|
Name |
Accession |
Description |
Interval |
E-value |
| fecB |
PRK11411 |
iron-dicitrate transporter substrate-binding subunit; Provisional |
1-300 |
0e+00 |
|
iron-dicitrate transporter substrate-binding subunit; Provisional
Pssm-ID: 183123 [Multi-domain] Cd Length: 303 Bit Score: 557.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 1 MLAFIRFVFAGLLLV--ISHAFAATVQDEHGTFTLEKTPQRIVVLELSFADALAAVDVSPIGIADDNDAKRILPEVRAHL 78
Cdd:PRK11411 1 MLAFIRLLFAGLLLLsgSSHAFAVTVQDEQGTFTLEKTPQRIVVLELSFVDALAAVGVSPVGVADDNDAKRILPEVRAHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 79 KPWQSVGTRAQPSLEAIAALKPDLIIADSSRHAGVYIALQQIAPVLLLKSRNETYAENLQSAAIIGEMVGKKREMQARLE 158
Cdd:PRK11411 81 KPWQSVGTRSQPSLEAIAALKPDLIIADSSRHAGVYIALQKIAPTLLLKSRNETYQENLQSAAIIGEVLGKKREMQARIE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 159 QHKERMAQWASQLPKGTRVAFGTSREQQFNLHTQETWTGSVLASLGLNVP-AAMAGASMPSIGLEQLLAVNPAWLLVAHY 237
Cdd:PRK11411 161 QHKERMAQFASQLPKGTRVAFGTSREQQFNLHSPESYTGSVLAALGLNVPkAPMNGAAMPSISLEQLLALNPDWLLVAHY 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446801908 238 REESIVKRWQQDPLWQMLTAAQKQQVASVDSNTWARMRGIFAAERIAADTVKIFHHQPLTVVK 300
Cdd:PRK11411 241 RQESIVKRWQQDPLWQMLTAAKKQQVASVDSNTWARMRGIFAAERIAKDTVKIFHHQPLTVVK 303
|
|
| FecB |
COG4594 |
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ... |
2-295 |
7.40e-134 |
|
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443650 [Multi-domain] Cd Length: 316 Bit Score: 381.96 E-value: 7.40e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 2 LAFIRFVFAGLLLVI-------------SHAFAATVQDEHGTFTLEKTPQRIVVLELSFADALAAVDVSPIGIADDNDAK 68
Cdd:COG4594 4 LLLLLILLLALLLLAacgssssdsssseAAAGARTVKHAMGETTIPGTPKRVVVLEWSFADALLALGVTPVGIADDNDYD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 69 RILPEVRAHLKPWQSVGTRAQPSLEAIAALKPDLIIADSSRHAGVYIALQQIAPVLLLKSRNETYAENLQSAAIIGEMVG 148
Cdd:COG4594 84 RWVPYLRDLIKGVTSVGTRSQPNLEAIAALKPDLIIADKSRHEAIYDQLSKIAPTVLFKSRNGDYQENLESFKTIAKALG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 149 KKREMQARLEQHKERMAQWASQLP---KGTRVAFGTSREQQFNLHTQETWTGSVLASLGLNVPAA---MAGASMPSIGLE 222
Cdd:COG4594 164 KEEEAEAVLADHDQRIAEAKAKLAaadKGKKVAVGQFRADGLRLYTPNSFAGSVLAALGFENPPKqskDNGYGYSEVSLE 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446801908 223 QLLAVNPAWLLVAHYREESIVKRWQQDPLWQMLTAAQKQQVASVDSNTWARMRGIFAAERIAADTVKIFHHQP 295
Cdd:COG4594 244 QLPALDPDVLFIATYDDPSILKEWKNNPLWKNLKAVKNGRVYEVDGDLWTRGRGPLAAELMADDLVEILLKKK 316
|
|
| FhuD |
cd01146 |
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ... |
35-284 |
1.47e-80 |
|
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: 244.50 E-value: 1.47e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 35 KTPQRIVVLELSFADALAAVDVSPIGIADDNDAKRILPEVRAHLKPWQSVGTRAQPSLEAIAALKPDLIIADSSRHAGVY 114
Cdd:cd01146 1 AKPQRIVALDWGALETLLALGVKPVGVADTAGYKPWIPEPALPLEGVVDVGTRGQPNLEAIAALKPDLILGSASRHDEIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 115 IALQQIAPVLLLKSRNeTYAENLQSAAIIGEMVGKKREMQARLEQHKERMAQWASQLPK--GTRVAF-GTSREQQFNLHT 191
Cdd:cd01146 81 DQLSQIAPTVLLDSSP-WLAEWKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKLPDkgPKPVSVvRFSDAGSIRLYG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 192 QETWTGSVLASLGLNVPAAMA---GASMPSIGLEQLLAVNPAWLLVAHYREESIVKRWQQDPLWQMLTAAQKQQVASVDS 268
Cdd:cd01146 160 PNSFAGSVLEDLGLQNPWAQEttnDSGFATISLERLAKADADVLFVFTYEDEELAQALQANPLWQNLPAVKNGRVYVVDD 239
|
250
....*....|....*.
gi 446801908 269 NTWARMRGIFAAERIA 284
Cdd:cd01146 240 VWWFFGGGLSAARLLL 255
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
41-269 |
1.76e-24 |
|
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: 98.59 E-value: 1.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 41 VVLELSFADALAAVDVSPIGIADDNDAKRILPEVRAHLKPwqSVGTRAQPSLEAIAALKPDLIIADSSRHAGV-YIALQQ 119
Cdd:pfam01497 1 AALSPAYTEILYALGATDSIVGVDAYTRDPLKADAVAAIV--KVGAYGEINVERLAALKPDLVILSTGYLTDEaEELLSL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 120 IAPVLLLKSRNeTYAENLQSAAIIGEMVGKKREMQARLEQHKERMA---QWASQLPKGTRVAFGTSREQQFNLHTQETWT 196
Cdd:pfam01497 79 IIPTVIFESSS-TGESLKEQIKQLGELLGLEDEAEELVAEIDSALAaakKAVPSLTRKPVLVFGGADGGGYVVAGSNTYI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446801908 197 GSVLASLGL-NVPAAMAGASMPSIGLEQLLAVNPAWLLVAHYREE--SIVKRWQQDPLWQMLTAAQKQQVASVDSN 269
Cdd:pfam01497 158 GDLLRILGIeNIAAELSGSEYAPISFEAILSSNPDVIIVSGRDSFtkTGPEFVAANPLWAGLPAVKNGRVYTLPSD 233
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| fecB |
PRK11411 |
iron-dicitrate transporter substrate-binding subunit; Provisional |
1-300 |
0e+00 |
|
iron-dicitrate transporter substrate-binding subunit; Provisional
Pssm-ID: 183123 [Multi-domain] Cd Length: 303 Bit Score: 557.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 1 MLAFIRFVFAGLLLV--ISHAFAATVQDEHGTFTLEKTPQRIVVLELSFADALAAVDVSPIGIADDNDAKRILPEVRAHL 78
Cdd:PRK11411 1 MLAFIRLLFAGLLLLsgSSHAFAVTVQDEQGTFTLEKTPQRIVVLELSFVDALAAVGVSPVGVADDNDAKRILPEVRAHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 79 KPWQSVGTRAQPSLEAIAALKPDLIIADSSRHAGVYIALQQIAPVLLLKSRNETYAENLQSAAIIGEMVGKKREMQARLE 158
Cdd:PRK11411 81 KPWQSVGTRSQPSLEAIAALKPDLIIADSSRHAGVYIALQKIAPTLLLKSRNETYQENLQSAAIIGEVLGKKREMQARIE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 159 QHKERMAQWASQLPKGTRVAFGTSREQQFNLHTQETWTGSVLASLGLNVP-AAMAGASMPSIGLEQLLAVNPAWLLVAHY 237
Cdd:PRK11411 161 QHKERMAQFASQLPKGTRVAFGTSREQQFNLHSPESYTGSVLAALGLNVPkAPMNGAAMPSISLEQLLALNPDWLLVAHY 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446801908 238 REESIVKRWQQDPLWQMLTAAQKQQVASVDSNTWARMRGIFAAERIAADTVKIFHHQPLTVVK 300
Cdd:PRK11411 241 RQESIVKRWQQDPLWQMLTAAKKQQVASVDSNTWARMRGIFAAERIAKDTVKIFHHQPLTVVK 303
|
|
| FecB |
COG4594 |
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ... |
2-295 |
7.40e-134 |
|
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443650 [Multi-domain] Cd Length: 316 Bit Score: 381.96 E-value: 7.40e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 2 LAFIRFVFAGLLLVI-------------SHAFAATVQDEHGTFTLEKTPQRIVVLELSFADALAAVDVSPIGIADDNDAK 68
Cdd:COG4594 4 LLLLLILLLALLLLAacgssssdsssseAAAGARTVKHAMGETTIPGTPKRVVVLEWSFADALLALGVTPVGIADDNDYD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 69 RILPEVRAHLKPWQSVGTRAQPSLEAIAALKPDLIIADSSRHAGVYIALQQIAPVLLLKSRNETYAENLQSAAIIGEMVG 148
Cdd:COG4594 84 RWVPYLRDLIKGVTSVGTRSQPNLEAIAALKPDLIIADKSRHEAIYDQLSKIAPTVLFKSRNGDYQENLESFKTIAKALG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 149 KKREMQARLEQHKERMAQWASQLP---KGTRVAFGTSREQQFNLHTQETWTGSVLASLGLNVPAA---MAGASMPSIGLE 222
Cdd:COG4594 164 KEEEAEAVLADHDQRIAEAKAKLAaadKGKKVAVGQFRADGLRLYTPNSFAGSVLAALGFENPPKqskDNGYGYSEVSLE 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446801908 223 QLLAVNPAWLLVAHYREESIVKRWQQDPLWQMLTAAQKQQVASVDSNTWARMRGIFAAERIAADTVKIFHHQP 295
Cdd:COG4594 244 QLPALDPDVLFIATYDDPSILKEWKNNPLWKNLKAVKNGRVYEVDGDLWTRGRGPLAAELMADDLVEILLKKK 316
|
|
| FhuD |
cd01146 |
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ... |
35-284 |
1.47e-80 |
|
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: 244.50 E-value: 1.47e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 35 KTPQRIVVLELSFADALAAVDVSPIGIADDNDAKRILPEVRAHLKPWQSVGTRAQPSLEAIAALKPDLIIADSSRHAGVY 114
Cdd:cd01146 1 AKPQRIVALDWGALETLLALGVKPVGVADTAGYKPWIPEPALPLEGVVDVGTRGQPNLEAIAALKPDLILGSASRHDEIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 115 IALQQIAPVLLLKSRNeTYAENLQSAAIIGEMVGKKREMQARLEQHKERMAQWASQLPK--GTRVAF-GTSREQQFNLHT 191
Cdd:cd01146 81 DQLSQIAPTVLLDSSP-WLAEWKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKLPDkgPKPVSVvRFSDAGSIRLYG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 192 QETWTGSVLASLGLNVPAAMA---GASMPSIGLEQLLAVNPAWLLVAHYREESIVKRWQQDPLWQMLTAAQKQQVASVDS 268
Cdd:cd01146 160 PNSFAGSVLEDLGLQNPWAQEttnDSGFATISLERLAKADADVLFVFTYEDEELAQALQANPLWQNLPAVKNGRVYVVDD 239
|
250
....*....|....*.
gi 446801908 269 NTWARMRGIFAAERIA 284
Cdd:cd01146 240 VWWFFGGGLSAARLLL 255
|
|
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
39-292 |
1.67e-39 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 138.98 E-value: 1.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 39 RIVVLELSFADALAAVDVSPIGIADDNDAKRILPEVRAHLKPwqSVGTRAQPSLEAIAALKPDLIIADSS-RHAGVYIAL 117
Cdd:COG0614 2 RIVSLSPSATELLLALGAGDRLVGVSDWGYCDYPELELKDLP--VVGGTGEPNLEAILALKPDLVLASSSgNDEEDYEQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 118 QQI-APVLLLKSRN-ETYAENLQsaaIIGEMVGKKREMQARLEQHKERMAQWASQLPKGT---RVAFGTSREQQFNLHTQ 192
Cdd:COG0614 80 EKIgIPVVVLDPRSlEDLYESIR---LLGELLGREERAEALIAEYEARLAAVRARLAGAEerpTVLYEIWSGDPLYTAGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 193 ETWTGSVLASLGLNVPAAMAGASMPSIGLEQLLAVNPAWLLVAHY-----REESIVKRWQQDPLWQMLTAAQKQQVASVD 267
Cdd:COG0614 157 GSFIGELLELAGGRNVAADLGGGYPEVSLEQVLALDPDVIILSGGgydaeTAEEALEALLADPGWQSLPAVKNGRVYVVP 236
|
250 260
....*....|....*....|....*..
gi 446801908 268 SNTWARM--RGIFAAERIAadtvKIFH 292
Cdd:COG0614 237 GDLLSRPgpRLLLALEDLA----KALH 259
|
|
| CeuA |
COG4607 |
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and ... |
6-271 |
2.86e-28 |
|
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443657 [Multi-domain] Cd Length: 310 Bit Score: 110.66 E-value: 2.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 6 RFVFAGLLLVISHAFAA-----------------TVQDEHGTFTLEKTPQRIVVLELSFADALAAVDVSPIGIADDNdak 68
Cdd:COG4607 3 KTLLAALALAAALALAAcgsssaaaasaaaaetvTVEHALGTVEVPKNPKRVVVFDNGALDTLDALGVEVAGVPKGL--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 69 riLPEvraHLKPWQS-----VGTRAQPSLEAIAALKPDLIIAdSSRHAGVYIALQQIAPVLLLKSRNETYAENL-QSAAI 142
Cdd:COG4607 80 --LPD---YLSKYADdkyanVGTLFEPDLEAIAALKPDLIII-GGRSAKKYDELSKIAPTIDLTVDGEDYLESLkRNTET 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 143 IGEMVGKKREMQARLEQHKERMAQWASQLPKGTRV-----------AFGtsreqqfnlhtqetwTGSVLASLG--LNVPA 209
Cdd:COG4607 154 LGEIFGKEDEAEELVADLDAKIAALKAAAAGKGTAlivltnggkisAYG---------------PGSRFGPIHdvLGFKP 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446801908 210 AMAGASMPS----IGLEQLLAVNPAWLLV-----AHYREESIVKRWQQDPLWQMLTAAQKQQVASVDSNTW 271
Cdd:COG4607 219 ADEDIEASThgqaISFEFIAEANPDWLFVidrdaAIGGEGPAAKQVLDNELVKQTTAWKNGQIVYLDPDAW 289
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
41-269 |
1.76e-24 |
|
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: 98.59 E-value: 1.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 41 VVLELSFADALAAVDVSPIGIADDNDAKRILPEVRAHLKPwqSVGTRAQPSLEAIAALKPDLIIADSSRHAGV-YIALQQ 119
Cdd:pfam01497 1 AALSPAYTEILYALGATDSIVGVDAYTRDPLKADAVAAIV--KVGAYGEINVERLAALKPDLVILSTGYLTDEaEELLSL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 120 IAPVLLLKSRNeTYAENLQSAAIIGEMVGKKREMQARLEQHKERMA---QWASQLPKGTRVAFGTSREQQFNLHTQETWT 196
Cdd:pfam01497 79 IIPTVIFESSS-TGESLKEQIKQLGELLGLEDEAEELVAEIDSALAaakKAVPSLTRKPVLVFGGADGGGYVVAGSNTYI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446801908 197 GSVLASLGL-NVPAAMAGASMPSIGLEQLLAVNPAWLLVAHYREE--SIVKRWQQDPLWQMLTAAQKQQVASVDSN 269
Cdd:pfam01497 158 GDLLRILGIeNIAAELSGSEYAPISFEAILSSNPDVIIVSGRDSFtkTGPEFVAANPLWAGLPAVKNGRVYTLPSD 233
|
|
| FeuA |
cd01138 |
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ... |
29-270 |
3.30e-23 |
|
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: 95.48 E-value: 3.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 29 GTFTLEKTPQRIVVLELSFADaLAAVDVSPIGIADDNDAKRILpevrAHLKPWQSVGTRAQPSLEAIAALKPDLIIAdSS 108
Cdd:cd01138 1 GEVEIPAKPKRIVALSGETEG-LALLGIKPVGAASIGGKNPYY----KKKTLAKVVGIVDEPNLEKVLELKPDLIIV-SS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 109 RHAGVYIALQQIAPVLLLKSRNETYAENLQSaaiIGEMVGKKREMQARLEQHKERMAQWASQLPK----GTRVAFGTSRE 184
Cdd:cd01138 75 KQEENYEKLSKIAPTVPVSYNSSDWEEQLKE---IGKLLNKEDEAEKWLADYKQKAKEAKEKIKKklgnDKSVAVLRGRK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 185 QQFNLHTQETWTGSVL-ASLGLNVPAAM----AGASMPSIGLEQLLAVNPAWLLVAHYREESIVKRWQQDPLWQMLTAAQ 259
Cdd:cd01138 152 QIYVFGEDGRGGGPILyADLGLKAPEKVkeieDKPGYAAISLEVLPEFDADYIFLLFFTGPEAKADFESLPIWKNLPAVK 231
|
250
....*....|.
gi 446801908 260 KQQVASVDSNT 270
Cdd:cd01138 232 NNHVYIVDAWV 242
|
|
| FatB |
cd01140 |
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ... |
28-271 |
1.57e-22 |
|
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: 94.25 E-value: 1.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 28 HGTFTLEKTPQRIVVLELSFADALAAVDVSPIGIADDndakRILPEVRAHLK--PWQSVGTRAQPSLEAIAALKPDLIIA 105
Cdd:cd01140 3 LGETKVPKNPEKVVVFDVGALDTLDALGVKVVGVPKS----STLPEYLKKYKddKYANVGTLFEPDLEAIAALKPDLIII 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 106 dSSRHAGVYIALQQIAP--VLLLKSRNeTYAENLQSAAIIGEMVGKKREMQARLEQHKERMAQWASQLPKGTRVAFGTSR 183
Cdd:cd01140 79 -GGRLAEKYDELKKIAPtiDLGADLKN-YLESVKQNIETLGKIFGKEEEAKELVAEIDASIAEAKSAAKGKKKALVVLVN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 184 EQQFNLHTQETWTGSVLASLGLNVPAAMAGASMP--SIGLEQLLAVNPAWLLVAhYREESIVKRWQQD------PLWQML 255
Cdd:cd01140 157 GGKLSAFGPGSRFGWLHDLLGFEPADENIKASSHgqPVSFEYILEANPDWLFVI-DRGAAIGAEGSSAkevldnDLVKNT 235
|
250
....*....|....*.
gi 446801908 256 TAAQKQQVASVDSNTW 271
Cdd:cd01140 236 TAWKNGKVIYLDPDLW 251
|
|
| TroA_e |
cd01142 |
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ... |
21-263 |
1.59e-21 |
|
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: 92.03 E-value: 1.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 21 AATVQDEHG-TFTLEKTPQRIVVLELSFADALAAVDVSPIGIADDNDAKRI--LPEVRAHLKPWQSVGTRAQPSLEAIAA 97
Cdd:cd01142 7 TRTITDMAGrKVTIPDEVKRIAALWGAGNAVVAALGGGKLIVATTSTVQQEpwLYRLAPSLENVATGGTGNDVNIEELLA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 98 LKPDLIIADSSRHAGVYIALQQIAPVLLLksRNETYAENLQSAAIIGEMVG---KKREMQARLEQHKERMAQWASQLPKG 174
Cdd:cd01142 87 LKPDVVIVWSTDGKEAGKAVLRLLNALSL--RDAELEEVKLTIALLGELLGrqeKAEALVAYFDDNLAYVAARTKKLPDS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 175 TRVAFGTSREQQFNLHTQETWTGSVLASLG-LNVPAAMAGASMPSIGLEQLLAVNPAWLLVAHYREESIVKrwqQDPLWQ 253
Cdd:cd01142 165 ERPRVYYAGPDPLTTDGTGSITNSWIDLAGgINVASEATKKGSGEVSLEQLLKWNPDVIIVGNADTKAAIL---ADPRWQ 241
|
250
....*....|
gi 446801908 254 MLTAAQKQQV 263
Cdd:cd01142 242 NLRAVKNGRV 251
|
|
| TroA-like |
cd00636 |
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ... |
38-179 |
3.36e-21 |
|
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: 87.61 E-value: 3.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 38 QRIVVLELSFADALAAVDVS--PIGIADDNDAKrilPEVRAHLKPWQSVGTRAQPSLEAIAALKPDLIIADSSRHAGVYI 115
Cdd:cd00636 1 KRVVALDPGATELLLALGGDdkPVGVADPSGYP---PEAKALLEKVPDVGHGYEPNLEKIAALKPDLIIANGSGLEAWLD 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446801908 116 ALQQIA-PVLLLKSRNE-TYAENLQSAAIIGEMVGKKREMQARLEQHKERMAQWASQLPKGTRVAF 179
Cdd:cd00636 78 KLSKIAiPVVVVDEASElSLENIKESIRLIGKALGKEENAEELIAELDARLAELRAKLAKIPKKKV 143
|
|
| FepB |
COG4592 |
ABC-type Fe2+-enterobactin transport system, periplasmic component [Inorganic ion transport ... |
23-263 |
2.14e-20 |
|
ABC-type Fe2+-enterobactin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443649 [Multi-domain] Cd Length: 330 Bit Score: 89.23 E-value: 2.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 23 TVQDEHGTFTLEKTPQRIVVLELSFADALAAVDV--------SPIGIADDN--------DAKRilpevrAHLKPWQSVgt 86
Cdd:COG4592 43 TVTTEKGTVTLPAKPQRIVSTSVTLTGSLLAIDApvvasgatTPNNVTDDQgffrqwadVAKE------RGVKRLYIG-- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 87 rAQPSLEAIAALKPDLII-----ADSSrhAGVYIALQQIAPVLLLksrNETYAENLQSAAIIGEMVGKKREMQARLEQHK 161
Cdd:COG4592 115 -LEPNAEAIAAAAPDLIIgsatgGDSA--LDLYDQLSAIAPTLVV---NYDDKSWQELATQLGEATGHEAQADAVIAAFD 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 162 ERMAQWAS--QLPKGTRVAFGTSREQQFNLHTQETWTGSVLASLGL---NVPAAMAGA-SMPS------IGLEQLLAV-- 227
Cdd:COG4592 189 ARVAEVKAaiTLPPQPVSALVYNEDGGANLWTPESAQGQLLQALGFtlaPLPAELATStSQGKrgdivqLSGENLAAAlt 268
|
250 260 270
....*....|....*....|....*....|....*.
gi 446801908 228 NPAWLLVAHyrEESIVKRWQQDPLWQMLTAAQKQQV 263
Cdd:COG4592 269 GPTLFLFAA--DDKDVDALKADPLLAHLPAVQAGRV 302
|
|
| PRK10957 |
PRK10957 |
iron-enterobactin transporter periplasmic binding protein; Provisional |
1-270 |
1.03e-14 |
|
iron-enterobactin transporter periplasmic binding protein; Provisional
Pssm-ID: 236806 [Multi-domain] Cd Length: 317 Bit Score: 73.08 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 1 MLAFIRFVFAGLLLV-ISHAFAA------TVQDEHGTFTLEKTPQRIVVLELSFADALAAVDVSPIG---------IADD 64
Cdd:PRK10957 1 PLYRLALLLLGLLLSgIAAAQASaagwprTVTDSRGSVTLESKPQRIVSTSVTLTGTLLAIDAPVIAsgattpntrVADD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 65 NDAKRILPEV--RAHLKP-WQSvgtraQPSLEAIAALKPDLII-----ADSSRHAgvYIALQQIAPVLLLKSRNETYAEn 136
Cdd:PRK10957 81 QGFFRQWSDVakERGVEVlYIG-----EPDAEAVAAQMPDLIVisatgGDSALAL--YDQLSAIAPTLVIDYDDKSWQE- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 137 lqSAAIIGEMVGKKREMQARLEQHKERMAQWAS--QLPKGTRVAFG-TSREQQFNLHTQETWTGSVLASLGL---NVPAA 210
Cdd:PRK10957 153 --LATQLGEATGLEKQAAAVIAQFDAQLAEVKAkiTLPPQPVSALVyNGAGHSANLWTPESAQGQLLEQLGFtlaELPAG 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 211 MAGASMPS-------IGLEQL---LAVNPAWLLVAhyrEESIVKRWQQDPLWQMLTAAQKQQVASVDSNT 270
Cdd:PRK10957 231 LQASTSQGkrhdiiqLGGENLaagLNGETLFLFAG---DDKDADAFLADPLLANLPAVQNKQVYALGTDT 297
|
|
| ChuT |
COG4558 |
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ... |
6-268 |
8.79e-11 |
|
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443619 [Multi-domain] Cd Length: 285 Bit Score: 61.36 E-value: 8.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 6 RFVFAGLLLVISHAFAAtvqdehGTFTLEKTPQRIVVL-----ELSFA----DALAAVDVS---PIGIADdndakriLPe 73
Cdd:COG4558 2 KRLALALLLLALAALAA------GASVAAAAAERIVSLggsvtEIVYAlgagDRLVGVDTTstyPAAAKA-------LP- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 74 vrahlkpwqSVGTRAQPSLEAIAALKPDLIIADSSrhAGVYIALQQIA----PVLLLKSRNeTYAENLQSAAIIGEMVGK 149
Cdd:COG4558 68 ---------DVGYMRQLSAEGILSLKPTLVLASEG--AGPPEVLDQLRaagvPVVVVPAAP-SLEGVLAKIRAVAAALGV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 150 K---REMQARLEQHKERMAQWASQLPKGTRVAFGTSREQ-QFNLHTQETWTGSVLASLGL-NVPAAMAGasMPSIGLEQL 224
Cdd:COG4558 136 PeagEALAARLEADLAALAARVAAIGKPPRVLFLLSRGGgRPMVAGRGTAADALIRLAGGvNAAAGFEG--YKPLSAEAL 213
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 446801908 225 LAVNPAWLLVAHYREESI--VKRWQQDPLWQMLTAAQKQQVASVDS 268
Cdd:COG4558 214 IAAAPDVILVMTRGLESLggVDGLLALPGLAQTPAGKNKRIVAMDD 259
|
|
| HemV-2 |
cd01147 |
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ... |
50-263 |
3.79e-10 |
|
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: 59.27 E-value: 3.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 50 ALAAVD-VSPIGIADDNDAKRILPEVRAHLKPWQSVGT---RAQPSLEAIAALKPDLIIaDSSRHAGVYIA--LQQIA-- 121
Cdd:cd01147 21 ALAAPDkIVGVDDAEKSDEGRPYFLASPELKDLPVIGRggrGNTPNYEKIAALKPDVVI-DVGSDDPTSIAddLQKKTgi 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 122 PVLLLKSRNeTYAENLQSAAIIGEMVGKKRE-------MQARLEQHKERMAqwasQLPKGTRVAFGTSREQQFNLH---- 190
Cdd:cd01147 100 PVVVLDGGD-SLEDTPEQIRLLGKVLGKEERaeelisfIESILADVEERTK----DIPDEEKPTVYFGRIGTKGAAgles 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446801908 191 TQETWTGSVLASLGLNVPAAMAGASMPSIGLEQLLAVNPAWLLVAHYREESIVKRWQQ-DPLWQMLTAAQKQQV 263
Cdd:cd01147 175 GLAGSIEVFELAGGINVADGLGGGGLKEVSPEQILLWNPDVIFLDTGSFYLSLEGYAKnRPFWQSLKAVKNGRV 248
|
|
| YvrC |
cd01143 |
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ... |
35-158 |
1.52e-09 |
|
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: 56.52 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 35 KTPQRIVVL-----ELSFA----DALAAVDvspigiADDNDAKRilpevrahLKPWQSVGTRAQPSLEAIAALKPDLIIA 105
Cdd:cd01143 1 KEPERIVSLspsitEILFAlgagDKIVGVD------TYSNYPKE--------VRKKPKVGSYSNPNVEKIVALKPDLVIV 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446801908 106 DSSRHAGVYIALQQIA-PVLLLKSRNeTYAENLQSAAIIGEMVGKKRE-------MQARLE 158
Cdd:cd01143 67 SSSSLAELLEKLKDAGiPVVVLPAAS-SLDEIYDQIELIGKITGAEEEaeklvkeMKQKID 126
|
|
| BtuF |
cd01144 |
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ... |
38-285 |
8.15e-09 |
|
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: 55.00 E-value: 8.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 38 QRIVVLELSFADALAAVDVSP--IGIADDND---AKRILPEVRAHLkpwqsvgtraQPSLEAIAALKPDLIIADSSRHAG 112
Cdd:cd01144 1 MRIVSLAPSATELLYALGLGDqlVGVTDYCDyppEAKKLPRVGGFY----------QLDLERVLALKPDLVIAWDDCNVC 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 113 VYIALQQIAPVLLLKSRNETYAENLQSAAIIGEMVGKKREMQARLEQHKERMAQWASQLPKGT--RVAFGTSREQQFNLh 190
Cdd:cd01144 71 AVVDQLRAAGIPVLVSEPQTLDDILADIRRLGTLAGRPARAEELAEALRRRLAALRKQYASKPppRVFYQEWIDPLMTA- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 191 tQETWTGSVLASLGLNVPAAMAGASMPSIGLEQLLAVNPAWLLVAHYREESIVKRWQQDPLWQMLTAAQKQQVASVDSNT 270
Cdd:cd01144 150 -GGDWVPELIALAGGVNVFADAGERSPQVSWEDVLAANPDVIVLSPCGFGFTPAILRKEPAWQALPAVRNGRVYAVDGNW 228
|
250
....*....|....*..
gi 446801908 271 WAR--MRGIFAAERIAA 285
Cdd:cd01144 229 YFRpsPRLVDGLEQLAA 245
|
|
| TroA_d |
cd01141 |
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ... |
32-195 |
1.39e-07 |
|
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: 50.88 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 32 TLEKTPQRIVVLELSFADALAAVDVSP--IGIAD-DNDAKRilPEVRAhlKPWQSVGTRAQPSLEAIAALKPDLII-ADS 107
Cdd:cd01141 3 TIKVPPKRIVVLSPTHVDLLLALDKADkiVGVSAsAYDLNT--PAVKE--RIDIQVGPTGSLNVELIVALKPDLVIlYGG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 108 SRHAGVYIALQQIAPVLLLKSRNETYAENLQSAAIIGEMVGKKREMQARleqhkERMAQWAS---QLPKGtrVAFGTSRE 184
Cdd:cd01141 79 FQAQTILDKLEQLGIPVLYVNEYPSPLGRAEWIKFAAAFYGVGKEDKAD-----EAFAQIAGryrDLAKK--VSNLNKPT 151
|
170
....*....|.
gi 446801908 185 QQFNLHTQETW 195
Cdd:cd01141 152 VAIGKPVKGLW 162
|
|
| HutB |
cd01149 |
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ... |
37-267 |
1.03e-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: 48.80 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 37 PQRIVVL-----ELSFA----DALAAVDVSPIgiaddndakriLPEVRAHLKpwqSVGTRAQPSLEAIAALKPDLIIAds 107
Cdd:cd01149 1 PERIVSLggsvtEIVYAlgagDRLVGVDSTST-----------YPEAAAKLP---DVGYMRQLSAEGVLSLKPTLVIA-- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 108 SRHAGVYIALQQIA----PVLLLksrNETYAEN--LQSAAIIGEMVG---KKREMQARLEQHKERMAQWASQLPKGTRVA 178
Cdd:cd01149 65 SDEAGPPEALDQLRaagvPVVTV---PSTPTLDglLTKIRQVAQALGvpeKGEALAQEVRQRLAALRKTVAAHKKPPRVL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 179 FGTSRE-QQFNLHTQETWTGSVLASLGLnVPAAMAGASMPSIGLEQLLAVNPAWLLVAHYREES---IVKRWQQdPLWQM 254
Cdd:cd01149 142 FLLSHGgGAAMAAGRNTAADAIIALAGA-VNAAAGFRGYKPLSAEALIAAQPDVILVMSRGLDAvggVDGLLKL-PGLAQ 219
|
250
....*....|...
gi 446801908 255 LTAAQKQQVASVD 267
Cdd:cd01149 220 TPAGRNKRILAMD 232
|
|
| TroA_a |
cd01148 |
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ... |
20-284 |
2.17e-04 |
|
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: 41.94 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 20 FAATVQDEHGTFTLEKTPQRIVVLELSFADALAAVDVSPIGIADDNDAKRILPEVRAHLKPWQSVGTRaQPSLEAIAALK 99
Cdd:cd01148 1 YPLTVENCGRSVTFDKAPQRVVSNDQNTTEMMLALGLQDRMVGTAGIDNKDLPELKAKYDKVPELAKK-YPSKETVLAAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 100 PDLIIADSSRHAGVYIAL--QQIAP----VLLLKSR----------NETYAENLQSAAIIG-EMVGKK--REMQARLEQH 160
Cdd:cd01148 80 PDLVFGGWSYGFDKGGLGtpDSLAElgikTYILPEScgqrrgeatlDDVYNDIRNLGKIFDvEDRADKlvADLKARLAEI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 161 KERMAQWAsqlpKGTRVAFGTSREqqfnLHTQETWTGS----VLASLGL-NVPAAMAgASMPSIGLEQLLAVNPAWLLVA 235
Cdd:cd01148 160 SAKVKGDG----KKVAVFVYDSGE----DKPFTSGRGGipnaIITAAGGrNVFADVD-ESWTTVSWETVIARNPDVIVII 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 446801908 236 HY----REESIVKRWQQDPLWQMLTAAQKQQVASVD-SNTWARMRGIFAAERIA 284
Cdd:cd01148 231 DYgdqnAAEQKIKFLKENPALKNVPAVKNNRFIVLPlAEATPGIRNVDAIEKLA 284
|
|
| PRK10576 |
PRK10576 |
Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD; |
37-266 |
1.29e-03 |
|
Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD;
Pssm-ID: 236719 Cd Length: 292 Bit Score: 39.61 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 37 PQRIVVLELSFADALAAVDVSPIGIADDNDAKRIL--PEVRAHLKpwqSVGTRAQPSLEAIAALKPDLIIAdSSRHAGVY 114
Cdd:PRK10576 32 PNRIVALEWLPVELLLALGVTPYGVADTHNYRLWVsePALPDSVI---DVGLRTEPNLELLTQMKPSLILW-SAGYGPSP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 115 IALQQIAPVL--LLKSRNETYAENLQSAAIIGEMVGKKREMQARLEQHKERMAQWASQL-PKGTR-------------VA 178
Cdd:PRK10576 108 EKLARIAPGRgfAFSDGKKPLAVARKSLVELAQRLNLEAAAETHLAQFDDFIASAKPRLaGRGQRpllltslidprhaLV 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446801908 179 FGTsreqqfNLHTQEtwtgsVLASLGLnvPAAMAGAS----MPSIGLEQLLAVNPAWLLVAHYREESIVKRWQQDPLWQM 254
Cdd:PRK10576 188 FGP------NSLFQE-----VLDELGI--ENAWQGETnfwgSTVVGIERLAAYKDADVICFDHGNSKDMQQLMATPLWQA 254
|
250
....*....|..
gi 446801908 255 LTAAQKQQVASV 266
Cdd:PRK10576 255 MPFVRAGRFQRV 266
|
|
| |
