|
Name |
Accession |
Description |
Interval |
E-value |
| FeuA |
cd01138 |
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ... |
45-288 |
3.90e-85 |
|
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: 255.72 E-value: 3.90e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 45 GKVEVPANPKRVVVLSSFAGNVMSLGVNLVGVDSWSKQNPRFDSKLKD--VAEVSDENVEKIAELNPDLIIGLSNVK-NV 121
Cdd:cd01138 1 GEVEIPAKPKRIVALSGETEGLALLGIKPVGAASIGGKNPYYKKKTLAkvVGIVDEPNLEKVLELKPDLIIVSSKQEeNY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 122 DKLKKIAPTVTYTYGKVDYLTQHLEIGKLLNKEKEAKTWVDDFKKRAQEAGKEIKAKIGEDATVSVVENfNKQLYVYGEN 201
Cdd:cd01138 81 EKLSKIAPTVPVSYNSSDWEEQLKEIGKLLNKEDEAEKWLADYKQKAKEAKEKIKKKLGNDKSVAVLRG-RKQIYVFGED 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 202 WGRGTEILYQEMKLKMPEKVKEKALKEGYYALSTEVLPEFAGDYLIVSKNKD--TDNSFQETESYKNIPAVKNNRVYEAN 279
Cdd:cd01138 160 GRGGGPILYADLGLKAPEKVKEIEDKPGYAAISLEVLPEFDADYIFLLFFTGpeAKADFESLPIWKNLPAVKNNHVYIVD 239
|
....*....
gi 446655233 280 MMEFYFNDP 288
Cdd:cd01138 240 AWVFYFADG 248
|
|
| FecB |
COG4594 |
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ... |
1-279 |
1.74e-56 |
|
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443650 [Multi-domain] Cd Length: 316 Bit Score: 184.74 E-value: 1.74e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 1 MKKL-FISLTVLFVLVMSACsnGSTDKKNDAKGSKSETITYQSENGKVEVPANPKRVVVL-SSFAGNVMSLGVNLVGV-D 77
Cdd:COG4594 1 MKKLlLLLILLLALLLLAAC--GSSSSDSSSSEAAAGARTVKHAMGETTIPGTPKRVVVLeWSFADALLALGVTPVGIaD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 78 SWSKQN--PRFDSKLKDVAEV---SDENVEKIAELNPDLIIGLSN--VKNVDKLKKIAPTVTYTYGKVDY---LTQHLEI 147
Cdd:COG4594 79 DNDYDRwvPYLRDLIKGVTSVgtrSQPNLEAIAALKPDLIIADKSrhEAIYDQLSKIAPTVLFKSRNGDYqenLESFKTI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 148 GKLLNKEKEAKTWVDDFKKRAQEAGKEIKAKiGEDATVSVVENFNKQLYVYGENWGRGtEILyQEMKLKMPEKVKEKAlK 227
Cdd:COG4594 159 AKALGKEEEAEAVLADHDQRIAEAKAKLAAA-DKGKKVAVGQFRADGLRLYTPNSFAG-SVL-AALGFENPPKQSKDN-G 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 446655233 228 EGYYALSTEVLPEFAGDYLIVSKNKDT--DNSFQETESYKNIPAVKNNRVYEAN 279
Cdd:COG4594 235 YGYSEVSLEQLPALDPDVLFIATYDDPsiLKEWKNNPLWKNLKAVKNGRVYEVD 288
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
56-277 |
2.96e-26 |
|
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: 103.60 E-value: 2.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 56 VVVLSSFAGNVMSLGV--NLVGVDSWSKqNPRFDSKLKDVAEV---SDENVEKIAELNPDLIIG---LSNVKNVDKLKKI 127
Cdd:pfam01497 1 AALSPAYTEILYALGAtdSIVGVDAYTR-DPLKADAVAAIVKVgayGEINVERLAALKPDLVILstgYLTDEAEELLSLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 128 APTVTYTYGKV--DYLTQHLEIGKLLNKEKEAKTWVDDFKKRAQEAGKEIKAKIgeDATVSVVENFNKQLYVYGENWGRG 205
Cdd:pfam01497 80 IPTVIFESSSTgeSLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLT--RKPVLVFGGADGGGYVVAGSNTYI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446655233 206 TEILyQEMKLKMPekvkEKALKEGYYA-LSTEVLPEFAGDYLIVS----KNKDTDNSFQETESYKNIPAVKNNRVYE 277
Cdd:pfam01497 158 GDLL-RILGIENI----AAELSGSEYApISFEAILSSNPDVIIVSgrdsFTKTGPEFVAANPLWAGLPAVKNGRVYT 229
|
|
| fecB |
PRK11411 |
iron-dicitrate transporter substrate-binding subunit; Provisional |
5-279 |
8.34e-17 |
|
iron-dicitrate transporter substrate-binding subunit; Provisional
Pssm-ID: 183123 [Multi-domain] Cd Length: 303 Bit Score: 78.95 E-value: 8.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 5 FISLTVLFVLVMSACSngstdkkndakgsKSETITYQSENGKVEVPANPKRVVVLS-SFAGNVMSLGVNLVGV-DSWSKQ 82
Cdd:PRK11411 4 FIRLLFAGLLLLSGSS-------------HAFAVTVQDEQGTFTLEKTPQRIVVLElSFVDALAAVGVSPVGVaDDNDAK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 83 N--PRFDSKLK---DVAEVSDENVEKIAELNPDLIIGLSNVKNV--DKLKKIAPTVTYTYGKVDYlTQHLE----IGKLL 151
Cdd:PRK11411 71 RilPEVRAHLKpwqSVGTRSQPSLEAIAALKPDLIIADSSRHAGvyIALQKIAPTLLLKSRNETY-QENLQsaaiIGEVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 152 NKEKEAKTWVDDFKKRAqeagKEIKAKIGEDATVSVVENFNKQLYVYGENWGRGTeiLYQEMKLKMPEKVKEKAlkeGYY 231
Cdd:PRK11411 150 GKKREMQARIEQHKERM----AQFASQLPKGTRVAFGTSREQQFNLHSPESYTGS--VLAALGLNVPKAPMNGA---AMP 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 446655233 232 ALSTEVLPEFAGDYLIVSKNKDTD--NSFQETESYKNIPAVKNNRVYEAN 279
Cdd:PRK11411 221 SISLEQLLALNPDWLLVAHYRQESivKRWQQDPLWQMLTAAKKQQVASVD 270
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FeuA |
cd01138 |
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ... |
45-288 |
3.90e-85 |
|
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: 255.72 E-value: 3.90e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 45 GKVEVPANPKRVVVLSSFAGNVMSLGVNLVGVDSWSKQNPRFDSKLKD--VAEVSDENVEKIAELNPDLIIGLSNVK-NV 121
Cdd:cd01138 1 GEVEIPAKPKRIVALSGETEGLALLGIKPVGAASIGGKNPYYKKKTLAkvVGIVDEPNLEKVLELKPDLIIVSSKQEeNY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 122 DKLKKIAPTVTYTYGKVDYLTQHLEIGKLLNKEKEAKTWVDDFKKRAQEAGKEIKAKIGEDATVSVVENfNKQLYVYGEN 201
Cdd:cd01138 81 EKLSKIAPTVPVSYNSSDWEEQLKEIGKLLNKEDEAEKWLADYKQKAKEAKEKIKKKLGNDKSVAVLRG-RKQIYVFGED 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 202 WGRGTEILYQEMKLKMPEKVKEKALKEGYYALSTEVLPEFAGDYLIVSKNKD--TDNSFQETESYKNIPAVKNNRVYEAN 279
Cdd:cd01138 160 GRGGGPILYADLGLKAPEKVKEIEDKPGYAAISLEVLPEFDADYIFLLFFTGpeAKADFESLPIWKNLPAVKNNHVYIVD 239
|
....*....
gi 446655233 280 MMEFYFNDP 288
Cdd:cd01138 240 AWVFYFADG 248
|
|
| FecB |
COG4594 |
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ... |
1-279 |
1.74e-56 |
|
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443650 [Multi-domain] Cd Length: 316 Bit Score: 184.74 E-value: 1.74e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 1 MKKL-FISLTVLFVLVMSACsnGSTDKKNDAKGSKSETITYQSENGKVEVPANPKRVVVL-SSFAGNVMSLGVNLVGV-D 77
Cdd:COG4594 1 MKKLlLLLILLLALLLLAAC--GSSSSDSSSSEAAAGARTVKHAMGETTIPGTPKRVVVLeWSFADALLALGVTPVGIaD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 78 SWSKQN--PRFDSKLKDVAEV---SDENVEKIAELNPDLIIGLSN--VKNVDKLKKIAPTVTYTYGKVDY---LTQHLEI 147
Cdd:COG4594 79 DNDYDRwvPYLRDLIKGVTSVgtrSQPNLEAIAALKPDLIIADKSrhEAIYDQLSKIAPTVLFKSRNGDYqenLESFKTI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 148 GKLLNKEKEAKTWVDDFKKRAQEAGKEIKAKiGEDATVSVVENFNKQLYVYGENWGRGtEILyQEMKLKMPEKVKEKAlK 227
Cdd:COG4594 159 AKALGKEEEAEAVLADHDQRIAEAKAKLAAA-DKGKKVAVGQFRADGLRLYTPNSFAG-SVL-AALGFENPPKQSKDN-G 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 446655233 228 EGYYALSTEVLPEFAGDYLIVSKNKDT--DNSFQETESYKNIPAVKNNRVYEAN 279
Cdd:COG4594 235 YGYSEVSLEQLPALDPDVLFIATYDDPsiLKEWKNNPLWKNLKAVKNGRVYEVD 288
|
|
| FhuD |
cd01146 |
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ... |
51-289 |
7.68e-42 |
|
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: 145.12 E-value: 7.68e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 51 ANPKRVVVLS-SFAGNVMSLGVNLVGVDSWSKQNPRFDSKLKDVAEVSDE------NVEKIAELNPDLIIGLS--NVKNV 121
Cdd:cd01146 1 AKPQRIVALDwGALETLLALGVKPVGVADTAGYKPWIPEPALPLEGVVDVgtrgqpNLEAIAALKPDLILGSAsrHDEIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 122 DKLKKIAPTVTYTYGKVDY-LTQHLE-IGKLLNKEKEAKTWVDDFKKRAQEAGKEIKAKIGEDATVSVVENfNKQLYVYG 199
Cdd:cd01146 81 DQLSQIAPTVLLDSSPWLAeWKENLRlIAKALGKEEEAEKLLAEYDQRLAELRQKLPDKGPKPVSVVRFSD-AGSIRLYG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 200 ENWGRGTeILyQEMKLKMPEKVkEKALKEGYYALSTEVLPEFAGDYLIVS--KNKDTDNSFQETESYKNIPAVKNNRVYE 277
Cdd:cd01146 160 PNSFAGS-VL-EDLGLQNPWAQ-ETTNDSGFATISLERLAKADADVLFVFtyEDEELAQALQANPLWQNLPAVKNGRVYV 236
|
250
....*....|..
gi 446655233 278 ANMMEFYFNDPL 289
Cdd:cd01146 237 VDDVWWFFGGGL 248
|
|
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
55-299 |
1.26e-37 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 134.36 E-value: 1.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 55 RVVVLS-SFAGNVMSLGV--NLVGVDSWSKQNPRfDSKLKDVAEVSDE---NVEKIAELNPDLIIG---LSNVKNVDKLK 125
Cdd:COG0614 2 RIVSLSpSATELLLALGAgdRLVGVSDWGYCDYP-ELELKDLPVVGGTgepNLEAILALKPDLVLAsssGNDEEDYEQLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 126 KI-APTVTYTYGKV-DYLTQHLEIGKLLNKEKEAKTWVDDFKKRAQEAGKEIkAKIGEDATVSVVENFNKQLYVYGENWG 203
Cdd:COG0614 81 KIgIPVVVLDPRSLeDLYESIRLLGELLGREERAEALIAEYEARLAAVRARL-AGAEERPTVLYEIWSGDPLYTAGGGSF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 204 RGTeiLYQEMKLKMPekvkEKALKEGYYALSTEVLPEFAGDYLIVS-------KNKDTDNSFQETESYKNIPAVKNNRVY 276
Cdd:COG0614 160 IGE--LLELAGGRNV----AADLGGGYPEVSLEQVLALDPDVIILSgggydaeTAEEALEALLADPGWQSLPAVKNGRVY 233
|
250 260
....*....|....*....|...
gi 446655233 277 EANMMEFYFNDPLTLDFQLDFFK 299
Cdd:COG0614 234 VVPGDLLSRPGPRLLLALEDLAK 256
|
|
| CeuA |
COG4607 |
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and ... |
1-286 |
9.76e-33 |
|
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443657 [Multi-domain] Cd Length: 310 Bit Score: 122.60 E-value: 9.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 1 MKK-LFISLTVLFVLVMSACSNGSTDkknDAKGSKSETITYQSENGKVEVPANPKRVVVLS-SFAGNVMSLGVNLVGV-- 76
Cdd:COG4607 1 MKKtLLAALALAAALALAACGSSSAA---AASAAAAETVTVEHALGTVEVPKNPKRVVVFDnGALDTLDALGVEVAGVpk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 77 DSWSKQNPRF-DSKLKDVAEVSDENVEKIAELNPDLII--GLSNvKNVDKLKKIAPTVTYTYGKVDYL---TQHLE-IGK 149
Cdd:COG4607 78 GLLPDYLSKYaDDKYANVGTLFEPDLEAIAALKPDLIIigGRSA-KKYDELSKIAPTIDLTVDGEDYLeslKRNTEtLGE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 150 LLNKEKEAKTWVDDFKKRAQEAgkeiKAKIGEDATVSVVENFNKQLYVYGEN--WGrgteILYQEMKLKmPEKVKEKALK 227
Cdd:COG4607 157 IFGKEDEAEELVADLDAKIAAL----KAAAAGKGTALIVLTNGGKISAYGPGsrFG----PIHDVLGFK-PADEDIEAST 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446655233 228 EGyYALSTEVLPEFAGDYLIV-------SKNKDTDNSFQETESYKNIPAVKNNRVYEANMMEFYFN 286
Cdd:COG4607 228 HG-QAISFEFIAEANPDWLFVidrdaaiGGEGPAAKQVLDNELVKQTTAWKNGQIVYLDPDAWYLA 292
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
56-277 |
2.96e-26 |
|
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: 103.60 E-value: 2.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 56 VVVLSSFAGNVMSLGV--NLVGVDSWSKqNPRFDSKLKDVAEV---SDENVEKIAELNPDLIIG---LSNVKNVDKLKKI 127
Cdd:pfam01497 1 AALSPAYTEILYALGAtdSIVGVDAYTR-DPLKADAVAAIVKVgayGEINVERLAALKPDLVILstgYLTDEAEELLSLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 128 APTVTYTYGKV--DYLTQHLEIGKLLNKEKEAKTWVDDFKKRAQEAGKEIKAKIgeDATVSVVENFNKQLYVYGENWGRG 205
Cdd:pfam01497 80 IPTVIFESSSTgeSLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLT--RKPVLVFGGADGGGYVVAGSNTYI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446655233 206 TEILyQEMKLKMPekvkEKALKEGYYA-LSTEVLPEFAGDYLIVS----KNKDTDNSFQETESYKNIPAVKNNRVYE 277
Cdd:pfam01497 158 GDLL-RILGIENI----AAELSGSEYApISFEAILSSNPDVIIVSgrdsFTKTGPEFVAANPLWAGLPAVKNGRVYT 229
|
|
| FatB |
cd01140 |
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ... |
44-285 |
2.81e-20 |
|
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: 88.08 E-value: 2.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 44 NGKVEVPANPKRVVVLSSFAGNVMS-LGVNLVGVDSwSKQNPRFDSKLKDVAEVS-----DENVEKIAELNPDLII-GLS 116
Cdd:cd01140 3 LGETKVPKNPEKVVVFDVGALDTLDaLGVKVVGVPK-SSTLPEYLKKYKDDKYANvgtlfEPDLEAIAALKPDLIIiGGR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 117 NVKNVDKLKKIAPTVTYTYGKVDYLT---QHLE-IGKLLNKEKEAKTWVDDFKKRAQeagkEIKAKIGEDATVSVVENFN 192
Cdd:cd01140 82 LAEKYDELKKIAPTIDLGADLKNYLEsvkQNIEtLGKIFGKEEEAKELVAEIDASIA----EAKSAAKGKKKALVVLVNG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 193 KQLYVYGEN--WGrgteILYQemKLKMPEKVKEKALKEGYYALSTEVLPEFAGDYLIV-------SKNKDTDNSFQETES 263
Cdd:cd01140 158 GKLSAFGPGsrFG----WLHD--LLGFEPADENIKASSHGQPVSFEYILEANPDWLFVidrgaaiGAEGSSAKEVLDNDL 231
|
250 260
....*....|....*....|..
gi 446655233 264 YKNIPAVKNNRVYEANMMEFYF 285
Cdd:cd01140 232 VKNTTAWKNGKVIYLDPDLWYL 253
|
|
| TroA-like |
cd00636 |
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ... |
54-187 |
2.99e-17 |
|
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: 76.83 E-value: 2.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 54 KRVVVLS-SFAGNVMSLG--VNLVGVDSWSKQNPRFDSKLKDVAEVSDE---NVEKIAELNPDLII--GLSNVKNVDKLK 125
Cdd:cd00636 1 KRVVALDpGATELLLALGgdDKPVGVADPSGYPPEAKALLEKVPDVGHGyepNLEKIAALKPDLIIanGSGLEAWLDKLS 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446655233 126 KIA-PTVTYTYGKVDYLTQHLE----IGKLLNKEKEAKTWVDDFKKRAQEAGKEIKAKIGEDATVSV 187
Cdd:cd00636 81 KIAiPVVVVDEASELSLENIKEsirlIGKALGKEENAEELIAELDARLAELRAKLAKIPKKKVSLVV 147
|
|
| fecB |
PRK11411 |
iron-dicitrate transporter substrate-binding subunit; Provisional |
5-279 |
8.34e-17 |
|
iron-dicitrate transporter substrate-binding subunit; Provisional
Pssm-ID: 183123 [Multi-domain] Cd Length: 303 Bit Score: 78.95 E-value: 8.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 5 FISLTVLFVLVMSACSngstdkkndakgsKSETITYQSENGKVEVPANPKRVVVLS-SFAGNVMSLGVNLVGV-DSWSKQ 82
Cdd:PRK11411 4 FIRLLFAGLLLLSGSS-------------HAFAVTVQDEQGTFTLEKTPQRIVVLElSFVDALAAVGVSPVGVaDDNDAK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 83 N--PRFDSKLK---DVAEVSDENVEKIAELNPDLIIGLSNVKNV--DKLKKIAPTVTYTYGKVDYlTQHLE----IGKLL 151
Cdd:PRK11411 71 RilPEVRAHLKpwqSVGTRSQPSLEAIAALKPDLIIADSSRHAGvyIALQKIAPTLLLKSRNETY-QENLQsaaiIGEVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 152 NKEKEAKTWVDDFKKRAqeagKEIKAKIGEDATVSVVENFNKQLYVYGENWGRGTeiLYQEMKLKMPEKVKEKAlkeGYY 231
Cdd:PRK11411 150 GKKREMQARIEQHKERM----AQFASQLPKGTRVAFGTSREQQFNLHSPESYTGS--VLAALGLNVPKAPMNGA---AMP 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 446655233 232 ALSTEVLPEFAGDYLIVSKNKDTD--NSFQETESYKNIPAVKNNRVYEAN 279
Cdd:PRK11411 221 SISLEQLLALNPDWLLVAHYRQESivKRWQQDPLWQMLTAAKKQQVASVD 270
|
|
| YvrC |
cd01143 |
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ... |
52-201 |
2.16e-13 |
|
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: 67.69 E-value: 2.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 52 NPKRVVVLS-SFAGNVMSLGV--NLVGVDSWSKQnPRFDSKLKDVAEVSDENVEKIAELNPDLIIGLSNVK--NVDKLKK 126
Cdd:cd01143 2 EPERIVSLSpSITEILFALGAgdKIVGVDTYSNY-PKEVRKKPKVGSYSNPNVEKIVALKPDLVIVSSSSLaeLLEKLKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 127 IAPTVTYTYGKVDY---LTQHLEIGKLLNKEKEAKTWVDDFKKRAQEAgkeikAKIGEDATVSVV--ENFNKQLYVYGEN 201
Cdd:cd01143 81 AGIPVVVLPAASSLdeiYDQIELIGKITGAEEEAEKLVKEMKQKIDKV-----KDKGKTIKKSKVyiEVSLGGPYTAGKN 155
|
|
| TroA_e |
cd01142 |
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ... |
37-278 |
2.48e-13 |
|
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: 68.92 E-value: 2.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 37 TITYQSeNGKVEVPANPKRVVVLSSFAGNV---MSLGVNLVGVDSWSKQNP---RFDSKLKDVAEV---SDENVEKIAEL 107
Cdd:cd01142 9 TITDMA-GRKVTIPDEVKRIAALWGAGNAVvaaLGGGKLIVATTSTVQQEPwlyRLAPSLENVATGgtgNDVNIEELLAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 108 NPDLIIGLSNVKN--VDKLKKIAPTVTYTYGKVDYLTQH-LEIGKLLNKEKEAKTWVDDFKKRaQEAGKEIKAKIGEDAT 184
Cdd:cd01142 88 KPDVVIVWSTDGKeaGKAVLRLLNALSLRDAELEEVKLTiALLGELLGRQEKAEALVAYFDDN-LAYVAARTKKLPDSER 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 185 VSVvenfnkqLYVYGENW---GRGTeILYQEMKLKMPEKVKEKALKEGYYALSTEVL----PEFagdylIVSKNKDTDNS 257
Cdd:cd01142 167 PRV-------YYAGPDPLttdGTGS-ITNSWIDLAGGINVASEATKKGSGEVSLEQLlkwnPDV-----IIVGNADTKAA 233
|
250 260
....*....|....*....|.
gi 446655233 258 FQETESYKNIPAVKNNRVYEA 278
Cdd:cd01142 234 ILADPRWQNLRAVKNGRVYVN 254
|
|
| PRK10957 |
PRK10957 |
iron-enterobactin transporter periplasmic binding protein; Provisional |
4-298 |
4.10e-13 |
|
iron-enterobactin transporter periplasmic binding protein; Provisional
Pssm-ID: 236806 [Multi-domain] Cd Length: 317 Bit Score: 68.46 E-value: 4.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 4 LFISLTVLFVLVMSACSNGSTdkkndAKGSKSETITyqSENGKVEVPANPKRVVVLS-SFAGNVMSLGVNLVGVDSWSKQ 82
Cdd:PRK10957 2 LYRLALLLLGLLLSGIAAAQA-----SAAGWPRTVT--DSRGSVTLESKPQRIVSTSvTLTGTLLAIDAPVIASGATTPN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 83 NPRFDSK--LKDVAEVSDE-----------NVEKIAELNPDLII-----GLSNVKNVDKLKKIAPTVTYTYGKVDYLTQH 144
Cdd:PRK10957 75 TRVADDQgfFRQWSDVAKErgvevlyigepDAEAVAAQMPDLIVisatgGDSALALYDQLSAIAPTLVIDYDDKSWQELA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 145 LEIGKLLNKEKEAKTWVDDFKKRAQEAGKEIKAKIGEdatVSVVenfnkqlyVYGENwGRGTEI---------LYQEMKL 215
Cdd:PRK10957 155 TQLGEATGLEKQAAAVIAQFDAQLAEVKAKITLPPQP---VSAL--------VYNGA-GHSANLwtpesaqgqLLEQLGF 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 216 KM---PEKVKEK---ALKEGYYALSTEVLPE-FAGD-YLIVSKNKDTDNSFQETESYKNIPAVKNNRVYeanmmefyfnd 287
Cdd:PRK10957 223 TLaelPAGLQAStsqGKRHDIIQLGGENLAAgLNGEtLFLFAGDDKDADAFLADPLLANLPAVQNKQVY----------- 291
|
330
....*....|..
gi 446655233 288 PLTLD-FQLDFF 298
Cdd:PRK10957 292 ALGTDtFRLDYY 303
|
|
| HemV-2 |
cd01147 |
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ... |
49-278 |
4.48e-13 |
|
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: 67.75 E-value: 4.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 49 VPANPKRVVVLSSFAGN-VMSLGV--NLVGVDS---WSKQNP--RFDSKLKDVAEVSDE------NVEKIAELNPDLII- 113
Cdd:cd01147 1 VPKPVERVVAAGPGALRlLYALAApdKIVGVDDaekSDEGRPyfLASPELKDLPVIGRGgrgntpNYEKIAALKPDVVId 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 114 -----GLSNVKNVDKLKKIAPTVTYTYGKVDYLTQHLE-IGKLLNKEKEAKTwVDDFKKRAQEAGKEIKAKIGEDATVSV 187
Cdd:cd01147 81 vgsddPTSIADDLQKKTGIPVVVLDGGDSLEDTPEQIRlLGKVLGKEERAEE-LISFIESILADVEERTKDIPDEEKPTV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 188 venfnkqlYV-YGENWG-RGTE----ILYQEMKLKMPEKVKEKALKEGYYALSTEVLPEFAGDYLIVsknkdTDNSFQET 261
Cdd:cd01147 160 --------YFgRIGTKGaAGLEsglaGSIEVFELAGGINVADGLGGGGLKEVSPEQILLWNPDVIFL-----DTGSFYLS 226
|
250 260
....*....|....*....|....*
gi 446655233 262 --------ESYKNIPAVKNNRVYEA 278
Cdd:cd01147 227 legyaknrPFWQSLKAVKNGRVYLL 251
|
|
| TroA_d |
cd01141 |
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ... |
51-199 |
5.46e-09 |
|
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: 54.73 E-value: 5.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 51 ANPKRVVVLSSFAGNVM-SLGVN--LVGVDSWS--KQNPRFDSKLK-DVAEVSDENVEKIAELNPDLII---GLSNVKNV 121
Cdd:cd01141 6 VPPKRIVVLSPTHVDLLlALDKAdkIVGVSASAydLNTPAVKERIDiQVGPTGSLNVELIVALKPDLVIlygGFQAQTIL 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446655233 122 DKLKKIAPTVTYTYGKVDYLTqHLEIGKLLnkekeAKTWVDDFKKRAQEAGKEIKAKIgeDATVSVVENFNKQLYVYG 199
Cdd:cd01141 86 DKLEQLGIPVLYVNEYPSPLG-RAEWIKFA-----AAFYGVGKEDKADEAFAQIAGRY--RDLAKKVSNLNKPTVAIG 155
|
|
| TroA_a |
cd01148 |
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ... |
37-275 |
5.73e-09 |
|
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: 55.81 E-value: 5.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 37 TITYQSENGKVEVPANPKRVVVLSSFAGNVM-SLGV--NLVGVDSWS-KQNPRFDSKLKDVAEVSDE--NVEKIAELNPD 110
Cdd:cd01148 2 PLTVENCGRSVTFDKAPQRVVSNDQNTTEMMlALGLqdRMVGTAGIDnKDLPELKAKYDKVPELAKKypSKETVLAARPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 111 LIIGLSNVKN-------VDKLKKI-APTVTYTYGKV---------DYLTQHLEIGKLLNKEKEAKTWVDDFKKRAQEAGK 173
Cdd:cd01148 82 LVFGGWSYGFdkgglgtPDSLAELgIKTYILPESCGqrrgeatldDVYNDIRNLGKIFDVEDRADKLVADLKARLAEISA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 174 EIKakiGEDATVSVVenfnkqLYVYGE--NWGRGTEILYQEMKLKMPEKVKEKALKEGYYALSTEVL----PEF--AGDY 245
Cdd:cd01148 162 KVK---GDGKKVAVF------VYDSGEdkPFTSGRGGIPNAIITAAGGRNVFADVDESWTTVSWETViarnPDVivIIDY 232
|
250 260 270
....*....|....*....|....*....|
gi 446655233 246 LIVSKNKDTDNSFQETESYKNIPAVKNNRV 275
Cdd:cd01148 233 GDQNAAEQKIKFLKENPALKNVPAVKNNRF 262
|
|
| HutB |
cd01149 |
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ... |
53-276 |
1.89e-08 |
|
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: 53.81 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 53 PKRVVVLSsfaGNV------MSLGVNLVGVDSwSKQNPRFDSKLKDVAEVSDENVEKIAELNPDLIIGL----------- 115
Cdd:cd01149 1 PERIVSLG---GSVteivyaLGAGDRLVGVDS-TSTYPEAAAKLPDVGYMRQLSAEGVLSLKPTLVIASdeagppealdq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 116 ---SNVKNVdklkkiapTVTYTYGKVDYLTQHLEIGKLLNKEKEAKTWVDDFKKRAQEAGKEIKAKIGEDATVSVVENFN 192
Cdd:cd01149 77 lraAGVPVV--------TVPSTPTLDGLLTKIRQVAQALGVPEKGEALAQEVRQRLAALRKTVAAHKKPPRVLFLLSHGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 193 KQLYVYGENWGRGTEIlyqemklKMPEKVKEKALKEGYYALSTEVLPEFAGDYLIVSKN-----KDTDNSFQeTESYKNI 267
Cdd:cd01149 149 GAAMAAGRNTAADAII-------ALAGAVNAAAGFRGYKPLSAEALIAAQPDVILVMSRgldavGGVDGLLK-LPGLAQT 220
|
....*....
gi 446655233 268 PAVKNNRVY 276
Cdd:cd01149 221 PAGRNKRIL 229
|
|
| ChuT |
COG4558 |
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ... |
51-276 |
3.01e-06 |
|
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443619 [Multi-domain] Cd Length: 285 Bit Score: 47.88 E-value: 3.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 51 ANPKRVVVLSS------FAgnvmsLGV--NLVGVDSWSkQNPRFDSKLKDVAEVSDENVEKIAELNPDLIIGLSNVKN-- 120
Cdd:COG4558 25 AAAERIVSLGGsvteivYA-----LGAgdRLVGVDTTS-TYPAAAKALPDVGYMRQLSAEGILSLKPTLVLASEGAGPpe 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 121 -VDKLKKI---------APTVTYTYGKVDyltqhlEIGKLLNKEKEAKTWVDDFKKRAQEAGKEIkAKIGEDATVsvven 190
Cdd:COG4558 99 vLDQLRAAgvpvvvvpaAPSLEGVLAKIR------AVAAALGVPEAGEALAARLEADLAALAARV-AAIGKPPRV----- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 191 fnkqLYVYGENWGR----GTEILYQEMklkmpekVK----EKALK--EGYYALSTEVLPEFAGDYLIVSknKDTDNSFQE 260
Cdd:COG4558 167 ----LFLLSRGGGRpmvaGRGTAADAL-------IRlaggVNAAAgfEGYKPLSAEALIAAAPDVILVM--TRGLESLGG 233
|
250 260
....*....|....*....|..
gi 446655233 261 TESYKNIP------AVKNNRVY 276
Cdd:COG4558 234 VDGLLALPglaqtpAGKNKRIV 255
|
|
| BtuF |
cd01144 |
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ... |
73-178 |
3.44e-06 |
|
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: 47.29 E-value: 3.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 73 LVGVDSWSKQNPRFDsKLKDVAEVSDENVEKIAELNPDLIIG--LSNVK-NVDKLKKIAPTVTYTYGK-VDYLTQHLE-I 147
Cdd:cd01144 23 LVGVTDYCDYPPEAK-KLPRVGGFYQLDLERVLALKPDLVIAwdDCNVCaVVDQLRAAGIPVLVSEPQtLDDILADIRrL 101
|
90 100 110
....*....|....*....|....*....|.
gi 446655233 148 GKLLNKEKEAKTWVDDFKKRAQEAGKEIKAK 178
Cdd:cd01144 102 GTLAGRPARAEELAEALRRRLAALRKQYASK 132
|
|
| btuF |
PRK09534 |
corrinoid ABC transporter substrate-binding protein; Reviewed |
4-288 |
6.52e-06 |
|
corrinoid ABC transporter substrate-binding protein; Reviewed
Pssm-ID: 236552 [Multi-domain] Cd Length: 359 Bit Score: 47.21 E-value: 6.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 4 LFISLTVLFVLVMSACSNGSTDKKNDAKGSKSETITyQSENGKVEVPANPKRVVVLSSFAGNVM-SLGVN--LVGVDSWS 80
Cdd:PRK09534 12 VALAVTMTAAGGALAPAPAAQHADADRACSFPVTET-DATGTEITLDERPERVVTLNPSAAQTMwELGARdrVVGVTQYA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 81 KQNPRFDSKlKDVAEVSD--ENVEKIAELNPDLIIGLSNVKN--VDKLKKIAPTVtYTYG---KVDYLTQHLE-IGKLLN 152
Cdd:PRK09534 91 SYLDGAEER-TNVSGGQPfgVNVEAVVGLDPDLVLAPNAVAGdtVTRLREAGITV-FHFPaatSIEDVAEKTAtIGRLTG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 153 KEKEAKTWVDDFKKRAQEAgkeikakigEDATVSvVENFNKQLYVYGENWGRGTEILYQE-MKLKMPEKVKEKALKEGYY 231
Cdd:PRK09534 169 NCEAAAETNAEMRDRVDAV---------EDRTAD-VDDRPRVLYPLGDGYTAGGNTFIGAlIEAAGGHNVAADATTDGYP 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 446655233 232 ALSTEVLPEFAGDYLIVSKNKDTdnsFQETESYKNIPAVKNNRVYEANMMefYFNDP 288
Cdd:PRK09534 239 QLSEEVIVQQDPDVIVVATASAL---VAETEPYASTTAGETGNVVTVNVN--HINQP 290
|
|
| TroA_f |
cd01139 |
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ... |
46-158 |
5.83e-04 |
|
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: 41.14 E-value: 5.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655233 46 KVEVPANPKRVVVLSSFAGNVMSL--GVN----LVGV---------DSWSKQNPRFdSKLKDVAEV-----SDENVEKIA 105
Cdd:cd01139 10 KVTLDAPVERVLLGEGRQLYALALleGENpfarIVGWggdlkkgdpDTYAKYKEKF-PEIADIPLIgstynGDFSVEKVL 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446655233 106 ELNPDLII-------GLSNVKNVDKLKKIAPTVTYTYGKVDYLTQHLE----IGKLLNKEKEAK 158
Cdd:cd01139 89 TLKPDLVIlniwaktTAEESGILEKLEQAGIPVVFVDFRQKPLKNTTPsmrlLGKALGREERAE 152
|
|
| |
