVPYFLQDLVFVYRGEKIPELEKKD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 155 AplnSWDLVLK-----PENLEKLKscgVSFLDAPEEIFStVLNYLGKDPNSTKAD--------DYTGPATDLLLKL---R 218
Cdd:pfam02030 168 V---YWSDVIKaivrhKDRFNKNR---LIAIDDARTIFS-LANIVQLENKNNIIDvnpkelktNYFLNVYESFSYLglkL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 219 PNIRYF----HSSQYINDLANGDICVAIGWAGDVWQAAN--------RAKEAKNGVNISYFIPKEGALAFFDVFAMPADA 286
Cdd:pfam02030 241 NNLSNMfvnsDSNIVINELAMGRRQGGIVYNGDAVYAALggdlrdeaDENMKPTGDNFHIVQPKDSPVALDFLIINSQQK 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 695799972 287 KNKDEAYQFLNYLLrpeviahisdhvyYANANKEATPLVSADIRN 331
Cdd:pfam02030 321 QFEQAAHEYINELA-------------LAGADQTKEPLEKTDEEN 352
|
|
| PBP2_MalE |
cd14747 |
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ... |
46-303 |
3.49e-04 |
|
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes the periplasmic maltose-binding component of an ABC transport system from the phytopathogen Xanthomonas citri and its related bacterial proteins. 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: 270450 [Multi-domain] Cd Length: 386 Bit Score: 42.30 E-value: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 46 VANFEKET-GIKVVYDVF---DSNEVLEGKLmAGSTGFDLVvpsasflerQL---------AAGVFQPLDkSKLPNWKNL 112
Cdd:cd14747 20 ADEFEKENpGIEVKVQVLpwgDAHTKITTAA-ASGDGPDVV---------QLgntwvaefaAMGALEDLT-PYLEDLGGD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 113 DPKVLQLVARHDPDNK-YAMPYMWATTGIGYNVDKVKAALGKDAPLNsWDLVLkpENLEKLKSCGVSF----LDAPEEIF 187
Cdd:cd14747 89 KDLFPGLVDTGTVDGKyYGVPWYADTRALFYRTDLLKKAGGDEAPKT-WDELE--AAAKKIKADGPDVsgfaIPGKNDVW 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 188 STVL--------NYLGKD--------PNSTKA-DDYTGPATDLL-LKLRPNiryfHSSQYINDLANGDICVAIGWAGDVW 249
Cdd:cd14747 166 HNALpfvwgaggDLATKDkwkatldsPEAVAGlEFYTSLYQKGLsPKSTLE----NSADVEQAFANGKVAMIISGPWEIG 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 250 QAANRAKEAKNgvNISYFI----PKEGALAFF--DVFAMPADAKNKDEAYQFLNYLLRPE 303
Cdd:cd14747 242 AIREAGPDLAG--KWGVAPlpggPGGGSPSFAggSNLAVFKGSKNKDLAWKFIEFLSSPE 299
|
|
| YnjB |
COG4134 |
ABC-type uncharacterized transport system YnjBCD, periplasmic component [General function ... |
6-307 |
1.11e-03 |
|
ABC-type uncharacterized transport system YnjBCD, periplasmic component [General function prediction only];
Pssm-ID: 443309 [Multi-domain] Cd Length: 401 Bit Score: 40.61 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 6 KKWLTGVITGALMAVSAGSL-----------AAEQKTLHVYNW------SDYIAPDTVANFEKETGIKVVY-DVFDSNEV 67
Cdd:COG4134 2 RRLALALALLALLLAACSAAlaaadwqaieaEARGQTVYFNAWggdpniNDYIDDWVAPQLKERYGITLEHvKLADTADA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 68 LE--------GKLMAGStgFDLVV----PSASFLERQLAAGVFqpldKSKLPNWKNLDPKVLQLvaRHD---PDNKYAMP 132
Cdd:COG4134 82 VNrvlaekqaGKDDGGS--VDLIWingeNFAAMKEAGLLFGPF----AEKLPNWAYVDTEKPTV--TTDfgvPVDGYEAP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 133 YMWATTGIGYNVDKVKAAlgkdaplnswdlvlkPENLEKLKS-----------------CGVSFLdapEEIFSTVLNY-- 193
Cdd:COG4134 154 WGMAQLVFIYDSARVPNP---------------PRSLAELLEwakanpgrftypappdfTGSTFL---KQALYELTGDpd 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 194 -LGKDPNSTKADDYTGPATDLLLKLRPNI----RYFHSS--QYINDLANGDICVAIgwagdVWQAANRAKEAKNGV---N 263
Cdd:COG4134 216 aLQQPVDEAKFAKVTAPLWAYLDELHPYLwrqgKTYPASnaALDQLLADGEIDMAM-----SFNPAEASSAIANGElppT 290
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 695799972 264 ISYFIPKEGALAFFDVFAMPADAKNKDEAYQFLNYLLRPEVIAH 307
Cdd:COG4134 291 VRTFVFDGGTIGNTHFLAIPFNAPNKAGAMVVANFLLSPEAQAR 334
|
|
| PBP2_BitB |
cd13546 |
Substrate binding domain of a putative iron transporter BitB, a member of the type 2 ... |
31-304 |
1.70e-03 |
|
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: 39.55 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 31 TLHVY--NWSDYIAPdTVANFEKETGIKVvydvfdsnevlegKLMAGSTGfDLvvpsasfLERqLAAGVFQPL------- 101
Cdd:cd13546 1 TLVVYspNSEEIIEP-IIKEFEEKPGIKV-------------EVVTGGTG-EL-------LAR-IKAEADNPQadvmwgg 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 102 DKSKLPNWKNL-----DPKVLQLVARHDPDNKYAMPYMWATTGIGYNVDKVKaalgKDAPLNSWDLVLKPenleKLKscG 176
Cdd:cd13546 58 GIETLEAYKDLfepyeSPEAAAIPDAYKSPEGLWTGFSVLPVVLMVNTDLVK----NIGAPKGWKDLLDP----KWK--G 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 177 -VSFLDaPEE------IFSTVLNYLGKDPnstkaddytgpatDLLLKLRPN--IRYFHSSQYINDLANGDICVAIGWAgd 247
Cdd:cd13546 128 kIAFAD-PNKsgsaytILYTILKLYGGAW-------------EYIEKLLDNlgVILSSSSAVYKAVADGEYAVGLTYE-- 191
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 695799972 248 vwqaANRAKEAKNGVNISYFIPKEGALAFFDVFAMPADAKNKDEAYQFLNYLLRPEV 304
Cdd:cd13546 192 ----DAAYKYVAGGAPVKIVYPKEGTTAVPDGVAIVKGAKNPENAKKFIDFLLSKEV 244
|
|
| PBP2_Fbp_like_6 |
cd13552 |
Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 ... |
44-313 |
2.34e-03 |
|
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: 39.36 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 44 DTVAN-FEKETGIKVVYDVFDSNEVLE----------GKLMAGStgfdlvvPSASFLERQlAAGVFQPLDksklPNWKN- 111
Cdd:cd13552 14 EYVEDaFEEKTGVEVEWLNMGSQELLDrvraekenpqADVWWGG-------PSQLFMQLK-EEGLLEPTE----PSWAEk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 112 LDPKVlqlvarHDPDNKYAMPYMWATTgIGYNVDKVKAAlgkDAPlNSWDLVLKPENLEKLKSCGVSFLDAPEEIFSTVL 191
Cdd:cd13552 82 VAAEF------KDADGYWYGTIQTPEV-IMYNTELLSEE---EAP-KDWDDLLDPKWKDKIIIRNPLASGTMRTIFAALI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695799972 192 NYlgkdpnSTKADDYTGPATDLLLKLRPNI-RYFHS-SQYINDLANGDICVAIGWAGDVWQAANrakeaKNGVNISYFIP 269
Cdd:cd13552 151 QR------ELKGTGSLDAGYAWLKKLDANTkEYAASpTMLYLKIGRGEAAISLWNLNDVLDQRE-----NNKMPFGFIDP 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 695799972 270 KEGALAFFDVFAMPADAKNKDEAYQFLNYLLRPEVIAHISDHVY 313
Cdd:cd13552 220 ASGAPVITDGIALIKGAPHPEAAKAFYEFVGSAEIQALLAEKFN 263
|
|
| |
