|
Name |
Accession |
Description |
Interval |
E-value |
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
114-358 |
5.31e-66 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 209.85 E-value: 5.31e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 114 MRIISLTPATTEILFALGLDKNIVAVT--TYCNYPP-EAENKEKIGSFSNPDIEKIFSLKPNIIFITG-QEQNKLNQKLK 189
Cdd:COG0614 1 MRIVSLSPSATELLLALGAGDRLVGVSdwGYCDYPElELKDLPVVGGTGEPNLEAILALKPDLVLASSsGNDEEDYEQLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 190 GLGLNTFQVDPKTIKEIIVSIRDIGEITNKKAEAKVLIKRISDRIDYYKNKTKKIIKKPRVFIEIYS-KPFMTVNKDTFI 268
Cdd:COG0614 81 KIGIPVVVLDPRSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGAEERPTVLYEIWSgDPLYTAGGGSFI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 269 NDIFDVIGCKNIFEDLTLSYSQISAESIVERNPEWIIVLSMQDS--------KDVLKR-GWGSVDAIRNKNIVdDINPDV 339
Cdd:COG0614 161 GELLELAGGRNVAADLGGGYPEVSLEQVLALDPDVIILSGGGYDaetaeealEALLADpGWQSLPAVKNGRVY-VVPGDL 239
|
250
....*....|....*....
gi 1085035289 340 FLRPGPRIIEGMDILYKVI 358
Cdd:COG0614 240 LSRPGPRLLLALEDLAKAL 258
|
|
| BtuF |
cd01144 |
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ... |
114-356 |
1.17e-63 |
|
Cobalamin binding protein BtuF. These proteins have been shown to function as initial receptors in ABC transport of vitamin B12 (cobalamin) in eubacterial and some archaeal species. 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: 238564 [Multi-domain] Cd Length: 245 Bit Score: 202.91 E-value: 1.17e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 114 MRIISLTPATTEILFALGLDKNIVAVTTYCNYPPEAENKEKIGSFSNPDIEKIFSLKPNII--FITGQEQNKLNQkLKGL 191
Cdd:cd01144 1 MRIVSLAPSATELLYALGLGDQLVGVTDYCDYPPEAKKLPRVGGFYQLDLERVLALKPDLViaWDDCNVCAVVDQ-LRAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 192 GLNTFQVDPKTIKEIIVSIRDIGEITNKKAEAKVLIKRISDRIDYYkNKTKKIIKKPRVFIEIYSKPFMTVNKDTfINDI 271
Cdd:cd01144 80 GIPVLVSEPQTLDDILADIRRLGTLAGRPARAEELAEALRRRLAAL-RKQYASKPPPRVFYQEWIDPLMTAGGDW-VPEL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 272 FDVIGCKNIFEDLTLSYSQISAESIVERNPEWIIVLSM---QDSKDVLKR-GWGSVDAIRNKNiVDDINPDVFLRPGPRI 347
Cdd:cd01144 158 IALAGGVNVFADAGERSPQVSWEDVLAANPDVIVLSPCgfgFTPAILRKEpAWQALPAVRNGR-VYAVDGNWYFRPSPRL 236
|
....*....
gi 1085035289 348 IEGMDILYK 356
Cdd:cd01144 237 VDGLEQLAA 245
|
|
| PRK03379 |
PRK03379 |
vitamin B12-transporter protein BtuF; Provisional |
99-348 |
4.01e-39 |
|
vitamin B12-transporter protein BtuF; Provisional
Pssm-ID: 179575 [Multi-domain] Cd Length: 260 Bit Score: 139.82 E-value: 4.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 99 LFLFLFINCLFAEKEMRIISLTPATTEILFALGLDKniVAVTTYCNYPPEAENKEKIGSFSNPDIEKIFSLKPNIIFI-- 176
Cdd:PRK03379 3 LVALLFLAPLWLNAAPRVITLSPANTELAFAAGITP--VGVSSYSDYPPQAKKIEQVATWQGMNLERIVALKPDLVLAwr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 177 TGQEQNKLNQkLKGLGLNTFQVDPKTIKEIIVSIRDIGEI--TNKKAE--AKVLIKRISDRIDYYKNKTKKiikkpRVFI 252
Cdd:PRK03379 81 GGNAERQVDQ-LASLGIKVMWVDATSIEQIANALRQLAPWspQPEKAEqaAQSLLQQYAALKAQYADKPKK-----RVFL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 253 EIYSKPFMTVNKDTFINDIFDVIGCKNIFEDLTLSYSQISAESIVERNPEWIIVLSMQDSKDVLKRGWGSVDAIRnkniV 332
Cdd:PRK03379 155 QFGTNPLFTSGKHSIQSQVLSLCGGENIFADSRVPWPQVSREQVLARKPQAIVITGGPDQIPKIKQFWGPQLKIP----V 230
|
250
....*....|....*.
gi 1085035289 333 DDINPDVFLRPGPRII 348
Cdd:PRK03379 231 IPLNSDWFERASPRII 246
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
117-333 |
1.99e-33 |
|
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: 124.02 E-value: 1.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 117 ISLTPATTEILFALGLDKNIVAVTTYCNYPPEAENKE---KIGSFSNPDIEKIFSLKPNIIFITGQEQNKLNQKLKGLGL 193
Cdd:pfam01497 1 AALSPAYTEILYALGATDSIVGVDAYTRDPLKADAVAaivKVGAYGEINVERLAALKPDLVILSTGYLTDEAEELLSLII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 194 NT-FQVDPKTIKEIIVSIRDIGEITNKKAEAKVLIKRISDRIDYYKNKTKKIIKKPR-VFIEIYSKPFMTVNKDTFINDI 271
Cdd:pfam01497 81 PTvIFESSSTGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPVlVFGGADGGGYVVAGSNTYIGDL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1085035289 272 FDVIGCKNIFEDLTLSYS-QISAESIVERNPEWIIVLSMQDSKDVLK------RGWGSVDAIRNKNIVD 333
Cdd:pfam01497 161 LRILGIENIAAELSGSEYaPISFEAILSSNPDVIIVSGRDSFTKTGPefvaanPLWAGLPAVKNGRVYT 229
|
|
| TroA_like |
NF038402 |
helical backbone metal receptor; |
115-307 |
1.63e-05 |
|
helical backbone metal receptor;
Pssm-ID: 439691 Cd Length: 219 Bit Score: 45.31 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 115 RIISLTPATTEILfALGLDKNIVAVTTYCNYPPEAEnKEKIGSFSNPDIEKIFSLKPNIIfITGQEQN-KLN-QKLKGLG 192
Cdd:NF038402 1 RVVSLVPSLTEAI-AATAPELLVGATDWCTHPADLD-VARVRGTKNPDRAAIAALRPDLV-VANQEENrELDvDRLRAAG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 193 LNTFQVDPKTIKEIIVSIR-------DIGEITNKKAEAKVLIKRISDRidyyknktkkiikKPRVFIEIYSKPFMTVNKD 265
Cdd:NF038402 78 VPVWVTRIETVDEALASLRrlftealGVPVPGWLDEAEREWAAPAPAP-------------RRRAVVPIWRDPWMVVGRD 144
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1085035289 266 TFINDIFDVIGCKNIFEDLTLSYSQISAESIVERNPEwIIVL 307
Cdd:NF038402 145 TFTGDLLARLGLRNVFADHPERYPHVDLDELDAAGPD-LVLL 185
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
114-358 |
5.31e-66 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 209.85 E-value: 5.31e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 114 MRIISLTPATTEILFALGLDKNIVAVT--TYCNYPP-EAENKEKIGSFSNPDIEKIFSLKPNIIFITG-QEQNKLNQKLK 189
Cdd:COG0614 1 MRIVSLSPSATELLLALGAGDRLVGVSdwGYCDYPElELKDLPVVGGTGEPNLEAILALKPDLVLASSsGNDEEDYEQLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 190 GLGLNTFQVDPKTIKEIIVSIRDIGEITNKKAEAKVLIKRISDRIDYYKNKTKKIIKKPRVFIEIYS-KPFMTVNKDTFI 268
Cdd:COG0614 81 KIGIPVVVLDPRSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGAEERPTVLYEIWSgDPLYTAGGGSFI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 269 NDIFDVIGCKNIFEDLTLSYSQISAESIVERNPEWIIVLSMQDS--------KDVLKR-GWGSVDAIRNKNIVdDINPDV 339
Cdd:COG0614 161 GELLELAGGRNVAADLGGGYPEVSLEQVLALDPDVIILSGGGYDaetaeealEALLADpGWQSLPAVKNGRVY-VVPGDL 239
|
250
....*....|....*....
gi 1085035289 340 FLRPGPRIIEGMDILYKVI 358
Cdd:COG0614 240 LSRPGPRLLLALEDLAKAL 258
|
|
| BtuF |
cd01144 |
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ... |
114-356 |
1.17e-63 |
|
Cobalamin binding protein BtuF. These proteins have been shown to function as initial receptors in ABC transport of vitamin B12 (cobalamin) in eubacterial and some archaeal species. 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: 238564 [Multi-domain] Cd Length: 245 Bit Score: 202.91 E-value: 1.17e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 114 MRIISLTPATTEILFALGLDKNIVAVTTYCNYPPEAENKEKIGSFSNPDIEKIFSLKPNII--FITGQEQNKLNQkLKGL 191
Cdd:cd01144 1 MRIVSLAPSATELLYALGLGDQLVGVTDYCDYPPEAKKLPRVGGFYQLDLERVLALKPDLViaWDDCNVCAVVDQ-LRAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 192 GLNTFQVDPKTIKEIIVSIRDIGEITNKKAEAKVLIKRISDRIDYYkNKTKKIIKKPRVFIEIYSKPFMTVNKDTfINDI 271
Cdd:cd01144 80 GIPVLVSEPQTLDDILADIRRLGTLAGRPARAEELAEALRRRLAAL-RKQYASKPPPRVFYQEWIDPLMTAGGDW-VPEL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 272 FDVIGCKNIFEDLTLSYSQISAESIVERNPEWIIVLSM---QDSKDVLKR-GWGSVDAIRNKNiVDDINPDVFLRPGPRI 347
Cdd:cd01144 158 IALAGGVNVFADAGERSPQVSWEDVLAANPDVIVLSPCgfgFTPAILRKEpAWQALPAVRNGR-VYAVDGNWYFRPSPRL 236
|
....*....
gi 1085035289 348 IEGMDILYK 356
Cdd:cd01144 237 VDGLEQLAA 245
|
|
| YvrC |
cd01143 |
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ... |
115-306 |
1.62e-59 |
|
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: 190.57 E-value: 1.62e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 115 RIISLTPATTEILFALGLDKNIVAVTTYCNYPPEAENKEKIGSFSNPDIEKIFSLKPNIIFITGQEQNKLNQKLKGLGLN 194
Cdd:cd01143 5 RIVSLSPSITEILFALGAGDKIVGVDTYSNYPKEVRKKPKVGSYSNPNVEKIVALKPDLVIVSSSSLAELLEKLKDAGIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 195 TFQV-DPKTIKEIIVSIRDIGEITNKKAEAKVLIKRISDRIDyYKNKTKKIIKKPRVFIEIYSKPFMTVNKDTFINDIFD 273
Cdd:cd01143 85 VVVLpAASSLDEIYDQIELIGKITGAEEEAEKLVKEMKQKID-KVKDKGKTIKKSKVYIEVSLGGPYTAGKNTFINELIR 163
|
170 180 190
....*....|....*....|....*....|...
gi 1085035289 274 VIGCKNIFEDlTLSYSQISAESIVERNPEWIIV 306
Cdd:cd01143 164 LAGAKNIAAD-SGGWPQVSPEEILKANPDVIIL 195
|
|
| ChuT |
COG4558 |
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ... |
94-363 |
3.45e-44 |
|
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443619 [Multi-domain] Cd Length: 285 Bit Score: 153.81 E-value: 3.45e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 94 KNLVILFLFLFINCLFA------EKEMRIISLTPATTEILFALGLDKNIVAVTTYCNYPPEAENKEKIGSFSNPDIEKIF 167
Cdd:COG4558 2 KRLALALLLLALAALAAgasvaaAAAERIVSLGGSVTEIVYALGAGDRLVGVDTTSTYPAAAKALPDVGYMRQLSAEGIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 168 SLKPNIIFITGQEQNK--LNQkLKGLGLNTFQVDPK-TIKEIIVSIRDIGEITNKKAEAKVLIKRISDRIDYYKNKTKKI 244
Cdd:COG4558 82 SLKPTLVLASEGAGPPevLDQ-LRAAGVPVVVVPAApSLEGVLAKIRAVAAALGVPEAGEALAARLEADLAALAARVAAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 245 IKKPRVFIeIYS---KPFMTVNKDTFINDIFDVIGCKNIFEDLTlSYSQISAESIVERNPEWIIVlsMQDSKDVLkrgwG 321
Cdd:COG4558 161 GKPPRVLF-LLSrggGRPMVAGRGTAADALIRLAGGVNAAAGFE-GYKPLSAEALIAAAPDVILV--MTRGLESL----G 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1085035289 322 SVDAI------------RNKNIVdDINPDVFLRPGPRIIEGMDILYKVIFEKSK 363
Cdd:COG4558 233 GVDGLlalpglaqtpagKNKRIV-AMDDLLLLGFGPRTPQAALALAQALYPAAA 285
|
|
| PRK03379 |
PRK03379 |
vitamin B12-transporter protein BtuF; Provisional |
99-348 |
4.01e-39 |
|
vitamin B12-transporter protein BtuF; Provisional
Pssm-ID: 179575 [Multi-domain] Cd Length: 260 Bit Score: 139.82 E-value: 4.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 99 LFLFLFINCLFAEKEMRIISLTPATTEILFALGLDKniVAVTTYCNYPPEAENKEKIGSFSNPDIEKIFSLKPNIIFI-- 176
Cdd:PRK03379 3 LVALLFLAPLWLNAAPRVITLSPANTELAFAAGITP--VGVSSYSDYPPQAKKIEQVATWQGMNLERIVALKPDLVLAwr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 177 TGQEQNKLNQkLKGLGLNTFQVDPKTIKEIIVSIRDIGEI--TNKKAE--AKVLIKRISDRIDYYKNKTKKiikkpRVFI 252
Cdd:PRK03379 81 GGNAERQVDQ-LASLGIKVMWVDATSIEQIANALRQLAPWspQPEKAEqaAQSLLQQYAALKAQYADKPKK-----RVFL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 253 EIYSKPFMTVNKDTFINDIFDVIGCKNIFEDLTLSYSQISAESIVERNPEWIIVLSMQDSKDVLKRGWGSVDAIRnkniV 332
Cdd:PRK03379 155 QFGTNPLFTSGKHSIQSQVLSLCGGENIFADSRVPWPQVSREQVLARKPQAIVITGGPDQIPKIKQFWGPQLKIP----V 230
|
250
....*....|....*.
gi 1085035289 333 DDINPDVFLRPGPRII 348
Cdd:PRK03379 231 IPLNSDWFERASPRII 246
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
117-333 |
1.99e-33 |
|
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: 124.02 E-value: 1.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 117 ISLTPATTEILFALGLDKNIVAVTTYCNYPPEAENKE---KIGSFSNPDIEKIFSLKPNIIFITGQEQNKLNQKLKGLGL 193
Cdd:pfam01497 1 AALSPAYTEILYALGATDSIVGVDAYTRDPLKADAVAaivKVGAYGEINVERLAALKPDLVILSTGYLTDEAEELLSLII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 194 NT-FQVDPKTIKEIIVSIRDIGEITNKKAEAKVLIKRISDRIDYYKNKTKKIIKKPR-VFIEIYSKPFMTVNKDTFINDI 271
Cdd:pfam01497 81 PTvIFESSSTGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPVlVFGGADGGGYVVAGSNTYIGDL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1085035289 272 FDVIGCKNIFEDLTLSYS-QISAESIVERNPEWIIVLSMQDSKDVLK------RGWGSVDAIRNKNIVD 333
Cdd:pfam01497 161 LRILGIENIAAELSGSEYaPISFEAILSSNPDVIIVSGRDSFTKTGPefvaanPLWAGLPAVKNGRVYT 229
|
|
| TroA_a |
cd01148 |
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ... |
109-350 |
3.76e-27 |
|
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors in ABC transport of metal ions in eubacteria. 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.
Pssm-ID: 238568 [Multi-domain] Cd Length: 284 Bit Score: 108.58 E-value: 3.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 109 FAEKEMRIISLTPATTEILFALGLDKNIVAvTTYCNYP--PEAENK-EKIGSFS--NPDIEKIFSLKPNIIFITGQEQNK 183
Cdd:cd01148 14 FDKAPQRVVSNDQNTTEMMLALGLQDRMVG-TAGIDNKdlPELKAKyDKVPELAkkYPSKETVLAARPDLVFGGWSYGFD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 184 LN-----QKLKGLGLNTF-------QVDPK-TIKEIIVSIRDIGEITNKKAEAKVLIKRISDRIDYYKNKTKKIIKKPRV 250
Cdd:cd01148 93 KGglgtpDSLAELGIKTYilpescgQRRGEaTLDDVYNDIRNLGKIFDVEDRADKLVADLKARLAEISAKVKGDGKKVAV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 251 FIEIYS--KPFmTVNKDTFINDIFDVIGCKNIFEDLTLSYSQISAESIVERNPEWIIVLSMQDSKDVLKR--------GW 320
Cdd:cd01148 173 FVYDSGedKPF-TSGRGGIPNAIITAAGGRNVFADVDESWTTVSWETVIARNPDVIVIIDYGDQNAAEQKikflkenpAL 251
|
250 260 270
....*....|....*....|....*....|
gi 1085035289 321 GSVDAIRNKNIVddINPDVFLRPGPRIIEG 350
Cdd:cd01148 252 KNVPAVKNNRFI--VLPLAEATPGIRNVDA 279
|
|
| TroA-like |
cd00636 |
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ... |
114-237 |
1.21e-25 |
|
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: 100.71 E-value: 1.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 114 MRIISLTPATTEILFALGLDKNIVAVTTYCNYPPEA----ENKEKIGSFSNPDIEKIFSLKPNIIFITGQEQNKLNQKLK 189
Cdd:cd00636 1 KRVVALDPGATELLLALGGDDKPVGVADPSGYPPEAkallEKVPDVGHGYEPNLEKIAALKPDLIIANGSGLEAWLDKLS 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1085035289 190 GLGLNTFQVDPK---TIKEIIVSIRDIGEITNKKAEAKVLIKRISDRIDYY 237
Cdd:cd00636 81 KIAIPVVVVDEAselSLENIKESIRLIGKALGKEENAEELIAELDARLAEL 131
|
|
| FatB |
cd01140 |
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ... |
115-333 |
3.18e-22 |
|
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: 94.63 E-value: 3.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 115 RIISLTPATTEILFALGLDknIVAVTTYCNYPP-----EAENKEKIGSFSNPDIEKIFSLKPNIIFITGQEQNKLNQKLK 189
Cdd:cd01140 14 KVVVFDVGALDTLDALGVK--VVGVPKSSTLPEylkkyKDDKYANVGTLFEPDLEAIAALKPDLIIIGGRLAEKYDELKK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 190 GLGLNTFQVDPK-TIKEIIVSIRDIGEITNKKAEAKVLIKRISDRIDyykNKTKKIIKKPRVFIEIYSKP-FMTVNKDTF 267
Cdd:cd01140 92 IAPTIDLGADLKnYLESVKQNIETLGKIFGKEEEAKELVAEIDASIA---EAKSAAKGKKKALVVLVNGGkLSAFGPGSR 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1085035289 268 INDIFDVIGCKNIFEDLTLS--YSQISAESIVERNPEWIIVLSM--------QDSKDVLKRG-WGSVDAIRNKNIVD 333
Cdd:cd01140 169 FGWLHDLLGFEPADENIKASshGQPVSFEYILEANPDWLFVIDRgaaigaegSSAKEVLDNDlVKNTTAWKNGKVIY 245
|
|
| TroA_e |
cd01142 |
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ... |
115-355 |
9.61e-22 |
|
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: 93.57 E-value: 9.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 115 RIISLTPATTEILFALGLDKNIVAVTTYC-NYP------PEAENKEKIGSFSNPDIEKIFSLKPNIIFITGQEQNKLNQK 187
Cdd:cd01142 26 RIAALWGAGNAVVAALGGGKLIVATTSTVqQEPwlyrlaPSLENVATGGTGNDVNIEELLALKPDVVIVWSTDGKEAGKA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 188 LKGLgLNTFQVDPKTIKEIIVSIRDIGEITNKKAEAKVLIKRISDRIDYYKNKTKKIIKK--PRVFIEiYSKPFMTVNKD 265
Cdd:cd01142 106 VLRL-LNALSLRDAELEEVKLTIALLGELLGRQEKAEALVAYFDDNLAYVAARTKKLPDSerPRVYYA-GPDPLTTDGTG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 266 TFINDIFDVIGCKNIFEDLTLSYS-QISAESIVERNPEWIIVLSMQDSKDVL--KRgWGSVDAIRNKNIVddINPD-VFL 341
Cdd:cd01142 184 SITNSWIDLAGGINVASEATKKGSgEVSLEQLLKWNPDVIIVGNADTKAAILadPR-WQNLRAVKNGRVY--VNPEgAFW 260
|
250
....*....|....
gi 1085035289 342 RPGPRIIEGMDILY 355
Cdd:cd01142 261 WDRPSAEEALLGLW 274
|
|
| HutB |
cd01149 |
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ... |
115-332 |
9.30e-20 |
|
Hemin binding protein HutB. These proteins have been shown to function as initial receptors in ABC transport of hemin and hemoproteins in many 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 the metal ion in the cleft between these domains.
Pssm-ID: 238569 [Multi-domain] Cd Length: 235 Bit Score: 86.94 E-value: 9.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 115 RIISLTPATTEILFALGLDKNIVAVTTYCNYPPEAENKEKIGSFSNPDIEKIFSLKPNIIFITGQEQNK--LNQkLKGLG 192
Cdd:cd01149 3 RIVSLGGSVTEIVYALGAGDRLVGVDSTSTYPEAAAKLPDVGYMRQLSAEGVLSLKPTLVIASDEAGPPeaLDQ-LRAAG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 193 LNTFQVDPKTIKEIIVS-IRDIGEITNKKAEAKVLIKRISDRIDYYKNKTKKIIKKPRVFIeIYSK---PFMTVNKDTFI 268
Cdd:cd01149 82 VPVVTVPSTPTLDGLLTkIRQVAQALGVPEKGEALAQEVRQRLAALRKTVAAHKKPPRVLF-LLSHgggAAMAAGRNTAA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1085035289 269 NDIFDVIGCKNIFEDLTlSYSQISAESIVERNPEWIIVLSMQDSKDvlkrgwGSVDAI------------RNKNIV 332
Cdd:cd01149 161 DAIIALAGAVNAAAGFR-GYKPLSAEALIAAQPDVILVMSRGLDAV------GGVDGLlklpglaqtpagRNKRIL 229
|
|
| FhuD |
cd01146 |
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ... |
115-345 |
2.39e-17 |
|
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: 80.79 E-value: 2.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 115 RIISLTPATTEILFALGLDknIVAVTTYCNYPPEAENK-------EKIGSFSNPDIEKIFSLKPNIIFITGQEQNKLNQK 187
Cdd:cd01146 5 RIVALDWGALETLLALGVK--PVGVADTAGYKPWIPEPalplegvVDVGTRGQPNLEAIAALKPDLILGSASRHDEIYDQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 188 LKG----LGLNTFQVDPKTIKeiivSIRDIGEITNKKAEAKVLIKRISDRIDYYKNKTKKIIKKPRVFIEIYSKPFMTV- 262
Cdd:cd01146 83 LSQiaptVLLDSSPWLAEWKE----NLRLIAKALGKEEEAEKLLAEYDQRLAELRQKLPDKGPKPVSVVRFSDAGSIRLy 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 263 NKDTFINDIFDVIGCKNIFEDLTLS---YSQISAESIVERNPEWIIVLSMQDSKDVLK----RGWGSVDAIRNKNIVdDI 335
Cdd:cd01146 159 GPNSFAGSVLEDLGLQNPWAQETTNdsgFATISLERLAKADADVLFVFTYEDEELAQAlqanPLWQNLPAVKNGRVY-VV 237
|
250
....*....|
gi 1085035289 336 NPDVFLRPGP 345
Cdd:cd01146 238 DDVWWFFGGG 247
|
|
| HemV-2 |
cd01147 |
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ... |
115-335 |
1.40e-15 |
|
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: 75.83 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 115 RIISLTPATTEILFALGLDKNIVAV---------TTYCNYPPEAENKEKIGSF---SNPDIEKIFSLKPNIIFITG---- 178
Cdd:cd01147 7 RVVAAGPGALRLLYALAAPDKIVGVddaeksdegRPYFLASPELKDLPVIGRGgrgNTPNYEKIAALKPDVVIDVGsddp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 179 QEQNKLNQKLKG---LGLNTfqvdPKTIKEIIVSIRDIGEITNKKAEAKVLI-------KRISDRIDyyknkTKKIIKKP 248
Cdd:cd01147 87 TSIADDLQKKTGipvVVLDG----GDSLEDTPEQIRLLGKVLGKEERAEELIsfiesilADVEERTK-----DIPDEEKP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 249 RVFIEiyskPFMTVNKDTFIND------IFDVIGCKNIFEDLTLSYS-QISAESIVERNPEwIIVLSMQDSKDVLKR--- 318
Cdd:cd01147 158 TVYFG----RIGTKGAAGLESGlagsieVFELAGGINVADGLGGGGLkEVSPEQILLWNPD-VIFLDTGSFYLSLEGyak 232
|
250 260
....*....|....*....|
gi 1085035289 319 ---GWGSVDAIRNKNIVDDI 335
Cdd:cd01147 233 nrpFWQSLKAVKNGRVYLLP 252
|
|
| btuF |
PRK09534 |
corrinoid ABC transporter substrate-binding protein; Reviewed |
111-351 |
1.40e-13 |
|
corrinoid ABC transporter substrate-binding protein; Reviewed
Pssm-ID: 236552 [Multi-domain] Cd Length: 359 Bit Score: 71.09 E-value: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 111 EKEMRIISLTPATTEILFALGLDKNIVAVTTYCNYPPEAENKEKI--GSFSNPDIEKIFSLKPNIIFITGQEQNKLNQKL 188
Cdd:PRK09534 58 ERPERVVTLNPSAAQTMWELGARDRVVGVTQYASYLDGAEERTNVsgGQPFGVNVEAVVGLDPDLVLAPNAVAGDTVTRL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 189 KGLGLNTFQVDPKT-IKEIIVSIRDIGEITNKKAEAKVLIKRISDRIDYYKNKTKKIIKKPRVFIeiyskPF---MTVNK 264
Cdd:PRK09534 138 REAGITVFHFPAATsIEDVAEKTATIGRLTGNCEAAAETNAEMRDRVDAVEDRTADVDDRPRVLY-----PLgdgYTAGG 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 265 DTFINDIFDVIGCKNIFEDLTLS-YSQISAESIVERNPEWIIVLSmqDSKDVLKRG-WGSVDAIRNKNIV----DDINpd 338
Cdd:PRK09534 213 NTFIGALIEAAGGHNVAADATTDgYPQLSEEVIVQQDPDVIVVAT--ASALVAETEpYASTTAGETGNVVtvnvNHIN-- 288
|
250
....*....|...
gi 1085035289 339 vflRPGPRIIEGM 351
Cdd:PRK09534 289 ---QPAPRIVESM 298
|
|
| CeuA |
COG4607 |
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and ... |
115-332 |
2.12e-12 |
|
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443657 [Multi-domain] Cd Length: 310 Bit Score: 67.13 E-value: 2.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 115 RIISLTPATTEILFALGLDknIVAVTTYcNYPP-----EAENKEKIGSFSNPDIEKIFSLKPNIIFItGQEQNKLNQKLK 189
Cdd:COG4607 53 RVVVFDNGALDTLDALGVE--VAGVPKG-LLPDylskyADDKYANVGTLFEPDLEAIAALKPDLIII-GGRSAKKYDELS 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 190 GLG--LNtFQVDPK-TIKEIIVSIRDIGEITNKKAEAKVLIKRISDRIDyykNKTKKIIKKPRVFIEIYSKPFMTV--NK 264
Cdd:COG4607 129 KIAptID-LTVDGEdYLESLKRNTETLGEIFGKEDEAEELVADLDAKIA---ALKAAAAGKGTALIVLTNGGKISAygPG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 265 DTF-IndIFDVIGCKNIFEDLTLSY--SQISAESIVERNPEWIIVL--------SMQDSKDVLK----RGwgsVDAIRNK 329
Cdd:COG4607 205 SRFgP--IHDVLGFKPADEDIEASThgQAISFEFIAEANPDWLFVIdrdaaiggEGPAAKQVLDnelvKQ---TTAWKNG 279
|
...
gi 1085035289 330 NIV 332
Cdd:COG4607 280 QIV 282
|
|
| FecB |
COG4594 |
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ... |
115-342 |
1.33e-11 |
|
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443650 [Multi-domain] Cd Length: 316 Bit Score: 64.56 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 115 RIISLTPATTEILFALGLDKniVAVTTYCNYPP-------EAENKEKIGSFSNPDIEKIFSLKPNIIFITGQEQNKLNQK 187
Cdd:COG4594 54 RVVVLEWSFADALLALGVTP--VGIADDNDYDRwvpylrdLIKGVTSVGTRSQPNLEAIAALKPDLIIADKSRHEAIYDQ 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 188 LKG----LGLNTFqvdPKTIKEIIVSIRDIGEITNKKAEAKVLIKRISDRI-DYYKNKTKKIIKKPRVFIEIYSKPFMTV 262
Cdd:COG4594 132 LSKiaptVLFKSR---NGDYQENLESFKTIAKALGKEEEAEAVLADHDQRIaEAKAKLAAADKGKKVAVGQFRADGLRLY 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 263 NKDTFINDIFDVIGCKNIFEDLTL---SYSQISAESIVERNPEWIIVlsMQDSKDVLKRG------WGSVDAIRNKNiVD 333
Cdd:COG4594 209 TPNSFAGSVLAALGFENPPKQSKDngyGYSEVSLEQLPALDPDVLFI--ATYDDPSILKEwknnplWKNLKAVKNGR-VY 285
|
....*....
gi 1085035289 334 DINPDVFLR 342
Cdd:COG4594 286 EVDGDLWTR 294
|
|
| TroA_f |
cd01139 |
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ... |
147-331 |
2.74e-10 |
|
Periplasmic binding protein TroA_f. 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: 238559 [Multi-domain] Cd Length: 342 Bit Score: 60.78 E-value: 2.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 147 PEAENKEKIGSFSNPD--IEKIFSLKPNIIFI-----TGQEQNKLNQKLKGLGLNTFQVD--PKTIKEIIVSIRDIGEIT 217
Cdd:cd01139 66 PEIADIPLIGSTYNGDfsVEKVLTLKPDLVILniwakTTAEESGILEKLEQAGIPVVFVDfrQKPLKNTTPSMRLLGKAL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 218 NKKAEAKVLIKRISDRID-YYKNKTKKIIKKPRVFIE---IYSKPFMTVNKDTFINDIFDVIGCKNIFEDL-TLSYSQIS 292
Cdd:cd01139 146 GREERAEEFIEFYQERIDrIRDRLAKINEPKPKVFIElgaGGPEECCSTYGNGNWGELVDAAGGDNIADGLiPGTSGELN 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1085035289 293 AESIVERNPEWIIVLSMQDSKDV----------------------LKR-GWGSVDAIRNKNI 331
Cdd:cd01139 226 AEYVIAANPEIIIATGGNWAKDPsgvslgpdgttadakesllralLKRpGWSSLQAVKNGRV 287
|
|
| TroA_d |
cd01141 |
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ... |
115-224 |
1.33e-09 |
|
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: 57.05 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 115 RIISLTPATTEILFALGLDKNIVAVTTYCN--YPPEAENK--EKIGSFSNPDIEKIFSLKPNIIFI--TGQEQNKLnQKL 188
Cdd:cd01141 10 RIVVLSPTHVDLLLALDKADKIVGVSASAYdlNTPAVKERidIQVGPTGSLNVELIVALKPDLVILygGFQAQTIL-DKL 88
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1085035289 189 KGLGLNTFQV----DPKTIKEIIVSirdIGEITNKKAEAK 224
Cdd:cd01141 89 EQLGIPVLYVneypSPLGRAEWIKF---AAAFYGVGKEDK 125
|
|
| TroA_like |
NF038402 |
helical backbone metal receptor; |
115-307 |
1.63e-05 |
|
helical backbone metal receptor;
Pssm-ID: 439691 Cd Length: 219 Bit Score: 45.31 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 115 RIISLTPATTEILfALGLDKNIVAVTTYCNYPPEAEnKEKIGSFSNPDIEKIFSLKPNIIfITGQEQN-KLN-QKLKGLG 192
Cdd:NF038402 1 RVVSLVPSLTEAI-AATAPELLVGATDWCTHPADLD-VARVRGTKNPDRAAIAALRPDLV-VANQEENrELDvDRLRAAG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 193 LNTFQVDPKTIKEIIVSIR-------DIGEITNKKAEAKVLIKRISDRidyyknktkkiikKPRVFIEIYSKPFMTVNKD 265
Cdd:NF038402 78 VPVWVTRIETVDEALASLRrlftealGVPVPGWLDEAEREWAAPAPAP-------------RRRAVVPIWRDPWMVVGRD 144
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1085035289 266 TFINDIFDVIGCKNIFEDLTLSYSQISAESIVERNPEwIIVL 307
Cdd:NF038402 145 TFTGDLLARLGLRNVFADHPERYPHVDLDELDAAGPD-LVLL 185
|
|
| FeuA |
cd01138 |
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ... |
115-331 |
2.02e-05 |
|
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: 45.40 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 115 RIISLTpATTEILFALGLdkNIVAVTTYCNYPPEAENKEKIGSF---SNPDIEKIFSLKPNIIfITGQEQNKLNQKLKGL 191
Cdd:cd01138 11 RIVALS-GETEGLALLGI--KPVGAASIGGKNPYYKKKTLAKVVgivDEPNLEKVLELKPDLI-IVSSKQEENYEKLSKI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 192 G----LNTFQVDPKtikeiiVSIRDIGEITNKKAEAKVLIKrisdriDYYKNKTKKIIKKPRVFIEIYSKPFMTVNKDTF 267
Cdd:cd01138 87 AptvpVSYNSSDWE------EQLKEIGKLLNKEDEAEKWLA------DYKQKAKEAKEKIKKKLGNDKSVAVLRGRKQIY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085035289 268 INDIFDVIGCKNIFEDLTL-------------SYSQISAESIVERNPEWIIVLSMQDSKDV----LKRGWGSVDAIRNKN 330
Cdd:cd01138 155 VFGEDGRGGGPILYADLGLkapekvkeiedkpGYAAISLEVLPEFDADYIFLLFFTGPEAKadfeSLPIWKNLPAVKNNH 234
|
.
gi 1085035289 331 I 331
Cdd:cd01138 235 V 235
|
|
| |
