|
Name |
Accession |
Description |
Interval |
E-value |
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
52-294 |
3.42e-66 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 208.31 E-value: 3.42e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 52 RVVSLNPVTTELLFALGVGDRAVGRTTWDLF---PEAAKAVPDLGPGMGPNVEAVMGQRPDLVLLYASESNRAAVQQLRA 128
Cdd:COG0614 2 RIVSLSPSATELLLALGAGDRLVGVSDWGYCdypELELKDLPVVGGTGEPNLEAILALKPDLVLASSSGNDEEDYEQLEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 129 AGIATLTHRTDKVADLQRVLPVIAAALGVDSLGRLVADSVRASVEAVRA-MPRPAEPVRAFWHIW-DAPIMTIGGGSYMS 206
Cdd:COG0614 82 IGIPVVVLDPRSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRArLAGAEERPTVLYEIWsGDPLYTAGGGSFIG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 207 ELLEIAGAVNVFADAEQPSPAVSLEEIARRNPDVILAGPNN---------ARKLRANPLWQAVPAVRAGRILVIDTTVVG 277
Cdd:COG0614 162 ELLELAGGRNVAADLGGGYPEVSLEQVLALDPDVIILSGGGydaetaeeaLEALLADPGWQSLPAVKNGRVYVVPGDLLS 241
|
250
....*....|....*..
gi 2777341883 278 RPGVRMGEAARFLRRAL 294
Cdd:COG0614 242 RPGPRLLLALEDLAKAL 258
|
|
| BtuF |
cd01144 |
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ... |
51-290 |
1.02e-56 |
|
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: 183.27 E-value: 1.02e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 51 QRVVSLNPVTTELLFALGVGDRAVGRTTWDLFPEAAKAVPDLGPGMGPNVEAVMGQRPDLVLLYASESNRAAVQQLRAAG 130
Cdd:cd01144 1 MRIVSLAPSATELLYALGLGDQLVGVTDYCDYPPEAKKLPRVGGFYQLDLERVLALKPDLVIAWDDCNVCAVVDQLRAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 131 IATLTHRTDKVADLQRVLPVIAAALGVDSLGRLVADSVRASVEAVRAMPRPAEPVRAFWHIWDAPIMTiGGGSYMSELLE 210
Cdd:cd01144 81 IPVLVSEPQTLDDILADIRRLGTLAGRPARAEELAEALRRRLAALRKQYASKPPPRVFYQEWIDPLMT-AGGDWVPELIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 211 IAGAVNVFADAEQPSPAVSLEEIARRNPDVILAGP----NNARKLRANPLWQAVPAVRAGRILVIDTTVVGRPGVRMGEA 286
Cdd:cd01144 160 LAGGVNVFADAGERSPQVSWEDVLAANPDVIVLSPcgfgFTPAILRKEPAWQALPAVRNGRVYAVDGNWYFRPSPRLVDG 239
|
....
gi 2777341883 287 ARFL 290
Cdd:cd01144 240 LEQL 243
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
54-272 |
1.38e-33 |
|
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: 122.86 E-value: 1.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 54 VSLNPVTTELLFALGVGDRAVGRTTWDLFPEAAKAVPDL---GPGMGPNVEAVMGQRPDLVLLYASESNRAAVQQLrAAG 130
Cdd:pfam01497 1 AALSPAYTEILYALGATDSIVGVDAYTRDPLKADAVAAIvkvGAYGEINVERLAALKPDLVILSTGYLTDEAEELL-SLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 131 IATLTHRTDK-VADLQRVLPVIAAALGV-DSLGRLVADSVRASVEAVRAMPRPAEPVRAFWHIWD-APIMTIGGGSYMSE 207
Cdd:pfam01497 80 IPTVIFESSStGESLKEQIKQLGELLGLeDEAEELVAEIDSALAAAKKAVPSLTRKPVLVFGGADgGGYVVAGSNTYIGD 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2777341883 208 LLEIAGAVNVFAD-AEQPSPAVSLEEIARRNPDVIL----AGPNNARK--LRANPLWQAVPAVRAGRILVID 272
Cdd:pfam01497 160 LLRILGIENIAAElSGSEYAPISFEAILSSNPDVIIvsgrDSFTKTGPefVAANPLWAGLPAVKNGRVYTLP 231
|
|
| PRK03379 |
PRK03379 |
vitamin B12-transporter protein BtuF; Provisional |
50-269 |
7.88e-25 |
|
vitamin B12-transporter protein BtuF; Provisional
Pssm-ID: 179575 [Multi-domain] Cd Length: 260 Bit Score: 100.53 E-value: 7.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 50 AQRVVSLNPVTTELLFALGVGDRAVgrTTWDLFPEAAKAVPDLGPGMGPNVEAVMGQRPDLVLLYASESNRAAVQQLRAA 129
Cdd:PRK03379 17 APRVITLSPANTELAFAAGITPVGV--SSYSDYPPQAKKIEQVATWQGMNLERIVALKPDLVLAWRGGNAERQVDQLASL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 130 GIATLTHRTDKVADLQRVLPVIAAALGVDSLGRLVADSVRASVEAVRAMPRPAEPVRAFWHIWDAPIMTIGGGSYMSELL 209
Cdd:PRK03379 95 GIKVMWVDATSIEQIANALRQLAPWSPQPEKAEQAAQSLLQQYAALKAQYADKPKKRVFLQFGTNPLFTSGKHSIQSQVL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2777341883 210 EIAGAVNVFADAEQPSPAVSLEEIARRNPDVILAGPNNARKLRANPLWQ---AVPAV--------RAG-RIL 269
Cdd:PRK03379 175 SLCGGENIFADSRVPWPQVSREQVLARKPQAIVITGGPDQIPKIKQFWGpqlKIPVIplnsdwfeRASpRII 246
|
|
| TroA_like |
NF038402 |
helical backbone metal receptor; |
52-242 |
1.67e-19 |
|
helical backbone metal receptor;
Pssm-ID: 439691 Cd Length: 219 Bit Score: 84.98 E-value: 1.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 52 RVVSLNPVTTELLfALGVGDRAVGRTTWDLFPeAAKAVPDLGPGMGPNVEAVMGQRPDLVLLYASESNRAAVQQLRAAGI 131
Cdd:NF038402 1 RVVSLVPSLTEAI-AATAPELLVGATDWCTHP-ADLDVARVRGTKNPDRAAIAALRPDLVVANQEENRELDVDRLRAAGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 132 ATLTHRTDKVADlqrvlpviaaalGVDSLGRLVADSVRASV-------EAVRAMPRPAEPVRAFWHIWDAPIMTIGGGSY 204
Cdd:NF038402 79 PVWVTRIETVDE------------ALASLRRLFTEALGVPVpgwldeaEREWAAPAPAPRRRAVVPIWRDPWMVVGRDTF 146
|
170 180 190
....*....|....*....|....*....|....*...
gi 2777341883 205 MSELLEIAGAVNVFADAEQPSPAVSLEEIARRNPDVIL 242
Cdd:NF038402 147 TGDLLARLGLRNVFADHPERYPHVDLDELDAAGPDLVL 184
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
52-294 |
3.42e-66 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 208.31 E-value: 3.42e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 52 RVVSLNPVTTELLFALGVGDRAVGRTTWDLF---PEAAKAVPDLGPGMGPNVEAVMGQRPDLVLLYASESNRAAVQQLRA 128
Cdd:COG0614 2 RIVSLSPSATELLLALGAGDRLVGVSDWGYCdypELELKDLPVVGGTGEPNLEAILALKPDLVLASSSGNDEEDYEQLEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 129 AGIATLTHRTDKVADLQRVLPVIAAALGVDSLGRLVADSVRASVEAVRA-MPRPAEPVRAFWHIW-DAPIMTIGGGSYMS 206
Cdd:COG0614 82 IGIPVVVLDPRSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRArLAGAEERPTVLYEIWsGDPLYTAGGGSFIG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 207 ELLEIAGAVNVFADAEQPSPAVSLEEIARRNPDVILAGPNN---------ARKLRANPLWQAVPAVRAGRILVIDTTVVG 277
Cdd:COG0614 162 ELLELAGGRNVAADLGGGYPEVSLEQVLALDPDVIILSGGGydaetaeeaLEALLADPGWQSLPAVKNGRVYVVPGDLLS 241
|
250
....*....|....*..
gi 2777341883 278 RPGVRMGEAARFLRRAL 294
Cdd:COG0614 242 RPGPRLLLALEDLAKAL 258
|
|
| BtuF |
cd01144 |
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ... |
51-290 |
1.02e-56 |
|
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: 183.27 E-value: 1.02e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 51 QRVVSLNPVTTELLFALGVGDRAVGRTTWDLFPEAAKAVPDLGPGMGPNVEAVMGQRPDLVLLYASESNRAAVQQLRAAG 130
Cdd:cd01144 1 MRIVSLAPSATELLYALGLGDQLVGVTDYCDYPPEAKKLPRVGGFYQLDLERVLALKPDLVIAWDDCNVCAVVDQLRAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 131 IATLTHRTDKVADLQRVLPVIAAALGVDSLGRLVADSVRASVEAVRAMPRPAEPVRAFWHIWDAPIMTiGGGSYMSELLE 210
Cdd:cd01144 81 IPVLVSEPQTLDDILADIRRLGTLAGRPARAEELAEALRRRLAALRKQYASKPPPRVFYQEWIDPLMT-AGGDWVPELIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 211 IAGAVNVFADAEQPSPAVSLEEIARRNPDVILAGP----NNARKLRANPLWQAVPAVRAGRILVIDTTVVGRPGVRMGEA 286
Cdd:cd01144 160 LAGGVNVFADAGERSPQVSWEDVLAANPDVIVLSPcgfgFTPAILRKEPAWQALPAVRNGRVYAVDGNWYFRPSPRLVDG 239
|
....
gi 2777341883 287 ARFL 290
Cdd:cd01144 240 LEQL 243
|
|
| ChuT |
COG4558 |
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ... |
43-294 |
1.66e-44 |
|
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443619 [Multi-domain] Cd Length: 285 Bit Score: 153.04 E-value: 1.66e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 43 TSRFARPAQRVVSLNPVTTELLFALGVGDRAVGRTTWDLFPEAAKAVPDLGPGMGPNVEAVMGQRPDLVLLYASESNRAA 122
Cdd:COG4558 20 ASVAAAAAERIVSLGGSVTEIVYALGAGDRLVGVDTTSTYPAAAKALPDVGYMRQLSAEGILSLKPTLVLASEGAGPPEV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 123 VQQLRAAGIATLT-HRTDKVADLQRVLPVIAAALGVDSLGRLVADSVRASVEAVRAMP-RPAEPVRAFWhiwdapIMTIG 200
Cdd:COG4558 100 LDQLRAAGVPVVVvPAAPSLEGVLAKIRAVAAALGVPEAGEALAARLEADLAALAARVaAIGKPPRVLF------LLSRG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 201 GGSYM--------SELLEIAGAVNVFADAEQPSPaVSLEEIARRNPDVIL------AGPNNARKLRANPLWQAVPAVRAG 266
Cdd:COG4558 174 GGRPMvagrgtaaDALIRLAGGVNAAAGFEGYKP-LSAEALIAAAPDVILvmtrglESLGGVDGLLALPGLAQTPAGKNK 252
|
250 260
....*....|....*....|....*...
gi 2777341883 267 RILVIDTTVVGRPGVRMGEAARFLRRAL 294
Cdd:COG4558 253 RIVAMDDLLLLGFGPRTPQAALALAQAL 280
|
|
| YvrC |
cd01143 |
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ... |
48-242 |
1.55e-40 |
|
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: 139.72 E-value: 1.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 48 RPAQRVVSLNPVTTELLFALGVGDRAVGRTTWDLFPEAAKAVPDLGPGMGPNVEAVMGQRPDLVLlyASESNRAAV-QQL 126
Cdd:cd01143 1 KEPERIVSLSPSITEILFALGAGDKIVGVDTYSNYPKEVRKKPKVGSYSNPNVEKIVALKPDLVI--VSSSSLAELlEKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 127 RAAGIATL-THRTDKVADLQRVLPVIAAALGVDSLGRLVADSVRASVEAVRAMPRpAEPVRAFWHIWDAP-IMTIGGGSY 204
Cdd:cd01143 79 KDAGIPVVvLPAASSLDEIYDQIELIGKITGAEEEAEKLVKEMKQKIDKVKDKGK-TIKKSKVYIEVSLGgPYTAGKNTF 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 2777341883 205 MSELLEIAGAVNVFADAEQpSPAVSLEEIARRNPDVIL 242
Cdd:cd01143 158 INELIRLAGAKNIAADSGG-WPQVSPEEILKANPDVII 194
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
54-272 |
1.38e-33 |
|
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: 122.86 E-value: 1.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 54 VSLNPVTTELLFALGVGDRAVGRTTWDLFPEAAKAVPDL---GPGMGPNVEAVMGQRPDLVLLYASESNRAAVQQLrAAG 130
Cdd:pfam01497 1 AALSPAYTEILYALGATDSIVGVDAYTRDPLKADAVAAIvkvGAYGEINVERLAALKPDLVILSTGYLTDEAEELL-SLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 131 IATLTHRTDK-VADLQRVLPVIAAALGV-DSLGRLVADSVRASVEAVRAMPRPAEPVRAFWHIWD-APIMTIGGGSYMSE 207
Cdd:pfam01497 80 IPTVIFESSStGESLKEQIKQLGELLGLeDEAEELVAEIDSALAAAKKAVPSLTRKPVLVFGGADgGGYVVAGSNTYIGD 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2777341883 208 LLEIAGAVNVFAD-AEQPSPAVSLEEIARRNPDVIL----AGPNNARK--LRANPLWQAVPAVRAGRILVID 272
Cdd:pfam01497 160 LLRILGIENIAAElSGSEYAPISFEAILSSNPDVIIvsgrDSFTKTGPefVAANPLWAGLPAVKNGRVYTLP 231
|
|
| TroA_e |
cd01142 |
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ... |
35-290 |
4.18e-31 |
|
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: 117.84 E-value: 4.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 35 TVIDDFGDTSRFARPAQRVVSLNPVTTELLFALGVGDRAVGRT---TWD-----LFPEAAKaVPDLGPGMGPNVEAVMGQ 106
Cdd:cd01142 9 TITDMAGRKVTIPDEVKRIAALWGAGNAVVAALGGGKLIVATTstvQQEpwlyrLAPSLEN-VATGGTGNDVNIEELLAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 107 RPDLVLLYAS---ESNRAAVQQLRAAGIatlthrtdKVADLQRVLPVIAAaLGVDSLGRLVADS----VRASVEAVRAMP 179
Cdd:cd01142 88 KPDVVIVWSTdgkEAGKAVLRLLNALSL--------RDAELEEVKLTIAL-LGELLGRQEKAEAlvayFDDNLAYVAART 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 180 R--PAEPVRAFWHIWDAPIMTIGGGSYMSELLEIAGAVNVFADAEQP-SPAVSLEEIARRNPDVILAG-PNNARKLRANP 255
Cdd:cd01142 159 KklPDSERPRVYYAGPDPLTTDGTGSITNSWIDLAGGINVASEATKKgSGEVSLEQLLKWNPDVIIVGnADTKAAILADP 238
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2777341883 256 LWQAVPAVRAGRILVIDTTVV--GRPGVRMG----EAARFL 290
Cdd:cd01142 239 RWQNLRAVKNGRVYVNPEGAFwwDRPSAEEAllglWLAKTL 279
|
|
| TroA_a |
cd01148 |
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ... |
37-272 |
4.45e-31 |
|
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: 117.82 E-value: 4.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 37 IDDFGDTSRFARPAQRVVSLNPVTTELLFALGVGDRAVGRTTWD-----LFPEAAKAVPDLGPGMgPNVEAVMGQRPDLV 111
Cdd:cd01148 5 VENCGRSVTFDKAPQRVVSNDQNTTEMMLALGLQDRMVGTAGIDnkdlpELKAKYDKVPELAKKY-PSKETVLAARPDLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 112 LLYASESNR----AAVQQLRAAGIATLTHRTDKVadlQRVLPVIAAALGVD--SLGR----------LVADSvRASVEAV 175
Cdd:cd01148 84 FGGWSYGFDkgglGTPDSLAELGIKTYILPESCG---QRRGEATLDDVYNDirNLGKifdvedradkLVADL-KARLAEI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 176 RA-MPRPAEPVRAFWHIW--DAPiMTIGGGSYMSELLEIAGAVNVFADAEQPSPAVSLEEIARRNPDVILA-------GP 245
Cdd:cd01148 160 SAkVKGDGKKVAVFVYDSgeDKP-FTSGRGGIPNAIITAAGGRNVFADVDESWTTVSWETVIARNPDVIVIidygdqnAA 238
|
250 260
....*....|....*....|....*...
gi 2777341883 246 NNARK-LRANPLWQAVPAVRAGRILVID 272
Cdd:cd01148 239 EQKIKfLKENPALKNVPAVKNNRFIVLP 266
|
|
| HutB |
cd01149 |
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ... |
50-272 |
7.89e-29 |
|
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: 110.43 E-value: 7.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 50 AQRVVSLNPVTTELLFALGVGDRAVGRTTWDLFPEAAKAVPDLGPGMGPNVEAVMGQRPDLVLlyASESN--RAAVQQLR 127
Cdd:cd01149 1 PERIVSLGGSVTEIVYALGAGDRLVGVDSTSTYPEAAAKLPDVGYMRQLSAEGVLSLKPTLVI--ASDEAgpPEALDQLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 128 AAGIATLThrTDKVADLQRVLP---VIAAALGVDSLGRLVADSVRASVEAVRAMP--RPAEPVRAFWHIWDA-PIMTIGG 201
Cdd:cd01149 79 AAGVPVVT--VPSTPTLDGLLTkirQVAQALGVPEKGEALAQEVRQRLAALRKTVaaHKKPPRVLFLLSHGGgAAMAAGR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2777341883 202 GSYMSELLEIAGAVNVfADAEQPSPAVSLEEIARRNPDVIL------AGPNNARKLRANPLWQAVPAVRAGRILVID 272
Cdd:cd01149 157 NTAADAIIALAGAVNA-AAGFRGYKPLSAEALIAAQPDVILvmsrglDAVGGVDGLLKLPGLAQTPAGRNKRILAMD 232
|
|
| PRK03379 |
PRK03379 |
vitamin B12-transporter protein BtuF; Provisional |
50-269 |
7.88e-25 |
|
vitamin B12-transporter protein BtuF; Provisional
Pssm-ID: 179575 [Multi-domain] Cd Length: 260 Bit Score: 100.53 E-value: 7.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 50 AQRVVSLNPVTTELLFALGVGDRAVgrTTWDLFPEAAKAVPDLGPGMGPNVEAVMGQRPDLVLLYASESNRAAVQQLRAA 129
Cdd:PRK03379 17 APRVITLSPANTELAFAAGITPVGV--SSYSDYPPQAKKIEQVATWQGMNLERIVALKPDLVLAWRGGNAERQVDQLASL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 130 GIATLTHRTDKVADLQRVLPVIAAALGVDSLGRLVADSVRASVEAVRAMPRPAEPVRAFWHIWDAPIMTIGGGSYMSELL 209
Cdd:PRK03379 95 GIKVMWVDATSIEQIANALRQLAPWSPQPEKAEQAAQSLLQQYAALKAQYADKPKKRVFLQFGTNPLFTSGKHSIQSQVL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2777341883 210 EIAGAVNVFADAEQPSPAVSLEEIARRNPDVILAGPNNARKLRANPLWQ---AVPAV--------RAG-RIL 269
Cdd:PRK03379 175 SLCGGENIFADSRVPWPQVSREQVLARKPQAIVITGGPDQIPKIKQFWGpqlKIPVIplnsdwfeRASpRII 246
|
|
| FhuD |
cd01146 |
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ... |
49-292 |
8.35e-22 |
|
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: 91.96 E-value: 8.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 49 PAQRVVSLNPVTTELLFALGVGDRAVGrTTWDLFP------EAAKAVPDLGPGMGPNVEAVMGQRPDLVLlyASES-NRA 121
Cdd:cd01146 2 KPQRIVALDWGALETLLALGVKPVGVA-DTAGYKPwipepaLPLEGVVDVGTRGQPNLEAIAALKPDLIL--GSASrHDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 122 AVQQLRAagIA---TLTHRTDkVADLQRVLPVIAAALGVDSLGRLVADSVRASVEAVRA-MPRPAEPVRAFWHIWDAPIM 197
Cdd:cd01146 79 IYDQLSQ--IAptvLLDSSPW-LAEWKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQkLPDKGPKPVSVVRFSDAGSI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 198 TI-GGGSYMSELLEIAGAVNVFADAE---QPSPAVSLEEIARRNPDVIL----AGPNNARKLRANPLWQAVPAVRAGRIL 269
Cdd:cd01146 156 RLyGPNSFAGSVLEDLGLQNPWAQETtndSGFATISLERLAKADADVLFvftyEDEELAQALQANPLWQNLPAVKNGRVY 235
|
250 260
....*....|....*....|...
gi 2777341883 270 VIDTTVVGRPGVRMgeAARFLRR 292
Cdd:cd01146 236 VVDDVWWFFGGGLS--AARLLLD 256
|
|
| HemV-2 |
cd01147 |
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ... |
46-270 |
2.49e-20 |
|
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: 88.16 E-value: 2.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 46 FARPAQRVVSLNPVTTELLFALGVGDRAVG----------RTTWDLFPEAAKaVPDLGPGMG---PNVEAVMGQRPDLVL 112
Cdd:cd01147 1 VPKPVERVVAAGPGALRLLYALAAPDKIVGvddaeksdegRPYFLASPELKD-LPVIGRGGRgntPNYEKIAALKPDVVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 113 L---YASESNRAAVQQlrAAGIA-TLTHRTDKVADLQRVLPVIAAALGVDSLGRLVAD---SVRASVEAVRAMPRPAEPV 185
Cdd:cd01147 80 DvgsDDPTSIADDLQK--KTGIPvVVLDGGDSLEDTPEQIRLLGKVLGKEERAEELISfieSILADVEERTKDIPDEEKP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 186 RAFWhiwdAPIMTIGGGSYMS------ELLEIAGAVNVFADAEQPSPA-VSLEEIARRNPDVILAGPNN-----ARKLRA 253
Cdd:cd01147 158 TVYF----GRIGTKGAAGLESglagsiEVFELAGGINVADGLGGGGLKeVSPEQILLWNPDVIFLDTGSfylslEGYAKN 233
|
250
....*....|....*..
gi 2777341883 254 NPLWQAVPAVRAGRILV 270
Cdd:cd01147 234 RPFWQSLKAVKNGRVYL 250
|
|
| TroA_like |
NF038402 |
helical backbone metal receptor; |
52-242 |
1.67e-19 |
|
helical backbone metal receptor;
Pssm-ID: 439691 Cd Length: 219 Bit Score: 84.98 E-value: 1.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 52 RVVSLNPVTTELLfALGVGDRAVGRTTWDLFPeAAKAVPDLGPGMGPNVEAVMGQRPDLVLLYASESNRAAVQQLRAAGI 131
Cdd:NF038402 1 RVVSLVPSLTEAI-AATAPELLVGATDWCTHP-ADLDVARVRGTKNPDRAAIAALRPDLVVANQEENRELDVDRLRAAGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 132 ATLTHRTDKVADlqrvlpviaaalGVDSLGRLVADSVRASV-------EAVRAMPRPAEPVRAFWHIWDAPIMTIGGGSY 204
Cdd:NF038402 79 PVWVTRIETVDE------------ALASLRRLFTEALGVPVpgwldeaEREWAAPAPAPRRRAVVPIWRDPWMVVGRDTF 146
|
170 180 190
....*....|....*....|....*....|....*...
gi 2777341883 205 MSELLEIAGAVNVFADAEQPSPAVSLEEIARRNPDVIL 242
Cdd:NF038402 147 TGDLLARLGLRNVFADHPERYPHVDLDELDAAGPDLVL 184
|
|
| FecB |
COG4594 |
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ... |
31-272 |
3.39e-17 |
|
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443650 [Multi-domain] Cd Length: 316 Bit Score: 80.35 E-value: 3.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 31 AFSHTVIDDFGDTSRFARPaQRVVSLNPVTTELLFALGV-----GDRAVGRTTWDLFPEAAKAVPDLGPGMGPNVEAVMG 105
Cdd:COG4594 34 AGARTVKHAMGETTIPGTP-KRVVVLEWSFADALLALGVtpvgiADDNDYDRWVPYLRDLIKGVTSVGTRSQPNLEAIAA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 106 QRPDLVLlyASESNRAAV-QQLRAagIA-TLT--HRTDKVADLQRVLPVIAAALGVDSLGRLV-------ADSVRASVEA 174
Cdd:COG4594 113 LKPDLII--ADKSRHEAIyDQLSK--IApTVLfkSRNGDYQENLESFKTIAKALGKEEEAEAVladhdqrIAEAKAKLAA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 175 VRAmPRPAEPVRAFwhiwdAPIMTI-GGGSYMSELLEIAGAVNVFADAEQPSPA---VSLEEIARRNPDVILAG----PN 246
Cdd:COG4594 189 ADK-GKKVAVGQFR-----ADGLRLyTPNSFAGSVLAALGFENPPKQSKDNGYGyseVSLEQLPALDPDVLFIAtyddPS 262
|
250 260
....*....|....*....|....*.
gi 2777341883 247 NARKLRANPLWQAVPAVRAGRILVID 272
Cdd:COG4594 263 ILKEWKNNPLWKNLKAVKNGRVYEVD 288
|
|
| btuF |
PRK09534 |
corrinoid ABC transporter substrate-binding protein; Reviewed |
48-296 |
3.50e-16 |
|
corrinoid ABC transporter substrate-binding protein; Reviewed
Pssm-ID: 236552 [Multi-domain] Cd Length: 359 Bit Score: 78.03 E-value: 3.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 48 RPAqRVVSLNPVTTELLFALGVGDRAVGRTTWDLFPEAAKAVPDL--GPGMGPNVEAVMGQRPDLVLLYASESNRAaVQQ 125
Cdd:PRK09534 59 RPE-RVVTLNPSAAQTMWELGARDRVVGVTQYASYLDGAEERTNVsgGQPFGVNVEAVVGLDPDLVLAPNAVAGDT-VTR 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 126 LRAAGI--------ATLTHRTDKVADLQRVLPVIAAALGVDSLGRLVADSVRASVEAVRAMPRpaepvrAFWHIWDApiM 197
Cdd:PRK09534 137 LREAGItvfhfpaaTSIEDVAEKTATIGRLTGNCEAAAETNAEMRDRVDAVEDRTADVDDRPR------VLYPLGDG--Y 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 198 TIGGGSYMSELLEIAGAVNVFADAEQPS-PAVSLEEIARRNPDVILAGPNNARKLRANPlWQAVPAVRAGRILVIDTTVV 276
Cdd:PRK09534 209 TAGGNTFIGALIEAAGGHNVAADATTDGyPQLSEEVIVQQDPDVIVVATASALVAETEP-YASTTAGETGNVVTVNVNHI 287
|
250 260
....*....|....*....|
gi 2777341883 277 GRPGVRMGEAARFLRRALVD 296
Cdd:PRK09534 288 NQPAPRIVESMATMATAFHN 307
|
|
| TroA-like |
cd00636 |
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ... |
51-188 |
3.97e-15 |
|
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: 71.05 E-value: 3.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 51 QRVVSLNPVTTELLFALGVGDRAVGRTTWDLFPEAAKA----VPDLGPGMGPNVEAVMGQRPDLVlLYASESNRAAVQQL 126
Cdd:cd00636 1 KRVVALDPGATELLLALGGDDKPVGVADPSGYPPEAKAllekVPDVGHGYEPNLEKIAALKPDLI-IANGSGLEAWLDKL 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2777341883 127 RAAGIATLTHRTDKVADLQRVLP---VIAAALGVDSLGRLVADSVRASVEAVRAMPRPAEPVRAF 188
Cdd:cd00636 80 SKIAIPVVVVDEASELSLENIKEsirLIGKALGKEENAEELIAELDARLAELRAKLAKIPKKKVS 144
|
|
| TroA_d |
cd01141 |
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ... |
48-220 |
5.31e-14 |
|
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: 68.99 E-value: 5.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 48 RPAQRVVSLNPVTTELLFALGVGDRAVGRTTWDLFPE----AAKAVPDLGPGMGPNVEAVMGQRPDLVLLYASESNRAAV 123
Cdd:cd01141 6 VPPKRIVVLSPTHVDLLLALDKADKIVGVSASAYDLNtpavKERIDIQVGPTGSLNVELIVALKPDLVILYGGFQAQTIL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 124 QQLRAAGIATLThrTDKVAD-LQRVLPVIAAALGVDSLGRLVADSVRASVEAVR-----AMPRPAEPVRAFWHIWDAPIM 197
Cdd:cd01141 86 DKLEQLGIPVLY--VNEYPSpLGRAEWIKFAAAFYGVGKEDKADEAFAQIAGRYrdlakKVSNLNKPTVAIGKPVKGLWY 163
|
170 180
....*....|....*....|...
gi 2777341883 198 TIGGGSYMSELLEIAGAVNVFAD 220
Cdd:cd01141 164 MPGGNSYVAKMLRDAGGRYLSAE 186
|
|
| FatB |
cd01140 |
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ... |
38-272 |
2.17e-13 |
|
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: 68.82 E-value: 2.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 38 DDFGDTSRFARPaQRVVSLNPVTTELLFALGVgdRAVGRTTWDLFPEAAKAV-----PDLGPGMGPNVEAVMGQRPDLVL 112
Cdd:cd01140 1 HALGETKVPKNP-EKVVVFDVGALDTLDALGV--KVVGVPKSSTLPEYLKKYkddkyANVGTLFEPDLEAIAALKPDLII 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 113 LyaseSNRAAvqqlraagiatlthrtDKVADLQRVLPVIAAALG-----------VDSLGR----------LVADsVRAS 171
Cdd:cd01140 78 I----GGRLA----------------EKYDELKKIAPTIDLGADlknylesvkqnIETLGKifgkeeeakeLVAE-IDAS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 172 VEAVRAMPRPAEPVRAFWHIwDAPIMTIGGGSYMSELLEIAGAVNVFADAEQPSP--AVSLEEIARRNPDVIL------- 242
Cdd:cd01140 137 IAEAKSAAKGKKKALVVLVN-GGKLSAFGPGSRFGWLHDLLGFEPADENIKASSHgqPVSFEYILEANPDWLFvidrgaa 215
|
250 260 270
....*....|....*....|....*....|..
gi 2777341883 243 --AGPNNARKLRANPLWQAVPAVRAGRILVID 272
Cdd:cd01140 216 igAEGSSAKEVLDNDLVKNTTAWKNGKVIYLD 247
|
|
| CeuA |
COG4607 |
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and ... |
16-272 |
7.90e-09 |
|
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443657 [Multi-domain] Cd Length: 310 Bit Score: 55.57 E-value: 7.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 16 LAACtGQERAATGGPAFSHTV-IDDFGDTSRFARPAQRVVSLNPVTTELLFALGVGDRAVGRttwDLFPE-----AAKAV 89
Cdd:COG4607 17 LAAC-GSSSAAAASAAAAETVtVEHALGTVEVPKNPKRVVVFDNGALDTLDALGVEVAGVPK---GLLPDylskyADDKY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 90 PDLGPGMGPNVEAVMGQRPDLVLLyaseSNRAAvqqlraagiatlthrtDKVADLQRVLPVIaaALGVDS---------- 159
Cdd:COG4607 93 ANVGTLFEPDLEAIAALKPDLIII----GGRSA----------------KKYDELSKIAPTI--DLTVDGedyleslkrn 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 160 ---LGR----------LVADsVRASVEAVRAMPRPAEPVRAfwhiwdapIMTIGG-------GSYMSELLEIAGAVNVFA 219
Cdd:COG4607 151 tetLGEifgkedeaeeLVAD-LDAKIAALKAAAAGKGTALI--------VLTNGGkisaygpGSRFGPIHDVLGFKPADE 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2777341883 220 DAE-----QPspaVSLEEIARRNPDVIL---------AGPNNARKLRANPLWQAVPAVRAGRILVID 272
Cdd:COG4607 222 DIEasthgQA---ISFEFIAEANPDWLFvidrdaaigGEGPAAKQVLDNELVKQTTAWKNGQIVYLD 285
|
|
| PRK10576 |
PRK10576 |
Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD; |
50-267 |
2.23e-08 |
|
Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD;
Pssm-ID: 236719 Cd Length: 292 Bit Score: 54.25 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 50 AQRVVSLNPVTTELLFALGVGDRAVGRT----TWDLFPEAAKAVPDLGPGMGPNVEAVMGQRPDLVLLyaSESNRAAVQQ 125
Cdd:PRK10576 32 PNRIVALEWLPVELLLALGVTPYGVADThnyrLWVSEPALPDSVIDVGLRTEPNLELLTQMKPSLILW--SAGYGPSPEK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 126 LRAagIA-----TLTHRTDKVADLQRVLPVIAAALGVDSLGRLVADSVRASVEAVRA--MPRPAEPVRAFWHIWDAPIMT 198
Cdd:PRK10576 110 LAR--IApgrgfAFSDGKKPLAVARKSLVELAQRLNLEAAAETHLAQFDDFIASAKPrlAGRGQRPLLLTSLIDPRHALV 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2777341883 199 IGGGSYMSELLEIAGAVNVFADAEQ--PSPAVSLEEIAR-RNPDVILAGPNNAR---KLRANPLWQAVPAVRAGR 267
Cdd:PRK10576 188 FGPNSLFQEVLDELGIENAWQGETNfwGSTVVGIERLAAyKDADVICFDHGNSKdmqQLMATPLWQAMPFVRAGR 262
|
|
| TroA_f |
cd01139 |
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ... |
35-268 |
3.48e-08 |
|
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: 53.85 E-value: 3.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 35 TVIDDFGDTSRFARPAQRVV--------SLNPVTTELLFALGVG---DRAVGRT-TWDL----FPEAAKaVPDLGPGMGP 98
Cdd:cd01139 2 TVTDVAGRKVTLDAPVERVLlgegrqlyALALLEGENPFARIVGwggDLKKGDPdTYAKykekFPEIAD-IPLIGSTYNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 99 --NVEAVMGQRPDLVLL----YASESNRAAVQQLRAAGI---------ATLTHRTDKVadlqRVLpviAAALGVDSLGRL 163
Cdd:cd01139 81 dfSVEKVLTLKPDLVILniwaKTTAEESGILEKLEQAGIpvvfvdfrqKPLKNTTPSM----RLL---GKALGREERAEE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 164 VADSVRASVEAVRA------MPRPAEPVRAFWHIWDAPIMTIGGGSyMSELLEIAGAVNVfADAEQPSP--AVSLEEIAR 235
Cdd:cd01139 154 FIEFYQERIDRIRDrlakinEPKPKVFIELGAGGPEECCSTYGNGN-WGELVDAAGGDNI-ADGLIPGTsgELNAEYVIA 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2777341883 236 RNPD-VILAGPNNA----------------------RKLRANPLWQAVPAVRAGRI 268
Cdd:cd01139 232 ANPEiIIATGGNWAkdpsgvslgpdgttadakesllRALLKRPGWSSLQAVKNGRV 287
|
|
| fecB |
PRK11411 |
iron-dicitrate transporter substrate-binding subunit; Provisional |
200-272 |
2.18e-06 |
|
iron-dicitrate transporter substrate-binding subunit; Provisional
Pssm-ID: 183123 [Multi-domain] Cd Length: 303 Bit Score: 48.52 E-value: 2.18e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2777341883 200 GGGSYMSELLEIAG-AVNVFADAEQPSPAVSLEEIARRNPDVILAG----PNNARKLRANPLWQAVPAVRAGRILVID 272
Cdd:PRK11411 193 SPESYTGSVLAALGlNVPKAPMNGAAMPSISLEQLLALNPDWLLVAhyrqESIVKRWQQDPLWQMLTAAKKQQVASVD 270
|
|
| PRK10957 |
PRK10957 |
iron-enterobactin transporter periplasmic binding protein; Provisional |
98-268 |
8.84e-03 |
|
iron-enterobactin transporter periplasmic binding protein; Provisional
Pssm-ID: 236806 [Multi-domain] Cd Length: 317 Bit Score: 37.26 E-value: 8.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 98 PNVEAVMGQRPDLVLLYAS--ESNRAAVQQLRAAGIATLTHRTDKvaDLQRVLPVIAAALGVDSLGRLVADSVRASVEAV 175
Cdd:PRK10957 104 PDAEAVAAQMPDLIVISATggDSALALYDQLSAIAPTLVIDYDDK--SWQELATQLGEATGLEKQAAAVIAQFDAQLAEV 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 176 RA-MPRPAEPVRAFWHIWDAPIMTIG-GGSYMSELLEIAGavnvFADAEQPsPAVSLEEIARRNPDVILAGPNN------ 247
Cdd:PRK10957 182 KAkITLPPQPVSALVYNGAGHSANLWtPESAQGQLLEQLG----FTLAELP-AGLQASTSQGKRHDIIQLGGENlaagln 256
|
170 180 190
....*....|....*....|....*....|....
gi 2777341883 248 -------------ARKLRANPLWQAVPAVRAGRI 268
Cdd:PRK10957 257 getlflfagddkdADAFLADPLLANLPAVQNKQV 290
|
|
|