|
Name |
Accession |
Description |
Interval |
E-value |
| TroA_d |
cd01141 |
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ... |
42-236 |
1.69e-38 |
|
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: 135.24 E-value: 1.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152415899 42 EQTIKLPVsKIAYIGSYVEVPAMLNVWN--RVVGVSDYAFkddivkaTLKGEDLKRVKHMSTDHTAALNVELLKKLGPDL 119
Cdd:cd01141 1 AKTIKVPP-KRIVVLSPTHVDLLLALDKadKIVGVSASAY-------DLNTPAVKERIDIQVGPTGSLNVELIVALKPDL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152415899 120 VVTFVGNPK--AVEHAKRFGISFLSFQE----TTIAEAMQAMQAQATVleidasKKFAKMQETLDFIADRLKNVKKKKGV 193
Cdd:cd01141 73 VILYGGFQAqtILDKLEQLGIPVLYVNEypspLGRAEWIKFAAAFYGV------GKEDKADEAFAQIAGRYRDLAKKVSN 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1152415899 194 elFHKANKISGHQaISSDILEKGGIDNFGLKYVKFGRADISVE 236
Cdd:cd01141 147 --LNKPTVAIGKP-VKGLWYMPGGNSYVAKMLRDAGGRYLSAE 186
|
|
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
52-306 |
1.26e-25 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 103.15 E-value: 1.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152415899 52 IAYIGSYVEVPAMLNVWNRVVGVSDYAFKDDivkATLKGEDLKRVKHMSTdhtaaLNVELLKKLGPDLVVT--FVGNPKA 129
Cdd:COG0614 4 VSLSPSATELLLALGAGDRLVGVSDWGYCDY---PELELKDLPVVGGTGE-----PNLEAILALKPDLVLAssSGNDEED 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152415899 130 VEHAKRFGISFLSFQETTIAEAMQAMQAQATVL--EIDASKKFAKMQETLDFIADRLKNVKKKKGVELFHKANK---ISG 204
Cdd:COG0614 76 YEQLEKIGIPVVVLDPRSLEDLYESIRLLGELLgrEERAEALIAEYEARLAAVRARLAGAEERPTVLYEIWSGDplyTAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152415899 205 HQAISSDILEKGGIDNFGLKyVKFGRADISVEKIVKENPEIIFIWWVSPLTP------EDVLNNPKFATIKAIKNKQVYK 278
Cdd:COG0614 156 GGSFIGELLELAGGRNVAAD-LGGGYPEVSLEQVLALDPDVIILSGGGYDAEtaeealEALLADPGWQSLPAVKNGRVYV 234
|
250 260 270
....*....|....*....|....*....|
gi 1152415899 279 LP--TMDIGGPRAPLISLYIALKAHPEAFK 306
Cdd:COG0614 235 VPgdLLSRPGPRLLLALEDLAKALHPELFA 264
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
52-280 |
7.52e-19 |
|
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: 83.96 E-value: 7.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152415899 52 IAYIGSYVEVPAMLNVWNRVVGVSDYAFkdDIVKATLKGEDLKRVKHMStdhtaaLNVELLKKLGPDLVvtFVGNPKAVE 131
Cdd:pfam01497 1 AALSPAYTEILYALGATDSIVGVDAYTR--DPLKADAVAAIVKVGAYGE------INVERLAALKPDLV--ILSTGYLTD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152415899 132 HAKRF---GISFLSFQETTIAEAM--QAMQ-AQATVLEIDASKKFAKMQETLDFIADRLKNVKKKKgVELFHKANK---- 201
Cdd:pfam01497 71 EAEELlslIIPTVIFESSSTGESLkeQIKQlGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKP-VLVFGGADGggyv 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152415899 202 ISGHQAISSDILEKGGIDNFGLKYVKFGRADISVEKIVKENPEIIFI-WWVSPLT--PEDVLNNPKFATIKAIKNKQVYK 278
Cdd:pfam01497 150 VAGSNTYIGDLLRILGIENIAAELSGSEYAPISFEAILSSNPDVIIVsGRDSFTKtgPEFVAANPLWAGLPAVKNGRVYT 229
|
..
gi 1152415899 279 LP 280
Cdd:pfam01497 230 LP 231
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| TroA_d |
cd01141 |
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ... |
42-236 |
1.69e-38 |
|
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: 135.24 E-value: 1.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152415899 42 EQTIKLPVsKIAYIGSYVEVPAMLNVWN--RVVGVSDYAFkddivkaTLKGEDLKRVKHMSTDHTAALNVELLKKLGPDL 119
Cdd:cd01141 1 AKTIKVPP-KRIVVLSPTHVDLLLALDKadKIVGVSASAY-------DLNTPAVKERIDIQVGPTGSLNVELIVALKPDL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152415899 120 VVTFVGNPK--AVEHAKRFGISFLSFQE----TTIAEAMQAMQAQATVleidasKKFAKMQETLDFIADRLKNVKKKKGV 193
Cdd:cd01141 73 VILYGGFQAqtILDKLEQLGIPVLYVNEypspLGRAEWIKFAAAFYGV------GKEDKADEAFAQIAGRYRDLAKKVSN 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1152415899 194 elFHKANKISGHQaISSDILEKGGIDNFGLKYVKFGRADISVE 236
Cdd:cd01141 147 --LNKPTVAIGKP-VKGLWYMPGGNSYVAKMLRDAGGRYLSAE 186
|
|
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
52-306 |
1.26e-25 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 103.15 E-value: 1.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152415899 52 IAYIGSYVEVPAMLNVWNRVVGVSDYAFKDDivkATLKGEDLKRVKHMSTdhtaaLNVELLKKLGPDLVVT--FVGNPKA 129
Cdd:COG0614 4 VSLSPSATELLLALGAGDRLVGVSDWGYCDY---PELELKDLPVVGGTGE-----PNLEAILALKPDLVLAssSGNDEED 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152415899 130 VEHAKRFGISFLSFQETTIAEAMQAMQAQATVL--EIDASKKFAKMQETLDFIADRLKNVKKKKGVELFHKANK---ISG 204
Cdd:COG0614 76 YEQLEKIGIPVVVLDPRSLEDLYESIRLLGELLgrEERAEALIAEYEARLAAVRARLAGAEERPTVLYEIWSGDplyTAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152415899 205 HQAISSDILEKGGIDNFGLKyVKFGRADISVEKIVKENPEIIFIWWVSPLTP------EDVLNNPKFATIKAIKNKQVYK 278
Cdd:COG0614 156 GGSFIGELLELAGGRNVAAD-LGGGYPEVSLEQVLALDPDVIILSGGGYDAEtaeealEALLADPGWQSLPAVKNGRVYV 234
|
250 260 270
....*....|....*....|....*....|
gi 1152415899 279 LP--TMDIGGPRAPLISLYIALKAHPEAFK 306
Cdd:COG0614 235 VPgdLLSRPGPRLLLALEDLAKALHPELFA 264
|
|
| TroA_e |
cd01142 |
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ... |
29-310 |
2.16e-23 |
|
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: 97.81 E-value: 2.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152415899 29 ASAQEVKVKDYFGEQ-TIKLPVSKIAYI-GSYVEVPAMLNVWNRVVGVSDYAFKDDIVKATLKGedLKRVKHMSTDHTaa 106
Cdd:cd01142 3 ATAATRTITDMAGRKvTIPDEVKRIAALwGAGNAVVAALGGGKLIVATTSTVQQEPWLYRLAPS--LENVATGGTGND-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152415899 107 LNVELLKKLGPDLVVTFVGNPKAVEHAKRFGISFLSFQETTIAEAMQAMQAQATVL--EIDASKKFAKMQETLDFIADRL 184
Cdd:cd01142 79 VNIEELLALKPDVVIVWSTDGKEAGKAVLRLLNALSLRDAELEEVKLTIALLGELLgrQEKAEALVAYFDDNLAYVAART 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152415899 185 KNVKKKKGVELFHKAN---KISGHQAISSDILEKGGIDNFGLKYVKFGRADISVEKIVKENPEIIFIWwvSPLTPEDVLN 261
Cdd:cd01142 159 KKLPDSERPRVYYAGPdplTTDGTGSITNSWIDLAGGINVASEATKKGSGEVSLEQLLKWNPDVIIVG--NADTKAAILA 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1152415899 262 NPKFATIKAIKNKQVYKLPTM----DIGGPRAPLISLYIALKAHPEAFKGVDI 310
Cdd:cd01142 237 DPRWQNLRAVKNGRVYVNPEGafwwDRPSAEEALLGLWLAKTLYPERFTDDDM 289
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
52-280 |
7.52e-19 |
|
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: 83.96 E-value: 7.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152415899 52 IAYIGSYVEVPAMLNVWNRVVGVSDYAFkdDIVKATLKGEDLKRVKHMStdhtaaLNVELLKKLGPDLVvtFVGNPKAVE 131
Cdd:pfam01497 1 AALSPAYTEILYALGATDSIVGVDAYTR--DPLKADAVAAIVKVGAYGE------INVERLAALKPDLV--ILSTGYLTD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152415899 132 HAKRF---GISFLSFQETTIAEAM--QAMQ-AQATVLEIDASKKFAKMQETLDFIADRLKNVKKKKgVELFHKANK---- 201
Cdd:pfam01497 71 EAEELlslIIPTVIFESSSTGESLkeQIKQlGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKP-VLVFGGADGggyv 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152415899 202 ISGHQAISSDILEKGGIDNFGLKYVKFGRADISVEKIVKENPEIIFI-WWVSPLT--PEDVLNNPKFATIKAIKNKQVYK 278
Cdd:pfam01497 150 VAGSNTYIGDLLRILGIENIAAELSGSEYAPISFEAILSSNPDVIIVsGRDSFTKtgPEFVAANPLWAGLPAVKNGRVYT 229
|
..
gi 1152415899 279 LP 280
Cdd:pfam01497 230 LP 231
|
|
| HemV-2 |
cd01147 |
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ... |
45-281 |
6.04e-15 |
|
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors in ABC transport of metal ions. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains. In addition, these proteins sometimes have a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence).
Pssm-ID: 238567 [Multi-domain] Cd Length: 262 Bit Score: 73.52 E-value: 6.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152415899 45 IKLPVSKIAYIGSY-VEVPAMLNVWNRVVGVsDYAFKDDIVKA-TLKGEDLK------RVKHMSTdhtaaLNVELLKKLG 116
Cdd:cd01147 1 VPKPVERVVAAGPGaLRLLYALAAPDKIVGV-DDAEKSDEGRPyFLASPELKdlpvigRGGRGNT-----PNYEKIAALK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152415899 117 PDLVVTFVGNPKAVEH---AKRFGISFLS----FQETTIAEAMQAMqaqATVL--EIDASKKFAKMQETLDFIADRLKNV 187
Cdd:cd01147 75 PDVVIDVGSDDPTSIAddlQKKTGIPVVVldggDSLEDTPEQIRLL---GKVLgkEERAEELISFIESILADVEERTKDI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152415899 188 KKKKGVELFHKANKISGHQAISSDilEKGGIDNF---GLKYV-----KFGRADISVEKIVKENPEIIFI-WWVSPLTPED 258
Cdd:cd01147 152 PDEEKPTVYFGRIGTKGAAGLESG--LAGSIEVFelaGGINVadglgGGGLKEVSPEQILLWNPDVIFLdTGSFYLSLEG 229
|
250 260
....*....|....*....|....
gi 1152415899 259 VL-NNPKFATIKAIKNKQVYKLPT 281
Cdd:cd01147 230 YAkNRPFWQSLKAVKNGRVYLLPA 253
|
|
| YvrC |
cd01143 |
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ... |
64-247 |
3.69e-11 |
|
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: 61.53 E-value: 3.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152415899 64 MLNVWNRVVGVSDYafkDDIVKatlkgEDLKRVKHMSTDHtaaLNVELLKKLGPDLVVTFVGNPKAV-EHAKRFGISFLS 142
Cdd:cd01143 19 ALGAGDKIVGVDTY---SNYPK-----EVRKKPKVGSYSN---PNVEKIVALKPDLVIVSSSSLAELlEKLKDAGIPVVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152415899 143 F-QETTIAEAMQAMQ--AQATVLEIDASKKFAKMQETLDFIADRLKNVKKKKG-VELFHKANKISGHQAISSDILEKGGI 218
Cdd:cd01143 88 LpAASSLDEIYDQIEliGKITGAEEEAEKLVKEMKQKIDKVKDKGKTIKKSKVyIEVSLGGPYTAGKNTFINELIRLAGA 167
|
170 180
....*....|....*....|....*....
gi 1152415899 219 DNFGLKYVkfGRADISVEKIVKENPEIIF 247
Cdd:cd01143 168 KNIAADSG--GWPQVSPEEILKANPDVII 194
|
|
| BtuF |
cd01144 |
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ... |
70-280 |
6.51e-10 |
|
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: 58.85 E-value: 6.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152415899 70 RVVGVSDYAFKDDivkatlkgeDLKRVKHMSTDHTaaLNVELLKKLGPDLVVTF-VGNPKA-VEHAKRFGISFLSFQETT 147
Cdd:cd01144 22 QLVGVTDYCDYPP---------EAKKLPRVGGFYQ--LDLERVLALKPDLVIAWdDCNVCAvVDQLRAAGIPVLVSEPQT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152415899 148 IAEAMQAMQAQATVLeiDASKKFAKMQETLDFIADRLKNVKKKKG-----VELFHKANKISGHQAISSDILEKGGIDNF- 221
Cdd:cd01144 91 LDDILADIRRLGTLA--GRPARAEELAEALRRRLAALRKQYASKPpprvfYQEWIDPLMTAGGDWVPELIALAGGVNVFa 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1152415899 222 --GLKYVKfgradISVEKIVKENPEIIFIWWV-SPLTPEDVLNNPKFATIKAIKNKQVYKLP 280
Cdd:cd01144 169 daGERSPQ-----VSWEDVLAANPDVIVLSPCgFGFTPAILRKEPAWQALPAVRNGRVYAVD 225
|
|
| TroA_f |
cd01139 |
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ... |
36-319 |
2.10e-09 |
|
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: 58.09 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152415899 36 VKDYFGEQ-TIKLPVSKIaYIGSYVEVPAMLNV-----WNRVVGVSDYAFKDDIVKATLKGEDLKRVKHMST---DHTAA 106
Cdd:cd01139 3 VTDVAGRKvTLDAPVERV-LLGEGRQLYALALLegenpFARIVGWGGDLKKGDPDTYAKYKEKFPEIADIPLigsTYNGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152415899 107 LNVELLKKLGPDLVV------TFVGNPKAVEHAKRFGIS--FLSFQETTIAEAMQAMQAQATVL-EIDASKKFAKM-QET 176
Cdd:cd01139 82 FSVEKVLTLKPDLVIlniwakTTAEESGILEKLEQAGIPvvFVDFRQKPLKNTTPSMRLLGKALgREERAEEFIEFyQER 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152415899 177 LDFIADRLKNVKKKKGVELFHKANKISGHQAIS------SDILEKGGIDNFGLKYVKFGRADISVEKIVKENPEIIFI-- 248
Cdd:cd01139 162 IDRIRDRLAKINEPKPKVFIELGAGGPEECCSTygngnwGELVDAAGGDNIADGLIPGTSGELNAEYVIAANPEIIIAtg 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152415899 249 --WWVSPLTPEDV----------------LNNPKFATIKAIKNKQVYKLPTmdiGGPRAPLisLYIALKA-----HPEAF 305
Cdd:cd01139 242 gnWAKDPSGVSLGpdgttadakesllralLKRPGWSSLQAVKNGRVYALWH---QFYRSPY--NFVALEAfakwlYPELF 316
|
330
....*....|....
gi 1152415899 306 KGVDINAIIKDYYK 319
Cdd:cd01139 317 KDLDPEATLQEFHR 330
|
|
| FecB |
COG4594 |
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ... |
15-280 |
1.01e-08 |
|
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443650 [Multi-domain] Cd Length: 316 Bit Score: 55.70 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152415899 15 LGALVASLLLNVC----------NASAQEVKVKDYFGEQTIKLPVSKIAYIG-SYVEVPAMLNVwnRVVGVSDYAFKDDI 83
Cdd:COG4594 8 LILLLALLLLAACgssssdssssEAAAGARTVKHAMGETTIPGTPKRVVVLEwSFADALLALGV--TPVGIADDNDYDRW 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152415899 84 VKatLKGEDLKRVKHMSTdhTAALNVELLKKLGPDLVVTFVGNPKAV-EHAKR------FGISFLSFQET-----TIAEA 151
Cdd:COG4594 86 VP--YLRDLIKGVTSVGT--RSQPNLEAIAALKPDLIIADKSRHEAIyDQLSKiaptvlFKSRNGDYQENlesfkTIAKA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152415899 152 MQaMQAQATVLEIDASKKFAKMQETldfIADRLKNVK------KKKGVELFHKankisghQAISSDILEKGGIDN--FGL 223
Cdd:COG4594 162 LG-KEEEAEAVLADHDQRIAEAKAK---LAAADKGKKvavgqfRADGLRLYTP-------NSFAGSVLAALGFENppKQS 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1152415899 224 KYVKFGRADISVEKIVKENPEIIFIW-WVSPLTPEDVLNNPKFATIKAIKNKQVYKLP 280
Cdd:COG4594 231 KDNGYGYSEVSLEQLPALDPDVLFIAtYDDPSILKEWKNNPLWKNLKAVKNGRVYEVD 288
|
|
| FhuD |
cd01146 |
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ... |
57-280 |
2.95e-08 |
|
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: 53.83 E-value: 2.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152415899 57 SYVEVPAMLNVwnRVVGVSDYA-FKDDIVKATLKGEDLKRVkhmstDHTAALNVELLKKLGPDLVVTFV-GNPKAVEHAK 134
Cdd:cd01146 12 GALETLLALGV--KPVGVADTAgYKPWIPEPALPLEGVVDV-----GTRGQPNLEAIAALKPDLILGSAsRHDEIYDQLS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152415899 135 RFG--ISFLSFQETTIAEAMQAMQAQATVLEIDASKKFAKMQETLDFIADRLKNVKKKKGVEL-FHKANKISGHQAIS-- 209
Cdd:cd01146 85 QIAptVLLDSSPWLAEWKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKLPDKGPKPVSVVrFSDAGSIRLYGPNSfa 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1152415899 210 SDILEKGGIDN--FGLKYVKFGRADISVEKIVKENPEIIFIWWVSPLTPED-VLNNPKFATIKAIKNKQVYKLP 280
Cdd:cd01146 165 GSVLEDLGLQNpwAQETTNDSGFATISLERLAKADADVLFVFTYEDEELAQaLQANPLWQNLPAVKNGRVYVVD 238
|
|
| FatB |
cd01140 |
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ... |
108-280 |
1.47e-06 |
|
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type initial receptors in the siderophore-mediated iron uptake in some eubacterial species. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.
Pssm-ID: 238560 [Multi-domain] Cd Length: 270 Bit Score: 48.79 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152415899 108 NVELLKKLGPDLVvtFVGNPKAVEHAKRFGISFLSFQETTIAEAMQAMQAQATVLeidaSKKFAKMQETLDFIAD----- 182
Cdd:cd01140 64 DLEAIAALKPDLI--IIGGRLAEKYDELKKIAPTIDLGADLKNYLESVKQNIETL----GKIFGKEEEAKELVAEidasi 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152415899 183 ---RLKNVKKKKGVELFHKANKIS--GHQAISSDILEKGGIDNfGLKYVKFGR--ADISVEKIVKENPEIIFIW------ 249
Cdd:cd01140 138 aeaKSAAKGKKKALVVLVNGGKLSafGPGSRFGWLHDLLGFEP-ADENIKASShgQPVSFEYILEANPDWLFVIdrgaai 216
|
170 180 190
....*....|....*....|....*....|.
gi 1152415899 250 WVSPLTPEDVLNNPKFATIKAIKNKQVYKLP 280
Cdd:cd01140 217 GAEGSSAKEVLDNDLVKNTTAWKNGKVIYLD 247
|
|
| TroA_a |
cd01148 |
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ... |
165-291 |
1.72e-06 |
|
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: 48.87 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152415899 165 DASKKFAKMQETLDFIADRLKNVKKKKGVELF---HKANKISGHQAISSDILEKGGIDNfGLKYVKFGRADISVEKIVKE 241
Cdd:cd01148 144 RADKLVADLKARLAEISAKVKGDGKKVAVFVYdsgEDKPFTSGRGGIPNAIITAAGGRN-VFADVDESWTTVSWETVIAR 222
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1152415899 242 NPE-IIFIWWVSPLTPED----VLNNPKFATIKAIKNKQVYKLP-TMDIGGPRAPL 291
Cdd:cd01148 223 NPDvIVIIDYGDQNAAEQkikfLKENPALKNVPAVKNNRFIVLPlAEATPGIRNVD 278
|
|
| TroA-like |
cd00636 |
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ... |
52-191 |
3.53e-05 |
|
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: 43.32 E-value: 3.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152415899 52 IAYIGSYVEVPAMLNVWNRVVGVSDYAFKDDIVKATLKgedlkrvKHMSTDHTAALNVELLKKLGPDLVVTF-VGNPKAV 130
Cdd:cd00636 4 VALDPGATELLLALGGDDKPVGVADPSGYPPEAKALLE-------KVPDVGHGYEPNLEKIAALKPDLIIANgSGLEAWL 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1152415899 131 EHAKRFGISFLSFQET---TIAEAMQAMQ--AQATVLEIDASKKFAKMQETLDFIADRLKNVKKKK 191
Cdd:cd00636 77 DKLSKIAIPVVVVDEAselSLENIKESIRliGKALGKEENAEELIAELDARLAELRAKLAKIPKKK 142
|
|
| |
