|
Name |
Accession |
Description |
Interval |
E-value |
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
59-325 |
2.04e-41 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 145.14 E-value: 2.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032724191 59 KVFVNTKPAAELLLHLGLKDNIVGVGADFGRGDSEVkkEYETLKKI-STDYVGKELAISTEPDLIFGRGTLFTEEEwgng 137
Cdd:COG0614 2 RIVSLSPSATELLLALGAGDRLVGVSDWGYCDYPEL--ELKDLPVVgGTGEPNLEAILALKPDLVLASSSGNDEED---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032724191 138 sVETLENMKLPTFILESsiqgGTIDSIYSDIEKIGKVFKVEDEANSFSEKLQKKEKTIKKTIGTREKATFAYLHMSTKDE 217
Cdd:COG0614 76 -YEQLEKIGIPVVVLDP----RSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGAEERPTVLYEIWSGDP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032724191 218 VvvYSAAKETFFQSVFELLNLDNIFKDEKGN---VSVEALIKADPDYLIVPDWSDGEGngvTSDELIEGIKADKRLSGMK 294
Cdd:COG0614 151 L--YTAGGGSFIGELLELAGGRNVAADLGGGypeVSLEQVLALDPDVIILSGGGYDAE---TAEEALEALLADPGWQSLP 225
|
250 260 270
....*....|....*....|....*....|.
gi 2032724191 295 AVKENKIYGLDYNAMFGYGYQSFDGIETLAK 325
Cdd:COG0614 226 AVKNGRVYVVPGDLLSRPGPRLLLALEDLAK 256
|
|
| TroA_a |
cd01148 |
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ... |
48-324 |
5.19e-41 |
|
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: 144.79 E-value: 5.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032724191 48 EKEMTYKEIPKKVFVNTKPAAELLLHLGLKDNIVGVGADFGRGDSEVKKEYETLKKISTDYVGKELAISTEPDLIFGRGT 127
Cdd:cd01148 9 GRSVTFDKAPQRVVSNDQNTTEMMLALGLQDRMVGTAGIDNKDLPELKAKYDKVPELAKKYPSKETVLAARPDLVFGGWS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032724191 128 LFTEEEwGNGSVETLENMKLPTFILESSIQGG----TIDSIYSDIEKIGKVFKVEDEANSFSEKLQKKEKTIKKTIGTRE 203
Cdd:cd01148 89 YGFDKG-GLGTPDSLAELGIKTYILPESCGQRrgeaTLDDVYNDIRNLGKIFDVEDRADKLVADLKARLAEISAKVKGDG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032724191 204 KATFAYLHMS---TKDEVVVYSAAketffQSVFELLNLDNIFKDEK---GNVSVEALIKADPDYLIVPDWSDGEGngvtS 277
Cdd:cd01148 168 KKVAVFVYDSgedKPFTSGRGGIP-----NAIITAAGGRNVFADVDeswTTVSWETVIARNPDVIVIIDYGDQNA----A 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2032724191 278 DELIEGIKADKRLSGMKAVKENKIYGLDYNAMFGyGYQSFDGIETLA 324
Cdd:cd01148 239 EQKIKFLKENPALKNVPAVKNNRFIVLPLAEATP-GIRNVDAIEKLA 284
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
68-305 |
1.34e-20 |
|
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: 88.96 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032724191 68 AELLLHLGLKDNIVGVGADfgrgDSEVKKEYETLKKISTDYVGK---ELAISTEPDLIFGRGTLFTEEEwgngsvETLEN 144
Cdd:pfam01497 8 TEILYALGATDSIVGVDAY----TRDPLKADAVAAIVKVGAYGEinvERLAALKPDLVILSTGYLTDEA------EELLS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032724191 145 MKLPTFILESSiqgGTIDSIYSDIEKIGKVFKVEDEANSFSEKLQKKEKTIKKTIGTREKATFAYLHMStkDEVVVYSAA 224
Cdd:pfam01497 78 LIIPTVIFESS---STGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPVLVFGGA--DGGGYVVAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032724191 225 KETFFQSVFELLNLDNIFKDEKGN----VSVEALIKADPDYLIVPDWSDGegngvtSDELIEGIKADKRLSGMKAVKENK 300
Cdd:pfam01497 153 SNTYIGDLLRILGIENIAAELSGSeyapISFEAILSSNPDVIIVSGRDSF------TKTGPEFVAANPLWAGLPAVKNGR 226
|
....*
gi 2032724191 301 IYGLD 305
Cdd:pfam01497 227 VYTLP 231
|
|
| btuF |
PRK09534 |
corrinoid ABC transporter substrate-binding protein; Reviewed |
44-266 |
4.92e-05 |
|
corrinoid ABC transporter substrate-binding protein; Reviewed
Pssm-ID: 236552 [Multi-domain] Cd Length: 359 Bit Score: 44.51 E-value: 4.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032724191 44 TDFKEKEMTYKEIPKKVFVNTKPAAELLLHLGLKDNIVGVgADFGrGDSEVKKEYETLKKISTDYVGKELAISTEPDLIF 123
Cdd:PRK09534 47 TDATGTEITLDERPERVVTLNPSAAQTMWELGARDRVVGV-TQYA-SYLDGAEERTNVSGGQPFGVNVEAVVGLDPDLVL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032724191 124 GRGTLfteeewGNGSVETLENMKLPTFILESsiqGGTIDSIYSDIEKIGKVFKVEDEANSFSEKLQKKEKTIKKTIGTRE 203
Cdd:PRK09534 125 APNAV------AGDTVTRLREAGITVFHFPA---ATSIEDVAEKTATIGRLTGNCEAAAETNAEMRDRVDAVEDRTADVD 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032724191 204 KATFAYLHMSTKdevvvYSAAKETFFQSVFELLNLDNIFKDEKGN----VSVEALIKADPDYLIVPD 266
Cdd:PRK09534 196 DRPRVLYPLGDG-----YTAGGNTFIGALIEAAGGHNVAADATTDgypqLSEEVIVQQDPDVIVVAT 257
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
59-325 |
2.04e-41 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 145.14 E-value: 2.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032724191 59 KVFVNTKPAAELLLHLGLKDNIVGVGADFGRGDSEVkkEYETLKKI-STDYVGKELAISTEPDLIFGRGTLFTEEEwgng 137
Cdd:COG0614 2 RIVSLSPSATELLLALGAGDRLVGVSDWGYCDYPEL--ELKDLPVVgGTGEPNLEAILALKPDLVLASSSGNDEED---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032724191 138 sVETLENMKLPTFILESsiqgGTIDSIYSDIEKIGKVFKVEDEANSFSEKLQKKEKTIKKTIGTREKATFAYLHMSTKDE 217
Cdd:COG0614 76 -YEQLEKIGIPVVVLDP----RSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGAEERPTVLYEIWSGDP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032724191 218 VvvYSAAKETFFQSVFELLNLDNIFKDEKGN---VSVEALIKADPDYLIVPDWSDGEGngvTSDELIEGIKADKRLSGMK 294
Cdd:COG0614 151 L--YTAGGGSFIGELLELAGGRNVAADLGGGypeVSLEQVLALDPDVIILSGGGYDAE---TAEEALEALLADPGWQSLP 225
|
250 260 270
....*....|....*....|....*....|.
gi 2032724191 295 AVKENKIYGLDYNAMFGYGYQSFDGIETLAK 325
Cdd:COG0614 226 AVKNGRVYVVPGDLLSRPGPRLLLALEDLAK 256
|
|
| TroA_a |
cd01148 |
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ... |
48-324 |
5.19e-41 |
|
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: 144.79 E-value: 5.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032724191 48 EKEMTYKEIPKKVFVNTKPAAELLLHLGLKDNIVGVGADFGRGDSEVKKEYETLKKISTDYVGKELAISTEPDLIFGRGT 127
Cdd:cd01148 9 GRSVTFDKAPQRVVSNDQNTTEMMLALGLQDRMVGTAGIDNKDLPELKAKYDKVPELAKKYPSKETVLAARPDLVFGGWS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032724191 128 LFTEEEwGNGSVETLENMKLPTFILESSIQGG----TIDSIYSDIEKIGKVFKVEDEANSFSEKLQKKEKTIKKTIGTRE 203
Cdd:cd01148 89 YGFDKG-GLGTPDSLAELGIKTYILPESCGQRrgeaTLDDVYNDIRNLGKIFDVEDRADKLVADLKARLAEISAKVKGDG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032724191 204 KATFAYLHMS---TKDEVVVYSAAketffQSVFELLNLDNIFKDEK---GNVSVEALIKADPDYLIVPDWSDGEGngvtS 277
Cdd:cd01148 168 KKVAVFVYDSgedKPFTSGRGGIP-----NAIITAAGGRNVFADVDeswTTVSWETVIARNPDVIVIIDYGDQNA----A 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2032724191 278 DELIEGIKADKRLSGMKAVKENKIYGLDYNAMFGyGYQSFDGIETLA 324
Cdd:cd01148 239 EQKIKFLKENPALKNVPAVKNNRFIVLPLAEATP-GIRNVDAIEKLA 284
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
68-305 |
1.34e-20 |
|
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: 88.96 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032724191 68 AELLLHLGLKDNIVGVGADfgrgDSEVKKEYETLKKISTDYVGK---ELAISTEPDLIFGRGTLFTEEEwgngsvETLEN 144
Cdd:pfam01497 8 TEILYALGATDSIVGVDAY----TRDPLKADAVAAIVKVGAYGEinvERLAALKPDLVILSTGYLTDEA------EELLS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032724191 145 MKLPTFILESSiqgGTIDSIYSDIEKIGKVFKVEDEANSFSEKLQKKEKTIKKTIGTREKATFAYLHMStkDEVVVYSAA 224
Cdd:pfam01497 78 LIIPTVIFESS---STGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPVLVFGGA--DGGGYVVAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032724191 225 KETFFQSVFELLNLDNIFKDEKGN----VSVEALIKADPDYLIVPDWSDGegngvtSDELIEGIKADKRLSGMKAVKENK 300
Cdd:pfam01497 153 SNTYIGDLLRILGIENIAAELSGSeyapISFEAILSSNPDVIIVSGRDSF------TKTGPEFVAANPLWAGLPAVKNGR 226
|
....*
gi 2032724191 301 IYGLD 305
Cdd:pfam01497 227 VYTLP 231
|
|
| YvrC |
cd01143 |
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ... |
57-264 |
8.37e-19 |
|
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: 83.10 E-value: 8.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032724191 57 PKKVfVNTKPAA-ELLLHLGLKDNIVGVgADFgrgDSEVKKEYETLKKISTDYVGKELAISTEPDLIFgrgtlfTEEEWG 135
Cdd:cd01143 3 PERI-VSLSPSItEILFALGAGDKIVGV-DTY---SNYPKEVRKKPKVGSYSNPNVEKIVALKPDLVI------VSSSSL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032724191 136 NGSVETLENMKLPTFILESSiqgGTIDSIYSDIEKIGKVFKVEDEANSFSEKLQKKEKTIKKTIGTREKATFAYLHMSTK 215
Cdd:cd01143 72 AELLEKLKDAGIPVVVLPAA---SSLDEIYDQIELIGKITGAEEEAEKLVKEMKQKIDKVKDKGKTIKKSKVYIEVSLGG 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2032724191 216 DevvvYSAAKETFFQSVFELLNLDNIFKDEKG--NVSVEALIKADPDYLIV 264
Cdd:cd01143 149 P----YTAGKNTFINELIRLAGAKNIAADSGGwpQVSPEEILKANPDVIIL 195
|
|
| ChuT |
COG4558 |
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ... |
68-325 |
2.29e-18 |
|
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443619 [Multi-domain] Cd Length: 285 Bit Score: 83.70 E-value: 2.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032724191 68 AELLLHLGLKDNIVGVgadfgrgD--SEVKKEYETLKKistdyVGKELAISTE------PDLIFGRGTLFTEEewgngSV 139
Cdd:COG4558 38 TEIVYALGAGDRLVGV-------DttSTYPAAAKALPD-----VGYMRQLSAEgilslkPTLVLASEGAGPPE-----VL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032724191 140 ETLENMKLPTFILESsiqGGTIDSIYSDIEKIGKVFKVEDEANSFSEKLQ---KKEKTIKKTIGTREKATFAYLHmstkD 216
Cdd:COG4558 101 DQLRAAGVPVVVVPA---APSLEGVLAKIRAVAAALGVPEAGEALAARLEadlAALAARVAAIGKPPRVLFLLSR----G 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032724191 217 EVVVYSAAKETFFQSVFELLNLDNIFKDEKGN--VSVEALIKADPDYLIVPDwsdgegNGVTSDELIEGIKADKRLSGMK 294
Cdd:COG4558 174 GGRPMVAGRGTAADALIRLAGGVNAAAGFEGYkpLSAEALIAAAPDVILVMT------RGLESLGGVDGLLALPGLAQTP 247
|
250 260 270
....*....|....*....|....*....|.
gi 2032724191 295 AVKENKIYGLDYNAMFGYGYQSFDGIETLAK 325
Cdd:COG4558 248 AGKNKRIVAMDDLLLLGFGPRTPQAALALAQ 278
|
|
| HemV-2 |
cd01147 |
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ... |
56-302 |
3.20e-17 |
|
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: 80.07 E-value: 3.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032724191 56 IPK---KVFVNTKPAAELLLHLGLKDNIVGVGA----DFGRGDSEVKKEYETLKKISTDYVGK----ELAISTEPDLIFG 124
Cdd:cd01147 1 VPKpveRVVAAGPGALRLLYALAAPDKIVGVDDaeksDEGRPYFLASPELKDLPVIGRGGRGNtpnyEKIAALKPDVVID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032724191 125 RGTLfteeeWGNGSVETLENMKLPTFILESSiqGGTIDSIYSDIEKIGKVFKVEDEAN---SFSEKLQKKEKTIKKTIGT 201
Cdd:cd01147 81 VGSD-----DPTSIADDLQKKTGIPVVVLDG--GDSLEDTPEQIRLLGKVLGKEERAEeliSFIESILADVEERTKDIPD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032724191 202 REKATFAYLHMSTKDEVVVYSAAKEtfFQSVFELLNLDNIFKDEKG----NVSVEALIKADPDYLIVpdwsdgeGNGVTS 277
Cdd:cd01147 154 EEKPTVYFGRIGTKGAAGLESGLAG--SIEVFELAGGINVADGLGGgglkEVSPEQILLWNPDVIFL-------DTGSFY 224
|
250 260
....*....|....*....|....*
gi 2032724191 278 DELIEGIKADKRLSGMKAVKENKIY 302
Cdd:cd01147 225 LSLEGYAKNRPFWQSLKAVKNGRVY 249
|
|
| FecB |
COG4594 |
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ... |
1-329 |
1.03e-15 |
|
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443650 [Multi-domain] Cd Length: 316 Bit Score: 76.50 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032724191 1 MKK--LVVGIVLSSLLLVGCGSNESKKENNKAgvtvtnywnKAGATDFKEK--EMTYKEIPKKVFVNTKPAAELLLHLGL 76
Cdd:COG4594 1 MKKllLLLILLLALLLLAACGSSSSDSSSSEA---------AAGARTVKHAmgETTIPGTPKRVVVLEWSFADALLALGV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032724191 77 KDniVGVgADFGRGDsevkKEYETLKKISTDY--VGKELAISTE------PDLIFGrgTLFTEEewgnGSVETLEnmKL- 147
Cdd:COG4594 72 TP--VGI-ADDNDYD----RWVPYLRDLIKGVtsVGTRSQPNLEaiaalkPDLIIA--DKSRHE----AIYDQLS--KIa 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032724191 148 PTFILESSiqGGTIDSIYSDIEKIGKVFKVEDEA-----------NSFSEKLQKKEKTikktigtrEKATFAylhMSTKD 216
Cdd:COG4594 137 PTVLFKSR--NGDYQENLESFKTIAKALGKEEEAeavladhdqriAEAKAKLAAADKG--------KKVAVG---QFRAD 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032724191 217 EVVVYSaaKETFFQSVFELLNLDNIFKDEKGN------VSVEALIKADPDYLIVpdwsdgegnGVTSDELIEG-IKADKR 289
Cdd:COG4594 204 GLRLYT--PNSFAGSVLAALGFENPPKQSKDNgygyseVSLEQLPALDPDVLFI---------ATYDDPSILKeWKNNPL 272
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2032724191 290 LSGMKAVKENKIYGLDYNA-MFGYGYQSfdgIETLAKEMVE 329
Cdd:COG4594 273 WKNLKAVKNGRVYEVDGDLwTRGRGPLA---AELMADDLVE 310
|
|
| BtuF |
cd01144 |
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ... |
67-325 |
2.80e-14 |
|
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: 71.18 E-value: 2.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032724191 67 AAELLLHLGLKDNIVGVgADFGRGDSEVKKeyetLKKISTDYVGK-ELAISTEPDLIFGRGTLFTEEEwgngsVETLENM 145
Cdd:cd01144 10 ATELLYALGLGDQLVGV-TDYCDYPPEAKK----LPRVGGFYQLDlERVLALKPDLVIAWDDCNVCAV-----VDQLRAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032724191 146 KLPTFILEssiqGGTIDSIYSDIEKIGKVFKVEDEANSFSEKLQKKEKTIKKTIGTREKATFAYLHMSTKdevvVYSAAK 225
Cdd:cd01144 80 GIPVLVSE----PQTLDDILADIRRLGTLAGRPARAEELAEALRRRLAALRKQYASKPPPRVFYQEWIDP----LMTAGG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032724191 226 ETFfQSVFELLNLDNIFKDEKG---NVSVEALIKADPDYLIVPDwsdgEGNGVTSDELiegiKADKRLSGMKAVKENKIY 302
Cdd:cd01144 152 DWV-PELIALAGGVNVFADAGErspQVSWEDVLAANPDVIVLSP----CGFGFTPAIL----RKEPAWQALPAVRNGRVY 222
|
250 260
....*....|....*....|...
gi 2032724191 303 GLDYNAMFGYGYQSFDGIETLAK 325
Cdd:cd01144 223 AVDGNWYFRPSPRLVDGLEQLAA 245
|
|
| CeuA |
COG4607 |
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and ... |
1-329 |
5.39e-12 |
|
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443657 [Multi-domain] Cd Length: 310 Bit Score: 65.59 E-value: 5.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032724191 1 MKKLVVGIVL--SSLLLVGCGSNESKKE--NNKAGVTVTnywNKAGATDFKEKemtykeiPKKVFVNTKPAAELLLHLGL 76
Cdd:COG4607 1 MKKTLLAALAlaAALALAACGSSSAAAAsaAAAETVTVE---HALGTVEVPKN-------PKRVVVFDNGALDTLDALGV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032724191 77 KdnIVGVgadfgrgdseVKKEY-ETLKKISTDY---VG--KEL---AIST-EPDLIF--GRgtlfteeewgngSVETLEN 144
Cdd:COG4607 71 E--VAGV----------PKGLLpDYLSKYADDKyanVGtlFEPdleAIAAlKPDLIIigGR------------SAKKYDE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032724191 145 MK--LPTFILESSiQGGTIDSIYSDIEKIGKVFKVEDEANSFSEKLQKKEKTIKKTIGTREKATFAylhMSTKDEVVVYs 222
Cdd:COG4607 127 LSkiAPTIDLTVD-GEDYLESLKRNTETLGEIFGKEDEAEELVADLDAKIAALKAAAAGKGTALIV---LTNGGKISAY- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032724191 223 aAKETFFQSVFELLNLDNIFKDEKG-----NVSVEALIKADPDYLIVPDWSDGEGNGVTSDELIEGIKAdkrLSGMKAVK 297
Cdd:COG4607 202 -GPGSRFGPIHDVLGFKPADEDIEAsthgqAISFEFIAEANPDWLFVIDRDAAIGGEGPAAKQVLDNEL---VKQTTAWK 277
|
330 340 350
....*....|....*....|....*....|..
gi 2032724191 298 ENKIYGLDYNAMfgygYQSFDGIETLaKEMVE 329
Cdd:COG4607 278 NGQIVYLDPDAW----YLAGGGIQSL-TEMLD 304
|
|
| TroA-like |
cd00636 |
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ... |
58-189 |
1.61e-11 |
|
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: 61.42 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032724191 58 KKVFVNTKPAAELLLHLGLKDNIVGVgADFGRGDSEVKKEYETLKKISTDY-VGKELAISTEPDLIFGRGTLfteeewGN 136
Cdd:cd00636 1 KRVVALDPGATELLLALGGDDKPVGV-ADPSGYPPEAKALLEKVPDVGHGYePNLEKIAALKPDLIIANGSG------LE 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2032724191 137 GSVETLENMKLPTFILESSIqGGTIDSIYSDIEKIGKVFKVEDEANSFSEKLQ 189
Cdd:cd00636 74 AWLDKLSKIAIPVVVVDEAS-ELSLENIKESIRLIGKALGKEENAEELIAELD 125
|
|
| FhuD |
cd01146 |
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ... |
55-314 |
3.84e-10 |
|
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: 59.61 E-value: 3.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032724191 55 EIPKKVFVNTKPAAELLLHLGLKdnIVGVgADFGRGDSEVKKEYETLKKIStdYVGK------ELAISTEPDLIFGRGTL 128
Cdd:cd01146 1 AKPQRIVALDWGALETLLALGVK--PVGV-ADTAGYKPWIPEPALPLEGVV--DVGTrgqpnlEAIAALKPDLILGSASR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032724191 129 FTEeewgngSVETLEnmKL-PTFILESSIQGGTIDSIysdIEKIGKVFKVEDEANSFSEKLQKKEKTIKKTIGTREKATF 207
Cdd:cd01146 76 HDE------IYDQLS--QIaPTVLLDSSPWLAEWKEN---LRLIAKALGKEEEAEKLLAEYDQRLAELRQKLPDKGPKPV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032724191 208 AYLHMSTKDEVVVYSaaKETFFQSVFELLNLDNIFKDEKGN------VSVEALIKADPDYLIVPDWSDgegngvtsDELI 281
Cdd:cd01146 145 SVVRFSDAGSIRLYG--PNSFAGSVLEDLGLQNPWAQETTNdsgfatISLERLAKADADVLFVFTYED--------EELA 214
|
250 260 270
....*....|....*....|....*....|...
gi 2032724191 282 EGIKADKRLSGMKAVKENKIYGLDYNAMFGYGY 314
Cdd:cd01146 215 QALQANPLWQNLPAVKNGRVYVVDDVWWFFGGG 247
|
|
| FatB |
cd01140 |
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ... |
57-329 |
6.21e-10 |
|
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: 59.19 E-value: 6.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032724191 57 PKKVFVNTKPAAELLLHLGLKdnIVGVGADfgrgdSEVKKEYETLKKISTDYVGK------ELAISTEPDLIFGRGTLft 130
Cdd:cd01140 12 PEKVVVFDVGALDTLDALGVK--VVGVPKS-----STLPEYLKKYKDDKYANVGTlfepdlEAIAALKPDLIIIGGRL-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032724191 131 eeewgngsVETLENMK--LPTfILESSIQGGTIDSIYSDIEKIGKVFKVEDEANSFSEKLQKKEKTIKKTIGTREKATFA 208
Cdd:cd01140 83 --------AEKYDELKkiAPT-IDLGADLKNYLESVKQNIETLGKIFGKEEEAKELVAEIDASIAEAKSAAKGKKKALVV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032724191 209 yLHMSTKdevvVYSAAKETFFQSVFELLNLDNIFKDEKG-----NVSVEALIKADPDYLIVPDWSDGEGNGVTSDeliEG 283
Cdd:cd01140 154 -LVNGGK----LSAFGPGSRFGWLHDLLGFEPADENIKAsshgqPVSFEYILEANPDWLFVIDRGAAIGAEGSSA---KE 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2032724191 284 IKADKRLSGMKAVKENKIYGLDYNamfgYGYQSFDGIETLaKEMVE 329
Cdd:cd01140 226 VLDNDLVKNTTAWKNGKVIYLDPD----LWYLSGGGLESL-KQMID 266
|
|
| TroA_e |
cd01142 |
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ... |
44-303 |
2.28e-08 |
|
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: 54.67 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032724191 44 TDFKEKEMTYKEIPKKVFVNTKPAAELLLHLGLKDNIVGvgadfgrgDSEVKKEYETLKKISTDY-----------VGKE 112
Cdd:cd01142 11 TDMAGRKVTIPDEVKRIAALWGAGNAVVAALGGGKLIVA--------TTSTVQQEPWLYRLAPSLenvatggtgndVNIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032724191 113 LAISTEPDLIFGRGTLFTEEewgngsvetleNMKLPTFILESSIQGGTIDSIYSDIEKIGKVFKVEDEANSFSEKLQkke 192
Cdd:cd01142 83 ELLALKPDVVIVWSTDGKEA-----------GKAVLRLLNALSLRDAELEEVKLTIALLGELLGRQEKAEALVAYFD--- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032724191 193 ktikktigTREKATFAYLHMSTKDE-VVVYSAA--------KETFFQSVFELLNLDNIFKD----EKGNVSVEALIKADP 259
Cdd:cd01142 149 --------DNLAYVAARTKKLPDSErPRVYYAGpdplttdgTGSITNSWIDLAGGINVASEatkkGSGEVSLEQLLKWNP 220
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2032724191 260 DYLIVpdwsdgeGNGVTSDEliegIKADKRLSGMKAVKENKIYG 303
Cdd:cd01142 221 DVIIV-------GNADTKAA----ILADPRWQNLRAVKNGRVYV 253
|
|
| HutB |
cd01149 |
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ... |
57-305 |
5.10e-06 |
|
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: 46.87 E-value: 5.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032724191 57 PKKVFVNTKPAAELLLHLGLKDNIVGVgadfgrgDSEVKKEYETLKKISTDYvGKELA----ISTEPDLIFGrgtlfTEE 132
Cdd:cd01149 1 PERIVSLGGSVTEIVYALGAGDRLVGV-------DSTSTYPEAAAKLPDVGY-MRQLSaegvLSLKPTLVIA-----SDE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032724191 133 ewgNGSVETLENMK---LPTFILESSiqgGTIDSIYSDIEKIGKVFKVEDEANSFSEKLQ---KKEKTIKKTIGTREKAT 206
Cdd:cd01149 68 ---AGPPEALDQLRaagVPVVTVPST---PTLDGLLTKIRQVAQALGVPEKGEALAQEVRqrlAALRKTVAAHKKPPRVL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032724191 207 FAYLHMSTKdevvVYSAAKETFFQSVFELLNLDNIFKDEKG--NVSVEALIKADPDYLIVPDwsdgegNGVTSDELIEGI 284
Cdd:cd01149 142 FLLSHGGGA----AMAAGRNTAADAIIALAGAVNAAAGFRGykPLSAEALIAAQPDVILVMS------RGLDAVGGVDGL 211
|
250 260
....*....|....*....|.
gi 2032724191 285 KADKRLSGMKAVKENKIYGLD 305
Cdd:cd01149 212 LKLPGLAQTPAGRNKRILAMD 232
|
|
| btuF |
PRK09534 |
corrinoid ABC transporter substrate-binding protein; Reviewed |
44-266 |
4.92e-05 |
|
corrinoid ABC transporter substrate-binding protein; Reviewed
Pssm-ID: 236552 [Multi-domain] Cd Length: 359 Bit Score: 44.51 E-value: 4.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032724191 44 TDFKEKEMTYKEIPKKVFVNTKPAAELLLHLGLKDNIVGVgADFGrGDSEVKKEYETLKKISTDYVGKELAISTEPDLIF 123
Cdd:PRK09534 47 TDATGTEITLDERPERVVTLNPSAAQTMWELGARDRVVGV-TQYA-SYLDGAEERTNVSGGQPFGVNVEAVVGLDPDLVL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032724191 124 GRGTLfteeewGNGSVETLENMKLPTFILESsiqGGTIDSIYSDIEKIGKVFKVEDEANSFSEKLQKKEKTIKKTIGTRE 203
Cdd:PRK09534 125 APNAV------AGDTVTRLREAGITVFHFPA---ATSIEDVAEKTATIGRLTGNCEAAAETNAEMRDRVDAVEDRTADVD 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032724191 204 KATFAYLHMSTKdevvvYSAAKETFFQSVFELLNLDNIFKDEKGN----VSVEALIKADPDYLIVPD 266
Cdd:PRK09534 196 DRPRVLYPLGDG-----YTAGGNTFIGALIEAAGGHNVAADATTDgypqLSEEVIVQQDPDVIVVAT 257
|
|
| FeuA |
cd01138 |
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ... |
138-310 |
9.62e-03 |
|
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: 36.93 E-value: 9.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032724191 138 SVETLENMKlPTFILESSIQGGTIDS--------IYSDIEK--------IGKVFKVEDEANSFSEKLQKKEKTIKKTIGT 201
Cdd:cd01138 58 NLEKVLELK-PDLIIVSSKQEENYEKlskiaptvPVSYNSSdweeqlkeIGKLLNKEDEAEKWLADYKQKAKEAKEKIKK 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032724191 202 REKATFAYLHMSTKDEVVVYSAAKETFFQSVFELLNL-------DNIFKDEKGNVSVEALIKADPDYLIVPDWSDGEGng 274
Cdd:cd01138 137 KLGNDKSVAVLRGRKQIYVFGEDGRGGGPILYADLGLkapekvkEIEDKPGYAAISLEVLPEFDADYIFLLFFTGPEA-- 214
|
170 180 190
....*....|....*....|....*....|....*.
gi 2032724191 275 vtsDELIEGIKADKRLsgmKAVKENKIYGLDYNAMF 310
Cdd:cd01138 215 ---KADFESLPIWKNL---PAVKNNHVYIVDAWVFY 244
|
|
| |
