|
Name |
Accession |
Description |
Interval |
E-value |
| TroA_e |
cd01142 |
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ... |
19-329 |
6.18e-85 |
|
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: 258.44 E-value: 6.18e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 19 SSQASRQITDQIGRQVSIPDHVDRIVVLQHQTLNLLEQMNATDKIVGVMTNWKQqlGDGYARLAPELNHMATLGDLTHVD 98
Cdd:cd01142 3 ATAATRTITDMAGRKVTIPDEVKRIAALWGAGNAVVAALGGGKLIVATTSTVQQ--EPWLYRLAPSLENVATGGTGNDVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 99 PEKLVALHPQVVFITNYAPHEMIDSITALgIPVVAIslrhdlpgeqdkmnptlSDEEMaydKGLREGITLIGEIVNKPAQ 178
Cdd:cd01142 81 IEELLALKPDVVIVWSTDGKEAGKAVLRL-LNALSL-----------------RDAEL---EEVKLTIALLGELLGRQEK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 179 AKALIEATDQGRKIVSDRLKDIPADKRIRAYMANP-QLTTYGSGKYTGLMMQHAGAVNVAA-ATVKGFKTVSMEQVIAWD 256
Cdd:cd01142 140 AEALVAYFDDNLAYVAARTKKLPDSERPRVYYAGPdPLTTDGTGSITNSWIDLAGGINVASeATKKGSGEVSLEQLLKWN 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1240938646 257 PQVIFVQDRYPSVvnEINSSPQWQAIDAVKNHRVYLMPDYAKAWGYPMPEaMGLGELWMAKKLYPQKFQDVDM 329
Cdd:cd01142 220 PDVIIVGNADTKA--AILADPRWQNLRAVKNGRVYVNPEGAFWWDRPSAE-EALLGLWLAKTLYPERFTDDDM 289
|
|
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
42-325 |
1.51e-54 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 179.81 E-value: 1.51e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 42 RIVVLQHQTLNLLEQMNATDKIVGVmTNWkqqlgdGYARLAP-ELNHMATLGDLTHVDPEKLVALHPQVVFITNYAPHE- 119
Cdd:COG0614 2 RIVSLSPSATELLLALGAGDRLVGV-SDW------GYCDYPElELKDLPVVGGTGEPNLEAILALKPDLVLASSSGNDEe 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 120 MIDSITALGIPVVAISLRhdlpgeqdkmnpTLSDeemaydkgLREGITLIGEIVNKPAQAKALIEATDQGRKIVSDRLKD 199
Cdd:COG0614 75 DYEQLEKIGIPVVVLDPR------------SLED--------LYESIRLLGELLGREERAEALIAEYEARLAAVRARLAG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 200 ipADKRIRAYMA---NPQLTTYGSGKYTGLMMQHAGAVNVAAATVKGFKTVSMEQVIAWDPQVIFVQDRYP------SVV 270
Cdd:COG0614 135 --AEERPTVLYEiwsGDPLYTAGGGSFIGELLELAGGRNVAADLGGGYPEVSLEQVLALDPDVIILSGGGYdaetaeEAL 212
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1240938646 271 NEINSSPQWQAIDAVKNHRVYLMPDYakAWGYPMPEAMgLGELWMAKKLYPQKFQ 325
Cdd:COG0614 213 EALLADPGWQSLPAVKNGRVYVVPGD--LLSRPGPRLL-LALEDLAKALHPELFA 264
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
47-296 |
4.41e-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: 95.90 E-value: 4.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 47 QHQTLNLLeqmNATDKIVGVmtnwkqqlgDGYAR---LAPELNHMATLGDLTHVDPEKLVALHPQVVFITNYAPHEMIDS 123
Cdd:pfam01497 7 YTEILYAL---GATDSIVGV---------DAYTRdplKADAVAAIVKVGAYGEINVERLAALKPDLVILSTGYLTDEAEE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 124 ITALGIPVVAislrhdlpgeqdkMNPTLSDEEmaydkgLREGITLIGEIVNKPAQAKALIEATDQgrKIVSDRlKDIPAD 203
Cdd:pfam01497 75 LLSLIIPTVI-------------FESSSTGES------LKEQIKQLGELLGLEDEAEELVAEIDS--ALAAAK-KAVPSL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 204 KR-IRAYMANPQLTTY---GSGKYTGLMMQHAGAVNVAAATVK-GFKTVSMEQVIAWDPQVIFVQDR---YPSVVNEINS 275
Cdd:pfam01497 133 TRkPVLVFGGADGGGYvvaGSNTYIGDLLRILGIENIAAELSGsEYAPISFEAILSSNPDVIIVSGRdsfTKTGPEFVAA 212
|
250 260
....*....|....*....|.
gi 1240938646 276 SPQWQAIDAVKNHRVYLMPDY 296
Cdd:pfam01497 213 NPLWAGLPAVKNGRVYTLPSD 233
|
|
| btuF |
PRK09534 |
corrinoid ABC transporter substrate-binding protein; Reviewed |
27-272 |
3.03e-12 |
|
corrinoid ABC transporter substrate-binding protein; Reviewed
Pssm-ID: 236552 [Multi-domain] Cd Length: 359 Bit Score: 66.86 E-value: 3.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 27 TDQIGRQVSIPDHVDRIVVLQHQTLNLLEQMNATDKIVGVmTNWKQQLgDGyarlAPELNHMATLGDLThVDPEKLVALH 106
Cdd:PRK09534 47 TDATGTEITLDERPERVVTLNPSAAQTMWELGARDRVVGV-TQYASYL-DG----AEERTNVSGGQPFG-VNVEAVVGLD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 107 PQVVFITNYAPHEMIDSITALGIPVVaislrhdlpgeQDKMNPTLSDeemaydkgLREGITLIGEIVNKPAQAKALIEAT 186
Cdd:PRK09534 120 PDLVLAPNAVAGDTVTRLREAGITVF-----------HFPAATSIED--------VAEKTATIGRLTGNCEAAAETNAEM 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 187 DQGRKIVSDRLKDIpaDKRIRAYMANPQLTTYGSGKYTGLMMQHAGAVNVAA-ATVKGFKTVSMEQVIAWDPQVIFVQDR 265
Cdd:PRK09534 181 RDRVDAVEDRTADV--DDRPRVLYPLGDGYTAGGNTFIGALIEAAGGHNVAAdATTDGYPQLSEEVIVQQDPDVIVVATA 258
|
....*..
gi 1240938646 266 YPSVVNE 272
Cdd:PRK09534 259 SALVAET 265
|
|
| IsdE |
TIGR03659 |
heme ABC transporter, heme-binding protein isdE; This family of ABC substrate-binding proteins ... |
160-291 |
4.84e-08 |
|
heme ABC transporter, heme-binding protein isdE; This family of ABC substrate-binding proteins is observed primarily in close proximity with proteins localized to the cell wall and bearing the NEAT (NEAr Transporter, pfam05031) heme-binding domain. IsdE has been shown to bind heme and is involved in the process of scavenging heme for the purpose of obtaining iron.
Pssm-ID: 274706 [Multi-domain] Cd Length: 289 Bit Score: 53.43 E-value: 4.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 160 KGLREGITLIGEIVNKPAQAKALIEATDQGRKIVsdrLKDIPADKRIR---------AYManpqLTTYGSgkYTGLMMQH 230
Cdd:TIGR03659 125 DGMKKSITELGEKYGREEQAEKLVKEINEKEAEV---KKKVKGKKKPKvlilmgvpgSYL----VATENS--YIGDLVKL 195
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1240938646 231 AGAVNVAAATVKGFKTVSMEQVIAWDPQVIFVQDR-YPSVV-----NEINSSPQWQAIDAVKNHRVY 291
Cdd:TIGR03659 196 AGGENVYKGNKQEYLSSNTEYLLKANPDIILRAAHgMPDEVkkmfdEEFKTNDIWKHFEAVKNNRVY 262
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| TroA_e |
cd01142 |
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ... |
19-329 |
6.18e-85 |
|
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: 258.44 E-value: 6.18e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 19 SSQASRQITDQIGRQVSIPDHVDRIVVLQHQTLNLLEQMNATDKIVGVMTNWKQqlGDGYARLAPELNHMATLGDLTHVD 98
Cdd:cd01142 3 ATAATRTITDMAGRKVTIPDEVKRIAALWGAGNAVVAALGGGKLIVATTSTVQQ--EPWLYRLAPSLENVATGGTGNDVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 99 PEKLVALHPQVVFITNYAPHEMIDSITALgIPVVAIslrhdlpgeqdkmnptlSDEEMaydKGLREGITLIGEIVNKPAQ 178
Cdd:cd01142 81 IEELLALKPDVVIVWSTDGKEAGKAVLRL-LNALSL-----------------RDAEL---EEVKLTIALLGELLGRQEK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 179 AKALIEATDQGRKIVSDRLKDIPADKRIRAYMANP-QLTTYGSGKYTGLMMQHAGAVNVAA-ATVKGFKTVSMEQVIAWD 256
Cdd:cd01142 140 AEALVAYFDDNLAYVAARTKKLPDSERPRVYYAGPdPLTTDGTGSITNSWIDLAGGINVASeATKKGSGEVSLEQLLKWN 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1240938646 257 PQVIFVQDRYPSVvnEINSSPQWQAIDAVKNHRVYLMPDYAKAWGYPMPEaMGLGELWMAKKLYPQKFQDVDM 329
Cdd:cd01142 220 PDVIIVGNADTKA--AILADPRWQNLRAVKNGRVYVNPEGAFWWDRPSAE-EALLGLWLAKTLYPERFTDDDM 289
|
|
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
42-325 |
1.51e-54 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 179.81 E-value: 1.51e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 42 RIVVLQHQTLNLLEQMNATDKIVGVmTNWkqqlgdGYARLAP-ELNHMATLGDLTHVDPEKLVALHPQVVFITNYAPHE- 119
Cdd:COG0614 2 RIVSLSPSATELLLALGAGDRLVGV-SDW------GYCDYPElELKDLPVVGGTGEPNLEAILALKPDLVLASSSGNDEe 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 120 MIDSITALGIPVVAISLRhdlpgeqdkmnpTLSDeemaydkgLREGITLIGEIVNKPAQAKALIEATDQGRKIVSDRLKD 199
Cdd:COG0614 75 DYEQLEKIGIPVVVLDPR------------SLED--------LYESIRLLGELLGREERAEALIAEYEARLAAVRARLAG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 200 ipADKRIRAYMA---NPQLTTYGSGKYTGLMMQHAGAVNVAAATVKGFKTVSMEQVIAWDPQVIFVQDRYP------SVV 270
Cdd:COG0614 135 --AEERPTVLYEiwsGDPLYTAGGGSFIGELLELAGGRNVAADLGGGYPEVSLEQVLALDPDVIILSGGGYdaetaeEAL 212
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1240938646 271 NEINSSPQWQAIDAVKNHRVYLMPDYakAWGYPMPEAMgLGELWMAKKLYPQKFQ 325
Cdd:COG0614 213 EALLADPGWQSLPAVKNGRVYVVPGD--LLSRPGPRLL-LALEDLAKALHPELFA 264
|
|
| HemV-2 |
cd01147 |
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ... |
36-294 |
1.83e-51 |
|
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: 171.75 E-value: 1.83e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 36 IPDHVDRIVVLQHQTLNLLEQMNATDKIVGVMTNWKQQLGDGYARLAPELNHMATLGDLTH---VDPEKLVALHPQVVFI 112
Cdd:cd01147 1 VPKPVERVVAAGPGALRLLYALAAPDKIVGVDDAEKSDEGRPYFLASPELKDLPVIGRGGRgntPNYEKIAALKPDVVID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 113 T-NYAPHEMIDSI-TALGIPVVAISLRHDLpgeqdkmnptlsdEEMaydkglREGITLIGEIVNKPAQAKALIEATDQGR 190
Cdd:cd01147 81 VgSDDPTSIADDLqKKTGIPVVVLDGGDSL-------------EDT------PEQIRLLGKVLGKEERAEELISFIESIL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 191 KIVSDRLKDIPADKRIRAYMAnPQLTTYGSGKYTGL-----MMQHAGAVNVA-AATVKGFKTVSMEQVIAWDPQVIFVQD 264
Cdd:cd01147 142 ADVEERTKDIPDEEKPTVYFG-RIGTKGAAGLESGLagsieVFELAGGINVAdGLGGGGLKEVSPEQILLWNPDVIFLDT 220
|
250 260 270
....*....|....*....|....*....|..
gi 1240938646 265 R--YPSVVNEINSSPQWQAIDAVKNHRVYLMP 294
Cdd:cd01147 221 GsfYLSLEGYAKNRPFWQSLKAVKNGRVYLLP 252
|
|
| TroA_f |
cd01139 |
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ... |
26-347 |
3.41e-37 |
|
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: 136.67 E-value: 3.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 26 ITDQIGRQVSIPDHVDRIVV---LQHQTLNLLEQMNATDKIVGVMTNWKQQLGDGYARLA---PELNHMATLGDLTH--V 97
Cdd:cd01139 3 VTDVAGRKVTLDAPVERVLLgegRQLYALALLEGENPFARIVGWGGDLKKGDPDTYAKYKekfPEIADIPLIGSTYNgdF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 98 DPEKLVALHPQVVFITN--YAPH---EMIDSITALGIPVVAISLRhdlpgeQDKMNPTLsdeemaydkglrEGITLIGEI 172
Cdd:cd01139 83 SVEKVLTLKPDLVILNIwaKTTAeesGILEKLEQAGIPVVFVDFR------QKPLKNTT------------PSMRLLGKA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 173 VNKPAQAKALIEATDQGRKIVSDRLKDIpADKRIRAYM------ANPQLTTYGSGKYtGLMMQHAGAVNVAAATVKG-FK 245
Cdd:cd01139 145 LGREERAEEFIEFYQERIDRIRDRLAKI-NEPKPKVFIelgaggPEECCSTYGNGNW-GELVDAAGGDNIADGLIPGtSG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 246 TVSMEQVIAWDPQVIFVQDR-YPSVVNEINSSPQ-------------------WQAIDAVKNHRVYlmpdyaKAW--GYP 303
Cdd:cd01139 223 ELNAEYVIAANPEIIIATGGnWAKDPSGVSLGPDgttadakesllrallkrpgWSSLQAVKNGRVY------ALWhqFYR 296
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1240938646 304 MPEAMGLGELwMAKKLYPQKFQDVDMNKLANRWYQRFYRTTYQG 347
Cdd:cd01139 297 SPYNFVALEA-FAKWLYPELFKDLDPEATLQEFHRQFLPVDYSG 339
|
|
| YvrC |
cd01143 |
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ... |
42-262 |
7.54e-29 |
|
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: 110.45 E-value: 7.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 42 RIVVLQHQTLNLLEQMNATDKIVGVmtnwkqqlgDGYARLAPELNHMATLGDLTHVDPEKLVALHPQVVFITNYAPHEMI 121
Cdd:cd01143 5 RIVSLSPSITEILFALGAGDKIVGV---------DTYSNYPKEVRKKPKVGSYSNPNVEKIVALKPDLVIVSSSSLAELL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 122 DSITALGIPVVAIslrhdlpgeqdkmnPTLSDEEMAYDKglregITLIGEIVNKPAQAKALIEATDQGRKIVSDRLKDIp 201
Cdd:cd01143 76 EKLKDAGIPVVVL--------------PAASSLDEIYDQ-----IELIGKITGAEEEAEKLVKEMKQKIDKVKDKGKTI- 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1240938646 202 adKRIRAY--MANPQLTTYGSGKYTGLMMQHAGAVNVAAATvKGFKTVSMEQVIAWDPQVIFV 262
Cdd:cd01143 136 --KKSKVYieVSLGGPYTAGKNTFINELIRLAGAKNIAADS-GGWPQVSPEEILKANPDVIIL 195
|
|
| ChuT |
COG4558 |
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ... |
31-322 |
4.89e-26 |
|
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443619 [Multi-domain] Cd Length: 285 Bit Score: 105.27 E-value: 4.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 31 GRQVSIPDhVDRIVVLQHQTLNLLEQMNATDKIVGVmtnwkqqlgDGYARLAPELNHMATLGDLTHVDPEKLVALHPQVV 110
Cdd:COG4558 19 GASVAAAA-AERIVSLGGSVTEIVYALGAGDRLVGV---------DTTSTYPAAAKALPDVGYMRQLSAEGILSLKPTLV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 111 FITNYA-PHEMIDSITALGIPVVAISLRHDLpgeqdkmnptlsdeemaydKGLREGITLIGEIVNKPAQAKALIEATDQG 189
Cdd:COG4558 89 LASEGAgPPEVLDQLRAAGVPVVVVPAAPSL-------------------EGVLAKIRAVAAALGVPEAGEALAARLEAD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 190 RKIVSDRLKDIPADKRIRAYMANPQLTTYGSGKYTGL--MMQHAGAVNvAAATVKGFKTVSMEQVIAWDPQVIFVQDR-Y 266
Cdd:COG4558 150 LAALAARVAAIGKPPRVLFLLSRGGGRPMVAGRGTAAdaLIRLAGGVN-AAAGFEGYKPLSAEALIAAAPDVILVMTRgL 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1240938646 267 PSV--VNEINSSPQWQAIDAVKNHRVYLMPD-YAKAWGYPMPEAmgLGELwmAKKLYPQ 322
Cdd:COG4558 229 ESLggVDGLLALPGLAQTPAGKNKRIVAMDDlLLLGFGPRTPQA--ALAL--AQALYPA 283
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
47-296 |
4.41e-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: 95.90 E-value: 4.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 47 QHQTLNLLeqmNATDKIVGVmtnwkqqlgDGYAR---LAPELNHMATLGDLTHVDPEKLVALHPQVVFITNYAPHEMIDS 123
Cdd:pfam01497 7 YTEILYAL---GATDSIVGV---------DAYTRdplKADAVAAIVKVGAYGEINVERLAALKPDLVILSTGYLTDEAEE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 124 ITALGIPVVAislrhdlpgeqdkMNPTLSDEEmaydkgLREGITLIGEIVNKPAQAKALIEATDQgrKIVSDRlKDIPAD 203
Cdd:pfam01497 75 LLSLIIPTVI-------------FESSSTGES------LKEQIKQLGELLGLEDEAEELVAEIDS--ALAAAK-KAVPSL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 204 KR-IRAYMANPQLTTY---GSGKYTGLMMQHAGAVNVAAATVK-GFKTVSMEQVIAWDPQVIFVQDR---YPSVVNEINS 275
Cdd:pfam01497 133 TRkPVLVFGGADGGGYvvaGSNTYIGDLLRILGIENIAAELSGsEYAPISFEAILSSNPDVIIVSGRdsfTKTGPEFVAA 212
|
250 260
....*....|....*....|.
gi 1240938646 276 SPQWQAIDAVKNHRVYLMPDY 296
Cdd:pfam01497 213 NPLWAGLPAVKNGRVYTLPSD 233
|
|
| HutB |
cd01149 |
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ... |
40-295 |
3.38e-18 |
|
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: 82.31 E-value: 3.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 40 VDRIVVLQHQTLNLLEQMNATDKIVGVmtnwkqqlgDGYARLAPELNHMATLGDLTHVDPEKLVALHPQVVFITNYA-PH 118
Cdd:cd01149 1 PERIVSLGGSVTEIVYALGAGDRLVGV---------DSTSTYPEAAAKLPDVGYMRQLSAEGVLSLKPTLVIASDEAgPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 119 EMIDSITALGIPVVAislrhdLPGEqdkmnPTLsdeemaydKGLREGITLIGEIVNKPAQAKALIEATDQGRKIVSDRLK 198
Cdd:cd01149 72 EALDQLRAAGVPVVT------VPST-----PTL--------DGLLTKIRQVAQALGVPEKGEALAQEVRQRLAALRKTVA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 199 DIPADKRIRAYMANPQLTTYGSGKYTG--LMMQHAGAVNvAAATVKGFKTVSMEQVIAWDPQVIFVQDR-YPSV--VNEI 273
Cdd:cd01149 133 AHKKPPRVLFLLSHGGGAAMAAGRNTAadAIIALAGAVN-AAAGFRGYKPLSAEALIAAQPDVILVMSRgLDAVggVDGL 211
|
250 260
....*....|....*....|..
gi 1240938646 274 NSSPQWQAIDAVKNHRVYLMPD 295
Cdd:cd01149 212 LKLPGLAQTPAGRNKRILAMDD 233
|
|
| FhuD |
cd01146 |
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ... |
42-296 |
1.17e-17 |
|
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: 81.18 E-value: 1.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 42 RIVVLqhqTLNLLEQMNATD-KIVGV--MTNWKQQLGDGYARLAPELNhmatLGDLTHVDPEKLVALHPqvvfitnyaph 118
Cdd:cd01146 5 RIVAL---DWGALETLLALGvKPVGVadTAGYKPWIPEPALPLEGVVD----VGTRGQPNLEAIAALKP----------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 119 emiDSItalgipvVAISLRHDLPGEQ-DKMNPTLSDEEMAYDKGLREGITLIGEIVNKPAQAKALIEATDQGRKIVSDRL 197
Cdd:cd01146 67 ---DLI-------LGSASRHDEIYDQlSQIAPTVLLDSSPWLAEWKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 198 KDIPaDKRIR--AYMANPQLTTYGSGKYTGLMMQHAG---AVNVAAATVKGFKTVSMEQVIAWDPQVIFV-QDRYPSVVN 271
Cdd:cd01146 137 PDKG-PKPVSvvRFSDAGSIRLYGPNSFAGSVLEDLGlqnPWAQETTNDSGFATISLERLAKADADVLFVfTYEDEELAQ 215
|
250 260
....*....|....*....|....*
gi 1240938646 272 EINSSPQWQAIDAVKNHRVYLMPDY 296
Cdd:cd01146 216 ALQANPLWQNLPAVKNGRVYVVDDV 240
|
|
| FecB |
COG4594 |
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ... |
19-295 |
1.82e-17 |
|
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443650 [Multi-domain] Cd Length: 316 Bit Score: 81.89 E-value: 1.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 19 SSQASRQITDQIGrQVSIPDHVDRIVVLqhqtlnllEQMNATD------KIVGVMTNWKQQLGDGYarLAPELNHMATLG 92
Cdd:COG4594 32 AAAGARTVKHAMG-ETTIPGTPKRVVVL--------EWSFADAllalgvTPVGIADDNDYDRWVPY--LRDLIKGVTSVG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 93 DLTHVDPEKLVALHPqvvfitnyaphemiDSItalgipvVAISLRH-DLPGEQDKMNPTLSDEEMAYD-KGLREGITLIG 170
Cdd:COG4594 101 TRSQPNLEAIAALKP--------------DLI-------IADKSRHeAIYDQLSKIAPTVLFKSRNGDyQENLESFKTIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 171 EIVNKPAQAKALIEATDQGRKIVSDRLKDIPADKRIRAYMANP-QLTTYGSGKYTGLMMQHAGAVNVAAA---TVKGFKT 246
Cdd:COG4594 160 KALGKEEEAEAVLADHDQRIAEAKAKLAAADKGKKVAVGQFRAdGLRLYTPNSFAGSVLAALGFENPPKQskdNGYGYSE 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1240938646 247 VSMEQVIAWDPQVIFV-QDRYPSVVNEINSSPQWQAIDAVKNHRVYLMPD 295
Cdd:COG4594 240 VSLEQLPALDPDVLFIaTYDDPSILKEWKNNPLWKNLKAVKNGRVYEVDG 289
|
|
| TroA-like |
cd00636 |
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ... |
42-205 |
2.55e-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: 72.21 E-value: 2.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 42 RIVVLQHQTLNLLEQMNATDKIVGVMTNWKQQLGDGYARLAPelnhmATLGDLTHVDPEKLVALHPQVVFITNYAPHEMI 121
Cdd:cd00636 2 RVVALDPGATELLLALGGDDKPVGVADPSGYPPEAKALLEKV-----PDVGHGYEPNLEKIAALKPDLIIANGSGLEAWL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 122 DSITALGIPVVAISLRHDLPgeqdkmnptlsdeemayDKGLREGITLIGEIVNKPAQAKALIEATDQGRKIVSDRLKDIP 201
Cdd:cd00636 77 DKLSKIAIPVVVVDEASELS-----------------LENIKESIRLIGKALGKEENAEELIAELDARLAELRAKLAKIP 139
|
....
gi 1240938646 202 ADKR 205
Cdd:cd00636 140 KKKV 143
|
|
| BtuF |
cd01144 |
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ... |
42-291 |
7.88e-15 |
|
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: 73.10 E-value: 7.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 42 RIVVLQHQTLNLLEQMNATDKIVGVmtnwkqqlgDGYARLAPELNHMATLGDLTHVDPEKLVALHPQVVfITNYA--PHE 119
Cdd:cd01144 2 RIVSLAPSATELLYALGLGDQLVGV---------TDYCDYPPEAKKLPRVGGFYQLDLERVLALKPDLV-IAWDDcnVCA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 120 MIDSITALGIPVVaislrhdlpgeqdkMNPTLSDEEMAYDkglregITLIGEIVNKPAQAKALIEATdqgRKIVSDRLKD 199
Cdd:cd01144 72 VVDQLRAAGIPVL--------------VSEPQTLDDILAD------IRRLGTLAGRPARAEELAEAL---RRRLAALRKQ 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 200 IPADKRIRAYM---ANPqLTTYGSGKYTGLMMQhAGAVNVAAATVKGFKTVSMEQVIAWDPQVIFVQDRYPSVVNEI-NS 275
Cdd:cd01144 129 YASKPPPRVFYqewIDP-LMTAGGDWVPELIAL-AGGVNVFADAGERSPQVSWEDVLAANPDVIVLSPCGFGFTPAIlRK 206
|
250
....*....|....*.
gi 1240938646 276 SPQWQAIDAVKNHRVY 291
Cdd:cd01144 207 EPAWQALPAVRNGRVY 222
|
|
| TroA_a |
cd01148 |
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ... |
41-301 |
3.03e-14 |
|
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: 71.99 E-value: 3.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 41 DRIVVLQHQTLNLLEQMNATDKIVGVmTNWkqqlgdgYARLAPEL-NHMATLGDLTHVDP--EKLVALHPQVVFI-TNYA 116
Cdd:cd01148 19 QRVVSNDQNTTEMMLALGLQDRMVGT-AGI-------DNKDLPELkAKYDKVPELAKKYPskETVLAARPDLVFGgWSYG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 117 PHE----MIDSITALGIPVvaislrHDLP--GEQDKMNPTLSDeemaydkgLREGITLIGEIVNKPAQAKALIEATDqgr 190
Cdd:cd01148 91 FDKgglgTPDSLAELGIKT------YILPesCGQRRGEATLDD--------VYNDIRNLGKIFDVEDRADKLVADLK--- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 191 kivsDRLKDIPA-----DKRIRAYMANP-QLTTYGSGKYT--GLMMQHAGAVNVAAATVKGFKTVSMEQVIAWDPQVIFV 262
Cdd:cd01148 154 ----ARLAEISAkvkgdGKKVAVFVYDSgEDKPFTSGRGGipNAIITAAGGRNVFADVDESWTTVSWETVIARNPDVIVI 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1240938646 263 QDrYPSV------VNEINSSPQWQAIDAVKNHRVYLMPdYAKAWG 301
Cdd:cd01148 230 ID-YGDQnaaeqkIKFLKENPALKNVPAVKNNRFIVLP-LAEATP 272
|
|
| FatB |
cd01140 |
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ... |
33-301 |
6.38e-14 |
|
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: 70.75 E-value: 6.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 33 QVSIPDHVDRIVVLQHQTLNLLEQMNAtdKIVGVMTnwKQQLGDGYARLAPElnHMATLGDLTHVDPEKLVALHPQVVFI 112
Cdd:cd01140 5 ETKVPKNPEKVVVFDVGALDTLDALGV--KVVGVPK--SSTLPEYLKKYKDD--KYANVGTLFEPDLEAIAALKPDLIII 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 113 TNYApHEMIDSI-TALGIPVVAISLRHdlpgeqdkmnptlsdeemaYDKGLREGITLIGEIVNKPAQAKALIEATDQgrK 191
Cdd:cd01140 79 GGRL-AEKYDELkKIAPTIDLGADLKN-------------------YLESVKQNIETLGKIFGKEEEAKELVAEIDA--S 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 192 IvsDRLKDI-PADKRIRAYMAN-PQLTTYGSGKYTGLMMQHAGAVNVA---AATVKGfKTVSMEQVIAWDPQVIFVQDR- 265
Cdd:cd01140 137 I--AEAKSAaKGKKKALVVLVNgGKLSAFGPGSRFGWLHDLLGFEPADeniKASSHG-QPVSFEYILEANPDWLFVIDRg 213
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1240938646 266 -----YPSVVNEINSSPQWQAIDAVKNHRVYLMPdyAKAWG 301
Cdd:cd01140 214 aaigaEGSSAKEVLDNDLVKNTTAWKNGKVIYLD--PDLWY 252
|
|
| FeuA |
cd01138 |
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ... |
34-305 |
9.88e-13 |
|
Periplasmic binding protein FeuA. These proteins have predicted to function as initial receptors in ABC transport of metal ions in some eubacterial species. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.
Pssm-ID: 238558 [Multi-domain] Cd Length: 248 Bit Score: 66.97 E-value: 9.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 34 VSIPDHVDRIVVLQHQTLNLLeqmnATD-KIVGVMTnwkqqlgdgYARLAPELNHMATLGDLTHVDP---EKLVALHPQV 109
Cdd:cd01138 3 VEIPAKPKRIVALSGETEGLA----LLGiKPVGAAS---------IGGKNPYYKKKTLAKVVGIVDEpnlEKVLELKPDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 110 VFITNYaphemidsitalgipvvaislrhdLPGEQDKMN---PT--LSDEEMAYDKGLREgitlIGEIVNKPAQAKALIE 184
Cdd:cd01138 70 IIVSSK------------------------QEENYEKLSkiaPTvpVSYNSSDWEEQLKE----IGKLLNKEDEAEKWLA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 185 ATDQGRKIVSDRLKD-IPADKRIRAYMANPQLTTYGSGK-------YTGLMMQHAGAVNVAAATvKGFKTVSMEQVIAWD 256
Cdd:cd01138 122 DYKQKAKEAKEKIKKkLGNDKSVAVLRGRKQIYVFGEDGrgggpilYADLGLKAPEKVKEIEDK-PGYAAISLEVLPEFD 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1240938646 257 PQVIFVQ-DRYPSVVNEINSSPQWQAIDAVKNHRVYLMpdyaKAWGYPMP 305
Cdd:cd01138 201 ADYIFLLfFTGPEAKADFESLPIWKNLPAVKNNHVYIV----DAWVFYFA 246
|
|
| btuF |
PRK09534 |
corrinoid ABC transporter substrate-binding protein; Reviewed |
27-272 |
3.03e-12 |
|
corrinoid ABC transporter substrate-binding protein; Reviewed
Pssm-ID: 236552 [Multi-domain] Cd Length: 359 Bit Score: 66.86 E-value: 3.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 27 TDQIGRQVSIPDHVDRIVVLQHQTLNLLEQMNATDKIVGVmTNWKQQLgDGyarlAPELNHMATLGDLThVDPEKLVALH 106
Cdd:PRK09534 47 TDATGTEITLDERPERVVTLNPSAAQTMWELGARDRVVGV-TQYASYL-DG----AEERTNVSGGQPFG-VNVEAVVGLD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 107 PQVVFITNYAPHEMIDSITALGIPVVaislrhdlpgeQDKMNPTLSDeemaydkgLREGITLIGEIVNKPAQAKALIEAT 186
Cdd:PRK09534 120 PDLVLAPNAVAGDTVTRLREAGITVF-----------HFPAATSIED--------VAEKTATIGRLTGNCEAAAETNAEM 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 187 DQGRKIVSDRLKDIpaDKRIRAYMANPQLTTYGSGKYTGLMMQHAGAVNVAA-ATVKGFKTVSMEQVIAWDPQVIFVQDR 265
Cdd:PRK09534 181 RDRVDAVEDRTADV--DDRPRVLYPLGDGYTAGGNTFIGALIEAAGGHNVAAdATTDGYPQLSEEVIVQQDPDVIVVATA 258
|
....*..
gi 1240938646 266 YPSVVNE 272
Cdd:PRK09534 259 SALVAET 265
|
|
| fecB |
PRK11411 |
iron-dicitrate transporter substrate-binding subunit; Provisional |
19-290 |
2.09e-11 |
|
iron-dicitrate transporter substrate-binding subunit; Provisional
Pssm-ID: 183123 [Multi-domain] Cd Length: 303 Bit Score: 63.92 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 19 SSQAS-RQITDQIGrQVSIPDHVDRIVVLQHQTLNLLEQMNATDkiVGVMTnwkqqlgDGYA-RLAPELNhmatlgdlTH 96
Cdd:PRK11411 18 SSHAFaVTVQDEQG-TFTLEKTPQRIVVLELSFVDALAAVGVSP--VGVAD-------DNDAkRILPEVR--------AH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 97 VDPEKLVALHPQvvfitnyaPHemIDSITALGiP--VVAISLRHD-LPGEQDKMNPTL---SDEEmAYDKGLrEGITLIG 170
Cdd:PRK11411 80 LKPWQSVGTRSQ--------PS--LEAIAALK-PdlIIADSSRHAgVYIALQKIAPTLllkSRNE-TYQENL-QSAAIIG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 171 EIVNKPAQAKALIEatdQGRKIVSDRLKDIPADKRIR-AYMANPQLTTYGSGKYTGLMMQHAG-AVNVAAATVKGFKTVS 248
Cdd:PRK11411 147 EVLGKKREMQARIE---QHKERMAQFASQLPKGTRVAfGTSREQQFNLHSPESYTGSVLAALGlNVPKAPMNGAAMPSIS 223
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1240938646 249 MEQVIAWDPQVIFVQD-RYPSVVNEINSSPQWQAIDAVKNHRV 290
Cdd:PRK11411 224 LEQLLALNPDWLLVAHyRQESIVKRWQQDPLWQMLTAAKKQQV 266
|
|
| IsdE |
TIGR03659 |
heme ABC transporter, heme-binding protein isdE; This family of ABC substrate-binding proteins ... |
160-291 |
4.84e-08 |
|
heme ABC transporter, heme-binding protein isdE; This family of ABC substrate-binding proteins is observed primarily in close proximity with proteins localized to the cell wall and bearing the NEAT (NEAr Transporter, pfam05031) heme-binding domain. IsdE has been shown to bind heme and is involved in the process of scavenging heme for the purpose of obtaining iron.
Pssm-ID: 274706 [Multi-domain] Cd Length: 289 Bit Score: 53.43 E-value: 4.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 160 KGLREGITLIGEIVNKPAQAKALIEATDQGRKIVsdrLKDIPADKRIR---------AYManpqLTTYGSgkYTGLMMQH 230
Cdd:TIGR03659 125 DGMKKSITELGEKYGREEQAEKLVKEINEKEAEV---KKKVKGKKKPKvlilmgvpgSYL----VATENS--YIGDLVKL 195
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1240938646 231 AGAVNVAAATVKGFKTVSMEQVIAWDPQVIFVQDR-YPSVV-----NEINSSPQWQAIDAVKNHRVY 291
Cdd:TIGR03659 196 AGGENVYKGNKQEYLSSNTEYLLKANPDIILRAAHgMPDEVkkmfdEEFKTNDIWKHFEAVKNNRVY 262
|
|
| TroA_d |
cd01141 |
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ... |
33-181 |
1.93e-07 |
|
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial receptors in the ABC metal ion uptake in eubacteria and archaea. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.
Pssm-ID: 238561 [Multi-domain] Cd Length: 186 Bit Score: 50.50 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 33 QVSIPDHVDRIVVLQHQTLNLLEQMNATDKIVGVmTNWKQQLGDgyarlaPELNHM--ATLGDLTHVDPEKLVALHPQVV 110
Cdd:cd01141 1 AKTIKVPPKRIVVLSPTHVDLLLALDKADKIVGV-SASAYDLNT------PAVKERidIQVGPTGSLNVELIVALKPDLV 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1240938646 111 FITNYA-PHEMIDSITALGIPVVAIslrhdlpgeQDKMNPTlsdeemaydkGLREGITLIGEIVNKPAQAKA 181
Cdd:cd01141 74 ILYGGFqAQTILDKLEQLGIPVLYV---------NEYPSPL----------GRAEWIKFAAAFYGVGKEDKA 126
|
|
| PRK14048 |
PRK14048 |
ferrichrome/ferrioxamine B periplasmic transporter; Provisional |
26-347 |
5.87e-04 |
|
ferrichrome/ferrioxamine B periplasmic transporter; Provisional
Pssm-ID: 172540 [Multi-domain] Cd Length: 374 Bit Score: 41.42 E-value: 5.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 26 ITDQIGRQVSIPDHVDriVVLQHQTLNLLEQMNATDKIVGVMTNWKQQL-GD------GYARLAPELNHMATL--GDLTH 96
Cdd:PRK14048 34 VTDAVGREVTIPAPPK--AVLLGSGFNLIALSLIHPDPVSLLAGWSGDMkGDnpeiyeSFLRKFPELADVPLIddGSGPG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 97 VDPEKLVALHPQVVFITNY-----APHEMIDSITALGIPVVAISLRHD-LPGEQDKMNptlsdeemaydkglregitLIG 170
Cdd:PRK14048 112 LSFETILTLKADLAILANWqadteAGQRAIEYLESIGVPVIVVDFNNEaLKNTPDNMR-------------------LLG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 171 EIVNKPAQAKALIEATDQGRKIVSDRLKDIP-ADKRI--RAYMANPQLT-TYGSGKyTGLMMQHAGAVNVAA-ATVKGFK 245
Cdd:PRK14048 173 KVFEREEQAEDFARFYEERLARIRDRVAKHSePGPTVlmEAFPAADRCCwAYGRGG-LGEFIALTGSRNIAEgALPRPGG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240938646 246 TVSMEQVIAWDPQVIFVQD----RY------PSV--------VNEINSSPQWQAIDAVKNHRVYLMPDYAKAwgypMPEA 307
Cdd:PRK14048 252 MMNAEAIMAENPDVYIATSspggKYsgfsigPGVsaeeaettLANVVDKPVMASIAAVRDGRVHGLWNFFNA----VPLN 327
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1240938646 308 MGLGELWmAKKLYPQKFQDVDMNKLANRWYQRFYRTTYQG 347
Cdd:PRK14048 328 IVAAEAF-ASWLRPELFADIDPAATLAEINRRFAAVPFEG 366
|
|
| |
