|
Name |
Accession |
Description |
Interval |
E-value |
| ChuT |
COG4558 |
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ... |
1-272 |
4.12e-117 |
|
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443619 [Multi-domain] Cd Length: 285 Bit Score: 337.16 E-value: 4.12e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039037 1 MKR-----WLVLLTALPLFAS---AAAERIVSLGGDVTEVVFALDARQQLVAKDSTSTWPAEAQSLPDVGYLRQLNAEGI 72
Cdd:COG4558 1 MKRlalalLLLALAALAAGASvaaAAAERIVSLGGSVTEIVYALGAGDRLVGVDTTSTYPAAAKALPDVGYMRQLSAEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039037 73 LSLRPTLVLASAQAQPSLVLKKVQESGVKVVDVPGGYSLASIDSKVATIAAALGKQAQGDALLQKVHQQIAQIPTQP--- 149
Cdd:COG4558 81 LSLKPTLVLASEGAGPPEVLDQLRAAGVPVVVVPAAPSLEGVLAKIRAVAAALGVPEAGEALAARLEADLAALAARVaai 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039037 150 -LNKRVLFILSHGGMNTLVAGKQTAADGAIRAAGLQNAMQGFDHYRSMSQEGVVASLPDLVVISADGLKGMGGEGGLWKL 228
Cdd:COG4558 161 gKPPRVLFLLSRGGGRPMVAGRGTAADALIRLAGGVNAAAGFEGYKPLSAEALIAAAPDVILVMTRGLESLGGVDGLLAL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2294039037 229 PGLAQTPAGRHKQVLVIDDMALLGFGPRTPQAVITLRQKAEQLP 272
Cdd:COG4558 241 PGLAQTPAGKNKRIVAMDDLLLLGFGPRTPQAALALAQALYPAA 284
|
|
| HutB |
cd01149 |
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ... |
19-249 |
5.07e-90 |
|
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: 266.44 E-value: 5.07e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039037 19 AERIVSLGGDVTEVVFALDARQQLVAKDSTSTWPAEAQSLPDVGYLRQLNAEGILSLRPTLVLASAQAQPSLVLKKVQES 98
Cdd:cd01149 1 PERIVSLGGSVTEIVYALGAGDRLVGVDSTSTYPEAAAKLPDVGYMRQLSAEGVLSLKPTLVIASDEAGPPEALDQLRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039037 99 GVKVVDVPGGYSLASIDSKVATIAAALGKQAQGDALLQKVHQQIA----QIPTQPLNKRVLFILSHGGMNTLVAGKQTAA 174
Cdd:cd01149 81 GVPVVTVPSTPTLDGLLTKIRQVAQALGVPEKGEALAQEVRQRLAalrkTVAAHKKPPRVLFLLSHGGGAAMAAGRNTAA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2294039037 175 DGAIRAAGLQNAMQGFDHYRSMSQEGVVASLPDLVVISADGLKGMGGEGGLWKLPGLAQTPAGRHKQVLVIDDMA 249
Cdd:cd01149 161 DAIIALAGAVNAAAGFRGYKPLSAEALIAAQPDVILVMSRGLDAVGGVDGLLKLPGLAQTPAGRNKRILAMDDLL 235
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
23-247 |
4.87e-25 |
|
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: 99.36 E-value: 4.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039037 23 VSLGGDVTEVVFALDARQQLVAKDSTSTWPAEAQ---SLPDVGYLRQLNAEGILSLRPTLVLASAQAQPSLvLKKVQESG 99
Cdd:pfam01497 1 AALSPAYTEILYALGATDSIVGVDAYTRDPLKADavaAIVKVGAYGEINVERLAALKPDLVILSTGYLTDE-AEELLSLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039037 100 VKVVDVPGGYSLASIDSKVATIAAALGKQAQGDALLQKVHQQIAQI----PTQPLNKRVLFILSHGGMnTLVAGKQTAAD 175
Cdd:pfam01497 80 IPTVIFESSSTGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAkkavPSLTRKPVLVFGGADGGG-YVVAGSNTYIG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2294039037 176 GAIRAAGLQNAMQGFDH--YRSMSQEGVVASLPDLVVISADGLKGMGGEGGLWKLPGLAQTPAGRHKQVLVIDD 247
Cdd:pfam01497 159 DLLRILGIENIAAELSGseYAPISFEAILSSNPDVIIVSGRDSFTKTGPEFVAANPLWAGLPAVKNGRVYTLPS 232
|
|
| btuF |
PRK09534 |
corrinoid ABC transporter substrate-binding protein; Reviewed |
20-264 |
2.61e-11 |
|
corrinoid ABC transporter substrate-binding protein; Reviewed
Pssm-ID: 236552 [Multi-domain] Cd Length: 359 Bit Score: 63.00 E-value: 2.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039037 20 ERIVSLGGDVTEVVFALDARQQLVAKDSTSTWPAEAQSLPDVGYLR--QLNAEGILSLRPTLVLASaQAQPSLVLKKVQE 97
Cdd:PRK09534 61 ERVVTLNPSAAQTMWELGARDRVVGVTQYASYLDGAEERTNVSGGQpfGVNVEAVVGLDPDLVLAP-NAVAGDTVTRLRE 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039037 98 SGVKVVDVPGGYSLASIDSKVATI-------AAALGKQAQGDALLQKVHQQIAQIPTQPlnkRVLFILSHGgmntLVAGK 170
Cdd:PRK09534 140 AGITVFHFPAATSIEDVAEKTATIgrltgncEAAAETNAEMRDRVDAVEDRTADVDDRP---RVLYPLGDG----YTAGG 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039037 171 QTAADGAIRAAGLQN--AMQGFDHYRSMSQEGVVASLPDLVVISADGLKGMGGEGglwklpgLAQTPAGRHKQVLVIDDM 248
Cdd:PRK09534 213 NTFIGALIEAAGGHNvaADATTDGYPQLSEEVIVQQDPDVIVVATASALVAETEP-------YASTTAGETGNVVTVNVN 285
|
250
....*....|....*.
gi 2294039037 249 ALLGFGPRTPQAVITL 264
Cdd:PRK09534 286 HINQPAPRIVESMATM 301
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ChuT |
COG4558 |
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ... |
1-272 |
4.12e-117 |
|
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443619 [Multi-domain] Cd Length: 285 Bit Score: 337.16 E-value: 4.12e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039037 1 MKR-----WLVLLTALPLFAS---AAAERIVSLGGDVTEVVFALDARQQLVAKDSTSTWPAEAQSLPDVGYLRQLNAEGI 72
Cdd:COG4558 1 MKRlalalLLLALAALAAGASvaaAAAERIVSLGGSVTEIVYALGAGDRLVGVDTTSTYPAAAKALPDVGYMRQLSAEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039037 73 LSLRPTLVLASAQAQPSLVLKKVQESGVKVVDVPGGYSLASIDSKVATIAAALGKQAQGDALLQKVHQQIAQIPTQP--- 149
Cdd:COG4558 81 LSLKPTLVLASEGAGPPEVLDQLRAAGVPVVVVPAAPSLEGVLAKIRAVAAALGVPEAGEALAARLEADLAALAARVaai 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039037 150 -LNKRVLFILSHGGMNTLVAGKQTAADGAIRAAGLQNAMQGFDHYRSMSQEGVVASLPDLVVISADGLKGMGGEGGLWKL 228
Cdd:COG4558 161 gKPPRVLFLLSRGGGRPMVAGRGTAADALIRLAGGVNAAAGFEGYKPLSAEALIAAAPDVILVMTRGLESLGGVDGLLAL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2294039037 229 PGLAQTPAGRHKQVLVIDDMALLGFGPRTPQAVITLRQKAEQLP 272
Cdd:COG4558 241 PGLAQTPAGKNKRIVAMDDLLLLGFGPRTPQAALALAQALYPAA 284
|
|
| HutB |
cd01149 |
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ... |
19-249 |
5.07e-90 |
|
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: 266.44 E-value: 5.07e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039037 19 AERIVSLGGDVTEVVFALDARQQLVAKDSTSTWPAEAQSLPDVGYLRQLNAEGILSLRPTLVLASAQAQPSLVLKKVQES 98
Cdd:cd01149 1 PERIVSLGGSVTEIVYALGAGDRLVGVDSTSTYPEAAAKLPDVGYMRQLSAEGVLSLKPTLVIASDEAGPPEALDQLRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039037 99 GVKVVDVPGGYSLASIDSKVATIAAALGKQAQGDALLQKVHQQIA----QIPTQPLNKRVLFILSHGGMNTLVAGKQTAA 174
Cdd:cd01149 81 GVPVVTVPSTPTLDGLLTKIRQVAQALGVPEKGEALAQEVRQRLAalrkTVAAHKKPPRVLFLLSHGGGAAMAAGRNTAA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2294039037 175 DGAIRAAGLQNAMQGFDHYRSMSQEGVVASLPDLVVISADGLKGMGGEGGLWKLPGLAQTPAGRHKQVLVIDDMA 249
Cdd:cd01149 161 DAIIALAGAVNAAAGFRGYKPLSAEALIAAQPDVILVMSRGLDAVGGVDGLLKLPGLAQTPAGRNKRILAMDDLL 235
|
|
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
21-266 |
6.17e-38 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 133.97 E-value: 6.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039037 21 RIVSLGGDVTEVVFALDARQQLVA--KDSTSTWPA-EAQSLPDVGYLRQLNAEGILSLRPTLVLASAQAQPSLVLKKVQE 97
Cdd:COG0614 2 RIVSLSPSATELLLALGAGDRLVGvsDWGYCDYPElELKDLPVVGGTGEPNLEAILALKPDLVLASSSGNDEEDYEQLEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039037 98 SGVKVVdVPGGYSLASIDSKVATIAAALGKQAQGDALLQKVHQQIAQI----PTQPLNKRVLFILSHGGmNTLVAGKQTA 173
Cdd:COG0614 82 IGIPVV-VLDPRSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVrarlAGAEERPTVLYEIWSGD-PLYTAGGGSF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039037 174 ADGAIRAAGLQNAMQGFD-HYRSMSQEGVVASLPDLVVISADGLKGMGGEGGLWKL---PGLAQTPAGRHKQVLVIDDMA 249
Cdd:COG0614 160 IGELLELAGGRNVAADLGgGYPEVSLEQVLALDPDVIILSGGGYDAETAEEALEALladPGWQSLPAVKNGRVYVVPGDL 239
|
250
....*....|....*..
gi 2294039037 250 LLGFGPRTPQAVITLRQ 266
Cdd:COG0614 240 LSRPGPRLLLALEDLAK 256
|
|
| YvrC |
cd01143 |
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ... |
20-210 |
4.60e-31 |
|
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: 114.30 E-value: 4.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039037 20 ERIVSLGGDVTEVVFALDARQQLVAKDSTSTWPAEAQSLPDVGYLRQLNAEGILSLRPTLVLASAQAQPSlVLKKVQESG 99
Cdd:cd01143 4 ERIVSLSPSITEILFALGAGDKIVGVDTYSNYPKEVRKKPKVGSYSNPNVEKIVALKPDLVIVSSSSLAE-LLEKLKDAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039037 100 VKVVDVPGGYSLASIDSKVATIAAALGKQAQGDALLQKVHQQIAQIPTQPLNKR---VLFILSHGGMNTlvAGKQTAADG 176
Cdd:cd01143 83 IPVVVLPAASSLDEIYDQIELIGKITGAEEEAEKLVKEMKQKIDKVKDKGKTIKkskVYIEVSLGGPYT--AGKNTFINE 160
|
170 180 190
....*....|....*....|....*....|....
gi 2294039037 177 AIRAAGLQNAMQGFDHYRSMSQEGVVASLPDLVV 210
Cdd:cd01143 161 LIRLAGAKNIAADSGGWPQVSPEEILKANPDVII 194
|
|
| BtuF |
cd01144 |
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ... |
20-261 |
4.35e-30 |
|
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: 113.16 E-value: 4.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039037 20 ERIVSLGGDVTEVVFALDARQQLVAKDSTSTWPAEAQSLPDVGYLRQLNAEGILSLRPTLVLASAQAQPSLVLKKVQESG 99
Cdd:cd01144 1 MRIVSLAPSATELLYALGLGDQLVGVTDYCDYPPEAKKLPRVGGFYQLDLERVLALKPDLVIAWDDCNVCAVVDQLRAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039037 100 VKVVDVPgGYSLASIDSKVATIAAALGKQAQGDALLQKVHQQIAQIPTQPLNK---RVLFILSH-----GGMNTLvagkq 171
Cdd:cd01144 81 IPVLVSE-PQTLDDILADIRRLGTLAGRPARAEELAEALRRRLAALRKQYASKpppRVFYQEWIdplmtAGGDWV----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039037 172 taaDGAIRAAGLQNAmqgFD----HYRSMSQEGVVASLPDLVVISADglKGMGGEGGLWKLPGLAQTPAGRHKQVLVIDD 247
Cdd:cd01144 155 ---PELIALAGGVNV---FAdageRSPQVSWEDVLAANPDVIVLSPC--GFGFTPAILRKEPAWQALPAVRNGRVYAVDG 226
|
250
....*....|....
gi 2294039037 248 MALLGFGPRTPQAV 261
Cdd:cd01144 227 NWYFRPSPRLVDGL 240
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
23-247 |
4.87e-25 |
|
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: 99.36 E-value: 4.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039037 23 VSLGGDVTEVVFALDARQQLVAKDSTSTWPAEAQ---SLPDVGYLRQLNAEGILSLRPTLVLASAQAQPSLvLKKVQESG 99
Cdd:pfam01497 1 AALSPAYTEILYALGATDSIVGVDAYTRDPLKADavaAIVKVGAYGEINVERLAALKPDLVILSTGYLTDE-AEELLSLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039037 100 VKVVDVPGGYSLASIDSKVATIAAALGKQAQGDALLQKVHQQIAQI----PTQPLNKRVLFILSHGGMnTLVAGKQTAAD 175
Cdd:pfam01497 80 IPTVIFESSSTGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAkkavPSLTRKPVLVFGGADGGG-YVVAGSNTYIG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2294039037 176 GAIRAAGLQNAMQGFDH--YRSMSQEGVVASLPDLVVISADGLKGMGGEGGLWKLPGLAQTPAGRHKQVLVIDD 247
Cdd:pfam01497 159 DLLRILGIENIAAELSGseYAPISFEAILSSNPDVIIVSGRDSFTKTGPEFVAANPLWAGLPAVKNGRVYTLPS 232
|
|
| TroA-like |
cd00636 |
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ... |
20-145 |
5.55e-20 |
|
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: 83.76 E-value: 5.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039037 20 ERIVSLGGDVTEVVFALDARQQLVAKDSTSTWPAEAQ----SLPDVGYLRQLNAEGILSLRPTLVLASAQAQPSlVLKKV 95
Cdd:cd00636 1 KRVVALDPGATELLLALGGDDKPVGVADPSGYPPEAKalleKVPDVGHGYEPNLEKIAALKPDLIIANGSGLEA-WLDKL 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2294039037 96 QESGVKVV--DVPGGYSLASIDSKVATIAAALGKQAQGDALLQKVHQQIAQI 145
Cdd:cd00636 80 SKIAIPVVvvDEASELSLENIKESIRLIGKALGKEENAEELIAELDARLAEL 131
|
|
| TroA_a |
cd01148 |
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ... |
17-265 |
4.04e-15 |
|
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: 73.53 E-value: 4.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039037 17 AAAERIVSLGGDVTEVVFALDARQQLVAK-----DSTSTWPAEAQSLPDVGYlRQLNAEGILSLRPTLVLA--SAQAQPS 89
Cdd:cd01148 16 KAPQRVVSNDQNTTEMMLALGLQDRMVGTagidnKDLPELKAKYDKVPELAK-KYPSKETVLAARPDLVFGgwSYGFDKG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039037 90 LVL--KKVQESGVKVVDVP-------GGYSLASIDSKVATIAAALGKQAQGDALLQKVHQQIAQIPTQP--LNKRV-LFI 157
Cdd:cd01148 95 GLGtpDSLAELGIKTYILPescgqrrGEATLDDVYNDIRNLGKIFDVEDRADKLVADLKARLAEISAKVkgDGKKVaVFV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039037 158 LSHGGMNTLVAGKQTAADGAIRAAGLQNAMQGFD-HYRSMSQEGVVASLPDLVVI--SADGLKGMGGEGGLWKLPGLAQT 234
Cdd:cd01148 175 YDSGEDKPFTSGRGGIPNAIITAAGGRNVFADVDeSWTTVSWETVIARNPDVIVIidYGDQNAAEQKIKFLKENPALKNV 254
|
250 260 270
....*....|....*....|....*....|.
gi 2294039037 235 PAGRHKQVLVIDDMALLGfGPRTPQAVITLR 265
Cdd:cd01148 255 PAVKNNRFIVLPLAEATP-GIRNVDAIEKLA 284
|
|
| FhuD |
cd01146 |
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ... |
17-247 |
2.84e-14 |
|
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: 70.78 E-value: 2.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039037 17 AAAERIVSLGGDVTEVVFALDArqQLVAkdSTSTW---------PAEAQSLPDVGYLRQLNAEGILSLRPTLVLASAQAQ 87
Cdd:cd01146 1 AKPQRIVALDWGALETLLALGV--KPVG--VADTAgykpwipepALPLEGVVDVGTRGQPNLEAIAALKPDLILGSASRH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039037 88 PSLV--LKKVqesgVKVVDVPGGYSLASIDSKVATIAAALGKQAQGDALLQKVHQQIAQIPTQ---PLNKRVLFILSHGG 162
Cdd:cd01146 77 DEIYdqLSQI----APTVLLDSSPWLAEWKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKlpdKGPKPVSVVRFSDA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039037 163 MNTLVAGKQTAADGAIRAAGLQNA----MQGFDHYRSMSQEGVVASLPDLVVISADGLKGMGGEGG---LWKlpglaQTP 235
Cdd:cd01146 153 GSIRLYGPNSFAGSVLEDLGLQNPwaqeTTNDSGFATISLERLAKADADVLFVFTYEDEELAQALQanpLWQ-----NLP 227
|
250
....*....|..
gi 2294039037 236 AGRHKQVLVIDD 247
Cdd:cd01146 228 AVKNGRVYVVDD 239
|
|
| btuF |
PRK09534 |
corrinoid ABC transporter substrate-binding protein; Reviewed |
20-264 |
2.61e-11 |
|
corrinoid ABC transporter substrate-binding protein; Reviewed
Pssm-ID: 236552 [Multi-domain] Cd Length: 359 Bit Score: 63.00 E-value: 2.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039037 20 ERIVSLGGDVTEVVFALDARQQLVAKDSTSTWPAEAQSLPDVGYLR--QLNAEGILSLRPTLVLASaQAQPSLVLKKVQE 97
Cdd:PRK09534 61 ERVVTLNPSAAQTMWELGARDRVVGVTQYASYLDGAEERTNVSGGQpfGVNVEAVVGLDPDLVLAP-NAVAGDTVTRLRE 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039037 98 SGVKVVDVPGGYSLASIDSKVATI-------AAALGKQAQGDALLQKVHQQIAQIPTQPlnkRVLFILSHGgmntLVAGK 170
Cdd:PRK09534 140 AGITVFHFPAATSIEDVAEKTATIgrltgncEAAAETNAEMRDRVDAVEDRTADVDDRP---RVLYPLGDG----YTAGG 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039037 171 QTAADGAIRAAGLQN--AMQGFDHYRSMSQEGVVASLPDLVVISADGLKGMGGEGglwklpgLAQTPAGRHKQVLVIDDM 248
Cdd:PRK09534 213 NTFIGALIEAAGGHNvaADATTDGYPQLSEEVIVQQDPDVIVVATASALVAETEP-------YASTTAGETGNVVTVNVN 285
|
250
....*....|....*.
gi 2294039037 249 ALLGFGPRTPQAVITL 264
Cdd:PRK09534 286 HINQPAPRIVESMATM 301
|
|
| TroA_e |
cd01142 |
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ... |
19-245 |
4.91e-11 |
|
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: 61.60 E-value: 4.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039037 19 AERIVSLGGDVTEVVFALDARQQLVAKDSTSTW-PAEAQSLPD------VGYLRQLNAEGILSLRPTLVLASAQAQPSLV 91
Cdd:cd01142 24 VKRIAALWGAGNAVVAALGGGKLIVATTSTVQQePWLYRLAPSlenvatGGTGNDVNIEELLALKPDVVIVWSTDGKEAG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039037 92 LKKVqesGVKVVDVPGGYSLASIDSKVATIAAALGKQAQGDAL-------LQKVHQQIAQIPTQPlNKRVLFIlshGGMN 164
Cdd:cd01142 104 KAVL---RLLNALSLRDAELEEVKLTIALLGELLGRQEKAEALvayfddnLAYVAARTKKLPDSE-RPRVYYA---GPDP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039037 165 TLVAGKQTAADGAIRAAGLQNAMQ--GFDHYRSMSQEGVVASLPDLVVI-SADGLKGMGGEGGLWKLpglaqtPAGRHKQ 241
Cdd:cd01142 177 LTTDGTGSITNSWIDLAGGINVASeaTKKGSGEVSLEQLLKWNPDVIIVgNADTKAAILADPRWQNL------RAVKNGR 250
|
....
gi 2294039037 242 VLVI 245
Cdd:cd01142 251 VYVN 254
|
|
| HemV-2 |
cd01147 |
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ... |
20-254 |
8.46e-11 |
|
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: 60.81 E-value: 8.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039037 20 ERIVSLGGDVTEVVFALDARQQLVAKDSTSTWPAEA---------QSLPDVGYL---RQLNAEGILSLRPTLVLASAQAQ 87
Cdd:cd01147 6 ERVVAAGPGALRLLYALAAPDKIVGVDDAEKSDEGRpyflaspelKDLPVIGRGgrgNTPNYEKIAALKPDVVIDVGSDD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039037 88 PSLVLKKVQES-GVKVVDVPGGYSLASIDSKVATIAAALGKQAQGDAL-------LQKVHQQIAQIPTQPlNKRVLFils 159
Cdd:cd01147 86 PTSIADDLQKKtGIPVVVLDGGDSLEDTPEQIRLLGKVLGKEERAEELisfiesiLADVEERTKDIPDEE-KPTVYF--- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039037 160 HGGMNTLVAGKQTAADGA---IRAAGLQNAMQGFDHYRS--MSQEGVVASLPDlVVISADGLKGMGGEGGLWKLPGLAQT 234
Cdd:cd01147 162 GRIGTKGAAGLESGLAGSievFELAGGINVADGLGGGGLkeVSPEQILLWNPD-VIFLDTGSFYLSLEGYAKNRPFWQSL 240
|
250 260
....*....|....*....|
gi 2294039037 235 PAGRHKQVLvidDMALLGFG 254
Cdd:cd01147 241 KAVKNGRVY---LLPALPFN 257
|
|
| TroA_d |
cd01141 |
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ... |
19-182 |
1.30e-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: 56.28 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039037 19 AERIVSLGGDVTEVVFALDARQQLVAKDSTSTW---PAEAQSLP-DVGYLRQLNAEGILSLRPTLVLASAQAQPSLVLKK 94
Cdd:cd01141 8 PKRIVVLSPTHVDLLLALDKADKIVGVSASAYDlntPAVKERIDiQVGPTGSLNVELIVALKPDLVILYGGFQAQTILDK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039037 95 VQESGVKVVDVP-GGYSLASIDSKVATIA-AALGKQAQGDallqKVHQQIAQIPTQPLNK-------RVLFILSHGGMnT 165
Cdd:cd01141 88 LEQLGIPVLYVNeYPSPLGRAEWIKFAAAfYGVGKEDKAD----EAFAQIAGRYRDLAKKvsnlnkpTVAIGKPVKGL-W 162
|
170
....*....|....*..
gi 2294039037 166 LVAGKQTAADGAIRAAG 182
Cdd:cd01141 163 YMPGGNSYVAKMLRDAG 179
|
|
| PRK03379 |
PRK03379 |
vitamin B12-transporter protein BtuF; Provisional |
5-214 |
6.63e-09 |
|
vitamin B12-transporter protein BtuF; Provisional
Pssm-ID: 179575 [Multi-domain] Cd Length: 260 Bit Score: 55.08 E-value: 6.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039037 5 LVLLTALPLFAsaaAERIVSLGGDVTEVVFAldARQQLVAKDSTSTWPAEAQSLPDVGYLRQLNAEGILSLRPTLVLASA 84
Cdd:PRK03379 6 LLFLAPLWLNA---APRVITLSPANTELAFA--AGITPVGVSSYSDYPPQAKKIEQVATWQGMNLERIVALKPDLVLAWR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039037 85 QAQPSLVLKKVQESGVKVVdvpggYSLAsidSKVATIAAALGKQAQ-----------GDALLQKVHQQIAQIPTQPlNKR 153
Cdd:PRK03379 81 GGNAERQVDQLASLGIKVM-----WVDA---TSIEQIANALRQLAPwspqpekaeqaAQSLLQQYAALKAQYADKP-KKR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2294039037 154 VLFILshgGMNTL-VAGKQTAADGAIRAAGLQNAmqgFDHYR----SMSQEGVVASLPDLVVISAD 214
Cdd:PRK03379 152 VFLQF---GTNPLfTSGKHSIQSQVLSLCGGENI---FADSRvpwpQVSREQVLARKPQAIVITGG 211
|
|
| FecB |
COG4594 |
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ... |
17-214 |
1.60e-07 |
|
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443650 [Multi-domain] Cd Length: 316 Bit Score: 51.46 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039037 17 AAAERIVSLGGDVTEVVFALDARQQLVAKDST-STWPAEAQSL----PDVGYLRQLNAEGILSLRPTLVLASAQAQ---- 87
Cdd:COG4594 50 GTPKRVVVLEWSFADALLALGVTPVGIADDNDyDRWVPYLRDLikgvTSVGTRSQPNLEAIAALKPDLIIADKSRHeaiy 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039037 88 -------PSLVLKkvqesgvkvvdvPGGYSLASIDSKVATIAAALGKQAQGDALLQKVHQQIA----QIPTQPLNKRVLF 156
Cdd:COG4594 130 dqlskiaPTVLFK------------SRNGDYQENLESFKTIAKALGKEEEAEAVLADHDQRIAeakaKLAAADKGKKVAV 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2294039037 157 ILSHGGmNTLVAGKQTAADGAIRAAGLQNAMQGFD----HYRSMSQEGVVASLPDLVVISAD 214
Cdd:COG4594 198 GQFRAD-GLRLYTPNSFAGSVLAALGFENPPKQSKdngyGYSEVSLEQLPALDPDVLFIATY 258
|
|
| FatB |
cd01140 |
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ... |
20-246 |
2.70e-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: 47.64 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039037 20 ERIVSLGGDVTEVVFALDARqqLVAKDSTSTWPA-----EAQSLPDVGYLRQLNAEGILSLRPTLVLASAQAQPSLVlKK 94
Cdd:cd01140 13 EKVVVFDVGALDTLDALGVK--VVGVPKSSTLPEylkkyKDDKYANVGTLFEPDLEAIAALKPDLIIIGGRLAEKYD-EL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039037 95 VQESGVKVVDVPGGYSLASIDSKVATIAAALGKQAQGDALLQKVHQQIAQIPTQ-PLNKRVLFILSHGGmNTLVAGKQTA 173
Cdd:cd01140 90 KKIAPTIDLGADLKNYLESVKQNIETLGKIFGKEEEAKELVAEIDASIAEAKSAaKGKKKALVVLVNGG-KLSAFGPGSR 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2294039037 174 ADGAIRAAGLQNA---MQGFDHYRSMSQEGVVASLPD-LVVISADGLKGMGGEGGLWKL--PGLAQTPAGRHKQVLVID 246
Cdd:cd01140 169 FGWLHDLLGFEPAdenIKASSHGQPVSFEYILEANPDwLFVIDRGAAIGAEGSSAKEVLdnDLVKNTTAWKNGKVIYLD 247
|
|
| PRK10576 |
PRK10576 |
Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD; |
7-189 |
1.35e-04 |
|
Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD;
Pssm-ID: 236719 Cd Length: 292 Bit Score: 42.31 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039037 7 LLTALPL------FASAAAE-----RIVSLGGDVTEVVFALDARQQLVA-KDSTSTW---PAEAQSLPDVGYLRQLNAEG 71
Cdd:PRK10576 9 LLTAMALspllwqMNTAAAAaidpnRIVALEWLPVELLLALGVTPYGVAdTHNYRLWvsePALPDSVIDVGLRTEPNLEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039037 72 ILSLRPTLVLASAQAQPSLV-LKKVQES-GVKVVDvpGGYSLASIDSKVATIAAALGKQAQGDALLQKVHQQIAQ--IPT 147
Cdd:PRK10576 89 LTQMKPSLILWSAGYGPSPEkLARIAPGrGFAFSD--GKKPLAVARKSLVELAQRLNLEAAAETHLAQFDDFIASakPRL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2294039037 148 QPLNKRVLFILS-----HggmnTLVAGKQTAADGAIRAAGLQNAMQG 189
Cdd:PRK10576 167 AGRGQRPLLLTSlidprH----ALVFGPNSLFQEVLDELGIENAWQG 209
|
|
| |
