|
Name |
Accession |
Description |
Interval |
E-value |
| ChuT |
COG4558 |
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ... |
1-288 |
1.32e-72 |
|
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443619 [Multi-domain] Cd Length: 285 Bit Score: 224.69 E-value: 1.32e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143559383 1 MRRFRLYLIGLLICLFIVGCnpskeSTTSDESYRIISLMPSNTEILYALDLGTSVVGVTDQDDYPKDVQSLPQF-NTYEL 79
Cdd:COG4558 1 MKRLALALLLLALAALAAGA-----SVAAAAAERIVSLGGSVTEIVYALGAGDRLVGVDTTSTYPAAAKALPDVgYMRQL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143559383 80 NAEALLKLKPTHIVTHEIAYPTQqkVLDQLKKEGVEIITVDDATTIDEVYDTFNQVATPFDRTDKSEQLVEETKSQVQAV 159
Cdd:COG4558 76 SAEGILSLKPTLVLASEGAGPPE--VLDQLRAAGVPVVVVPAAPSLEGVLAKIRAVAAALGVPEAGEALAARLEADLAAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143559383 160 LDDIPSSDTMTRVYYEVSLEPERYT-SGSETLHHDMIAQLKAKNIYEDLKGWQSIALESLIEKNPDIYLHASDITEEDL- 237
Cdd:COG4558 154 AARVAAIGKPPRVLFLLSRGGGRPMvAGRGTAADALIRLAGGVNAAAGFEGYKPLSAEALIAAAPDVILVMTRGLESLGg 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1143559383 238 MNDIQGNKALKKIKAVQNDKVYVLDPDILNRPTPRIDEALKLLRDHIYEAS 288
Cdd:COG4558 234 VDGLLALPGLAQTPAGKNKRIVAMDDLLLLGFGPRTPQAALALAQALYPAA 284
|
|
| YvrC |
cd01143 |
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ... |
34-225 |
2.75e-52 |
|
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: 169.38 E-value: 2.75e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143559383 34 RIISLMPSNTEILYALDLGTSVVGVTDQDDYPKDVQSLPQFNTY-ELNAEALLKLKPTHIVTHEIAYPTqqkVLDQLKKE 112
Cdd:cd01143 5 RIVSLSPSITEILFALGAGDKIVGVDTYSNYPKEVRKKPKVGSYsNPNVEKIVALKPDLVIVSSSSLAE---LLEKLKDA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143559383 113 GVEIITVDDATTIDEVYDTFNQVATPFDRTDKSEQLVEETKSQVQAVLDDIPSSDTMTrVYYEVSLEPErYTSGSETLHH 192
Cdd:cd01143 82 GIPVVVLPAASSLDEIYDQIELIGKITGAEEEAEKLVKEMKQKIDKVKDKGKTIKKSK-VYIEVSLGGP-YTAGKNTFIN 159
|
170 180 190
....*....|....*....|....*....|...
gi 1143559383 193 DMIAQLKAKNIYEDLKGWQSIALESLIEKNPDI 225
Cdd:cd01143 160 ELIRLAGAKNIAADSGGWPQVSPEEILKANPDV 192
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
36-264 |
8.33e-30 |
|
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: 112.46 E-value: 8.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143559383 36 ISLMPSNTEILYALDLGTSVVGVTDQDDYP---KDVQSLPQFNTY-ELNAEALLKLKPTHIVtheIAYPTQQKVLDQLKK 111
Cdd:pfam01497 1 AALSPAYTEILYALGATDSIVGVDAYTRDPlkaDAVAAIVKVGAYgEINVERLAALKPDLVI---LSTGYLTDEAEELLS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143559383 112 EGVEIITVDDATTIDEVYDTFNQVATPFDRTDKSEQLVEETKSQVQAVLDDIPSSDTMTRVYYEVSLEPERYTSGSETLH 191
Cdd:pfam01497 78 LIIPTVIFESSSTGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPVLVFGGADGGGYVVAGSNTYI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1143559383 192 HDMIAQLKAKNIYEDLKGWQS--IALESLIEKNPDIYLHASDITEEDLMND-IQGNKALKKIKAVQNDKVYVLDPD 264
Cdd:pfam01497 158 GDLLRILGIENIAAELSGSEYapISFEAILSSNPDVIIVSGRDSFTKTGPEfVAANPLWAGLPAVKNGRVYTLPSD 233
|
|
| PRK03379 |
PRK03379 |
vitamin B12-transporter protein BtuF; Provisional |
34-280 |
2.32e-20 |
|
vitamin B12-transporter protein BtuF; Provisional
Pssm-ID: 179575 [Multi-domain] Cd Length: 260 Bit Score: 87.82 E-value: 2.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143559383 34 RIISLMPSNTEILYALDLGTsvVGVTDQDDYPKDVQSLPQFNTYE-LNAEALLKLKPTHIVTHEIAYPtqQKVLDQLKKE 112
Cdd:PRK03379 19 RVITLSPANTELAFAAGITP--VGVSSYSDYPPQAKKIEQVATWQgMNLERIVALKPDLVLAWRGGNA--ERQVDQLASL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143559383 113 GVEIITVdDATTIDEVYDTFNQVATPFDRTDKSEQLVEETKSQVQAVLDDIPSSdTMTRVYYEVSLEPeRYTSGSETLHH 192
Cdd:PRK03379 95 GIKVMWV-DATSIEQIANALRQLAPWSPQPEKAEQAAQSLLQQYAALKAQYADK-PKKRVFLQFGTNP-LFTSGKHSIQS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143559383 193 DMIAQLKAKNIYEDLK-GWQSIALESLIEKNPDIYLhasditeedlmndIQGNKalKKIKAVQ-------NDKVYVLDPD 264
Cdd:PRK03379 172 QVLSLCGGENIFADSRvPWPQVSREQVLARKPQAIV-------------ITGGP--DQIPKIKqfwgpqlKIPVIPLNSD 236
|
250
....*....|....*.
gi 1143559383 265 ILNRPTPRIDEALKLL 280
Cdd:PRK03379 237 WFERASPRIILAAQQL 252
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ChuT |
COG4558 |
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ... |
1-288 |
1.32e-72 |
|
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443619 [Multi-domain] Cd Length: 285 Bit Score: 224.69 E-value: 1.32e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143559383 1 MRRFRLYLIGLLICLFIVGCnpskeSTTSDESYRIISLMPSNTEILYALDLGTSVVGVTDQDDYPKDVQSLPQF-NTYEL 79
Cdd:COG4558 1 MKRLALALLLLALAALAAGA-----SVAAAAAERIVSLGGSVTEIVYALGAGDRLVGVDTTSTYPAAAKALPDVgYMRQL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143559383 80 NAEALLKLKPTHIVTHEIAYPTQqkVLDQLKKEGVEIITVDDATTIDEVYDTFNQVATPFDRTDKSEQLVEETKSQVQAV 159
Cdd:COG4558 76 SAEGILSLKPTLVLASEGAGPPE--VLDQLRAAGVPVVVVPAAPSLEGVLAKIRAVAAALGVPEAGEALAARLEADLAAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143559383 160 LDDIPSSDTMTRVYYEVSLEPERYT-SGSETLHHDMIAQLKAKNIYEDLKGWQSIALESLIEKNPDIYLHASDITEEDL- 237
Cdd:COG4558 154 AARVAAIGKPPRVLFLLSRGGGRPMvAGRGTAADALIRLAGGVNAAAGFEGYKPLSAEALIAAAPDVILVMTRGLESLGg 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1143559383 238 MNDIQGNKALKKIKAVQNDKVYVLDPDILNRPTPRIDEALKLLRDHIYEAS 288
Cdd:COG4558 234 VDGLLALPGLAQTPAGKNKRIVAMDDLLLLGFGPRTPQAALALAQALYPAA 284
|
|
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
34-285 |
2.52e-58 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 187.51 E-value: 2.52e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143559383 34 RIISLMPSNTEILYALDLGTSVVGVTDQ--DDYPK-DVQSLPQF-NTYELNAEALLKLKPTHIVTHeiAYPTQQKVLDQL 109
Cdd:COG0614 2 RIVSLSPSATELLLALGAGDRLVGVSDWgyCDYPElELKDLPVVgGTGEPNLEAILALKPDLVLAS--SSGNDEEDYEQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143559383 110 KKEGVEIITVDdATTIDEVYDTFNQVATPFDRTDKSEQLVEETKSQVQAVLDDIPSSDTMTRVYYEVSLEPERYTSGSET 189
Cdd:COG0614 80 EKIGIPVVVLD-PRSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGAEERPTVLYEIWSGDPLYTAGGGS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143559383 190 LHHDMIAQLKAKNIYEDLK-GWQSIALESLIEKNPDIYLHAS----DITEEDLMNDIQGNKALKKIKAVQNDKVYVLDPD 264
Cdd:COG0614 159 FIGELLELAGGRNVAADLGgGYPEVSLEQVLALDPDVIILSGggydAETAEEALEALLADPGWQSLPAVKNGRVYVVPGD 238
|
250 260
....*....|....*....|.
gi 1143559383 265 ILNRPTPRIDEALKLLRDHIY 285
Cdd:COG0614 239 LLSRPGPRLLLALEDLAKALH 259
|
|
| YvrC |
cd01143 |
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ... |
34-225 |
2.75e-52 |
|
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: 169.38 E-value: 2.75e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143559383 34 RIISLMPSNTEILYALDLGTSVVGVTDQDDYPKDVQSLPQFNTY-ELNAEALLKLKPTHIVTHEIAYPTqqkVLDQLKKE 112
Cdd:cd01143 5 RIVSLSPSITEILFALGAGDKIVGVDTYSNYPKEVRKKPKVGSYsNPNVEKIVALKPDLVIVSSSSLAE---LLEKLKDA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143559383 113 GVEIITVDDATTIDEVYDTFNQVATPFDRTDKSEQLVEETKSQVQAVLDDIPSSDTMTrVYYEVSLEPErYTSGSETLHH 192
Cdd:cd01143 82 GIPVVVLPAASSLDEIYDQIELIGKITGAEEEAEKLVKEMKQKIDKVKDKGKTIKKSK-VYIEVSLGGP-YTAGKNTFIN 159
|
170 180 190
....*....|....*....|....*....|...
gi 1143559383 193 DMIAQLKAKNIYEDLKGWQSIALESLIEKNPDI 225
Cdd:cd01143 160 ELIRLAGAKNIAADSGGWPQVSPEEILKANPDV 192
|
|
| BtuF |
cd01144 |
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ... |
34-280 |
9.95e-52 |
|
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: 169.79 E-value: 9.95e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143559383 34 RIISLMPSNTEILYALDLGTSVVGVTDQDDYPKDVQSLPQF-NTYELNAEALLKLKPTHIVTHEIAYPtqQKVLDQLKKE 112
Cdd:cd01144 2 RIVSLAPSATELLYALGLGDQLVGVTDYCDYPPEAKKLPRVgGFYQLDLERVLALKPDLVIAWDDCNV--CAVVDQLRAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143559383 113 GVEIItVDDATTIDEVYDTFNQVATPFDRTDKSEQLVEETKSQVQAVLDDiPSSDTMTRVYYEVSLEPeRYTSGSETLhH 192
Cdd:cd01144 80 GIPVL-VSEPQTLDDILADIRRLGTLAGRPARAEELAEALRRRLAALRKQ-YASKPPPRVFYQEWIDP-LMTAGGDWV-P 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143559383 193 DMIAQLKAKNIYEDL-KGWQSIALESLIEKNPDIYL---HASDITEEDLmndiQGNKALKKIKAVQNDKVYVLDPDILNR 268
Cdd:cd01144 156 ELIALAGGVNVFADAgERSPQVSWEDVLAANPDVIVlspCGFGFTPAIL----RKEPAWQALPAVRNGRVYAVDGNWYFR 231
|
250
....*....|..
gi 1143559383 269 PTPRIDEALKLL 280
Cdd:cd01144 232 PSPRLVDGLEQL 243
|
|
| HutB |
cd01149 |
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ... |
34-263 |
2.57e-35 |
|
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: 127.00 E-value: 2.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143559383 34 RIISLMPSNTEILYALDLGTSVVGVTDQDDYPKDVQSLPQFnTY--ELNAEALLKLKPTHIVTHEIAYPTQqkVLDQLKK 111
Cdd:cd01149 3 RIVSLGGSVTEIVYALGAGDRLVGVDSTSTYPEAAAKLPDV-GYmrQLSAEGVLSLKPTLVIASDEAGPPE--ALDQLRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143559383 112 EGVEIITVDDATTIDEVYDTFNQVATPFDRTDKSEQLVEETKSQVQAVLDDIPSSDTMTRVYYEVSLEPER-YTSGSETL 190
Cdd:cd01149 80 AGVPVVTVPSTPTLDGLLTKIRQVAQALGVPEKGEALAQEVRQRLAALRKTVAAHKKPPRVLFLLSHGGGAaMAAGRNTA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1143559383 191 HHDMIAQLKAKNIYEDLKGWQSIALESLIEKNPDIYLhasdITEEDLMNDIqGNKALKKIKAV------QNDKVYVLDP 263
Cdd:cd01149 160 ADAIIALAGAVNAAAGFRGYKPLSAEALIAAQPDVIL----VMSRGLDAVG-GVDGLLKLPGLaqtpagRNKRILAMDD 233
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
36-264 |
8.33e-30 |
|
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: 112.46 E-value: 8.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143559383 36 ISLMPSNTEILYALDLGTSVVGVTDQDDYP---KDVQSLPQFNTY-ELNAEALLKLKPTHIVtheIAYPTQQKVLDQLKK 111
Cdd:pfam01497 1 AALSPAYTEILYALGATDSIVGVDAYTRDPlkaDAVAAIVKVGAYgEINVERLAALKPDLVI---LSTGYLTDEAEELLS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143559383 112 EGVEIITVDDATTIDEVYDTFNQVATPFDRTDKSEQLVEETKSQVQAVLDDIPSSDTMTRVYYEVSLEPERYTSGSETLH 191
Cdd:pfam01497 78 LIIPTVIFESSSTGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPVLVFGGADGGGYVVAGSNTYI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1143559383 192 HDMIAQLKAKNIYEDLKGWQS--IALESLIEKNPDIYLHASDITEEDLMND-IQGNKALKKIKAVQNDKVYVLDPD 264
Cdd:pfam01497 158 GDLLRILGIENIAAELSGSEYapISFEAILSSNPDVIIVSGRDSFTKTGPEfVAANPLWAGLPAVKNGRVYTLPSD 233
|
|
| TroA_a |
cd01148 |
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ... |
34-279 |
4.32e-28 |
|
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: 109.35 E-value: 4.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143559383 34 RIISLMPSNTEILYALDLGTSVVGVT--DQDDYP---KDVQSLPQFNTYELNAEALLKLKPtHIVTHEIAYPTQQKVL-- 106
Cdd:cd01148 20 RVVSNDQNTTEMMLALGLQDRMVGTAgiDNKDLPelkAKYDKVPELAKKYPSKETVLAARP-DLVFGGWSYGFDKGGLgt 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143559383 107 -DQLKKEGVEI-------ITVDDATTIDEVYDTFNQVATPFDRTDKSEQLVEETKSQVQAVLDDIPSSDTMTRVYYEVSL 178
Cdd:cd01148 99 pDSLAELGIKTyilpescGQRRGEATLDDVYNDIRNLGKIFDVEDRADKLVADLKARLAEISAKVKGDGKKVAVFVYDSG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143559383 179 EPERYTSGSETLHHDMIAQLKAKNIYEDLK-GWQSIALESLIEKNPD--IYLHASDITE-EDLMNDIQGNKALKKIKAVQ 254
Cdd:cd01148 179 EDKPFTSGRGGIPNAIITAAGGRNVFADVDeSWTTVSWETVIARNPDviVIIDYGDQNAaEQKIKFLKENPALKNVPAVK 258
|
250 260
....*....|....*....|....*
gi 1143559383 255 NDKVYVLDPDILNRPTPRIDEALKL 279
Cdd:cd01148 259 NNRFIVLPLAEATPGIRNVDAIEKL 283
|
|
| FhuD |
cd01146 |
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ... |
34-265 |
3.04e-21 |
|
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: 90.04 E-value: 3.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143559383 34 RIISLMPSNTEILyaLDLGTSVVGVTDQDDYPKDVQSLPQF--------NTYELNAEALLKLKPTHIVtheIAYPTQQKV 105
Cdd:cd01146 5 RIVALDWGALETL--LALGVKPVGVADTAGYKPWIPEPALPlegvvdvgTRGQPNLEAIAALKPDLIL---GSASRHDEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143559383 106 LDQLKKegveI---ITVDDATTIDEVYDTFNQVATPFDRTDKSEQLVEETKSQVQAVLDDIPSSDTmTRVYYeVSLEPER 182
Cdd:cd01146 80 YDQLSQ----IaptVLLDSSPWLAEWKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKLPDKGP-KPVSV-VRFSDAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143559383 183 YTS--GSETLHHDMIAQLKAKNIYE----DLKGWQSIALESLIEKNPDIyLHASDITEEDLMNDIQGNKALKKIKAVQND 256
Cdd:cd01146 154 SIRlyGPNSFAGSVLEDLGLQNPWAqettNDSGFATISLERLAKADADV-LFVFTYEDEELAQALQANPLWQNLPAVKNG 232
|
....*....
gi 1143559383 257 KVYVLDPDI 265
Cdd:cd01146 233 RVYVVDDVW 241
|
|
| PRK03379 |
PRK03379 |
vitamin B12-transporter protein BtuF; Provisional |
34-280 |
2.32e-20 |
|
vitamin B12-transporter protein BtuF; Provisional
Pssm-ID: 179575 [Multi-domain] Cd Length: 260 Bit Score: 87.82 E-value: 2.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143559383 34 RIISLMPSNTEILYALDLGTsvVGVTDQDDYPKDVQSLPQFNTYE-LNAEALLKLKPTHIVTHEIAYPtqQKVLDQLKKE 112
Cdd:PRK03379 19 RVITLSPANTELAFAAGITP--VGVSSYSDYPPQAKKIEQVATWQgMNLERIVALKPDLVLAWRGGNA--ERQVDQLASL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143559383 113 GVEIITVdDATTIDEVYDTFNQVATPFDRTDKSEQLVEETKSQVQAVLDDIPSSdTMTRVYYEVSLEPeRYTSGSETLHH 192
Cdd:PRK03379 95 GIKVMWV-DATSIEQIANALRQLAPWSPQPEKAEQAAQSLLQQYAALKAQYADK-PKKRVFLQFGTNP-LFTSGKHSIQS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143559383 193 DMIAQLKAKNIYEDLK-GWQSIALESLIEKNPDIYLhasditeedlmndIQGNKalKKIKAVQ-------NDKVYVLDPD 264
Cdd:PRK03379 172 QVLSLCGGENIFADSRvPWPQVSREQVLARKPQAIV-------------ITGGP--DQIPKIKqfwgpqlKIPVIPLNSD 236
|
250
....*....|....*.
gi 1143559383 265 ILNRPTPRIDEALKLL 280
Cdd:PRK03379 237 WFERASPRIILAAQQL 252
|
|
| FecB |
COG4594 |
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ... |
1-268 |
4.28e-18 |
|
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443650 [Multi-domain] Cd Length: 316 Bit Score: 82.66 E-value: 4.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143559383 1 MRRFRLYLIGLLICLFIVGC----NPSKESTTSDESY----------------RIISLMPSNTEILyaLDLGTSVVGVTD 60
Cdd:COG4594 1 MKKLLLLLILLLALLLLAACgsssSDSSSSEAAAGARtvkhamgettipgtpkRVVVLEWSFADAL--LALGVTPVGIAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143559383 61 QDDYPKDVQSLPQF--------NTYELNAEALLKLKPTHIVT----HEiayptqqKVLDQLKKegveiItvddATTI--- 125
Cdd:COG4594 79 DNDYDRWVPYLRDLikgvtsvgTRSQPNLEAIAALKPDLIIAdksrHE-------AIYDQLSK-----I----APTVlfk 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143559383 126 ------DEVYDTFNQVATPFDRTDKSEQLVEETKSQVQAVLDDIPSSDTMTRVYYEVSLEPERYTSGSETLHHDMIAQLK 199
Cdd:COG4594 143 srngdyQENLESFKTIAKALGKEEEAEAVLADHDQRIAEAKAKLAAADKGKKVAVGQFRADGLRLYTPNSFAGSVLAALG 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1143559383 200 AKNIYEDLK----GWQSIALESLIEKNPDIYLHASDiTEEDLMNDIQGNKALKKIKAVQNDKVYVLDPDILNR 268
Cdd:COG4594 223 FENPPKQSKdngyGYSEVSLEQLPALDPDVLFIATY-DDPSILKEWKNNPLWKNLKAVKNGRVYEVDGDLWTR 294
|
|
| TroA-like |
cd00636 |
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ... |
34-174 |
5.56e-18 |
|
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: 78.75 E-value: 5.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143559383 34 RIISLMPSNTEILYALDLGTSVVGVTDQDDYPKDVQSLPQ-----FNTYELNAEALLKLKPTHIVTHEIAYPtqqKVLDQ 108
Cdd:cd00636 2 RVVALDPGATELLLALGGDDKPVGVADPSGYPPEAKALLEkvpdvGHGYEPNLEKIAALKPDLIIANGSGLE---AWLDK 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1143559383 109 LKKEGVEIITVDDAT--TIDEVYDTFNQVATPFDRTDKSEQLVEETKSQVQAVLDDIPSSDTMTRVYY 174
Cdd:cd00636 79 LSKIAIPVVVVDEASelSLENIKESIRLIGKALGKEENAEELIAELDARLAELRAKLAKIPKKKVSLV 146
|
|
| TroA_e |
cd01142 |
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ... |
30-260 |
2.11e-16 |
|
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: 77.39 E-value: 2.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143559383 30 DESYRIISLMPSNTEILYALDLGTSVVG----VTDQDDYPKDVQSLPQFNTY----ELNAEALLKLKPTHIVTheIAYPT 101
Cdd:cd01142 22 DEVKRIAALWGAGNAVVAALGGGKLIVAttstVQQEPWLYRLAPSLENVATGgtgnDVNIEELLALKPDVVIV--WSTDG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143559383 102 QQKVLDQLKKEGVEIItvdDATTIDEVYDTFNQVATPFDRTDKSEQLV---EETKSQVQAVLDDIPSSDTMtRVYYE--V 176
Cdd:cd01142 100 KEAGKAVLRLLNALSL---RDAELEEVKLTIALLGELLGRQEKAEALVayfDDNLAYVAARTKKLPDSERP-RVYYAgpD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143559383 177 SLEperyTSGSETLHHDMIAQLKAKNIYEDL--KGWQSIALESLIEKNPDIYLHASDITEEDLMNDiqgnKALKKIKAVQ 254
Cdd:cd01142 176 PLT----TDGTGSITNSWIDLAGGINVASEAtkKGSGEVSLEQLLKWNPDVIIVGNADTKAAILAD----PRWQNLRAVK 247
|
....*.
gi 1143559383 255 NDKVYV 260
Cdd:cd01142 248 NGRVYV 253
|
|
| FatB |
cd01140 |
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ... |
40-264 |
1.24e-14 |
|
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: 71.91 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143559383 40 PSNTEILYALD---------LGTSVVGVTDQDDYP---KDVQSLPQFNT---YELNAEALLKLKPTHIvtheIAYPTQQK 104
Cdd:cd01140 9 PKNPEKVVVFDvgaldtldaLGVKVVGVPKSSTLPeylKKYKDDKYANVgtlFEPDLEAIAALKPDLI----IIGGRLAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143559383 105 VLDQLKKE-GVEIITVDDATTIDEVYDTFNQVATPFDRTDKSEQLVEETKSQVQAVLDDIPSSDTMTRVYY---EVSLep 180
Cdd:cd01140 85 KYDELKKIaPTIDLGADLKNYLESVKQNIETLGKIFGKEEEAKELVAEIDASIAEAKSAAKGKKKALVVLVnggKLSA-- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143559383 181 erYTSGSET--LHHDmiaqLKAKNIYEDLKG---WQSIALESLIEKNPDIYL---------HASDITEEDLMNDIqgnka 246
Cdd:cd01140 163 --FGPGSRFgwLHDL----LGFEPADENIKAsshGQPVSFEYILEANPDWLFvidrgaaigAEGSSAKEVLDNDL----- 231
|
250
....*....|....*...
gi 1143559383 247 LKKIKAVQNDKVYVLDPD 264
Cdd:cd01140 232 VKNTTAWKNGKVIYLDPD 249
|
|
| HemV-2 |
cd01147 |
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ... |
34-261 |
1.53e-14 |
|
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: 71.60 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143559383 34 RIISLMPSNTEILYALDLGTSVVGVTDQDD---------YPKDVQSLPQFNT----YELNAEALLKLKPTHIVTHEIAYP 100
Cdd:cd01147 7 RVVAAGPGALRLLYALAAPDKIVGVDDAEKsdegrpyflASPELKDLPVIGRggrgNTPNYEKIAALKPDVVIDVGSDDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143559383 101 TqqKVLDQL-KKEGVEIITVDDATTIDEVYDTFNQVATPFDRTDKSEQLV---EETKSQVQAVLDDIPSSDtMTRVYYEV 176
Cdd:cd01147 87 T--SIADDLqKKTGIPVVVLDGGDSLEDTPEQIRLLGKVLGKEERAEELIsfiESILADVEERTKDIPDEE-KPTVYFGR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143559383 177 SLE--PERYTSGSETLhHDMIAQLKAKNIYEDLKGWQSIAL--ESLIEKNPDIYLHASDITEEDLMNDIQGNKALKKIKA 252
Cdd:cd01147 164 IGTkgAAGLESGLAGS-IEVFELAGGINVADGLGGGGLKEVspEQILLWNPDVIFLDTGSFYLSLEGYAKNRPFWQSLKA 242
|
....*....
gi 1143559383 253 VQNDKVYVL 261
Cdd:cd01147 243 VKNGRVYLL 251
|
|
| FeuA |
cd01138 |
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ... |
34-264 |
7.56e-14 |
|
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: 69.67 E-value: 7.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143559383 34 RIISLmpSNTEILYALdLGTSVVGVTDQD----DYPKDVQSLPQFNTYELNAEALLKLKPTHIvtheIAYPTQQKVLDQL 109
Cdd:cd01138 11 RIVAL--SGETEGLAL-LGIKPVGAASIGgknpYYKKKTLAKVVGIVDEPNLEKVLELKPDLI----IVSSKQEENYEKL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143559383 110 KKEGVEIITVDDATTIDEVYDTFNQVatpFDRTDKSE-------QLVEETKSQVQAVLDDIpSSDTMTRVYYEVSLEPER 182
Cdd:cd01138 84 SKIAPTVPVSYNSSDWEEQLKEIGKL---LNKEDEAEkwladykQKAKEAKEKIKKKLGND-KSVAVLRGRKQIYVFGED 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143559383 183 YTSGSETLHHDMiaQLKAKNIYEDL---KGWQSIALESLIEKNPDiYLHASDITEEDLMNDIQGNKALKKIKAVQNDKVY 259
Cdd:cd01138 160 GRGGGPILYADL--GLKAPEKVKEIedkPGYAAISLEVLPEFDAD-YIFLLFFTGPEAKADFESLPIWKNLPAVKNNHVY 236
|
....*
gi 1143559383 260 VLDPD 264
Cdd:cd01138 237 IVDAW 241
|
|
| btuF |
PRK09534 |
corrinoid ABC transporter substrate-binding protein; Reviewed |
25-287 |
1.53e-11 |
|
corrinoid ABC transporter substrate-binding protein; Reviewed
Pssm-ID: 236552 [Multi-domain] Cd Length: 359 Bit Score: 63.77 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143559383 25 ESTTSDESYRIISLMPSNTEILYALDLGTSVVGVTDQDDYPKDVQS---LPQFNTYELNAEALLKLKPTHIVTHEIAYPT 101
Cdd:PRK09534 53 EITLDERPERVVTLNPSAAQTMWELGARDRVVGVTQYASYLDGAEErtnVSGGQPFGVNVEAVVGLDPDLVLAPNAVAGD 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143559383 102 qqkVLDQLKKEGVEIITVDDATTIDEVYDTFNQVATPFDRTDKSEQLVEETKSQVQAVLDDIPSSDTMTRVYYEVSlepE 181
Cdd:PRK09534 133 ---TVTRLREAGITVFHFPAATSIEDVAEKTATIGRLTGNCEAAAETNAEMRDRVDAVEDRTADVDDRPRVLYPLG---D 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143559383 182 RYTSGSETLHHDMIAQLKAKNIYED--LKGWQSIALESLIEKNPDIYLHASDITEedlmndIQGNKALKKIKAVQNDKVY 259
Cdd:PRK09534 207 GYTAGGNTFIGALIEAAGGHNVAADatTDGYPQLSEEVIVQQDPDVIVVATASAL------VAETEPYASTTAGETGNVV 280
|
250 260
....*....|....*....|....*...
gi 1143559383 260 VLDPDILNRPTPRIDEALKLLRDHIYEA 287
Cdd:PRK09534 281 TVNVNHINQPAPRIVESMATMATAFHNT 308
|
|
| TroA_d |
cd01141 |
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ... |
34-124 |
1.26e-05 |
|
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: 44.72 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143559383 34 RIISLMPSNTEILYALDLGTSVVGVTDQDDYPK--DVQSLPQF---NTYELNAEALLKLKPTHIVTHEIAYPtqQKVLDQ 108
Cdd:cd01141 10 RIVVLSPTHVDLLLALDKADKIVGVSASAYDLNtpAVKERIDIqvgPTGSLNVELIVALKPDLVILYGGFQA--QTILDK 87
|
90
....*....|....*.
gi 1143559383 109 LKKEGVEIITVDDATT 124
Cdd:cd01141 88 LEQLGIPVLYVNEYPS 103
|
|
| |
