|
Name |
Accession |
Description |
Interval |
E-value |
| FeuA |
cd01138 |
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ... |
15-258 |
1.03e-82 |
|
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: 248.40 E-value: 1.03e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 15 GKVEVPANPQRVVVLSSFAGNVMSLGVNLVGVDSWSKQNPRFDSKLKN--VAEVSDENVEKIAELNPDLIIGLSNIK-NV 91
Cdd:cd01138 1 GEVEIPAKPKRIVALSGETEGLALLGIKPVGAASIGGKNPYYKKKTLAkvVGIVDEPNLEKVLELKPDLIIVSSKQEeNY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 92 DKLKKIAPTVTYTYGKVDYLTQHLEIGKLLNKEKEAKTWVDDFKKRAQTAGKDIKAKIGEDATVSVVENfNKQLYVYGEN 171
Cdd:cd01138 81 EKLSKIAPTVPVSYNSSDWEEQLKEIGKLLNKEDEAEKWLADYKQKAKEAKEKIKKKLGNDKSVAVLRG-RKQIYVFGED 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 172 WGRGTEILYQEMKLKMPEKVKEKALKEGYYALSTEVLPEFAGDYLIVSKNKD--TDNSFQETESYKNIPAVKNNRVYEAN 249
Cdd:cd01138 160 GRGGGPILYADLGLKAPEKVKEIEDKPGYAAISLEVLPEFDADYIFLLFFTGpeAKADFESLPIWKNLPAVKNNHVYIVD 239
|
....*....
gi 1634475675 250 MMEFYFNDP 258
Cdd:cd01138 240 AWVFYFADG 248
|
|
| FecB |
COG4594 |
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ... |
1-249 |
5.94e-47 |
|
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443650 [Multi-domain] Cd Length: 316 Bit Score: 159.32 E-value: 5.94e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 1 KGKKSETITYQSENGKVEVPANPQRVVVL-SSFAGNVMSLGVNLVGV-DSWSKQN--PRFDSKLKNVAEV---SDENVEK 73
Cdd:COG4594 30 SEAAAGARTVKHAMGETTIPGTPKRVVVLeWSFADALLALGVTPVGIaDDNDYDRwvPYLRDLIKGVTSVgtrSQPNLEA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 74 IAELNPDLIIGLSNI--KNVDKLKKIAPTVTYTYGKVDY---LTQHLEIGKLLNKEKEAKTWVDDFKKRAQTAGKDIKAK 148
Cdd:COG4594 110 IAALKPDLIIADKSRheAIYDQLSKIAPTVLFKSRNGDYqenLESFKTIAKALGKEEEAEAVLADHDQRIAEAKAKLAAA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 149 iGEDATVSVVENFNKQLYVYGENWGRGtEILyQEMKLKMPEKVKEKAlKEGYYALSTEVLPEFAGDYLIVSKNKDT--DN 226
Cdd:COG4594 190 -DKGKKVAVGQFRADGLRLYTPNSFAG-SVL-AALGFENPPKQSKDN-GYGYSEVSLEQLPALDPDVLFIATYDDPsiLK 265
|
250 260
....*....|....*....|...
gi 1634475675 227 SFQETESYKNIPAVKNNRVYEAN 249
Cdd:COG4594 266 EWKNNPLWKNLKAVKNGRVYEVD 288
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
26-247 |
1.98e-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: 103.22 E-value: 1.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 26 VVVLSSFAGNVMSLGV--NLVGVDSWSKqNPRFDSKLKNVAEV---SDENVEKIAELNPDLIIGLSNI---KNVDKLKKI 97
Cdd:pfam01497 1 AALSPAYTEILYALGAtdSIVGVDAYTR-DPLKADAVAAIVKVgayGEINVERLAALKPDLVILSTGYltdEAEELLSLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 98 APTVTYTYGKV--DYLTQHLEIGKLLNKEKEAKTWVDDFKKRAQTAGKDIKAKIgeDATVSVVENFNKQLYVYGENWGRG 175
Cdd:pfam01497 80 IPTVIFESSSTgeSLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLT--RKPVLVFGGADGGGYVVAGSNTYI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1634475675 176 TEILyQEMKLKMPEKvkekALKEGYYA-LSTEVLPEFAGDYLIVS----KNKDTDNSFQETESYKNIPAVKNNRVYE 247
Cdd:pfam01497 158 GDLL-RILGIENIAA----ELSGSEYApISFEAILSSNPDVIIVSgrdsFTKTGPEFVAANPLWAGLPAVKNGRVYT 229
|
|
| fecB |
PRK11411 |
iron-dicitrate transporter substrate-binding subunit; Provisional |
7-249 |
5.26e-17 |
|
iron-dicitrate transporter substrate-binding subunit; Provisional
Pssm-ID: 183123 [Multi-domain] Cd Length: 303 Bit Score: 78.95 E-value: 5.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 7 TITYQSENGKVEVPANPQRVVVLS-SFAGNVMSLGVNLVGV-DSWSKQN--PRFDSKLK---NVAEVSDENVEKIAELNP 79
Cdd:PRK11411 23 AVTVQDEQGTFTLEKTPQRIVVLElSFVDALAAVGVSPVGVaDDNDAKRilPEVRAHLKpwqSVGTRSQPSLEAIAALKP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 80 DLIIGLSNIKNV--DKLKKIAPTVTYTYGKVDYlTQHLE----IGKLLNKEKEAKTWVDDFKKRAqtagKDIKAKIGEDA 153
Cdd:PRK11411 103 DLIIADSSRHAGvyIALQKIAPTLLLKSRNETY-QENLQsaaiIGEVLGKKREMQARIEQHKERM----AQFASQLPKGT 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 154 TVSVVENFNKQLYVYGENWGRGTeiLYQEMKLKMPEKVKEKAlkeGYYALSTEVLPEFAGDYLIVSKNKDTD--NSFQET 231
Cdd:PRK11411 178 RVAFGTSREQQFNLHSPESYTGS--VLAALGLNVPKAPMNGA---AMPSISLEQLLALNPDWLLVAHYRQESivKRWQQD 252
|
250
....*....|....*...
gi 1634475675 232 ESYKNIPAVKNNRVYEAN 249
Cdd:PRK11411 253 PLWQMLTAAKKQQVASVD 270
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FeuA |
cd01138 |
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ... |
15-258 |
1.03e-82 |
|
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: 248.40 E-value: 1.03e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 15 GKVEVPANPQRVVVLSSFAGNVMSLGVNLVGVDSWSKQNPRFDSKLKN--VAEVSDENVEKIAELNPDLIIGLSNIK-NV 91
Cdd:cd01138 1 GEVEIPAKPKRIVALSGETEGLALLGIKPVGAASIGGKNPYYKKKTLAkvVGIVDEPNLEKVLELKPDLIIVSSKQEeNY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 92 DKLKKIAPTVTYTYGKVDYLTQHLEIGKLLNKEKEAKTWVDDFKKRAQTAGKDIKAKIGEDATVSVVENfNKQLYVYGEN 171
Cdd:cd01138 81 EKLSKIAPTVPVSYNSSDWEEQLKEIGKLLNKEDEAEKWLADYKQKAKEAKEKIKKKLGNDKSVAVLRG-RKQIYVFGED 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 172 WGRGTEILYQEMKLKMPEKVKEKALKEGYYALSTEVLPEFAGDYLIVSKNKD--TDNSFQETESYKNIPAVKNNRVYEAN 249
Cdd:cd01138 160 GRGGGPILYADLGLKAPEKVKEIEDKPGYAAISLEVLPEFDADYIFLLFFTGpeAKADFESLPIWKNLPAVKNNHVYIVD 239
|
....*....
gi 1634475675 250 MMEFYFNDP 258
Cdd:cd01138 240 AWVFYFADG 248
|
|
| FecB |
COG4594 |
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ... |
1-249 |
5.94e-47 |
|
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443650 [Multi-domain] Cd Length: 316 Bit Score: 159.32 E-value: 5.94e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 1 KGKKSETITYQSENGKVEVPANPQRVVVL-SSFAGNVMSLGVNLVGV-DSWSKQN--PRFDSKLKNVAEV---SDENVEK 73
Cdd:COG4594 30 SEAAAGARTVKHAMGETTIPGTPKRVVVLeWSFADALLALGVTPVGIaDDNDYDRwvPYLRDLIKGVTSVgtrSQPNLEA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 74 IAELNPDLIIGLSNI--KNVDKLKKIAPTVTYTYGKVDY---LTQHLEIGKLLNKEKEAKTWVDDFKKRAQTAGKDIKAK 148
Cdd:COG4594 110 IAALKPDLIIADKSRheAIYDQLSKIAPTVLFKSRNGDYqenLESFKTIAKALGKEEEAEAVLADHDQRIAEAKAKLAAA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 149 iGEDATVSVVENFNKQLYVYGENWGRGtEILyQEMKLKMPEKVKEKAlKEGYYALSTEVLPEFAGDYLIVSKNKDT--DN 226
Cdd:COG4594 190 -DKGKKVAVGQFRADGLRLYTPNSFAG-SVL-AALGFENPPKQSKDN-GYGYSEVSLEQLPALDPDVLFIATYDDPsiLK 265
|
250 260
....*....|....*....|...
gi 1634475675 227 SFQETESYKNIPAVKNNRVYEAN 249
Cdd:COG4594 266 EWKNNPLWKNLKAVKNGRVYEVD 288
|
|
| FhuD |
cd01146 |
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ... |
21-259 |
9.69e-40 |
|
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: 138.57 E-value: 9.69e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 21 ANPQRVVVLS-SFAGNVMSLGVNLVGVDSWSKQNPRFDSKLKNVAEVSDE------NVEKIAELNPDLIIGLS--NIKNV 91
Cdd:cd01146 1 AKPQRIVALDwGALETLLALGVKPVGVADTAGYKPWIPEPALPLEGVVDVgtrgqpNLEAIAALKPDLILGSAsrHDEIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 92 DKLKKIAPTVTYTYGKVDY-LTQHLE-IGKLLNKEKEAKTWVDDFKKRAQTAGKDIKAKIGEDATVSVVENfNKQLYVYG 169
Cdd:cd01146 81 DQLSQIAPTVLLDSSPWLAeWKENLRlIAKALGKEEEAEKLLAEYDQRLAELRQKLPDKGPKPVSVVRFSD-AGSIRLYG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 170 ENwGRGTEILyQEMKLKMPEKVkEKALKEGYYALSTEVLPEFAGDYLIVS--KNKDTDNSFQETESYKNIPAVKNNRVYE 247
Cdd:cd01146 160 PN-SFAGSVL-EDLGLQNPWAQ-ETTNDSGFATISLERLAKADADVLFVFtyEDEELAQALQANPLWQNLPAVKNGRVYV 236
|
250
....*....|..
gi 1634475675 248 ANMMEFYFNDPL 259
Cdd:cd01146 237 VDDVWWFFGGGL 248
|
|
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
25-269 |
7.65e-37 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 131.27 E-value: 7.65e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 25 RVVVLS-SFAGNVMSLGV--NLVGVDSWSKQNPRfDSKLKNVAEVSDE---NVEKIAELNPDLIIGLSNI---KNVDKLK 95
Cdd:COG0614 2 RIVSLSpSATELLLALGAgdRLVGVSDWGYCDYP-ELELKDLPVVGGTgepNLEAILALKPDLVLASSSGndeEDYEQLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 96 KI-APTVTYTYGKV-DYLTQHLEIGKLLNKEKEAKTWVDDFKKRAQTAGKDIkAKIGEDATVSVVENFNKQLYVYGENWG 173
Cdd:COG0614 81 KIgIPVVVLDPRSLeDLYESIRLLGELLGREERAEALIAEYEARLAAVRARL-AGAEERPTVLYEIWSGDPLYTAGGGSF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 174 RGTeiLYQEMKLKMPekvkEKALKEGYYALSTEVLPEFAGDYLIVS-------KNKDTDNSFQETESYKNIPAVKNNRVY 246
Cdd:COG0614 160 IGE--LLELAGGRNV----AADLGGGYPEVSLEQVLALDPDVIILSgggydaeTAEEALEALLADPGWQSLPAVKNGRVY 233
|
250 260
....*....|....*....|...
gi 1634475675 247 EANMMEFYFNDPLTLDFQLDFFK 269
Cdd:COG0614 234 VVPGDLLSRPGPRLLLALEDLAK 256
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
26-247 |
1.98e-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: 103.22 E-value: 1.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 26 VVVLSSFAGNVMSLGV--NLVGVDSWSKqNPRFDSKLKNVAEV---SDENVEKIAELNPDLIIGLSNI---KNVDKLKKI 97
Cdd:pfam01497 1 AALSPAYTEILYALGAtdSIVGVDAYTR-DPLKADAVAAIVKVgayGEINVERLAALKPDLVILSTGYltdEAEELLSLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 98 APTVTYTYGKV--DYLTQHLEIGKLLNKEKEAKTWVDDFKKRAQTAGKDIKAKIgeDATVSVVENFNKQLYVYGENWGRG 175
Cdd:pfam01497 80 IPTVIFESSSTgeSLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLT--RKPVLVFGGADGGGYVVAGSNTYI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1634475675 176 TEILyQEMKLKMPEKvkekALKEGYYA-LSTEVLPEFAGDYLIVS----KNKDTDNSFQETESYKNIPAVKNNRVYE 247
Cdd:pfam01497 158 GDLL-RILGIENIAA----ELSGSEYApISFEAILSSNPDVIIVSgrdsFTKTGPEFVAANPLWAGLPAVKNGRVYT 229
|
|
| CeuA |
COG4607 |
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and ... |
4-256 |
1.91e-25 |
|
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443657 [Multi-domain] Cd Length: 310 Bit Score: 102.18 E-value: 1.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 4 KSETITYQSENGKVEVPANPQRVVVLS-SFAGNVMSLGVNLVGV--DSWSKQNPRF-DSKLKNVAEVSDENVEKIAELNP 79
Cdd:COG4607 32 AAETVTVEHALGTVEVPKNPKRVVVFDnGALDTLDALGVEVAGVpkGLLPDYLSKYaDDKYANVGTLFEPDLEAIAALKP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 80 DLII--GLSNiKNVDKLKKIAPTVTYTYGKVDYL---TQHLE-IGKLLNKEKEAKTWVDDFKKRAQtagkDIKAKIGEDA 153
Cdd:COG4607 112 DLIIigGRSA-KKYDELSKIAPTIDLTVDGEDYLeslKRNTEtLGEIFGKEDEAEELVADLDAKIA----ALKAAAAGKG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 154 TVSVVENFNKQLYVYGEN--WGrgteILYQEMKLKmPEKVKEKALKEGyYALSTEVLPEFAGDYLIV-------SKNKDT 224
Cdd:COG4607 187 TALIVLTNGGKISAYGPGsrFG----PIHDVLGFK-PADEDIEASTHG-QAISFEFIAEANPDWLFVidrdaaiGGEGPA 260
|
250 260 270
....*....|....*....|....*....|..
gi 1634475675 225 DNSFQETESYKNIPAVKNNRVYEANMMEFYFN 256
Cdd:COG4607 261 AKQVLDNELVKQTTAWKNGQIVYLDPDAWYLA 292
|
|
| FatB |
cd01140 |
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ... |
14-255 |
8.62e-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: 86.16 E-value: 8.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 14 NGKVEVPANPQRVVVLSSFAGNVMS-LGVNLVGVDSwSKQNPRFDSKLK-----NVAEVSDENVEKIAELNPDLII-GLS 86
Cdd:cd01140 3 LGETKVPKNPEKVVVFDVGALDTLDaLGVKVVGVPK-SSTLPEYLKKYKddkyaNVGTLFEPDLEAIAALKPDLIIiGGR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 87 NIKNVDKLKKIAPTVTYTYGKVDYLT---QHLE-IGKLLNKEKEAKTWVDDFKKRAQtagkDIKAKIGEDATVSVVENFN 162
Cdd:cd01140 82 LAEKYDELKKIAPTIDLGADLKNYLEsvkQNIEtLGKIFGKEEEAKELVAEIDASIA----EAKSAAKGKKKALVVLVNG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 163 KQLYVYGEN--WGrgteILYQemKLKMPEKVKEKALKEGYYALSTEVLPEFAGDYLIV-------SKNKDTDNSFQETES 233
Cdd:cd01140 158 GKLSAFGPGsrFG----WLHD--LLGFEPADENIKASSHGQPVSFEYILEANPDWLFVidrgaaiGAEGSSAKEVLDNDL 231
|
250 260
....*....|....*....|..
gi 1634475675 234 YKNIPAVKNNRVYEANMMEFYF 255
Cdd:cd01140 232 VKNTTAWKNGKVIYLDPDLWYL 253
|
|
| fecB |
PRK11411 |
iron-dicitrate transporter substrate-binding subunit; Provisional |
7-249 |
5.26e-17 |
|
iron-dicitrate transporter substrate-binding subunit; Provisional
Pssm-ID: 183123 [Multi-domain] Cd Length: 303 Bit Score: 78.95 E-value: 5.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 7 TITYQSENGKVEVPANPQRVVVLS-SFAGNVMSLGVNLVGV-DSWSKQN--PRFDSKLK---NVAEVSDENVEKIAELNP 79
Cdd:PRK11411 23 AVTVQDEQGTFTLEKTPQRIVVLElSFVDALAAVGVSPVGVaDDNDAKRilPEVRAHLKpwqSVGTRSQPSLEAIAALKP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 80 DLIIGLSNIKNV--DKLKKIAPTVTYTYGKVDYlTQHLE----IGKLLNKEKEAKTWVDDFKKRAqtagKDIKAKIGEDA 153
Cdd:PRK11411 103 DLIIADSSRHAGvyIALQKIAPTLLLKSRNETY-QENLQsaaiIGEVLGKKREMQARIEQHKERM----AQFASQLPKGT 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 154 TVSVVENFNKQLYVYGENWGRGTeiLYQEMKLKMPEKVKEKAlkeGYYALSTEVLPEFAGDYLIVSKNKDTD--NSFQET 231
Cdd:PRK11411 178 RVAFGTSREQQFNLHSPESYTGS--VLAALGLNVPKAPMNGA---AMPSISLEQLLALNPDWLLVAHYRQESivKRWQQD 252
|
250
....*....|....*...
gi 1634475675 232 ESYKNIPAVKNNRVYEAN 249
Cdd:PRK11411 253 PLWQMLTAAKKQQVASVD 270
|
|
| TroA-like |
cd00636 |
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ... |
24-158 |
1.24e-15 |
|
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function in the ABC transport of ferric siderophores and metal ions such as Mn2+, Fe3+, Cu2+ and/or Zn2+. Their ligand binding site is formed in the interface between two globular domains linked by a single helix. Many of these proteins also possess a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence). The TroA-like proteins differ in their fold and ligand-binding mechanism from the PBPI and PBPII proteins, but are structurally similar, however, to the beta-subunit of the nitrogenase molybdenum-iron protein MoFe. Most TroA-like proteins are encoded by ABC-type operons and appear to function as periplasmic components of ABC transporters in metal ion uptake.
Pssm-ID: 238347 [Multi-domain] Cd Length: 148 Bit Score: 72.21 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 24 QRVVVLS-SFAGNVMSLG--VNLVGVDSWSKQNPRFDSKLKNVAEVSDE---NVEKIAELNPDLII--GLSNIKNVDKLK 95
Cdd:cd00636 1 KRVVALDpGATELLLALGgdDKPVGVADPSGYPPEAKALLEKVPDVGHGyepNLEKIAALKPDLIIanGSGLEAWLDKLS 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1634475675 96 KIA-PTVTYTYGKVDYLTQHLE----IGKLLNKEKEAKTWVDDFKKRAqtagKDIKAKIGEDATVSVV 158
Cdd:cd00636 81 KIAiPVVVVDEASELSLENIKEsirlIGKALGKEENAEELIAELDARL----AELRAKLAKIPKKKVS 144
|
|
| TroA_e |
cd01142 |
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ... |
7-248 |
1.37e-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: 69.31 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 7 TITYQSeNGKVEVPANPQRVVVLSSFAGNV---MSLGVNLVGVDSWSKQNP---RFDSKLKNVAEV---SDENVEKIAEL 77
Cdd:cd01142 9 TITDMA-GRKVTIPDEVKRIAALWGAGNAVvaaLGGGKLIVATTSTVQQEPwlyRLAPSLENVATGgtgNDVNIEELLAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 78 NPDLIIGLSNIKN--VDKLKKIAPTVTYTYGKVDYLTQH-LEIGKLLNKEKEAKTWVDDF-----KKRAQTAgkdikaKI 149
Cdd:cd01142 88 KPDVVIVWSTDGKeaGKAVLRLLNALSLRDAELEEVKLTiALLGELLGRQEKAEALVAYFddnlaYVAARTK------KL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 150 GEDATVSVvenfnkqLYVYGENW---GRGTeILYQEMKLKMPEKVKEKALKEGYYALSTEVLPEFAGDyLIVSKNKDTDN 226
Cdd:cd01142 162 PDSERPRV-------YYAGPDPLttdGTGS-ITNSWIDLAGGINVASEATKKGSGEVSLEQLLKWNPD-VIIVGNADTKA 232
|
250 260
....*....|....*....|..
gi 1634475675 227 SFQETESYKNIPAVKNNRVYEA 248
Cdd:cd01142 233 AILADPRWQNLRAVKNGRVYVN 254
|
|
| HemV-2 |
cd01147 |
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ... |
19-248 |
2.54e-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: 68.13 E-value: 2.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 19 VPANPQRVVVLSSFAGN-VMSLGV--NLVGVDS---WSKQNP--RFDSKLKNVAEVSDE------NVEKIAELNPDLII- 83
Cdd:cd01147 1 VPKPVERVVAAGPGALRlLYALAApdKIVGVDDaekSDEGRPyfLASPELKDLPVIGRGgrgntpNYEKIAALKPDVVId 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 84 -----GLSNIKNVDKLKKIAPTVTYTYGKVDYLTQHLE-IGKLLNKEKEAKTwVDDFKKRAQtagKDIkakigEDATVSV 157
Cdd:cd01147 81 vgsddPTSIADDLQKKTGIPVVVLDGGDSLEDTPEQIRlLGKVLGKEERAEE-LISFIESIL---ADV-----EERTKDI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 158 VENFNKQLYV-YGENWG-RGTE----ILYQEMKLKMPEKVKEKALKEGYYALSTEVLPEFAGDYLIVsknkdTDNSFQET 231
Cdd:cd01147 152 PDEEKPTVYFgRIGTKGaAGLEsglaGSIEVFELAGGINVADGLGGGGLKEVSPEQILLWNPDVIFL-----DTGSFYLS 226
|
250 260
....*....|....*....|....*
gi 1634475675 232 --------ESYKNIPAVKNNRVYEA 248
Cdd:cd01147 227 legyaknrPFWQSLKAVKNGRVYLL 251
|
|
| YvrC |
cd01143 |
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ... |
22-171 |
4.94e-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: 66.15 E-value: 4.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 22 NPQRVVVLS-SFAGNVMSLGV--NLVGVDSWSKQNPRFDSKLKnVAEVSDENVEKIAELNPDLIIG--LSNIKNVDKLKK 96
Cdd:cd01143 2 EPERIVSLSpSITEILFALGAgdKIVGVDTYSNYPKEVRKKPK-VGSYSNPNVEKIVALKPDLVIVssSSLAELLEKLKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 97 IAPTVTYTYGKVDY---LTQHLEIGKLLNKEKEAKTWVDDFKKRAqtagKDIKAKiGEDATVSVV--ENFNKQLYVYGEN 171
Cdd:cd01143 81 AGIPVVVLPAASSLdeiYDQIELIGKITGAEEEAEKLVKEMKQKI----DKVKDK-GKTIKKSKVyiEVSLGGPYTAGKN 155
|
|
| PRK10957 |
PRK10957 |
iron-enterobactin transporter periplasmic binding protein; Provisional |
9-268 |
8.98e-11 |
|
iron-enterobactin transporter periplasmic binding protein; Provisional
Pssm-ID: 236806 [Multi-domain] Cd Length: 317 Bit Score: 61.14 E-value: 8.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 9 TYQSENGKVEVPANPQRVVVLS-SFAGNVMSLGVNLVGVDSWSKQNPRFDSK--LKNVAEVSDE-----------NVEKI 74
Cdd:PRK10957 30 TVTDSRGSVTLESKPQRIVSTSvTLTGTLLAIDAPVIASGATTPNTRVADDQgfFRQWSDVAKErgvevlyigepDAEAV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 75 AELNPDLII-----GLSNIKNVDKLKKIAPTVTYTYGKVDYLTQHLEIGKLLNKEKEAKTWVDDFKKRAQTAGKDIKAKI 149
Cdd:PRK10957 110 AAQMPDLIVisatgGDSALALYDQLSAIAPTLVIDYDDKSWQELATQLGEATGLEKQAAAVIAQFDAQLAEVKAKITLPP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 150 GEdatVSVVenfnkqlyVYGENwGRGTEI---------LYQEMKLKM---PEKVKEK---ALKEGYYALSTEVLPE-FAG 213
Cdd:PRK10957 190 QP---VSAL--------VYNGA-GHSANLwtpesaqgqLLEQLGFTLaelPAGLQAStsqGKRHDIIQLGGENLAAgLNG 257
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1634475675 214 D-YLIVSKNKDTDNSFQETESYKNIPAVKNNRVYeanmmefyfndPLTLD-FQLDFF 268
Cdd:PRK10957 258 EtLFLFAGDDKDADAFLADPLLANLPAVQNKQVY-----------ALGTDtFRLDYY 303
|
|
| TroA_a |
cd01148 |
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ... |
7-245 |
5.48e-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: 5.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 7 TITYQSENGKVEVPANPQRVVVLSSFAGNVM-SLGV--NLVGVDSWS-KQNPRFDSKLKNVAEVSDE--NVEKIAELNPD 80
Cdd:cd01148 2 PLTVENCGRSVTFDKAPQRVVSNDQNTTEMMlALGLqdRMVGTAGIDnKDLPELKAKYDKVPELAKKypSKETVLAARPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 81 LIIGLSNIKN-------VDKLKKI-APTVTYTYGKV---------DYLTQHLEIGKLLNKEKEAKTWVDDFKKRAQTAGK 143
Cdd:cd01148 82 LVFGGWSYGFdkgglgtPDSLAELgIKTYILPESCGqrrgeatldDVYNDIRNLGKIFDVEDRADKLVADLKARLAEISA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 144 DIKakiGEDATVSVVenfnkqLYVYGE--NWGRGTEILYQEMKLKMPEKVKEKALKEGYYALSTEVL----PEF--AGDY 215
Cdd:cd01148 162 KVK---GDGKKVAVF------VYDSGEdkPFTSGRGGIPNAIITAAGGRNVFADVDESWTTVSWETViarnPDVivIIDY 232
|
250 260 270
....*....|....*....|....*....|
gi 1634475675 216 LIVSKNKDTDNSFQETESYKNIPAVKNNRV 245
Cdd:cd01148 233 GDQNAAEQKIKFLKENPALKNVPAVKNNRF 262
|
|
| TroA_d |
cd01141 |
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ... |
21-171 |
2.05e-08 |
|
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: 52.81 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 21 ANPQRVVVLSSFAGNVM-SLGVN--LVGVDSWS--KQNPRFDSKLKN-VAEVSDENVEKIAELNPDLII---GLSNIKNV 91
Cdd:cd01141 6 VPPKRIVVLSPTHVDLLlALDKAdkIVGVSASAydLNTPAVKERIDIqVGPTGSLNVELIVALKPDLVIlygGFQAQTIL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 92 DKLKKIAPTVTYTYGKVDYLTqHLEIGKLL------NKEKEAKTWVDDFKKRaqtaGKDIKAKIG--EDATVSVVENFNK 163
Cdd:cd01141 86 DKLEQLGIPVLYVNEYPSPLG-RAEWIKFAaafygvGKEDKADEAFAQIAGR----YRDLAKKVSnlNKPTVAIGKPVKG 160
|
....*...
gi 1634475675 164 QLYVYGEN 171
Cdd:cd01141 161 LWYMPGGN 168
|
|
| HutB |
cd01149 |
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ... |
23-246 |
2.10e-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: 53.42 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 23 PQRVVVLSsfaGNV------MSLGVNLVGVDSwSKQNPRFDSKLKNVAEVSDENVEKIAELNPDLIIGL----------- 85
Cdd:cd01149 1 PERIVSLG---GSVteivyaLGAGDRLVGVDS-TSTYPEAAAKLPDVGYMRQLSAEGVLSLKPTLVIASdeagppealdq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 86 ---SNIKNVdklkkiapTVTYTYGKVDYLTQHLEIGKLLNKEKEAKTWVDDFKKRAQTAGKDIKAKIGEDATVSVVENFN 162
Cdd:cd01149 77 lraAGVPVV--------TVPSTPTLDGLLTKIRQVAQALGVPEKGEALAQEVRQRLAALRKTVAAHKKPPRVLFLLSHGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 163 KQLYVYGENWGRGTEIlyqemklKMPEKVKEKALKEGYYALSTEVLPEFAGDYLIVSKN-----KDTDNSFQeTESYKNI 237
Cdd:cd01149 149 GAAMAAGRNTAADAII-------ALAGAVNAAAGFRGYKPLSAEALIAAQPDVILVMSRgldavGGVDGLLK-LPGLAQT 220
|
....*....
gi 1634475675 238 PAVKNNRVY 246
Cdd:cd01149 221 PAGRNKRIL 229
|
|
| ChuT |
COG4558 |
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ... |
21-246 |
3.61e-06 |
|
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443619 [Multi-domain] Cd Length: 285 Bit Score: 47.11 E-value: 3.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 21 ANPQRVVVLSS------FAgnvmsLGV--NLVGVDSWSkQNPRFDSKLKNVAEVSDENVEKIAELNPDLIIGLSNIKN-- 90
Cdd:COG4558 25 AAAERIVSLGGsvteivYA-----LGAgdRLVGVDTTS-TYPAAAKALPDVGYMRQLSAEGILSLKPTLVLASEGAGPpe 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 91 -VDKLKKI---------APTVTYTYGKVDyltqhlEIGKLLNKEKEAKTWVDDFKKRAQTAGKDIkAKIGEDATVsvven 160
Cdd:COG4558 99 vLDQLRAAgvpvvvvpaAPSLEGVLAKIR------AVAAALGVPEAGEALAARLEADLAALAARV-AAIGKPPRV----- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 161 fnkqLYVYGENWGR----GTEILYQEMklkmpekVK----EKALK--EGYYALSTEVLPEFAGDYLIVSknKDTDNSFQE 230
Cdd:COG4558 167 ----LFLLSRGGGRpmvaGRGTAADAL-------IRlaggVNAAAgfEGYKPLSAEALIAAAPDVILVM--TRGLESLGG 233
|
250 260
....*....|....*....|..
gi 1634475675 231 TESYKNIP------AVKNNRVY 246
Cdd:COG4558 234 VDGLLALPglaqtpAGKNKRIV 255
|
|
| btuF |
PRK09534 |
corrinoid ABC transporter substrate-binding protein; Reviewed |
14-258 |
1.37e-05 |
|
corrinoid ABC transporter substrate-binding protein; Reviewed
Pssm-ID: 236552 [Multi-domain] Cd Length: 359 Bit Score: 45.67 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 14 NGKVEVPANPQRVVVLSSFAGNVM-SLGVN--LVGVDSWSKQNPRFDSKlKNVAEVSD--ENVEKIAELNPDLIIGLSNI 88
Cdd:PRK09534 51 GTEITLDERPERVVTLNPSAAQTMwELGARdrVVGVTQYASYLDGAEER-TNVSGGQPfgVNVEAVVGLDPDLVLAPNAV 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 89 KN--VDKLKKIAPTVtYTYG---KVDYLTQHLE-IGKLLNKEKEAKTWVDDFKKRAQTAgkdikakigEDATVSvVENFN 162
Cdd:PRK09534 130 AGdtVTRLREAGITV-FHFPaatSIEDVAEKTAtIGRLTGNCEAAAETNAEMRDRVDAV---------EDRTAD-VDDRP 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 163 KQLYVYGENWGRGTEILYQE-MKLKMPEKVKEKALKEGYYALSTEVLPEFAGDYLIVSKNKDTdnsFQETESYKNIPAVK 241
Cdd:PRK09534 199 RVLYPLGDGYTAGGNTFIGAlIEAAGGHNVAADATTDGYPQLSEEVIVQQDPDVIVVATASAL---VAETEPYASTTAGE 275
|
250
....*....|....*..
gi 1634475675 242 NNRVYEANMMefYFNDP 258
Cdd:PRK09534 276 TGNVVTVNVN--HINQP 290
|
|
| BtuF |
cd01144 |
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ... |
43-139 |
6.01e-05 |
|
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: 43.44 E-value: 6.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 43 LVGVDSWSKQNPRFDsKLKNVAEVSDENVEKIAELNPDLIIG--LSNIK-NVDKLKKIAPTVTYTYGK-VDYLTQHLE-I 117
Cdd:cd01144 23 LVGVTDYCDYPPEAK-KLPRVGGFYQLDLERVLALKPDLVIAwdDCNVCaVVDQLRAAGIPVLVSEPQtLDDILADIRrL 101
|
90 100
....*....|....*....|..
gi 1634475675 118 GKLLNKEKEAKTWVDDFKKRAQ 139
Cdd:cd01144 102 GTLAGRPARAEELAEALRRRLA 123
|
|
| TroA_f |
cd01139 |
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ... |
16-128 |
5.27e-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: 40.75 E-value: 5.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634475675 16 KVEVPANPQRVVVLSSFAGNVMSLG------VNLVG---------VDSWSKQNPRFdSKLKNVAEV-----SDENVEKIA 75
Cdd:cd01139 10 KVTLDAPVERVLLGEGRQLYALALLegenpfARIVGwggdlkkgdPDTYAKYKEKF-PEIADIPLIgstynGDFSVEKVL 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1634475675 76 ELNPDLII-------GLSNIKNVDKLKKIAPTVTYTYGKVDYLTQHLE----IGKLLNKEKEAK 128
Cdd:cd01139 89 TLKPDLVIlniwaktTAEESGILEKLEQAGIPVVFVDFRQKPLKNTTPsmrlLGKALGREERAE 152
|
|
| |
