|
Name |
Accession |
Description |
Interval |
E-value |
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
20-264 |
2.77e-49 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 163.63 E-value: 2.77e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892157 20 RIISLDPASVETLFMLKADDQIIGIASLTHSDiYPKEKTSKIASVGTFTNPSVEKIISLNPTLVILSSYSLN--LKQKLD 97
Cdd:COG0614 2 RIVSLSPSATELLLALGAGDRLVGVSDWGYCD-YPELELKDLPVVGGTGEPNLEAILALKPDLVLASSSGNDeeDYEQLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892157 98 NFGIKTMVLKAQHLNDIKDNIKILAKITQKEKEGDKILKNFENKLKNL-EKNPLNKS----AIYLYSSNPLMAFSDNSLI 172
Cdd:COG0614 81 KIGIPVVVLDPRSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVrARLAGAEErptvLYEIWSGDPLYTAGGGSFI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892157 173 ADILKLIGIKNLSPKSNIARPIISEEYILKQNPDLLIFGINATEKNLLNNNSLLKN-------TKAVKKNQIYTYkNTYL 245
Cdd:COG0614 161 GELLELAGGRNVAADLGGGYPEVSLEQVLALDPDVIILSGGGYDAETAEEALEALLadpgwqsLPAVKNGRVYVV-PGDL 239
|
250
....*....|....*....
gi 2199892157 246 LLRLSPKIIDRIEEFKAEL 264
Cdd:COG0614 240 LSRPGPRLLLALEDLAKAL 258
|
|
| YvrC |
cd01143 |
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ... |
19-210 |
1.85e-48 |
|
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: 159.37 E-value: 1.85e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892157 19 ERIISLDPASVETLFMLKADDQIIGIASLthsDIYPKEKTSKIaSVGTFTNPSVEKIISLNPTLVILSSYSLN-LKQKLD 97
Cdd:cd01143 4 ERIVSLSPSITEILFALGAGDKIVGVDTY---SNYPKEVRKKP-KVGSYSNPNVEKIVALKPDLVIVSSSSLAeLLEKLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892157 98 NFGIKTMVLK-AQHLNDIKDNIKILAKITQKEKEGDKILKNFENKLKNLEKNPLNK---SAIYLYSSNPLMAFSDNSLIA 173
Cdd:cd01143 80 DAGIPVVVLPaASSLDEIYDQIELIGKITGAEEEAEKLVKEMKQKIDKVKDKGKTIkksKVYIEVSLGGPYTAGKNTFIN 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 2199892157 174 DILKLIGIKNLSPKSNiARPIISEEYILKQNPDLLIF 210
Cdd:cd01143 160 ELIRLAGAKNIAADSG-GWPQVSPEEILKANPDVIIL 195
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
22-242 |
2.57e-28 |
|
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: 108.22 E-value: 2.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892157 22 ISLDPASVETLFMLKADDQIIGIaSLTHSDIYPKEKTSKIASVGTFTNPSVEKIISLNPTLVILSSYSLN--LKQKLDNf 99
Cdd:pfam01497 1 AALSPAYTEILYALGATDSIVGV-DAYTRDPLKADAVAAIVKVGAYGEINVERLAALKPDLVILSTGYLTdeAEELLSL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892157 100 GIKTM-VLKAQHLNDIKDNIKILAKITQKEKEGDKILKNFENKLKNLEK---NPLNKSAIYLYSSN--PLMAFSDNSLIA 173
Cdd:pfam01497 79 IIPTViFESSSTGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKavpSLTRKPVLVFGGADggGYVVAGSNTYIG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2199892157 174 DILKLIGIKNLSP-KSNIARPIISEEYILKQNPDLLIFGINATEKNLLNNNSLL----KNTKAVKKNQIYTYKN 242
Cdd:pfam01497 159 DLLRILGIENIAAeLSGSEYAPISFEAILSSNPDVIIVSGRDSFTKTGPEFVAAnplwAGLPAVKNGRVYTLPS 232
|
|
| PRK03379 |
PRK03379 |
vitamin B12-transporter protein BtuF; Provisional |
5-216 |
4.65e-17 |
|
vitamin B12-transporter protein BtuF; Provisional
Pssm-ID: 179575 [Multi-domain] Cd Length: 260 Bit Score: 78.57 E-value: 4.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892157 5 LILCFTFIIILQAKERIISLDPASVETLFMLKADDqiIGIASltHSDiYPKEkTSKIASVGTFTNPSVEKIISLNPTLvI 84
Cdd:PRK03379 4 VALLFLAPLWLNAAPRVITLSPANTELAFAAGITP--VGVSS--YSD-YPPQ-AKKIEQVATWQGMNLERIVALKPDL-V 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892157 85 LSSYSLNLKQKLD---NFGIKTMVLKAQHLNDIKDNIKILAKIT----QKEKEGDKILKNFeNKLKNLEKNPLNKSAIYL 157
Cdd:PRK03379 77 LAWRGGNAERQVDqlaSLGIKVMWVDATSIEQIANALRQLAPWSpqpeKAEQAAQSLLQQY-AALKAQYADKPKKRVFLQ 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2199892157 158 YSSNPLMAFSDNSLIADILKLIGIKNLSPKSNIARPIISEEYILKQNPDLLIFGINATE 216
Cdd:PRK03379 156 FGTNPLFTSGKHSIQSQVLSLCGGENIFADSRVPWPQVSREQVLARKPQAIVITGGPDQ 214
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
20-264 |
2.77e-49 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 163.63 E-value: 2.77e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892157 20 RIISLDPASVETLFMLKADDQIIGIASLTHSDiYPKEKTSKIASVGTFTNPSVEKIISLNPTLVILSSYSLN--LKQKLD 97
Cdd:COG0614 2 RIVSLSPSATELLLALGAGDRLVGVSDWGYCD-YPELELKDLPVVGGTGEPNLEAILALKPDLVLASSSGNDeeDYEQLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892157 98 NFGIKTMVLKAQHLNDIKDNIKILAKITQKEKEGDKILKNFENKLKNL-EKNPLNKS----AIYLYSSNPLMAFSDNSLI 172
Cdd:COG0614 81 KIGIPVVVLDPRSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVrARLAGAEErptvLYEIWSGDPLYTAGGGSFI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892157 173 ADILKLIGIKNLSPKSNIARPIISEEYILKQNPDLLIFGINATEKNLLNNNSLLKN-------TKAVKKNQIYTYkNTYL 245
Cdd:COG0614 161 GELLELAGGRNVAADLGGGYPEVSLEQVLALDPDVIILSGGGYDAETAEEALEALLadpgwqsLPAVKNGRVYVV-PGDL 239
|
250
....*....|....*....
gi 2199892157 246 LLRLSPKIIDRIEEFKAEL 264
Cdd:COG0614 240 LSRPGPRLLLALEDLAKAL 258
|
|
| YvrC |
cd01143 |
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ... |
19-210 |
1.85e-48 |
|
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: 159.37 E-value: 1.85e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892157 19 ERIISLDPASVETLFMLKADDQIIGIASLthsDIYPKEKTSKIaSVGTFTNPSVEKIISLNPTLVILSSYSLN-LKQKLD 97
Cdd:cd01143 4 ERIVSLSPSITEILFALGAGDKIVGVDTY---SNYPKEVRKKP-KVGSYSNPNVEKIVALKPDLVIVSSSSLAeLLEKLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892157 98 NFGIKTMVLK-AQHLNDIKDNIKILAKITQKEKEGDKILKNFENKLKNLEKNPLNK---SAIYLYSSNPLMAFSDNSLIA 173
Cdd:cd01143 80 DAGIPVVVLPaASSLDEIYDQIELIGKITGAEEEAEKLVKEMKQKIDKVKDKGKTIkksKVYIEVSLGGPYTAGKNTFIN 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 2199892157 174 DILKLIGIKNLSPKSNiARPIISEEYILKQNPDLLIF 210
Cdd:cd01143 160 ELIRLAGAKNIAADSG-GWPQVSPEEILKANPDVIIL 195
|
|
| BtuF |
cd01144 |
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ... |
19-262 |
5.99e-30 |
|
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: 112.78 E-value: 5.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892157 19 ERIISLDPASVETLFMLKADDQIIGIaslTHSDIYPKEKtSKIASVGTFTNPSVEKIISLNPTLVILSSySLNLK---QK 95
Cdd:cd01144 1 MRIVSLAPSATELLYALGLGDQLVGV---TDYCDYPPEA-KKLPRVGGFYQLDLERVLALKPDLVIAWD-DCNVCavvDQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892157 96 LDNFGIKTMVLKAQHLNDIKDNIKILAKITQKEKEGDKILKNFENKLKNLEKNPLNK---SAIYLYSSNPLMAfSDNSLI 172
Cdd:cd01144 76 LRAAGIPVLVSEPQTLDDILADIRRLGTLAGRPARAEELAEALRRRLAALRKQYASKpppRVFYQEWIDPLMT-AGGDWV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892157 173 ADILKLIGIKNLSPKSNIARPIISEEYILKQNPDLLIFG--INATEKNLLNNNSLLKNTKAVKKNQIYTYKNTyLLLRLS 250
Cdd:cd01144 155 PELIALAGGVNVFADAGERSPQVSWEDVLAANPDVIVLSpcGFGFTPAILRKEPAWQALPAVRNGRVYAVDGN-WYFRPS 233
|
250
....*....|..
gi 2199892157 251 PKIIDRIEEFKA 262
Cdd:cd01144 234 PRLVDGLEQLAA 245
|
|
| ChuT |
COG4558 |
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ... |
1-267 |
2.08e-28 |
|
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443619 [Multi-domain] Cd Length: 285 Bit Score: 109.51 E-value: 2.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892157 1 MKKILILCFTFIIIL---------QAKERIISLDPASVETLFMLKADDQIIGIASlthSDIYPKEkTSKIASVGTFTNPS 71
Cdd:COG4558 1 MKRLALALLLLALAAlaagasvaaAAAERIVSLGGSVTEIVYALGAGDRLVGVDT---TSTYPAA-AKALPDVGYMRQLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892157 72 VEKIISLNPTLVILSSYSLN---LKQkLDNFGIKTMVLKAQH-LNDIKDNIKILAKITQKEKEGDKILKNFENKLKNLEK 147
Cdd:COG4558 77 AEGILSLKPTLVLASEGAGPpevLDQ-LRAAGVPVVVVPAAPsLEGVLAKIRAVAAALGVPEAGEALAARLEADLAALAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892157 148 NPLNKSA------IYLYSSNPLMAFSDNSLIADILKLIGIKNLSPKSNIARPiISEEYILKQNPDLLIF----------- 210
Cdd:COG4558 156 RVAAIGKpprvlfLLSRGGGRPMVAGRGTAADALIRLAGGVNAAAGFEGYKP-LSAEALIAAAPDVILVmtrgleslggv 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2199892157 211 -------GINATEknllnnnsllkntkAVKKNQIYTYkNTYLLLRLSPKIIDRIEEFKAELEKA 267
Cdd:COG4558 235 dgllalpGLAQTP--------------AGKNKRIVAM-DDLLLLGFGPRTPQAALALAQALYPA 283
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
22-242 |
2.57e-28 |
|
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: 108.22 E-value: 2.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892157 22 ISLDPASVETLFMLKADDQIIGIaSLTHSDIYPKEKTSKIASVGTFTNPSVEKIISLNPTLVILSSYSLN--LKQKLDNf 99
Cdd:pfam01497 1 AALSPAYTEILYALGATDSIVGV-DAYTRDPLKADAVAAIVKVGAYGEINVERLAALKPDLVILSTGYLTdeAEELLSL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892157 100 GIKTM-VLKAQHLNDIKDNIKILAKITQKEKEGDKILKNFENKLKNLEK---NPLNKSAIYLYSSN--PLMAFSDNSLIA 173
Cdd:pfam01497 79 IIPTViFESSSTGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKavpSLTRKPVLVFGGADggGYVVAGSNTYIG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2199892157 174 DILKLIGIKNLSP-KSNIARPIISEEYILKQNPDLLIFGINATEKNLLNNNSLL----KNTKAVKKNQIYTYKN 242
Cdd:pfam01497 159 DLLRILGIENIAAeLSGSEYAPISFEAILSSNPDVIIVSGRDSFTKTGPEFVAAnplwAGLPAVKNGRVYTLPS 232
|
|
| FhuD |
cd01146 |
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ... |
19-238 |
2.81e-23 |
|
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: 95.43 E-value: 2.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892157 19 ERIISLDPASVETLfmLKADDQIIGIASLTHSD---IYPKEKTSKIASVGTFTNPSVEKIISLNPTLvILSSYSLN--LK 93
Cdd:cd01146 4 QRIVALDWGALETL--LALGVKPVGVADTAGYKpwiPEPALPLEGVVDVGTRGQPNLEAIAALKPDL-ILGSASRHdeIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892157 94 QKLDNFGiKTMVLK-AQHLNDIKDNIKILAKITQKEKEGDKILKNFENKLKNL-----EKNPLNKSAIYLYSSNPLMAFS 167
Cdd:cd01146 81 DQLSQIA-PTVLLDsSPWLAEWKENLRLIAKALGKEEEAEKLLAEYDQRLAELrqklpDKGPKPVSVVRFSDAGSIRLYG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2199892157 168 DNSLIADILKLIGIKNLSPKSNIARPI---ISEEYILKQNPDLLIFGINATEKNLLNNNSLL--KNTKAVKKNQIY 238
Cdd:cd01146 160 PNSFAGSVLEDLGLQNPWAQETTNDSGfatISLERLAKADADVLFVFTYEDEELAQALQANPlwQNLPAVKNGRVY 235
|
|
| TroA-like |
cd00636 |
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ... |
19-147 |
2.44e-22 |
|
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: 89.93 E-value: 2.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892157 19 ERIISLDPASVETLFMLKADDQIIGIASLTHSDIYPKEKTSKIASVGTFTNPSVEKIISLNPTLVILSSYSLN-LKQKLD 97
Cdd:cd00636 1 KRVVALDPGATELLLALGGDDKPVGVADPSGYPPEAKALLEKVPDVGHGYEPNLEKIAALKPDLIIANGSGLEaWLDKLS 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2199892157 98 NFGIKTMVLK---AQHLNDIKDNIKILAKITQKEKEGDKILKNFENKLKNLEK 147
Cdd:cd00636 81 KIAIPVVVVDeasELSLENIKESIRLIGKALGKEENAEELIAELDARLAELRA 133
|
|
| FatB |
cd01140 |
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ... |
19-247 |
1.60e-21 |
|
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: 90.78 E-value: 1.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892157 19 ERIISLDPASVETLFMLKADdqIIGIASLTH-SDIYPKEKTSKIASVGTFTNPSVEKIISLNPTLVILS-SYSLNLKQKL 96
Cdd:cd01140 13 EKVVVFDVGALDTLDALGVK--VVGVPKSSTlPEYLKKYKDDKYANVGTLFEPDLEAIAALKPDLIIIGgRLAEKYDELK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892157 97 DNFGIKTMVL-KAQHLNDIKDNIKILAKITQKEKEGDKILKNFENKLKNL-EKNPLNKSA-IYLYSSNPLMAFSDNSLIA 173
Cdd:cd01140 91 KIAPTIDLGAdLKNYLESVKQNIETLGKIFGKEEEAKELVAEIDASIAEAkSAAKGKKKAlVVLVNGGKLSAFGPGSRFG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892157 174 DILKLIGIKNLSPKSNIARP--IISEEYILKQNPDLL-------IFGINATEKNLLNNNSLLKNTKAVKKNQIYTYKNTY 244
Cdd:cd01140 171 WLHDLLGFEPADENIKASSHgqPVSFEYILEANPDWLfvidrgaAIGAEGSSAKEVLDNDLVKNTTAWKNGKVIYLDPDL 250
|
...
gi 2199892157 245 LLL 247
Cdd:cd01140 251 WYL 253
|
|
| TroA_e |
cd01142 |
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ... |
19-238 |
3.74e-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: 84.71 E-value: 3.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892157 19 ERIISLDPASVETLFMLKADDQIIGIASLTHSDIYPKEKT---SKIASVGTFTNPSVEKIISLNPTLVILSSYSLN--LK 93
Cdd:cd01142 25 KRIAALWGAGNAVVAALGGGKLIVATTSTVQQEPWLYRLApslENVATGGTGNDVNIEELLALKPDVVIVWSTDGKeaGK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892157 94 QKLDnfGIKTMVLKAQHLNDIKDNIKILAKITQKEKEGDKILKNFENKLK----NLEKNPLN-KSAIYLYSSNPLMAFSD 168
Cdd:cd01142 105 AVLR--LLNALSLRDAELEEVKLTIALLGELLGRQEKAEALVAYFDDNLAyvaaRTKKLPDSeRPRVYYAGPDPLTTDGT 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2199892157 169 NSLIADILKLIGIKN-LSPKSNIARPIISEEYILKQNPDLLIFGiNATEKNLLNNNSLLKNTKAVKKNQIY 238
Cdd:cd01142 183 GSITNSWIDLAGGINvASEATKKGSGEVSLEQLLKWNPDVIIVG-NADTKAAILADPRWQNLRAVKNGRVY 252
|
|
| HutB |
cd01149 |
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ... |
19-209 |
5.87e-19 |
|
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: 83.08 E-value: 5.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892157 19 ERIISLDPASVETLFMLKADDQIIGIASlthSDIYPKEkTSKIASVGTFTNPSVEKIISLNPTLVILSSYS---LNLKQk 95
Cdd:cd01149 2 ERIVSLGGSVTEIVYALGAGDRLVGVDS---TSTYPEA-AAKLPDVGYMRQLSAEGVLSLKPTLVIASDEAgppEALDQ- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892157 96 LDNFGIKTMVLKAQ-HLNDIKDNIKILAKITQKEKEGDKILKNFENKLKNLEKNP----LNKSAIYLYS--SNPLMAFSD 168
Cdd:cd01149 77 LRAAGVPVVTVPSTpTLDGLLTKIRQVAQALGVPEKGEALAQEVRQRLAALRKTVaahkKPPRVLFLLShgGGAAMAAGR 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2199892157 169 NSLIADILKLIGIKNLSPKSNIARPiISEEYILKQNPDLLI 209
Cdd:cd01149 157 NTAADAIIALAGAVNAAAGFRGYKP-LSAEALIAAQPDVIL 196
|
|
| PRK03379 |
PRK03379 |
vitamin B12-transporter protein BtuF; Provisional |
5-216 |
4.65e-17 |
|
vitamin B12-transporter protein BtuF; Provisional
Pssm-ID: 179575 [Multi-domain] Cd Length: 260 Bit Score: 78.57 E-value: 4.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892157 5 LILCFTFIIILQAKERIISLDPASVETLFMLKADDqiIGIASltHSDiYPKEkTSKIASVGTFTNPSVEKIISLNPTLvI 84
Cdd:PRK03379 4 VALLFLAPLWLNAAPRVITLSPANTELAFAAGITP--VGVSS--YSD-YPPQ-AKKIEQVATWQGMNLERIVALKPDL-V 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892157 85 LSSYSLNLKQKLD---NFGIKTMVLKAQHLNDIKDNIKILAKIT----QKEKEGDKILKNFeNKLKNLEKNPLNKSAIYL 157
Cdd:PRK03379 77 LAWRGGNAERQVDqlaSLGIKVMWVDATSIEQIANALRQLAPWSpqpeKAEQAAQSLLQQY-AALKAQYADKPKKRVFLQ 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2199892157 158 YSSNPLMAFSDNSLIADILKLIGIKNLSPKSNIARPIISEEYILKQNPDLLIFGINATE 216
Cdd:PRK03379 156 FGTNPLFTSGKHSIQSQVLSLCGGENIFADSRVPWPQVSREQVLARKPQAIVITGGPDQ 214
|
|
| FecB |
COG4594 |
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ... |
19-238 |
7.36e-17 |
|
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443650 [Multi-domain] Cd Length: 316 Bit Score: 78.81 E-value: 7.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892157 19 ERIISLDPASVETLfmLKADDQIIGIAslthsDI--------YPKEKTSKIASVGTFTNPSVEKIISLNPTLVILSsysl 90
Cdd:COG4594 53 KRVVVLEWSFADAL--LALGVTPVGIA-----DDndydrwvpYLRDLIKGVTSVGTRSQPNLEAIAALKPDLIIAD---- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892157 91 nlkqKLDNFGIK--------TMVLKA--QHLNDIKDNIKILAKITQKEKEGDKILKNFENKLKN----LEKNPLNKSAIY 156
Cdd:COG4594 122 ----KSRHEAIYdqlskiapTVLFKSrnGDYQENLESFKTIAKALGKEEEAEAVLADHDQRIAEakakLAAADKGKKVAV 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892157 157 LYSSNP-LMAFSDNSLIADILKLIGIKN---LSPKSNIARPIISEEYILKQNPDLLIFGINATEKNLLNNNSLL--KNTK 230
Cdd:COG4594 198 GQFRADgLRLYTPNSFAGSVLAALGFENppkQSKDNGYGYSEVSLEQLPALDPDVLFIATYDDPSILKEWKNNPlwKNLK 277
|
....*...
gi 2199892157 231 AVKKNQIY 238
Cdd:COG4594 278 AVKNGRVY 285
|
|
| CeuA |
COG4607 |
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and ... |
19-238 |
8.20e-16 |
|
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443657 [Multi-domain] Cd Length: 310 Bit Score: 75.60 E-value: 8.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892157 19 ERIISLDPASVETLFMLKADdqIIGIASlthsDIYPKE----KTSKIASVGTFTNPSVEKIISLNPTLVILSSYSLNLKQ 94
Cdd:COG4607 52 KRVVVFDNGALDTLDALGVE--VAGVPK----GLLPDYlskyADDKYANVGTLFEPDLEAIAALKPDLIIIGGRSAKKYD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892157 95 KLD------NFGIKTmvlkAQHLNDIKDNIKILAKITQKEKEGDKILKNFENKLKNL-EKNPLNKSA-IYLYSSNPLMAF 166
Cdd:COG4607 126 ELSkiaptiDLTVDG----EDYLESLKRNTETLGEIFGKEDEAEELVADLDAKIAALkAAAAGKGTAlIVLTNGGKISAY 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892157 167 SDNSLIADILKLIGIKNLSP--KSNIARPIISEEYILKQNPDLLI-------FGINATEKNLLNNNSLLKNTKAVKKNQI 237
Cdd:COG4607 202 GPGSRFGPIHDVLGFKPADEdiEASTHGQAISFEFIAEANPDWLFvidrdaaIGGEGPAAKQVLDNELVKQTTAWKNGQI 281
|
.
gi 2199892157 238 Y 238
Cdd:COG4607 282 V 282
|
|
| HemV-2 |
cd01147 |
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ... |
19-238 |
5.84e-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: 72.75 E-value: 5.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892157 19 ERIISLDPASVETLFMLKADDQIIGIASLTHSD-----IYPKEKTSKIASVGTF---TNPSVEKIISLNPTLVILSsYSL 90
Cdd:cd01147 6 ERVVAAGPGALRLLYALAAPDKIVGVDDAEKSDegrpyFLASPELKDLPVIGRGgrgNTPNYEKIAALKPDVVIDV-GSD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892157 91 NLKQKLDN----FGIKTMVLKAQ-HLNDIKDNIKILAKITQKEKEGDKILKNFENKLKNLEK-----NPLNKSAIYL--- 157
Cdd:cd01147 85 DPTSIADDlqkkTGIPVVVLDGGdSLEDTPEQIRLLGKVLGKEERAEELISFIESILADVEErtkdiPDEEKPTVYFgri 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892157 158 -YSSNPLMAFSDNSLIADILKLIGIKNLSPKSNIARPIISEEYILKQNPDLLIFGINATEKNLLNNNSLLKN---TKAVK 233
Cdd:cd01147 165 gTKGAAGLESGLAGSIEVFELAGGINVADGLGGGGLKEVSPEQILLWNPDVIFLDTGSFYLSLEGYAKNRPFwqsLKAVK 244
|
....*
gi 2199892157 234 KNQIY 238
Cdd:cd01147 245 NGRVY 249
|
|
| TroA_a |
cd01148 |
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ... |
7-237 |
4.33e-13 |
|
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: 67.75 E-value: 4.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892157 7 LCFTfiiilQAKERIISLDPASVETLFMLKADDQIIGIASLTHSDIyP--KEKTSKIASVGTfTNPSVEKIISLNPTLVI 84
Cdd:cd01148 12 VTFD-----KAPQRVVSNDQNTTEMMLALGLQDRMVGTAGIDNKDL-PelKAKYDKVPELAK-KYPSKETVLAARPDLVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892157 85 LSSYSLNLKQK------LDNFGIKTMVLKAQH--------LNDIKDNIKILAKITQKEKEGDKILKNFENKLKNLEKNP- 149
Cdd:cd01148 85 GGWSYGFDKGGlgtpdsLAELGIKTYILPESCgqrrgeatLDDVYNDIRNLGKIFDVEDRADKLVADLKARLAEISAKVk 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892157 150 --LNKSAIYLYSSNPL--MAFSDNSLIADILKLIGIKNLSPKSNIARPIISEEYILKQNPDLLIF----GINATEKNLL- 220
Cdd:cd01148 165 gdGKKVAVFVYDSGEDkpFTSGRGGIPNAIITAAGGRNVFADVDESWTTVSWETVIARNPDVIVIidygDQNAAEQKIKf 244
|
250
....*....|....*...
gi 2199892157 221 -NNNSLLKNTKAVKKNQI 237
Cdd:cd01148 245 lKENPALKNVPAVKNNRF 262
|
|
| TroA_d |
cd01141 |
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ... |
12-147 |
1.90e-11 |
|
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: 61.28 E-value: 1.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892157 12 IIILQAKeRIISLDPASVETLFMLKADDQIIGIASLTHSDIYPKEKTSKIASVGTFTNPSVEKIISLNPTLVILS--SYS 89
Cdd:cd01141 3 TIKVPPK-RIVVLSPTHVDLLLALDKADKIVGVSASAYDLNTPAVKERIDIQVGPTGSLNVELIVALKPDLVILYggFQA 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2199892157 90 LNLKQKLDNFGIKTMVLkaQHLNDIKDNIKILAK-----ITQKEKEGDKILKNFENKLKNLEK 147
Cdd:cd01141 82 QTILDKLEQLGIPVLYV--NEYPSPLGRAEWIKFaaafyGVGKEDKADEAFAQIAGRYRDLAK 142
|
|
| btuF |
PRK09534 |
corrinoid ABC transporter substrate-binding protein; Reviewed |
10-271 |
5.68e-11 |
|
corrinoid ABC transporter substrate-binding protein; Reviewed
Pssm-ID: 236552 [Multi-domain] Cd Length: 359 Bit Score: 61.85 E-value: 5.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892157 10 TFIIILQAKERIISLDPASVETLFMLKADDQIIGIASLThSDIYPKEKTSKIASVGTFTNpSVEKIISLNPTLVILSSYS 89
Cdd:PRK09534 52 TEITLDERPERVVTLNPSAAQTMWELGARDRVVGVTQYA-SYLDGAEERTNVSGGQPFGV-NVEAVVGLDPDLVLAPNAV 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892157 90 LNLK-QKLDNFGIKTMVLK-AQHLNDIKDNIKILAKIT-------QKEKEGDKILKNFENKLKNLEKNPlnkSAIYLYSS 160
Cdd:PRK09534 130 AGDTvTRLREAGITVFHFPaATSIEDVAEKTATIGRLTgnceaaaETNAEMRDRVDAVEDRTADVDDRP---RVLYPLGD 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892157 161 NPLMAfsDNSLIADILKLIGIKNLSPKSNIAR-PIISEEYILKQNPDLLIFginATEKNLLNNNSLLKNTKAVKKNQIYT 239
Cdd:PRK09534 207 GYTAG--GNTFIGALIEAAGGHNVAADATTDGyPQLSEEVIVQQDPDVIVV---ATASALVAETEPYASTTAGETGNVVT 281
|
250 260 270
....*....|....*....|....*....|..
gi 2199892157 240 YkNTYLLLRLSPKIIDRIEEFKAELEKANSAT 271
Cdd:PRK09534 282 V-NVNHINQPAPRIVESMATMATAFHNTTTND 312
|
|
| FeuA |
cd01138 |
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ... |
41-243 |
6.31e-11 |
|
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: 60.81 E-value: 6.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892157 41 IIGIASLTHSDIYPK-EKTSKIASVGTFTNPSVEKIISLNPTLVILSSYSLNLKQKLDNfgIKTMVLKAQHLNDIKDNIK 119
Cdd:cd01138 27 IKPVGAASIGGKNPYyKKKTLAKVVGIVDEPNLEKVLELKPDLIIVSSKQEENYEKLSK--IAPTVPVSYNSSDWEEQLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892157 120 ILAKITQKEKEGDKILKNFENKLKNL-----EKNPLNKSAIYLYSSNPLMAFSDNSLIADIL--KLIGIKnlSPK----- 187
Cdd:cd01138 105 EIGKLLNKEDEAEKWLADYKQKAKEAkekikKKLGNDKSVAVLRGRKQIYVFGEDGRGGGPIlyADLGLK--APEkvkei 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892157 188 -SNIARPIISEEYILKQNPDlLIFGINATEKNLLNNNSLLKN---TKAVKKNQIYTYKNT 243
Cdd:cd01138 183 eDKPGYAAISLEVLPEFDAD-YIFLLFFTGPEAKADFESLPIwknLPAVKNNHVYIVDAW 241
|
|
| TroA_f |
cd01139 |
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ... |
51-209 |
2.09e-07 |
|
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: 51.15 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892157 51 DIYPKekTSKIASVGTFTNP--SVEKIISLNPTLVILSS------YSLNLKQKLDNFGIKTMV--LKAQHLNDIKDNIKI 120
Cdd:cd01139 63 EKFPE--IADIPLIGSTYNGdfSVEKVLTLKPDLVILNIwakttaEESGILEKLEQAGIPVVFvdFRQKPLKNTTPSMRL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892157 121 LAKITQKEKEGDKILKNFENKLK----NLEKNPLNKSAIYL-----YSSNPLMAFSDNSLiADILKLIGiknlspKSNIA 191
Cdd:cd01139 141 LGKALGREERAEEFIEFYQERIDrirdRLAKINEPKPKVFIelgagGPEECCSTYGNGNW-GELVDAAG------GDNIA 213
|
170 180
....*....|....*....|....*
gi 2199892157 192 RPII-------SEEYILKQNPDLLI 209
Cdd:cd01139 214 DGLIpgtsgelNAEYVIAANPEIII 238
|
|
| fecB |
PRK11411 |
iron-dicitrate transporter substrate-binding subunit; Provisional |
63-211 |
1.51e-06 |
|
iron-dicitrate transporter substrate-binding subunit; Provisional
Pssm-ID: 183123 [Multi-domain] Cd Length: 303 Bit Score: 48.52 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892157 63 SVGTFTNPSVEKIISLNPTLVIL-SSYSLNLKQKLDNFGiKTMVLKAQHlNDIKDNIKILAKITQ---KEKEGDKILKNF 138
Cdd:PRK11411 85 SVGTRSQPSLEAIAALKPDLIIAdSSRHAGVYIALQKIA-PTLLLKSRN-ETYQENLQSAAIIGEvlgKKREMQARIEQH 162
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2199892157 139 ENKLKNLEKN-PLNKSAIYLYSSNPLMAF-SDNSLIADILKLIGIKN-LSPKSNIARPIISEEYILKQNPDLLIFG 211
Cdd:PRK11411 163 KERMAQFASQlPKGTRVAFGTSREQQFNLhSPESYTGSVLAALGLNVpKAPMNGAAMPSISLEQLLALNPDWLLVA 238
|
|
| PRK14048 |
PRK14048 |
ferrichrome/ferrioxamine B periplasmic transporter; Provisional |
53-209 |
3.53e-03 |
|
ferrichrome/ferrioxamine B periplasmic transporter; Provisional
Pssm-ID: 172540 [Multi-domain] Cd Length: 374 Bit Score: 38.34 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892157 53 YPKEKTSKIASVGTFTNPSVEKIISLNPTLVILSSYSLNLK------QKLDNFGIKTMVLKAQH--LNDIKDNIKILAKI 124
Cdd:PRK14048 95 FPELADVPLIDDGSGPGLSFETILTLKADLAILANWQADTEagqraiEYLESIGVPVIVVDFNNeaLKNTPDNMRLLGKV 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199892157 125 TQKEKEGDKILKNFENKLKN----------------LEKNPLNKSAIYLYSSNPLMAFsdnsliadiLKLIGIKNLSpKS 188
Cdd:PRK14048 175 FEREEQAEDFARFYEERLARirdrvakhsepgptvlMEAFPAADRCCWAYGRGGLGEF---------IALTGSRNIA-EG 244
|
170 180
....*....|....*....|...
gi 2199892157 189 NIARP--IISEEYILKQNPDLLI 209
Cdd:PRK14048 245 ALPRPggMMNAEAIMAENPDVYI 267
|
|
| |
