|
Name |
Accession |
Description |
Interval |
E-value |
| ChuT |
COG4558 |
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ... |
1-273 |
1.02e-109 |
|
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443619 [Multi-domain] Cd Length: 285 Bit Score: 318.29 E-value: 1.02e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604920740 1 MKK--WLAVLSALPLMA-----FAATQEKIVTLGGDVTEIVFALGAQSSLVARDSTSQWPQAANDLPDVGYLRQLNAEGI 73
Cdd:COG4558 1 MKRlaLALLLLALAALAagasvAAAAAERIVSLGGSVTEIVYALGAGDRLVGVDTTSTYPAAAKALPDVGYMRQLSAEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604920740 74 LSMRPTLVLASAQAQPSLALKQVEQSHIRVVTVPASNALGVIDEKVRVIAQATHREVEGEILRNTLRQALTALPASL--- 150
Cdd:COG4558 81 LSLKPTLVLASEGAGPPEVLDQLRAAGVPVVVVPAAPSLEGVLAKIRAVAAALGVPEAGEALAARLEADLAALAARVaai 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604920740 151 -LNKRVLFILNHGGMTAMAAGQQTAADAAIQAAGLRNAMQGFTRYQPLSQEGVIASQPDLVVISQEGINALGGEDNLWKL 229
Cdd:COG4558 161 gKPPRVLFLLSRGGGRPMVAGRGTAADALIRLAGGVNAAAGFEGYKPLSAEALIAAAPDVILVMTRGLESLGGVDGLLAL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1604920740 230 PGLAQTPAGRNKQLLAIDDMALLGFGVRTPQAIQQLRVRAEQLP 273
Cdd:COG4558 241 PGLAQTPAGKNKRIVAMDDLLLLGFGPRTPQAALALAQALYPAA 284
|
|
| HutB |
cd01149 |
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ... |
20-250 |
2.83e-95 |
|
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: 279.92 E-value: 2.83e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604920740 20 QEKIVTLGGDVTEIVFALGAQSSLVARDSTSQWPQAANDLPDVGYLRQLNAEGILSMRPTLVLASAQAQPSLALKQVEQS 99
Cdd:cd01149 1 PERIVSLGGSVTEIVYALGAGDRLVGVDSTSTYPEAAAKLPDVGYMRQLSAEGVLSLKPTLVIASDEAGPPEALDQLRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604920740 100 HIRVVTVPASNALGVIDEKVRVIAQATHREVEGEILRNTLRQALTAL----PASLLNKRVLFILNHGGMTAMAAGQQTAA 175
Cdd:cd01149 81 GVPVVTVPSTPTLDGLLTKIRQVAQALGVPEKGEALAQEVRQRLAALrktvAAHKKPPRVLFLLSHGGGAAMAAGRNTAA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1604920740 176 DAAIQAAGLRNAMQGFTRYQPLSQEGVIASQPDLVVISQEGINALGGEDNLWKLPGLAQTPAGRNKQLLAIDDMA 250
Cdd:cd01149 161 DAIIALAGAVNAAAGFRGYKPLSAEALIAAQPDVILVMSRGLDAVGGVDGLLKLPGLAQTPAGRNKRILAMDDLL 235
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
24-248 |
1.54e-23 |
|
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: 95.51 E-value: 1.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604920740 24 VTLGGDVTEIVFALGAQSSLVARDSTSQWPQAANDLPD---VGYLRQLNAEGILSMRPTLVLASAQAQPSLALKQvEQSH 100
Cdd:pfam01497 1 AALSPAYTEILYALGATDSIVGVDAYTRDPLKADAVAAivkVGAYGEINVERLAALKPDLVILSTGYLTDEAEEL-LSLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604920740 101 IRVVTVPASNALGVIDEKVRVIAQATHREVEGEILRNTLRQALTAL--PASLLNKRVLFIL-NHGGMTAMAAGQQTAADA 177
Cdd:pfam01497 80 IPTVIFESSSTGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAkkAVPSLTRKPVLVFgGADGGGYVVAGSNTYIGD 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1604920740 178 AIQAAGLRN--AMQGFTRYQPLSQEGVIASQPDLVVISQEGINALGGEDNLWKLPGLAQTPAGRNKQLLAIDD 248
Cdd:pfam01497 160 LLRILGIENiaAELSGSEYAPISFEAILSSNPDVIIVSGRDSFTKTGPEFVAANPLWAGLPAVKNGRVYTLPS 232
|
|
| PRK03379 |
PRK03379 |
vitamin B12-transporter protein BtuF; Provisional |
5-213 |
2.98e-06 |
|
vitamin B12-transporter protein BtuF; Provisional
Pssm-ID: 179575 [Multi-domain] Cd Length: 260 Bit Score: 47.37 E-value: 2.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604920740 5 LAVLSALPLMAFAAtqEKIVTLGGDVTEIVFALGAQSslVARDSTSQWPQAANDLPDVGYLRQLNAEGILSMRPTLVLAS 84
Cdd:PRK03379 4 VALLFLAPLWLNAA--PRVITLSPANTELAFAAGITP--VGVSSYSDYPPQAKKIEQVATWQGMNLERIVALKPDLVLAW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604920740 85 AQAQPSLALKQVEQSHIRVVTVPASNALGVIDEkVRVIAQATHREVEGEILRNTLRQ---ALTALPASLLNKRVLfiLNH 161
Cdd:PRK03379 80 RGGNAERQVDQLASLGIKVMWVDATSIEQIANA-LRQLAPWSPQPEKAEQAAQSLLQqyaALKAQYADKPKKRVF--LQF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1604920740 162 GGMTAMAAGQQTAADAAIQAAGLRNAMQGFTRYQP-LSQEGVIASQPDLVVIS 213
Cdd:PRK03379 157 GTNPLFTSGKHSIQSQVLSLCGGENIFADSRVPWPqVSREQVLARKPQAIVIT 209
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ChuT |
COG4558 |
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ... |
1-273 |
1.02e-109 |
|
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443619 [Multi-domain] Cd Length: 285 Bit Score: 318.29 E-value: 1.02e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604920740 1 MKK--WLAVLSALPLMA-----FAATQEKIVTLGGDVTEIVFALGAQSSLVARDSTSQWPQAANDLPDVGYLRQLNAEGI 73
Cdd:COG4558 1 MKRlaLALLLLALAALAagasvAAAAAERIVSLGGSVTEIVYALGAGDRLVGVDTTSTYPAAAKALPDVGYMRQLSAEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604920740 74 LSMRPTLVLASAQAQPSLALKQVEQSHIRVVTVPASNALGVIDEKVRVIAQATHREVEGEILRNTLRQALTALPASL--- 150
Cdd:COG4558 81 LSLKPTLVLASEGAGPPEVLDQLRAAGVPVVVVPAAPSLEGVLAKIRAVAAALGVPEAGEALAARLEADLAALAARVaai 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604920740 151 -LNKRVLFILNHGGMTAMAAGQQTAADAAIQAAGLRNAMQGFTRYQPLSQEGVIASQPDLVVISQEGINALGGEDNLWKL 229
Cdd:COG4558 161 gKPPRVLFLLSRGGGRPMVAGRGTAADALIRLAGGVNAAAGFEGYKPLSAEALIAAAPDVILVMTRGLESLGGVDGLLAL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1604920740 230 PGLAQTPAGRNKQLLAIDDMALLGFGVRTPQAIQQLRVRAEQLP 273
Cdd:COG4558 241 PGLAQTPAGKNKRIVAMDDLLLLGFGPRTPQAALALAQALYPAA 284
|
|
| HutB |
cd01149 |
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ... |
20-250 |
2.83e-95 |
|
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: 279.92 E-value: 2.83e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604920740 20 QEKIVTLGGDVTEIVFALGAQSSLVARDSTSQWPQAANDLPDVGYLRQLNAEGILSMRPTLVLASAQAQPSLALKQVEQS 99
Cdd:cd01149 1 PERIVSLGGSVTEIVYALGAGDRLVGVDSTSTYPEAAAKLPDVGYMRQLSAEGVLSLKPTLVIASDEAGPPEALDQLRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604920740 100 HIRVVTVPASNALGVIDEKVRVIAQATHREVEGEILRNTLRQALTAL----PASLLNKRVLFILNHGGMTAMAAGQQTAA 175
Cdd:cd01149 81 GVPVVTVPSTPTLDGLLTKIRQVAQALGVPEKGEALAQEVRQRLAALrktvAAHKKPPRVLFLLSHGGGAAMAAGRNTAA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1604920740 176 DAAIQAAGLRNAMQGFTRYQPLSQEGVIASQPDLVVISQEGINALGGEDNLWKLPGLAQTPAGRNKQLLAIDDMA 250
Cdd:cd01149 161 DAIIALAGAVNAAAGFRGYKPLSAEALIAAQPDVILVMSRGLDAVGGVDGLLKLPGLAQTPAGRNKRILAMDDLL 235
|
|
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
22-265 |
4.42e-34 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 123.95 E-value: 4.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604920740 22 KIVTLGGDVTEIVFALGAQSSLVARDST--SQWPQ-AANDLPDVGYLRQLNAEGILSMRPTLVLASAQAQPSLALKQVEQ 98
Cdd:COG0614 2 RIVSLSPSATELLLALGAGDRLVGVSDWgyCDYPElELKDLPVVGGTGEPNLEAILALKPDLVLASSSGNDEEDYEQLEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604920740 99 SHIRVVTVPASNaLGVIDEKVRVIAQATHREVEGEILRNTLRQALTALPASLLN----KRVLFILNHGGmTAMAAGQQTA 174
Cdd:COG0614 82 IGIPVVVLDPRS-LEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGaeerPTVLYEIWSGD-PLYTAGGGSF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604920740 175 ADAAIQAAGLRNAMQGF-TRYQPLSQEGVIASQPDLVVISQEGINALGGEDNLWKL---PGLAQTPAGRNKQLLAIDDMA 250
Cdd:COG0614 160 IGELLELAGGRNVAADLgGGYPEVSLEQVLALDPDVIILSGGGYDAETAEEALEALladPGWQSLPAVKNGRVYVVPGDL 239
|
250
....*....|....*
gi 1604920740 251 LLGFGVRTPQAIQQL 265
Cdd:COG0614 240 LSRPGPRLLLALEDL 254
|
|
| YvrC |
cd01143 |
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ... |
21-211 |
3.04e-26 |
|
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: 101.59 E-value: 3.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604920740 21 EKIVTLGGDVTEIVFALGAQSSLVARDSTSQWPQAANDLPDVGYLRQLNAEGILSMRPTLVLASAQAQPSLaLKQVEQSH 100
Cdd:cd01143 4 ERIVSLSPSITEILFALGAGDKIVGVDTYSNYPKEVRKKPKVGSYSNPNVEKIVALKPDLVIVSSSSLAEL-LEKLKDAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604920740 101 IRVVTVPASNALGVIDEKVRVIAQATHREVEGEILRNTLRQALTALPASLLNKR---VLFILNHGGMtaMAAGQQTAADA 177
Cdd:cd01143 83 IPVVVLPAASSLDEIYDQIELIGKITGAEEEAEKLVKEMKQKIDKVKDKGKTIKkskVYIEVSLGGP--YTAGKNTFINE 160
|
170 180 190
....*....|....*....|....*....|....
gi 1604920740 178 AIQAAGLRNAMQGFTRYQPLSQEGVIASQPDLVV 211
Cdd:cd01143 161 LIRLAGAKNIAADSGGWPQVSPEEILKANPDVII 194
|
|
| BtuF |
cd01144 |
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ... |
21-265 |
6.15e-24 |
|
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: 96.98 E-value: 6.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604920740 21 EKIVTLGGDVTEIVFALGAQSSLVARDSTSQWPQAANDLPDVGYLRQLNAEGILSMRPTLVLASAQAQPSLALKQVEQSH 100
Cdd:cd01144 1 MRIVSLAPSATELLYALGLGDQLVGVTDYCDYPPEAKKLPRVGGFYQLDLERVLALKPDLVIAWDDCNVCAVVDQLRAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604920740 101 IRVVTVPASNALGVIDEkVRVIAQATHREVEGEILRNTLRQ---ALTALPASLLNKRVLFI--------LNHGGMTAMAA 169
Cdd:cd01144 81 IPVLVSEPQTLDDILAD-IRRLGTLAGRPARAEELAEALRRrlaALRKQYASKPPPRVFYQewidplmtAGGDWVPELIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604920740 170 gqqtaadaaiqAAGLRN--AMQGfTRYQPLSQEGVIASQPDLVVISQEGINALggEDNLWKLPGLAQTPAGRNKQLLAID 247
Cdd:cd01144 160 -----------LAGGVNvfADAG-ERSPQVSWEDVLAANPDVIVLSPCGFGFT--PAILRKEPAWQALPAVRNGRVYAVD 225
|
250
....*....|....*...
gi 1604920740 248 DMALLGFGVRTPQAIQQL 265
Cdd:cd01144 226 GNWYFRPSPRLVDGLEQL 243
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
24-248 |
1.54e-23 |
|
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: 95.51 E-value: 1.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604920740 24 VTLGGDVTEIVFALGAQSSLVARDSTSQWPQAANDLPD---VGYLRQLNAEGILSMRPTLVLASAQAQPSLALKQvEQSH 100
Cdd:pfam01497 1 AALSPAYTEILYALGATDSIVGVDAYTRDPLKADAVAAivkVGAYGEINVERLAALKPDLVILSTGYLTDEAEEL-LSLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604920740 101 IRVVTVPASNALGVIDEKVRVIAQATHREVEGEILRNTLRQALTAL--PASLLNKRVLFIL-NHGGMTAMAAGQQTAADA 177
Cdd:pfam01497 80 IPTVIFESSSTGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAkkAVPSLTRKPVLVFgGADGGGYVVAGSNTYIGD 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1604920740 178 AIQAAGLRN--AMQGFTRYQPLSQEGVIASQPDLVVISQEGINALGGEDNLWKLPGLAQTPAGRNKQLLAIDD 248
Cdd:pfam01497 160 LLRILGIENiaAELSGSEYAPISFEAILSSNPDVIIVSGRDSFTKTGPEFVAANPLWAGLPAVKNGRVYTLPS 232
|
|
| TroA-like |
cd00636 |
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ... |
21-158 |
3.34e-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: 79.14 E-value: 3.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604920740 21 EKIVTLGGDVTEIVFALGAQSSLVARDSTSQWPQAAN----DLPDVGYLRQLNAEGILSMRPTLVLASAQAQPSLaLKQV 96
Cdd:cd00636 1 KRVVALDPGATELLLALGGDDKPVGVADPSGYPPEAKalleKVPDVGHGYEPNLEKIAALKPDLIIANGSGLEAW-LDKL 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1604920740 97 EQSHIRVVTVPASNALGV--IDEKVRVIAQATHREVEGEILRNTLRQ---ALTALPASLLNKRVLFI 158
Cdd:cd00636 80 SKIAIPVVVVDEASELSLenIKESIRLIGKALGKEENAEELIAELDArlaELRAKLAKIPKKKVSLV 146
|
|
| TroA_d |
cd01141 |
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ... |
21-170 |
6.64e-11 |
|
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: 60.13 E-value: 6.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604920740 21 EKIVTLGGDVTEIVFALGAQSSLVARDSTSQW---PQAANDLP-DVGYLRQLNAEGILSMRPTLVLASAQAQPSLALKQV 96
Cdd:cd01141 9 KRIVVLSPTHVDLLLALDKADKIVGVSASAYDlntPAVKERIDiQVGPTGSLNVELIVALKPDLVILYGGFQAQTILDKL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604920740 97 EQSHIRVVTVP-ASNALGVIDEKVRVIAQATH------REVEGEILRNtlRQALTALPASLLNKRVLFILNHGGMTAMAA 169
Cdd:cd01141 89 EQLGIPVLYVNeYPSPLGRAEWIKFAAAFYGVgkedkaDEAFAQIAGR--YRDLAKKVSNLNKPTVAIGKPVKGLWYMPG 166
|
.
gi 1604920740 170 G 170
Cdd:cd01141 167 G 167
|
|
| TroA_a |
cd01148 |
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ... |
14-266 |
2.79e-09 |
|
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: 56.58 E-value: 2.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604920740 14 MAFAATQEKIVTLGGDVTEIVFALGAQSSLVArdsTSQWpqAANDLPDV-GYLRQLNA--------EGILSMRPTLVLAS 84
Cdd:cd01148 12 VTFDKAPQRVVSNDQNTTEMMLALGLQDRMVG---TAGI--DNKDLPELkAKYDKVPElakkypskETVLAARPDLVFGG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604920740 85 ----AQAQPSLALKQVEQSHIRVVTVPASNA-------LGVIDEKVRVIAQATHREVEGEILRNTLRQALTALPASL--L 151
Cdd:cd01148 87 wsygFDKGGLGTPDSLAELGIKTYILPESCGqrrgeatLDDVYNDIRNLGKIFDVEDRADKLVADLKARLAEISAKVkgD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604920740 152 NKRV-LFILNHGGMTAMAAGQQTAADAAIQAAGLRNAMQGF-TRYQPLSQEGVIASQPDLVVI----SQEGINALggEDN 225
Cdd:cd01148 167 GKKVaVFVYDSGEDKPFTSGRGGIPNAIITAAGGRNVFADVdESWTTVSWETVIARNPDVIVIidygDQNAAEQK--IKF 244
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1604920740 226 LWKLPGLAQTPAGRNKQLLAIDDMALLGfGVRTPQAIQQLR 266
Cdd:cd01148 245 LKENPALKNVPAVKNNRFIVLPLAEATP-GIRNVDAIEKLA 284
|
|
| FhuD |
cd01146 |
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ... |
21-248 |
4.88e-09 |
|
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: 55.76 E-value: 4.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604920740 21 EKIVTLGGDVTEIVFALGAQSSLVARDSTS-QW----PQAANDLPDVGYLRQLNAEGILSMRPTLVLASAqaqpSLALKQ 95
Cdd:cd01146 4 QRIVALDWGALETLLALGVKPVGVADTAGYkPWipepALPLEGVVDVGTRGQPNLEAIAALKPDLILGSA----SRHDEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604920740 96 VEQ-SHIR-VVTVPASNALGVIDEKVRVIAQATHREVEGEILRNTLRQALTALPASL---LNKRVLFILNHGGMTAMAAG 170
Cdd:cd01146 80 YDQlSQIApTVLLDSSPWLAEWKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKLpdkGPKPVSVVRFSDAGSIRLYG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604920740 171 QQTAADAAIQAAGLRNA-MQGFTR---YQPLSQEGVIASQPDLVVISQEGINALggEDNLWKLPGLAQTPAGRNKQLLAI 246
Cdd:cd01146 160 PNSFAGSVLEDLGLQNPwAQETTNdsgFATISLERLAKADADVLFVFTYEDEEL--AQALQANPLWQNLPAVKNGRVYVV 237
|
..
gi 1604920740 247 DD 248
Cdd:cd01146 238 DD 239
|
|
| HemV-2 |
cd01147 |
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ... |
21-255 |
2.53e-08 |
|
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: 53.49 E-value: 2.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604920740 21 EKIVTLGGDVTEIVFALGAQSSLVARDSTSQWPQAAN---------DLPDVGYL---RQLNAEGILSMRPTLVLASAQAQ 88
Cdd:cd01147 6 ERVVAAGPGALRLLYALAAPDKIVGVDDAEKSDEGRPyflaspelkDLPVIGRGgrgNTPNYEKIAALKPDVVIDVGSDD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604920740 89 PSLALKQV-EQSHIRVVTVPASNALGVIDEKVRVIAQATHREVEGEIL-------RNTLRQALTALPASlLNKRVLFiln 160
Cdd:cd01147 86 PTSIADDLqKKTGIPVVVLDGGDSLEDTPEQIRLLGKVLGKEERAEELisfiesiLADVEERTKDIPDE-EKPTVYF--- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604920740 161 HGGMTAMAAG---QQTAADAAIQAAGLRN---AMQGFTRYQpLSQEGVIASQPDlVVISQEGINALGGEDNLWKLPGLAQ 234
Cdd:cd01147 162 GRIGTKGAAGlesGLAGSIEVFELAGGINvadGLGGGGLKE-VSPEQILLWNPD-VIFLDTGSFYLSLEGYAKNRPFWQS 239
|
250 260
....*....|....*....|.
gi 1604920740 235 TPAGRNKQLLaidDMALLGFG 255
Cdd:cd01147 240 LKAVKNGRVY---LLPALPFN 257
|
|
| PRK03379 |
PRK03379 |
vitamin B12-transporter protein BtuF; Provisional |
5-213 |
2.98e-06 |
|
vitamin B12-transporter protein BtuF; Provisional
Pssm-ID: 179575 [Multi-domain] Cd Length: 260 Bit Score: 47.37 E-value: 2.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604920740 5 LAVLSALPLMAFAAtqEKIVTLGGDVTEIVFALGAQSslVARDSTSQWPQAANDLPDVGYLRQLNAEGILSMRPTLVLAS 84
Cdd:PRK03379 4 VALLFLAPLWLNAA--PRVITLSPANTELAFAAGITP--VGVSSYSDYPPQAKKIEQVATWQGMNLERIVALKPDLVLAW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604920740 85 AQAQPSLALKQVEQSHIRVVTVPASNALGVIDEkVRVIAQATHREVEGEILRNTLRQ---ALTALPASLLNKRVLfiLNH 161
Cdd:PRK03379 80 RGGNAERQVDQLASLGIKVMWVDATSIEQIANA-LRQLAPWSPQPEKAEQAAQSLLQqyaALKAQYADKPKKRVF--LQF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1604920740 162 GGMTAMAAGQQTAADAAIQAAGLRNAMQGFTRYQP-LSQEGVIASQPDLVVIS 213
Cdd:PRK03379 157 GTNPLFTSGKHSIQSQVLSLCGGENIFADSRVPWPqVSREQVLARKPQAIVIT 209
|
|
| TroA_e |
cd01142 |
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ... |
21-157 |
5.28e-05 |
|
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: 43.88 E-value: 5.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604920740 21 EKIVTLGGDVTEIVFALGAQSSLVARDSTSQW--------PQAANdLPDVGYLRQLNAEGILSMRPTLVLASAQAQPSlA 92
Cdd:cd01142 25 KRIAALWGAGNAVVAALGGGKLIVATTSTVQQepwlyrlaPSLEN-VATGGTGNDVNIEELLALKPDVVIVWSTDGKE-A 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1604920740 93 LKQVEQShIRVVTVPASnALGVIDEKVRVIAQATHREVEGEILRNTLRQALTALPASLLN------KRVLF 157
Cdd:cd01142 103 GKAVLRL-LNALSLRDA-ELEEVKLTIALLGELLGRQEKAEALVAYFDDNLAYVAARTKKlpdserPRVYY 171
|
|
| TroA_f |
cd01139 |
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ... |
18-246 |
6.01e-05 |
|
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: 43.84 E-value: 6.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604920740 18 ATQEKIVTLGGDvteivFALGAQSSLVArdSTSQWPQAAnDLPDVGYL--RQLNAEGILSMRPTLV-LASAQAQPSLA-- 92
Cdd:cd01139 38 NPFARIVGWGGD-----LKKGDPDTYAK--YKEKFPEIA-DIPLIGSTynGDFSVEKVLTLKPDLViLNIWAKTTAEEsg 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604920740 93 -LKQVEQSHIRVVTV-----PASNALgvidEKVRVIAQATHREVEGE---ILRNTLRQALTA-LPASLLNKRVLFI---- 158
Cdd:cd01139 110 iLEKLEQAGIPVVFVdfrqkPLKNTT----PSMRLLGKALGREERAEefiEFYQERIDRIRDrLAKINEPKPKVFIelga 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604920740 159 ------------LNHGGMTAMAAGQQTAADAAIQAAGlrnamqgftryqPLSQEGVIASQPDLVVIS-------QEGINA 219
Cdd:cd01139 186 ggpeeccstygnGNWGELVDAAGGDNIADGLIPGTSG------------ELNAEYVIAANPEIIIATggnwakdPSGVSL 253
|
250 260 270
....*....|....*....|....*....|....*..
gi 1604920740 220 LGG----------EDNLWKLPGLAQTPAGRNKQLLAI 246
Cdd:cd01139 254 GPDgttadakeslLRALLKRPGWSSLQAVKNGRVYAL 290
|
|
| FatB |
cd01140 |
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ... |
15-242 |
1.20e-03 |
|
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: 39.55 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604920740 15 AFAATQEKIVTLGGDVTEIVFALGAqsSLVARDSTSQWPQ-----AANDLPDVGYLRQLNAEGILSMRPTLVLASAQAQP 89
Cdd:cd01140 7 KVPKNPEKVVVFDVGALDTLDALGV--KVVGVPKSSTLPEylkkyKDDKYANVGTLFEPDLEAIAALKPDLIIIGGRLAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604920740 90 SLAlKQVEQSHIRVVTVPASNALGVIDEKVRVIAQATHREVEGEILRNTLRQALTAL-PASLLNKRVLFILNHGGmTAMA 168
Cdd:cd01140 85 KYD-ELKKIAPTIDLGADLKNYLESVKQNIETLGKIFGKEEEAKELVAEIDASIAEAkSAAKGKKKALVVLVNGG-KLSA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604920740 169 AGQQTAADAAIQAAGLRNA---MQGFTRYQPLSQEGVIASQPDLV-------VISQEGINALGGEDN-LWKlpglaQTPA 237
Cdd:cd01140 163 FGPGSRFGWLHDLLGFEPAdenIKASSHGQPVSFEYILEANPDWLfvidrgaAIGAEGSSAKEVLDNdLVK-----NTTA 237
|
....*
gi 1604920740 238 GRNKQ 242
Cdd:cd01140 238 WKNGK 242
|
|
| |
