|
Name |
Accession |
Description |
Interval |
E-value |
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
75-331 |
8.18e-74 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 228.73 E-value: 8.18e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 75 RIVSTSPAETEILFALGLENRIVVVSD--YDDYPE-AAKAKPKIGGVVKPNEEAILAQTPDMVVGGIS-MEKPVADKLKS 150
Cdd:COG0614 2 RIVSLSPSATELLLALGAGDRLVGVSDwgYCDYPElELKDLPVVGGTGEPNLEAILALKPDLVLASSSgNDEEDYEQLEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 151 LGMPVYITHPTKMDDILNNVLAMGVITNKQEQAEKVVAQMKKDIAYVQEAVKnvKPEEKKKVYLEFSPG---WTVGKGEF 227
Cdd:COG0614 82 IGIPVVVLDPRSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLA--GAEERPTVLYEIWSGdplYTAGGGSF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 228 MDELITLAGATNIASDT-QGWNPISEEKILQNDPEVILYASGITDEKTGVKLEDMIAKRNGWDKMKAIREKQIFGMDQNI 306
Cdd:COG0614 160 IGELLELAGGRNVAADLgGGYPEVSLEQVLALDPDVIILSGGGYDAETAEEALEALLADPGWQSLPAVKNGRVYVVPGDL 239
|
250 260
....*....|....*....|....*
gi 1032348493 307 LSRPGPRITQGLIEVAKAIYPDLVK 331
Cdd:COG0614 240 LSRPGPRLLLALEDLAKALHPELFA 264
|
|
| YvrC |
cd01143 |
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ... |
71-265 |
1.88e-67 |
|
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: 209.83 E-value: 1.88e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 71 KAPERIVSTSPAETEILFALGLENRIVVVSDYDDYPEAAKAKPKIGGVVKPNEEAILAQTPDMVVGGISMEKPVADKLKS 150
Cdd:cd01143 1 KEPERIVSLSPSITEILFALGAGDKIVGVDTYSNYPKEVRKKPKVGSYSNPNVEKIVALKPDLVIVSSSSLAELLEKLKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 151 LGMPVYITH-PTKMDDILNNVLAMGVITNKQEQAEKVVAQMKKDIAYVQEAVKNVKpeeKKKVYLEFSPG--WTVGKGEF 227
Cdd:cd01143 81 AGIPVVVLPaASSLDEIYDQIELIGKITGAEEEAEKLVKEMKQKIDKVKDKGKTIK---KSKVYIEVSLGgpYTAGKNTF 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 1032348493 228 MDELITLAGATNIASDTQGWNPISEEKILQNDPEVILY 265
Cdd:cd01143 158 INELIRLAGAKNIAADSGGWPQVSPEEILKANPDVIIL 195
|
|
| peripla_PGF_1 |
TIGR04281 |
putative ABC transporter PGF-CTERM-modified substrate-binding protein; Members of this ... |
54-328 |
4.19e-50 |
|
putative ABC transporter PGF-CTERM-modified substrate-binding protein; Members of this archaeal protein family resemble periplasmic substrate-binding proteins of ABC transporters and appear in gene neighborhoods with permease and ATP-binding cassette proteins. Notably, essentially all members also have the PGF-CTERM putative protein-sorting domain at the C-terminus, while more distant homologs (excluded by the trusted cutoff) instead have what appear to be lipoprotein signal peptides at the N-terminus.
Pssm-ID: 275101 [Multi-domain] Cd Length: 330 Bit Score: 169.46 E-value: 4.19e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 54 TYPLTVKDATGKEVTFAKAPERIVSTSPAETEILFALGLENRIVVVSDYDDYPEAAKAKPKIGGV--VKPNEEAILAQTP 131
Cdd:TIGR04281 2 EFPVTETDATGTEVTLEEEPERVVTLNPSAAQTMWEIGARDKVVGVSQYTDYLDGADERTNVSGDdgLTVNVEAVVDLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 132 DMVVGGISMEKPVADKLKSLGMPVY-ITHPTKMDDILNNVLAMGVITNKQEQAEKVVAQMKKDIAYVQEAVKNvkpEEKK 210
Cdd:TIGR04281 82 DLVLAPNTANDDTVEQLRDAGLTVYvFPAATSIDDVAEKTETTGRLTGECEGAAETVDWMDDRLEAVEEALAD---EDRP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 211 KVYLEFSPGWTVGKGEFMDELITLAGATNIASDT--QGWNPISEEKILQNDPEVILYASGITdektgvkledmIAKRNGW 288
Cdd:TIGR04281 159 LVLYAMGDGYTAGSGTFIHDIITTAGGENVAAEAgiTGYPQISEEVVVEQDPEWIVYPDTAE-----------VPPTPAY 227
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1032348493 289 DKMKAIREKQIFGMDQNILSRPGPRITQGLIEVAKAIYPD 328
Cdd:TIGR04281 228 ESTTAVEEGNVVAVNANYLSQPAPRVVEAVETLAEAFHPE 267
|
|
| btuF |
PRK09534 |
corrinoid ABC transporter substrate-binding protein; Reviewed |
29-325 |
1.35e-35 |
|
corrinoid ABC transporter substrate-binding protein; Reviewed
Pssm-ID: 236552 [Multi-domain] Cd Length: 359 Bit Score: 132.34 E-value: 1.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 29 APGGqTSAPQTAPQENTAEQSAkqtTYPLTVKDATGKEVTFAKAPERIVSTSPAETEILFALGLENRIVVVSDYDDYPEA 108
Cdd:PRK09534 20 AAGG-ALAPAPAAQHADADRAC---SFPVTETDATGTEITLDERPERVVTLNPSAAQTMWELGARDRVVGVTQYASYLDG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 109 AKAKPKIGGV--VKPNEEAILAQTPDMVVGGISMEKPVADKLKSLGMPVY-ITHPTKMDDILNNVLAMGVITNKQEQAEK 185
Cdd:PRK09534 96 AEERTNVSGGqpFGVNVEAVVGLDPDLVLAPNAVAGDTVTRLREAGITVFhFPAATSIEDVAEKTATIGRLTGNCEAAAE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 186 VVAQMKKDIAYVQEAVKNVkpEEKKKVYLEFSPGWTVGKGEFMDELITLAGATNIASD--TQGWNPISEEKILQNDPEVI 263
Cdd:PRK09534 176 TNAEMRDRVDAVEDRTADV--DDRPRVLYPLGDGYTAGGNTFIGALIEAAGGHNVAADatTDGYPQLSEEVIVQQDPDVI 253
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1032348493 264 LYASGitdektgvklEDMIAKRNGWDKMKAIREKQIFGMDQNILSRPGPRITQGLIEVAKAI 325
Cdd:PRK09534 254 VVATA----------SALVAETEPYASTTAGETGNVVTVNVNHINQPAPRIVESMATMATAF 305
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
77-305 |
1.79e-29 |
|
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: 112.85 E-value: 1.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 77 VSTSPAETEILFALGLENRIVVVSDYDDYPEAAK---AKPKIGGVVKPNEEAILAQTPDMVVGGISMEKPVADKLKSLGM 153
Cdd:pfam01497 1 AALSPAYTEILYALGATDSIVGVDAYTRDPLKADavaAIVKVGAYGEINVERLAALKPDLVILSTGYLTDEAEELLSLII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 154 PVYITHPTK-MDDILNNVLAMGVITNKQEQAEKVVAQMKKDIAYVQEAVKNVKPeeKKKVYLEFSPGWTV---GKGEFMD 229
Cdd:pfam01497 81 PTVIFESSStGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTR--KPVLVFGGADGGGYvvaGSNTYIG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1032348493 230 ELITLAGATNIASD--TQGWNPISEEKILQNDPEVILYASGITDEKTGVkleDMIAKRNGWDKMKAIREKQIFGMDQN 305
Cdd:pfam01497 159 DLLRILGIENIAAElsGSEYAPISFEAILSSNPDVIIVSGRDSFTKTGP---EFVAANPLWAGLPAVKNGRVYTLPSD 233
|
|
| PqiC |
COG3009 |
Intermembrane transporter PqiABC lipoprotein subunit PqiC [Cell wall/membrane/envelope ... |
1-42 |
4.15e-03 |
|
Intermembrane transporter PqiABC lipoprotein subunit PqiC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442246 [Multi-domain] Cd Length: 198 Bit Score: 37.66 E-value: 4.15e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1032348493 1 MKRSLRFMIPLLVAASLAGCAGNDNSQ----PAPGGQTSAPQTAPQ 42
Cdd:COG3009 1 MKRPLRLLLLLLLALLLAACASSPPTRyytlPPPAAPAAAAAAAAA 46
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
75-331 |
8.18e-74 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 228.73 E-value: 8.18e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 75 RIVSTSPAETEILFALGLENRIVVVSD--YDDYPE-AAKAKPKIGGVVKPNEEAILAQTPDMVVGGIS-MEKPVADKLKS 150
Cdd:COG0614 2 RIVSLSPSATELLLALGAGDRLVGVSDwgYCDYPElELKDLPVVGGTGEPNLEAILALKPDLVLASSSgNDEEDYEQLEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 151 LGMPVYITHPTKMDDILNNVLAMGVITNKQEQAEKVVAQMKKDIAYVQEAVKnvKPEEKKKVYLEFSPG---WTVGKGEF 227
Cdd:COG0614 82 IGIPVVVLDPRSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLA--GAEERPTVLYEIWSGdplYTAGGGSF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 228 MDELITLAGATNIASDT-QGWNPISEEKILQNDPEVILYASGITDEKTGVKLEDMIAKRNGWDKMKAIREKQIFGMDQNI 306
Cdd:COG0614 160 IGELLELAGGRNVAADLgGGYPEVSLEQVLALDPDVIILSGGGYDAETAEEALEALLADPGWQSLPAVKNGRVYVVPGDL 239
|
250 260
....*....|....*....|....*
gi 1032348493 307 LSRPGPRITQGLIEVAKAIYPDLVK 331
Cdd:COG0614 240 LSRPGPRLLLALEDLAKALHPELFA 264
|
|
| YvrC |
cd01143 |
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ... |
71-265 |
1.88e-67 |
|
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: 209.83 E-value: 1.88e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 71 KAPERIVSTSPAETEILFALGLENRIVVVSDYDDYPEAAKAKPKIGGVVKPNEEAILAQTPDMVVGGISMEKPVADKLKS 150
Cdd:cd01143 1 KEPERIVSLSPSITEILFALGAGDKIVGVDTYSNYPKEVRKKPKVGSYSNPNVEKIVALKPDLVIVSSSSLAELLEKLKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 151 LGMPVYITH-PTKMDDILNNVLAMGVITNKQEQAEKVVAQMKKDIAYVQEAVKNVKpeeKKKVYLEFSPG--WTVGKGEF 227
Cdd:cd01143 81 AGIPVVVLPaASSLDEIYDQIELIGKITGAEEEAEKLVKEMKQKIDKVKDKGKTIK---KSKVYIEVSLGgpYTAGKNTF 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 1032348493 228 MDELITLAGATNIASDTQGWNPISEEKILQNDPEVILY 265
Cdd:cd01143 158 INELIRLAGAKNIAADSGGWPQVSPEEILKANPDVIIL 195
|
|
| BtuF |
cd01144 |
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ... |
74-318 |
1.14e-55 |
|
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: 181.34 E-value: 1.14e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 74 ERIVSTSPAETEILFALGLENRIVVVSDYDDYPEAAKAKPKIGGVVKPNEEAILAQTPDMVVGGISMEKP-VADKLKSLG 152
Cdd:cd01144 1 MRIVSLAPSATELLYALGLGDQLVGVTDYCDYPPEAKKLPRVGGFYQLDLERVLALKPDLVIAWDDCNVCaVVDQLRAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 153 MPVYITHPTKMDDILNNVLAMGVITNKQEQAEKVVAQMKKDIAYVQEAVKNVKPeekKKVYLEFS--PGWTVGkGEFMDE 230
Cdd:cd01144 81 IPVLVSEPQTLDDILADIRRLGTLAGRPARAEELAEALRRRLAALRKQYASKPP---PRVFYQEWidPLMTAG-GDWVPE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 231 LITLAGATNIASDT-QGWNPISEEKILQNDPEVILyasgITDEKTGVKLEDmIAKRNGWDKMKAIREKQIFGMDQNILSR 309
Cdd:cd01144 157 LIALAGGVNVFADAgERSPQVSWEDVLAANPDVIV----LSPCGFGFTPAI-LRKEPAWQALPAVRNGRVYAVDGNWYFR 231
|
....*....
gi 1032348493 310 PGPRITQGL 318
Cdd:cd01144 232 PSPRLVDGL 240
|
|
| ChuT |
COG4558 |
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ... |
68-329 |
1.27e-55 |
|
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443619 [Multi-domain] Cd Length: 285 Bit Score: 182.31 E-value: 1.27e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 68 TFAKAPERIVSTSPAETEILFALGLENRIVVVSDYDDYPEAAKAKPKIGGVVKPNEEAILAQTPDMVVGGISMEKP-VAD 146
Cdd:COG4558 22 VAAAAAERIVSLGGSVTEIVYALGAGDRLVGVDTTSTYPAAAKALPDVGYMRQLSAEGILSLKPTLVLASEGAGPPeVLD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 147 KLKSLGMPVY-ITHPTKMDDILNNVLAMGVITNKQEQAEKVVAQMKKDIAYVQEAVKNVKpeEKKKVYLEFSPGWTV--- 222
Cdd:COG4558 102 QLRAAGVPVVvVPAAPSLEGVLAKIRAVAAALGVPEAGEALAARLEADLAALAARVAAIG--KPPRVLFLLSRGGGRpmv 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 223 -GKGEFMDELITLAGATNIASDTQGWNPISEEKILQNDPEVILYASGITDEKTGVkleDMIAKRNGWDKMKAIREKQIFG 301
Cdd:COG4558 180 aGRGTAADALIRLAGGVNAAAGFEGYKPLSAEALIAAAPDVILVMTRGLESLGGV---DGLLALPGLAQTPAGKNKRIVA 256
|
250 260
....*....|....*....|....*...
gi 1032348493 302 MDQNILSRPGPRITQGLIEVAKAIYPDL 329
Cdd:COG4558 257 MDDLLLLGFGPRTPQAALALAQALYPAA 284
|
|
| peripla_PGF_1 |
TIGR04281 |
putative ABC transporter PGF-CTERM-modified substrate-binding protein; Members of this ... |
54-328 |
4.19e-50 |
|
putative ABC transporter PGF-CTERM-modified substrate-binding protein; Members of this archaeal protein family resemble periplasmic substrate-binding proteins of ABC transporters and appear in gene neighborhoods with permease and ATP-binding cassette proteins. Notably, essentially all members also have the PGF-CTERM putative protein-sorting domain at the C-terminus, while more distant homologs (excluded by the trusted cutoff) instead have what appear to be lipoprotein signal peptides at the N-terminus.
Pssm-ID: 275101 [Multi-domain] Cd Length: 330 Bit Score: 169.46 E-value: 4.19e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 54 TYPLTVKDATGKEVTFAKAPERIVSTSPAETEILFALGLENRIVVVSDYDDYPEAAKAKPKIGGV--VKPNEEAILAQTP 131
Cdd:TIGR04281 2 EFPVTETDATGTEVTLEEEPERVVTLNPSAAQTMWEIGARDKVVGVSQYTDYLDGADERTNVSGDdgLTVNVEAVVDLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 132 DMVVGGISMEKPVADKLKSLGMPVY-ITHPTKMDDILNNVLAMGVITNKQEQAEKVVAQMKKDIAYVQEAVKNvkpEEKK 210
Cdd:TIGR04281 82 DLVLAPNTANDDTVEQLRDAGLTVYvFPAATSIDDVAEKTETTGRLTGECEGAAETVDWMDDRLEAVEEALAD---EDRP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 211 KVYLEFSPGWTVGKGEFMDELITLAGATNIASDT--QGWNPISEEKILQNDPEVILYASGITdektgvkledmIAKRNGW 288
Cdd:TIGR04281 159 LVLYAMGDGYTAGSGTFIHDIITTAGGENVAAEAgiTGYPQISEEVVVEQDPEWIVYPDTAE-----------VPPTPAY 227
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1032348493 289 DKMKAIREKQIFGMDQNILSRPGPRITQGLIEVAKAIYPD 328
Cdd:TIGR04281 228 ESTTAVEEGNVVAVNANYLSQPAPRVVEAVETLAEAFHPE 267
|
|
| TroA_a |
cd01148 |
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ... |
55-322 |
8.13e-40 |
|
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: 141.32 E-value: 8.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 55 YPLTVkDATGKEVTFAKAPERIVSTSPAETEILFALGLENRIVVVS--DYDDYPEAAKAKPKIGGVVK--PNEEAILAQT 130
Cdd:cd01148 1 YPLTV-ENCGRSVTFDKAPQRVVSNDQNTTEMMLALGLQDRMVGTAgiDNKDLPELKAKYDKVPELAKkyPSKETVLAAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 131 PDMVVGGIS--MEKPVA---DKLKSLGMPVYI--------THPTKMDDILNNVLAMGVITNKQEQAEKVVAQMKKDIAYV 197
Cdd:cd01148 80 PDLVFGGWSygFDKGGLgtpDSLAELGIKTYIlpescgqrRGEATLDDVYNDIRNLGKIFDVEDRADKLVADLKARLAEI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 198 QEAVKNVKPEEKKKVYLEFSPG-WTVGKGEFMDELITLAGATNIASD-TQGWNPISEEKILQNDPEVI-LYASGitDEKT 274
Cdd:cd01148 160 SAKVKGDGKKVAVFVYDSGEDKpFTSGRGGIPNAIITAAGGRNVFADvDESWTTVSWETVIARNPDVIvIIDYG--DQNA 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1032348493 275 GVKLEDMIAKRNGWDKMKAIREKQIFGMDQNILSrPGPRITQGLIEVA 322
Cdd:cd01148 238 AEQKIKFLKENPALKNVPAVKNNRFIVLPLAEAT-PGIRNVDAIEKLA 284
|
|
| btuF |
PRK09534 |
corrinoid ABC transporter substrate-binding protein; Reviewed |
29-325 |
1.35e-35 |
|
corrinoid ABC transporter substrate-binding protein; Reviewed
Pssm-ID: 236552 [Multi-domain] Cd Length: 359 Bit Score: 132.34 E-value: 1.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 29 APGGqTSAPQTAPQENTAEQSAkqtTYPLTVKDATGKEVTFAKAPERIVSTSPAETEILFALGLENRIVVVSDYDDYPEA 108
Cdd:PRK09534 20 AAGG-ALAPAPAAQHADADRAC---SFPVTETDATGTEITLDERPERVVTLNPSAAQTMWELGARDRVVGVTQYASYLDG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 109 AKAKPKIGGV--VKPNEEAILAQTPDMVVGGISMEKPVADKLKSLGMPVY-ITHPTKMDDILNNVLAMGVITNKQEQAEK 185
Cdd:PRK09534 96 AEERTNVSGGqpFGVNVEAVVGLDPDLVLAPNAVAGDTVTRLREAGITVFhFPAATSIEDVAEKTATIGRLTGNCEAAAE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 186 VVAQMKKDIAYVQEAVKNVkpEEKKKVYLEFSPGWTVGKGEFMDELITLAGATNIASD--TQGWNPISEEKILQNDPEVI 263
Cdd:PRK09534 176 TNAEMRDRVDAVEDRTADV--DDRPRVLYPLGDGYTAGGNTFIGALIEAAGGHNVAADatTDGYPQLSEEVIVQQDPDVI 253
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1032348493 264 LYASGitdektgvklEDMIAKRNGWDKMKAIREKQIFGMDQNILSRPGPRITQGLIEVAKAI 325
Cdd:PRK09534 254 VVATA----------SALVAETEPYASTTAGETGNVVTVNVNHINQPAPRIVESMATMATAF 305
|
|
| TroA_e |
cd01142 |
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ... |
58-331 |
1.45e-34 |
|
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: 127.86 E-value: 1.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 58 TVKDATGKEVTFAKAPERIVSTSPAETEILFALGLENRIVVVSD--------YDDYPEAAKAKPkIGGVVKPNEEAILAQ 129
Cdd:cd01142 9 TITDMAGRKVTIPDEVKRIAALWGAGNAVVAALGGGKLIVATTStvqqepwlYRLAPSLENVAT-GGTGNDVNIEELLAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 130 TPDMVVG----GISMEKPVADKLKSLGMPVyithpTKMDDILNNVLAMGVITNKQEQAEKVVAQMKKDIAYVQEAVKNVK 205
Cdd:cd01142 88 KPDVVIVwstdGKEAGKAVLRLLNALSLRD-----AELEEVKLTIALLGELLGRQEKAEALVAYFDDNLAYVAARTKKLP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 206 PEEKKKVYLEFSPGWTV-GKGEFMDELITLAGATNIASDTQ--GWNPISEEKILQNDPEVILYASGitDEKTGVKLEDMi 282
Cdd:cd01142 163 DSERPRVYYAGPDPLTTdGTGSITNSWIDLAGGINVASEATkkGSGEVSLEQLLKWNPDVIIVGNA--DTKAAILADPR- 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1032348493 283 akrngWDKMKAIREKQIFGMDQNILSRPGPRITQGL--IEVAKAIYPDLVK 331
Cdd:cd01142 240 -----WQNLRAVKNGRVYVNPEGAFWWDRPSAEEALlgLWLAKTLYPERFT 285
|
|
| HutB |
cd01149 |
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ... |
73-306 |
4.46e-30 |
|
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: 114.28 E-value: 4.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 73 PERIVSTSPAETEILFALGLENRIVVVSDYDDYPEAAKAKPKIGGVVKPNEEAILAQTPDMVVGGISMEKPVA-DKLKSL 151
Cdd:cd01149 1 PERIVSLGGSVTEIVYALGAGDRLVGVDSTSTYPEAAAKLPDVGYMRQLSAEGVLSLKPTLVIASDEAGPPEAlDQLRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 152 GMPVYI--THPTkMDDILNNVLAMGVITNKQEQAEKVVAQMKKDIAYVQeAVKNVKPEEKKKVYLEFSPGWTV---GKGE 226
Cdd:cd01149 81 GVPVVTvpSTPT-LDGLLTKIRQVAQALGVPEKGEALAQEVRQRLAALR-KTVAAHKKPPRVLFLLSHGGGAAmaaGRNT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 227 FMDELITLAGATNIASDTQGWNPISEEKILQNDPEVILYASGITDektGVKLEDMIAKRNGWDKMKAIREKQIFGMDQNI 306
Cdd:cd01149 159 AADAIIALAGAVNAAAGFRGYKPLSAEALIAAQPDVILVMSRGLD---AVGGVDGLLKLPGLAQTPAGRNKRILAMDDLL 235
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
77-305 |
1.79e-29 |
|
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: 112.85 E-value: 1.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 77 VSTSPAETEILFALGLENRIVVVSDYDDYPEAAK---AKPKIGGVVKPNEEAILAQTPDMVVGGISMEKPVADKLKSLGM 153
Cdd:pfam01497 1 AALSPAYTEILYALGATDSIVGVDAYTRDPLKADavaAIVKVGAYGEINVERLAALKPDLVILSTGYLTDEAEELLSLII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 154 PVYITHPTK-MDDILNNVLAMGVITNKQEQAEKVVAQMKKDIAYVQEAVKNVKPeeKKKVYLEFSPGWTV---GKGEFMD 229
Cdd:pfam01497 81 PTVIFESSStGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTR--KPVLVFGGADGGGYvvaGSNTYIG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1032348493 230 ELITLAGATNIASD--TQGWNPISEEKILQNDPEVILYASGITDEKTGVkleDMIAKRNGWDKMKAIREKQIFGMDQN 305
Cdd:pfam01497 159 DLLRILGIENIAAElsGSEYAPISFEAILSSNPDVIIVSGRDSFTKTGP---EFVAANPLWAGLPAVKNGRVYTLPSD 233
|
|
| PRK03379 |
PRK03379 |
vitamin B12-transporter protein BtuF; Provisional |
72-314 |
2.47e-28 |
|
vitamin B12-transporter protein BtuF; Provisional
Pssm-ID: 179575 [Multi-domain] Cd Length: 260 Bit Score: 110.54 E-value: 2.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 72 APERIVSTSPAETEILFALGLENriVVVSDYDDYPEAAKAKPKIGGVVKPNEEAILAQTPDMVV---GGiSMEKPVaDKL 148
Cdd:PRK03379 16 AAPRVITLSPANTELAFAAGITP--VGVSSYSDYPPQAKKIEQVATWQGMNLERIVALKPDLVLawrGG-NAERQV-DQL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 149 KSLGMPVYITHPTKMDDILNNVLAMGVITNKQEQAEKVVAQMKKDIAYVQEAVKNVKPeekKKVYLEF--SPGWTVGKGE 226
Cdd:PRK03379 92 ASLGIKVMWVDATSIEQIANALRQLAPWSPQPEKAEQAAQSLLQQYAALKAQYADKPK---KRVFLQFgtNPLFTSGKHS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 227 FMDELITLAGATNIASDTQ-GWNPISEEKILQNDPEVILYASGitdektgvklEDMIAK-RNGWDKMKAIrekQIFGMDQ 304
Cdd:PRK03379 169 IQSQVLSLCGGENIFADSRvPWPQVSREQVLARKPQAIVITGG----------PDQIPKiKQFWGPQLKI---PVIPLNS 235
|
250
....*....|
gi 1032348493 305 NILSRPGPRI 314
Cdd:PRK03379 236 DWFERASPRI 245
|
|
| HemV-2 |
cd01147 |
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ... |
74-302 |
8.32e-26 |
|
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: 103.57 E-value: 8.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 74 ERIVSTSPAETEILFALGLENRIVVVSDYDDYPEAA---------KAKPKIGGVVK---PNEEAILAQTPDMVV--GGIS 139
Cdd:cd01147 6 ERVVAAGPGALRLLYALAAPDKIVGVDDAEKSDEGRpyflaspelKDLPVIGRGGRgntPNYEKIAALKPDVVIdvGSDD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 140 MEKPVADKLKSLGMPV-YITHPTKMDDILNNVLAMGVITNKQEQAEKVVAQMKKDIAYVQEAVKNVKPEEKKKVYLEfsP 218
Cdd:cd01147 86 PTSIADDLQKKTGIPVvVLDGGDSLEDTPEQIRLLGKVLGKEERAEELISFIESILADVEERTKDIPDEEKPTVYFG--R 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 219 GWTVGKGEFM------DELITLAGATNIASDTQGWN--PISEEKILQNDPEVILyasgITDEKTGVKLEDMIAKRNGWDK 290
Cdd:cd01147 164 IGTKGAAGLEsglagsIEVFELAGGINVADGLGGGGlkEVSPEQILLWNPDVIF----LDTGSFYLSLEGYAKNRPFWQS 239
|
250
....*....|..
gi 1032348493 291 MKAIREKQIFGM 302
Cdd:cd01147 240 LKAVKNGRVYLL 251
|
|
| TroA_f |
cd01139 |
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ... |
57-331 |
7.56e-25 |
|
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: 102.77 E-value: 7.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 57 LTVKDATGKEVTFAKAPERIVStspAETEILFALGL------ENRIVVVSD-------------YDDYPEAAKAkPKIGG 117
Cdd:cd01139 1 ITVTDVAGRKVTLDAPVERVLL---GEGRQLYALALlegenpFARIVGWGGdlkkgdpdtyakyKEKFPEIADI-PLIGS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 118 VVKP--NEEAILAQTPDMVVGGISMEKPVAD-----KLKSLGMP-VYITHPTK-MDDILNNVLAMGVITNKQEQAEKVVA 188
Cdd:cd01139 77 TYNGdfSVEKVLTLKPDLVILNIWAKTTAEEsgileKLEQAGIPvVFVDFRQKpLKNTTPSMRLLGKALGREERAEEFIE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 189 QMKKDIAYVQEAVKNVKpEEKKKVYLEFSP------GWTVGKGEFmDELITLAGATNIASD----TQGwnPISEEKILQN 258
Cdd:cd01139 157 FYQERIDRIRDRLAKIN-EPKPKVFIELGAggpeecCSTYGNGNW-GELVDAAGGDNIADGlipgTSG--ELNAEYVIAA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 259 DPEVIL--------YASGITDEKTGVK------LEDMIAKRNGWDKMKAIREKQIFGMDQNILSRPGPRItqGLIEVAKA 324
Cdd:cd01139 233 NPEIIIatggnwakDPSGVSLGPDGTTadakesLLRALLKRPGWSSLQAVKNGRVYALWHQFYRSPYNFV--ALEAFAKW 310
|
....*..
gi 1032348493 325 IYPDLVK 331
Cdd:cd01139 311 LYPELFK 317
|
|
| TroA-like |
cd00636 |
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ... |
74-212 |
1.01e-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: 97.63 E-value: 1.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 74 ERIVSTSPAETEILFALGLENRIVVVSDYDDYPEAAKA----KPKIGGVVKPNEEAILAQTPDMVVGGISMEKPVADKLK 149
Cdd:cd00636 1 KRVVALDPGATELLLALGGDDKPVGVADPSGYPPEAKAllekVPDVGHGYEPNLEKIAALKPDLIIANGSGLEAWLDKLS 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1032348493 150 SLGMPVYITHPTK---MDDILNNVLAMGVITNKQEQAEKVVAQMKKDIAYVQEAVKNVKPEEKKKV 212
Cdd:cd00636 81 KIAIPVVVVDEASelsLENIKESIRLIGKALGKEENAEELIAELDARLAELRAKLAKIPKKKVSLV 146
|
|
| CeuA |
COG4607 |
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and ... |
1-325 |
8.66e-24 |
|
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443657 [Multi-domain] Cd Length: 310 Bit Score: 99.10 E-value: 8.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 1 MKRSLRFMIPLLVAASLAGCAGNDNSQPAPggqtSAPQTapqentaeqsakqttypLTVKDATGkEVTFAKAPERIVSTS 80
Cdd:COG4607 1 MKKTLLAALALAAALALAACGSSSAAAASA----AAAET-----------------VTVEHALG-TVEVPKNPKRVVVFD 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 81 PAETEILFALGLENRIVVVSDYDDYPEAAKAK--PKIGGVVKPNEEAILAQTPDMV-VGGISMEKpvADKLKSLGMPVYI 157
Cdd:COG4607 59 NGALDTLDALGVEVAGVPKGLLPDYLSKYADDkyANVGTLFEPDLEAIAALKPDLIiIGGRSAKK--YDELSKIAPTIDL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 158 THPTK--MDDILNNVLAMGVITNKQEQAEKVVAQMKKDIAYVQEAVKNvkpeeKKKVYL---------EFSPGWTVGkge 226
Cdd:COG4607 137 TVDGEdyLESLKRNTETLGEIFGKEDEAEELVADLDAKIAALKAAAAG-----KGTALIvltnggkisAYGPGSRFG--- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 227 FM-DEL-ITLAgATNIASDTQGwNPISEEKILQNDPEVILY---ASGITDEKTGVKLE---DMIAkrngwdKMKAIREKQ 298
Cdd:COG4607 209 PIhDVLgFKPA-DEDIEASTHG-QAISFEFIAEANPDWLFVidrDAAIGGEGPAAKQVldnELVK------QTTAWKNGQ 280
|
330 340 350
....*....|....*....|....*....|
gi 1032348493 299 IFGMDQNI--LSRPGPRITQGLI-EVAKAI 325
Cdd:COG4607 281 IVYLDPDAwyLAGGGIQSLTEMLdEVADAL 310
|
|
| FhuD |
cd01146 |
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ... |
71-312 |
3.40e-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: 96.20 E-value: 3.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 71 KAPERIVSTSPAETEILFALGLEnrIVVVSDYDDY-PEAAKAKPKIGGVVK------PNEEAILAQTPDMVVGGISMEKP 143
Cdd:cd01146 1 AKPQRIVALDWGALETLLALGVK--PVGVADTAGYkPWIPEPALPLEGVVDvgtrgqPNLEAIAALKPDLILGSASRHDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 144 VADKLKSLGMPVYITHPTKMDDILNNVLAMGVITNKQEQAEKVVAQMKKDIAYVQEAVKNvkPEEKKKVYLEFSPG---W 220
Cdd:cd01146 79 IYDQLSQIAPTVLLDSSPWLAEWKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKLPD--KGPKPVSVVRFSDAgsiR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 221 TVGKGEFMDELITLAGATNIAS----DTQGWNPISEEKILQNDPEVILYASGITDEktgvkLEDMIAKRNGWDKMKAIRE 296
Cdd:cd01146 157 LYGPNSFAGSVLEDLGLQNPWAqettNDSGFATISLERLAKADADVLFVFTYEDEE-----LAQALQANPLWQNLPAVKN 231
|
250
....*....|....*.
gi 1032348493 297 KQIFGMDQNILSRPGP 312
Cdd:cd01146 232 GRVYVVDDVWWFFGGG 247
|
|
| FecB |
COG4594 |
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ... |
1-309 |
1.49e-21 |
|
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443650 [Multi-domain] Cd Length: 316 Bit Score: 93.06 E-value: 1.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 1 MKRSLRFMIPLLVAASLAGCAGNDNSQpapggqtsapqtAPQENTAEqsakqttyPLTVKDATGkEVTFAKAPERIVSTS 80
Cdd:COG4594 1 MKKLLLLLILLLALLLLAACGSSSSDS------------SSSEAAAG--------ARTVKHAMG-ETTIPGTPKRVVVLE 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 81 PAETEILFALGLENriVVVSDYDDYPE-AAKAKPKIGGVV------KPNEEAILAQTPDMVVGGISMEKPVADKLKSLGm 153
Cdd:COG4594 60 WSFADALLALGVTP--VGIADDNDYDRwVPYLRDLIKGVTsvgtrsQPNLEAIAALKPDLIIADKSRHEAIYDQLSKIA- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 154 pvyithPTKM--------DDILNNVLAMGVITNKQEQAEKVVAQMKKDIAYVQEAVKNvKPEEKKKVYLEFSPG--WTVG 223
Cdd:COG4594 137 ------PTVLfksrngdyQENLESFKTIAKALGKEEEAEAVLADHDQRIAEAKAKLAA-ADKGKKVAVGQFRADglRLYT 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 224 KGEFMDELITLAGATNIASDTQ----GWNPISEEKILQNDPEVILYAsgiTDEKtgVKLEDMIAKRNGWDKMKAIREKQI 299
Cdd:COG4594 210 PNSFAGSVLAALGFENPPKQSKdngyGYSEVSLEQLPALDPDVLFIA---TYDD--PSILKEWKNNPLWKNLKAVKNGRV 284
|
330
....*....|
gi 1032348493 300 FGMDQNILSR 309
Cdd:COG4594 285 YEVDGDLWTR 294
|
|
| FatB |
cd01140 |
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ... |
66-303 |
1.03e-20 |
|
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: 90.01 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 66 EVTFAKAPERIVSTSPAETEILFALGLENRIVVVSD-----YDDYPEAAKAkpKIGGVVKPNEEAILAQTPDMVV-GGIS 139
Cdd:cd01140 5 ETKVPKNPEKVVVFDVGALDTLDALGVKVVGVPKSStlpeyLKKYKDDKYA--NVGTLFEPDLEAIAALKPDLIIiGGRL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 140 MEKpvADKLKSLGMPVYITHPTK--MDDILNNVLAMGVITNKQEQAEKVVAQMKKDIAYVQEAVKNvkpeeKKKV----- 212
Cdd:cd01140 83 AEK--YDELKKIAPTIDLGADLKnyLESVKQNIETLGKIFGKEEEAKELVAEIDASIAEAKSAAKG-----KKKAlvvlv 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 213 ----YLEFSPGWTVGKgefmdeLITLAGATNIASD----TQGwNPISEEKILQNDPEVILyasgITDEKTGVKLEDMIAK 284
Cdd:cd01140 156 nggkLSAFGPGSRFGW------LHDLLGFEPADENikasSHG-QPVSFEYILEANPDWLF----VIDRGAAIGAEGSSAK 224
|
250 260
....*....|....*....|...
gi 1032348493 285 RNG----WDKMKAIREKQIFGMD 303
Cdd:cd01140 225 EVLdndlVKNTTAWKNGKVIYLD 247
|
|
| FeuA |
cd01138 |
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ... |
65-303 |
1.85e-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: 71.98 E-value: 1.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 65 KEVTFAKAPERIVsTSPAETEILFALGLenRIVVVSDYDDYPEAAKAKPKIGGVV---KPNEEAILAQTPDMVVGGiSME 141
Cdd:cd01138 1 GEVEIPAKPKRIV-ALSGETEGLALLGI--KPVGAASIGGKNPYYKKKTLAKVVGivdEPNLEKVLELKPDLIIVS-SKQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 142 KPVADKLKSLGMPVYITHPTKmdDILNNVLAMGVITNKQEQAEKVVAQMKKDIAYVQEAVKNVKPEEK--------KKVY 213
Cdd:cd01138 77 EENYEKLSKIAPTVPVSYNSS--DWEEQLKEIGKLLNKEDEAEKWLADYKQKAKEAKEKIKKKLGNDKsvavlrgrKQIY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 214 LEFSPGWTVGKGEFMDELITLAGATNIASDTQGWNPISEEKILQNDPEVILYaSGITDEKTGVKLEdmiaKRNGWDKMKA 293
Cdd:cd01138 155 VFGEDGRGGGPILYADLGLKAPEKVKEIEDKPGYAAISLEVLPEFDADYIFL-LFFTGPEAKADFE----SLPIWKNLPA 229
|
250
....*....|
gi 1032348493 294 IREKQIFGMD 303
Cdd:cd01138 230 VKNNHVYIVD 239
|
|
| TroA_d |
cd01141 |
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ... |
73-243 |
7.31e-10 |
|
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial receptors in the ABC metal ion uptake in eubacteria and archaea. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.
Pssm-ID: 238561 [Multi-domain] Cd Length: 186 Bit Score: 57.43 E-value: 7.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 73 PERIVSTSPAETEILFALGLENRIVVVSDYDDYPE----AAKAKPKIGGVVKPNEEAILAQTPDMVVG-GISMEKPVADK 147
Cdd:cd01141 8 PKRIVVLSPTHVDLLLALDKADKIVGVSASAYDLNtpavKERIDIQVGPTGSLNVELIVALKPDLVILyGGFQAQTILDK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 148 LKSLGMPVYITH----PTKMDDILNNVLAmGVITNKQEQAEKVVAQmkkdIAYVQEAVKNVKPEEKKKVYLEFSP---GW 220
Cdd:cd01141 88 LEQLGIPVLYVNeypsPLGRAEWIKFAAA-FYGVGKEDKADEAFAQ----IAGRYRDLAKKVSNLNKPTVAIGKPvkgLW 162
|
170 180
....*....|....*....|....
gi 1032348493 221 TV-GKGEFMDELITLAGATNIASD 243
Cdd:cd01141 163 YMpGGNSYVAKMLRDAGGRYLSAE 186
|
|
| PRK14048 |
PRK14048 |
ferrichrome/ferrioxamine B periplasmic transporter; Provisional |
52-302 |
3.07e-09 |
|
ferrichrome/ferrioxamine B periplasmic transporter; Provisional
Pssm-ID: 172540 [Multi-domain] Cd Length: 374 Bit Score: 57.60 E-value: 3.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 52 QTTYPLTVKDATGKEVTFAKAPERIVSTSPAEteiLFALGL------------------ENRIVVVSDYDDYPEAAKAkP 113
Cdd:PRK14048 27 EVQWPMTVTDAVGREVTIPAPPKAVLLGSGFN---LIALSLihpdpvsllagwsgdmkgDNPEIYESFLRKFPELADV-P 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 114 KIGGVVKP--NEEAILAQTPDMVV-----GGISMEKPVADKLKSLGMPVYIT--HPTKMDDILNNVLAMGVITNKQEQAE 184
Cdd:PRK14048 103 LIDDGSGPglSFETILTLKADLAIlanwqADTEAGQRAIEYLESIGVPVIVVdfNNEALKNTPDNMRLLGKVFEREEQAE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 185 KVVAQMKKDIAYVQEAVKNvKPEEKKKVYLEFSPG-----WTVGKGEfMDELITLAGATNIASDT---QGwNPISEEKIL 256
Cdd:PRK14048 183 DFARFYEERLARIRDRVAK-HSEPGPTVLMEAFPAadrccWAYGRGG-LGEFIALTGSRNIAEGAlprPG-GMMNAEAIM 259
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1032348493 257 QNDPEVILYAS-------------GITDEKTGVKLEDMIAK--RNGwdkMKAIREKQIFGM 302
Cdd:PRK14048 260 AENPDVYIATSspggkysgfsigpGVSAEEAETTLANVVDKpvMAS---IAAVRDGRVHGL 317
|
|
| PRK10957 |
PRK10957 |
iron-enterobactin transporter periplasmic binding protein; Provisional |
49-200 |
3.51e-08 |
|
iron-enterobactin transporter periplasmic binding protein; Provisional
Pssm-ID: 236806 [Multi-domain] Cd Length: 317 Bit Score: 54.21 E-value: 3.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 49 SAKQTTYPLTVKDATGkEVTFAKAPERIVSTSPAETEILFALGLEnriVVVS--------DYDD------YPEAAKAKpk 114
Cdd:PRK10957 21 QASAAGWPRTVTDSRG-SVTLESKPQRIVSTSVTLTGTLLAIDAP---VIASgattpntrVADDqgffrqWSDVAKER-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032348493 115 igGVVK-----PNEEAILAQTPDMVV----GGISMEKPVaDKLKSLGmpvyithPTKM---DDILNNVLA--MGVITNKQ 180
Cdd:PRK10957 95 --GVEVlyigePDAEAVAAQMPDLIVisatGGDSALALY-DQLSAIA-------PTLVidyDDKSWQELAtqLGEATGLE 164
|
170 180
....*....|....*....|
gi 1032348493 181 EQAEKVVAQMKkdiAYVQEA 200
Cdd:PRK10957 165 KQAAAVIAQFD---AQLAEV 181
|
|
| PqiC |
COG3009 |
Intermembrane transporter PqiABC lipoprotein subunit PqiC [Cell wall/membrane/envelope ... |
1-42 |
4.15e-03 |
|
Intermembrane transporter PqiABC lipoprotein subunit PqiC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442246 [Multi-domain] Cd Length: 198 Bit Score: 37.66 E-value: 4.15e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1032348493 1 MKRSLRFMIPLLVAASLAGCAGNDNSQ----PAPGGQTSAPQTAPQ 42
Cdd:COG3009 1 MKRPLRLLLLLLLALLLAACASSPPTRyytlPPPAAPAAAAAAAAA 46
|
|
| |
