|
Name |
Accession |
Description |
Interval |
E-value |
| TroA_f |
cd01139 |
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ... |
28-360 |
5.96e-102 |
|
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: 304.62 E-value: 5.96e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 28 LTVTDFDGRSVTIQQEPQRIILQDGRDIMAMALLDRDNPFQRLVAWNNLAKKQDTATWDMLKGKWPQSVGILDMGFSDKG 107
Cdd:cd01139 1 ITVTDVAGRKVTLDAPVERVLLGEGRQLYALALLEGENPFARIVGWGGDLKKGDPDTYAKYKEKFPEIADIPLIGSTYNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 108 NVDLESVLSKQPDLMIAQLRAKAALKESGVIDKLSALNIPVLFVDYEVNPAKDTAPSIDLLGKVLNREANAKAYTDFYRQ 187
Cdd:cd01139 81 DFSVEKVLTLKPDLVILNIWAKTTAEESGILEKLEQAGIPVVFVDFRQKPLKNTTPSMRLLGKALGREERAEEFIEFYQE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 188 HFDAIQQKTAAIT-PKPSVFVEPIAGNSDSCCFTHSNSGWGGLVEAVGAKNIGSDLLPGATGFVSLEKIISMKPDVYIMT 266
Cdd:cd01139 161 RIDRIRDRLAKINePKPKVFIELGAGGPEECCSTYGNGNWGELVDAAGGDNIADGLIPGTSGELNAEYVIAANPEIIIAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 267 GS----KRGNSQVLPLGYGAsvEDVRNQANVLLSRTGISQIPAVQAKHVYGVYHHFYNHPYNIVGMEYLAKDIYPQALTS 342
Cdd:cd01139 241 GGnwakDPSGVSLGPDGTTA--DAKESLLRALLKRPGWSSLQAVKNGRVYALWHQFYRSPYNFVALEAFAKWLYPELFKD 318
|
330
....*....|....*...
gi 1373058621 343 LNPDDTYHHIIQNFTSLP 360
Cdd:cd01139 319 LDPEATLQEFHRQFLPVD 336
|
|
| PRK14048 |
PRK14048 |
ferrichrome/ferrioxamine B periplasmic transporter; Provisional |
3-360 |
5.14e-53 |
|
ferrichrome/ferrioxamine B periplasmic transporter; Provisional
Pssm-ID: 172540 [Multi-domain] Cd Length: 374 Bit Score: 179.71 E-value: 5.14e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 3 RKSVRSLFLTALLSAPLFSYA-TQYPLTVTDFDGRSVTIQQEPQRIILQDGRDIMAMALLDRDnPFQRLVAWNNLAKKQD 81
Cdd:PRK14048 6 RSLVRLVAFLAIAFLALSALAeVQWPMTVTDAVGREVTIPAPPKAVLLGSGFNLIALSLIHPD-PVSLLAGWSGDMKGDN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 82 TATWDMLKGKWPQ--SVGILDMGfsDKGNVDLESVLSKQPDLMIaqLRAKAALKESGV--IDKLSALNIPVLFVDYEVNP 157
Cdd:PRK14048 85 PEIYESFLRKFPElaDVPLIDDG--SGPGLSFETILTLKADLAI--LANWQADTEAGQraIEYLESIGVPVIVVDFNNEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 158 AKDTAPSIDLLGKVLNREANAKAYTDFYRQHFDAIQQKTAAIT-PKPSVFVEPIAgNSDSCCFTHSNSGWGGLVEAVGAK 236
Cdd:PRK14048 161 LKNTPDNMRLLGKVFEREEQAEDFARFYEERLARIRDRVAKHSePGPTVLMEAFP-AADRCCWAYGRGGLGEFIALTGSR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 237 NIGSDLLPGATGFVSLEKIISMKPDVYIMTGSKRGNSQVLPLGYGASVEDVRNQANVLLSRTGISQIPAVQAKHVYGVYH 316
Cdd:PRK14048 240 NIAEGALPRPGGMMNAEAIMAENPDVYIATSSPGGKYSGFSIGPGVSAEEAETTLANVVDKPVMASIAAVRDGRVHGLWN 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1373058621 317 HFYNHPYNIVGMEYLAKDIYPQALTSLNPDDTYHHIIQNFTSLP 360
Cdd:PRK14048 320 FFNAVPLNIVAAEAFASWLRPELFADIDPAATLAEINRRFAAVP 363
|
|
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
46-340 |
4.65e-52 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 174.03 E-value: 4.65e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 46 RIILQDGRDIMAMALLDRDNpfqRLVAWnnlakkqdtATWDMLKGKWPQSVGILDMGFSDkgNVDLESVLSKQPDLMIAQ 125
Cdd:COG0614 2 RIVSLSPSATELLLALGAGD---RLVGV---------SDWGYCDYPELELKDLPVVGGTG--EPNLEAILALKPDLVLAS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 126 lrakAALKESGVIDKLSALNIPVLFVDYevNPAKDTAPSIDLLGKVLNREANAKAYTDFYRQHFDAIQQKTAAITPKPSV 205
Cdd:COG0614 68 ----SSGNDEEDYEQLEKIGIPVVVLDP--RSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGAEERPTV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 206 FVEPIAGnsDSCCFTHSNSGWGGLVEAVGAKNIGSDlLPGATGFVSLEKIISMKPDVYIMTgskrgnsqvlplGYGASVE 285
Cdd:COG0614 142 LYEIWSG--DPLYTAGGGSFIGELLELAGGRNVAAD-LGGGYPEVSLEQVLALDPDVIILS------------GGGYDAE 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1373058621 286 DVRNQANVLLSRTGISQIPAVQAKHVYGVYHHF--YNHPYNIVGMEYLAKDIYPQAL 340
Cdd:COG0614 207 TAEEALEALLADPGWQSLPAVKNGRVYVVPGDLlsRPGPRLLLALEDLAKALHPELF 263
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
72-313 |
1.07e-18 |
|
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: 83.96 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 72 AWNNLAKKqDTATWDMLKGKWPQSVgildMGFSDKGNVDLESVLSKQPDLMIAQLRAKAALkesgvIDKLSALNIPVLFV 151
Cdd:pfam01497 16 ATDSIVGV-DAYTRDPLKADAVAAI----VKVGAYGEINVERLAALKPDLVILSTGYLTDE-----AEELLSLIIPTVIF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 152 --DYEVNPAKDTapsIDLLGKVLNREANAKAYTDFYRQHFDAIQQKTAAITPKP-SVFvepIAGNSDSCCFTHSNSGWGG 228
Cdd:pfam01497 86 esSSTGESLKEQ---IKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPvLVF---GGADGGGYVVAGSNTYIGD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 229 LVEAVGAKNIGSDLLPGATGFVSLEKIISMKPDVYIMTGSKRGNSQVlplgygasvedvrnqANVLLSRTGISQIPAVQA 308
Cdd:pfam01497 160 LLRILGIENIAAELSGSEYAPISFEAILSSNPDVIIVSGRDSFTKTG---------------PEFVAANPLWAGLPAVKN 224
|
....*
gi 1373058621 309 KHVYG 313
Cdd:pfam01497 225 GRVYT 229
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| TroA_f |
cd01139 |
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ... |
28-360 |
5.96e-102 |
|
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: 304.62 E-value: 5.96e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 28 LTVTDFDGRSVTIQQEPQRIILQDGRDIMAMALLDRDNPFQRLVAWNNLAKKQDTATWDMLKGKWPQSVGILDMGFSDKG 107
Cdd:cd01139 1 ITVTDVAGRKVTLDAPVERVLLGEGRQLYALALLEGENPFARIVGWGGDLKKGDPDTYAKYKEKFPEIADIPLIGSTYNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 108 NVDLESVLSKQPDLMIAQLRAKAALKESGVIDKLSALNIPVLFVDYEVNPAKDTAPSIDLLGKVLNREANAKAYTDFYRQ 187
Cdd:cd01139 81 DFSVEKVLTLKPDLVILNIWAKTTAEESGILEKLEQAGIPVVFVDFRQKPLKNTTPSMRLLGKALGREERAEEFIEFYQE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 188 HFDAIQQKTAAIT-PKPSVFVEPIAGNSDSCCFTHSNSGWGGLVEAVGAKNIGSDLLPGATGFVSLEKIISMKPDVYIMT 266
Cdd:cd01139 161 RIDRIRDRLAKINePKPKVFIELGAGGPEECCSTYGNGNWGELVDAAGGDNIADGLIPGTSGELNAEYVIAANPEIIIAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 267 GS----KRGNSQVLPLGYGAsvEDVRNQANVLLSRTGISQIPAVQAKHVYGVYHHFYNHPYNIVGMEYLAKDIYPQALTS 342
Cdd:cd01139 241 GGnwakDPSGVSLGPDGTTA--DAKESLLRALLKRPGWSSLQAVKNGRVYALWHQFYRSPYNFVALEAFAKWLYPELFKD 318
|
330
....*....|....*...
gi 1373058621 343 LNPDDTYHHIIQNFTSLP 360
Cdd:cd01139 319 LDPEATLQEFHRQFLPVD 336
|
|
| PRK14048 |
PRK14048 |
ferrichrome/ferrioxamine B periplasmic transporter; Provisional |
3-360 |
5.14e-53 |
|
ferrichrome/ferrioxamine B periplasmic transporter; Provisional
Pssm-ID: 172540 [Multi-domain] Cd Length: 374 Bit Score: 179.71 E-value: 5.14e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 3 RKSVRSLFLTALLSAPLFSYA-TQYPLTVTDFDGRSVTIQQEPQRIILQDGRDIMAMALLDRDnPFQRLVAWNNLAKKQD 81
Cdd:PRK14048 6 RSLVRLVAFLAIAFLALSALAeVQWPMTVTDAVGREVTIPAPPKAVLLGSGFNLIALSLIHPD-PVSLLAGWSGDMKGDN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 82 TATWDMLKGKWPQ--SVGILDMGfsDKGNVDLESVLSKQPDLMIaqLRAKAALKESGV--IDKLSALNIPVLFVDYEVNP 157
Cdd:PRK14048 85 PEIYESFLRKFPElaDVPLIDDG--SGPGLSFETILTLKADLAI--LANWQADTEAGQraIEYLESIGVPVIVVDFNNEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 158 AKDTAPSIDLLGKVLNREANAKAYTDFYRQHFDAIQQKTAAIT-PKPSVFVEPIAgNSDSCCFTHSNSGWGGLVEAVGAK 236
Cdd:PRK14048 161 LKNTPDNMRLLGKVFEREEQAEDFARFYEERLARIRDRVAKHSePGPTVLMEAFP-AADRCCWAYGRGGLGEFIALTGSR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 237 NIGSDLLPGATGFVSLEKIISMKPDVYIMTGSKRGNSQVLPLGYGASVEDVRNQANVLLSRTGISQIPAVQAKHVYGVYH 316
Cdd:PRK14048 240 NIAEGALPRPGGMMNAEAIMAENPDVYIATSSPGGKYSGFSIGPGVSAEEAETTLANVVDKPVMASIAAVRDGRVHGLWN 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1373058621 317 HFYNHPYNIVGMEYLAKDIYPQALTSLNPDDTYHHIIQNFTSLP 360
Cdd:PRK14048 320 FFNAVPLNIVAAEAFASWLRPELFADIDPAATLAEINRRFAAVP 363
|
|
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
46-340 |
4.65e-52 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 174.03 E-value: 4.65e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 46 RIILQDGRDIMAMALLDRDNpfqRLVAWnnlakkqdtATWDMLKGKWPQSVGILDMGFSDkgNVDLESVLSKQPDLMIAQ 125
Cdd:COG0614 2 RIVSLSPSATELLLALGAGD---RLVGV---------SDWGYCDYPELELKDLPVVGGTG--EPNLEAILALKPDLVLAS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 126 lrakAALKESGVIDKLSALNIPVLFVDYevNPAKDTAPSIDLLGKVLNREANAKAYTDFYRQHFDAIQQKTAAITPKPSV 205
Cdd:COG0614 68 ----SSGNDEEDYEQLEKIGIPVVVLDP--RSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGAEERPTV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 206 FVEPIAGnsDSCCFTHSNSGWGGLVEAVGAKNIGSDlLPGATGFVSLEKIISMKPDVYIMTgskrgnsqvlplGYGASVE 285
Cdd:COG0614 142 LYEIWSG--DPLYTAGGGSFIGELLELAGGRNVAAD-LGGGYPEVSLEQVLALDPDVIILS------------GGGYDAE 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1373058621 286 DVRNQANVLLSRTGISQIPAVQAKHVYGVYHHF--YNHPYNIVGMEYLAKDIYPQAL 340
Cdd:COG0614 207 TAEEALEALLADPGWQSLPAVKNGRVYVVPGDLlsRPGPRLLLALEDLAKALHPELF 263
|
|
| TroA_e |
cd01142 |
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ... |
23-345 |
1.46e-21 |
|
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: 93.19 E-value: 1.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 23 ATQYPLTVTDFDGRSVTIQQEPQRI-ILQDGRDIMAMALLDRDnpfqRLVAwNNLAKKQDTatwdMLKGKWPQSVGILDM 101
Cdd:cd01142 3 ATAATRTITDMAGRKVTIPDEVKRIaALWGAGNAVVAALGGGK----LIVA-TTSTVQQEP----WLYRLAPSLENVATG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 102 GFSDKGNVdlESVLSKQPDLMIAqlrAKAALKESG--VIDKLSALNIPVLFVDyevnpakDTAPSIDLLGKVLNREANAK 179
Cdd:cd01142 74 GTGNDVNI--EELLALKPDVVIV---WSTDGKEAGkaVLRLLNALSLRDAELE-------EVKLTIALLGELLGRQEKAE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 180 AYTDFYRQHFDAIQQKTAAI--TPKPSVFVEpiagNSDSCCFTHSNSGWGGLVEAVGAKNIGSDLLPGATGFVSLEKIIS 257
Cdd:cd01142 142 ALVAYFDDNLAYVAARTKKLpdSERPRVYYA----GPDPLTTDGTGSITNSWIDLAGGINVASEATKKGSGEVSLEQLLK 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 258 MKPDVYImtgskrgnsqvlpLGYGASVEDVRNQANvllsrtgISQIPAVQAKHVYGV-YHHFYNHPY---NIVGMEYLAK 333
Cdd:cd01142 218 WNPDVII-------------VGNADTKAAILADPR-------WQNLRAVKNGRVYVNpEGAFWWDRPsaeEALLGLWLAK 277
|
330
....*....|..
gi 1373058621 334 DIYPQALTSLNP 345
Cdd:cd01142 278 TLYPERFTDDDM 289
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
72-313 |
1.07e-18 |
|
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: 83.96 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 72 AWNNLAKKqDTATWDMLKGKWPQSVgildMGFSDKGNVDLESVLSKQPDLMIAQLRAKAALkesgvIDKLSALNIPVLFV 151
Cdd:pfam01497 16 ATDSIVGV-DAYTRDPLKADAVAAI----VKVGAYGEINVERLAALKPDLVILSTGYLTDE-----AEELLSLIIPTVIF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 152 --DYEVNPAKDTapsIDLLGKVLNREANAKAYTDFYRQHFDAIQQKTAAITPKP-SVFvepIAGNSDSCCFTHSNSGWGG 228
Cdd:pfam01497 86 esSSTGESLKEQ---IKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPvLVF---GGADGGGYVVAGSNTYIGD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 229 LVEAVGAKNIGSDLLPGATGFVSLEKIISMKPDVYIMTGSKRGNSQVlplgygasvedvrnqANVLLSRTGISQIPAVQA 308
Cdd:pfam01497 160 LLRILGIENIAAELSGSEYAPISFEAILSSNPDVIIVSGRDSFTKTG---------------PEFVAANPLWAGLPAVKN 224
|
....*
gi 1373058621 309 KHVYG 313
Cdd:pfam01497 225 GRVYT 229
|
|
| ChuT |
COG4558 |
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ... |
112-312 |
2.50e-18 |
|
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443619 [Multi-domain] Cd Length: 285 Bit Score: 84.09 E-value: 2.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 112 ESVLSKQPDLMIAqlrAKAALKESgVIDKLSALNIPVLFVDYEVNPAkDTAPSIDLLGKVLNREANAKAYTDFYRQHFDA 191
Cdd:COG4558 78 EGILSLKPTLVLA---SEGAGPPE-VLDQLRAAGVPVVVVPAAPSLE-GVLAKIRAVAAALGVPEAGEALAARLEADLAA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 192 IQQKTAAITPKPSV-FV------EP-IAGnsdsccfthSNSGWGGLVEAVGAKNIGSDLlpgaTGF--VSLEKIISMKPD 261
Cdd:COG4558 153 LAARVAAIGKPPRVlFLlsrgggRPmVAG---------RGTAADALIRLAGGVNAAAGF----EGYkpLSAEALIAAAPD 219
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1373058621 262 VYIMTgsKRGnsqvlplgyGASVEDVRNqanvLLSRTGISQIPAVQAKHVY 312
Cdd:COG4558 220 VILVM--TRG---------LESLGGVDG----LLALPGLAQTPAGKNKRIV 255
|
|
| TroA_a |
cd01148 |
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ... |
26-273 |
4.46e-18 |
|
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: 83.16 E-value: 4.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 26 YPLTVtDFDGRSVTIQQEPQRIILQDGR--DIM-AMALLDRdnpfqrlVAWNNLAKKQDTATWDMLKGKWPQSvgildmg 102
Cdd:cd01148 1 YPLTV-ENCGRSVTFDKAPQRVVSNDQNttEMMlALGLQDR-------MVGTAGIDNKDLPELKAKYDKVPEL------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 103 fsDKGNVDLESVLSKQPDLMIAQLRAKAALKESGVIDKLSALNIPVlFVDYEVNPAKDTAPSIDL-------LGKVLNRE 175
Cdd:cd01148 66 --AKKYPSKETVLAARPDLVFGGWSYGFDKGGLGTPDSLAELGIKT-YILPESCGQRRGEATLDDvyndirnLGKIFDVE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 176 ANAKAYTDFYRQHFDAIQQKTAAITPKPSVFVePIAGNSDSccFThsnSGWGG----LVEAVGAKNIGSDlLPGATGFVS 251
Cdd:cd01148 143 DRADKLVADLKARLAEISAKVKGDGKKVAVFV-YDSGEDKP--FT---SGRGGipnaIITAAGGRNVFAD-VDESWTTVS 215
|
250 260
....*....|....*....|..
gi 1373058621 252 LEKIISMKPDVYIMTGSKRGNS 273
Cdd:cd01148 216 WETVIARNPDVIVIIDYGDQNA 237
|
|
| HemV-2 |
cd01147 |
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ... |
107-312 |
6.53e-18 |
|
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: 82.38 E-value: 6.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 107 GNVDLESVLSKQPDLMIAQLrakaALKESGVIDKLSA-LNIPVLFVDYEVNPaKDTAPSIDLLGKVLNREANAKAYTDFY 185
Cdd:cd01147 63 NTPNYEKIAALKPDVVIDVG----SDDPTSIADDLQKkTGIPVVVLDGGDSL-EDTPEQIRLLGKVLGKEERAEELISFI 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 186 RQHFDAIQQKTAAI--TPKPSVFVEPIagnsdsccfthSNSGWGGL----------VEAVGAKNIGSDLLPGATGFVSLE 253
Cdd:cd01147 138 ESILADVEERTKDIpdEEKPTVYFGRI-----------GTKGAAGLesglagsievFELAGGINVADGLGGGGLKEVSPE 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1373058621 254 KIISMKPDVyIMTGSKrgnsqvlplGYGASVEDvrnqanVLLSRTGISQIPAVQAKHVY 312
Cdd:cd01147 207 QILLWNPDV-IFLDTG---------SFYLSLEG------YAKNRPFWQSLKAVKNGRVY 249
|
|
| BtuF |
cd01144 |
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ... |
107-314 |
2.93e-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: 74.64 E-value: 2.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 107 GNVDLESVLSKQPDLMIAQLRAKAALkesgVIDKLSALNIPVLFVdyEVNPAKDTAPSIDLLGKVLNREANAKAYTDFYR 186
Cdd:cd01144 46 YQLDLERVLALKPDLVIAWDDCNVCA----VVDQLRAAGIPVLVS--EPQTLDDILADIRRLGTLAGRPARAEELAEALR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 187 QHFDAIQQKTAAITPkPSVFVE----PIagnsdsccFThSNSGW-GGLVEAVGAKNIGSDlLPGATGFVSLEKIISMKPD 261
Cdd:cd01144 120 RRLAALRKQYASKPP-PRVFYQewidPL--------MT-AGGDWvPELIALAGGVNVFAD-AGERSPQVSWEDVLAANPD 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1373058621 262 VYImtgskrgnsqVLPLGYGASVEDVRNqanvllsRTGISQIPAVQAKHVYGV 314
Cdd:cd01144 189 VIV----------LSPCGFGFTPAILRK-------EPAWQALPAVRNGRVYAV 224
|
|
| TroA-like |
cd00636 |
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ... |
45-207 |
1.99e-14 |
|
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: 69.90 E-value: 1.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 45 QRII-LQDGRDIMAMALLDRDNPfqrlVAWnnlakkQDTATWDMLKGKWPQSVGILDMGFsdkgNVDLESVLSKQPDLMI 123
Cdd:cd00636 1 KRVVaLDPGATELLLALGGDDKP----VGV------ADPSGYPPEAKALLEKVPDVGHGY----EPNLEKIAALKPDLII 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 124 AQLRAKAAlkesgVIDKLSALNIPVLFVDYEVNPAKDTAP-SIDLLGKVLNREANAKAYTDFYRQHFDAIQQKTAAITPK 202
Cdd:cd00636 67 ANGSGLEA-----WLDKLSKIAIPVVVVDEASELSLENIKeSIRLIGKALGKEENAEELIAELDARLAELRAKLAKIPKK 141
|
....*
gi 1373058621 203 PSVFV 207
Cdd:cd00636 142 KVSLV 146
|
|
| YvrC |
cd01143 |
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ... |
107-264 |
5.40e-14 |
|
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: 70.00 E-value: 5.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 107 GNVDLESVLSKQPDLMIAqlrAKAALKEsgVIDKLSALNIPVLFVDYEVNpAKDTAPSIDLLGKVLNREANAKAYTDFYR 186
Cdd:cd01143 49 SNPNVEKIVALKPDLVIV---SSSSLAE--LLEKLKDAGIPVVVLPAASS-LDEIYDQIELIGKITGAEEEAEKLVKEMK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 187 QHFDAIQQKTAAItPKPSVFVEPIAGNSdsccFTHSNSGW-GGLVEAVGAKNIGSDllpgATGF--VSLEKIISMKPDVY 263
Cdd:cd01143 123 QKIDKVKDKGKTI-KKSKVYIEVSLGGP----YTAGKNTFiNELIRLAGAKNIAAD----SGGWpqVSPEEILKANPDVI 193
|
.
gi 1373058621 264 I 264
Cdd:cd01143 194 I 194
|
|
| HutB |
cd01149 |
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ... |
112-314 |
6.65e-14 |
|
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: 70.37 E-value: 6.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 112 ESVLSKQPDLMIAQLRAKAALkesgVIDKLSALNIPVLFVDYEVNPAkDTAPSIDLLGKVLNREANAKAYTDFYRQHFDA 191
Cdd:cd01149 52 EGVLSLKPTLVIASDEAGPPE----ALDQLRAAGVPVVTVPSTPTLD-GLLTKIRQVAQALGVPEKGEALAQEVRQRLAA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 192 IQQKTAAITPKPSV-FV-------EPIAGnsdsccfthSNSGWGGLVEAVGAKNIGSDLlpgaTGF--VSLEKIISMKPD 261
Cdd:cd01149 127 LRKTVAAHKKPPRVlFLlshgggaAMAAG---------RNTAADAIIALAGAVNAAAGF----RGYkpLSAEALIAAQPD 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1373058621 262 VYIMTgsKRGnsqvlplgyGASVEDVRNqanvLLSRTGISQIPAVQAKHVYGV 314
Cdd:cd01149 194 VILVM--SRG---------LDAVGGVDG----LLKLPGLAQTPAGRNKRILAM 231
|
|
| FhuD |
cd01146 |
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ... |
110-314 |
5.56e-13 |
|
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial receptors in ABC transport of Fe3+-siderophores in many eubacterial species. They belong to the TroA-like superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA-like protein is comprised of two globular subdomains connected by a long alpha helix and binds its specific ligands in the cleft between these domains.
Pssm-ID: 238566 [Multi-domain] Cd Length: 256 Bit Score: 68.08 E-value: 5.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 110 DLESVLSKQPDLMIA-QLRAKAalkesgVIDKLSAlnI-PVLFVDYeVNPAKDTAPSIDLLGKVLNREANAKAYTDFYRQ 187
Cdd:cd01146 57 NLEAIAALKPDLILGsASRHDE------IYDQLSQ--IaPTVLLDS-SPWLAEWKENLRLIAKALGKEEEAEKLLAEYDQ 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 188 HFDAIQQKTAAITPKPSVFVEPIAGNSDSccFTHSNSGWGGLVEAVGAKNIGSDLLPGATGF--VSLEKIISMKPDV-YI 264
Cdd:cd01146 128 RLAELRQKLPDKGPKPVSVVRFSDAGSIR--LYGPNSFAGSVLEDLGLQNPWAQETTNDSGFatISLERLAKADADVlFV 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1373058621 265 MTGSKRGNSQVLplgygasvedvrnQANVLLsrtgiSQIPAVQAKHVYGV 314
Cdd:cd01146 206 FTYEDEELAQAL-------------QANPLW-----QNLPAVKNGRVYVV 237
|
|
| FecB |
COG4594 |
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ... |
1-344 |
3.87e-12 |
|
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443650 [Multi-domain] Cd Length: 316 Bit Score: 66.48 E-value: 3.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 1 MLR-KSVRSLFLTALLSAPLFSYATQYPLTVTDFDGRSV-------TIQQEPQRIILQDGRDIMAMALLD-------RDN 65
Cdd:COG4594 1 MKKlLLLLILLLALLLLAACGSSSSDSSSSEAAAGARTVkhamgetTIPGTPKRVVVLEWSFADALLALGvtpvgiaDDN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 66 PFQRLVAWnnLAKKQDTatwdmlkgkwPQSVGIldmgfsdKGNVDLESVLSKQPDLMIA-QLRAKAalkesgVIDKLSAl 144
Cdd:COG4594 81 DYDRWVPY--LRDLIKG----------VTSVGT-------RSQPNLEAIAALKPDLIIAdKSRHEA------IYDQLSK- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 145 nI-PVLFVDYEVNPAKDTAPSIDLLGKVLNREANAKAYTDFYRQHFDAIQQKTAAITPKPSVFVepIAGNSDSCCFTHSN 223
Cdd:COG4594 135 -IaPTVLFKSRNGDYQENLESFKTIAKALGKEEEAEAVLADHDQRIAEAKAKLAAADKGKKVAV--GQFRADGLRLYTPN 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 224 SGWGGLVEAVGAKNIGSDLLPGATGF--VSLEKIISMKPDV-YIMTGSKRGNSQVLplgygasvedvrnQANVLLsrtgi 300
Cdd:COG4594 212 SFAGSVLAALGFENPPKQSKDNGYGYseVSLEQLPALDPDVlFIATYDDPSILKEW-------------KNNPLW----- 273
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1373058621 301 SQIPAVQAKHVYGVyhhfynhPYN-------IVGMEYLAKDIYpQALTSLN 344
Cdd:COG4594 274 KNLKAVKNGRVYEV-------DGDlwtrgrgPLAAELMADDLV-EILLKKK 316
|
|
| PRK10957 |
PRK10957 |
iron-enterobactin transporter periplasmic binding protein; Provisional |
3-314 |
6.54e-09 |
|
iron-enterobactin transporter periplasmic binding protein; Provisional
Pssm-ID: 236806 [Multi-domain] Cd Length: 317 Bit Score: 56.52 E-value: 6.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 3 RKSVRSLFLTALLSAPLFSYATQ---YPLTVTDFDGrSVTIQQEPQRII----------LQDGRDIMAMAL------LDR 63
Cdd:PRK10957 1 PLYRLALLLLGLLLSGIAAAQASaagWPRTVTDSRG-SVTLESKPQRIVstsvtltgtlLAIDAPVIASGAttpntrVAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 64 DNPFQRlvAWNNLAKKQDtatwdmlkgkwpqsVGILDMGfsdkgNVDLESVLSKQPDLMIAQLR-AKAALKEsgvIDKLS 142
Cdd:PRK10957 80 DQGFFR--QWSDVAKERG--------------VEVLYIG-----EPDAEAVAAQMPDLIVISATgGDSALAL---YDQLS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 143 ALnIPVLFVDYEVNPAKDTApsiDLLGKVLNREANAKAYTdfyrQHFDA-IQQKTAAITPKP---SVFVEPIAGNSDScC 218
Cdd:PRK10957 136 AI-APTLVIDYDDKSWQELA---TQLGEATGLEKQAAAVI----AQFDAqLAEVKAKITLPPqpvSALVYNGAGHSAN-L 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 219 FTHsNSGWGGLVEAVGAKNigSDLLPGATGFVSLEKiismKPDVYIMTGSK-----RGNSQVLPLGYGASVEDVrnQANV 293
Cdd:PRK10957 207 WTP-ESAQGQLLEQLGFTL--AELPAGLQASTSQGK----RHDIIQLGGENlaaglNGETLFLFAGDDKDADAF--LADP 277
|
330 340
....*....|....*....|.
gi 1373058621 294 LLsrtgiSQIPAVQAKHVYGV 314
Cdd:PRK10957 278 LL-----ANLPAVQNKQVYAL 293
|
|
| FatB |
cd01140 |
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ... |
37-312 |
4.66e-08 |
|
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: 53.80 E-value: 4.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 37 SVTIQQEPQRIILQDgrdimaMALLDRdnpfqrLVAWN----NLAKKQDT-ATWDMLKGKWPQSVGILDmgfsdkgNVDL 111
Cdd:cd01140 5 ETKVPKNPEKVVVFD------VGALDT------LDALGvkvvGVPKSSTLpEYLKKYKDDKYANVGTLF-------EPDL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 112 ESVLSKQPDLMIAQLRAKAALKEsgvidKLSALNIPVLFVDYEvNPAKDTAPSIDLLGKVLNREANAKAYTDFYRQHFDA 191
Cdd:cd01140 66 EAIAALKPDLIIIGGRLAEKYDE-----LKKIAPTIDLGADLK-NYLESVKQNIETLGKIFGKEEEAKELVAEIDASIAE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 192 IQQKTAAitpKPSVFVEPIAGNSDScCFThSNSGWGGLVEAVGAKNIGSDLLPGATGF-VSLEKIISMKPDVyimtgskr 270
Cdd:cd01140 140 AKSAAKG---KKKALVVLVNGGKLS-AFG-PGSRFGWLHDLLGFEPADENIKASSHGQpVSFEYILEANPDW-------- 206
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1373058621 271 gnsqVLPLGYGASVEDVRNQANVLLSRTGISQIPAVQAKHVY 312
Cdd:cd01140 207 ----LFVIDRGAAIGAEGSSAKEVLDNDLVKNTTAWKNGKVI 244
|
|
| btuF |
PRK09534 |
corrinoid ABC transporter substrate-binding protein; Reviewed |
23-266 |
5.26e-08 |
|
corrinoid ABC transporter substrate-binding protein; Reviewed
Pssm-ID: 236552 [Multi-domain] Cd Length: 359 Bit Score: 54.14 E-value: 5.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 23 ATQYPLTVTDFDGRSVTIQQEPQRIILQDGRDIMAM-ALLDRDnpfqRLVAWNNLAKKQDTATWDMlkgkwpqsvgilDM 101
Cdd:PRK09534 39 ACSFPVTETDATGTEITLDERPERVVTLNPSAAQTMwELGARD----RVVGVTQYASYLDGAEERT------------NV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 102 GFSDKGNVDLESVLSKQPDLMIAQLRAK----AALKESGV-IDKLSAlnipvlfvdyeVNPAKDTAPSIDLLGKVLNREA 176
Cdd:PRK09534 103 SGGQPFGVNVEAVVGLDPDLVLAPNAVAgdtvTRLREAGItVFHFPA-----------ATSIEDVAEKTATIGRLTGNCE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 177 NAKAYTDFYRQHFDAIQQKTAAITPKPSVFVePIAGNsdsccFTH-SNSGWGGLVEAVGAKNIGSDllPGATGF--VSLE 253
Cdd:PRK09534 172 AAAETNAEMRDRVDAVEDRTADVDDRPRVLY-PLGDG-----YTAgGNTFIGALIEAAGGHNVAAD--ATTDGYpqLSEE 243
|
250
....*....|...
gi 1373058621 254 KIISMKPDVYIMT 266
Cdd:PRK09534 244 VIVQQDPDVIVVA 256
|
|
| fecB |
PRK11411 |
iron-dicitrate transporter substrate-binding subunit; Provisional |
2-314 |
7.76e-08 |
|
iron-dicitrate transporter substrate-binding subunit; Provisional
Pssm-ID: 183123 [Multi-domain] Cd Length: 303 Bit Score: 53.14 E-value: 7.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 2 LRKSVRSLFLTALLsapLFSYATQYPLTVTDFDGrSVTIQQEPQRIILQDGRDIMAMALLD-------RDNPFQRLVAwn 74
Cdd:PRK11411 1 MLAFIRLLFAGLLL---LSGSSHAFAVTVQDEQG-TFTLEKTPQRIVVLELSFVDALAAVGvspvgvaDDNDAKRILP-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 75 nlAKKQDTATWdmlkgkwpQSVGIldmgfsdKGNVDLESVLSKQPDLMIAQLRakaalKESGVIDKLSALnIPVLFV--- 151
Cdd:PRK11411 75 --EVRAHLKPW--------QSVGT-------RSQPSLEAIAALKPDLIIADSS-----RHAGVYIALQKI-APTLLLksr 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 152 --DYEVNpaKDTAPSIdllGKVLNREANAKAYTDFYRQHFDAIQQKTAAitPKPSVFvepiaGNSDSCCFT-HSNSGW-G 227
Cdd:PRK11411 132 neTYQEN--LQSAAII---GEVLGKKREMQARIEQHKERMAQFASQLPK--GTRVAF-----GTSREQQFNlHSPESYtG 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 228 GLVEAVGAKNIGSDLLPGATGFVSLEKIISMKPDvYIMTGSKRGNSQVlplgygasvedVRNQANVLLsrtgiSQIPAVQ 307
Cdd:PRK11411 200 SVLAALGLNVPKAPMNGAAMPSISLEQLLALNPD-WLLVAHYRQESIV-----------KRWQQDPLW-----QMLTAAK 262
|
....*..
gi 1373058621 308 AKHVYGV 314
Cdd:PRK11411 263 KQQVASV 269
|
|
| PRK03379 |
PRK03379 |
vitamin B12-transporter protein BtuF; Provisional |
109-269 |
2.60e-05 |
|
vitamin B12-transporter protein BtuF; Provisional
Pssm-ID: 179575 [Multi-domain] Cd Length: 260 Bit Score: 45.06 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 109 VDLESVLSKQPDLMIAqLRAKAALKEsgvIDKLSALNIPVLFVDyeVNPAKDTAPSIDLLGKVLNREANAKAYTDFYRQH 188
Cdd:PRK03379 63 MNLERIVALKPDLVLA-WRGGNAERQ---VDQLASLGIKVMWVD--ATSIEQIANALRQLAPWSPQPEKAEQAAQSLLQQ 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 189 FDAIQQKTAAITPKPsVFVE----PIagnsdsccFThsnSGWGGL----VEAVGAKNIGSD-LLPGATgfVSLEKIISMK 259
Cdd:PRK03379 137 YAALKAQYADKPKKR-VFLQfgtnPL--------FT---SGKHSIqsqvLSLCGGENIFADsRVPWPQ--VSREQVLARK 202
|
170
....*....|
gi 1373058621 260 PDVYIMTGSK 269
Cdd:PRK03379 203 PQAIVITGGP 212
|
|
| TroA_d |
cd01141 |
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ... |
93-210 |
4.65e-04 |
|
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: 40.87 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 93 PQSVGILDMGFSDKGNVDLESVLSKQPDLMIaqlrAKAALKESGVIDKLSALNIPVLFvdyeVNPAKDTAPSIDLLGKVL 172
Cdd:cd01141 44 PAVKERIDIQVGPTGSLNVELIVALKPDLVI----LYGGFQAQTILDKLEQLGIPVLY----VNEYPSPLGRAEWIKFAA 115
|
90 100 110
....*....|....*....|....*....|....*...
gi 1373058621 173 nREANAKAYtDFYRQHFDAIQQKTAAITPKPSVFVEPI 210
Cdd:cd01141 116 -AFYGVGKE-DKADEAFAQIAGRYRDLAKKVSNLNKPT 151
|
|
| FeuA |
cd01138 |
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ... |
38-312 |
4.75e-04 |
|
Periplasmic binding protein FeuA. These proteins have predicted to function as initial receptors in ABC transport of metal ions in some eubacterial species. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.
Pssm-ID: 238558 [Multi-domain] Cd Length: 248 Bit Score: 41.17 E-value: 4.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 38 VTIQQEPQRIILQDGRDiMAMALLDRdNPF-QRLVAWNNLAKKQDTatwdmlkgkwpqsvgiLDMGFSDKGNVDLESVLS 116
Cdd:cd01138 3 VEIPAKPKRIVALSGET-EGLALLGI-KPVgAASIGGKNPYYKKKT----------------LAKVVGIVDEPNLEKVLE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 117 KQPDLMIaqlrakAALKESGVIDKLSALNiPVLFVDYEvnpAKDTAPSIDLLGKVLNREANAKAYTDFYRQHFDAIQQKT 196
Cdd:cd01138 65 LKPDLII------VSSKQEENYEKLSKIA-PTVPVSYN---SSDWEEQLKEIGKLLNKEDEAEKWLADYKQKAKEAKEKI 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373058621 197 A-AITPKPSVFVepIAGNSDSCCFthsNSGWGGLVEAVGA-------KNIGSDLLPGATGFVSLEKIISMKPDvYIMTGS 268
Cdd:cd01138 135 KkKLGNDKSVAV--LRGRKQIYVF---GEDGRGGGPILYAdlglkapEKVKEIEDKPGYAAISLEVLPEFDAD-YIFLLF 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1373058621 269 KRGNSqvlplgygasvedvrnqANVLLSRTGISQ-IPAVQAKHVY 312
Cdd:cd01138 209 FTGPE-----------------AKADFESLPIWKnLPAVKNNHVY 236
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