|
Name |
Accession |
Description |
Interval |
E-value |
| TroA_f |
cd01139 |
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ... |
19-362 |
1.82e-141 |
|
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: 405.15 E-value: 1.82e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 19 KTVTDILGRQVTIPDNPQRIILGESRMLYTLALLQPDNPAKHVVGWPGDMARYDAQSWSRYIEKFPQLSQIPQLGNGSLQ 98
Cdd:cd01139 1 ITVTDVAGRKVTLDAPVERVLLGEGRQLYALALLEGENPFARIVGWGGDLKKGDPDTYAKYKEKFPEIADIPLIGSTYNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 99 AMNAEMLLPLKPDLVILPRLAKNAANEDLLQQTLTRAGIPFIYVDLRIDLLNNTLPSIHLLGEVLNQSSRATAFSNFYQQ 178
Cdd:cd01139 81 DFSVEKVLTLKPDLVILNIWAKTTAEESGILEKLEQAGIPVVFVDFRQKPLKNTTPSMRLLGKALGREERAEEFIEFYQE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 179 HMDVIRQRIAQYHGKKPTVMLHLHLGRRDTCCTTAVGGSLGDLLTFAGGENIASGTINSVYGELSPERVLAANPDVYIAT 258
Cdd:cd01139 161 RIDRIRDRLAKINEPKPKVFIELGAGGPEECCSTYGNGNWGELVDAAGGDNIADGLIPGTSGELNAEYVIAANPEIIIAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 259 GMAGPegKRFSSLMLGPLVNAEQAKESFDTLIRQEPILSHLRAVQTGHAWSMWHNFYLSPYHVVMVEMFAKALYPERFAD 338
Cdd:cd01139 241 GGNWA--KDPSGVSLGPDGTTADAKESLLRALLKRPGWSSLQAVKNGRVYALWHQFYRSPYNFVALEAFAKWLYPELFKD 318
|
330 340
....*....|....*....|....
gi 748795526 339 IDPQQTLQQLYQQFLPIEFSGIYW 362
Cdd:cd01139 319 LDPEATLQEFHRQFLPVDYSGTFW 342
|
|
| PRK14048 |
PRK14048 |
ferrichrome/ferrioxamine B periplasmic transporter; Provisional |
20-362 |
9.34e-68 |
|
ferrichrome/ferrioxamine B periplasmic transporter; Provisional
Pssm-ID: 172540 [Multi-domain] Cd Length: 374 Bit Score: 217.84 E-value: 9.34e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 20 TVTDILGRQVTIPDNPQRIILGESRMLYTLALLQPDnPAKHVVGWPGDMARYDAQSWSRYIEKFPQLSQIPQLGNGSLQA 99
Cdd:PRK14048 33 TVTDAVGREVTIPAPPKAVLLGSGFNLIALSLIHPD-PVSLLAGWSGDMKGDNPEIYESFLRKFPELADVPLIDDGSGPG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 100 MNAEMLLPLKPDLVILprlAKNAANEDLLQQT---LTRAGIPFIYVDLRIDLLNNTLPSIHLLGEVLNQSSRATAFSNFY 176
Cdd:PRK14048 112 LSFETILTLKADLAIL---ANWQADTEAGQRAieyLESIGVPVIVVDFNNEALKNTPDNMRLLGKVFEREEQAEDFARFY 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 177 QQHMDVIRQRIAQYHGKKPTVMLHLHLGRrDTCCTTAVGGSLGDLLTFAGGENIASGTINSVYGELSPERVLAANPDVYI 256
Cdd:PRK14048 189 EERLARIRDRVAKHSEPGPTVLMEAFPAA-DRCCWAYGRGGLGEFIALTGSRNIAEGALPRPGGMMNAEAIMAENPDVYI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 257 ATgmAGPEGKrFSSLMLGPLVNAEQAKESFDTLIRQePILSHLRAVQTGHAWSMWHNFYLSPYHVVMVEMFAKALYPERF 336
Cdd:PRK14048 268 AT--SSPGGK-YSGFSIGPGVSAEEAETTLANVVDK-PVMASIAAVRDGRVHGLWNFFNAVPLNIVAAEAFASWLRPELF 343
|
330 340
....*....|....*....|....*.
gi 748795526 337 ADIDPQQTLQQLYQQFLPIEFSGIYW 362
Cdd:PRK14048 344 ADIDPAATLAEINRRFAAVPFEGSYW 369
|
|
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
37-337 |
2.21e-51 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 172.10 E-value: 2.21e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 37 RIILGESRMLYTLALL-QPDnpakHVVGWPGDmaRYDAQSWSryiekfpQLSQIPQLGNGslQAMNAEMLLPLKPDLVIL 115
Cdd:COG0614 2 RIVSLSPSATELLLALgAGD----RLVGVSDW--GYCDYPEL-------ELKDLPVVGGT--GEPNLEAILALKPDLVLA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 116 PRLAKNAANEDLLQQtltrAGIPFIYVDLRidLLNNTLPSIHLLGEVLNQSSRATAFSNFYQQHMDVIRQRIAQyHGKKP 195
Cdd:COG0614 67 SSSGNDEEDYEQLEK----IGIPVVVLDPR--SLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAG-AEERP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 196 TVMLHLHLGrrDTCCTTAVGGSLGDLLTFAGGENIASGTiNSVYGELSPERVLAANPDVYIATGMAGPEgkrfsslmlgp 275
Cdd:COG0614 140 TVLYEIWSG--DPLYTAGGGSFIGELLELAGGRNVAADL-GGGYPEVSLEQVLALDPDVIILSGGGYDA----------- 205
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 748795526 276 lvnaEQAKESFDTLiRQEPILSHLRAVQTGHAWSMWHNFYL--SPYHVVMVEMFAKALYPERFA 337
Cdd:COG0614 206 ----ETAEEALEAL-LADPGWQSLPAVKNGRVYVVPGDLLSrpGPRLLLALEDLAKALHPELFA 264
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
76-310 |
9.61e-21 |
|
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: 89.73 E-value: 9.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 76 WSRYIEKFPQLSQIPQLGNGSLqaMNAEMLLPLKPDLVILPRLAKNAANEDLLQqtltrAGIPFIYVDLRIDLLNNtLPS 155
Cdd:pfam01497 26 YTRDPLKADAVAAIVKVGAYGE--INVERLAALKPDLVILSTGYLTDEAEELLS-----LIIPTVIFESSSTGESL-KEQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 156 IHLLGEVLNQSSRATAFSNFYQQHMDVIRQRIAQyHGKKPTVMLHLHLGRRDTccTTAVGGSLGDLLTFAGGENIASGTI 235
Cdd:pfam01497 98 IKQLGELLGLEDEAEELVAEIDSALAAAKKAVPS-LTRKPVLVFGGADGGGYV--VAGSNTYIGDLLRILGIENIAAELS 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 748795526 236 NSVYGELSPERVLAANPDVYIATGMagpegkrfsslmlgplvnAEQAKESFDtLIRQEPILSHLRAVQTGHAWSM 310
Cdd:pfam01497 175 GSEYAPISFEAILSSNPDVIIVSGR------------------DSFTKTGPE-FVAANPLWAGLPAVKNGRVYTL 230
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| TroA_f |
cd01139 |
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ... |
19-362 |
1.82e-141 |
|
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: 405.15 E-value: 1.82e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 19 KTVTDILGRQVTIPDNPQRIILGESRMLYTLALLQPDNPAKHVVGWPGDMARYDAQSWSRYIEKFPQLSQIPQLGNGSLQ 98
Cdd:cd01139 1 ITVTDVAGRKVTLDAPVERVLLGEGRQLYALALLEGENPFARIVGWGGDLKKGDPDTYAKYKEKFPEIADIPLIGSTYNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 99 AMNAEMLLPLKPDLVILPRLAKNAANEDLLQQTLTRAGIPFIYVDLRIDLLNNTLPSIHLLGEVLNQSSRATAFSNFYQQ 178
Cdd:cd01139 81 DFSVEKVLTLKPDLVILNIWAKTTAEESGILEKLEQAGIPVVFVDFRQKPLKNTTPSMRLLGKALGREERAEEFIEFYQE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 179 HMDVIRQRIAQYHGKKPTVMLHLHLGRRDTCCTTAVGGSLGDLLTFAGGENIASGTINSVYGELSPERVLAANPDVYIAT 258
Cdd:cd01139 161 RIDRIRDRLAKINEPKPKVFIELGAGGPEECCSTYGNGNWGELVDAAGGDNIADGLIPGTSGELNAEYVIAANPEIIIAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 259 GMAGPegKRFSSLMLGPLVNAEQAKESFDTLIRQEPILSHLRAVQTGHAWSMWHNFYLSPYHVVMVEMFAKALYPERFAD 338
Cdd:cd01139 241 GGNWA--KDPSGVSLGPDGTTADAKESLLRALLKRPGWSSLQAVKNGRVYALWHQFYRSPYNFVALEAFAKWLYPELFKD 318
|
330 340
....*....|....*....|....
gi 748795526 339 IDPQQTLQQLYQQFLPIEFSGIYW 362
Cdd:cd01139 319 LDPEATLQEFHRQFLPVDYSGTFW 342
|
|
| PRK14048 |
PRK14048 |
ferrichrome/ferrioxamine B periplasmic transporter; Provisional |
20-362 |
9.34e-68 |
|
ferrichrome/ferrioxamine B periplasmic transporter; Provisional
Pssm-ID: 172540 [Multi-domain] Cd Length: 374 Bit Score: 217.84 E-value: 9.34e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 20 TVTDILGRQVTIPDNPQRIILGESRMLYTLALLQPDnPAKHVVGWPGDMARYDAQSWSRYIEKFPQLSQIPQLGNGSLQA 99
Cdd:PRK14048 33 TVTDAVGREVTIPAPPKAVLLGSGFNLIALSLIHPD-PVSLLAGWSGDMKGDNPEIYESFLRKFPELADVPLIDDGSGPG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 100 MNAEMLLPLKPDLVILprlAKNAANEDLLQQT---LTRAGIPFIYVDLRIDLLNNTLPSIHLLGEVLNQSSRATAFSNFY 176
Cdd:PRK14048 112 LSFETILTLKADLAIL---ANWQADTEAGQRAieyLESIGVPVIVVDFNNEALKNTPDNMRLLGKVFEREEQAEDFARFY 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 177 QQHMDVIRQRIAQYHGKKPTVMLHLHLGRrDTCCTTAVGGSLGDLLTFAGGENIASGTINSVYGELSPERVLAANPDVYI 256
Cdd:PRK14048 189 EERLARIRDRVAKHSEPGPTVLMEAFPAA-DRCCWAYGRGGLGEFIALTGSRNIAEGALPRPGGMMNAEAIMAENPDVYI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 257 ATgmAGPEGKrFSSLMLGPLVNAEQAKESFDTLIRQePILSHLRAVQTGHAWSMWHNFYLSPYHVVMVEMFAKALYPERF 336
Cdd:PRK14048 268 AT--SSPGGK-YSGFSIGPGVSAEEAETTLANVVDK-PVMASIAAVRDGRVHGLWNFFNAVPLNIVAAEAFASWLRPELF 343
|
330 340
....*....|....*....|....*.
gi 748795526 337 ADIDPQQTLQQLYQQFLPIEFSGIYW 362
Cdd:PRK14048 344 ADIDPAATLAEINRRFAAVPFEGSYW 369
|
|
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
37-337 |
2.21e-51 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 172.10 E-value: 2.21e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 37 RIILGESRMLYTLALL-QPDnpakHVVGWPGDmaRYDAQSWSryiekfpQLSQIPQLGNGslQAMNAEMLLPLKPDLVIL 115
Cdd:COG0614 2 RIVSLSPSATELLLALgAGD----RLVGVSDW--GYCDYPEL-------ELKDLPVVGGT--GEPNLEAILALKPDLVLA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 116 PRLAKNAANEDLLQQtltrAGIPFIYVDLRidLLNNTLPSIHLLGEVLNQSSRATAFSNFYQQHMDVIRQRIAQyHGKKP 195
Cdd:COG0614 67 SSSGNDEEDYEQLEK----IGIPVVVLDPR--SLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAG-AEERP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 196 TVMLHLHLGrrDTCCTTAVGGSLGDLLTFAGGENIASGTiNSVYGELSPERVLAANPDVYIATGMAGPEgkrfsslmlgp 275
Cdd:COG0614 140 TVLYEIWSG--DPLYTAGGGSFIGELLELAGGRNVAADL-GGGYPEVSLEQVLALDPDVIILSGGGYDA----------- 205
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 748795526 276 lvnaEQAKESFDTLiRQEPILSHLRAVQTGHAWSMWHNFYL--SPYHVVMVEMFAKALYPERFA 337
Cdd:COG0614 206 ----ETAEEALEAL-LADPGWQSLPAVKNGRVYVVPGDLLSrpGPRLLLALEDLAKALHPELFA 264
|
|
| TroA_e |
cd01142 |
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ... |
17-341 |
2.01e-34 |
|
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: 128.24 E-value: 2.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 17 QAKTVTDILGRQVTIPDNPQRIILGESRMLYTLALLQPDnpaKHVVGWPGDMarydaQSWSRYIEKFPQLSQIPQLGNGS 96
Cdd:cd01142 6 ATRTITDMAGRKVTIPDEVKRIAALWGAGNAVVAALGGG---KLIVATTSTV-----QQEPWLYRLAPSLENVATGGTGN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 97 lqAMNAEMLLPLKPDLVILPRLAKNAANEDLLQqtltraGIPFIYvdLRIDLLNNTLPSIHLLGEVLNQSSRATAFSNFY 176
Cdd:cd01142 78 --DVNIEELLALKPDVVIVWSTDGKEAGKAVLR------LLNALS--LRDAELEEVKLTIALLGELLGRQEKAEALVAYF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 177 QQHMDVIRQRIAQY-HGKKPTVMLhlhlgRRDTCCTTAVGGSL-GDLLTFAGGENIASGTINSVYGELSPERVLAANPDV 254
Cdd:cd01142 148 DDNLAYVAARTKKLpDSERPRVYY-----AGPDPLTTDGTGSItNSWIDLAGGINVASEATKKGSGEVSLEQLLKWNPDV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 255 YIATGMAGPEGkrfsslmlgplvnaeqakesfdtlIRQEPILSHLRAVQTGH------AWSMWHnfYLSPYHVVMVEMFA 328
Cdd:cd01142 223 IIVGNADTKAA------------------------ILADPRWQNLRAVKNGRvyvnpeGAFWWD--RPSAEEALLGLWLA 276
|
330
....*....|...
gi 748795526 329 KALYPERFADIDP 341
Cdd:cd01142 277 KTLYPERFTDDDM 289
|
|
| HemV-2 |
cd01147 |
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ... |
31-319 |
7.73e-25 |
|
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: 101.64 E-value: 7.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 31 IPDNPQRII-LGESRMLYTLALLQPDNpakhVVGWpGDMARYDAQSwsRYIEKFPQLSQIPQLGNGSL-QAMNAEMLLPL 108
Cdd:cd01147 1 VPKPVERVVaAGPGALRLLYALAAPDK----IVGV-DDAEKSDEGR--PYFLASPELKDLPVIGRGGRgNTPNYEKIAAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 109 KPDLVILPRLAKNAANEDLLQQtltRAGIPFIYVDLRIDlLNNTLPSIHLLGEVLNQSSRATAFSNFYQQHMDVIRQRIA 188
Cdd:cd01147 74 KPDVVIDVGSDDPTSIADDLQK---KTGIPVVVLDGGDS-LEDTPEQIRLLGKVLGKEERAEELISFIESILADVEERTK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 189 QYH-GKKPTVmlhlHLGRRDTccTTAVG-----GSLGDLLTFAGGENIASGtINSVYG-ELSPERVLAANPDVYIATGMA 261
Cdd:cd01147 150 DIPdEEKPTV----YFGRIGT--KGAAGlesglAGSIEVFELAGGINVADG-LGGGGLkEVSPEQILLWNPDVIFLDTGS 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 748795526 262 gpegkrfsslmlGPLVNAEQAKesfdtlirQEPILSHLRAVQTGhawsmwhNFYLSPY 319
Cdd:cd01147 223 ------------FYLSLEGYAK--------NRPFWQSLKAVKNG-------RVYLLPA 253
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
76-310 |
9.61e-21 |
|
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: 89.73 E-value: 9.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 76 WSRYIEKFPQLSQIPQLGNGSLqaMNAEMLLPLKPDLVILPRLAKNAANEDLLQqtltrAGIPFIYVDLRIDLLNNtLPS 155
Cdd:pfam01497 26 YTRDPLKADAVAAIVKVGAYGE--INVERLAALKPDLVILSTGYLTDEAEELLS-----LIIPTVIFESSSTGESL-KEQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 156 IHLLGEVLNQSSRATAFSNFYQQHMDVIRQRIAQyHGKKPTVMLHLHLGRRDTccTTAVGGSLGDLLTFAGGENIASGTI 235
Cdd:pfam01497 98 IKQLGELLGLEDEAEELVAEIDSALAAAKKAVPS-LTRKPVLVFGGADGGGYV--VAGSNTYIGDLLRILGIENIAAELS 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 748795526 236 NSVYGELSPERVLAANPDVYIATGMagpegkrfsslmlgplvnAEQAKESFDtLIRQEPILSHLRAVQTGHAWSM 310
Cdd:pfam01497 175 GSEYAPISFEAILSSNPDVIIVSGR------------------DSFTKTGPE-FVAANPLWAGLPAVKNGRVYTL 230
|
|
| ChuT |
COG4558 |
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ... |
25-310 |
5.55e-19 |
|
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443619 [Multi-domain] Cd Length: 285 Bit Score: 86.01 E-value: 5.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 25 LGRQVTIPDnPQRII-LGES--RMLYTLALlqpdnpAKHVVG------WPgdmarydaqswsryiekfPQLSQIPQLGNG 95
Cdd:COG4558 18 AGASVAAAA-AERIVsLGGSvtEIVYALGA------GDRLVGvdttstYP------------------AAAKALPDVGYM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 96 slQAMNAEMLLPLKPDLVILprlAKNAANEDLLQQtLTRAGIPFIYVDLRIDLlNNTLPSIHLLGEVLNQSSRATAFSNF 175
Cdd:COG4558 73 --RQLSAEGILSLKPTLVLA---SEGAGPPEVLDQ-LRAAGVPVVVVPAAPSL-EGVLAKIRAVAAALGVPEAGEALAAR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 176 YQQHMDVIRQRIAQyHGKKPTVMLHLHLGRRDTccTTAVGGSLGD-LLTFAGGENIASGTINsvYGELSPERVLAANPDV 254
Cdd:COG4558 146 LEADLAALAARVAA-IGKPPRVLFLLSRGGGRP--MVAGRGTAADaLIRLAGGVNAAAGFEG--YKPLSAEALIAAAPDV 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 748795526 255 YIAT-----GMAGPEGkrfsslmlgplvnaeqakesfdtlIRQEPILSHLRAVQTGHAWSM 310
Cdd:COG4558 221 ILVMtrgleSLGGVDG------------------------LLALPGLAQTPAGKNKRIVAM 257
|
|
| YvrC |
cd01143 |
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ... |
95-256 |
2.93e-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: 70.77 E-value: 2.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 95 GSLQAMNAEMLLPLKPDLVILPRLAKNAANEDLLQqtltrAGIPFIYVDLRiDLLNNTLPSIHLLGEVLNQSSRATAFSN 174
Cdd:cd01143 46 GSYSNPNVEKIVALKPDLVIVSSSSLAELLEKLKD-----AGIPVVVLPAA-SSLDEIYDQIELIGKITGAEEEAEKLVK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 175 FYQQHMDVIRQRIAQYhgKKPTVMLHLHLGRRDTccttaVGG--SLGDLLTFAGGENIASGTINSVYgeLSPERVLAANP 252
Cdd:cd01143 120 EMKQKIDKVKDKGKTI--KKSKVYIEVSLGGPYT-----AGKntFINELIRLAGAKNIAADSGGWPQ--VSPEEILKANP 190
|
....
gi 748795526 253 DVYI 256
Cdd:cd01143 191 DVII 194
|
|
| HutB |
cd01149 |
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ... |
84-254 |
3.67e-13 |
|
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: 68.45 E-value: 3.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 84 PQLSQIPQLGNGslQAMNAEMLLPLKPDLVIlprLAKNAANEDLLQQtLTRAGIPFIYVDlRIDLLNNTLPSIHLLGEVL 163
Cdd:cd01149 35 EAAAKLPDVGYM--RQLSAEGVLSLKPTLVI---ASDEAGPPEALDQ-LRAAGVPVVTVP-STPTLDGLLTKIRQVAQAL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 164 NQSSRATAFSNFYQQHMDVIRQRIAQyHGKKPTVM-LHLHLGRRdtccTTAVG-GSLGD-LLTFAGGENIASGTINsvYG 240
Cdd:cd01149 108 GVPEKGEALAQEVRQRLAALRKTVAA-HKKPPRVLfLLSHGGGA----AMAAGrNTAADaIIALAGAVNAAAGFRG--YK 180
|
170
....*....|....
gi 748795526 241 ELSPERVLAANPDV 254
Cdd:cd01149 181 PLSAEALIAAQPDV 194
|
|
| TroA-like |
cd00636 |
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ... |
36-198 |
4.23e-13 |
|
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: 66.04 E-value: 4.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 36 QRIILGESRMLYTLALLQPDnpaKHVVGWPG-DMARYDAQSWSRYIEKFPQLSQIpqlgngslqamNAEMLLPLKPDLVI 114
Cdd:cd00636 1 KRVVALDPGATELLLALGGD---DKPVGVADpSGYPPEAKALLEKVPDVGHGYEP-----------NLEKIAALKPDLII 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 115 LprlakNAANEDLLQQTLTRAGIPFIYVDLRIDL-LNNTLPSIHLLGEVLNQSSRATAFSNFYQQHMDVIRQRIAQYHGK 193
Cdd:cd00636 67 A-----NGSGLEAWLDKLSKIAIPVVVVDEASELsLENIKESIRLIGKALGKEENAEELIAELDARLAELRAKLAKIPKK 141
|
....*
gi 748795526 194 KPTVM 198
Cdd:cd00636 142 KVSLV 146
|
|
| BtuF |
cd01144 |
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ... |
84-308 |
2.11e-12 |
|
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: 66.17 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 84 PQLSQIPQLGngSLQAMNAEMLLPLKPDLVILPRLAKNAANEDLLQqtltRAGIPfiYVDLRIDLLNNTLPSIHLLGEVL 163
Cdd:cd01144 34 PEAKKLPRVG--GFYQLDLERVLALKPDLVIAWDDCNVCAVVDQLR----AAGIP--VLVSEPQTLDDILADIRRLGTLA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 164 NQSSRATAFSNFYQQHMDVIRQRIAQYhgKKPTVMLHLHlgrrDTCCTTAVGGSLGDLLTFAGGENIAsGTINSVYGELS 243
Cdd:cd01144 106 GRPARAEELAEALRRRLAALRKQYASK--PPPRVFYQEW----IDPLMTAGGDWVPELIALAGGVNVF-ADAGERSPQVS 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 748795526 244 PERVLAANPDVYIatgmAGPEGKRFSslmlgplvnaeqakesfDTLIRQEPILSHLRAVQTGHAW 308
Cdd:cd01144 179 WEDVLAANPDVIV----LSPCGFGFT-----------------PAILRKEPAWQALPAVRNGRVY 222
|
|
| btuF |
PRK09534 |
corrinoid ABC transporter substrate-binding protein; Reviewed |
20-263 |
1.03e-11 |
|
corrinoid ABC transporter substrate-binding protein; Reviewed
Pssm-ID: 236552 [Multi-domain] Cd Length: 359 Bit Score: 65.32 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 20 TVTDILGRQVTIPDNPQRIIlgesrmlyTLallqpdNPAKHVVGWP-GDMARydAQSWSRYIEKFPQLSQIPQLGNGSLQ 98
Cdd:PRK09534 45 TETDATGTEITLDERPERVV--------TL------NPSAAQTMWElGARDR--VVGVTQYASYLDGAEERTNVSGGQPF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 99 AMNAEMLLPLKPDLVILPRLAKNAANEDLLQQTLTRAGIPFIYVdlridlLNNTLPSIHLLGEVLNQSSRATAFSNFYQQ 178
Cdd:PRK09534 109 GVNVEAVVGLDPDLVLAPNAVAGDTVTRLREAGITVFHFPAATS------IEDVAEKTATIGRLTGNCEAAAETNAEMRD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 179 HMDVIRQRIAQYHgKKPTVMLHLHLGRrdtcctTAVGGS-LGDLLTFAGGENIASGTINSVYGELSPERVLAANPDVYIA 257
Cdd:PRK09534 183 RVDAVEDRTADVD-DRPRVLYPLGDGY------TAGGNTfIGALIEAAGGHNVAADATTDGYPQLSEEVIVQQDPDVIVV 255
|
....*.
gi 748795526 258 TGMAGP 263
Cdd:PRK09534 256 ATASAL 261
|
|
| FatB |
cd01140 |
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ... |
28-306 |
8.69e-10 |
|
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: 58.81 E-value: 8.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 28 QVTIPDNPQRIILGESRMLYTLALLQPDnpakhVVGWPgdmaryDAQSWSRYIEKFPQlSQIPQLgnGSLQAMNAEMLLP 107
Cdd:cd01140 5 ETKVPKNPEKVVVFDVGALDTLDALGVK-----VVGVP------KSSTLPEYLKKYKD-DKYANV--GTLFEPDLEAIAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 108 LKPDLVIL-PRLAKNaanedlLQQTLTRAGIPFIYVDLRiDLLNNTLPSIHLLGEVLNQSSRATAFSNFYQQHMDVIRQR 186
Cdd:cd01140 71 LKPDLIIIgGRLAEK------YDELKKIAPTIDLGADLK-NYLESVKQNIETLGKIFGKEEEAKELVAEIDASIAEAKSA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 187 IAqyhgKKPTVMLHLHLGrrDTCCTTAVGGSLGDLLTFAGGENIASGTINSVYGE-LSPERVLAANPDVY--IATGMA-G 262
Cdd:cd01140 144 AK----GKKKALVVLVNG--GKLSAFGPGSRFGWLHDLLGFEPADENIKASSHGQpVSFEYILEANPDWLfvIDRGAAiG 217
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 748795526 263 PEGKrfsslmlgplvNAEQAKESfdtlirqePILSHLRAVQTGH 306
Cdd:cd01140 218 AEGS-----------SAKEVLDN--------DLVKNTTAWKNGK 242
|
|
| FecB |
COG4594 |
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ... |
17-307 |
6.85e-09 |
|
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443650 [Multi-domain] Cd Length: 316 Bit Score: 56.47 E-value: 6.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 17 QAKTVTDILGrQVTIPDNPQRIILGESRMLYTLALL--QP-----DNPAKHVVGWPGDMarydaqswsryIEKFPQLsqi 89
Cdd:COG4594 35 GARTVKHAMG-ETTIPGTPKRVVVLEWSFADALLALgvTPvgiadDNDYDRWVPYLRDL-----------IKGVTSV--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 90 pqlgnGSLQAMNAEMLLPLKPDLvILPRLAKNAANEDLLQQtltragI-PFIYVDLRIDLLNNTLPSIHLLGEVLNQSSR 168
Cdd:COG4594 100 -----GTRSQPNLEAIAALKPDL-IIADKSRHEAIYDQLSK------IaPTVLFKSRNGDYQENLESFKTIAKALGKEEE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 169 ATAFSNFYQQHMDVIRQRIAQYHGKKPTVMLhlhlgrrdtcctTAVGGSL---------GDLLTFAGGENIASGTINSVY 239
Cdd:COG4594 168 AEAVLADHDQRIAEAKAKLAAADKGKKVAVG------------QFRADGLrlytpnsfaGSVLAALGFENPPKQSKDNGY 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 748795526 240 G--ELSPERVLAANPDV-YIATGmagpegkrfsslmlgplvnaeqAKESFDTLIRQEPILSHLRAVQTGHA 307
Cdd:COG4594 236 GysEVSLEQLPALDPDVlFIATY----------------------DDPSILKEWKNNPLWKNLKAVKNGRV 284
|
|
| FhuD |
cd01146 |
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ... |
33-310 |
1.29e-08 |
|
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: 54.98 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 33 DNPQRII-LGESRMLYTLAL-LQPdnpakhvVGwpgdMAryDAQSWSRYI-EKFPQLSQIPQLGNGSlqAMNAEMLLPLK 109
Cdd:cd01146 1 AKPQRIVaLDWGALETLLALgVKP-------VG----VA--DTAGYKPWIpEPALPLEGVVDVGTRG--QPNLEAIAALK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 110 PDLVILPRLAkNAANEDLLQQtltragI-PFIYVDLRIDLlNNTLPSIHLLGEVLNQSSRATAFSNFYQQHMDVIRQRIA 188
Cdd:cd01146 66 PDLILGSASR-HDEIYDQLSQ------IaPTVLLDSSPWL-AEWKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKLP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 189 QYHGKKPTVML-----HLHLGRRDtcctTAVGGSLGDL-LTFAGGENIASGtinSVYGELSPERVLAANPDVyiatgmag 262
Cdd:cd01146 138 DKGPKPVSVVRfsdagSIRLYGPN----SFAGSVLEDLgLQNPWAQETTND---SGFATISLERLAKADADV-------- 202
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 748795526 263 pegkrfssLMLGPLVNAEQAKEsfdtlIRQEPILSHLRAVQTGHAWSM 310
Cdd:cd01146 203 --------LFVFTYEDEELAQA-----LQANPLWQNLPAVKNGRVYVV 237
|
|
| TroA_a |
cd01148 |
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ... |
103-265 |
2.62e-08 |
|
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: 54.65 E-value: 2.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 103 EMLLPLKPDLVILPRLAKNAANEDLLQQTLTRAGIP---------FIYVDLRIDLLNNtlpSIHLLGEVLNQSSRATAFS 173
Cdd:cd01148 73 ETVLAARPDLVFGGWSYGFDKGGLGTPDSLAELGIKtyilpescgQRRGEATLDDVYN---DIRNLGKIFDVEDRADKLV 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 174 NFYQQHMDVIRQRIAQyHGKKPTVMLhLHLGRRDTccTTAVGGSL-GDLLTFAGGENIASgTINSVYGELSPERVLAANP 252
Cdd:cd01148 150 ADLKARLAEISAKVKG-DGKKVAVFV-YDSGEDKP--FTSGRGGIpNAIITAAGGRNVFA-DVDESWTTVSWETVIARNP 224
|
170
....*....|...
gi 748795526 253 DVYIATGMAGPEG 265
Cdd:cd01148 225 DVIVIIDYGDQNA 237
|
|
| PRK03379 |
PRK03379 |
vitamin B12-transporter protein BtuF; Provisional |
75-259 |
5.69e-06 |
|
vitamin B12-transporter protein BtuF; Provisional
Pssm-ID: 179575 [Multi-domain] Cd Length: 260 Bit Score: 47.37 E-value: 5.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 75 SWSRYIEKFPQLSQIpqlgnGSLQAMNAEMLLPLKPDLVILPRlAKNAanEDLLQQtLTRAGIPFIYVDLR-IDLLNNTL 153
Cdd:PRK03379 43 SYSDYPPQAKKIEQV-----ATWQGMNLERIVALKPDLVLAWR-GGNA--ERQVDQ-LASLGIKVMWVDATsIEQIANAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 154 PSihlLGEVLNQSSRATAFSNFYQQHMDVIRQRIAQyhgkKPTVMLHLHLGRRDTccTTAVGGSL-GDLLTFAGGENIAS 232
Cdd:PRK03379 114 RQ---LAPWSPQPEKAEQAAQSLLQQYAALKAQYAD----KPKKRVFLQFGTNPL--FTSGKHSIqSQVLSLCGGENIFA 184
|
170 180
....*....|....*....|....*..
gi 748795526 233 GTiNSVYGELSPERVLAANPDVYIATG 259
Cdd:PRK03379 185 DS-RVPWPQVSREQVLARKPQAIVITG 210
|
|
| TroA_d |
cd01141 |
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ... |
28-142 |
2.19e-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: 41.64 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748795526 28 QVTIPDNPQRIILgesrMLYTLA--LLQPDNPAKhVVGWPGdmarydaqswSRYIEKFPQLSQIPQLGNGSLQAMNAEML 105
Cdd:cd01141 1 AKTIKVPPKRIVV----LSPTHVdlLLALDKADK-IVGVSA----------SAYDLNTPAVKERIDIQVGPTGSLNVELI 65
|
90 100 110
....*....|....*....|....*....|....*..
gi 748795526 106 LPLKPDLVILPRLAKNAANEDLLQQtltrAGIPFIYV 142
Cdd:cd01141 66 VALKPDLVILYGGFQAQTILDKLEQ----LGIPVLYV 98
|
|
| |
