|
Name |
Accession |
Description |
Interval |
E-value |
| PRK03379 |
PRK03379 |
vitamin B12-transporter protein BtuF; Provisional |
7-266 |
0e+00 |
|
vitamin B12-transporter protein BtuF; Provisional
Pssm-ID: 179575 [Multi-domain] Cd Length: 260 Bit Score: 506.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 7 RALVALSFLAPLWLNAAPRVITLSPANTELAFAAGITPVGVSSYSDYPPQAQKIEQVSTWQGMNLERIVALKPDLVIAWR 86
Cdd:PRK03379 1 RALVALLFLAPLWLNAAPRVITLSPANTELAFAAGITPVGVSSYSDYPPQAKKIEQVATWQGMNLERIVALKPDLVLAWR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 87 GGNAERQVDQLASLGIKVMWVDATSIEQIANALRQLAPWSPQPDKAEQAAQSLLDQYAQLKAQYADKPKKRVFLQFGINP 166
Cdd:PRK03379 81 GGNAERQVDQLASLGIKVMWVDATSIEQIANALRQLAPWSPQPEKAEQAAQSLLQQYAALKAQYADKPKKRVFLQFGTNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 167 PFTSGKESIQNQVLEVCGGENIFKDSRVPWPQVSREQVLARSPQAIVITGGPDQIPKIKQYWGEQLKIPVIPLTSDWFER 246
Cdd:PRK03379 161 LFTSGKHSIQSQVLSLCGGENIFADSRVPWPQVSREQVLARKPQAIVITGGPDQIPKIKQFWGPQLKIPVIPLNSDWFER 240
|
250 260
....*....|....*....|
gi 16128151 247 ASPRIILAAQQLCNALSQVD 266
Cdd:PRK03379 241 ASPRIILAAQQLCNALSQVD 260
|
|
| BtuF |
cd01144 |
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ... |
25-260 |
1.54e-84 |
|
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: 252.61 E-value: 1.54e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 25 RVITLSPANTELAFAAGI--TPVGVSSYSDYPPQAQKIEQVSTWQGMNLERIVALKPDLVIAWRGGNAERQVDQLASLGI 102
Cdd:cd01144 2 RIVSLAPSATELLYALGLgdQLVGVTDYCDYPPEAKKLPRVGGFYQLDLERVLALKPDLVIAWDDCNVCAVVDQLRAAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 103 KVMWVDATSIEQIANALRQLAPWSPQPDKAEQAAQSLLDQYAQLKAQYADKPKKRVFLQFGINPPFTSGKEsIQNQVLEV 182
Cdd:cd01144 82 PVLVSEPQTLDDILADIRRLGTLAGRPARAEELAEALRRRLAALRKQYASKPPPRVFYQEWIDPLMTAGGD-WVPELIAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 183 CGGENIFKDSRVPWPQVSREQVLARSPQAIVITGGP----DQIPKIKQYWGEQ---LKIPVIPLTSDWFERASPRIILAA 255
Cdd:cd01144 161 AGGVNVFADAGERSPQVSWEDVLAANPDVIVLSPCGfgftPAILRKEPAWQALpavRNGRVYAVDGNWYFRPSPRLVDGL 240
|
....*
gi 16128151 256 QQLCN 260
Cdd:cd01144 241 EQLAA 245
|
|
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
25-262 |
9.04e-63 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 197.91 E-value: 9.04e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 25 RVITLSPANTELAFAAGITP--VGVSS--YSDYPP-QAQKIEQVSTWQGMNLERIVALKPDLVIAWRGGNAERQVDQLAS 99
Cdd:COG0614 2 RIVSLSPSATELLLALGAGDrlVGVSDwgYCDYPElELKDLPVVGGTGEPNLEAILALKPDLVLASSSGNDEEDYEQLEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 100 LGIKVMWVDATSIEQIANALRQLAPWSPQPDKAEQAAQSLLDQYAQLKAQYAD-KPKKRVFLQFGI-NPPFTSGKESIQN 177
Cdd:COG0614 82 IGIPVVVLDPRSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGaEERPTVLYEIWSgDPLYTAGGGSFIG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 178 QVLEVCGGENIFKDSRVPWPQVSREQVLARSPQAIVITGGPDQIPKIKQYWGEQLKIP------------VIPLTSDWFE 245
Cdd:COG0614 162 ELLELAGGRNVAADLGGGYPEVSLEQVLALDPDVIILSGGGYDAETAEEALEALLADPgwqslpavkngrVYVVPGDLLS 241
|
250
....*....|....*..
gi 16128151 246 RASPRIILAAQQLCNAL 262
Cdd:COG0614 242 RPGPRLLLALEDLAKAL 258
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
27-226 |
3.10e-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: 78.18 E-value: 3.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 27 ITLSPANTELAFAAGITP--VGVSSYSDYPPQAQKIEQ---VSTWQGMNLERIVALKPDLVIAWRGGNAERQvDQLASLG 101
Cdd:pfam01497 1 AALSPAYTEILYALGATDsiVGVDAYTRDPLKADAVAAivkVGAYGEINVERLAALKPDLVILSTGYLTDEA-EELLSLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 102 IKVMWVDATS-IEQIANALRQLAPWSPQPDKAEQAAQSLLDQYAQLKAQYADKPKKRVFLQFGIN--PPFTSGKESIQNQ 178
Cdd:pfam01497 80 IPTVIFESSStGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPVLVFGGADggGYVVAGSNTYIGD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16128151 179 VLEVCGGENIFKD-SRVPWPQVSREQVLARSPQAIVITGGPDQIPKIKQ 226
Cdd:pfam01497 160 LLRILGIENIAAElSGSEYAPISFEAILSSNPDVIIVSGRDSFTKTGPE 208
|
|
| TroA_like |
NF038402 |
helical backbone metal receptor; |
25-220 |
6.86e-07 |
|
helical backbone metal receptor;
Pssm-ID: 439691 Cd Length: 219 Bit Score: 48.77 E-value: 6.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 25 RVITLSPANTE-LAFAAGITPVGVSSYSDYPPQAQkIEQVSTWQGMNLERIVALKPDLVIAWRGGNAERQVDQLASLGIK 103
Cdd:NF038402 1 RVVSLVPSLTEaIAATAPELLVGATDWCTHPADLD-VARVRGTKNPDRAAIAALRPDLVVANQEENRELDVDRLRAAGVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 104 VmWVdaTSIEQIANALRQL------APWSPQPDkaeqaaqsLLDQYAQLKAQYADKPKKRVFLQFGINPPFTSGKESIQN 177
Cdd:NF038402 80 V-WV--TRIETVDEALASLrrlfteALGVPVPG--------WLDEAEREWAAPAPAPRRRAVVPIWRDPWMVVGRDTFTG 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 16128151 178 QVLEVCGGENIFKDSRVPWPQVSREQVLARSPQAIVItggPDQ 220
Cdd:NF038402 149 DLLARLGLRNVFADHPERYPHVDLDELDAAGPDLVLL---PDE 188
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK03379 |
PRK03379 |
vitamin B12-transporter protein BtuF; Provisional |
7-266 |
0e+00 |
|
vitamin B12-transporter protein BtuF; Provisional
Pssm-ID: 179575 [Multi-domain] Cd Length: 260 Bit Score: 506.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 7 RALVALSFLAPLWLNAAPRVITLSPANTELAFAAGITPVGVSSYSDYPPQAQKIEQVSTWQGMNLERIVALKPDLVIAWR 86
Cdd:PRK03379 1 RALVALLFLAPLWLNAAPRVITLSPANTELAFAAGITPVGVSSYSDYPPQAKKIEQVATWQGMNLERIVALKPDLVLAWR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 87 GGNAERQVDQLASLGIKVMWVDATSIEQIANALRQLAPWSPQPDKAEQAAQSLLDQYAQLKAQYADKPKKRVFLQFGINP 166
Cdd:PRK03379 81 GGNAERQVDQLASLGIKVMWVDATSIEQIANALRQLAPWSPQPEKAEQAAQSLLQQYAALKAQYADKPKKRVFLQFGTNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 167 PFTSGKESIQNQVLEVCGGENIFKDSRVPWPQVSREQVLARSPQAIVITGGPDQIPKIKQYWGEQLKIPVIPLTSDWFER 246
Cdd:PRK03379 161 LFTSGKHSIQSQVLSLCGGENIFADSRVPWPQVSREQVLARKPQAIVITGGPDQIPKIKQFWGPQLKIPVIPLNSDWFER 240
|
250 260
....*....|....*....|
gi 16128151 247 ASPRIILAAQQLCNALSQVD 266
Cdd:PRK03379 241 ASPRIILAAQQLCNALSQVD 260
|
|
| BtuF |
cd01144 |
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ... |
25-260 |
1.54e-84 |
|
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: 252.61 E-value: 1.54e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 25 RVITLSPANTELAFAAGI--TPVGVSSYSDYPPQAQKIEQVSTWQGMNLERIVALKPDLVIAWRGGNAERQVDQLASLGI 102
Cdd:cd01144 2 RIVSLAPSATELLYALGLgdQLVGVTDYCDYPPEAKKLPRVGGFYQLDLERVLALKPDLVIAWDDCNVCAVVDQLRAAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 103 KVMWVDATSIEQIANALRQLAPWSPQPDKAEQAAQSLLDQYAQLKAQYADKPKKRVFLQFGINPPFTSGKEsIQNQVLEV 182
Cdd:cd01144 82 PVLVSEPQTLDDILADIRRLGTLAGRPARAEELAEALRRRLAALRKQYASKPPPRVFYQEWIDPLMTAGGD-WVPELIAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 183 CGGENIFKDSRVPWPQVSREQVLARSPQAIVITGGP----DQIPKIKQYWGEQ---LKIPVIPLTSDWFERASPRIILAA 255
Cdd:cd01144 161 AGGVNVFADAGERSPQVSWEDVLAANPDVIVLSPCGfgftPAILRKEPAWQALpavRNGRVYAVDGNWYFRPSPRLVDGL 240
|
....*
gi 16128151 256 QQLCN 260
Cdd:cd01144 241 EQLAA 245
|
|
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
25-262 |
9.04e-63 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 197.91 E-value: 9.04e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 25 RVITLSPANTELAFAAGITP--VGVSS--YSDYPP-QAQKIEQVSTWQGMNLERIVALKPDLVIAWRGGNAERQVDQLAS 99
Cdd:COG0614 2 RIVSLSPSATELLLALGAGDrlVGVSDwgYCDYPElELKDLPVVGGTGEPNLEAILALKPDLVLASSSGNDEEDYEQLEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 100 LGIKVMWVDATSIEQIANALRQLAPWSPQPDKAEQAAQSLLDQYAQLKAQYAD-KPKKRVFLQFGI-NPPFTSGKESIQN 177
Cdd:COG0614 82 IGIPVVVLDPRSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGaEERPTVLYEIWSgDPLYTAGGGSFIG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 178 QVLEVCGGENIFKDSRVPWPQVSREQVLARSPQAIVITGGPDQIPKIKQYWGEQLKIP------------VIPLTSDWFE 245
Cdd:COG0614 162 ELLELAGGRNVAADLGGGYPEVSLEQVLALDPDVIILSGGGYDAETAEEALEALLADPgwqslpavkngrVYVVPGDLLS 241
|
250
....*....|....*..
gi 16128151 246 RASPRIILAAQQLCNAL 262
Cdd:COG0614 242 RPGPRLLLALEDLAKAL 258
|
|
| YvrC |
cd01143 |
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ... |
25-213 |
9.17e-41 |
|
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: 139.34 E-value: 9.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 25 RVITLSPANTELAFA--AGITPVGVSSYSDYPPQAQKIEQVSTWQGMNLERIVALKPDLVIAwRGGNAERQVDQLASLGI 102
Cdd:cd01143 5 RIVSLSPSITEILFAlgAGDKIVGVDTYSNYPKEVRKKPKVGSYSNPNVEKIVALKPDLVIV-SSSSLAELLEKLKDAGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 103 KVMWV-DATSIEQIANALRQLAPWSPQPDKAEQAAQSLLDQYAQLKAQYADKPKKRVFLQFGINPPFTSGKESIQNQVLE 181
Cdd:cd01143 84 PVVVLpAASSLDEIYDQIELIGKITGAEEEAEKLVKEMKQKIDKVKDKGKTIKKSKVYIEVSLGGPYTAGKNTFINELIR 163
|
170 180 190
....*....|....*....|....*....|..
gi 16128151 182 VCGGENIFKDSrVPWPQVSREQVLARSPQAIV 213
Cdd:cd01143 164 LAGAKNIAADS-GGWPQVSPEEILKANPDVII 194
|
|
| ChuT |
COG4558 |
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ... |
8-264 |
5.13e-37 |
|
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443619 [Multi-domain] Cd Length: 285 Bit Score: 132.24 E-value: 5.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 8 ALVALSFLAPLWLNAAPRVITLSPANTELAFA--AGITPVGVSSYSDYPPQAQKIEQVSTWQGMNLERIVALKPDLVIAW 85
Cdd:COG4558 12 ALAALAAGASVAAAAAERIVSLGGSVTEIVYAlgAGDRLVGVDTTSTYPAAAKALPDVGYMRQLSAEGILSLKPTLVLAS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 86 RGGNAERQVDQLASLGIKVMWVD-ATSIEQIANALRQLAPWSPQPDKAEQAAQSLLDQYAQLKAQYADKP-KKRVF--LQ 161
Cdd:COG4558 92 EGAGPPEVLDQLRAAGVPVVVVPaAPSLEGVLAKIRAVAAALGVPEAGEALAARLEADLAALAARVAAIGkPPRVLflLS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 162 FGINPPFTSGKESIQNQVLEVCGGENIFKDSRvPWPQVSREQVLARSPQAIVIT-------GGPDQIpkikqywgeqLKI 234
Cdd:COG4558 172 RGGGRPMVAGRGTAADALIRLAGGVNAAAGFE-GYKPLSAEALIAAAPDVILVMtrgleslGGVDGL----------LAL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 16128151 235 PVIPLTSDWFERA------------SPRIILAAQQLCNALSQ 264
Cdd:COG4558 241 PGLAQTPAGKNKRivamddllllgfGPRTPQAALALAQALYP 282
|
|
| HutB |
cd01149 |
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ... |
23-215 |
5.87e-25 |
|
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: 99.26 E-value: 5.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 23 APRVITLSPANTELAFA--AGITPVGVSSYSDYPPQAQKIEQVSTWQGMNLERIVALKPDLVIAWRGGNAERQVDQLASL 100
Cdd:cd01149 1 PERIVSLGGSVTEIVYAlgAGDRLVGVDSTSTYPEAAAKLPDVGYMRQLSAEGVLSLKPTLVIASDEAGPPEALDQLRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 101 GIKVMWVDAT-SIEQIANALRQLAPWSPQPDKAEQAAQSLLDQYAQLKAQYAD--KPKKRVF-LQFGINPPFTSGKESIQ 176
Cdd:cd01149 81 GVPVVTVPSTpTLDGLLTKIRQVAQALGVPEKGEALAQEVRQRLAALRKTVAAhkKPPRVLFlLSHGGGAAMAAGRNTAA 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 16128151 177 NQVLEVCGGENIFKDSRvPWPQVSREQVLARSPQAIVIT 215
Cdd:cd01149 161 DAIIALAGAVNAAAGFR-GYKPLSAEALIAAQPDVILVM 198
|
|
| TroA-like |
cd00636 |
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ... |
24-163 |
1.46e-24 |
|
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: 95.70 E-value: 1.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 24 PRVITLSPANTELAFAAG--ITPVGVSSYSDYPPQAQ----KIEQVSTWQGMNLERIVALKPDLVIAWrGGNAERQVDQL 97
Cdd:cd00636 1 KRVVALDPGATELLLALGgdDKPVGVADPSGYPPEAKalleKVPDVGHGYEPNLEKIAALKPDLIIAN-GSGLEAWLDKL 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128151 98 ASLGIKVMWVD---ATSIEQIANALRQLAPWSPQPDKAEQAAQSLLDQYAQLKAQYADKPKKRVFLQFG 163
Cdd:cd00636 80 SKIAIPVVVVDeasELSLENIKESIRLIGKALGKEENAEELIAELDARLAELRAKLAKIPKKKVSLVVG 148
|
|
| TroA_a |
cd01148 |
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ... |
22-220 |
4.54e-23 |
|
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: 95.10 E-value: 4.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 22 AAP-RVITLSPANTELAFAAGITP--VGVS--SYSDYPP---QAQKIEQVSTWQgMNLERIVALKPDLVIAWRG-GNAE- 91
Cdd:cd01148 16 KAPqRVVSNDQNTTEMMLALGLQDrmVGTAgiDNKDLPElkaKYDKVPELAKKY-PSKETVLAARPDLVFGGWSyGFDKg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 92 --RQVDQLASLGIKV--------MWVDATSIEQIANALRQLAPWSPQPDKAEQAAQSLLDQYAQLKAQYADKPKK-RVFL 160
Cdd:cd01148 95 glGTPDSLAELGIKTyilpescgQRRGEATLDDVYNDIRNLGKIFDVEDRADKLVADLKARLAEISAKVKGDGKKvAVFV 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128151 161 -QFGINPPFTSGKESIQNQVLEVCGGENIFKDSRVPWPQVSREQVLARSPQAIVITGGPDQ 220
Cdd:cd01148 175 yDSGEDKPFTSGRGGIPNAIITAAGGRNVFADVDESWTTVSWETVIARNPDVIVIIDYGDQ 235
|
|
| TroA_e |
cd01142 |
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ... |
25-258 |
1.72e-19 |
|
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: 85.48 E-value: 1.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 25 RVITLSPANTELAFAAGITPVGVSSYS------DYP---PQAQKIEQVSTWQGMNLERIVALKPDLVIAWRGGNAERQVD 95
Cdd:cd01142 26 RIAALWGAGNAVVAALGGGKLIVATTStvqqepWLYrlaPSLENVATGGTGNDVNIEELLALKPDVVIVWSTDGKEAGKA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 96 QLAslGIKVMWVDATSIEQIANALRQLAPWSPQPDKAEQAAQSL---LDQYAQLKAQYADKPKKRVFLQfGINPPFTSGK 172
Cdd:cd01142 106 VLR--LLNALSLRDAELEEVKLTIALLGELLGRQEKAEALVAYFddnLAYVAARTKKLPDSERPRVYYA-GPDPLTTDGT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 173 ESIQNQVLEVCGGENIFKDSRVPW-PQVSREQVLARSPQAIVI--TGGPDQIPKIKQYWG----EQLKIPVIPLTSDWFE 245
Cdd:cd01142 183 GSITNSWIDLAGGINVASEATKKGsGEVSLEQLLKWNPDVIIVgnADTKAAILADPRWQNlravKNGRVYVNPEGAFWWD 262
|
250
....*....|....*..
gi 16128151 246 RASPRIIL----AAQQL 258
Cdd:cd01142 263 RPSAEEALlglwLAKTL 279
|
|
| FhuD |
cd01146 |
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ... |
25-220 |
8.12e-19 |
|
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: 83.10 E-value: 8.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 25 RVITLSPANTELAFAAGITPVGVSSYSDYPPQAQK-------IEQVSTWQGMNLERIVALKPDLVIAWRGGNAErQVDQL 97
Cdd:cd01146 5 RIVALDWGALETLLALGVKPVGVADTAGYKPWIPEpalplegVVDVGTRGQPNLEAIAALKPDLILGSASRHDE-IYDQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 98 A---------SLGIKVMWVDatSIEQIANALrqlapwspqpDKAEQAAQsLLDQY----AQLKAQYADKPKKRVFLQFGI 164
Cdd:cd01146 84 SqiaptvlldSSPWLAEWKE--NLRLIAKAL----------GKEEEAEK-LLAEYdqrlAELRQKLPDKGPKPVSVVRFS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128151 165 NPPFTS--GKESIQNQVLEVCG---GENIFKDSRVPWPQVSREQVLARSPQAIVITGGPDQ 220
Cdd:cd01146 151 DAGSIRlyGPNSFAGSVLEDLGlqnPWAQETTNDSGFATISLERLAKADADVLFVFTYEDE 211
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
27-226 |
3.10e-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: 78.18 E-value: 3.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 27 ITLSPANTELAFAAGITP--VGVSSYSDYPPQAQKIEQ---VSTWQGMNLERIVALKPDLVIAWRGGNAERQvDQLASLG 101
Cdd:pfam01497 1 AALSPAYTEILYALGATDsiVGVDAYTRDPLKADAVAAivkVGAYGEINVERLAALKPDLVILSTGYLTDEA-EELLSLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 102 IKVMWVDATS-IEQIANALRQLAPWSPQPDKAEQAAQSLLDQYAQLKAQYADKPKKRVFLQFGIN--PPFTSGKESIQNQ 178
Cdd:pfam01497 80 IPTVIFESSStGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPVLVFGGADggGYVVAGSNTYIGD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16128151 179 VLEVCGGENIFKD-SRVPWPQVSREQVLARSPQAIVITGGPDQIPKIKQ 226
Cdd:pfam01497 160 LLRILGIENIAAElSGSEYAPISFEAILSSNPDVIIVSGRDSFTKTGPE 208
|
|
| HemV-2 |
cd01147 |
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ... |
25-227 |
4.54e-16 |
|
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: 75.45 E-value: 4.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 25 RVITLSPANTEL--AFAAGITPVGVSS---------YSDYPPQAQK---IEQVSTWQGMNLERIVALKPDLVIAWRGGNA 90
Cdd:cd01147 7 RVVAAGPGALRLlyALAAPDKIVGVDDaeksdegrpYFLASPELKDlpvIGRGGRGNTPNYEKIAALKPDVVIDVGSDDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 91 ERQVDQL-ASLGIKVMWVDA-TSIEQIANALRQLAPWSPQPDKAEQAAQSLLDQYAQLK---AQYADKPKKRVFlqFGin 165
Cdd:cd01147 87 TSIADDLqKKTGIPVVVLDGgDSLEDTPEQIRLLGKVLGKEERAEELISFIESILADVEertKDIPDEEKPTVY--FG-- 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128151 166 PPFTSGKESIQN------QVLEVCGGENIFKDSRVP-WPQVSREQVLARSPQAIVIT--GGPDQIPKIKQY 227
Cdd:cd01147 163 RIGTKGAAGLESglagsiEVFELAGGINVADGLGGGgLKEVSPEQILLWNPDVIFLDtgSFYLSLEGYAKN 233
|
|
| btuF |
PRK09534 |
corrinoid ABC transporter substrate-binding protein; Reviewed |
25-266 |
2.58e-14 |
|
corrinoid ABC transporter substrate-binding protein; Reviewed
Pssm-ID: 236552 [Multi-domain] Cd Length: 359 Bit Score: 71.86 E-value: 2.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 25 RVITLSP--ANTELAFAAGITPVGVSSYSDYPPQAQKIEQVSTWQ--GMNLERIVALKPDLVIAwRGGNAERQVDQLASL 100
Cdd:PRK09534 62 RVVTLNPsaAQTMWELGARDRVVGVTQYASYLDGAEERTNVSGGQpfGVNVEAVVGLDPDLVLA-PNAVAGDTVTRLREA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 101 GIKVMWVD-ATSIEQIANALRQLAPWSPQPDKAEQAAQSLLDQYAQLKAQYAD-KPKKRVFLQFGINppFTSGKESIQNQ 178
Cdd:PRK09534 141 GITVFHFPaATSIEDVAEKTATIGRLTGNCEAAAETNAEMRDRVDAVEDRTADvDDRPRVLYPLGDG--YTAGGNTFIGA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 179 VLEVCGGENIFKDSRVP-WPQVSREQVLARSPQAIVITGGPDQIPKIKQY----WGEQLKipVIPLTSDWFERASPRIIL 253
Cdd:PRK09534 219 LIEAAGGHNVAADATTDgYPQLSEEVIVQQDPDVIVVATASALVAETEPYasttAGETGN--VVTVNVNHINQPAPRIVE 296
|
250
....*....|...
gi 16128151 254 AAQQLCNALSQVD 266
Cdd:PRK09534 297 SMATMATAFHNTT 309
|
|
| FecB |
COG4594 |
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ... |
20-228 |
1.55e-13 |
|
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443650 [Multi-domain] Cd Length: 316 Bit Score: 69.18 E-value: 1.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 20 LNAAP-RVITLSPANTELAFAAGITPVGVSSYSDYPPQAQKI-------EQVSTWQGMNLERIVALKPDLVIAwrggNAE 91
Cdd:COG4594 48 IPGTPkRVVVLEWSFADALLALGVTPVGIADDNDYDRWVPYLrdlikgvTSVGTRSQPNLEAIAALKPDLIIA----DKS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 92 RQV---DQLASLGIKVM-------WVDA-TSIEQIANALrqlapwspqpDKAEQAAQSL--LDQ-YAQLKAQYADKPKKR 157
Cdd:COG4594 124 RHEaiyDQLSKIAPTVLfksrngdYQENlESFKTIAKAL----------GKEEEAEAVLadHDQrIAEAKAKLAAADKGK 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128151 158 --VFLQFGINPPFTSGKESIQNQVLEVCGGENIFKDSRV-PWP--QVSREQVLARSPQAIVITGGPDqiPKIKQYW 228
Cdd:COG4594 194 kvAVGQFRADGLRLYTPNSFAGSVLAALGFENPPKQSKDnGYGysEVSLEQLPALDPDVLFIATYDD--PSILKEW 267
|
|
| TroA_d |
cd01141 |
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ... |
23-191 |
1.72e-13 |
|
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: 67.06 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 23 APRVITLSPANTELAFAAGITP--VGVSSYSD--YPP--QAQKIEQVSTWQGMNLERIVALKPDLVIAWRGGNAERQVDQ 96
Cdd:cd01141 8 PKRIVVLSPTHVDLLLALDKADkiVGVSASAYdlNTPavKERIDIQVGPTGSLNVELIVALKPDLVILYGGFQAQTILDK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 97 LASLGIKVMWVDA-----TSIEQIANALRQLApwSPQPDKAEQAAQSLLDQYAQL--KAQYADKPKKRVFLQFGiNPPFT 169
Cdd:cd01141 88 LEQLGIPVLYVNEypsplGRAEWIKFAAAFYG--VGKEDKADEAFAQIAGRYRDLakKVSNLNKPTVAIGKPVK-GLWYM 164
|
170 180
....*....|....*....|..
gi 16128151 170 SGKESIQNQVLEVCGGENIFKD 191
Cdd:cd01141 165 PGGNSYVAKMLRDAGGRYLSAE 186
|
|
| TroA_f |
cd01139 |
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ... |
48-219 |
1.72e-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: 60.40 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 48 SSYSDYPPQAQKIEQVSTW-----QGMNLERIVALKPDLVI----AWRGGNAERQVDQLASLGIKVMWVD---------A 109
Cdd:cd01139 56 DTYAKYKEKFPEIADIPLIgstynGDFSVEKVLTLKPDLVIlniwAKTTAEESGILEKLEQAGIPVVFVDfrqkplkntT 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 110 TSIEQIANAL-RQlapwspqpDKAEQAAQSLLDQYAQLKAQYA--DKPKKRVFLQFGINPPF---TSGKESIQNQVLEVC 183
Cdd:cd01139 136 PSMRLLGKALgRE--------ERAEEFIEFYQERIDRIRDRLAkiNEPKPKVFIELGAGGPEeccSTYGNGNWGELVDAA 207
|
170 180 190
....*....|....*....|....*....|....*..
gi 16128151 184 GGENIFKD-SRVPWPQVSREQVLARSPQAIVITGGPD 219
Cdd:cd01139 208 GGDNIADGlIPGTSGELNAEYVIAANPEIIIATGGNW 244
|
|
| TroA_like |
NF038402 |
helical backbone metal receptor; |
25-220 |
6.86e-07 |
|
helical backbone metal receptor;
Pssm-ID: 439691 Cd Length: 219 Bit Score: 48.77 E-value: 6.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 25 RVITLSPANTE-LAFAAGITPVGVSSYSDYPPQAQkIEQVSTWQGMNLERIVALKPDLVIAWRGGNAERQVDQLASLGIK 103
Cdd:NF038402 1 RVVSLVPSLTEaIAATAPELLVGATDWCTHPADLD-VARVRGTKNPDRAAIAALRPDLVVANQEENRELDVDRLRAAGVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 104 VmWVdaTSIEQIANALRQL------APWSPQPDkaeqaaqsLLDQYAQLKAQYADKPKKRVFLQFGINPPFTSGKESIQN 177
Cdd:NF038402 80 V-WV--TRIETVDEALASLrrlfteALGVPVPG--------WLDEAEREWAAPAPAPRRRAVVPIWRDPWMVVGRDTFTG 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 16128151 178 QVLEVCGGENIFKDSRVPWPQVSREQVLARSPQAIVItggPDQ 220
Cdd:NF038402 149 DLLARLGLRNVFADHPERYPHVDLDELDAAGPDLVLL---PDE 188
|
|
| FeuA |
cd01138 |
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ... |
25-85 |
1.39e-06 |
|
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: 48.10 E-value: 1.39e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128151 25 RVITLSPAnTELAFAAGITPVGVSSYSD-YPPQAQKIEQVSTWQGM--NLERIVALKPDLVIAW 85
Cdd:cd01138 11 RIVALSGE-TEGLALLGIKPVGAASIGGkNPYYKKKTLAKVVGIVDepNLEKVLELKPDLIIVS 73
|
|
| FatB |
cd01140 |
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ... |
24-163 |
4.00e-06 |
|
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: 46.87 E-value: 4.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 24 PRVITLSPANTELAFAAGITPVGVSS-------YSDYPPQaqKIEQVSTWQGMNLERIVALKPDLVIAwrGGNAERQVDQ 96
Cdd:cd01140 13 EKVVVFDVGALDTLDALGVKVVGVPKsstlpeyLKKYKDD--KYANVGTLFEPDLEAIAALKPDLIII--GGRLAEKYDE 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128151 97 LASL-GIKVMWVDAT-SIEQIANALRQLAPWSPQPDKAEQAAQSLLDQYAQLKAQYADKPKKRVFLQFG 163
Cdd:cd01140 89 LKKIaPTIDLGADLKnYLESVKQNIETLGKIFGKEEEAKELVAEIDASIAEAKSAAKGKKKALVVLVNG 157
|
|
| CeuA |
COG4607 |
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and ... |
39-155 |
3.49e-05 |
|
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443657 [Multi-domain] Cd Length: 310 Bit Score: 44.40 E-value: 3.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 39 AAGITPVGV--SSYSDYPPQ--AQKIEQVSTWQGMNLERIVALKPDLVIAwrGGNAERQVDQLASLG-IKVMWVDATS-I 112
Cdd:COG4607 67 ALGVEVAGVpkGLLPDYLSKyaDDKYANVGTLFEPDLEAIAALKPDLIII--GGRSAKKYDELSKIApTIDLTVDGEDyL 144
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 16128151 113 EQIANALRQLAPWSPQPDKAEQAAQSLLDQYAQLKAQYADKPK 155
Cdd:COG4607 145 ESLKRNTETLGEIFGKEDEAEELVADLDAKIAALKAAAAGKGT 187
|
|
| fecB |
PRK11411 |
iron-dicitrate transporter substrate-binding subunit; Provisional |
20-215 |
6.79e-05 |
|
iron-dicitrate transporter substrate-binding subunit; Provisional
Pssm-ID: 183123 [Multi-domain] Cd Length: 303 Bit Score: 43.51 E-value: 6.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 20 LNAAP-RVITLspantELAF-----AAGITPVGVSSYSDyppqAQKI-----EQVSTWQ--GM----NLERIVALKPDLV 82
Cdd:PRK11411 35 LEKTPqRIVVL-----ELSFvdalaAVGVSPVGVADDND----AKRIlpevrAHLKPWQsvGTrsqpSLEAIAALKPDLI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 83 IAwrggnaerqvdqlaslgikvmwvDATSIEQIANALRQLAPWSPQPDKAEQAAQSL-------------------LDQY 143
Cdd:PRK11411 106 IA-----------------------DSSRHAGVYIALQKIAPTLLLKSRNETYQENLqsaaiigevlgkkremqarIEQH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 144 AQLKAQYADKPKKRVFLQFGinppfTS--------GKESIQNQVLEVCGGEN-IFKDSRVPWPQVSREQVLARSPQAIVI 214
Cdd:PRK11411 163 KERMAQFASQLPKGTRVAFG-----TSreqqfnlhSPESYTGSVLAALGLNVpKAPMNGAAMPSISLEQLLALNPDWLLV 237
|
.
gi 16128151 215 T 215
Cdd:PRK11411 238 A 238
|
|
| PRK14048 |
PRK14048 |
ferrichrome/ferrioxamine B periplasmic transporter; Provisional |
68-218 |
1.87e-03 |
|
ferrichrome/ferrioxamine B periplasmic transporter; Provisional
Pssm-ID: 172540 [Multi-domain] Cd Length: 374 Bit Score: 39.11 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 68 GMNLERIVALKPDLVIA--WRGGNAE--RQVDQLASLGIKVMWVDATS--IEQIANALRQLAPWSPQPDKAEQAAQSLLD 141
Cdd:PRK14048 111 GLSFETILTLKADLAILanWQADTEAgqRAIEYLESIGVPVIVVDFNNeaLKNTPDNMRLLGKVFEREEQAEDFARFYEE 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 142 QYAQLKAQYADKPKK--RVFLQFGINPP---FTSGKESIqNQVLEVCGGENIFKDSrVPWP--QVSREQVLARSPQAIVI 214
Cdd:PRK14048 191 RLARIRDRVAKHSEPgpTVLMEAFPAADrccWAYGRGGL-GEFIALTGSRNIAEGA-LPRPggMMNAEAIMAENPDVYIA 268
|
....
gi 16128151 215 TGGP 218
Cdd:PRK14048 269 TSSP 272
|
|
| PRK10576 |
PRK10576 |
Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD; |
7-149 |
4.26e-03 |
|
Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD;
Pssm-ID: 236719 Cd Length: 292 Bit Score: 37.68 E-value: 4.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 7 RALVALSfLAPLWLNAA---------PRVITLSPANTELAFAAGITPVGVSSYSDY------PPQAQKIEQVSTWQGMNL 71
Cdd:PRK10576 8 RLLTAMA-LSPLLWQMNtaaaaaidpNRIVALEWLPVELLLALGVTPYGVADTHNYrlwvsePALPDSVIDVGLRTEPNL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128151 72 ERIVALKPDLVIAWRG-GNAERQVDQLASlGIKVMWVDATSIEQIA-NALRQLApwspQPDKAEQAAQSLLDQYAQLKAQ 149
Cdd:PRK10576 87 ELLTQMKPSLILWSAGyGPSPEKLARIAP-GRGFAFSDGKKPLAVArKSLVELA----QRLNLEAAAETHLAQFDDFIAS 161
|
|
| |
