|
Name |
Accession |
Description |
Interval |
E-value |
| CeuA |
COG4607 |
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and ... |
10-332 |
1.32e-112 |
|
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443657 [Multi-domain] Cd Length: 310 Bit Score: 329.06 E-value: 1.32e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 10 RNIVVASVASLGLVLGACSTDAGNEDKSAAAgneSTITVTDNHGEQTVPAEIDSVVATDNRSFEMLDQWGIKLAAAPKPI 89
Cdd:COG4607 3 KTLLAALALAAALALAACGSSSAAAASAAAA---ETVTVEHALGTVEVPKNPKRVVVFDNGALDTLDALGVEVAGVPKGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 90 IPFTVSDYKDnPDVQDIGNHREPNLEIVAAADPDLIVNGQRFGKYYDDLKKLAPnsaIVEFEpREGKPLDEELKRHAKGL 169
Cdd:COG4607 80 LPDYLSKYAD-DKYANVGTLFEPDLEAIAALKPDLIIIGGRSAKKYDELSKIAP---TIDLT-VDGEDYLESLKRNTETL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 170 GAIFGKEKEADQLIADFDKALERARKAYNPDVKVMALNSSGGTLGYIAPtvGRTFGPLFDLIGMKPALEVDKASdDHqGD 249
Cdd:COG4607 155 GEIFGKEDEAEELVADLDAKIAALKAAAAGKGTALIVLTNGGKISAYGP--GSRFGPIHDVLGFKPADEDIEAS-TH-GQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 250 EISAESIAEANPDFIMVLDRDAGTSVRGTdeyrSAQSVVEEAApLKNVKAVKEGKIYYA-PEDTYTNE-SIITYTEILNG 327
Cdd:COG4607 231 AISFEFIAEANPDWLFVIDRDAAIGGEGP----AAKQVLDNEL-VKQTTAWKNGQIVYLdPDAWYLAGgGIQSLTEMLDE 305
|
....*
gi 1092600651 328 LADAF 332
Cdd:COG4607 306 VADAL 310
|
|
| FatB |
cd01140 |
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ... |
50-330 |
2.17e-77 |
|
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: 237.93 E-value: 2.17e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 50 DNHGEQTVPAEIDSVVATDNRSFEMLDQWGIKLAAAPK-PIIPFTVSDYKDNPdVQDIGNHREPNLEIVAAADPDLIVNG 128
Cdd:cd01140 1 HALGETKVPKNPEKVVVFDVGALDTLDALGVKVVGVPKsSTLPEYLKKYKDDK-YANVGTLFEPDLEAIAALKPDLIIIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 129 QRFGKYYDDLKKLAPNsaivEFEPREGKPLDEELKRHAKGLGAIFGKEKEADQLIADFDKALERARKAYNPDVKVMALNS 208
Cdd:cd01140 80 GRLAEKYDELKKIAPT----IDLGADLKNYLESVKQNIETLGKIFGKEEEAKELVAEIDASIAEAKSAAKGKKKALVVLV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 209 SGGTLGYIAPtvGRTFGPLFDLIGMKPALEVDKASddHQGDEISAESIAEANPDFIMVLDRDAGTSVRGTdeyrSAQSVV 288
Cdd:cd01140 156 NGGKLSAFGP--GSRFGWLHDLLGFEPADENIKAS--SHGQPVSFEYILEANPDWLFVIDRGAAIGAEGS----SAKEVL 227
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1092600651 289 EEaAPLKNVKAVKEGKIYYAPEDTYTNESIITyTEILNGLAD 330
Cdd:cd01140 228 DN-DLVKNTTAWKNGKVIYLDPDLWYLSGGGL-ESLKQMIDD 267
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
65-311 |
3.50e-37 |
|
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: 133.26 E-value: 3.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 65 VATDNRSFEMLDQWGIKLAAAPKPIIPFTVSDYKDNPDVQDIGNHREPNLEIVAAADPDLIVnGQRFGKYYDDLKKLAPN 144
Cdd:pfam01497 1 AALSPAYTEILYALGATDSIVGVDAYTRDPLKADAVAAIVKVGAYGEINVERLAALKPDLVI-LSTGYLTDEAEELLSLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 145 SAIVEFEPREGKpldEELKRHAKGLGAIFGKEKEADQLIADFDKALERARKAYNPDV-KVMALNSSGGTLGYIAPTVGRT 223
Cdd:pfam01497 80 IPTVIFESSSTG---ESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTrKPVLVFGGADGGGYVVAGSNTY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 224 FGPLFDLIGMKPALEvdkASDDHQGDEISAESIAEANPDFIMVLDRDAGTSVRgtdeyrsaQSVVEEAAPLKNVKAVKEG 303
Cdd:pfam01497 157 IGDLLRILGIENIAA---ELSGSEYAPISFEAILSSNPDVIIVSGRDSFTKTG--------PEFVAANPLWAGLPAVKNG 225
|
....*...
gi 1092600651 304 KIYYAPED 311
Cdd:pfam01497 226 RVYTLPSD 233
|
|
| PRK10957 |
PRK10957 |
iron-enterobactin transporter periplasmic binding protein; Provisional |
11-332 |
3.58e-12 |
|
iron-enterobactin transporter periplasmic binding protein; Provisional
Pssm-ID: 236806 [Multi-domain] Cd Length: 317 Bit Score: 66.15 E-value: 3.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 11 NIVVASVASLGLVLGACSTdagnedkSAAAGNESTITVTDNHGEQTVPAE-----------------IDS-VVA------ 66
Cdd:PRK10957 1 PLYRLALLLLGLLLSGIAA-------AQASAAGWPRTVTDSRGSVTLESKpqrivstsvtltgtllaIDApVIAsgattp 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 67 ----TDNRSFemLDQWgiklaaapkpiipftvSDYKDNPDVQ--DIGnhrEPNLEIVAAADPDLIVNGQRFG----KYYD 136
Cdd:PRK10957 74 ntrvADDQGF--FRQW----------------SDVAKERGVEvlYIG---EPDAEAVAAQMPDLIVISATGGdsalALYD 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 137 DLKKLAPnsAIVefepregkpLD------EELkrhAKGLGAIFGKEKEADQLIADFDKALERARKAYNP---DVKVMALN 207
Cdd:PRK10957 133 QLSAIAP--TLV---------IDyddkswQEL---ATQLGEATGLEKQAAAVIAQFDAQLAEVKAKITLppqPVSALVYN 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 208 SSGGT--LGYIAPTVGRTFGPL-FDLIGMKPALevdkASDDHQG-----DEISAESIAEA-NPDFIMVLdrdagtsvRGT 278
Cdd:PRK10957 199 GAGHSanLWTPESAQGQLLEQLgFTLAELPAGL----QASTSQGkrhdiIQLGGENLAAGlNGETLFLF--------AGD 266
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1092600651 279 DEyrSAQSVVeeAAP-LKNVKAVKEGKIYYAPEDTYTnesiITY---TEILNGLADAF 332
Cdd:PRK10957 267 DK--DADAFL--ADPlLANLPAVQNKQVYALGTDTFR----LDYysaTQLLDRLAALF 316
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CeuA |
COG4607 |
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and ... |
10-332 |
1.32e-112 |
|
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443657 [Multi-domain] Cd Length: 310 Bit Score: 329.06 E-value: 1.32e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 10 RNIVVASVASLGLVLGACSTDAGNEDKSAAAgneSTITVTDNHGEQTVPAEIDSVVATDNRSFEMLDQWGIKLAAAPKPI 89
Cdd:COG4607 3 KTLLAALALAAALALAACGSSSAAAASAAAA---ETVTVEHALGTVEVPKNPKRVVVFDNGALDTLDALGVEVAGVPKGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 90 IPFTVSDYKDnPDVQDIGNHREPNLEIVAAADPDLIVNGQRFGKYYDDLKKLAPnsaIVEFEpREGKPLDEELKRHAKGL 169
Cdd:COG4607 80 LPDYLSKYAD-DKYANVGTLFEPDLEAIAALKPDLIIIGGRSAKKYDELSKIAP---TIDLT-VDGEDYLESLKRNTETL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 170 GAIFGKEKEADQLIADFDKALERARKAYNPDVKVMALNSSGGTLGYIAPtvGRTFGPLFDLIGMKPALEVDKASdDHqGD 249
Cdd:COG4607 155 GEIFGKEDEAEELVADLDAKIAALKAAAAGKGTALIVLTNGGKISAYGP--GSRFGPIHDVLGFKPADEDIEAS-TH-GQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 250 EISAESIAEANPDFIMVLDRDAGTSVRGTdeyrSAQSVVEEAApLKNVKAVKEGKIYYA-PEDTYTNE-SIITYTEILNG 327
Cdd:COG4607 231 AISFEFIAEANPDWLFVIDRDAAIGGEGP----AAKQVLDNEL-VKQTTAWKNGQIVYLdPDAWYLAGgGIQSLTEMLDE 305
|
....*
gi 1092600651 328 LADAF 332
Cdd:COG4607 306 VADAL 310
|
|
| FatB |
cd01140 |
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ... |
50-330 |
2.17e-77 |
|
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: 237.93 E-value: 2.17e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 50 DNHGEQTVPAEIDSVVATDNRSFEMLDQWGIKLAAAPK-PIIPFTVSDYKDNPdVQDIGNHREPNLEIVAAADPDLIVNG 128
Cdd:cd01140 1 HALGETKVPKNPEKVVVFDVGALDTLDALGVKVVGVPKsSTLPEYLKKYKDDK-YANVGTLFEPDLEAIAALKPDLIIIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 129 QRFGKYYDDLKKLAPNsaivEFEPREGKPLDEELKRHAKGLGAIFGKEKEADQLIADFDKALERARKAYNPDVKVMALNS 208
Cdd:cd01140 80 GRLAEKYDELKKIAPT----IDLGADLKNYLESVKQNIETLGKIFGKEEEAKELVAEIDASIAEAKSAAKGKKKALVVLV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 209 SGGTLGYIAPtvGRTFGPLFDLIGMKPALEVDKASddHQGDEISAESIAEANPDFIMVLDRDAGTSVRGTdeyrSAQSVV 288
Cdd:cd01140 156 NGGKLSAFGP--GSRFGWLHDLLGFEPADENIKAS--SHGQPVSFEYILEANPDWLFVIDRGAAIGAEGS----SAKEVL 227
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1092600651 289 EEaAPLKNVKAVKEGKIYYAPEDTYTNESIITyTEILNGLAD 330
Cdd:cd01140 228 DN-DLVKNTTAWKNGKVIYLDPDLWYLSGGGL-ESLKQMIDD 267
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
65-311 |
3.50e-37 |
|
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: 133.26 E-value: 3.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 65 VATDNRSFEMLDQWGIKLAAAPKPIIPFTVSDYKDNPDVQDIGNHREPNLEIVAAADPDLIVnGQRFGKYYDDLKKLAPN 144
Cdd:pfam01497 1 AALSPAYTEILYALGATDSIVGVDAYTRDPLKADAVAAIVKVGAYGEINVERLAALKPDLVI-LSTGYLTDEAEELLSLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 145 SAIVEFEPREGKpldEELKRHAKGLGAIFGKEKEADQLIADFDKALERARKAYNPDV-KVMALNSSGGTLGYIAPTVGRT 223
Cdd:pfam01497 80 IPTVIFESSSTG---ESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTrKPVLVFGGADGGGYVVAGSNTY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 224 FGPLFDLIGMKPALEvdkASDDHQGDEISAESIAEANPDFIMVLDRDAGTSVRgtdeyrsaQSVVEEAAPLKNVKAVKEG 303
Cdd:pfam01497 157 IGDLLRILGIENIAA---ELSGSEYAPISFEAILSSNPDVIIVSGRDSFTKTG--------PEFVAANPLWAGLPAVKNG 225
|
....*...
gi 1092600651 304 KIYYAPED 311
Cdd:pfam01497 226 RVYTLPSD 233
|
|
| FecB |
COG4594 |
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ... |
13-335 |
1.07e-36 |
|
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443650 [Multi-domain] Cd Length: 316 Bit Score: 134.28 E-value: 1.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 13 VVASVASLGLVLGACSTDAgnEDKSAAAGNESTITVTDNHGEQTVPAEIDSVVATDNRSFEMLDQWGIKLAAA-----PK 87
Cdd:COG4594 6 LLLILLLALLLLAACGSSS--SDSSSSEAAAGARTVKHAMGETTIPGTPKRVVVLEWSFADALLALGVTPVGIaddndYD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 88 PIIPFTVSDYKDnpdVQDIGNHREPNLEIVAAADPDLIV-NGQRFGKYYDDLKKLAPNsaiVEFEPREGkPLDEELKRhA 166
Cdd:COG4594 84 RWVPYLRDLIKG---VTSVGTRSQPNLEAIAALKPDLIIaDKSRHEAIYDQLSKIAPT---VLFKSRNG-DYQENLES-F 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 167 KGLGAIFGKEKEADQLIADFDKALERARK---AYNPDVKVMALNSSGGTLgyiaptvgRTFGP------LFDLIGMKPAL 237
Cdd:COG4594 156 KTIAKALGKEEEAEAVLADHDQRIAEAKAklaAADKGKKVAVGQFRADGL--------RLYTPnsfagsVLAALGFENPP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 238 EVDKASDDHQgDEISAESIAEANPDFIMVLdrdagtsvrgtdEYRSAQSVVE-EAAPL-KNVKAVKEGKIYYAPEDTYT- 314
Cdd:COG4594 228 KQSKDNGYGY-SEVSLEQLPALDPDVLFIA------------TYDDPSILKEwKNNPLwKNLKAVKNGRVYEVDGDLWTr 294
|
330 340
....*....|....*....|.
gi 1092600651 315 NESIITYTEILNGLADAFEQA 335
Cdd:COG4594 295 GRGPLAAELMADDLVEILLKK 315
|
|
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
64-311 |
1.96e-30 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 116.25 E-value: 1.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 64 VVATDNRSFEMLdqwgIKLAAAPKpIIPFTVSDYKDNP-----DVQDIGNHREPNLEIVAAADPDLIVnGQRFGKYYDDL 138
Cdd:COG0614 3 IVSLSPSATELL----LALGAGDR-LVGVSDWGYCDYPelelkDLPVVGGTGEPNLEAILALKPDLVL-ASSSGNDEEDY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 139 KKLAPNSA-IVEFEPREGKPLDEELKRhakgLGAIFGKEKEADQLIADFDKALERARKAYNPD---VKVMALNSSGGTLg 214
Cdd:COG0614 77 EQLEKIGIpVVVLDPRSLEDLYESIRL----LGELLGREERAEALIAEYEARLAAVRARLAGAeerPTVLYEIWSGDPL- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 215 yIAPTVGRTFGPLFDLIGMKPAlevdkASDDHQG-DEISAESIAEANPDFIMVLDRDAgtsvrGTDEYRSAQSVVEEAAP 293
Cdd:COG0614 152 -YTAGGGSFIGELLELAGGRNV-----AADLGGGyPEVSLEQVLALDPDVIILSGGGY-----DAETAEEALEALLADPG 220
|
250
....*....|....*...
gi 1092600651 294 LKNVKAVKEGKIYYAPED 311
Cdd:COG0614 221 WQSLPAVKNGRVYVVPGD 238
|
|
| FhuD |
cd01146 |
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ... |
64-312 |
1.07e-26 |
|
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: 105.83 E-value: 1.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 64 VVATDNRSFEMLDQWGIKLAAAPKP--IIPFTVSDYKDNPDVQDIGNHREPNLEIVAAADPDLIV-NGQRFGKYYDDLKK 140
Cdd:cd01146 6 IVALDWGALETLLALGVKPVGVADTagYKPWIPEPALPLEGVVDVGTRGQPNLEAIAALKPDLILgSASRHDEIYDQLSQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 141 LAPnsaIVEFEPREGkplDEELKRHAKGLGAIFGKEKEADQLIADFDKALERARKAY----NPDVKVMALNSSGGTLGYI 216
Cdd:cd01146 86 IAP---TVLLDSSPW---LAEWKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKLpdkgPKPVSVVRFSDAGSIRLYG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 217 APTvgrTFGPLFDLIGMKPALEVDKASDDHQGdEISAESIAEANPDFIMVldrdagtsvrGTDEYRSAQSVVEEAAPLKN 296
Cdd:cd01146 160 PNS---FAGSVLEDLGLQNPWAQETTNDSGFA-TISLERLAKADADVLFV----------FTYEDEELAQALQANPLWQN 225
|
250
....*....|....*.
gi 1092600651 297 VKAVKEGKIYYAPEDT 312
Cdd:cd01146 226 LPAVKNGRVYVVDDVW 241
|
|
| FeuA |
cd01138 |
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ... |
53-306 |
2.96e-25 |
|
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: 102.03 E-value: 2.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 53 GEQTVPAEIDSVVAtDNRSFEMLDQWGIKLAAAPkpIIPFTVSDYKDNPDVQDIGNHREPNLEIVAAADPDLIVNGQRFG 132
Cdd:cd01138 1 GEVEIPAKPKRIVA-LSGETEGLALLGIKPVGAA--SIGGKNPYYKKKTLAKVVGIVDEPNLEKVLELKPDLIIVSSKQE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 133 KYYDDLKKLAPNSAIvefePREGKPLDEELKRHAKglgaIFGKEKEADQLIADFDKALERARK----AYNPDVKVMALNS 208
Cdd:cd01138 78 ENYEKLSKIAPTVPV----SYNSSDWEEQLKEIGK----LLNKEDEAEKWLADYKQKAKEAKEkikkKLGNDKSVAVLRG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 209 SGGTlgYIAPTVGRTFGP-LFDLIGMKPALEVDKASDDHQGDEISAESIAEANPDFIMVLDRDAGTSvrgtdeyrsaqSV 287
Cdd:cd01138 150 RKQI--YVFGEDGRGGGPiLYADLGLKAPEKVKEIEDKPGYAAISLEVLPEFDADYIFLLFFTGPEA-----------KA 216
|
250 260
....*....|....*....|
gi 1092600651 288 VEEAAPL-KNVKAVKEGKIY 306
Cdd:cd01138 217 DFESLPIwKNLPAVKNNHVY 236
|
|
| TroA_a |
cd01148 |
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ... |
64-334 |
5.05e-17 |
|
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: 79.69 E-value: 5.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 64 VVATDNRSFEMLDQWGIK-----LAAAPKPIIPFTVSDYKDNPDVqdigNHREPNLEIVAAADPDLIVNGQRFG---KYY 135
Cdd:cd01148 21 VVSNDQNTTEMMLALGLQdrmvgTAGIDNKDLPELKAKYDKVPEL----AKKYPSKETVLAARPDLVFGGWSYGfdkGGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 136 DDLKKLAPNSaIVEFEPRE------GKPLDEELKRHAKGLGAIFGKEKEADQLIADFDKALERARKA---YNPDVKVMAL 206
Cdd:cd01148 97 GTPDSLAELG-IKTYILPEscgqrrGEATLDDVYNDIRNLGKIFDVEDRADKLVADLKARLAEISAKvkgDGKKVAVFVY 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 207 NSSGGTlgyiAPTVGR--TFGPLFDLIGMKPALE-VDKASDDhqgdeISAESIAEANPDFIMVLDRDAGTSvrgtdeYRS 283
Cdd:cd01148 176 DSGEDK----PFTSGRggIPNAIITAAGGRNVFAdVDESWTT-----VSWETVIARNPDVIVIIDYGDQNA------AEQ 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1092600651 284 AQSVVEEAAPLKNVKAVKEGKIYYAPedtytnesiitYTEILNGLA--DAFEQ 334
Cdd:cd01148 241 KIKFLKENPALKNVPAVKNNRFIVLP-----------LAEATPGIRnvDAIEK 282
|
|
| TroA-like |
cd00636 |
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ... |
64-196 |
1.69e-16 |
|
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: 75.29 E-value: 1.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 64 VVATDNRSFEMLDQWG--IKLAAAPKPIiPFTVSDYKDNPDVQDIGNHREPNLEIVAAADPDLIV-NGQRFGKYYDDLKK 140
Cdd:cd00636 3 VVALDPGATELLLALGgdDKPVGVADPS-GYPPEAKALLEKVPDVGHGYEPNLEKIAALKPDLIIaNGSGLEAWLDKLSK 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1092600651 141 LAPNsaIVEFEPREGKPLDEeLKRHAKGLGAIFGKEKEADQLIADFDKALERARKA 196
Cdd:cd00636 82 IAIP--VVVVDEASELSLEN-IKESIRLIGKALGKEENAEELIAELDARLAELRAK 134
|
|
| HemV-2 |
cd01147 |
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ... |
57-309 |
3.78e-16 |
|
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: 76.99 E-value: 3.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 57 VPAEIDSVVATDNRSFEMLdqwgikLA-AAPKPII------------PFTVS--DYKDNPDVQDIGNHREPNLEIVAAAD 121
Cdd:cd01147 1 VPKPVERVVAAGPGALRLL------YAlAAPDKIVgvddaeksdegrPYFLAspELKDLPVIGRGGRGNTPNYEKIAALK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 122 PDLIVN--GQRFGKYYDDLKKLAPNSAIVEFEPREGKPLDEELKRhakgLGAIFGKEKEADQLIADFDKALERARK---- 195
Cdd:cd01147 75 PDVVIDvgSDDPTSIADDLQKKTGIPVVVLDGGDSLEDTPEQIRL----LGKVLGKEERAEELISFIESILADVEErtkd 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 196 ---AYNPDVKVMALnSSGGTLGYIapTVGRTFGPLFDLIGmkpALEVDKASDDHQGDEISAESIAEANPDFIMVLDRDAG 272
Cdd:cd01147 151 ipdEEKPTVYFGRI-GTKGAAGLE--SGLAGSIEVFELAG---GINVADGLGGGGLKEVSPEQILLWNPDVIFLDTGSFY 224
|
250 260 270
....*....|....*....|....*....|....*..
gi 1092600651 273 TSVRGTDEYRSAqsvveeaapLKNVKAVKEGKIYYAP 309
Cdd:cd01147 225 LSLEGYAKNRPF---------WQSLKAVKNGRVYLLP 252
|
|
| TroA_e |
cd01142 |
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ... |
39-313 |
7.21e-14 |
|
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: 70.85 E-value: 7.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 39 AAGNESTITVTDNHGEQ-TVPAEIDSVVATD---NRSFEMLDqwGIKLAAAPKPIIPFTVSDYKDNP---DVQDIGNHRE 111
Cdd:cd01142 1 PAATAATRTITDMAGRKvTIPDEVKRIAALWgagNAVVAALG--GGKLIVATTSTVQQEPWLYRLAPsleNVATGGTGND 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 112 PNLEIVAAADPDLIVNGQRFGK-YYDDLKKLAPNSAIVEFEpregkplDEELKRHAKGLGAIFGKEKEADQLIADFDKAL 190
Cdd:cd01142 79 VNIEELLALKPDVVIVWSTDGKeAGKAVLRLLNALSLRDAE-------LEEVKLTIALLGELLGRQEKAEALVAYFDDNL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 191 ERARKAYN--PD---VKVMalnssggtlgYIAPTVGRTFGP---LFDLIGMKPALEVDKASDDHQGDEISAESIAEANPD 262
Cdd:cd01142 152 AYVAARTKklPDserPRVY----------YAGPDPLTTDGTgsiTNSWIDLAGGINVASEATKKGSGEVSLEQLLKWNPD 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1092600651 263 FIMVLDRDAGTSVRGTDEYRsaqsvveeaaplkNVKAVKEGKIYYAPEDTY 313
Cdd:cd01142 222 VIIVGNADTKAAILADPRWQ-------------NLRAVKNGRVYVNPEGAF 259
|
|
| PRK10957 |
PRK10957 |
iron-enterobactin transporter periplasmic binding protein; Provisional |
11-332 |
3.58e-12 |
|
iron-enterobactin transporter periplasmic binding protein; Provisional
Pssm-ID: 236806 [Multi-domain] Cd Length: 317 Bit Score: 66.15 E-value: 3.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 11 NIVVASVASLGLVLGACSTdagnedkSAAAGNESTITVTDNHGEQTVPAE-----------------IDS-VVA------ 66
Cdd:PRK10957 1 PLYRLALLLLGLLLSGIAA-------AQASAAGWPRTVTDSRGSVTLESKpqrivstsvtltgtllaIDApVIAsgattp 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 67 ----TDNRSFemLDQWgiklaaapkpiipftvSDYKDNPDVQ--DIGnhrEPNLEIVAAADPDLIVNGQRFG----KYYD 136
Cdd:PRK10957 74 ntrvADDQGF--FRQW----------------SDVAKERGVEvlYIG---EPDAEAVAAQMPDLIVISATGGdsalALYD 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 137 DLKKLAPnsAIVefepregkpLD------EELkrhAKGLGAIFGKEKEADQLIADFDKALERARKAYNP---DVKVMALN 207
Cdd:PRK10957 133 QLSAIAP--TLV---------IDyddkswQEL---ATQLGEATGLEKQAAAVIAQFDAQLAEVKAKITLppqPVSALVYN 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 208 SSGGT--LGYIAPTVGRTFGPL-FDLIGMKPALevdkASDDHQG-----DEISAESIAEA-NPDFIMVLdrdagtsvRGT 278
Cdd:PRK10957 199 GAGHSanLWTPESAQGQLLEQLgFTLAELPAGL----QASTSQGkrhdiIQLGGENLAAGlNGETLFLF--------AGD 266
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1092600651 279 DEyrSAQSVVeeAAP-LKNVKAVKEGKIYYAPEDTYTnesiITY---TEILNGLADAF 332
Cdd:PRK10957 267 DK--DADAFL--ADPlLANLPAVQNKQVYALGTDTFR----LDYysaTQLLDRLAALF 316
|
|
| fecB |
PRK11411 |
iron-dicitrate transporter substrate-binding subunit; Provisional |
37-266 |
5.33e-11 |
|
iron-dicitrate transporter substrate-binding subunit; Provisional
Pssm-ID: 183123 [Multi-domain] Cd Length: 303 Bit Score: 62.38 E-value: 5.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 37 SAAAGNESTITVTDNHGEQTVPAEIDSVVATDnrsFEMLDqwgiklAAAPKPIIPFTVSDYKDN----PDV-------QD 105
Cdd:PRK11411 15 LSGSSHAFAVTVQDEQGTFTLEKTPQRIVVLE---LSFVD------ALAAVGVSPVGVADDNDAkrilPEVrahlkpwQS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 106 IGNHREPNLEIVAAADPDLIV-NGQRFGKYYDDLKKLAPnsaIVEFEPReGKPLDEELKRHAKgLGAIFGKEKEADQLIA 184
Cdd:PRK11411 86 VGTRSQPSLEAIAALKPDLIIaDSSRHAGVYIALQKIAP---TLLLKSR-NETYQENLQSAAI-IGEVLGKKREMQARIE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 185 DFDKALERARKAYNPDVKV---------MALNSSGGTLGYIAPTVGrtfgplfdligmkpaLEVDKASDDHQG-DEISAE 254
Cdd:PRK11411 161 QHKERMAQFASQLPKGTRVafgtsreqqFNLHSPESYTGSVLAALG---------------LNVPKAPMNGAAmPSISLE 225
|
250
....*....|..
gi 1092600651 255 SIAEANPDFIMV 266
Cdd:PRK11411 226 QLLALNPDWLLV 237
|
|
| YvrC |
cd01143 |
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ... |
93-264 |
1.67e-10 |
|
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: 59.60 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 93 TVSDY-KDNPDVQDIGNHREPNLEIVAAADPDLIV-NGQRFGKYYDDLKKLAPNSAIVEfeprEGKPLDEELKRHAKgLG 170
Cdd:cd01143 31 TYSNYpKEVRKKPKVGSYSNPNVEKIVALKPDLVIvSSSSLAELLEKLKDAGIPVVVLP----AASSLDEIYDQIEL-IG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 171 AIFGKEKEADQLIADFDKALERAR-KAYNPDVKVMALNSSGGTLGyiapTVGR-TF-GPLFDLIGMKPAlevdkASDDHQ 247
Cdd:cd01143 106 KITGAEEEAEKLVKEMKQKIDKVKdKGKTIKKSKVYIEVSLGGPY----TAGKnTFiNELIRLAGAKNI-----AADSGG 176
|
170
....*....|....*..
gi 1092600651 248 GDEISAESIAEANPDFI 264
Cdd:cd01143 177 WPQVSPEEILKANPDVI 193
|
|
| BtuF |
cd01144 |
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ... |
94-313 |
8.54e-09 |
|
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: 55.38 E-value: 8.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 94 VSDYKDNPD----VQDIGNHREPNLEIVAAADPDLIVnGQRFGKYYDDLKKL-APNSAIVEFEPREGKPLDEELKRhakg 168
Cdd:cd01144 26 VTDYCDYPPeakkLPRVGGFYQLDLERVLALKPDLVI-AWDDCNVCAVVDQLrAAGIPVLVSEPQTLDDILADIRR---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 169 LGAIFGKEKEADQLIADFDKALERARKAY--NPDVKVMALNSsggtlgyIAP--TVGRTFGP-LFDLIGMKPALevdkas 243
Cdd:cd01144 101 LGTLAGRPARAEELAEALRRRLAALRKQYasKPPPRVFYQEW-------IDPlmTAGGDWVPeLIALAGGVNVF------ 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1092600651 244 DDHQGD--EISAESIAEANPDFIMVLDRDAGTSVRGTDEYRSAQSvveeaaplknVKAVKEGKIYYAPEDTY 313
Cdd:cd01144 168 ADAGERspQVSWEDVLAANPDVIVLSPCGFGFTPAILRKEPAWQA----------LPAVRNGRVYAVDGNWY 229
|
|
| ChuT |
COG4558 |
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ... |
105-280 |
6.84e-08 |
|
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443619 [Multi-domain] Cd Length: 285 Bit Score: 52.89 E-value: 6.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 105 DIGNHREPNLEIVAAADPDLIVNGQRFGKYyDDLKKLapNSAIVEFEPREGKPLDEELKRHAKGLGAIFGKEKEADQLIA 184
Cdd:COG4558 68 DVGYMRQLSAEGILSLKPTLVLASEGAGPP-EVLDQL--RAAGVPVVVVPAAPSLEGVLAKIRAVAAALGVPEAGEALAA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 185 DFDK---ALERARKAYNPDVKVMALNSSGGTLGYIAptvGR--TFGPLFDLIGMKPALevdkasDDHQG-DEISAESIAE 258
Cdd:COG4558 145 RLEAdlaALAARVAAIGKPPRVLFLLSRGGGRPMVA---GRgtAADALIRLAGGVNAA------AGFEGyKPLSAEALIA 215
|
170 180
....*....|....*....|..
gi 1092600651 259 ANPDFIMVLDRDaGTSVRGTDE 280
Cdd:COG4558 216 AAPDVILVMTRG-LESLGGVDG 236
|
|
| HutB |
cd01149 |
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ... |
105-279 |
2.82e-07 |
|
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: 50.73 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 105 DIGNHREPNLEIVAAADPDLIVNGQRFGKYyDDLKKLApnSAIVEFEPREGKPLDEELKRHAKGLGAIFGKEKEADQLIA 184
Cdd:cd01149 42 DVGYMRQLSAEGVLSLKPTLVIASDEAGPP-EALDQLR--AAGVPVVTVPSTPTLDGLLTKIRQVAQALGVPEKGEALAQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 185 DFDKALERARK---AYNPDVKVMALNSSGGTLGYIA--PTVGRTfgpLFDLIGMKPALevdkasDDHQG-DEISAESIAE 258
Cdd:cd01149 119 EVRQRLAALRKtvaAHKKPPRVLFLLSHGGGAAMAAgrNTAADA---IIALAGAVNAA------AGFRGyKPLSAEALIA 189
|
170 180
....*....|....*....|.
gi 1092600651 259 ANPDFIMVLDRdAGTSVRGTD 279
Cdd:cd01149 190 AQPDVILVMSR-GLDAVGGVD 209
|
|
| PRK10576 |
PRK10576 |
Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD; |
52-194 |
1.86e-06 |
|
Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD;
Pssm-ID: 236719 Cd Length: 292 Bit Score: 48.86 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 52 HGEQTVPAEIDSVVATDNRSFEMLDQWGIK-LAAAPKPIIPFTVSDYKDNPDVQDIGNHREPNLEIVAAADPDLIVNGQR 130
Cdd:PRK10576 23 NTAAAAAIDPNRIVALEWLPVELLLALGVTpYGVADTHNYRLWVSEPALPDSVIDVGLRTEPNLELLTQMKPSLILWSAG 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1092600651 131 FGKYYDDLKKLAPNSAiVEFEPReGKPLdeELKRHA-KGLGAIFGKEKEADQLIADFDKALERAR 194
Cdd:PRK10576 103 YGPSPEKLARIAPGRG-FAFSDG-KKPL--AVARKSlVELAQRLNLEAAAETHLAQFDDFIASAK 163
|
|
| TroA_d |
cd01141 |
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ... |
95-254 |
6.20e-06 |
|
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: 46.26 E-value: 6.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 95 SDYKDNPDVQ-----DIGNHREPNLEIVAAADPDLIVNGQRFGKY--YDDLKKLAPNSAIVEFEPREgKPLDEELKRHAK 167
Cdd:cd01141 38 AYDLNTPAVKeridiQVGPTGSLNVELIVALKPDLVILYGGFQAQtiLDKLEQLGIPVLYVNEYPSP-LGRAEWIKFAAA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 168 GLGAifGKEKEADQLIADFDKALErarkayNPDVKVMALNSsggtlgyiaPTVGrTFGPLFDLIGMkPALE--VDKASDD 245
Cdd:cd01141 117 FYGV--GKEDKADEAFAQIAGRYR------DLAKKVSNLNK---------PTVA-IGKPVKGLWYM-PGGNsyVAKMLRD 177
|
....*....
gi 1092600651 246 HQGDEISAE 254
Cdd:cd01141 178 AGGRYLSAE 186
|
|
| TroA_f |
cd01139 |
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ... |
46-306 |
8.54e-05 |
|
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial receptors in the ABC metal ion uptake in eubacteria and archaea. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.
Pssm-ID: 238559 [Multi-domain] Cd Length: 342 Bit Score: 43.84 E-value: 8.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 46 ITVTDNHGEQ-TVPAEIDSVVATDNRS------------FEMLDQWGI-------KLAAAPKPIIPftvsDYKDNPDVQD 105
Cdd:cd01139 1 ITVTDVAGRKvTLDAPVERVLLGEGRQlyalallegenpFARIVGWGGdlkkgdpDTYAKYKEKFP----EIADIPLIGS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 106 IGNhREPNLEIVAAADPDLIV---NGQRFGKYYDDLKKLAPNSAIVEFEPREGKPLDEELKRhAKGLGAIFGKEKEADQL 182
Cdd:cd01139 77 TYN-GDFSVEKVLTLKPDLVIlniWAKTTAEESGILEKLEQAGIPVVFVDFRQKPLKNTTPS-MRLLGKALGREERAEEF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092600651 183 IADFDKALERAR---KAYNPDVKVMALNSSGGTLGYIAPTVGRT-FGPLFDLIGmkpALEVDKASDDHQGDEISAESIAE 258
Cdd:cd01139 155 IEFYQERIDRIRdrlAKINEPKPKVFIELGAGGPEECCSTYGNGnWGELVDAAG---GDNIADGLIPGTSGELNAEYVIA 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1092600651 259 ANPDFIMVLDRDAGTSVRG---------TDEYRSAQSVVEEAAPLKNVKAVKEGKIY 306
Cdd:cd01139 232 ANPEIIIATGGNWAKDPSGvslgpdgttADAKESLLRALLKRPGWSSLQAVKNGRVY 288
|
|
| |
