|
Name |
Accession |
Description |
Interval |
E-value |
| ChuT |
COG4558 |
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ... |
1-282 |
3.30e-91 |
|
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443619 [Multi-domain] Cd Length: 285 Bit Score: 272.06 E-value: 3.30e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333407657 1 MKKLALAFsLFLSIPFLSMESAYAQQETQannRIISAGSSITELLIALGAKDQLIAVDVTSRKYNADEALPQVGYHRQLS 80
Cdd:COG4558 1 MKRLALAL-LLLALAALAAGASVAAAAAE---RIVSLGGSVTEIVYALGAGDRLVGVDTTSTYPAAAKALPDVGYMRQLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333407657 81 AEGLMALSPTHLIGSHEMGPENTLTLLKSGGIKVETVPSGDTEEDLFGRIDKIAQITGTQEKAKALKASIDKQLNELKSR 160
Cdd:COG4558 77 AEGILSLKPTLVLASEGAGPPEVLDQLRAAGVPVVVVPAAPSLEGVLAKIRAVAAALGVPEAGEALAARLEADLAALAAR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333407657 161 --KLEHQPKVLFAMLTKGRPATIAGDQTTIDVIINLAGGQNPAkSEMSSYKPLTAEAIVQMQPDFLLVSTRAWEALGGHE 238
Cdd:COG4558 157 vaAIGKPPRVLFLLSRGGGRPMVAGRGTAADALIRLAGGVNAA-AGFEGYKPLSAEALIAAAPDVILVMTRGLESLGGVD 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1333407657 239 GILKeFPLLAATPvAGK-DRIIPVSSSAIIgGFGLES----LELTDKLY 282
Cdd:COG4558 236 GLLA-LPGLAQTP-AGKnKRIVAMDDLLLL-GFGPRTpqaaLALAQALY 281
|
|
| HutB |
cd01149 |
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ... |
33-261 |
6.82e-79 |
|
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: 239.09 E-value: 6.82e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333407657 33 RIISAGSSITELLIALGAKDQLIAVDVTSRKYNADEALPQVGYHRQLSAEGLMALSPTHLIGSHEMGPENTLTLLKSGGI 112
Cdd:cd01149 3 RIVSLGGSVTEIVYALGAGDRLVGVDSTSTYPEAAAKLPDVGYMRQLSAEGVLSLKPTLVIASDEAGPPEALDQLRAAGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333407657 113 KVETVPSGDTEEDLFGRIDKIAQITGTQEKAKALKASIDKQLNELKSRKLEHQ--PKVLFAMLTKGRPATIAGDQTTIDV 190
Cdd:cd01149 83 PVVTVPSTPTLDGLLTKIRQVAQALGVPEKGEALAQEVRQRLAALRKTVAAHKkpPRVLFLLSHGGGAAMAAGRNTAADA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1333407657 191 IINLAGGQNPAkSEMSSYKPLTAEAIVQMQPDFLLVSTRAWEALGGHEGILKeFPLLAATPvAGKD-RIIPV 261
Cdd:cd01149 163 IIALAGAVNAA-AGFRGYKPLSAEALIAAQPDVILVMSRGLDAVGGVDGLLK-LPGLAQTP-AGRNkRILAM 231
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
35-259 |
4.23e-35 |
|
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: 126.33 E-value: 4.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333407657 35 ISAGSSITELLIALGAKDQLIAVDVTSR---KYNADEALPQVGYHRQLSAEGLMALSPTHLIGSHEMGPENTLTLLKSGg 111
Cdd:pfam01497 1 AALSPAYTEILYALGATDSIVGVDAYTRdplKADAVAAIVKVGAYGEINVERLAALKPDLVILSTGYLTDEAEELLSLI- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333407657 112 IKVETVPSGDTEEDLFGRIDKIAQITGTQEKAKALKASIDKQLNELKSR-KLEHQPKVLFAMLTKGRPATIAGDQTTIDV 190
Cdd:pfam01497 80 IPTVIFESSSTGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAvPSLTRKPVLVFGGADGGGYVVAGSNTYIGD 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333407657 191 IINLAGGQNPAKSEM-SSYKPLTAEAIVQMQPDFLLVSTRAWEALGGHEGILKEfPLLAATPVAGKDRII 259
Cdd:pfam01497 160 LLRILGIENIAAELSgSEYAPISFEAILSSNPDVIIVSGRDSFTKTGPEFVAAN-PLWAGLPAVKNGRVY 228
|
|
| btuF |
PRK09534 |
corrinoid ABC transporter substrate-binding protein; Reviewed |
33-230 |
1.09e-13 |
|
corrinoid ABC transporter substrate-binding protein; Reviewed
Pssm-ID: 236552 [Multi-domain] Cd Length: 359 Bit Score: 70.32 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333407657 33 RIISAGSSITELLIALGAKDQLIAV-------DVTSRKYNADEALPQvgyhrQLSAEGLMALSPThLIGSHEMGPENTLT 105
Cdd:PRK09534 62 RVVTLNPSAAQTMWELGARDRVVGVtqyasylDGAEERTNVSGGQPF-----GVNVEAVVGLDPD-LVLAPNAVAGDTVT 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333407657 106 LLKSGGIKVETVPSGDTEEDLFGRIDKIAQITGTQEKAKALKASIDKQLNELKSR--KLEHQPKVLFAmLTKGRpatIAG 183
Cdd:PRK09534 136 RLREAGITVFHFPAATSIEDVAEKTATIGRLTGNCEAAAETNAEMRDRVDAVEDRtaDVDDRPRVLYP-LGDGY---TAG 211
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1333407657 184 DQTTIDVIINLAGGQN-PAKSEMSSYKPLTAEAIVQMQPDFLLVSTRA 230
Cdd:PRK09534 212 GNTFIGALIEAAGGHNvAADATTDGYPQLSEEVIVQQDPDVIVVATAS 259
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ChuT |
COG4558 |
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ... |
1-282 |
3.30e-91 |
|
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443619 [Multi-domain] Cd Length: 285 Bit Score: 272.06 E-value: 3.30e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333407657 1 MKKLALAFsLFLSIPFLSMESAYAQQETQannRIISAGSSITELLIALGAKDQLIAVDVTSRKYNADEALPQVGYHRQLS 80
Cdd:COG4558 1 MKRLALAL-LLLALAALAAGASVAAAAAE---RIVSLGGSVTEIVYALGAGDRLVGVDTTSTYPAAAKALPDVGYMRQLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333407657 81 AEGLMALSPTHLIGSHEMGPENTLTLLKSGGIKVETVPSGDTEEDLFGRIDKIAQITGTQEKAKALKASIDKQLNELKSR 160
Cdd:COG4558 77 AEGILSLKPTLVLASEGAGPPEVLDQLRAAGVPVVVVPAAPSLEGVLAKIRAVAAALGVPEAGEALAARLEADLAALAAR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333407657 161 --KLEHQPKVLFAMLTKGRPATIAGDQTTIDVIINLAGGQNPAkSEMSSYKPLTAEAIVQMQPDFLLVSTRAWEALGGHE 238
Cdd:COG4558 157 vaAIGKPPRVLFLLSRGGGRPMVAGRGTAADALIRLAGGVNAA-AGFEGYKPLSAEALIAAAPDVILVMTRGLESLGGVD 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1333407657 239 GILKeFPLLAATPvAGK-DRIIPVSSSAIIgGFGLES----LELTDKLY 282
Cdd:COG4558 236 GLLA-LPGLAQTP-AGKnKRIVAMDDLLLL-GFGPRTpqaaLALAQALY 281
|
|
| HutB |
cd01149 |
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ... |
33-261 |
6.82e-79 |
|
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: 239.09 E-value: 6.82e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333407657 33 RIISAGSSITELLIALGAKDQLIAVDVTSRKYNADEALPQVGYHRQLSAEGLMALSPTHLIGSHEMGPENTLTLLKSGGI 112
Cdd:cd01149 3 RIVSLGGSVTEIVYALGAGDRLVGVDSTSTYPEAAAKLPDVGYMRQLSAEGVLSLKPTLVIASDEAGPPEALDQLRAAGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333407657 113 KVETVPSGDTEEDLFGRIDKIAQITGTQEKAKALKASIDKQLNELKSRKLEHQ--PKVLFAMLTKGRPATIAGDQTTIDV 190
Cdd:cd01149 83 PVVTVPSTPTLDGLLTKIRQVAQALGVPEKGEALAQEVRQRLAALRKTVAAHKkpPRVLFLLSHGGGAAMAAGRNTAADA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1333407657 191 IINLAGGQNPAkSEMSSYKPLTAEAIVQMQPDFLLVSTRAWEALGGHEGILKeFPLLAATPvAGKD-RIIPV 261
Cdd:cd01149 163 IIALAGAVNAA-AGFRGYKPLSAEALIAAQPDVILVMSRGLDAVGGVDGLLK-LPGLAQTP-AGRNkRILAM 231
|
|
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
33-285 |
6.20e-44 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 150.15 E-value: 6.20e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333407657 33 RIISAGSSITELLIALGAKDQLIAVD---VTSRKYNADEALPQVGYHRQLSAEGLMALSPTHLIGSHEMGPENTLTLLKS 109
Cdd:COG0614 2 RIVSLSPSATELLLALGAGDRLVGVSdwgYCDYPELELKDLPVVGGTGEPNLEAILALKPDLVLASSSGNDEEDYEQLEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333407657 110 GGIKVETVPSGDTEeDLFGRIDKIAQITGTQEKAKALKASIDKQLNELKSR--KLEHQPKVLFAMLTkGRPATIAGDQTT 187
Cdd:COG0614 82 IGIPVVVLDPRSLE-DLYESIRLLGELLGREERAEALIAEYEARLAAVRARlaGAEERPTVLYEIWS-GDPLYTAGGGSF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333407657 188 IDVIINLAGGQNPAKSEMSSYKPLTAEAIVQMQPDFLLVSTRAWEALGGHEGI--LKEFPLLAATPVAGKDRIIPVSSSA 265
Cdd:COG0614 160 IGELLELAGGRNVAADLGGGYPEVSLEQVLALDPDVIILSGGGYDAETAEEALeaLLADPGWQSLPAVKNGRVYVVPGDL 239
|
250 260
....*....|....*....|
gi 1333407657 266 IIGGfGLESLELTDKLYKTF 285
Cdd:COG0614 240 LSRP-GPRLLLALEDLAKAL 258
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
35-259 |
4.23e-35 |
|
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: 126.33 E-value: 4.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333407657 35 ISAGSSITELLIALGAKDQLIAVDVTSR---KYNADEALPQVGYHRQLSAEGLMALSPTHLIGSHEMGPENTLTLLKSGg 111
Cdd:pfam01497 1 AALSPAYTEILYALGATDSIVGVDAYTRdplKADAVAAIVKVGAYGEINVERLAALKPDLVILSTGYLTDEAEELLSLI- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333407657 112 IKVETVPSGDTEEDLFGRIDKIAQITGTQEKAKALKASIDKQLNELKSR-KLEHQPKVLFAMLTKGRPATIAGDQTTIDV 190
Cdd:pfam01497 80 IPTVIFESSSTGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAvPSLTRKPVLVFGGADGGGYVVAGSNTYIGD 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333407657 191 IINLAGGQNPAKSEM-SSYKPLTAEAIVQMQPDFLLVSTRAWEALGGHEGILKEfPLLAATPVAGKDRII 259
Cdd:pfam01497 160 LLRILGIENIAAELSgSEYAPISFEAILSSNPDVIIVSGRDSFTKTGPEFVAAN-PLWAGLPAVKNGRVY 228
|
|
| YvrC |
cd01143 |
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ... |
30-226 |
2.50e-32 |
|
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: 118.15 E-value: 2.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333407657 30 ANNRIISAGSSITELLIALGAKDQLIAVDVTS-RKYNADEALPQVGYHrQLSAEGLMALSPThLIGSHEMGPENTLTLLK 108
Cdd:cd01143 2 EPERIVSLSPSITEILFALGAGDKIVGVDTYSnYPKEVRKKPKVGSYS-NPNVEKIVALKPD-LVIVSSSSLAELLEKLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333407657 109 SGGIKVETVPSGDTEEDLFGRIDKIAQITGTQEKAKALKASIDKQLNELKSRKLEHQPKVLFAMLTKGRPATiAGDQTTI 188
Cdd:cd01143 80 DAGIPVVVLPAASSLDEIYDQIELIGKITGAEEEAEKLVKEMKQKIDKVKDKGKTIKKSKVYIEVSLGGPYT-AGKNTFI 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 1333407657 189 DVIINLAGGQNPAkSEMSSYKPLTAEAIVQMQPDFLLV 226
Cdd:cd01143 159 NELIRLAGAKNIA-ADSGGWPQVSPEEILKANPDVIIL 195
|
|
| TroA_a |
cd01148 |
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ... |
28-269 |
3.95e-21 |
|
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: 90.47 E-value: 3.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333407657 28 TQANNRIISAGSSITELLIALGAKDQLIA-----VDVTSRKYNADEALPQVGyHRQLSAEGLMALSPTHLIG--SHEMGP 100
Cdd:cd01148 15 DKAPQRVVSNDQNTTEMMLALGLQDRMVGtagidNKDLPELKAKYDKVPELA-KKYPSKETVLAARPDLVFGgwSYGFDK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333407657 101 ENTLTL--LKSGGIKVETVPSG-------DTEEDLFGRIDKIAQITGTQEKAKALKASIDKQLNELKSR--KLEHQPKVL 169
Cdd:cd01148 94 GGLGTPdsLAELGIKTYILPEScgqrrgeATLDDVYNDIRNLGKIFDVEDRADKLVADLKARLAEISAKvkGDGKKVAVF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333407657 170 FAMLTKGRPATiAGDQTTIDVIINLAGGQNPAKSEMSSYKPLTAEAIVQMQPDFLLV----STRAWEALgghEGILKEFP 245
Cdd:cd01148 174 VYDSGEDKPFT-SGRGGIPNAIITAAGGRNVFADVDESWTTVSWETVIARNPDVIVIidygDQNAAEQK---IKFLKENP 249
|
250 260
....*....|....*....|....
gi 1333407657 246 LLAATPVAGKDRIIPVSSSAIIGG 269
Cdd:cd01148 250 ALKNVPAVKNNRFIVLPLAEATPG 273
|
|
| BtuF |
cd01144 |
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ... |
33-266 |
1.82e-20 |
|
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: 87.74 E-value: 1.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333407657 33 RIISAGSSITELLIALGAKDQLIAVDVTSrKYNADEA-LPQVGYHRQLSAEGLMALSPTHLIGSHEMGPENTLTLLKSGG 111
Cdd:cd01144 2 RIVSLAPSATELLYALGLGDQLVGVTDYC-DYPPEAKkLPRVGGFYQLDLERVLALKPDLVIAWDDCNVCAVVDQLRAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333407657 112 IKVETVPsGDTEEDLFGRIDKIAQITGTQEKAKALKASIDKQLNELKSRKL-EHQPKVLFAMLTKgrPaTIAGDQTTIDV 190
Cdd:cd01144 81 IPVLVSE-PQTLDDILADIRRLGTLAGRPARAEELAEALRRRLAALRKQYAsKPPPRVFYQEWID--P-LMTAGGDWVPE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1333407657 191 IINLAGGQNPAKSEMSSYKPLTAEAIVQMQPDFLLVStraWEALGGHEGILKEFPLLAATPVAGKDRIIPVSSSAI 266
Cdd:cd01144 157 LIALAGGVNVFADAGERSPQVSWEDVLAANPDVIVLS---PCGFGFTPAILRKEPAWQALPAVRNGRVYAVDGNWY 229
|
|
| TroA-like |
cd00636 |
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ... |
33-160 |
1.43e-18 |
|
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function in the ABC transport of ferric siderophores and metal ions such as Mn2+, Fe3+, Cu2+ and/or Zn2+. Their ligand binding site is formed in the interface between two globular domains linked by a single helix. Many of these proteins also possess a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence). The TroA-like proteins differ in their fold and ligand-binding mechanism from the PBPI and PBPII proteins, but are structurally similar, however, to the beta-subunit of the nitrogenase molybdenum-iron protein MoFe. Most TroA-like proteins are encoded by ABC-type operons and appear to function as periplasmic components of ABC transporters in metal ion uptake.
Pssm-ID: 238347 [Multi-domain] Cd Length: 148 Bit Score: 80.30 E-value: 1.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333407657 33 RIISAGSSITELLIALGAKDQLIAVDVTS----RKYNADEALPQVGYHRQLSAEGLMALSPTHLIGShEMGPENTLTLLK 108
Cdd:cd00636 2 RVVALDPGATELLLALGGDDKPVGVADPSgyppEAKALLEKVPDVGHGYEPNLEKIAALKPDLIIAN-GSGLEAWLDKLS 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1333407657 109 SGGIKVETVP--SGDTEEDLFGRIDKIAQITGTQEKAKALKASIDKQLNELKSR 160
Cdd:cd00636 81 KIAIPVVVVDeaSELSLENIKESIRLIGKALGKEENAEELIAELDARLAELRAK 134
|
|
| HemV-2 |
cd01147 |
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ... |
32-248 |
1.29e-16 |
|
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: 77.38 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333407657 32 NRIISAGSSITELLIALGAKDQLIAVD-----VTSRKYNAdeALPQV---------GYHRQLSAEGLMALSPTHLIGSHE 97
Cdd:cd01147 6 ERVVAAGPGALRLLYALAAPDKIVGVDdaeksDEGRPYFL--ASPELkdlpvigrgGRGNTPNYEKIAALKPDVVIDVGS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333407657 98 MGPENTL-TLLKSGGIKVETVPSGDTEEDLFGRIDKIAQITGTQEKAKALKASIDKQLNELKSR----KLEHQPKVLFAM 172
Cdd:cd01147 84 DDPTSIAdDLQKKTGIPVVVLDGGDSLEDTPEQIRLLGKVLGKEERAEELISFIESILADVEERtkdiPDEEKPTVYFGR 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1333407657 173 LTKGRPATIAGDQTTIDVIINLAGGQNPAKS-EMSSYKPLTAEAIVQMQPDFLLVSTRAWEALGghEGILKEFPLLA 248
Cdd:cd01147 164 IGTKGAAGLESGLAGSIEVFELAGGINVADGlGGGGLKEVSPEQILLWNPDVIFLDTGSFYLSL--EGYAKNRPFWQ 238
|
|
| TroA_e |
cd01142 |
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ... |
32-230 |
5.22e-15 |
|
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: 73.54 E-value: 5.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333407657 32 NRIISAGSSITELLIALGAKDQLIAVdvTSRKYNAD---------EALPQVGYHRQLSAEGLMALSPTHLIGSHEMGPEn 102
Cdd:cd01142 25 KRIAALWGAGNAVVAALGGGKLIVAT--TSTVQQEPwlyrlapslENVATGGTGNDVNIEELLALKPDVVIVWSTDGKE- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333407657 103 tltllkSGGIKVETVPSG----DTEEDLFGRIDKIAQITGTQEKAKALKASIDKQLNELKSR----KLEHQPKVLFAMlt 174
Cdd:cd01142 102 ------AGKAVLRLLNALslrdAELEEVKLTIALLGELLGRQEKAEALVAYFDDNLAYVAARtkklPDSERPRVYYAG-- 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333407657 175 kGRPATIAGDQTTIDVIINLAGGQNPA----KSEMSSYkplTAEAIVQMQPDFLLVSTRA 230
Cdd:cd01142 174 -PDPLTTDGTGSITNSWIDLAGGINVAseatKKGSGEV---SLEQLLKWNPDVIIVGNAD 229
|
|
| btuF |
PRK09534 |
corrinoid ABC transporter substrate-binding protein; Reviewed |
33-230 |
1.09e-13 |
|
corrinoid ABC transporter substrate-binding protein; Reviewed
Pssm-ID: 236552 [Multi-domain] Cd Length: 359 Bit Score: 70.32 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333407657 33 RIISAGSSITELLIALGAKDQLIAV-------DVTSRKYNADEALPQvgyhrQLSAEGLMALSPThLIGSHEMGPENTLT 105
Cdd:PRK09534 62 RVVTLNPSAAQTMWELGARDRVVGVtqyasylDGAEERTNVSGGQPF-----GVNVEAVVGLDPD-LVLAPNAVAGDTVT 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333407657 106 LLKSGGIKVETVPSGDTEEDLFGRIDKIAQITGTQEKAKALKASIDKQLNELKSR--KLEHQPKVLFAmLTKGRpatIAG 183
Cdd:PRK09534 136 RLREAGITVFHFPAATSIEDVAEKTATIGRLTGNCEAAAETNAEMRDRVDAVEDRtaDVDDRPRVLYP-LGDGY---TAG 211
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1333407657 184 DQTTIDVIINLAGGQN-PAKSEMSSYKPLTAEAIVQMQPDFLLVSTRA 230
Cdd:PRK09534 212 GNTFIGALIEAAGGHNvAADATTDGYPQLSEEVIVQQDPDVIVVATAS 259
|
|
| FhuD |
cd01146 |
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ... |
33-280 |
7.45e-13 |
|
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: 66.93 E-value: 7.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333407657 33 RIISAGSSITELLIALGAKDQLIAVDVTSRKYNADEALP-----QVGYHRQLSAEGLMALSPTHLIGSHEMGPENTLTLl 107
Cdd:cd01146 5 RIVALDWGALETLLALGVKPVGVADTAGYKPWIPEPALPlegvvDVGTRGQPNLEAIAALKPDLILGSASRHDEIYDQL- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333407657 108 kSGGIKVETVPSGDTEEDLFGRIDKIAQITGTQEKAKALKASIDKQLNELKSR-KLEHQPKVLFAMLTKGRPATIAGDQT 186
Cdd:cd01146 84 -SQIAPTVLLDSSPWLAEWKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKlPDKGPKPVSVVRFSDAGSIRLYGPNS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333407657 187 TIDVIINLAGGQNP---AKSEMSSYKPLTAEAIVQMQPDFLLVSTRAWEALGGHegiLKEFPLLAATPVAGKDRIIPVSS 263
Cdd:cd01146 163 FAGSVLEDLGLQNPwaqETTNDSGFATISLERLAKADADVLFVFTYEDEELAQA---LQANPLWQNLPAVKNGRVYVVDD 239
|
250
....*....|....*..
gi 1333407657 264 SAIIGGFGLESLELTDK 280
Cdd:cd01146 240 VWWFFGGGLSAARLLLD 256
|
|
| FatB |
cd01140 |
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ... |
33-283 |
1.40e-12 |
|
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: 66.13 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333407657 33 RIISAGSSITELLIALGAKdqLIAVDVTSR-----KYNADEALPQVGYHRQLSAEGLMALSPTHLIGSHEMGpENTLTLL 107
Cdd:cd01140 14 KVVVFDVGALDTLDALGVK--VVGVPKSSTlpeylKKYKDDKYANVGTLFEPDLEAIAALKPDLIIIGGRLA-EKYDELK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333407657 108 KSGGIKVETVPSGDTEEDLFGRIDKIAQITGTQEKAKALKASIDKQLNELKSrKLEHQPKVLFAMLTKGRpATIAGDQTT 187
Cdd:cd01140 91 KIAPTIDLGADLKNYLESVKQNIETLGKIFGKEEEAKELVAEIDASIAEAKS-AAKGKKKALVVLVNGGK-LSAFGPGSR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333407657 188 IDVIINLAGGQNPAKSEMSS--YKPLTAEAIVQMQPDFLLVSTRAwEALGGHEGILKEF---PLLAATPVAGKDRIIPVS 262
Cdd:cd01140 169 FGWLHDLLGFEPADENIKASshGQPVSFEYILEANPDWLFVIDRG-AAIGAEGSSAKEVldnDLVKNTTAWKNGKVIYLD 247
|
250 260
....*....|....*....|...
gi 1333407657 263 SSA-IIGGFGLESLE-LTDKLYK 283
Cdd:cd01140 248 PDLwYLSGGGLESLKqMIDDLKK 270
|
|
| TroA_d |
cd01141 |
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ... |
32-197 |
1.87e-09 |
|
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: 55.89 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333407657 32 NRIISAGSSITELLIALGAKDQLIAVDVTS-RKYNADEA---LPQVGYHRQLSAEGLMALSPTHLIGSHEMGPENTLTLL 107
Cdd:cd01141 9 KRIVVLSPTHVDLLLALDKADKIVGVSASAyDLNTPAVKeriDIQVGPTGSLNVELIVALKPDLVILYGGFQAQTILDKL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333407657 108 KSGGIKVETVPSGDTEEdlfGRIDKI----AQ-ITGTQEKAKALKASIDKQLNELKSR-KLEHQPKVLFAMLTKGRPAtI 181
Cdd:cd01141 89 EQLGIPVLYVNEYPSPL---GRAEWIkfaaAFyGVGKEDKADEAFAQIAGRYRDLAKKvSNLNKPTVAIGKPVKGLWY-M 164
|
170
....*....|....*.
gi 1333407657 182 AGDQTTIDVIINLAGG 197
Cdd:cd01141 165 PGGNSYVAKMLRDAGG 180
|
|
| PRK03379 |
PRK03379 |
vitamin B12-transporter protein BtuF; Provisional |
30-199 |
1.36e-07 |
|
vitamin B12-transporter protein BtuF; Provisional
Pssm-ID: 179575 [Multi-domain] Cd Length: 260 Bit Score: 51.61 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333407657 30 ANNRIISAGSSITELLIALGAKDqlIAVDVTSRKYNADEALPQVGYHRQLSAEGLMALSPTHLIGSHEMGPENTLTLLKS 109
Cdd:PRK03379 16 AAPRVITLSPANTELAFAAGITP--VGVSSYSDYPPQAKKIEQVATWQGMNLERIVALKPDLVLAWRGGNAERQVDQLAS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333407657 110 GGIKVETVpSGDTEEDLFGRIDKIAQITGTQEKAKALKASIDKQLNELKSRKLEHQPKVLFamLTKG-RPATIAGDQTTI 188
Cdd:PRK03379 94 LGIKVMWV-DATSIEQIANALRQLAPWSPQPEKAEQAAQSLLQQYAALKAQYADKPKKRVF--LQFGtNPLFTSGKHSIQ 170
|
170
....*....|.
gi 1333407657 189 DVIINLAGGQN 199
Cdd:PRK03379 171 SQVLSLCGGEN 181
|
|
| FeuA |
cd01138 |
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ... |
30-227 |
2.21e-04 |
|
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: 41.94 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333407657 30 ANNRIISAGSSITELLIALGAKDQ-LIAVDVTSRKYNADEALPQVGYHRQLSAEGLMALSPThLIGSHEMGPENTLTLLK 108
Cdd:cd01138 7 AKPKRIVALSGETEGLALLGIKPVgAASIGGKNPYYKKKTLAKVVGIVDEPNLEKVLELKPD-LIIVSSKQEENYEKLSK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333407657 109 SGgikvETVPSGDTEEDLFGRIDKIAQITGTQEKA-----------KALKASIDKQLNELKSRKLEHQPKVLFAMLTKGR 177
Cdd:cd01138 86 IA----PTVPVSYNSSDWEEQLKEIGKLLNKEDEAekwladykqkaKEAKEKIKKKLGNDKSVAVLRGRKQIYVFGEDGR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1333407657 178 PATIagdqttidVIINLAGGQNPAKSEMS----SYKPLTAEAIVQMQPDFLLVS 227
Cdd:cd01138 162 GGGP--------ILYADLGLKAPEKVKEIedkpGYAAISLEVLPEFDADYIFLL 207
|
|
| TroA_f |
cd01139 |
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ... |
70-231 |
2.30e-04 |
|
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: 41.91 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333407657 70 LPQVG--YHRQLSAEGLMALSPTHLI---GSHEMGPEN-TLTLLKSGGIKVETVP-SGDTEEDLFGRIDKIAQITGTQEK 142
Cdd:cd01139 71 IPLIGstYNGDFSVEKVLTLKPDLVIlniWAKTTAEESgILEKLEQAGIPVVFVDfRQKPLKNTTPSMRLLGKALGREER 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333407657 143 AKALKASIDKQLNELKSRKL---EHQPKVLFAMLTKG-RPATIAGDQTTIDVIINLAGGQNPAKSEMSS-YKPLTAEAIV 217
Cdd:cd01139 151 AEEFIEFYQERIDRIRDRLAkinEPKPKVFIELGAGGpEECCSTYGNGNWGELVDAAGGDNIADGLIPGtSGELNAEYVI 230
|
170
....*....|....
gi 1333407657 218 QMQPDFLLVSTRAW 231
Cdd:cd01139 231 AANPEIIIATGGNW 244
|
|
| |
