|
Name |
Accession |
Description |
Interval |
E-value |
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
109-378 |
1.03e-37 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 136.67 E-value: 1.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496329379 109 VMCMTSLQLSNFIRLDACDYVVGITSTRHLFNKEmnerLKSGETVKIGIEGNFDNEVIMSMNPDVIFISPFKRGG--YDA 186
Cdd:COG0614 3 IVSLSPSATELLLALGAGDRLVGVSDWGYCDYPE----LELKDLPVVGGTGEPNLEAILALKPDLVLASSSGNDEedYEQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496329379 187 MREIGIPLVPhLGYKEMTPLgqAEWIKFIGMFIGQEVEANEKFAAIEKRYNELKELAANVKKRPMVFSGEIRGGNWYAVG 266
Cdd:COG0614 79 LEKIGIPVVV-LDPRSLEDL--YESIRLLGELLGREERAEALIAEYEARLAAVRARLAGAEERPTVLYEIWSGDPLYTAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496329379 267 GKSFLAELFRDAGADYfLKDDPRSGGVTLDFETVYSQAesADYWrIVNSYDGTF-----TYDALKSlDPRYADFRAFREK 341
Cdd:COG0614 156 GGSFIGELLELAGGRN-VAADLGGGYPEVSLEQVLALD--PDVI-ILSGGGYDAetaeeALEALLA-DPGWQSLPAVKNG 230
|
250 260 270
....*....|....*....|....*....|....*....
gi 496329379 342 GVVYCnmrekPFYESMPMQPEIV--LEDLIHAFHPDLLP 378
Cdd:COG0614 231 RVYVV-----PGDLLSRPGPRLLlaLEDLAKALHPELFA 264
|
|
| TroA_d |
cd01141 |
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ... |
101-286 |
3.17e-28 |
|
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial receptors in the ABC metal ion uptake in eubacteria and archaea. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.
Pssm-ID: 238561 [Multi-domain] Cd Length: 186 Bit Score: 109.05 E-value: 3.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496329379 101 VIETPVEHVMCMTSLQLSNFIRLDACDYVVGITSTRhlfNKEMNERLKSGETVKIGIEGNFDNEVIMSMNPDVIFIS--P 178
Cdd:cd01141 3 TIKVPPKRIVVLSPTHVDLLLALDKADKIVGVSASA---YDLNTPAVKERIDIQVGPTGSLNVELIVALKPDLVILYggF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496329379 179 FKRGGYDAMREIGIPLVphLGYKEMTPLGQAEWIKFIGMFIGQEVE--ANEKFAAIEKRYNELKELAANvKKRPMVFSGE 256
Cdd:cd01141 80 QAQTILDKLEQLGIPVL--YVNEYPSPLGRAEWIKFAAAFYGVGKEdkADEAFAQIAGRYRDLAKKVSN-LNKPTVAIGK 156
|
170 180 190
....*....|....*....|....*....|
gi 496329379 257 IRGGNWYAVGGKSFLAELFRDAGADYFLKD 286
Cdd:cd01141 157 PVKGLWYMPGGNSYVAKMLRDAGGRYLSAE 186
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
111-347 |
1.56e-17 |
|
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding proteins, several of which are involved in iron and cobalamin transport. Among its ligands are siderophores bacillibactin, enterobactin and iron(III)-hydroxamates (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1 https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 426291 [Multi-domain] Cd Length: 233 Bit Score: 80.88 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496329379 111 CMTSLQLSNFIRLDACDYVVGI-TSTRHLFNKEMNERLKSGETVKigiEGNFdnEVIMSMNPDVIFISPFkrGGYDAMRE 189
Cdd:pfam01497 2 ALSPAYTEILYALGATDSIVGVdAYTRDPLKADAVAAIVKVGAYG---EINV--ERLAALKPDLVILSTG--YLTDEAEE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496329379 190 IGIPLVPHLGYKE-MTPLGQAEWIKFIGMFIGQEVEANEKFAAIEKRYNELKELAANVKKRPMVFSGEIRGGNWYAVGGK 268
Cdd:pfam01497 75 LLSLIIPTVIFESsSTGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPVLVFGGADGGGYVVAGSN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496329379 269 SFLAELFRDAGADYFLKDDPRSGGVTLDFETVYSQAesADYWrIVNSYDG--TFTYDALKSlDPRYADFRAFREKGVVYC 346
Cdd:pfam01497 155 TYIGDLLRILGIENIAAELSGSEYAPISFEAILSSN--PDVI-IVSGRDSftKTGPEFVAA-NPLWAGLPAVKNGRVYTL 230
|
.
gi 496329379 347 N 347
Cdd:pfam01497 231 P 231
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
109-378 |
1.03e-37 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 136.67 E-value: 1.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496329379 109 VMCMTSLQLSNFIRLDACDYVVGITSTRHLFNKEmnerLKSGETVKIGIEGNFDNEVIMSMNPDVIFISPFKRGG--YDA 186
Cdd:COG0614 3 IVSLSPSATELLLALGAGDRLVGVSDWGYCDYPE----LELKDLPVVGGTGEPNLEAILALKPDLVLASSSGNDEedYEQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496329379 187 MREIGIPLVPhLGYKEMTPLgqAEWIKFIGMFIGQEVEANEKFAAIEKRYNELKELAANVKKRPMVFSGEIRGGNWYAVG 266
Cdd:COG0614 79 LEKIGIPVVV-LDPRSLEDL--YESIRLLGELLGREERAEALIAEYEARLAAVRARLAGAEERPTVLYEIWSGDPLYTAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496329379 267 GKSFLAELFRDAGADYfLKDDPRSGGVTLDFETVYSQAesADYWrIVNSYDGTF-----TYDALKSlDPRYADFRAFREK 341
Cdd:COG0614 156 GGSFIGELLELAGGRN-VAADLGGGYPEVSLEQVLALD--PDVI-ILSGGGYDAetaeeALEALLA-DPGWQSLPAVKNG 230
|
250 260 270
....*....|....*....|....*....|....*....
gi 496329379 342 GVVYCnmrekPFYESMPMQPEIV--LEDLIHAFHPDLLP 378
Cdd:COG0614 231 RVYVV-----PGDLLSRPGPRLLlaLEDLAKALHPELFA 264
|
|
| TroA_d |
cd01141 |
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ... |
101-286 |
3.17e-28 |
|
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial receptors in the ABC metal ion uptake in eubacteria and archaea. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.
Pssm-ID: 238561 [Multi-domain] Cd Length: 186 Bit Score: 109.05 E-value: 3.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496329379 101 VIETPVEHVMCMTSLQLSNFIRLDACDYVVGITSTRhlfNKEMNERLKSGETVKIGIEGNFDNEVIMSMNPDVIFIS--P 178
Cdd:cd01141 3 TIKVPPKRIVVLSPTHVDLLLALDKADKIVGVSASA---YDLNTPAVKERIDIQVGPTGSLNVELIVALKPDLVILYggF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496329379 179 FKRGGYDAMREIGIPLVphLGYKEMTPLGQAEWIKFIGMFIGQEVE--ANEKFAAIEKRYNELKELAANvKKRPMVFSGE 256
Cdd:cd01141 80 QAQTILDKLEQLGIPVL--YVNEYPSPLGRAEWIKFAAAFYGVGKEdkADEAFAQIAGRYRDLAKKVSN-LNKPTVAIGK 156
|
170 180 190
....*....|....*....|....*....|
gi 496329379 257 IRGGNWYAVGGKSFLAELFRDAGADYFLKD 286
Cdd:cd01141 157 PVKGLWYMPGGNSYVAKMLRDAGGRYLSAE 186
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
111-347 |
1.56e-17 |
|
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding proteins, several of which are involved in iron and cobalamin transport. Among its ligands are siderophores bacillibactin, enterobactin and iron(III)-hydroxamates (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1 https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 426291 [Multi-domain] Cd Length: 233 Bit Score: 80.88 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496329379 111 CMTSLQLSNFIRLDACDYVVGI-TSTRHLFNKEMNERLKSGETVKigiEGNFdnEVIMSMNPDVIFISPFkrGGYDAMRE 189
Cdd:pfam01497 2 ALSPAYTEILYALGATDSIVGVdAYTRDPLKADAVAAIVKVGAYG---EINV--ERLAALKPDLVILSTG--YLTDEAEE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496329379 190 IGIPLVPHLGYKE-MTPLGQAEWIKFIGMFIGQEVEANEKFAAIEKRYNELKELAANVKKRPMVFSGEIRGGNWYAVGGK 268
Cdd:pfam01497 75 LLSLIIPTVIFESsSTGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPVLVFGGADGGGYVVAGSN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496329379 269 SFLAELFRDAGADYFLKDDPRSGGVTLDFETVYSQAesADYWrIVNSYDG--TFTYDALKSlDPRYADFRAFREKGVVYC 346
Cdd:pfam01497 155 TYIGDLLRILGIENIAAELSGSEYAPISFEAILSSN--PDVI-IVSGRDSftKTGPEFVAA-NPLWAGLPAVKNGRVYTL 230
|
.
gi 496329379 347 N 347
Cdd:pfam01497 231 P 231
|
|
| YvrC |
cd01143 |
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ... |
123-280 |
1.13e-12 |
|
Periplasmic binding protein YvrC. These proteins are predicted to function as initial receptors in ABC transport of metal ions in eubacteria and archaea. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains.
Pssm-ID: 238563 [Multi-domain] Cd Length: 195 Bit Score: 66.15 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496329379 123 LDACDYVVGITSTRHlFNKEMNErlksgeTVKIGIEGNFDNEVIMSMNPDVIFISP-FKRGGYDAMREIGIPLVPhlgyk 201
Cdd:cd01143 20 LGAGDKIVGVDTYSN-YPKEVRK------KPKVGSYSNPNVEKIVALKPDLVIVSSsSLAELLEKLKDAGIPVVV----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496329379 202 emTPLGQA-----EWIKFIGMFIGQEVEANEkfaAIEKRYNELKELAANVK-KRPMVFSGEIRGGNWYAVGGKSFLAELF 275
Cdd:cd01143 88 --LPAASSldeiyDQIELIGKITGAEEEAEK---LVKEMKQKIDKVKDKGKtIKKSKVYIEVSLGGPYTAGKNTFINELI 162
|
....*
gi 496329379 276 RDAGA 280
Cdd:cd01143 163 RLAGA 167
|
|
| TroA-like |
cd00636 |
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ... |
107-253 |
9.70e-12 |
|
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function in the ABC transport of ferric siderophores and metal ions such as Mn2+, Fe3+, Cu2+ and/or Zn2+. Their ligand binding site is formed in the interface between two globular domains linked by a single helix. Many of these proteins also possess a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence). The TroA-like proteins differ in their fold and ligand-binding mechanism from the PBPI and PBPII proteins, but are structurally similar, however, to the beta-subunit of the nitrogenase molybdenum-iron protein MoFe. Most TroA-like proteins are encoded by ABC-type operons and appear to function as periplasmic components of ABC transporters in metal ion uptake.
Pssm-ID: 238347 [Multi-domain] Cd Length: 148 Bit Score: 62.58 E-value: 9.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496329379 107 EHVMCMTSLQLSNFIRLDACDYVVGITSTrhlFNKEMNERLKSGETVKIGIEGNFDNEVIMSMNPDVIFISPF-KRGGYD 185
Cdd:cd00636 1 KRVVALDPGATELLLALGGDDKPVGVADP---SGYPPEAKALLEKVPDVGHGYEPNLEKIAALKPDLIIANGSgLEAWLD 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496329379 186 AMREIGIPLVPHLGYKEMTPLGQAEWIKFIGMFIGQEVEANEKFAAIEKRYNELKELAANVKKRPMVF 253
Cdd:cd00636 78 KLSKIAIPVVVVDEASELSLENIKESIRLIGKALGKEENAEELIAELDARLAELRAKLAKIPKKKVSL 145
|
|
| HemV-2 |
cd01147 |
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ... |
102-343 |
1.79e-10 |
|
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors in ABC transport of metal ions. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains. In addition, these proteins sometimes have a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence).
Pssm-ID: 238567 [Multi-domain] Cd Length: 262 Bit Score: 60.81 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496329379 102 IETPVEHVMCmTSLQLSNFIR-LDACDYVVGITSTRHLFNKEM----NERLKSGETVKIGIEGNFDN-EVIMSMNPDVIF 175
Cdd:cd01147 1 VPKPVERVVA-AGPGALRLLYaLAAPDKIVGVDDAEKSDEGRPyflaSPELKDLPVIGRGGRGNTPNyEKIAALKPDVVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496329379 176 IspfkRGGYDAMREI-------GIPLVphLGYkemTPLGQAEW---IKFIGMFIGQEVEANEKFAAIEKRYNELKELAAN 245
Cdd:cd01147 80 D----VGSDDPTSIAddlqkktGIPVV--VLD---GGDSLEDTpeqIRLLGKVLGKEERAEELISFIESILADVEERTKD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496329379 246 VK--KRPMVFSGEI-RGGNWYAVGGKSFLAELFRDAGADYFLKDDPRSGGVTLDFETVYsqAESADYWRIVNSYDGTFTY 322
Cdd:cd01147 151 IPdeEKPTVYFGRIgTKGAAGLESGLAGSIEVFELAGGINVADGLGGGGLKEVSPEQIL--LWNPDVIFLDTGSFYLSLE 228
|
250 260
....*....|....*....|.
gi 496329379 323 DALKSlDPRYADFRAFREKGV 343
Cdd:cd01147 229 GYAKN-RPFWQSLKAVKNGRV 248
|
|
| FhuD |
cd01146 |
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ... |
146-279 |
3.90e-09 |
|
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial receptors in ABC transport of Fe3+-siderophores in many eubacterial species. They belong to the TroA-like superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA-like protein is comprised of two globular subdomains connected by a long alpha helix and binds its specific ligands in the cleft between these domains.
Pssm-ID: 238566 [Multi-domain] Cd Length: 256 Bit Score: 56.91 E-value: 3.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496329379 146 RLKSGETVKIGIEGNFDNEVIMSMNPDVIFISPF-KRGGYDAMREIgiplVPHLGYKEMTPLGQA-EWIKFIGMFIGQEV 223
Cdd:cd01146 41 ALPLEGVVDVGTRGQPNLEAIAALKPDLILGSASrHDEIYDQLSQI----APTVLLDSSPWLAEWkENLRLIAKALGKEE 116
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 496329379 224 EANEKFAAIEKRYNELKELAANVKKRPMVFSGEIRGGNWYAVGGKSFLAELFRDAG 279
Cdd:cd01146 117 EAEKLLAEYDQRLAELRQKLPDKGPKPVSVVRFSDAGSIRLYGPNSFAGSVLEDLG 172
|
|
| TroA_e |
cd01142 |
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ... |
122-380 |
1.18e-08 |
|
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial receptors in the ABC metal ion uptake in eubacteria and archaea. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.
Pssm-ID: 238562 [Multi-domain] Cd Length: 289 Bit Score: 55.82 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496329379 122 RLDACDYVVGITSTRHLFN--KEMNERLKSGETVKIGIEGNFdnEVIMSMNPDVIFI--SPFKRGGYDAMREIgiplvPH 197
Cdd:cd01142 40 ALGGGKLIVATTSTVQQEPwlYRLAPSLENVATGGTGNDVNI--EELLALKPDVVIVwsTDGKEAGKAVLRLL-----NA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496329379 198 LGYKEMTPLGQAEWIKFIGMFIGQEVEANEKFAAIEKRYNELKELAANVK--KRPMVFSGEIRGGNwyAVGGKSFLAELF 275
Cdd:cd01142 113 LSLRDAELEEVKLTIALLGELLGRQEKAEALVAYFDDNLAYVAARTKKLPdsERPRVYYAGPDPLT--TDGTGSITNSWI 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496329379 276 RDAGADYFLKDDPRSGGVTLDFETVYSqaesadyWR----IVNSYDgtfTYDALKSlDPRYADFRAFREKGVVYCNmrEK 351
Cdd:cd01142 191 DLAGGINVASEATKKGSGEVSLEQLLK-------WNpdviIVGNAD---TKAAILA-DPRWQNLRAVKNGRVYVNP--EG 257
|
250 260 270
....*....|....*....|....*....|
gi 496329379 352 PFYESMPMQPEIVLED-LIHAFHPDLLPDY 380
Cdd:cd01142 258 AFWWDRPSAEEALLGLwLAKTLYPERFTDD 287
|
|
| FatB |
cd01140 |
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ... |
123-300 |
7.88e-08 |
|
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type initial receptors in the siderophore-mediated iron uptake in some eubacterial species. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.
Pssm-ID: 238560 [Multi-domain] Cd Length: 270 Bit Score: 53.03 E-value: 7.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496329379 123 LDACDY----VVGITSTRHLFNKEmnERLKSGETVKIGIEGNFDNEVIMSMNPDVIFISPFKRGGYDAMREI------GI 192
Cdd:cd01140 23 LDTLDAlgvkVVGVPKSSTLPEYL--KKYKDDKYANVGTLFEPDLEAIAALKPDLIIIGGRLAEKYDELKKIaptidlGA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496329379 193 PLVPHL--GYKEMTPLGQaewiKFigmfiGQEVEANEKFAAIEKRYNELKELAANvKKRPMVFSgeIRGGNWYAVGGKSF 270
Cdd:cd01140 101 DLKNYLesVKQNIETLGK----IF-----GKEEEAKELVAEIDASIAEAKSAAKG-KKKALVVL--VNGGKLSAFGPGSR 168
|
170 180 190
....*....|....*....|....*....|.
gi 496329379 271 LAELFRDAGADYFLKDDPRSG-GVTLDFETV 300
Cdd:cd01140 169 FGWLHDLLGFEPADENIKASShGQPVSFEYI 199
|
|
| FecB |
COG4594 |
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ... |
1-330 |
1.43e-06 |
|
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443650 [Multi-domain] Cd Length: 316 Bit Score: 49.53 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496329379 1 MTRISAIGIALLCILCVTSCGLKSRQTTTESSSETGYSpVTTDTAATIVPcyakgytvkylphhvrlvdiHDPQK----E 76
Cdd:COG4594 1 MKKLLLLLILLLALLLLAACGSSSSDSSSSEAAAGART-VKHAMGETTIP--------------------GTPKRvvvlE 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496329379 77 SSSTfhYALVPKGIKPVGI--PSDYTVIETPVEhvmcmtslqlsnfirldacdyvvgitstrhlfnkemnERLKSGETVK 154
Cdd:COG4594 60 WSFA--DALLALGVTPVGIadDNDYDRWVPYLR-------------------------------------DLIKGVTSVG 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496329379 155 IGIEGNFdnEVIMSMNPDVIFISPFKRGG-YDAMREIG--IPLVP-HLGYKEMTplgqaEWIKFIGMFIGQEVEANEKFA 230
Cdd:COG4594 101 TRSQPNL--EAIAALKPDLIIADKSRHEAiYDQLSKIAptVLFKSrNGDYQENL-----ESFKTIAKALGKEEEAEAVLA 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496329379 231 AIEKRYNELKE-LAANVKKRPMVFsGEIRGGNWYAVGGKSFLAELFRDAGADYFLKDDP--RSGGVTLDFETVysQAESA 307
Cdd:COG4594 174 DHDQRIAEAKAkLAAADKGKKVAV-GQFRADGLRLYTPNSFAGSVLAALGFENPPKQSKdnGYGYSEVSLEQL--PALDP 250
|
330 340
....*....|....*....|...
gi 496329379 308 DyWRIVNSYDGTFTYDALKSlDP 330
Cdd:COG4594 251 D-VLFIATYDDPSILKEWKN-NP 271
|
|
| FeuA |
cd01138 |
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ... |
151-261 |
8.12e-03 |
|
Periplasmic binding protein FeuA. These proteins have predicted to function as initial receptors in ABC transport of metal ions in some eubacterial species. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.
Pssm-ID: 238558 [Multi-domain] Cd Length: 248 Bit Score: 37.70 E-value: 8.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496329379 151 ETVKIGIEGNFDNEVIMSMNPDVIFISPFKRGGYDAMREIGiPLVPhLGYKEMTPLGQaewIKFIGMFIGQEVEANEKFA 230
Cdd:cd01138 47 LAKVVGIVDEPNLEKVLELKPDLIIVSSKQEENYEKLSKIA-PTVP-VSYNSSDWEEQ---LKEIGKLLNKEDEAEKWLA 121
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 496329379 231 AIEKRYNELKELAAN------------VKKRPMVFSGEIRGGN 261
Cdd:cd01138 122 DYKQKAKEAKEKIKKklgndksvavlrGRKQIYVFGEDGRGGG 164
|
|
| |
