|
Name |
Accession |
Description |
Interval |
E-value |
| PBP1_LsrB_Quorum_Sensing |
cd20003 |
ligand-binding protein LsrB of ABC transporter periplasmic binding protein; Periplasmic ... |
401-694 |
3.36e-154 |
|
ligand-binding protein LsrB of ABC transporter periplasmic binding protein; Periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium and its close homologs from other bacteria. The members of this group are homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transporters of many sugar based solutes in bacteria and archaea and that are a member of the type 1 periplasmic binding protein superfamily. LsrB, which is part of the ABC transporter complex LsrABCD, binds a chemically distinct form of the AI-2 signal that lacks boron, in contrast to the Vibrio harveyi AI-2 signaling molecule that has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LsrB to function as a periplasmic AI-2 binding protein in interspecies signaling.
Pssm-ID: 380658 Cd Length: 298 Bit Score: 448.26 E-value: 3.36e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 401 VIAMMPKAKGDPYFVSCKQGADEAAKELGVELLWDGPTDLDPAKQNEVVEAWITRGVDVIAVSVENKVGISTVLRKAKEK 480
Cdd:cd20003 1 TIAMIPKLVGVPYFTAAGQGAQEAAKELGVDVTYDGPTEASVSKQVEVINNFINQGYDVIAVSANDPDALAPALKKAMKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 481 GIKVITWDADAEKDARDFLIDQATPQGIGYTLTDEAARILGNKGDFAIITASLSAANQNEWIKYIKERLAEKYPDLHLVA 560
Cdd:cd20003 81 GIKVVTWDSDVNPDARDFFVNQATPEGIGKTLVDMVAEQTGEKGKVAIVTSSPTATNQNAWIKAMKAYIAEKYPDMKIVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 561 VQPSEGDRDRAFSETQTVLKVYPNVKLIMAIAAPAVPGAAEAVKQSGRT-DVKVTGLSLPNMNKPYVHDGVVESVVLWNT 639
Cdd:cd20003 161 TQYGQEDPAKSLQVAENILKAYPDLKAIIAPDSVALPGAAEAVEQLGRTgKVAVTGLSTPNVMRPYVKDGTVKSVVLWDV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1400863670 640 VDLGYLTVYAANALATGTLKRGDKELNAGRLGKIEVV---DDEVRLGAPFIFNKENID 694
Cdd:cd20003 241 VDLGYLAVYVARALADGTLLKVGDFFVAGRLGTFTVVpkgNGIILLGEPLIFTKENID 298
|
|
| PBP1_LsrB_Quorum_Sensing-like |
cd06302 |
periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium ... |
402-694 |
1.76e-114 |
|
periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium and its close homologs; Periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium and its close homologs from other bacteria. The members of this group are homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transporters of many sugar based solutes in bacteria and archaea and that are a member of the type 1 periplasmic binding protein superfamily. LsrB, which is part of the ABC transporter complex LsrABCD, binds a chemically distinct form of the AI-2 signal that lacks boron, in contrast to the Vibrio harveyi AI-2 signaling molecule that has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LsrB to function as a periplasmic AI-2 binding protein in interspecies signaling.
Pssm-ID: 380525 [Multi-domain] Cd Length: 296 Bit Score: 346.15 E-value: 1.76e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 402 IAMMPKAKGDPYFVSCKQGADEAAKELGVELLWDGPTDLDPAKQNEVVEAWITRGVDVIAVSVENKVGISTVLRKAKEKG 481
Cdd:cd06302 2 IAFVPKVVGIPYFDAAEEGAKKAAKELGVEVVYTGPTQADAAQQVQIVENLIAQGVDAIAVSPNDADALAPVLKKAKDAG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 482 IKVITWDADAEKDARDFLIDQATPQGIGYTLTDEAARILGNKGDFAIITASLSAANQNEWIKYIKERLAEKYPDLHLVAV 561
Cdd:cd06302 82 IKVITWDSDAPPSARDYFVNQADDEGLGEALVDSLAKEIGGKGKVAILSGSLTATNLNAWIKAMKEYLKSKYPDIELVDT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 562 QPSEGDRDRAFSETQTVLKVYPNVKLIMAIAAPAVPGAAEAVKQSGRTD-VKVTGLSLPNMNKPYVHDGVVESVVLWNTV 640
Cdd:cd06302 162 YYTDDDQQKAYTQAQNLIQAYPDLKGIIGVSTTAPPAAAQAVEEAGKTGkVAVTGIGLPNTARPYLKDGSVKEGVLWDPA 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1400863670 641 DLGYLTVYAANALATGTLKRGDKE-LNAGRLGKIEVVDDEVRLGAPFIFNKENID 694
Cdd:cd06302 242 KLGYLTVYAAYQLLKGKGFTEDSDdVGTGGKVKVDVAGGEILLGPPLVFTKDNVD 296
|
|
| AraH |
COG1172 |
Ribose/xylose/arabinose/galactoside ABC-type transport system, permease component ... |
17-334 |
3.43e-109 |
|
Ribose/xylose/arabinose/galactoside ABC-type transport system, permease component [Carbohydrate transport and metabolism];
Pssm-ID: 440785 Cd Length: 322 Bit Score: 333.61 E-value: 3.43e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 17 APLRERLFPnnEWVLIAVLLVECAIFGVTGENFFSASNAFEITRLSVEIGLLALVMTPIIITGGIDLSVGSMMGLAAVVL 96
Cdd:COG1172 9 RSLLRRLLP--ELGLLLALVLLLVVFSILSPGFLSPGNLSNILRQAAILGILALGMTLVIITGGIDLSVGSVVALSGVVA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 97 GGLWREAHLPMAVAAIATLLVGALGGALNAALITRLNFPPLIVTLGTFSLFRGVAEGLTRGIeNYSGFSQQFLFLGQGYV 176
Cdd:COG1172 87 ALLLVALGLPILLAILLALLVGALLGLLNGLLVAKLRIPPFIVTLGTMFIARGLALLLTGGR-PISGLPDAFRALGQGSL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 177 GGlVPTQFFILIAAIAACWWWLHRTSYGRSLYAIGFSAEGARYAGIPVARRLFFIYVLSGLASSLAAIIYVAHLGQAKSD 256
Cdd:COG1172 166 LG-IPVPVLIALVVALVAWFLLRRTRFGRYIYAVGGNEEAARLSGINVRRVKILAYVLSGLLAGLAGILLAARLGSAQPN 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1400863670 257 AGTGYELMAITAVVLGGASIFGGRGTVLGTVLGLFAIVILQNGLRLSAQPAELAGILTGVLLVATILLDRLSRRAQAQ 334
Cdd:COG1172 245 AGSGYELDAIAAVVIGGTSLTGGRGSVLGTLLGALILGVLNNGLNLLGVSSYWQQIVKGAIILLAVLLDRLRRRRRAR 322
|
|
| PBP1_ABC_rhamnose |
cd20000 |
rhamnose ABC transporter substrate-binding protein; Rhamnose ABC transporter substrate-binding ... |
402-694 |
5.67e-92 |
|
rhamnose ABC transporter substrate-binding protein; Rhamnose ABC transporter substrate-binding protein similar to periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium. The members of this group are homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transporters of many sugar based solutes in bacteria and archaea and that are a member of the type 1 periplasmic binding protein superfamily. LsrB, which is part of the ABC transporter complex LsrABCD, binds a chemically distinct form of the AI-2 signal that lacks boron, in contrast to the Vibrio harveyi AI-2 signaling molecule that has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LsrB to function as a periplasmic AI-2 binding protein in interspecies signaling.
Pssm-ID: 380655 Cd Length: 298 Bit Score: 288.00 E-value: 5.67e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 402 IAMMPKAKGDPYFVSCKQGADEAAKELGVELLWDGPTDLDPAKQNEVVEAWITRGVDVIAVSVENKVGISTVLRKAKEKG 481
Cdd:cd20000 2 IAFLPKSLGNPYFDAARDGAKEAAKELGGELIFVGPTTATAEAQIPFINTLIQQGVDAIAISANDPDALAPALKKARAAG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 482 IKVITWDADAEKDARDFLIDQATPQGIGYTLTDEAARILGNKGDFAIITASLSAANQNEWIKYIKERLAE-KYPDLHLVA 560
Cdd:cd20000 82 IKVVTFDSDVAPEARDLFVNQADADGIGRAQVDMMAELIGGEGEFAILSATPTATNQNAWIDAMKKELASpEYAGMKLVK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 561 VQPSEGDRDRAFSETQTVLKVYPNVKLIMAIAAPAVPGAAEAVKQSGRTD-VKVTGLSLPNMNKPYVHDGVVESVVLWNT 639
Cdd:cd20000 162 VAYGDDDAQKSYQEAEALLQAYPDLKGIIAPTTVGIAAAARALEDSGLKGkVKVTGLGLPSEMAKYVKDGTVPAFALWNP 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1400863670 640 VDLGYLTVYAANALATG--TLKRGDKElNAGRLGKIEVVDD-EVRLGAPFIFNKENID 694
Cdd:cd20000 242 IDLGYLAAYAAAALAQGeiTGKEGETF-TAGRLGEYTVGEGgEVVLGPPFVFTADNID 298
|
|
| TM_PBP1_transp_AraH_like |
cd06579 |
Transmembrane subunit (TM) of Escherichia coli AraH and related proteins. E. coli AraH is the ... |
62-325 |
2.12e-89 |
|
Transmembrane subunit (TM) of Escherichia coli AraH and related proteins. E. coli AraH is the TM of a Periplasmic Binding Protein (PBP)-dependent ATP-Binding Cassette (ABC) transporter involved in the uptake of the monosaccharide arabinose. This group also contains E. coli RbsC, AlsC, and MglC, which are TMs of other monosaccharide transporters, the ribose transporter, the D-allose transporter and the galactose transporter, respectively. The D-allose transporter may also be involved in low affinity ribose transport. These transporters generally bind type 1 PBPs. PBP-dependent ABC transporters consist of a PBP, two TMs, and two cytoplasmic ABCs, and are mainly involved in importing solutes from the environment. The solute is captured by the PBP, which delivers it to a gated translocation pathway formed by the two TMs. The two ABCs bind and hydrolyze ATP and drive the transport reaction. Proteins in this subgroup have a single TM which homodimerizes to generate the transmembrane pore.
Pssm-ID: 119321 [Multi-domain] Cd Length: 263 Bit Score: 280.06 E-value: 2.12e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 62 SVEIGLLALVMTPIIITGGIDLSVGSMMGLAAVVLGGLWREAHLPMAVAAIATLLVGALGGALNAALITRLNFPPLIVTL 141
Cdd:cd06579 1 AAVLGILALGMTLVIITGGIDLSVGSVAALSAVVAALLLVNAGLPIPLAILAALAVGALIGLLNGLLVAYLRIPPFIVTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 142 GTFSLFRGVAEGLTRGiENYSGFSQQFLFLGQGYVGGLVPTQFFILIAAIAACWWWLHRTSYGRSLYAIGFSAEGARYAG 221
Cdd:cd06579 81 GTMFILRGLALLITGG-RPISGLPPLFSFFLGGGLILGIPVPVLIALAVALVAWFLLRRTRFGRYLYAVGGNPEAARLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 222 IPVARRLFFIYVLSGLASSLAAIIYVAHLGQAKSDAGTGYELMAITAVVLGGASIFGGRGTVLGTVLGLFAIVILQNGLR 301
Cdd:cd06579 160 INVRRVKILAYVLSGLLAGLAGILLAARLGSAQPTAGNGYELDAIAAVVLGGTSLTGGRGSVLGTLLGALLLGVLNNGLN 239
|
250 260
....*....|....*....|....
gi 1400863670 302 LSAQPAELAGILTGVLLVATILLD 325
Cdd:cd06579 240 LLGVSSFWQQIVKGAILLLAVALD 263
|
|
| COG4158 |
COG4158 |
Predicted ABC-type sugar transport system, permease component [General function prediction ... |
34-335 |
5.43e-66 |
|
Predicted ABC-type sugar transport system, permease component [General function prediction only];
Pssm-ID: 443324 Cd Length: 334 Bit Score: 220.96 E-value: 5.43e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 34 VLLVECAIFGVTGENFFSASNAFEITRLSVEIGLLALVMTPIIITGGIDLSVGSMMGLAAVVLGGLWREAHLPMaVAAIA 113
Cdd:COG4158 35 VLILLCIGFELLTPNFLTVQNLSNIARQASINIVLAAGMTFVILTGGIDLSVGSILAASAVVAVLVSLLPGLGL-LGIPA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 114 TLLVGALGGALNAALITRLNFPPLIVTLGTFSLFRGVAEGLTRG---IENYSGFSqqflFLGQGYVGGlVPTQFFILIAA 190
Cdd:COG4158 114 ALLVGLLFGLINGLLIAFLKLPPFIVTLGSLTALRGAARLLANGttvFNPDLPFA----WIGNGYLLG-IPWLVVIALAV 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 191 IAACWWWLHRTSYGRSLYAIGFSAEGARYAGIPVARRLFFIYVLSGLASSLAAIIYVAHLGQAKS-DAGTGYELMAITAV 269
Cdd:COG4158 189 VLASWFILRRTVLGVHIYAVGGNAQAARLTGIKVWRVLLFVYAVSGLLAGLGGVMSAARLYAANGlQLGQGYELDAIAAV 268
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1400863670 270 VLGGASIFGGRGTVLGTVLGLFAIVILQNGLRLSAQPAELAGILTGVLLVATILLDRLSRRAQAQP 335
Cdd:COG4158 269 ILGGTSFVGGIGSIWGTLIGALIIAVLNNGLILLGVSDFWQFIIKGLVIIIAVALDRYRQRGSART 334
|
|
| XylH |
COG4214 |
ABC-type xylose transport system, permease component [Carbohydrate transport and metabolism]; |
31-333 |
1.43e-63 |
|
ABC-type xylose transport system, permease component [Carbohydrate transport and metabolism];
Pssm-ID: 443360 [Multi-domain] Cd Length: 393 Bit Score: 216.52 E-value: 1.43e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 31 LIAVLLVECAIFGV-TGENFFSASNAFEITRLSVEIGLLALVMTPIIITGGIDLSVGSMMGLAAVVLGGLWREAHLPMAV 109
Cdd:COG4214 27 MIIALVVIWIVFQIlTGGTFLTPRNLSNLLLQNSYIGILAIGMVLVILLGHIDLSVGSVSGFVGAVAAVLMVNWGLPWWL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 110 AAIATLLVGALGGALNAALITRLNFPPLIVTLGTFSLFRGVAEGLTRGiENYSGFSQQFLFLGQGYVGGLVPTQFFILIA 189
Cdd:COG4214 107 AILAALLVGALIGAWQGFWVAYVGIPSFIVTLAGMLAFRGLTLLVLGG-GTIAPFDPTFQAIGNGFLPDILGTLSWVLGA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 190 AIAACWWW---------------------------------------------------------------LHRTSYGRS 206
Cdd:COG4214 186 VAVAAYVAlqlrsrrrrrryglpveplwlfvlklallavlilgavyllnsyrgipivvlillvlvvvytfvLTRTVFGRH 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 207 LYAIGFSAEGARYAGIPVARRLFFIYVLSGLASSLAAIIYVAHLGQAKSDAGTGYELMAITAVVLGGASIFGGRGTVLGT 286
Cdd:COG4214 266 IYAVGGNPEAARLSGINVRRVTFSVFVNMGVLAALAGIVFAARLNSATPSAGTGFELDAIAAAVIGGTSLFGGVGTVYGA 345
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1400863670 287 VLGLFAIVILQNGLRLSAQPAELAGILTGVLLVATILLDRLSRRAQA 333
Cdd:COG4214 346 VIGALVMGSLNNGMSLLGVDSDWQQIVKGLVLLLAVAFDVLSRRRRG 392
|
|
| PRK15408 |
PRK15408 |
autoinducer 2 ABC transporter substrate-binding protein LsrB; |
402-698 |
2.13e-63 |
|
autoinducer 2 ABC transporter substrate-binding protein LsrB;
Pssm-ID: 237961 Cd Length: 336 Bit Score: 214.27 E-value: 2.13e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 402 IAMMPKAKGDPYFVSCKQGADEAAKELGVELLWDGPTDLDPAKQNEVVEAWITRGVDVIAVSVENKVGISTVLRKAKEKG 481
Cdd:PRK15408 26 IAFIPKLVGVGFFTSGGNGAKEAGKELGVDVTYDGPTEPSVSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQRG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 482 IKVITWDADAEKDARDFLIDQATPQGIGYTLTDEAAR-ILGNKGDFAIITASLSAANQNEWIKYIKERLAEKYPDLHLVA 560
Cdd:PRK15408 106 VKVLTWDSDTKPECRSYYINQGTPEQLGSMLVEMAAKqVGKDKAKVAFFYSSPTVTDQNQWVKEAKAKIAKEHPGWEIVT 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 561 VQPSEGDRDRAFSETQTVLKVYPNVKLIMAIAAPAVPGAAEAVKQSGRTDVKVTGLSLPNMNKPYVHDGVVESVVLWNTV 640
Cdd:PRK15408 186 TQFGYNDATKSLQTAEGILKAYPDLDAIIAPDANALPAAAQAAENLKRDKVAIVGFSTPNVMRPYVKRGTVKEFGLWDVV 265
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1400863670 641 DLGYLTVYAANALATGT-LKRGDKeLNAGRLGKIEVVDDEVR-------------LGAPFIFNKENIDKFNF 698
Cdd:PRK15408 266 QQGKISVYVANELLKKGkLNVGDS-LDVPGIGKVEVSPNSVQgydyeakgngivlLPERVVFTKENIDKYDF 336
|
|
| RbsB |
COG1879 |
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ... |
353-693 |
6.12e-63 |
|
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH domain [Carbohydrate transport and metabolism];
Pssm-ID: 441483 [Multi-domain] Cd Length: 307 Bit Score: 211.71 E-value: 6.12e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 353 AVLSAVILAAALLVVGgnwllirslrqdlkngAAQPNSTTSQTNGHKPVIAMMPKAKGDPYFVSCKQGADEAAKELGVEL 432
Cdd:COG1879 3 LALLAAVLALALALAA----------------CGSAAAEAAAAAAKGKTIGFVVKTLGNPFFVAVRKGAEAAAKELGVEL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 433 LWDgPTDLDPAKQNEVVEAWITRGVDVIAVSVENKVGISTVLRKAKEKGIKVITWDADAEKDARDFLIdQATPQGIGYTL 512
Cdd:COG1879 67 IVV-DAEGDAAKQISQIEDLIAQGVDAIIVSPVDPDALAPALKKAKAAGIPVVTVDSDVDGSDRVAYV-GSDNYAAGRLA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 513 TDEAARILGNKGDFAIITASLSAANQNEWIKYIKERLAEkYPDLHLVAVQPSEGDRDRAFSETQTVLKVYPNVKLIMAIA 592
Cdd:COG1879 145 AEYLAKALGGKGKVAILTGSPGAPAANERTDGFKEALKE-YPGIKVVAEQYADWDREKALEVMEDLLQAHPDIDGIFAAN 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 593 APAVPGAAEAVKQSGRT-DVKVTGLSLPNMNKPYVHDGVVESVVLWNTVDLGYLTVYAANALATGtlkrgdkelnagrlg 671
Cdd:COG1879 224 DGMALGAAQALKAAGRKgDVKVVGFDGSPEALQAIKDGTIDATVAQDPYLQGYLAVDAALKLLKG--------------- 288
|
330 340
....*....|....*....|..
gi 1400863670 672 kiEVVDDEVRLGaPFIFNKENI 693
Cdd:COG1879 289 --KEVPKEILTP-PVLVTKENV 307
|
|
| Peripla_BP_4 |
pfam13407 |
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ... |
402-656 |
1.22e-60 |
|
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic binding proteins. This domain recognizes fructose (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 433182 [Multi-domain] Cd Length: 259 Bit Score: 204.08 E-value: 1.22e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 402 IAMMPKAKGDPYFVSCKQGADEAAKELGVELLWDGPTDLDPAKQNEVVEAWITRGVDVIAVSVENKVGISTVLRKAKEKG 481
Cdd:pfam13407 1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGEVIVVGPAEADAAEQVAQIEDAIAQGVDAIIVAPVDPTALAPVLKKAKDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 482 IKVITWDADAEKDARDFLIdQATPQGIGYTLTDEAARILGNKGDFAIITASLSAANQNEWIKYIKERLAEKYPDLHLVAV 561
Cdd:pfam13407 81 IPVVTFDSDAPSSPRLAYV-GFDNEAAGEAAGELLAEALGGKGKVAILSGSPGDPNANERIDGFKKVLKEKYPGIKVVAE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 562 -QPSEGDRDRAFSETQTVLKVYPN-VKLIMAIAAPAVPGAAEAVKQSGRTD-VKVTGLSLPNMNKPYVHDGVVESVVLWN 638
Cdd:pfam13407 160 vEGTNWDPEKAQQQMEALLTAYPNpLDGIISPNDGMAGGAAQALEAAGLAGkVVVTGFDATPEALEAIKDGTIDATVLQD 239
|
250
....*....|....*...
gi 1400863670 639 TVDLGYLTVYAANALATG 656
Cdd:pfam13407 240 PYGQGYAAVELAAALLKG 257
|
|
| PRK15038 |
PRK15038 |
autoinducer 2 ABC transporter permease LsrD; |
28-323 |
2.61e-60 |
|
autoinducer 2 ABC transporter permease LsrD;
Pssm-ID: 184998 Cd Length: 330 Bit Score: 205.83 E-value: 2.61e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 28 EWVLIAVLLVECAIFGVTGENFFSASNAFEITRLSVEIGLLALVMTPIIITGGIDLSVGSMMGLAAVVLGGLWrEAHLPM 107
Cdd:PRK15038 8 ELALAALLVIEILAFGLINPRMLDINVLLFSTSDFICIGIVALPLTMVIVSGGIDISFGSTIGLCAIALGVLF-QSGVPM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 108 AVAAIATLLVGALGGALNAALITRLNFPPLIVTLGTFSLFRGVAEGLT-----RGIENYSGFSQQFL-FLGQGYVGGLVP 181
Cdd:PRK15038 87 PLAILLTLLLGALCGLINAGLIIYTGVNPLVITLGTLYLFGGSALLLSgmagaTGYEGIGGFPMAFTdFANLDVLGLPVP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 182 TQFFILIAAIaaCWWWLHRTSYGRSLYAIGFSAEGARYAGIPVARRLFFIYVLSGLASSLAAIIYVAHLGQAKSDAGTGY 261
Cdd:PRK15038 167 LIIFLICLLV--FWLLMHRTHAGRNVFLIGQSPRVALYSAIPVNRTLCALYAMTGLASAIAAVLLVSYFGSARSDLGASF 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1400863670 262 ELMAITAVVLGGASIFGGRGTVLGTVLGLFAIVILQNGLRLSAQPAELAGILTGVLLVATIL 323
Cdd:PRK15038 245 LMPAITAVVLGGANIYGGSGSIIGTALAVLLVGYLQQGLQMAGVPNQISSALSGALLIVVVV 306
|
|
| PBP1_LsrB_Quorum_Sensing-like |
cd20001 |
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ... |
402-694 |
1.55e-55 |
|
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; Ligand-binding protein LsrB-like of a transport system, similar to periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium and its close homologs from other bacteria. The members of this group are homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transporters of many sugar based solutes in bacteria and archaea and that are a member of the type 1 periplasmic binding protein superfamily. LsrB, which is part of the ABC transporter complex LsrABCD, binds a chemically distinct form of the AI-2 signal that lacks boron, in contrast to the Vibrio harveyi AI-2 signaling molecule that has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LsrB to function as a periplasmic AI-2 binding protein in interspecies signaling.
Pssm-ID: 380656 Cd Length: 296 Bit Score: 191.72 E-value: 1.55e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 402 IAMMPKAKGDPYFVSCKQGADEAAKELGVELLWDGPTDLDPAKQNEVVEAWITRGVDVIAVsVENKVG-ISTVLRKAKEK 480
Cdd:cd20001 2 IAVVVKVTGIAWFDRMETGVEQFAKDTGVNVYQIGPATADAAQQVQIIEDLIAQGVDAICV-VPNDPEaLEPVLKKARDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 481 GIKVITWDADAEKDArDFLIDQATPQGIGYTLTDEAARILGNKGDFAIITASLSAANQNEWIKYIKERLAEKYPDLHLV- 559
Cdd:cd20001 81 GIVVITHEASNLKNV-DYDVEAFDNAAYGAFIMDKLAEAMGGKGKYVTFVGSLTSTSHMEWANAAVAYQKANYPDMLLVt 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 560 AVQPSEGDRDRAFSETQTVLKVYPNVKLIMAIAAPAVPGAAEAVKQSGRTD-VKVTGLSLPNMNKPYVHDGVVESVVLWN 638
Cdd:cd20001 160 DRVETNDDSETAYEKAKELLKTYPDLKGIVGCSSSDVPGAARAVEELGLQGkIAVVGTGLPSVAGEYLEDGTIDYIQFWD 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1400863670 639 TVDLGyltvYAANALATGTLKrGDK---ELNAGRLG--KIEVVDDEVRLG-APFIFNKENID 694
Cdd:cd20001 240 PADAG----YAMNALAVMVLE-GEKitdGTDLGVPGyeKVTVGKGKVLYGnAWLIVTKDNVD 296
|
|
| PBP1_LsrB_Quorum_Sensing-like |
cd20002 |
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ... |
402-694 |
2.29e-54 |
|
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; Ligand-binding protein LsrB-like of a transport system, similar to periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium and its close homologs from other bacteria. The members of this group are homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transporters of many sugar based solutes in bacteria and archaea and that are a member of the type 1 periplasmic binding protein superfamily. LsrB, which is part of the ABC transporter complex LsrABCD, binds a chemically distinct form of the AI-2 signal that lacks boron, in contrast to the Vibrio harveyi AI-2 signaling molecule that has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LsrB to function as a periplasmic AI-2 binding protein in interspecies signaling.
Pssm-ID: 380657 Cd Length: 295 Bit Score: 188.30 E-value: 2.29e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 402 IAMMPKAKGDPYFVSCKQGADEAAKELGVELLWDGPTDLDPAKQNEVVEAWITRGVDVIAVSVENKVGISTVLRKAKEKG 481
Cdd:cd20002 2 IVTVVKLAGIPWFNRMEQGVKKAGKEFGVNAYQVGPADADPAQQVRIIEDLIAQGVDAILVVPNDAKVLEPVFKKAREKG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 482 IKVITWDADAEKDArDFLIDQATPQGIGYTLTDEAARILGNKGDFAIITASLSAANQNEWIKYIKERLAEKYPDLHLVAV 561
Cdd:cd20002 82 IVVITHESPGQKGA-DWDVELIDNEKFGEAQMELLAKEMGGKGEYAIFVGSLTVPLHNLWADAAVEYQKEKYPNMKQVTD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 562 Q-PSEGDRDRAFSETQTVLKVYPNVKLIMAIAAPAVPGAAEAVKQSGRTD-VKVTGLSLPNMNKPYVHDGVVESVVLWNT 639
Cdd:cd20002 161 RiPGGEDVDVSRQTTLELLKAYPDLKGIISFGSLGPIGAGQALREKGLKGkVAVVGTVIPSQAAAYLKEGSITEGYLWDP 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1400863670 640 VDLGYLTVYAANALATGTLKRGDKELNAGRLGKIEVVDDEVRLGAPFIFNKENID 694
Cdd:cd20002 241 ADAGYAMVYIAKMLLDGKRKEIGDGFEIPGKGTPDIDGNVIIFDAPLEITKENAD 295
|
|
| rbsC |
PRK09512 |
ribose ABC transporter permease protein; Reviewed |
31-325 |
8.84e-53 |
|
ribose ABC transporter permease protein; Reviewed
Pssm-ID: 181922 [Multi-domain] Cd Length: 320 Bit Score: 184.92 E-value: 8.84e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 31 LIAvLLVECAIFGVTGENFFSASNAFEITRLSVEIGLLALVMTPIIITGGIDLSVGSMMGL----AAVVLGglwreAHLP 106
Cdd:PRK09512 22 LIA-LLVLIAIVSTLSPNFFTVNNLFNILQQTSVNAIMAVGMTLVILTSGIDLSVGSLLALtgavAASIVG-----IEVN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 107 MAVAAIATLLVGALGGALNAALITRLNFPPLIVTLGTFSLFRGVAEGLTRGIENYSGFSQQ---FLFLGQGYVGGlVPTQ 183
Cdd:PRK09512 96 ALVAVPAALALGAAIGAVTGVIVAKGKVQAFIATLVMMLLLRGVTMVYTDGSPINTGFTDNadlFGWFGIGRPLG-IPTP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 184 FFILIAAIAACWWWLHRTSYGRSLYAIGFSAEGARYAGIPVARRLFFIYVLSGLASSLAAIIYVAHLGQAKSDAGTGYEL 263
Cdd:PRK09512 175 VWIMAIVFLAAWYMLHHTRLGRYIYALGGNEAATRLSGINVNKVKIIVYALCGLLAALAGIIEVARLSSAQPTAGTGYEL 254
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1400863670 264 MAITAVVLGGASIFGGRGTVLGTVLGLFAIVILQNGLRLSAQPAELAGILTGVLLVATILLD 325
Cdd:PRK09512 255 DAIAAVVLGGTSLAGGKGRIVGTLIGALILGFLNNGLNLLGVSSYYQMIVKAVVILLAVLVD 316
|
|
| PBP1_tmGBP |
cd06314 |
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ... |
401-656 |
1.02e-51 |
|
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and its close homologs; Periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and its close homologs from other bacteria. They are members of the type 1 periplasmic binding protein superfamily which consists of two domains connected by a three-stranded hinge. TmGBP is specific for glucose and its binding pocket is buried at the interface of the two domains. TmGBP also exhibits high thermostability and the highest structural similarity to E. coli glucose binding protein (ecGBP).
Pssm-ID: 380537 [Multi-domain] Cd Length: 271 Bit Score: 180.47 E-value: 1.02e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 401 VIAMMPKAKGDPYFVSCKQGADEAAKELGVELLWDGPTDLDPAKQNEVVEAWITRGVDVIAVSVENKVGISTVLRKAKEK 480
Cdd:cd06314 1 TFALVPKGLNNPFWDLAEAGAEKAAKELGVNVEFVGPQKSDAAEQVQLIEDLIARGVDGIAISPNDPEAVTPVINKAADK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 481 GIKVITWDADAEKDARDFLIDQATPQGiGYTLTDEAARILGNKGDFAIITASLSAANQNEWIKYIKERLAeKYPDLHLVA 560
Cdd:cd06314 81 GIPVITFDSDAPDSKRLAYIGTDNYEA-GREAGELMKKALPGGGKVAIITGGLGADNLNERIQGFKDALK-GSPGIEIVD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 561 VQPSEGDRDRAFSETQTVLKVYPNVKLIMAIAAPAVPGAAEAVKQSGRT-DVKVTGL-SLPnMNKPYVHDGVVESVVLWN 638
Cdd:cd06314 159 PLSDNDDIAKAVQNVEDILKANPDLDAIFGVGAYNGPAIAAALKDAGKVgKVKIVGFdTLP-ETLQGIKDGVIAATVGQR 237
|
250
....*....|....*...
gi 1400863670 639 TVDLGYLTVYAANALATG 656
Cdd:cd06314 238 PYEMGYLSVKLLYKLLKG 255
|
|
| PBP1_ABC_sugar_binding-like |
cd01536 |
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ... |
401-656 |
4.31e-51 |
|
periplasmic sugar-binding domain of active transport systems that are members of the type 1 periplasmic binding protein (PBP1) superfamily; Periplasmic sugar-binding domain of active transport systems that are members of the type 1 periplasmic binding protein (PBP1) superfamily. The members of this family function as the primary receptors for chemotaxis and transport of many sugar based solutes in bacteria and archaea. The sugar binding domain is also homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR. Moreover, this periplasmic binding domain, also known as Venus flytrap domain, undergoes transition from an open to a closed conformational state upon the binding of ligands such as lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars. This family also includes the periplasmic binding domain of autoinducer-2 (AI-2) receptors such as LsrB and LuxP which are highly homologous to periplasmic pentose/hexose sugar-binding proteins.
Pssm-ID: 380478 [Multi-domain] Cd Length: 268 Bit Score: 178.53 E-value: 4.31e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 401 VIAMMPKAKGDPYFVSCKQGADEAAKELGVELLWDGPtDLDPAKQNEVVEAWITRGVDVIAVSVENKVGISTVLRKAKEK 480
Cdd:cd01536 1 KIGVVVKDLTNPFWVAVKKGAEAAAKELGVELVVLDA-QGDVAKQISQIEDLIAQGVDAIIIAPVDSEALVPAVKKANAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 481 GIKVITWDADAEKDA-RDFLIDQATPQGiGYTLTDEAARILGNKGDFAIITASLSAANQNEWIKYIKERLAeKYPDLHLV 559
Cdd:cd01536 80 GIPVVAVDTDIDGGGdVVAFVGTDNYEA-GKLAGEYLAEALGGKGKVAILEGPPGSSTAIDRTKGFKEALK-KYPDIEIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 560 AVQPSEGDRDRAFSETQTVLKVYPNVKLIMAIAAPAVPGAAEAVKQSGRT-DVKVTGLSLPNMNKPYVHDGVVESVVLWN 638
Cdd:cd01536 158 AEQPANWDRAKALTVTENLLQANPDIDAVFAANDDMALGAAEALKAAGRTgDIKIVGVDGTPEALKAIKDGELDATVAQD 237
|
250
....*....|....*...
gi 1400863670 639 TVDLGYLTVYAANALATG 656
Cdd:cd01536 238 PYLQGYLAVEAAVKLLNG 255
|
|
| PRK09699 |
PRK09699 |
D-allose ABC transporter permease; |
34-327 |
2.44e-47 |
|
D-allose ABC transporter permease;
Pssm-ID: 182035 [Multi-domain] Cd Length: 312 Bit Score: 169.95 E-value: 2.44e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 34 VLLVECAIFGVTG-ENFFSASNAFEITRLSVEIGLLALVMTPIIITGGIDLSVGSMMGLAAVVLGGLWREAHLPMAVAAI 112
Cdd:PRK09699 17 ILAIIVAIFGSLSpEYFLTTNNITQIFVQSSVTVLIGMGEFFAILVAGIDLSVGAILALSGMVTAKLMLAGVDPFLAALI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 113 ATLLVGALGGALNAALITRLNFPPLIVTLGTFSLFRGVAEGLTRGiENYSGFSQQFL-FLGQGYVGGLVPTQFFILIAAI 191
Cdd:PRK09699 97 GGVLVGGALGAINGCLVNWTGLHPFIITLGTNAIFRGITLVISDA-NSVYGFSFDFVnFFAASVIGIPVPVIFSLIVALI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 192 aaCWWWLHRTSYGRSLYAIGFSAEGARYAGIPVARRLFFIYVLSGLASSLAAIIYVAHLGQAKSDAGTGYELMAITAVVL 271
Cdd:PRK09699 176 --LWFLTTRMRLGRNIYALGGNKNSAFYSGIDVKFHILVVFIISGVCAGLAGVVSTARLGAAEPLAGMGFETYAIASAII 253
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1400863670 272 GGASIFGGRGTVLGTVLGLFAIVILQNGLRLSAQPAELAGILTGVLLVATILLDRL 327
Cdd:PRK09699 254 GGTSFFGGKGRIFSVVIGGLIIGTINNGLNILQVQTYYQLVVMGGLIIAAVALDRL 309
|
|
| PRK15432 |
PRK15432 |
autoinducer 2 ABC transporter permease LsrC; Provisional |
30-325 |
1.70e-42 |
|
autoinducer 2 ABC transporter permease LsrC; Provisional
Pssm-ID: 185330 [Multi-domain] Cd Length: 344 Bit Score: 157.20 E-value: 1.70e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 30 VLIAVLLVeCAIFGVTGENFFSASNAFEITRLSVEIGLLALVMTPIIITGGIDLSVGSMMGLAAVVLGGLWrEAHLPMAV 109
Cdd:PRK15432 13 ALLAIVLL-FVLLGFLDRQYLSLQTLTMVFSSAQILILLAIGATLVMLTRNIDVSVGSITGLCAVLVGMLL-NAGYSLPV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 110 AAIATLLVGALGGALNAALITRLNFPPLIVTLGTFSLFRGVAEGLTRG--IEnysGFSQQFLFLGQGYVGGLVPTQFFIL 187
Cdd:PRK15432 91 ACLATLLLGLLAGFFNGVLVAWLRIPAIVATLGTLGLYRGIMLLWTGGkwIE---GLPAELKQLSAPILLGISPIGWLTL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 188 IAaIAACWWWLHRTSYGRSLYAIGFSAEGARYAGIPVARRLFFIYVLSGLASSLAAIIYVAHLGQAKSDAGTGYELMAIT 267
Cdd:PRK15432 168 IL-ILAMAWLLAKTAFGRSFYATGDNLQGARQLGVRTEAIRIVAFSLNGCMAALAGIVFASQIGFIPNQTGTGLEMKAIA 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1400863670 268 AVVLGGASIFGGRGTVLGTVLGLFAIVILQNGLRLSAQPAELAGILTGVLLVATILLD 325
Cdd:PRK15432 247 ACVLGGISLLGGSGTIIGAVLGAYFLTQIDSVLVLLRIPAWWNDFIAGLVLLGVLVFD 304
|
|
| PRK11618 |
PRK11618 |
inner membrane ABC transporter permease protein YjfF; Provisional |
29-327 |
7.54e-40 |
|
inner membrane ABC transporter permease protein YjfF; Provisional
Pssm-ID: 183235 [Multi-domain] Cd Length: 317 Bit Score: 148.95 E-value: 7.54e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 29 WVLIAVLLVECAIFGVTGENFFSASNAFEITRLSVEIGLLALVMTPIIITGGIDLSVGSMMGLAAVVLGGLWREAHLPMA 108
Cdd:PRK11618 9 MITIGVFVLGYLFCLVQFPGFASTRVICNLLTDNAFLGIVAVGMTFVILSGGIDLSVGSVIAFTGVFLAKLIGDYGWSPL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 109 VAAIATLLVGALGGALNAALITRLNFPPLIVTLGTFSLFRGVA-----EGLTRGIENYSGFSQ-QFLFLGQGYVGGLVpt 182
Cdd:PRK11618 89 LAFPLVLVMGAAFGAFMGALIHYLKLPAFIVTLAGMFLARGVSflvseESIPINHPFYDTLSSlAWKLPGGGRLSAMA-- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 183 qfFILIAAIAACWWWLHRTSYGRSLYAIGFSAEGARYAGIPVARRLFFIYVLSGLASSLAAIIYVAHLGQAKSDAGTGYE 262
Cdd:PRK11618 167 --LIMLAVVAIGIFLAHRTRFGNNVYAIGGNATSANLMGIPVRRTTIRIYMLSGFLATLAGIVFSLYTSAGYALAAVGVE 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1400863670 263 LMAITAVVLGGASIFGGRGTVLGTVLGLFAIVILQNGLR----LSAQPAElagILTGVLLVATILLDRL 327
Cdd:PRK11618 245 LDAIAAVVIGGTLLTGGVGTVLGTLFGVLIQGLIQTYITfdgtLSSWWTK---IVIGILLFVFIALQRG 310
|
|
| araH |
PRK11285 |
L-arabinose transporter permease protein; Provisional |
3-333 |
1.41e-39 |
|
L-arabinose transporter permease protein; Provisional
Pssm-ID: 183076 [Multi-domain] Cd Length: 333 Bit Score: 148.67 E-value: 1.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 3 ETIPQSEIRIPQLVAPLRERLFPNNeWVLIAVLLVECAIFGVTGENFFSASNAFEITRLSVEIGLLALVMTPIIITGGID 82
Cdd:PRK11285 5 STSGSGAAAAAPPKSRFSLWRIWDQ-YGMLVVFAVLFIACSLFVPNFASFINMKGLGLAISMIGMVACTMLFCLASGDFD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 83 LSVGSMMGLAAVVLGGLWREAHlPMAVAAIATLLVGALGGALNAALITRLNFPPLIVTLGTFSLFRGVA----EGLTRGI 158
Cdd:PRK11285 84 LSVASVVAFAGVVTAVVINATE-SLWLGVAAGLLLGAAVGLVNGFVIARLKINALITTLATMQIVRGLAyiisDGKAVGI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 159 EnysgfSQQFLFLGQGYVGGlVPTQFFILIAAIAACWWWLHRTSYGRSLYAIGFSAEGARYAGIPVARRLFFIYVLSGLA 238
Cdd:PRK11285 163 S-----DERFFALGYANFFG-VPAPIWLTVACFVVFGFLLNKTTFGRNTLAIGGNEEAARLAGVPVVRTKIIIFVLQGLV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 239 SSLAAIIYVAHLGQAKSDAGTGYELMAITAVVLGGASIFGGRGTVLGTVLGLFAIVILQNGLRLSAQPAELAGILTGVLL 318
Cdd:PRK11285 237 SALAGVILASRMTSGQPMTSIGFELIVISACVLGGVSLKGGIAKISGVVAGVLILGTVENAMNLLNISPFYQYVVRGLIL 316
|
330
....*....|....*
gi 1400863670 319 VATILLDRLSRRAQA 333
Cdd:PRK11285 317 LAAVLFDRYKQRAKR 331
|
|
| mglC |
PRK09478 |
galactose/methyl galactoside ABC transporter permease MglC; |
33-327 |
6.73e-39 |
|
galactose/methyl galactoside ABC transporter permease MglC;
Pssm-ID: 181892 [Multi-domain] Cd Length: 336 Bit Score: 146.76 E-value: 6.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 33 AVLLVECAIFGVTGENFFSASNAFEI-TRLSVEIgLLALVMTPIIITGGIDLSVGSMMGLAAVVLGGLWREA-------- 103
Cdd:PRK09478 20 VVLLVLLAIIIIQDPTFLSLLNLSNIlTQSSVRI-IIALGVAGLIVTQGTDLSAGRQVGLAAVVAATLLQSMdnankvfp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 104 ---HLPMAVAAIATLLVGALGGALNAALITRLNFPPLIVTLGTFSLFRGVAEGLTR--GIENYSGFSQQFLFLGQGYVG- 177
Cdd:PRK09478 99 elaTMPIALVILIVCAIGAVIGLINGLIIAYLNVTPFIATLGTMIIVYGINSLYYDfvGASPISGFDSGFSTFAQGFVAl 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 178 GLVPTQFFILIAAIAACWWW--LHRTSYGRSLYAIGFSAEGARYAGIPVARRLFFIYVLSGLASSLAAIIYVAHLGQAKS 255
Cdd:PRK09478 179 GSFRLSYITFYALIAVAFVWvlWNKTRFGKNIFAIGGNPEAAKVSGVNVPLNLLMIYALSGVFYAFGGMLEAGRIGSATN 258
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1400863670 256 DAGTGYELMAITAVVLGGASIFGGRGTVLGTVLGLFAIVILQNGLRLSAQPAELAGILTGVLLVATILLDRL 327
Cdd:PRK09478 259 NLGFMYELDAIAACVVGGVSFSGGVGTVIGVVTGVIIFTVINYGLTYIGVNPYWQYIIKGAIIIFAVALDSL 330
|
|
| GguB |
NF040906 |
sugar ABC transporter permease; |
65-330 |
5.23e-37 |
|
sugar ABC transporter permease;
Pssm-ID: 468841 [Multi-domain] Cd Length: 375 Bit Score: 142.60 E-value: 5.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 65 IGLLALVMTPIIITGGIDLSVGSMMGLAAVVLGGLWREAHLPMAVAAIATLLVGALGGALNAALITRLNFPPLIVTLGTF 144
Cdd:NF040906 42 ILILAIGMLLVIIAGHIDLSVGSVVAFVGAVAAVLMVNWGMPWWLAVLLCLLVGALIGAWQGFWVAYVGIPAFIVTLAGM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 145 SLFRGVAEGLTRGiENYSGFSQQFLFLGQGYVGGLV---------------------------------------PTQFF 185
Cdd:NF040906 122 LVFRGLTLVVLGG-QSIGPFPDGFQKISSGFLPDLFggtglhlltlllgvlaaaalvwsqlrgrrrrikyglevePMALF 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 186 IL-----IAAIAACWWWL------------------------HRTSYGRSLYAIGFSAEGARYAGIPVARRLFFIYVLSG 236
Cdd:NF040906 201 IAklvliAAAILFFTYLLasyrglpnvliilgvlilvysfvtNRTVIGRHIYAVGGNEKAAKLSGIKTKRVTFLVFVNMG 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 237 LASSLAAIIYVAHLGQAKSDAGTGYELMAITAVVLGGASIFGGRGTVLGTVLGLFAIVILQNGLRLSAQPAELAGILTGV 316
Cdd:NF040906 281 VLAALAGLVFAARLNSATPKAGNGFELDAIAACFIGGASASGGVGTVVGAIIGALVMGVLNNGMSILGIGIDWQQVIKGL 360
|
330
....*....|....
gi 1400863670 317 LLVATILLDRLSRR 330
Cdd:NF040906 361 VLLAAVAFDVYNKR 374
|
|
| BPD_transp_2 |
pfam02653 |
Branched-chain amino acid transport system / permease component; This is a large family mainly ... |
54-321 |
5.74e-37 |
|
Branched-chain amino acid transport system / permease component; This is a large family mainly comprising high-affinity branched-chain amino acid transporter proteins such as E. coli LivH and LivM, both of which are form the LIV-I transport system. Also found with in this family are proteins from the galactose transport system permease and a ribose transport system.
Pssm-ID: 396977 [Multi-domain] Cd Length: 269 Bit Score: 139.32 E-value: 5.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 54 NAFEITRLSVEIGLLALVMTPII-ITGGIDLSVGSMMGLAAVVLGGLWREAHLPMAVAAIATLLVGALGGALNAALITRL 132
Cdd:pfam02653 1 NILNILTLASIYAIAALGLTLIYgIAGVINLGHGGFMMLGAYVAAMLLNLLGPGLWLALPVGILVGAAVGLLIGILTLRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 133 NFPPLIVTLGTFSLFRGVAEGLTRGIENYS---GFSQQFLFLGQGYVGGLVPTQFFILIAAIAACWWWLHRTSYGRSLYA 209
Cdd:pfam02653 81 KINEVIITLLLNLAALGLALFLVTGILGGEggtSGITGPSGFPGAFLSFAFAFIFLLALLLVLALWLLLYRTKFGRALRA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 210 IGFSAEGARYAGIPVARRLFFIYVLSGLASSLAAIIYVAHLGQAK-SDAGTGYELMAITAVVLGGAsifggrGTVLGTVL 288
Cdd:pfam02653 161 VGENEEAARAAGINVKKLKLLTFVISGALAGLAGALLALYTGVVPpSNFGVGLGLDAIAAVVLGGA------GSPIGVVI 234
|
250 260 270
....*....|....*....|....*....|....
gi 1400863670 289 GLFAIVILQNGLR-LSAQPAELAGILTGVLLVAT 321
Cdd:pfam02653 235 GSLIIGLVQSLGLgALGSPPELSLLVLGALLILV 268
|
|
| PBP1_ABC_sugar_binding-like |
cd19969 |
monosaccharide ABC transporter substrate binding protein; Periplasmic sugar-binding domain of ... |
404-659 |
5.21e-36 |
|
monosaccharide ABC transporter substrate binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380624 [Multi-domain] Cd Length: 278 Bit Score: 137.08 E-value: 5.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 404 MMPKAKGDPYFVSCKQGADEAAKELGVELLWDGPTDLDPAKQNEVVEAWITRGVDVIAVSVENKVGISTVLRKAKEKGIK 483
Cdd:cd19969 4 MVTFKSGHPYWDDVKEGFEDAGAELGVKTEYTGPATADVNEQITAIEQAIAKNPDGIAVSAIDPEALTPTINKAVDAGIP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 484 VITWDADAEKDARDFLIDQATpQGIGYTLTDEAARILGNKGDFAIITASLSaANQNEWIKYIKERLAEkYPDLHLVAVQP 563
Cdd:cd19969 84 VVTFDSDAPESKRISYVGTDN-YEAGYAAAEKLAELLGGKGKVAVLTGPGQ-PNHEERVEGFKEAFAE-YPGIEVVAVGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 564 SEGDRDRAFSETQTVLKVYPNVKLIMAIAAPAVPGAAEAVKQSGRT-DVKVTGLSLPNMNKPYVHDGVVESVVLWNTVDL 642
Cdd:cd19969 161 DNDDPEKAAQNTSALLQAHPDLVGIFGVDASGGVGAAQAVREAGKTgKVKIVAFDDDPETLDLIKDGVIDASIAQRPWMM 240
|
250
....*....|....*..
gi 1400863670 643 GYLTVYAANALATGTLK 659
Cdd:cd19969 241 GYWSLQFLYDLANGLVK 257
|
|
| PBP1_ABC_sugar_binding-like |
cd20007 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
402-657 |
8.82e-35 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380662 [Multi-domain] Cd Length: 271 Bit Score: 133.13 E-value: 8.82e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 402 IAMMPKAKGDPYFVSCKQGADEAAKELGVELLWDGPTDLDPAKQNEVVEAWITRGVDVIAVSVENKVGISTVLRKAKEKG 481
Cdd:cd20007 2 IALVPGVTGDPFYITMQCGAEAAAKELGVELDVQGPPTFDPTLQTPIVNAVIAKKPDALLIAPTDPQALIAPLKRAADAG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 482 IKVITWDADAekDARDFLIDQATP---QGiGYTLTDEAARILGNKGDFAIITASLSAANQNEWIKYIKERLAeKYPDLHL 558
Cdd:cd20007 82 IKVVTVDTTL--GDPSFVLSQIASdnvAG-GALAAEALAELIGGKGKVLVINSTPGVSTTDARVKGFAEEMK-KYPGIKV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 559 VAVQPSEGDRDRAFSETQTVLKVYPNVKLIMAIAAPAVPGAAEAVKQSGRTD-VKVTGLSLPNMNKPYVHDGVVESVVLW 637
Cdd:cd20007 158 LGVQYSENDPAKAASIVAAALQANPDLAGIFGTNTFSAEGAAAALRNAGKTGkVKVVGFDASPAQVEQLKAGTIDALIAQ 237
|
250 260
....*....|....*....|
gi 1400863670 638 NTVDLGYLTVYAANALATGT 657
Cdd:cd20007 238 KPAEIGYLAVEQAVAALTGK 257
|
|
| PBP1_ABC_sugar_binding-like |
cd20008 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
402-656 |
1.62e-33 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380663 [Multi-domain] Cd Length: 277 Bit Score: 130.04 E-value: 1.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 402 IAMMPKAKGDPYFVSCKQGADEAAKELGVELLWDGPTD-LDPAKQNEVVEAWITRGVDVIAVSVENKVGISTVLRKAKeK 480
Cdd:cd20008 2 IAVIVKDTDSEYWQTVLKGAEKAAKELGVEVTFLGPATeADIAGQVNLVENAISRKPDAIVLAPNDTAALVPAVEAAD-A 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 481 GIKVITWDADAEKDARDFLIdqATPQG-IGYTLTDEAARIL----GNKGDFAIITASLSAANQNEWIKYIKERLAEKYPD 555
Cdd:cd20008 81 GIPVVLVDSGANTDDYDAFL--ATDNVaAGALAADELAELLkasgGGKGKVAIISFQAGSQTLVDREEGFRDYIKEKYPD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 556 LHLVAVQPSEGDRDRAFSETQTVLKVYPNVKLIMAIAAPAVPGAAEAVKQSGRT-DVKVTGLSLPNMNKPYVHDGVVESV 634
Cdd:cd20008 159 IEIVDVQYSDGDIAKALNQTTDLLTANPDLVGIFGANNPSAVGVAQALAEAGKAgKIVLVGFDSSPDEVALLKSGVIKAL 238
|
250 260
....*....|....*....|..
gi 1400863670 635 VLWNTVDLGYLTVYAANALATG 656
Cdd:cd20008 239 VVQDPYQMGYEGVKTAVKALKG 260
|
|
| PBP1_ABC_sugar_binding-like |
cd20005 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
402-656 |
7.22e-32 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380660 [Multi-domain] Cd Length: 274 Bit Score: 125.05 E-value: 7.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 402 IAMMPKAKGDPYFVSCKQGADEAAKELGVELLWDGPTDLDP-AKQNEVVEAWITRGVDVIAVSVENKVGISTVLRKAKEK 480
Cdd:cd20005 2 IAVISKGFQHQFWKAVKKGAEQAAKELGVKITFEGPDTESDvDKQIEMLDNAIAKKPDAIALAALDTNALLPQLEKAKEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 481 GIKVITWDADAEKDArdflidqatPQGIGYT--------LTDEAARILGNKGDFAIITASLSAANQNEWIKYIKERLAEK 552
Cdd:cd20005 82 GIPVVTFDSGVPSDL---------PLATVATdnyaagalAADHLAELIGGKGKVAIVAHDATSETGIDRRDGFKDEIKEK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 553 YPDLHLVAVQPSEGDRDRAFSETQTVLKVYPNVKLIMAIAAPAVPGAAEAVKQSGRT-DVKVTGLSLPNMNKPYVHDGVV 631
Cdd:cd20005 153 YPDIKVVNVQYGVGDHAKAADIAKAILQANPDLKGIYATNEGAAIGVANALKEMGKLgKIKVVGFDSGEAQIDAIKNGVI 232
|
250 260
....*....|....*....|....*
gi 1400863670 632 ESVVLWNTVDLGYLTVYAANALATG 656
Cdd:cd20005 233 AGSVTQNPYGMGYKTVKAAVKALKG 257
|
|
| PBP1_ABC_sugar_binding-like |
cd06310 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
401-656 |
1.64e-31 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380533 [Multi-domain] Cd Length: 272 Bit Score: 123.99 E-value: 1.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 401 VIAMMPKAKGDPYFVSCKQGADEAAKELGVELLWDGP-TDLDPAKQNEVVEAWITRGVDVIAVSVENKVGISTVLRKAKE 479
Cdd:cd06310 1 KIGVVLKGTTSAFWRTVREGAEAAAKDLGVKIIFVGPeSEEDVAGQNSLLEELINKKPDAIVVAPLDSEDLVDPLKDAKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 480 KGIKVITWDADAEKDARDFLIDQATPQGiGYTLTDEAARILGNKGDFAIITASLSAANQNEWIKYIKERLAEKYPDLHLV 559
Cdd:cd06310 81 KGIPVIVIDSGIKGDAYLSYIATDNYAA-GRLAAQKLAEALGGKGKVAVLSLTAGNSTTDQREEGFKEYLKKHPGGIKVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 560 AVQPSEGDRDRAFSETQTVLKVYPNVKLIMAIAAPAVPGAAEAVKQSGRTD-VKVTGLSLPNMNKPYVHDGVVESVVLWN 638
Cdd:cd06310 160 ASQYAGSDYAKAANETEDLLGKYPDIDGIFATNEITALGAAVAIKSRKLSGqIKIVGFDSQEELLDALKNGKIDALVVQN 239
|
250
....*....|....*...
gi 1400863670 639 TVDLGYLTVYAANALATG 656
Cdd:cd06310 240 PYEIGYEGIKLALKLLKG 257
|
|
| PBP1_ABC_sugar_binding-like |
cd06322 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
411-617 |
3.64e-30 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group includes the periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consist of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380545 [Multi-domain] Cd Length: 270 Bit Score: 120.07 E-value: 3.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 411 DPYFVSCKQGADEAAKELGVELLWDGPtDLDPAKQNEVVEAWITRGVDVIAVSVENKVGISTVLRKAKEKGIKVITwdAD 490
Cdd:cd06322 11 HPFFVDIKDAMKKEAAELGVKVVVADA-NGDLAKQLSQIEDFIQQGVDAIILAPVDSGGIVPAIEAANEAGIPVFT--VD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 491 AEKDARDFLIDQATPQGIGYTLTDEAA--RILGNKGDFAIITaSLSAANQNEWIKYIKERLaEKYPDLHLVAVQPSEGDR 568
Cdd:cd06322 88 VKADGAKVVTHVGTDNYAGGKLAGEYAlkALLGGGGKIAIID-YPEVESVVLRVNGFKEAI-KKYPNIEIVAEQPGDGRR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1400863670 569 DRAFSETQTVLKVYPNVKLIMAIAAPAVPGAAEAVKQSGRTD-VKVTGLS 617
Cdd:cd06322 166 EEALAATEDMLQANPDLDGIFAIGDPAALGALTAIESAGKEDkIKVIGFD 215
|
|
| PBP1_ABC_sugar_binding-like |
cd20006 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
400-668 |
7.38e-28 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380661 [Multi-domain] Cd Length: 274 Bit Score: 113.46 E-value: 7.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 400 PVIAMMPKAKGDpYFVSCKQGADEAAKELGVELLWDGPT-DLDPAKQNEVVEAWITRGVDVIAVSVENKVGISTVLRKAK 478
Cdd:cd20006 3 ALILKSSDPNSD-FWQTVKSGAEAAAKEYGVDLEFLGPEsEEDIDGQIELIEEAIAQKPDAIVLAASDYDRLVEAVERAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 479 EKGIKVITWDADAEKDARDFLIdqATPQ-GIGYTLTDEAARILGNKGDFAIITASLSAANQNEWIKYIKERLAEkYPDLH 557
Cdd:cd20006 82 KAGIPVITIDSPVNSKKADSFV--ATDNyEAGKKAGEKLASLLGEKGKVAIVSFVKGSSTAIEREEGFKQALAE-YPNIK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 558 LVAVQPSEGDRDRAFSETQTVLKVYPNVKLIMAIAAPAVPGAAEAVKQSGRTD-VKVTGLSLPNMNKPYVHDGVVESVVL 636
Cdd:cd20006 159 IVETEYCDSDEEKAYEITKELLSKYPDINGIVALNEQSTLGAARALKELGLGGkVKVVGFDSSVEEIQLLEEGIIDALVV 238
|
250 260 270
....*....|....*....|....*....|..
gi 1400863670 637 WNTVDLGYLTVYAANALATGtlKRGDKELNAG 668
Cdd:cd20006 239 QNPFNMGYLSVQAAVDLLNG--KKIPKRIDTG 268
|
|
| PBP1_ribose_binding |
cd06323 |
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ... |
412-656 |
6.05e-27 |
|
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose binding protein (ttRBP) and its mesophilic homologs; Periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis D-ribose binding protein (ttRBP) and its mesophilic homologs. Members of this group belong to the type 1 periplasmic binding protein superfamily, whose members are involved in chemotaxis, ATP-binding cassette transport, and intercellular communication in central nervous system. The thermophilic and mesophilic ribose-binding proteins are structurally very similar, but differ substantially in thermal stability.
Pssm-ID: 380546 [Multi-domain] Cd Length: 268 Bit Score: 110.85 E-value: 6.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 412 PYFVSCKQGADEAAKELGVELLWDGPTDlDPAKQNEVVEAWITRGVDVIAVSVENKVGISTVLRKAKEKGIKVITWDADA 491
Cdd:cd06323 12 PFFVSLKDGAQAEAKELGVELVVLDAQN-DPAKQLSQVEDLIVRKVDALLINPTDSDAVSPAVEEANEAGIPVITVDRSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 492 EKDARDFLIDQATPQGiGYTLTDEAARILGNKGDFAIITASLSAANQNEWIKYIKERLaEKYPDLHLVAVQPSEGDRDRA 571
Cdd:cd06323 91 TGGKVVSHIASDNVAG-GEMAAEYIAKKLGGKGKVVELQGIPGTSAARERGKGFHNAI-AKYPKINVVASQTADFDRTKG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 572 FSETQTVLKVYPNVKLIMAIAAPAVPGAAEAVKQSGRTDVKVTGLSLPNMNKPYVHDGVVESVVLWNTVDLGYLTVYAAN 651
Cdd:cd06323 169 LNVMENLLQAHPDIDAVFAHNDEMALGAIQALKAAGRKDVIVVGFDGTPDAVKAVKDGKLAATVAQQPEEMGAKAVETAD 248
|
....*
gi 1400863670 652 ALATG 656
Cdd:cd06323 249 KYLKG 253
|
|
| PBP1_ABC_sugar_binding-like |
cd06321 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
401-615 |
6.41e-27 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group includes the periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consist of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380544 [Multi-domain] Cd Length: 270 Bit Score: 110.46 E-value: 6.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 401 VIAMMPKAKGDPYFVSCKQGADEAAKEL--GVELLWDGpTDLDPAKQNEVVEAWITRGVDVIAVSVENKVGISTVLRKAK 478
Cdd:cd06321 1 VIGVTVQDLGNPFFVAMVRGAEEAAAEInpGAKVTVVD-ARYDLAKQFSQIDDFIAQGVDLILLNAADSAGIEPAIKRAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 479 EKGIKVITWDADAE-------KDARdflidQAtpqgiGYTLTDEAARILGNKGDFAIITASLSAANQNEwIKYIKERLAE 551
Cdd:cd06321 80 DAGIIVVAVDVAAEgadatvtTDNV-----QA-----GYLACEYLVEQLGGKGKVAIIDGPPVSAVIDR-VNGCKEALAE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1400863670 552 kYPDLHLVAVQPSEGDRDRAFSETQTVLKVYPNVKLIMAIAAPAVPGAAEAVKQSGRTDVKVTG 615
Cdd:cd06321 149 -YPGIKLVDDQNGKGSRAGGLSVMTRMLTAHPDVDGVFAINDPGAIGALLAAQQAGRDDIVITS 211
|
|
| PBP1_ABC_sugar_binding-like |
cd06317 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
411-656 |
7.96e-26 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380540 [Multi-domain] Cd Length: 281 Bit Score: 107.85 E-value: 7.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 411 DPYFVSCKQGADEAAKELGVELLWDGPTDlDPAKQNEVVEAWITRGVDVIAVSVENKVGISTVLRKAKEKGIKVITWDAD 490
Cdd:cd06317 11 AQFFNQINQGAQAAAKDLGVDLVVFNAND-DPSKQNTAVDNYIARGVDAIILDAIDVNGSIPAIKRASEAGIPVIAYDAV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 491 AEKDARDFLI--DQA-TPQGIGYTLTDEAARILGNKGDFAIITAsLSAANQNEWIKYIKERLAEKyPDLHLVAVQPSEGD 567
Cdd:cd06317 90 IPSDFQAAQVgvDNLeGGKEIGKYAADYIKAELGGQAKIGVVGA-LSSLIQNQRQKGFEEALKAN-PGVEIVATVDGQNV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 568 RDRAFSETQTVLKVYPNVKLIMAIAAPAVPGAAEAVKQSGRT-DVKVTGLSL-PNMNKPYVHDGVVESVVLWNTVDLGYL 645
Cdd:cd06317 168 QEKALSAAENLLTANPDLDAIYATGEPALLGAVAAVRSQGRQgKIKVFGWDLtKQAIFLGIDEGVLQAVVQQDPEKMGYE 247
|
250
....*....|.
gi 1400863670 646 TVYAANALATG 656
Cdd:cd06317 248 AVKAAVKAIKG 258
|
|
| PBP1_ABC_sugar_binding-like |
cd20004 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
402-656 |
1.45e-25 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380659 [Multi-domain] Cd Length: 273 Bit Score: 106.93 E-value: 1.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 402 IAMMPKAKGDPYFVSCKQGADEAAKELGVELLWDGP-TDLDPAKQNEVVEAWITRGVDVIAVSVENKVGISTVLRKAKEK 480
Cdd:cd20004 2 IAVIPKGTTHDFWKSVKAGAEKAAQELGVEIYWRGPsREDDVEAQIQIIEYFIDQGVDGIVLAPLDRKALVAPVERARAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 481 GIKVITWDADAEKDARdflidqatpqgIGYTLTD----------EAARILGNKGDFAII--TASLSAANQNEwiKYIKER 548
Cdd:cd20004 82 GIPVVIIDSDLGGDAV-----------ISFVATDnyaagrlaakRMAKLLNGKGKVALLrlAKGSASTTDRE--RGFLEA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 549 LAEKYPDLHLVAVQPSEGDRDRAFSETQTVLKVYPNVKLIMAIAAPAVPGAAEAVKQSGR-TDVKVTGLslpNMNKPYV- 626
Cdd:cd20004 149 LKKLAPGLKVVDDQYAGGTVGEARSSAENLLNQYPDVDGIFTPNESTTIGALRALRRLGLaGKVKFIGF---DASDLLLd 225
|
250 260 270
....*....|....*....|....*....|..
gi 1400863670 627 --HDGVVESVVLWNTVDLGYLTVYAANALATG 656
Cdd:cd20004 226 alRAGEISALVVQDPYRMGYLGVKTAVAALRG 257
|
|
| PBP1_allose_binding |
cd06320 |
periplasmic allose-binding domain of bacterial transport systems that function as a primary ... |
402-634 |
8.46e-24 |
|
periplasmic allose-binding domain of bacterial transport systems that function as a primary receptor of active transport and chemotaxis; Periplasmic allose-binding domain of bacterial transport systems that function as a primary receptor of active transport and chemotaxis. The members of this group are belonging to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily. Like other periplasmic receptors of the ABC-type transport systems, the allose-binding protein consists of two alpha/beta domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding.
Pssm-ID: 380543 [Multi-domain] Cd Length: 283 Bit Score: 101.96 E-value: 8.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 402 IAMMPKAKGDPYFVSCKQGADEAAKELGVEL-LWDGPTDLDPAKQNEVVEAWITRGVDVIAVSVENKVGISTVLRKAKEK 480
Cdd:cd06320 2 IGVVLKTLSNPFWVAMKDGIEAEAKKLGVKVdVQAAPSETDTQGQLNLLETMLNKGYDAILVSPISDTNLIPPIEKANKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 481 GIKVITWDADAEKDARDflidQATPQGIGYTLTDEA----------ARILGNKGDFAIITASLSAANQNEWIKYIKERLa 550
Cdd:cd06320 82 GIPVINLDDAVDADALK----KAGGKVTSFIGTDNVaagalaaeyiAEKLPGGGKVAIIEGLPGNAAAEARTKGFKETF- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 551 EKYPDLHLVAVQPSEGDRDRAFSETQTVLKVYPNVKLI------MAIaapavpGAAEAVKQSGRT-DVKVTGLslpnmnk 623
Cdd:cd06320 157 KKAPGLKLVASQPADWDRTKALDAATAILQAHPDLKGIyaandtMAL------GAVEAVKAAGKTgKVLVVGT------- 223
|
250
....*....|.
gi 1400863670 624 pyvhDGVVESV 634
Cdd:cd06320 224 ----DGIPEAK 230
|
|
| PBP1_ABC_ThpA_XypA |
cd06313 |
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ... |
402-615 |
6.02e-23 |
|
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group includes periplasmic D-threitol-binding protein ThpA and xylitol/L-sorbitol-binding protein XypA, which are part of sugar ABC-type transport systems. Both ThpA and XypA share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge.
Pssm-ID: 380536 [Multi-domain] Cd Length: 277 Bit Score: 99.27 E-value: 6.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 402 IAMMPKAKGDPYFVSCKQGADEAAKELGVELLW-DGptDLDPAKQNEVVEAWITRGVDVIAVSVENKVGISTVLRKAKEK 480
Cdd:cd06313 2 IGFTVYGLSSEFITNLVEAMKAVAKELNVDLVVlDG--NGDVSTQINQVDTLIAQGVDAIIVVPVDADALAPAVEKAKEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 481 GIKVITWDADAEKDARDFLIdQATPQGIGYTLTDEAARILGNKGDFAIITASLSAANQNEWIKYIKERLAeKYPDLHLVA 560
Cdd:cd06313 80 GIPLVGVNALIENEDLTAYV-GSDDVVAGELEGQAVADRLGGKGNVVILEGPIGQSAQIDRGKGIENVLK-KYPDIKVLA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1400863670 561 VQPSEGDRDRAFSETQTVLKVYPNVklIMAIAAP----AVpGAAEAVKQSGRTDVKVTG 615
Cdd:cd06313 158 EQTANWSRDEAMSLMENWLQAYGDE--IDGIIAQnddmAL-GALQAVKAAGRDDIPVVG 213
|
|
| PBP1_ABC_sugar_binding-like |
cd19971 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
411-615 |
3.73e-22 |
|
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380626 [Multi-domain] Cd Length: 267 Bit Score: 96.50 E-value: 3.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 411 DPYFVSCKQGADEAAKELGVELLWDGPtDLDPAKQNEVVEAWITRGVDVIAVSVENKVGISTVLRKAKEKGIKVITWDAD 490
Cdd:cd19971 11 NPFFIAINDGIKKAVEANGDELITRDP-QLDQNKQNEQIEDMINQGVDAIFLNPVDSEGIRPALEAAKEAGIPVINVDTP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 491 -AEKDARDFLI--D--QAtpqgiGYTLTDEAARILGNKGDFAIITASlSAANQNEWIKYIKERLAeKYPDLHLVAVQPSE 565
Cdd:cd19971 90 vKDTDLVDSTIasDnyNA-----GKLCGEDMVKKLPEGAKIAVLDHP-TAESCVDRIDGFLDAIK-KNPKFEVVAQQDGK 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1400863670 566 GDRDRAFSETQTVLKVYPNVKLIMAIAAPAVPGAAEAVKQSGR-TDVKVTG 615
Cdd:cd19971 163 GQLEVAMPIMEDILQAHPDLDAVFALNDPSALGALAALKAAGKlGDILVYG 213
|
|
| TM_PBP1_branched-chain-AA_like |
cd06574 |
Transmembrane subunit (TM) of Periplasmic Binding Protein (PBP)-dependent ATP-Binding Cassette ... |
65-320 |
5.94e-22 |
|
Transmembrane subunit (TM) of Periplasmic Binding Protein (PBP)-dependent ATP-Binding Cassette (ABC) transporters which are involved in the uptake of branched-chain amino acids (AAs), as well as TMs of transporters involved in the uptake of monosaccharides including ribose, galactose, and arabinose. These transporters generally bind type 1 PBPs. PBP-dependent ABC transporters consist of a PBP, two TMs, and two cytoplasmic ABCs, and are mainly involved in importing solutes from the environment. The solute is captured by the PBP which delivers it to a gated translocation pathway formed by the two TMs. The two ABCs bind and hydrolyze ATP and drive the transport reaction. This group includes Escherichia coli LivM and LivH, two TMs which heterodimerize to form the translocation pathway of the E. coli branched-chain AA LIV-1/LS transporter. This transporter is comprised of two TMs (LivM and LivH), two ABCs (LivG and LivF), and one of two alternative PBPs, LivJ (LIV-BP) and LivK (LS-BP). In addition to transporting branched-chain AAs including leucine, isoleucine and valine, the E. coli LIV-1/LS transporter is involved in the uptake of the aromatic AA, phenylalanine. Included in this group are proteins from transport systems that contain a single TM which homodimerizes to generate the transmembrane pore; for example E. coli RbsC, AlsC, and MglC, the TMs of the high affinity ribose transporter, the D-allose transporter and the galactose transporter, respectively. The D-allose transporter may also to be involved in low affinity ribose transport.
Pssm-ID: 119320 [Multi-domain] Cd Length: 266 Bit Score: 96.19 E-value: 5.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 65 IGLLAL-VMTPIIITGGIDLSVGSMMGLAAVVLGGLWREAHLPMaVAAIATLLVGALGGALNAALITRLNFPPLIVTLGT 143
Cdd:cd06574 4 YAILALgVYIVFRILGFPDLTVDGSFPLGAAVAAILIVAGYNPW-LALIAAILAGAAAGLVTGFLHTRLKINGLLAGILI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 144 FSLFRGVAEGLTRG-----IENYSGFSQQFLFLGQGYVGGLVPTqfFILIAAIAACWWWLHRTSYGRSLYAIGFSAEGAR 218
Cdd:cd06574 83 MIGLYSINLRIMGGpniplGTRDTLLGLLLLFGISGTLSIPVVL--LLIVLLVLFLVIWFLRTKLGLAMRATGDNPDMAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 219 YAGIPVARRLFFIYVLSGLASSLAAIIYVAHLGQAKSDAGTGYELMAITAVVLGGASI--FGGRGTVLGTVLGLFAIVIL 296
Cdd:cd06574 161 SLGINVDRTRILGLVISNALAALGGALYAQYQGFADVNMGIGTGVIGLAAVIIGGAIVgrRTIKASILGVIIGAILYRIA 240
|
250 260
....*....|....*....|....
gi 1400863670 297 QNGLRLSAQPAELAGILTGVLLVA 320
Cdd:cd06574 241 LALALGSGLIPSDLKLITAGVIVL 264
|
|
| TM_PBP1_LivM_like |
cd06581 |
Transmembrane subunit (TM) of Escherichia coli LivM and related proteins. LivM is one of two ... |
78-324 |
4.43e-21 |
|
Transmembrane subunit (TM) of Escherichia coli LivM and related proteins. LivM is one of two TMs of the E. coli LIV-1/LS transporter, a Periplasmic Binding Protein (PBP)-dependent ATP-Binding Cassette (ABC) transporter involved in the uptake of branched-chain amino acids (AAs). These types of transporters generally bind type 1 PBPs. PBP-dependent ABC transporters consist of a PBP, two TMs, and two cytoplasmic ABCs, and are mainly involved in importing solutes from the environment. The solute is captured by the PBP, which delivers it to a gated translocation pathway formed by the two TMs. The two ABCs bind and hydrolyze ATP and drive the transport reaction. E. coli LivM forms a heterodimer with another TM, LivH, to generate the transmembrane pore. LivH is not included in this subgroup. The LIV-1/LS transporter is comprised of two TMs (LivM and LivH), two ABCs (LivG and LivF), and one of two alternative PBPs, LivJ (LIV-BP) or LivK (LS-BP). In addition to transporting branched-chain AAs including leucine, isoleucine and valine, the E. coli LIV-1/LS transporter is involved in the uptake of the aromatic AA, phenylalanine.
Pssm-ID: 119323 [Multi-domain] Cd Length: 268 Bit Score: 93.66 E-value: 4.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 78 TGGIDLSVGSMMGLAAVVLGGLWREAHLPMAVAAIATLLVGALGGALNAALITRLNFPPL-IVTLGTFSLFRGVA---EG 153
Cdd:cd06581 18 AGQLSLGHAAFFGIGAYTAALLATRLGLPFWLALLAAGLVAALVGLLLGLPALRLRGVYFaIATLAFAEIVRLLAlnwSS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 154 LTRGIENYSGFSQQFLFLGqgyvGGLVPTQFFILIAAIAA----CWWWLHRTSYGRSLYAIGFSAEGARYAGIPVARRLF 229
Cdd:cd06581 98 LTGGSNGLSGIPPPLLGGL----LLSSPLAFYYLVLAVLLlvllLLRRLVRSPFGRALRAIRENEVAAEALGINVTRYKL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 230 FIYVLSGLASSLAAIIYVAHLGQAK-SDAGTGYELMAITAVVLggasifGGRGTVLGTVLGLFAIVILQNGLRLSAQPAE 308
Cdd:cd06581 174 LAFALSAALAGLAGALYAHYLGFVSpESFGFALSIELLLMVVL------GGLGSLLGPVLGAALLVLLPELLRSLGPGLR 247
|
250
....*....|....*.
gi 1400863670 309 LagILTGVLLVATILL 324
Cdd:cd06581 248 L--LVFGLLLILVVLF 261
|
|
| NupP |
COG4603 |
ABC-type guanosine uptake system NupNOPQ, permease component NupP [Nucleotide transport and ... |
19-338 |
8.64e-21 |
|
ABC-type guanosine uptake system NupNOPQ, permease component NupP [Nucleotide transport and metabolism];
Pssm-ID: 443653 [Multi-domain] Cd Length: 356 Bit Score: 94.42 E-value: 8.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 19 LRERLFPNNEWV--LIAV---LLVECAIFGVTGENFFSASNAF--EITRLSVEIGLLALVMTPIIITGgidLSV------ 85
Cdd:COG4603 6 LERRLLRLRSLLipLLAVllaLLVGALLILLAGANPLEAYSALfqGAFGSPYGLGETLVKATPLILTG---LAVavafra 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 86 --------GSMM--GLAAVVLGGLWreAHLPMAVAAIATLLVGALGGALNAALI----TRLNFPPLIVTLGTFSLFRGVA 151
Cdd:COG4603 83 glfnigaeGQLYlgALAAAAVGLAL--PGLPGPLHLPLALLAGALAGALWAAIPgllkARFGVNEVITTLMLNYIALYLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 152 EGLTRG--IENYSGFSQQFLFLGQGYVGGLVPTQ-----FFILIAAIAACWWWLHRTSYGRSLYAIGFSAEGARYAGIPV 224
Cdd:COG4603 161 NYLVRGplRDPGSGFPQTPPIPESARLPRLLPGTrlhlgLLIALLAAVLVWVLLNRTTLGYELRAVGLNPRAARYAGINV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 225 ARRLFFIYVLSGLASSLAAIIYVA-HLGQAKSDAGTGYELMAITAVVLggasifgGRGTVLGTVLGLFAIVILQNG---L 300
Cdd:COG4603 241 KRLIVLAMLISGALAGLAGAVEVLgVQGRLTPGFSPGYGFTGIAVALL-------GRNNPLGIILAALLFGALYVGgdaM 313
|
330 340 350
....*....|....*....|....*....|....*....
gi 1400863670 301 RLSAQ-PAELAGILTGVLLVATILLDRLSRRAQAQPRAQ 338
Cdd:COG4603 314 QRALGvPSEIVDVIQGLIILFVLAADFLIRYRLRRRRRK 352
|
|
| PBP1_sensor_kinase-like |
cd06308 |
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ... |
410-636 |
4.65e-20 |
|
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic binding domain of two-component sensor kinase signaling systems, some of which are fused with a C-terminal histidine kinase A domain (HisK) and/or a signal receiver domain (REC). Members of this group share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily and are predicted to be involved in sensing of environmental stimuli; their substrate specificities, however, are not known in detail.
Pssm-ID: 380531 [Multi-domain] Cd Length: 268 Bit Score: 90.68 E-value: 4.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 410 GDPYFVSCKQGA-DEAAKELGVELLW-DGptDLDPAKQNEVVEAWITRGVDVIAVSVENKVGISTVLRKAKEKGIKVITW 487
Cdd:cd06308 10 NDPWRAAMNEEIkAEAAKYPNVELIVtDA--QGDAAKQIADIEDLIAQGVDLLIVSPNEADALTPVVKKAYDAGIPVIVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 488 DADAEKDARDFLI--DQAtpqGIGYTLTDEAARILGNKGDFAIITASLSAANQNEWIKYIKERLAeKYPDLHLVAVQPSE 565
Cdd:cd06308 88 DRKVSGDDYTAFIgaDNV---EIGRQAGEYIAELLNGKGNVVEIQGLPGSSPAIDRHKGFLEAIA-KYPGIKIVASQDGD 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1400863670 566 GDRDRAFSETQTVLKVYPNVKLIMAIAAPAVPGAAEAVKQSGR-TDVKVTGL-SLPNMNKPYVHDGVVESVVL 636
Cdd:cd06308 164 WLRDKAIKVMEDLLQAHPDIDAVYAHNDEMALGAYQALKKAGReKEIKIIGVdGLPEAGEKAVKDGILAATFL 236
|
|
| LivM |
COG4177 |
ABC-type branched-chain amino acid transport system, permease component [Amino acid transport ... |
78-324 |
2.18e-19 |
|
ABC-type branched-chain amino acid transport system, permease component [Amino acid transport and metabolism];
Pssm-ID: 443336 [Multi-domain] Cd Length: 285 Bit Score: 88.99 E-value: 2.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 78 TGGIDLSVGSMMGLAAVVLGGLWREAHLPMAVAAIATLLVGALGGALNAALITRLNFPPL-IVTLGTFSLFRGVA---EG 153
Cdd:COG4177 28 TGLLSLGHAAFFGIGAYAAALLTTHLGLPFWLALLLAGLVAALLGLLIGLPALRLRGDYLaIATLAFAEIVRLLAlnlES 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 154 LTRGIENYSGFSQQFLFLGQgyVGGLVPTQFFILIAAIAACW--WWLHRTSYGRSLYAIGFSAEGARYAGIPVARRLFFI 231
Cdd:COG4177 108 LTGGADGLSGIPRPTLFGLD--LGSPLAFYYLVLALLVLVLLllRRLVRSRFGRALRAIRENEIAAEALGINVTRYKLLA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 232 YVLSGLASSLAAIIYVAHLGQAK-SDAGTGYELMAITAVVLggasifGGRGTVLGTVLGLFAIVILQNGLRLSaqpAELA 310
Cdd:COG4177 186 FVLSAALAGLAGALYAHYVGFVSpESFSFLLSIEILLMVVL------GGLGSLLGPVLGAVLLVLLPELLRSL---PEYR 256
|
250
....*....|....
gi 1400863670 311 GILTGVLLVATILL 324
Cdd:COG4177 257 LLIFGLLLILVVLF 270
|
|
| PBP1_ABC_sugar_binding-like |
cd19972 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
413-656 |
1.19e-18 |
|
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380627 [Multi-domain] Cd Length: 269 Bit Score: 86.34 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 413 YFVSCKQGADEAAKELGVELLWDGPTDlDPAKQNEVVEAWITRGVDVIAVSVENKVGISTVLRKAKEKGIKVITWDADAE 492
Cdd:cd19972 13 FFNQIKQSVEAEAKKKGYKVITVDAKG-DSATQVNQIQDLITQNIDALIYIPAGATAAAVPVKAARAAGIPVIAVDRNPE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 493 KDARDFLIDQATPQGiGYTLTDEAARILGNKGDFAIITASLSAANQNEWIKYIKERLAEkYPDLHLVAVQPSEGDRDRAF 572
Cdd:cd19972 92 DAPGDTFIATDSVAA-AKELGEWVIKQTGGKGEIAILHGQLGTTPEVDRTKGFQEALAE-APGIKVVAEQTADWDQDEGF 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 573 SETQTVLKVYPNVKLIMAIA-APAVpGAAEAVKQSGR-TDVKVTGLS-LPNMNKPyVHDGVVESVVLWNTVDLGYLTVYA 649
Cdd:cd19972 170 KVAQDMLQANPNITVFFGQSdAMAL-GAAQAVKVAGLdHKIWVVGFDgDVAGLKA-VKDGVLDATMTQQTQKMGRLAVDS 247
|
....*..
gi 1400863670 650 ANALATG 656
Cdd:cd19972 248 AIDLLNG 254
|
|
| PBP1_TmRBP-like |
cd19967 |
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ... |
402-670 |
3.14e-18 |
|
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ribose binding protein (ttRBP); Periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose binding protein (ttRBP) and its mesophilic homologs. Members of this group are belonging to the type 1 periplasmic binding protein superfamily, whose members are involved in chemotaxis, ATP-binding cassette transport, and intercellular communication in central nervous system. The thermophilic and mesophilic ribose-binding proteins are structurally very similar, but differ substantially in thermal stability.
Pssm-ID: 380622 [Multi-domain] Cd Length: 272 Bit Score: 85.45 E-value: 3.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 402 IAMMPKAKGDPYFVSCKQGADEAAKELGVE-LLWDgpTDLDPAKQNEVVEAWITRGVDVIAV-SVENKVGISTVlRKAKE 479
Cdd:cd19967 2 VAVIVSTPNNPFFVVEAEGAKEKAKELGYEvTVFD--HQNDTAKEAELFDTAIASGAKAIILdPADADASIAAV-KKAKD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 480 KGIKVITwdADAEKDARDFLIDQATP---QGiGYTLTDEAARILGNKGDFAIITASLSAAN----QNEWIKYIKErlaek 552
Cdd:cd19967 79 AGIPVFL--IDREINAEGVAVAQIVSdnyQG-AVLLAQYFVKLMGEKGLYVELLGKESDTNaqlrSQGFHSVIDQ----- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 553 YPDLHLVAVQPSEGDRDRAFSETQTVLKVYPNVKLIMAIAAPAVPGAAEAVKQSGR-TDVKVTGLSLPNMNKPYVHDGVV 631
Cdd:cd19967 151 YPELKMVAQQSADWDRTEAFEKMESILQANPDIKGVICGNDEMALGAIAALKAAGRaGDVIIVGFDGSNDVRDAIKEGKI 230
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1400863670 632 ESVVLWNTVDLGYLTV-YAANALATGTLKRGDKELNAGRL 670
Cdd:cd19967 231 SATVLQPAKLIARLAVeQADQYLKGGSTGKEEKQLFDCVL 270
|
|
| PBP1_ABC_sugar_binding-like |
cd06312 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
407-651 |
7.30e-18 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380535 [Multi-domain] Cd Length: 272 Bit Score: 84.21 E-value: 7.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 407 KAKGDPYFVSCKQGADEAAKELGVELLWDGPTDLDPAKQNEVVEAWITRGVDVIAVSVENKVGISTVLRKAKEKGIKVIT 486
Cdd:cd06312 8 GSPSDPFWSVVKKGAKDAAKDLGVTVQYLGPQNNDIADQARLIEQAIAAKPDGIIVTIPDPDALEPALKRAVAAGIPVIA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 487 WDADAEKDARDflidqatpqgIGYtLT----DE------AARILGNKG--DFAIITASLSAANQNEWIKYIKERLAEKYP 554
Cdd:cd06312 88 INSGDDRSKER----------LGA-LTyvgqDEylagqaAGERALEAGpkNALCVNHEPGNPGLEARCKGFADAFKGAGI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 555 DLHLVAVQpseGDRDRAFSETQTVLKVYPNVKLIMAIAAPAVPGAAEAVKQSGRTD-VKVTGLSLPNMNKPYVHDGVVES 633
Cdd:cd06312 157 LVELLDVG---GDPTEAQEAIKAYLQADPDTDAVLTLGPVGADPALKAVKEAGLKGkVKIGTFDLSPETLEAIKDGKILF 233
|
250 260
....*....|....*....|...
gi 1400863670 634 vvlwnTVDL-----GYLTVYAAN 651
Cdd:cd06312 234 -----AIDQqpylqGYLAVVFLY 251
|
|
| PBP1_ABC_D-talitol-like |
cd06318 |
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; ... |
412-615 |
9.11e-18 |
|
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380541 [Multi-domain] Cd Length: 282 Bit Score: 84.00 E-value: 9.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 412 PYFVSCKQGADEAAKELGVELLW-DGPTDLDpaKQNEVVEAWITRGVDVIAVSVENKVGISTVLRKAKEKGIKVITWDAD 490
Cdd:cd06318 12 PYYAALVAAAKAEAKKLGVELVVtDAQNDLT--KQISDVEDLITRGVDVLILNPVDPEGLTPAVKAAKAAGIPVITVDSA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 491 AEKDARDFLIDQATPQGIGYTLTDEAARILGNKGDFAIItasLSAANQNE--------WIKYIKERLAEKY--PDLHLVA 560
Cdd:cd06318 90 LDPSANVATQVGRDNKQNGVLVGKEAAKALGGDPGKIIE---LSGDKGNEvsrdrrdgFLAGVNEYQLRKYgkSNIKVVA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1400863670 561 VQPSEGDRDRAFSETQTVLKVYPNVKLIMAIAAPAVPGAAEAVKQSGRTD-VKVTG 615
Cdd:cd06318 167 QPYGNWIRSGAVAAMEDLLQAHPDINVVYAENDDMALGAMKALKAAGMLDkVKVAG 222
|
|
| PBP1_galactofuranose_YtfQ-like |
cd06309 |
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ... |
412-616 |
2.12e-17 |
|
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; Periplasmic binding domain of ABC-type YtfQ-like transport systems. The YtfQ protein from Escherichia coli is up-regulated under glucose-limited conditions and shares homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their ligand specificity is not determined experimentally.
Pssm-ID: 380532 [Multi-domain] Cd Length: 285 Bit Score: 83.04 E-value: 2.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 412 PYFVSCKQGADEAAKELGVELLWDgPTDLDPAKQNEVVEAWITRGVDVIAVSVENKVGISTVLRKAKEKGIKVITWDADA 491
Cdd:cd06309 12 PWRVANTKSIKEAAKKRGYELVYT-DANQDQEKQINDIRDLIAQGVDAILISPIDATGWDPVLKEAKDAGIPVILVDRTI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 492 EKDARDfliDQATPQGIGYTLTDE-AARILGN-----KGDFAIITASLSAANQNEWIKYIKErLAEKYPDLHLVAVQPSE 565
Cdd:cd06309 91 DGEDGS---LYVTFIGSDFVEEGRrAAEWLVKnykggKGNVVELQGTAGSSVAIDRSKGFRE-VIKKHPNIKIVASQSGN 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1400863670 566 GDRDRAFSETQTVLKVYP-NVKLI------MAIaapavpGAAEAVKQSGRT---DVKVTGL 616
Cdd:cd06309 167 FTREKGQKVMENLLQAGPgDIDVIyahnddMAL------GAIQALKEAGLKpgkDVLVVGI 221
|
|
| TM_PBP1_transp_TpRbsC_like |
cd06580 |
Transmembrane subunit (TM) of Treponema pallidum (Tp) RbsC-1, RbsC-2 and related proteins. ... |
72-319 |
6.14e-17 |
|
Transmembrane subunit (TM) of Treponema pallidum (Tp) RbsC-1, RbsC-2 and related proteins. This is a functionally uncharacterized subgroup of TMs which belong to a larger group of TMs of Periplasmic Binding Protein (PBP)-dependent ATP-Binding Cassette (ABC) transporters, which are mainly involved in the uptake of branched-chain amino acids (AAs) or in the uptake of monosaccharides including ribose, galactose, and arabinose, and which generally bind type 1 PBPs. PBP-dependent ABC transporters consist of a PBP, two TMs, and two cytoplasmic ABCs, and are mainly involved in importing solutes from the environment. The solute is captured by the PBP, which delivers it to a gated translocation pathway formed by the two TMs. The two ABCs bind and hydrolyze ATP and drive the transport reaction.
Pssm-ID: 119322 [Multi-domain] Cd Length: 234 Bit Score: 80.56 E-value: 6.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 72 MTPIIITG--------------GID--LSVGSMMGLAAVVLGGLWREAHLPMAVaaIATLLVGALGGALNAALITRLNFP 135
Cdd:cd06580 1 ATPLILAAlgvaisfragvfniGLEgqMLLGAFAAALVALYLGLPATGSLPLGL--LAAALAGALWALLPALLKAKLGVN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 136 PLIVTLgtfsLFRGVAEGLTRGIenysgfsqqflflgqgyvgglvptqFFILIAAIAACWWWLHRTSYGRSLYAIGFSAE 215
Cdd:cd06580 79 EVISGL----MLNYIALGLTSYL-------------------------LLLALLLVILVWLLLYRTRFGLRLRAVGENPR 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 216 GARYAGIPVARRLFFIYVLSGLASSLA-AIIYVAHLGQAKSDAGTGYELMAITAVVLGGASIFGgrgtVLGTVLGLFAIV 294
Cdd:cd06580 130 AARYAGINVKRVRLLAMLISGALAGLAgAYLVLGVQGRFTEGMSAGYGFIAIAVALLGRWNPLG----ILLAALLFGALE 205
|
250 260
....*....|....*....|....*.
gi 1400863670 295 ILQNGLRLSAQ-PAELAGILTGVLLV 319
Cdd:cd06580 206 AGGIALQRSGGvPSELVQVLPGIIVL 231
|
|
| LivH |
COG0559 |
Branched-chain amino acid ABC-type transport system, permease component [Amino acid transport ... |
77-324 |
7.26e-17 |
|
Branched-chain amino acid ABC-type transport system, permease component [Amino acid transport and metabolism];
Pssm-ID: 440325 [Multi-domain] Cd Length: 290 Bit Score: 81.65 E-value: 7.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 77 ITGGIDLSVGSMMGLAAVVLGGLWREAHLPMAVAAIATLLV-GALGGALNAALITRL----NFPPLIVTLGTFSLFRGVA 151
Cdd:COG0559 31 VMGVINFAHGEFVMLGAYVAYTLATLLGLPLWLALLLAVLVaALLGVLLERLVIRPLrgapPLALLLATIGLSLVLQGLV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 152 EGLtrgienYSGFSQQF-LFLGQGY-VGGLV--PTQFFILIAAI---AACWWWLHRTSYGRSLYAIGFSAEGARYAGIPV 224
Cdd:COG0559 111 LLI------FGADPRSFpALLSGSVeLGGVSipAYRLFIIVVALvllAALWLFLRRTRLGLAMRAVAQNREAARLMGINV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 225 ARRLFFIYVLSGLASSLAAIIYvAHLGQAKSDAGTGYELMAITAVVLGGAsifggrGTVLGTVLGLFAIVILQNGLRLSA 304
Cdd:COG0559 185 DRVIALTFALGAALAGLAGVLL-APIYSVSPTMGFLLGLKAFAAVVLGGL------GSIPGAVVGGLLLGLAESLGAAYL 257
|
250 260
....*....|....*....|
gi 1400863670 305 qPAELAGILTGVLLVATILL 324
Cdd:COG0559 258 -PSGYKDVVAFVLLILVLLV 276
|
|
| TM_PBP1_LivH_like |
cd06582 |
Transmembrane subunit (TM) of Escherichia coli LivH and related proteins. LivH is one of two ... |
66-324 |
1.40e-16 |
|
Transmembrane subunit (TM) of Escherichia coli LivH and related proteins. LivH is one of two TMs of the E. coli LIV-1/LS transporter, a Periplasmic Binding Protein (PBP)-dependent ATP-Binding Cassette (ABC) transporter involved in the uptake of branched-chain amino acids (AAs). These types of transporters generally bind type 1 PBPs. PBP-dependent ABC transporters consist of a PBP, two TMs, and two cytoplasmic ABCs, and are mainly involved in importing solutes from the environment. The solute is captured by the PBP, which delivers it to a gated translocation pathway formed by the two TMs. The two ABCs bind and hydrolyze ATP and drive the transport reaction. E. coli LivH forms a heterodimer with another TM, LivM, to generate the transmembrane pore. LivM is not included in this subgroup. The LIV-1/LS transporter is comprised of two TMs (LivM and LivH), two ABCs (LivG and LivF), and one of two alternative PBPs, LivJ (LIV-BP) or LivK (LS-BP). In addition to transporting branched-chain AAs including leucine, isoleucine and valine, the E. coli LIV-1/LS transporter is involved in the uptake of the aromatic AA, phenylalanine.
Pssm-ID: 119324 [Multi-domain] Cd Length: 272 Bit Score: 80.55 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 66 GLLALVMTPII-ITGGIDLSVGSMMGLAAVVLGGLWREAHLPMAVAAIATLLVGA-LGGALNAALITRLNFPPLIVTLGT 143
Cdd:cd06582 9 ALIALGLTLIFgVTGVINFAHGEFYMLGAYVAYTLLVALGLPFWLALLLALLVAAlLGVLLERLVLRPLRGAPLLTLLIT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 144 FSLFRGVAEGLTRGIENYSGFSQQFLFLGQGYVGGLV--PTQFFILIAAIAAC---WWWLHRTSYGRSLYAIGFSAEGAR 218
Cdd:cd06582 89 FGGLLILLQGLLLIFGGDPRVPPPPLLSGSVELGGVTipPYRLFIIAVALVLLaalYLFLRRTRLGRAIRAVAQNPEAAR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 219 YAGIPVARRLFFIYVLSGLASSLAAIIYvAHLGQAKSDAGTGYELMAITAVVLGGAsifggrGTVLGTVLGLFAIVILQN 298
Cdd:cd06582 169 LLGINVRRVFALTFALGAALAGLAGVLL-APITGVSPTMGLLLLLKAFAAVVLGGL------GSIPGAVVGGLLLGLAES 241
|
250 260
....*....|....*....|....*...
gi 1400863670 299 glrLSAQ--PAELAGILTGVLLVATILL 324
Cdd:cd06582 242 ---LAAAylSSGYKDAVAFVLLILVLLV 266
|
|
| PBP1_ABC_IbpA-like |
cd19968 |
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ... |
412-615 |
5.08e-16 |
|
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The periplasmic binding protein (PBP) IbpA mediates the uptake of myo-inositol by an ABC transporter that consists of the PBP IbpA, the transmembrane permease IatP, and the ABC IatA. IbpA shares homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge.
Pssm-ID: 380623 [Multi-domain] Cd Length: 271 Bit Score: 78.58 E-value: 5.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 412 PYFVSCKQGADEAAKELGVELL-WDGPTDldPAKQNEVVEAWITRGVDVIAVSVENKVGISTVLRKAKEKGIKVITWDAD 490
Cdd:cd19968 12 PFFVYMHEQAVDEAAKLGVKLVvLDAQNS--SSKQASDLENAIAQGVDGIIVSPIDVKALVPAIEAAIKAGIPVVTVDRR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 491 AEKDARDFLIDQATPQGiGYTLTDEAARILGNKGDFAIITASLSAANQNEWIKYIKERLAeKYPDLHLVAVQPSEGDRDR 570
Cdd:cd19968 90 AEGAAPVPHVGADNVAG-GREVAKFVVDKLPNGAKVIELTGTPGSSPAIDRTKGFHEELA-AGPKIKVVFEQTGNFERDE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1400863670 571 AFSETQTVLKVYPN-VKLIMAIAAPAVPGAAEAVKQSG--RTDVKVTG 615
Cdd:cd19968 168 GLTVMENILTSLPGpPDAIICANDDMALGAIEAMRAAGldLKKVKVIG 215
|
|
| PBP1_ABC_xylose_binding-like |
cd19992 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
423-656 |
6.48e-16 |
|
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic xylose-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380647 [Multi-domain] Cd Length: 284 Bit Score: 78.78 E-value: 6.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 423 EAAKELGVELLWDGpTDLDPAKQNEVVEAWITRGVDVIAVSVENKVGISTVLRKAKEKGIKVITWDADAEKDARDFLIDQ 502
Cdd:cd19992 23 EEAKELGVELIFQV-ADNDAKTQASQVENLLAQGIDVLIIAPVDAGAAANIVDKAKAAGVPVISYDRLILNADVDLYVGR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 503 ATPQgIGYTLTdEAARILGNKGDFAIITASLSAAN----QNEWIKYIKErlAEKYPDLHLVAVQPSEG-DRDRAFSETQT 577
Cdd:cd19992 102 DNYK-VGQLQA-EYALEAVPKGNYVILSGDPGDNNaqliTAGAMDVLQP--AIDSGDIKIVLDQYVKGwSPDEAMKLVEN 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 578 VLKVYPNVklIMAIAAPA---VPGAAEAVKQSGRTD-VKVTGL--SLPNMNkpYVHDGVVESVVLWNTVDLGYLTVYAAN 651
Cdd:cd19992 178 ALTANNNN--IDAVLAPNdgmAGGAIQALKAQGLAGkVFVTGQdaELAALK--RIVEGTQTMTVWKDLKELARAAADAAV 253
|
....*
gi 1400863670 652 ALATG 656
Cdd:cd19992 254 KLAKG 258
|
|
| PBP1_ABC_sugar_binding-like |
cd19970 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
401-635 |
8.72e-16 |
|
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380625 [Multi-domain] Cd Length: 275 Bit Score: 78.06 E-value: 8.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 401 VIAMMPKAKGDPYFVSCKQGADEAAKE-LGVELLWDGPTD-LDPAKQNEVVEAWITRGVDVIAVSVENKVGISTVLRKAK 478
Cdd:cd19970 1 KVALVMKSLANEFFIEMEKGARKHAKEaNGYELLVKGIKQeTDIEQQIAIVENLIAQKVDAIVIAPADSKALVPVLKKAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 479 EKGIKVITWDADAEKDA-RDFLIDqaTP-------QGiGYTLTDEAARILGNKGDFAIITASLSAANQNEWIKYIKERLA 550
Cdd:cd19970 81 DAGIAVINIDNRLDADAlKEGGIN--VPfvgpdnrQG-AYLAGDYLAKKLGKGGKVAIIEGIPGADNAQQRKAGFLKAFE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 551 EKypDLHLVAVQPSEGDRDRAFSETQTVLKVYPNVKLIMAIAAPAVPGAAEAVKQSGRTD-VKVTGLSLPNMNKPYVHDG 629
Cdd:cd19970 158 EA--GMKIVASQSANWEIDEANTVAANLLTAHPDIRGILCANDNMALGAIKAVDAAGKAGkVLVVGFDNIPAVRPLLKDG 235
|
....*.
gi 1400863670 630 VVESVV 635
Cdd:cd19970 236 KMLATI 241
|
|
| PBP1_ABC_sugar_binding-like |
cd06316 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
420-614 |
1.84e-15 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380539 [Multi-domain] Cd Length: 294 Bit Score: 77.66 E-value: 1.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 420 GADEAAKELGVELLwdGPTD--LDPAKQNEVVEAWITRGVD-VIAVSVENkVGISTVLRKAKEKGIKVITWD--ADAEKD 494
Cdd:cd06316 20 GIKDTFEELGIEVV--AVTDanFDPAKQITDLETLIALKPDiIISIPVDP-VATAAAYKKVADAGIKLVFMDnvPDGLEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 495 ARDF--LI--DQatpQGIGYTLTDEAARILGNKGDFAIIT--ASLSAANQNEwiKYIKERLAEKYPDLHLVAVQPsEGDR 568
Cdd:cd06316 97 GKDYvsVVssDN---RGNGQIAAELLAEAIGGKGKVGIIYhdADFYATNQRD--KAFKDTLKEKYPDIKIVAEQG-FADP 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1400863670 569 DRAFSETQTVLKVYPNVKLIMAIAAPAVPGAAEAVKQSGRTDVKVT 614
Cdd:cd06316 171 NDAEEVASAMLTANPDIDGIYVSWDTPALGVISALRAAGRSDIKIT 216
|
|
| PBP1_ABC_sugar_binding-like |
cd19965 |
monosaccharide ABC transporter substrate binding protein CUT2 family and similar proteins; ... |
402-618 |
7.11e-15 |
|
monosaccharide ABC transporter substrate binding protein CUT2 family and similar proteins; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380620 [Multi-domain] Cd Length: 272 Bit Score: 75.39 E-value: 7.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 402 IAMMPKAKGDPYFVSCKQGADEAAKELGVELLWDGPTDLDPAKQNEVVEAWITRGVDVIAVSVENKVGISTVLRKAKEKG 481
Cdd:cd19965 2 FVFVTHVTTNPFFQPVKKGMDDACELLGAECQFTGPQTFDVAEQVSLLEAAIASGPDGIATTIVDPEAFDEVIKRALDAG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 482 IKVITWDADAEK--DARDFLIDQATPQgIGYTLTDEAARILGNKGDFAIITasLSAANQN---EWIKYIKERLAEkYPDL 556
Cdd:cd19965 82 IPVVAFNVDAPGgeNARLAFVGQDLYP-AGYVLGKRIAEKFKPGGGHVLLG--ISTPGQSaleQRLDGIKQALKE-YGRG 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1400863670 557 HLVAVQPSEGDRDRAFSETQTVLKVYPNVKLIMAIAAPAVPGAAEAVKQSGRTD-VKVTGLSL 618
Cdd:cd19965 158 ITYDVIDTGTDLAEALSRIEAYYTAHPDIKAIFATGAFDTAGAGQAIKDLGLKGkVLVGGFDL 220
|
|
| PBP1_ABC_sugar_binding-like |
cd19973 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
401-610 |
8.91e-15 |
|
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of active transport systems that are members of the type 1 periplasmic binding protein (PBP1) superfamily. The members of this family function as the primary receptors for chemotaxis and transport of many sugar based solutes in bacteria and archaea. The sugar binding domain is also homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR. Moreover, this periplasmic binding domain, also known as Venus flytrap domain, undergoes transition from an open to a closed conformational state upon the binding of ligands such as lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars. This family also includes the periplasmic binding domain of autoinducer-2 (AI-2) receptors such as LsrB and LuxP which are highly homologous to periplasmic pentose/hexose sugar-binding proteins.
Pssm-ID: 380628 [Multi-domain] Cd Length: 285 Bit Score: 75.20 E-value: 8.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 401 VIAMMPKAKGDPYFVSCKQGADEAAKELGVELL-WDGPTDLDPAKQNEVVEAWITRGVDVIAVSVENKVGISTVLRKAKE 479
Cdd:cd19973 1 TIGLITKTDTNPFFVKMKEGAQKAAKALGIKLMtAAGKIDGDNATQVTAIENMIAAGAKGILITPSDTKAIVPAVKKARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 480 KGIKVITWDADAE-KDARDFLIdqATPQGIGYTLTDEAARILGNKGDFAIITASLS------AANQNEWIK----YIKER 548
Cdd:cd19973 81 AGVLVIALDTPTDpIDAADATF--ATDNFKAGVLIGEWAKAALGAKDAKIATLDLTpghtvgVLRHQGFLKgfgiDEKDP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1400863670 549 LAEKYP-DLHLVAVQPSEGDRDRAFSETQTVLKVYPNVKLIMAIAAPAVPGAAEAVKQSGRTD 610
Cdd:cd19973 159 ESNEDEdDSQVVGSADTNGDQAKGQTAMENLLQKDPDINLVYTINEPAAAGAYQALKAAGKEK 221
|
|
| PBP1_methylthioribose_binding-like |
cd06305 |
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a ... |
419-615 |
8.16e-14 |
|
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily; Proteins similar to methylthioribose-binding protein of ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. The sugar-binding domain of the periplasmic proteins in this group is also homologous to the ligand-binding domain of eukaryotic receptors such as metabotropic glutamate receptor (mGluR), DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380528 [Multi-domain] Cd Length: 273 Bit Score: 72.33 E-value: 8.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 419 QGADEAAKELGVELL-WDGPTDLdpAKQNEVVEAWITRGVDVIAVSVENKVGISTVLRKAKEKGIKVITWDADAEKDArd 497
Cdd:cd06305 19 QGAVAEAEKLGGTVIvFDANGDD--ARMADQIQQAITQKVDAIIISHGDADALDPKLKKALDAGIPVVTFDTDSQVPG-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 498 flIDQATP--QGIGYTLTDEAARILGNKGDFAIITA---SLSAANQNEWIKYIKErlaekYPDLHLVavQPSEGD----- 567
Cdd:cd06305 95 --VNNITQddYALGTLSLGQLVKDLNGEGNIAVFNVfgvPPLDKRYDIYKAVLKA-----NPGIKKI--VAELGDvtpnt 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1400863670 568 RDRAFSETQTVLKVYPNVKlIMAIAA----PAVpGAAEAVKQSGRTDVKVTG 615
Cdd:cd06305 166 AADAQTQVEALLKKYPEGG-IDAIWAawdePAK-GAVQALEEAGRTDIKVYG 215
|
|
| PBP1_ABC_sugar_binding-like |
cd06319 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
412-656 |
2.36e-13 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380542 [Multi-domain] Cd Length: 278 Bit Score: 70.85 E-value: 2.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 412 PYFVSCKQGADEAAKELGVELLwdgPTDLDPAKQNEV--VEAWITRGVDVIAVSVENKVGISTVLRKAKEKGIKVITWDA 489
Cdd:cd06319 12 PFWQIMERGVQAAAEELGYEFV---TYDQKNSANEQVtnANDLIAQGVDGIIISPTNSSAAPTVLDLANEAKIPVVIADI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 490 DAEKDARDFLI---DQATPQGIGYTLtdeAARILGN---KGDFAIITASLSAANQNEWIKYIKERLAEKypDLHLVAVQP 563
Cdd:cd06319 89 GTGGGDYVSYIisdNYDGGYQAGEYL---AEALKENgwgGGSVGIIAIPQSRVNGQARTAGFEDALEEA--GVEEVALRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 564 SEGDR-DRAFSETQTVLKVYPNVKLIMAIAAPAVPGAAEAVKQSGRT-DVKVTGLSLPNMNKPYVHDGVVESVVLWNTVD 641
Cdd:cd06319 164 TPNSTvEETYSAAQDLLAANPDIKGIFAQNDQMAQGALQAIEEAGRTgDILVVGFDGDPEALDLIKDGKLDGTVAQQPFG 243
|
250
....*....|....*
gi 1400863670 642 LGYLTVYAANALATG 656
Cdd:cd06319 244 MGARAVELAIQALNG 258
|
|
| PBP1_ABC_sugar_binding-like |
cd06311 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
421-613 |
5.73e-13 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380534 [Multi-domain] Cd Length: 270 Bit Score: 69.70 E-value: 5.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 421 ADEAAKELGvELLWDGPTDLDPAKQNEVVEAWITRGVDVIAVSVENKVGISTVLRKAKEKGIKVITWDADAEKDARDFLI 500
Cdd:cd06311 21 AEKQAKELA-DLEYKLVTSSNANEQVSQLEDLIAQKVDAIVILPQDSEELTVAAQKAKDAGIPVVNFDRGLNVLIYDLYV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 501 DQATPqGIGYTLTDEAARILGNKGDFAIITASLSAANQNEWIKYIKERLAEKYPDLhLVAVQPSEGDRDRAFSETQTVLK 580
Cdd:cd06311 100 AGDNP-GMGVVSAEYIGKKLGGKGNVVVLEVPSSGSVNEERVAGFKEVIKGNPGIK-ILAMQAGDWTREDGLKVAQDILT 177
|
170 180 190
....*....|....*....|....*....|...
gi 1400863670 581 VYPNVKLIMAIAAPAVPGAAEAVKQSGRTDVKV 613
Cdd:cd06311 178 KNKKIDAVWAADDDMAIGVLQAIKEAGRTDIKV 210
|
|
| PRK10653 |
PRK10653 |
ribose ABC transporter substrate-binding protein RbsB; |
385-616 |
2.77e-12 |
|
ribose ABC transporter substrate-binding protein RbsB;
Pssm-ID: 182620 [Multi-domain] Cd Length: 295 Bit Score: 68.19 E-value: 2.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 385 AAQPNSTTSQTNGHKPVIAMMPKAKGDPYFVSCKQGADEAAKELGVELLWDGPTDlDPAKQNEVVEAWITRGVDVIAVSV 464
Cdd:PRK10653 12 AVALSATVSANAMAKDTIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQN-NPAKELANVQDLTVRGTKILLINP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 465 ENKVGISTVLRKAKEKGIKVITWDADAEKD----------------ARDFLIDQAtpqgigytltDEAARILGNKGdfai 528
Cdd:PRK10653 91 TDSDAVGNAVKMANQANIPVITLDRGATKGevvshiasdnvaggkmAGDFIAKKL----------GEGAKVIQLEG---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 529 iTASLSAAnqnewikyiKER-----LAEKYPDLHLVAVQPSEGDRDRAFSETQTVLKVYPNVKLIMAIAAPAVPGAAEAV 603
Cdd:PRK10653 157 -IAGTSAA---------RERgegfkQAVAAHKFNVLASQPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRAL 226
|
250
....*....|...
gi 1400863670 604 KQSGRTDVKVTGL 616
Cdd:PRK10653 227 QTAGKSDVMVVGF 239
|
|
| PBP1_rhizopine_binding-like |
cd06301 |
periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to ... |
422-615 |
4.05e-12 |
|
periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to rhizopines, which are simple sugar-like compounds produced in the nodules induced by the symbiotic root nodule bacteria, such as Rhizobium and Sinorhizobium. Rhizopine-binding-like proteins from other bacteria are also included. Two inositol based rhizopine compounds are known to date: L-3-O-methly-scyllo-inosamine (3-O-MSI) and scyllo-inosamine. Bacterial strains that can metabolize rhizopine have a greater competitive advantage in nodulation and rhizopine synthesis is regulated by NifA/NtrA regulatory transcription activators which are maximally expressed at the onset of nitrogen fixation in bacteroids. The members of this group belong to the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily.
Pssm-ID: 380524 [Multi-domain] Cd Length: 272 Bit Score: 67.26 E-value: 4.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 422 DEAAKELGVELLW-DGptDLDPAKQNEVVEAWITRGVDVIAVSVENKVGISTVLRKAKEKGIKVITWDA--DAEKDARDF 498
Cdd:cd06301 24 AYAKEYPGVKLVIvDA--QSDAAKQLSQVENFIAQGVDAIIVNPVDTDASAPAVDAAADAGIPLVYVNRepDSKPKGVAF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 499 L----IDQATPQGigytltDEAARILGNKGDFAIITASLSAANQNEWIKYIKERLAeKYPDLHLVAVQPSEGDRDRAFSE 574
Cdd:cd06301 102 VgsddIESGELQM------EYLAKLLGGKGNIAILDGVLGHEAQILRTEGNKDVLA-KYPGMKIVAEQTANWSREKAMDI 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1400863670 575 TQTVLKVYPNVKLI------MAIaapavpGAAEAVKQSGRTD-VKVTG 615
Cdd:cd06301 175 VENWLQSGDKIDAIvanndeMAI------GAILALEAAGKKDdILVAG 216
|
|
| PBP1_ABC_sugar_binding-like |
cd19999 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
438-695 |
7.49e-12 |
|
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail.
Pssm-ID: 380654 [Multi-domain] Cd Length: 313 Bit Score: 66.95 E-value: 7.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 438 TDLDPAKQNEVVEAWITRGVDVIAVSVENKVGISTVLRKAKEKGIKVITWDADAE-KDARDFLIDQATPQGIGytlTDEA 516
Cdd:cd19999 42 ADADATGQISQIRNMINEGVDAILIDPVSATALNPVIEKAQAAGILVVSFDQPVSsPDAINVVIDQYKWAAIQ---AQWL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 517 ARILGNKGDFAIITAsLSAANQNEW-IKYIKERLAeKYPDLHLVAVQPSEGDRDRAFSETQTVLKVYPNVKLIMAIAAPA 595
Cdd:cd19999 119 AEQLGGKGNIVAING-VAGNPANEArVKAADDVFA-KYPGIKVLASVPGGWDQATAQQVMATLLATYPDIDGVLTQDGMA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 596 vPGAAEAVKQSGRTDVKVTGlslpnmnkpyvhDGVVESVVLWNTVDLGYLTVYA--------ANALATGTLKRGDKELNA 667
Cdd:cd19999 197 -EGVLRAFQAAGKDPPVMTG------------DYRKGFLRKWKELDLPDFESIGvvnppgigATALRIAVRLLQGKELKE 263
|
250 260
....*....|....*....|....*....
gi 1400863670 668 GRLGKI-EVVDDEVRLGAPFIFNKENIDK 695
Cdd:cd19999 264 DALNPLdPYLVNTLYVPEPLVVTLENLQP 292
|
|
| PRK09701 |
PRK09701 |
D-allose transporter substrate-binding protein; |
398-615 |
8.77e-12 |
|
D-allose transporter substrate-binding protein;
Pssm-ID: 182037 [Multi-domain] Cd Length: 311 Bit Score: 66.82 E-value: 8.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 398 HKPVIAMMPKAKGDPYFVSCKQGADEAAKELGVEL-LWDGPTDLDPAKQNEVVEAWITRGVDVIAVSVENKVGISTVLRK 476
Cdd:PRK09701 23 AAAEYAVVLKTLSNPFWVDMKKGIEDEAKTLGVSVdIFASPSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVAR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 477 AKEKGIKVITWDADAEKDArdflIDQATPQGIGYTLTDEAA-----------RILGNKGDFAIITASLSAANqNEWIKYI 545
Cdd:PRK09701 103 AWKKGIYLVNLDEKIDMDN----LKKAGGNVEAFVTTDNVAvgakgasfiidKLGAEGGEVAIIEGKAGNAS-GEARRNG 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1400863670 546 KERLAEKYPDLHLVAVQPSEGDRDRAFSETQTVLKVYPNVKLIMAIAAPAVPGAAEAVKQSGRT-DVKVTG 615
Cdd:PRK09701 178 ATEAFKKASQIKLVASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKTgKVLVVG 248
|
|
| PBP1_ABC_sugar_binding-like |
cd19996 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
422-615 |
1.03e-10 |
|
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail.
Pssm-ID: 380651 [Multi-domain] Cd Length: 302 Bit Score: 63.41 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 422 DEAA--KELGVELLW-DGptDLDPAKQNEVVEAWITRGVDVIAVSVENKVGISTVLRKAKEKGIKVITWDADAEKDARDF 498
Cdd:cd19996 23 AEAAklKKLIKELIYtDA--QGDTQKQIADIQDLIAQGVDAIIVSPNSPTALLPAIEKAAAAGIPVVLFDSGVGSDKYTA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 499 LI--DQATpqgIGYTLTDEAARILGNKGDfaIITASLSAANQ--NEWIKYIKERLAEkYPDLHLVAVQPSEGDRDRAFSE 574
Cdd:cd19996 101 FVgvDDAA---FGRVGAEWLVKQLGGKGN--IIALRGIAGVSvsEDRWAGAKEVFKE-YPGIKIVGEVYADWDYAKAKQA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1400863670 575 TQTVLKVYPNVKLIMAIAAPAVPGAAEAVKQSGRTDVKVTG 615
Cdd:cd19996 175 VESLLAAYPDIDGVWSDGGAMTLGAIEAFEEAGRPLVPMTG 215
|
|
| PBP1_sugar_binding |
cd06307 |
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic ... |
408-610 |
4.12e-10 |
|
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic sugar-binding domain of uncharacterized transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily. The members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes.
Pssm-ID: 380530 [Multi-domain] Cd Length: 275 Bit Score: 61.04 E-value: 4.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 408 AKGDPYFVSCKQGADEAAKEL---GVELLWDGPTDLDPAKQNEVVEAwITRGVDVIAVSVENKVGISTVLRKAKEKGIKV 484
Cdd:cd06307 8 SPENPFYELLRRAIEAAAAALrdrRVRLRIHFVDSLDPEALAAALRR-LAAGCDGVALVAPDHPLVRAAIDELAARGIPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 485 ITWDADAEKDARDFLIdqatpqGI-----GYTltdeAARILGN-----KGDFAIITASLSAANQNEWIKYIKERLAEKYP 554
Cdd:cd06307 87 VTLVSDLPGSRRLAYV------GIdnraaGRT----AAWLMGRflgrrPGKVLVILGSHRFRGHEEREAGFRSVLRERFP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1400863670 555 DLHLVAVQPSEGDRDRAFSETQTVLKVYPNVKLIMAIAApAVPGAAEAVKQSGRTD 610
Cdd:cd06307 157 DLTVLEVLEGLDDDELAYELLRELLARHPDLVGIYNAGG-GNEGIARALREAGRAR 211
|
|
| PBP1_ABC_sugar_binding-like |
cd06324 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
406-616 |
6.66e-10 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group includes the periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380547 [Multi-domain] Cd Length: 317 Bit Score: 61.08 E-value: 6.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 406 PKAKGDPYFVSCKQGADEAAKELGVELLWDgPTDLDPAKQNEVVEAWITR--GVDVIAVSVENKVGiSTVLRKAKEKGIK 483
Cdd:cd06324 7 PGKEDEPFWQNVTRFMQAAAKDLGIELEVL-YANRNRFKMLELAEELLARppKPDYLILVNEKGVA-PELLELAEQAKIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 484 VITWDADAEKDARD----------FLIDQATP--QGIGYTLTD---EAARILGNKGDFAII----TASLSAANQNEwiKY 544
Cdd:cd06324 85 VFLINNDLTDEERAllgkprekfkYWLGSIVPdnEQAGYLLAKaliKAARKKSDDGKIRVLaisgDKSTPASILRE--QG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 545 IKERLAEkYPDLHLVAVQPSEGDRDRAFSETQTVLKVYPNVKLI------MAIaapavpGAAEAVKQSGRT---DVKVTG 615
Cdd:cd06324 163 LRDALAE-HPDVTLLQIVYANWSEDEAYQKTEKLLQRYPDIDIVwaandaMAL------GAIDALEEAGLKpgkDVLVGG 235
|
.
gi 1400863670 616 L 616
Cdd:cd06324 236 I 236
|
|
| PBP1_arabinose_binding |
cd01540 |
periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose ... |
401-607 |
1.33e-09 |
|
periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily; Periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily. ABP is only involved in transport contrary to other related sugar-binding proteins such as the glucose/galactose-binding protein (GGBP) and the ribose-binding protein (RBP), both of which are involved in chemotaxis as well as transport. The periplasmic ABP consists of two alpha/beta globular domains connected by a three-stranded hinge, a Venus flytrap-like domain, which undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, ABP is homologous to the ligand-binding domain of eukaryotic receptors such as metabotropic glutamate receptor (mGluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380482 [Multi-domain] Cd Length: 294 Bit Score: 60.00 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 401 VIAMMPKAKGDPYFVSCKQGADEAAKELGVELLWDGpTDLDPAKQNEVVEAWITRGVDVIAVSVEN-KVGiSTVLRKAKE 479
Cdd:cd01540 1 KIGFIVKQPDQPWFQDEWKGAKKAAKELGFEVIKID-AKMDGEKVLSAIDNLIAQGAQGIVICTPDqKLG-PAIAAKAKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 480 KGIKVITWDadaekdarDFLIDQATPQG----------IGYTLTDEAARIL-------GNKGDFAIITA-SLSAAnqNEW 541
Cdd:cd01540 79 AGIPVIAVD--------DQLVDADPMKIvpfvgidaykIGEAVGEWLAKEMkkrgwddVKEVGVLAITMdTLSVC--VDR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1400863670 542 IKYIKERLAEK-YPDLHLVAVQPSEGDRDRAFSETQTVLKVYPNVK--LIMAIAAPAVPGAAEAVKQSG 607
Cdd:cd01540 149 TDGAKDALKAAgFPEDQIFQAPYKGTDTEGAFNAANAVITAHPEVKhwLVVGCNDEGVLGAVRALEQAG 217
|
|
| PBP1_ABC_sugar_binding-like |
cd06300 |
periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are ... |
438-615 |
5.50e-09 |
|
periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail.
Pssm-ID: 380523 [Multi-domain] Cd Length: 302 Bit Score: 58.10 E-value: 5.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 438 TDLDPAKQNEVVEAWITRGVDVIAVSVENKVGISTVLRKAKEKGIKVITWD-ADAEKDARDFLIDQATpqgIGYTLTDEA 516
Cdd:cd06300 42 SNGDATEQIAQIRNLIDQGVDAIIINPSSPTALNAVIEQAADAGIPVVAFDgAVTSPDAYNVSNDQVE---WGRLGAKWL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 517 ARILGNKGDFAIITASLSAANQNEWIKYIKERLAEkYPDLHLVAVQPSEGDRDRAFSETQTVLKVYPNVKLIMAIAAPAV 596
Cdd:cd06300 119 FEALGGKGNVLVVRGIAGAPASADRHAGVKEALAE-YPGIKVVGEVFGGWDEATAQTAMLDFLATHPQVDGVWTQGGEDT 197
|
170
....*....|....*....
gi 1400863670 597 pGAAEAVKQSGRTDVKVTG 615
Cdd:cd06300 198 -GVLQAFQQAGRPPVPIVG 215
|
|
| XylF |
COG4213 |
ABC-type xylose transport system, periplasmic component [Carbohydrate transport and metabolism] ... |
423-488 |
6.77e-08 |
|
ABC-type xylose transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 443359 [Multi-domain] Cd Length: 310 Bit Score: 54.76 E-value: 6.77e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1400863670 423 EAAKELGVEllwdgpTDL-----DPAKQNEVVEAWITRGVDVIAVSVENKVGISTVLRKAKEKGIKVITWD 488
Cdd:COG4213 26 AALKELGYE------VDVqnangDVATQLSQIENMITKGADVLVIAPIDGTALAAVLEKAKAAGIPVIAYD 90
|
|
| PBP1_ABC_sugar_binding-like |
cd19966 |
monosaccharide ABC transporter substrate binding protein CUT2 family and simialr proteins; ... |
401-529 |
2.09e-07 |
|
monosaccharide ABC transporter substrate binding protein CUT2 family and simialr proteins; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380621 [Multi-domain] Cd Length: 278 Bit Score: 53.10 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 401 VIAMMP-KAKGDPYFVSCKQGADEAAKELGVELLWDGPtDLDPAKQNEVVEAWITRGVDVIAVSVENKVGIST-VLRKAK 478
Cdd:cd19966 1 KIYFIPgGAPGDPFWTVVYNGAKDAAADLGVDLDYVFS-SWDPEKMVEQFKEAIAAKPDGIAIMGHPGDGAYTpLIEAAK 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1400863670 479 EKGIKVITWDAD----AEKDARDFLIDQATPQGiGYTLTDEAARILGNK-GDFAII 529
Cdd:cd19966 80 KAGIIVTSFNTDlpklEYGDCGLGYVGADLYAA-GYTLAKELVKRGGLKtGDRVFV 134
|
|
| PBP1_TorT-like |
cd06306 |
TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor ... |
411-614 |
2.72e-07 |
|
TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor respiratory system upon trimethylamine N-oxide (TMAO) electron-acceptor binding in bacteria; TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor respiratory system upon trimethylamine N-oxide (TMAO) electron-acceptor binding in bacteria. The Tor respiratory system is consists of three proteins (TorC, TorA, and TorD) and is induced in the presence of TMAO. The TMAO control is tightly regulated by three proteins: TorS, TorT, and TorR. Thus, the disruption of any of these proteins can abolish the Tor respiratory induction. TorT shares homology with the sugar-binding domain of the type 1 periplasmic binding proteins. The members of TorT-like family bind TMAO or related compounds and are predicted to be involved in signal transduction and/or substrate transport.
Pssm-ID: 380529 [Multi-domain] Cd Length: 269 Bit Score: 52.58 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 411 DPYFVSCKQGADEAAKELGVEL-LWD--GPTDLdpAKQNEVVEAWITRGVDVIAVSVENKVGISTVLRKAKEKGIKVItw 487
Cdd:cd06306 11 DSYWVGVNYGIVDEAKRLGVKLtVYEagGYTNL--SKQISQLEDCVASGADAILLGAISFDGLDPKVAEAAAAGIPVI-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 488 dadaekdarDFLIDQATPQGIGYTLTD------EAARILGNKGDFAIITASLSAANQN-EWIKYIKERLAE--KYPDLHL 558
Cdd:cd06306 87 ---------DLVNGIDSPKVAARVLVDfydmgyLAGEYLVEHHPGKPVKVAWFPGPAGaGWAEDREKGFKEalAGSNVEI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1400863670 559 VAVQPSEGDRDRAFSETQTVLKVYPNVKLIMAiAAPAVPGAAEAVKQSGRT-DVKVT 614
Cdd:cd06306 158 VATKYGDTGKAVQLNLVEDALQAHPDIDYIVG-NAVAAEAAVGALREAGLTgKVKVV 213
|
|
| PBP1_LuxPQ_Quorum_Sensing |
cd06303 |
periplasmic binding protein (LuxP) of autoinducer-2 (AI-2) receptor LuxPQ from Vibrio harveyi ... |
512-615 |
4.72e-07 |
|
periplasmic binding protein (LuxP) of autoinducer-2 (AI-2) receptor LuxPQ from Vibrio harveyi and its close homologs; Periplasmic binding protein (LuxP) of autoinducer-2 (AI-2) receptor LuxPQ from Vibrio harveyi and its close homologs from other bacteria. The members of this group are highly homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transport of many sugar based solutes in bacteria and archaea, and that are members of the type 1 periplasmic binding protein superfamily. The Vibrio harveyi AI-2 receptor consists of two polypeptides, LuxP and LuxQ: LuxP is a periplasmic binding protein that binds AI-2 by clamping it between two domains, LuxQ is an integral membrane protein belonging to the two-component sensor kinase family. Unlike AI-2 bound to the LsrB receptor in Salmonella typhimurium, the Vibrio harveyi AI-2 signaling molecule has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LuxPQ to control light production as well as its motility behavior.
Pssm-ID: 380526 [Multi-domain] Cd Length: 320 Bit Score: 52.37 E-value: 4.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 512 LTDEAARILGNKGDFAII---TASLSAANQNEWIKYIKErlaekYPDLHLVAVQPSEGDRDRAFSETQTVLKVYPNVKLI 588
Cdd:cd06303 148 LAKHFIKIFPEEGKYAILyltEGYVSDQRGDTFIDEVAR-----HSNLELVSAYYTDFDRESAREAARALLARHPDLDFI 222
|
90 100
....*....|....*....|....*...
gi 1400863670 589 MAIAAPAVPGAAEAVKQSGR-TDVKVTG 615
Cdd:cd06303 223 YACSTDIALGAIDALQELGReTDIMING 250
|
|
| PBP1_ABC_xylose_binding-like |
cd01538 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems that belong ... |
423-500 |
5.62e-07 |
|
periplasmic xylose-like sugar-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily; Periplasmic xylose-like sugar-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380480 [Multi-domain] Cd Length: 283 Bit Score: 51.65 E-value: 5.62e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1400863670 423 EAAKELGVELLWDGpTDLDPAKQNEVVEAWITRGVDVIAVSVENKVGISTVLRKAKEKGIKVITWDADAEKDARDFLI 500
Cdd:cd01538 23 EQLEEKGAKVLVQS-ADGDKAKQASQIENLLTQGADVLVLAPVDGQALSPVVAEAKAEGIKVIAYDRLILNADVDYYI 99
|
|
| PBP1_ABC_sugar_binding-like |
cd19997 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
419-608 |
1.57e-06 |
|
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail.
Pssm-ID: 380652 [Multi-domain] Cd Length: 305 Bit Score: 50.37 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 419 QGADEAAKELGVE-LLWDGP---TDLDPAKQNEVVEAWITRGVDVIAVSVENKVGISTVLRKAKEKGIKVITWDADAEKD 494
Cdd:cd19997 19 DAFEEAAKKAKADgLIADYIvvnADGSATTQISQIQNLILQGVDAIVIDAASPTALNGAIQQACDAGIKVVVFDSGVTEP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 495 ARDFLIDQAtpQGIGYTLTDEAARILGNKGDFAIITASLSAANQNEWIKYIKERLAeKYPDLHLVAVQPSEGDRDRAFSE 574
Cdd:cd19997 99 CAYILNNDF--EDYGAASVEYVADRLGGKGNVLEVRGVAGTSPDEEIYAGQVEALK-KYPDLKVVAEVYGNWTQSVAQKA 175
|
170 180 190
....*....|....*....|....*....|....
gi 1400863670 575 TQTVLKVYPNVKLIMAIAAPAVpGAAEAVKQSGR 608
Cdd:cd19997 176 VTGILPSLPEVDAVITQGGDGY-GAAQAFEAAGR 208
|
|
| PBP1_ABC_xylose_binding-like |
cd19993 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
441-657 |
1.84e-06 |
|
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic xylose-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380648 [Multi-domain] Cd Length: 287 Bit Score: 50.17 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 441 DPAKQNEVVEAWITRGVDVIAVSVENKVGISTVLRKAKEKGIKVITWDAdaekdardfLIDQatpQGIGYTLTD------ 514
Cdd:cd19993 40 SAEKQLDDIESLISQGAKALIVLAQDGDAILPAVEKAAAEGIPVIAYDR---------LIEN---PIAFYISFDnvevgr 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 515 -EAARILG--NKGDFAIITASLSAANQNEWIKYIKERL--AEKYPDLHLVAVQPSEG-DRDRAFSETQTVLKVYPN-VKL 587
Cdd:cd19993 108 mQARGVLKakPEGNYVFIKGSPTDPNADFLRAGQMEVLqpAIDSGKIKIVGEQYTDGwKPANAQKNMEQILTANNNkVDA 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1400863670 588 IMAIAAPAVPGAAEAVKQSG-RTDVKVTGLSLPNMNKPYVHDGVVESVVLWNTVDLGYLTVYAANALATGT 657
Cdd:cd19993 188 VVASNDGTAGGAVAALAAQGlAGKVPVSGQDADKAALNRIALGTQTVTVWKDARELGKEAAEIAVELAKGT 258
|
|
| PBP1_ABC_sugar_binding-like |
cd19998 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
441-615 |
2.15e-06 |
|
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail.
Pssm-ID: 380653 [Multi-domain] Cd Length: 302 Bit Score: 49.98 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 441 DPAKQNEVVEAWITRGVDVIAVSVENKVGISTVLRKAKEKGIKVITWDADA-EKDARDFLIDQAtpqGIGYTLTDEAARI 519
Cdd:cd19998 44 DVQAQISAIDNMIAAGYDAILIYAISPTALNPVIKRACDAGIVVVAFDNVVdEPCAYNVNTDQA---KAGEQTAQWLVDK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 520 LGNKGDFAIITASLSAANQNEWIKYIKERLaEKYPDLHLVAvqPSEGDRDRAFSETQT--VLKVYPNVKLIMAIAAPAvp 597
Cdd:cd19998 121 LGGKGNILMVRGVPGTSVDRDRYEGAKEVF-KKYPDIKVVA--EYYGNWDDGTAQKAVadALAAHPDVDGVWTQGGET-- 195
|
170
....*....|....*...
gi 1400863670 598 GAAEAVKQSGRTDVKVTG 615
Cdd:cd19998 196 GVIKALQAAGHPLVPVGG 213
|
|
| PBP1_GGBP |
cd01539 |
periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and ... |
411-610 |
2.48e-06 |
|
periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and active transport of, glucose and galactose in various bacterial species; Periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and active transport of, glucose and galactose in various bacterial species. GGBP is a member of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic GGBP is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380481 [Multi-domain] Cd Length: 302 Bit Score: 49.89 E-value: 2.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 411 DPYFVSCKQGADEAAKELG-VELL-WDGptDLDPAKQNEVVEAWITRGVDVIAVSVENKVGISTVLRKAKEKGIKVITW- 487
Cdd:cd01539 12 DTFISSVRKALEKAAKAGGkIELEiYDA--QNDQSTQNDQIDTMIAKGVDLLVVNLVDRTAAQTIIDKAKAANIPVIFFn 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 488 ---DADAEKDARDFLIdqatpqgIGyTLTDEAARILG------------------NKGDFAIITASLSAANQNEWIKYIK 546
Cdd:cd01539 90 repSREDLKSYDKAYY-------VG-TDAEESGIMQGeiiadywkanpeidkngdGKIQYVMLKGEPGHQDAIARTKYSV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1400863670 547 ERLAEKYPDLHLVAVQPSEGDRDRAFSETQTVLKVYP-NVKLI------MAIaapavpGAAEAVKQSGRTD 610
Cdd:cd01539 162 KTLNDAGIKTEQLAEDTANWDRAQAKDKMDAWLSKYGdKIELViannddMAL------GAIEALKAAGYNT 226
|
|
| PBP1_ChvE |
cd19994 |
periplasmic sugar binding protein ChvE that interacts with a bacterial two-component signaling ... |
441-488 |
4.45e-06 |
|
periplasmic sugar binding protein ChvE that interacts with a bacterial two-component signaling system; Periplasmic aldose-monosaccharides binding protein ChvE that belongs to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380649 [Multi-domain] Cd Length: 304 Bit Score: 49.17 E-value: 4.45e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1400863670 441 DPAKQNEVVEAWITRGVDVIAVSVENKVGISTVLRKAKEKGIKVITWD 488
Cdd:cd19994 40 DVATQNSQIENMINKGAKVLVIAPVDGSALGDVLEEAKDAGIPVIAYD 87
|
|
| PBP1_ABC_xylose_binding |
cd19991 |
D-xylose binding periplasmic protein; Periplasmic xylose-binding component of the ABC-type ... |
423-488 |
5.99e-05 |
|
D-xylose binding periplasmic protein; Periplasmic xylose-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380646 [Multi-domain] Cd Length: 284 Bit Score: 45.30 E-value: 5.99e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1400863670 423 EAAKELGVELLWDGPTDlDPAKQNEVVEAWITRGVDVIAVSVENKVGISTVLRKAKEKGIKVITWD 488
Cdd:cd19991 23 KKAKELGAEVIVQSANG-DDEKQISQAEELIEQGVDVLVVVPNNGEALAPIVKEAKKAGVPVLAYD 87
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| Peripla_BP_1 |
pfam00532 |
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ... |
399-608 |
1.07e-04 |
|
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the periplasmic binding proteins, and the LacI family transcriptional regulators. The periplasmic binding proteins are the primary receptors for chemotaxis and transport of many sugar based solutes. The LacI family of proteins consist of transcriptional regulators related to the lac repressor. In this case, generally the sugar binding domain binds a sugar which changes the DNA binding activity of the repressor domain (pfam00356).
Pssm-ID: 395423 [Multi-domain] Cd Length: 281 Bit Score: 44.81 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 399 KPVIAMMPKAKGDPYFVSCKQGADEAAKELGVEL-LWDGPTDLDPA-KQNEVVEAWitrGVD-VIAVSVENKvgISTVLR 475
Cdd:pfam00532 1 TLKLGALVPQLDEPFFQDLVKGITKAAKDHGFDVfLLAVGDGEDTLtNAIDLLLAS---GADgIIITTPAPS--GDDITA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 476 KAKEKGIKVITWDadaekdaRDFLIDQATPQG------IGYTLTDEAARiLGNKGDFAIITASLSAANQNEWIKYIKERL 549
Cdd:pfam00532 76 KAEGYGIPVIAAD-------DAFDNPDGVPCVmpddtqAGYESTQYLIA-EGHKRPIAVMAGPASALTARERVQGFMAAL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1400863670 550 AEKYPDLHLVAVQPSEGDRDRAFSETQTVLKVYPNVKLIMAIAAPAVPGAAEAVKQSGR 608
Cdd:pfam00532 148 AAAGREVKIYHVATGDNDIPDAALAANAMLVSHPTIDAIVAMNDEAAMGAVRALLKQGR 206
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|
| PBP1_ABC_xylose_binding-like |
cd19995 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
441-509 |
2.49e-04 |
|
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic xylose-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380650 [Multi-domain] Cd Length: 294 Bit Score: 43.43 E-value: 2.49e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1400863670 441 DPAKQNEVVEAWITRGVDVIAVSVENKVGISTVLRKAKEKGIKVITWDADAEKDARDFLIdQATPQGIG 509
Cdd:cd19995 43 DASTQQQQAEAAITQGAKVLVVDPVDSNAAAGIVAKAAQAGVPVIAYDRLILGGPADYYV-SFDNVAVG 110
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|
| Med |
COG1744 |
Lipoprotein Med, regulator of KinD/Spo0A, PBP1-ABC superfamily, includes NupN [Signal ... |
418-500 |
1.25e-03 |
|
Lipoprotein Med, regulator of KinD/Spo0A, PBP1-ABC superfamily, includes NupN [Signal transduction mechanisms];
Pssm-ID: 441350 Cd Length: 300 Bit Score: 41.28 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400863670 418 KQGADEAAKELGVELLWDGPTDlDPAKQNEVVEAWITRGVDVIAvSVENKVGIStVLRKAKEKG-IKVITWDADAEKDAR 496
Cdd:COG1744 148 ALGAKYVNPDIKVLVVYTGSFS-DPAKGKEAALALIDQGADVIF-QAAGGTGVG-VIQAAKEAGkVYAIGVDSDQSALAP 224
|
....
gi 1400863670 497 DFLI 500
Cdd:COG1744 225 DVVL 228
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