|
Name |
Accession |
Description |
Interval |
E-value |
| TroA_a |
cd01148 |
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ... |
59-345 |
1.93e-99 |
|
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: 295.40 E-value: 1.93e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411745 59 YPVTITNynfagEEIKVIFDKTPEKVLTTNQTTIELMLDLGLEKYLVGTCYLDNPILDRLADKYKKVNVVSEKYPTKEQV 138
Cdd:cd01148 1 YPLTVEN-----CGRSVTFDKAPQRVVSNDQNTTEMMLALGLQDRMVGTAGIDNKDLPELKAKYDKVPELAKKYPSKETV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411745 139 LALQPDLIFGWKSVFADKT-LGDVKEWNDRNVKTFAQRNTVKT-VGNYTIENGFKDINDLGTIFNIKDKTDKYVKELRDR 216
Cdd:cd01148 76 LAARPDLVFGGWSYGFDKGgLGTPDSLAELGIKTYILPESCGQrRGEATLDDVYNDIRNLGKIFDVEDRADKLVADLKAR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411745 217 LNKIEEKTSKVKNKKKVL--ILGDKNKGEfrlYGKNDLVGDMVLKAGGENLG----EKSGTMSLENIVSANPDAIVFIHY 290
Cdd:cd01148 156 LAEISAKVKGDGKKVAVFvyDSGEDKPFT---SGRGGIPNAIITAAGGRNVFadvdESWTTVSWETVIARNPDVIVIIDY 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 499411745 291 GDEKEihDAELAKEFTENKALANVNAIKNKKIIITGLAETWAGGvRTVDAVERYA 345
Cdd:cd01148 233 GDQNA--AEQKIKFLKENPALKNVPAVKNNRFIVLPLAEATPGI-RNVDAIEKLA 284
|
|
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
83-354 |
2.67e-48 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 163.63 E-value: 2.67e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411745 83 KVLTTNQTTIELMLDLGLEKYLVGTCylDNPILDRLADKYKKVNVV-SEKYPTKEQVLALQPDLIFGWKSVFADKtlgDV 161
Cdd:COG0614 2 RIVSLSPSATELLLALGAGDRLVGVS--DWGYCDYPELELKDLPVVgGTGEPNLEAILALKPDLVLASSSGNDEE---DY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411745 162 KEWNDRNVKTFAqrntvktVGNYTIENGFKDINDLGTIFNIKDKTDKYVKELRDRLNKIEEKTSKVKNKKKVLILGDKNK 241
Cdd:COG0614 77 EQLEKIGIPVVV-------LDPRSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGAEERPTVLYEIWSGD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411745 242 GeFRLYGKNDLVGDMVLKAGGEN----LGEKSGTMSLENIVSANPDAIVFIHYGDEKEIHDaELAKEFTENKALANVNAI 317
Cdd:COG0614 150 P-LYTAGGGSFIGELLELAGGRNvaadLGGGYPEVSLEQVLALDPDVIILSGGGYDAETAE-EALEALLADPGWQSLPAV 227
|
250 260 270
....*....|....*....|....*....|....*..
gi 499411745 318 KNKKIIITGLAETWAGGVRTVDAVERYAKELYPELFK 354
Cdd:COG0614 228 KNGRVYVVPGDLLSRPGPRLLLALEDLAKALHPELFA 264
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
86-326 |
3.41e-16 |
|
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: 76.64 E-value: 3.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411745 86 TTNQTTIELMLDLGLEKYLVG--TCYLDNPILDRLADKyKKVNVVSEkyPTKEQVLALQPDLIFGwkSVFADKTLGDVKE 163
Cdd:pfam01497 2 ALSPAYTEILYALGATDSIVGvdAYTRDPLKADAVAAI-VKVGAYGE--INVERLAALKPDLVIL--STGYLTDEAEELL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411745 164 wnDRNVKTFAQRNtvktvgNYTIENGFKDINDLGTIFNIKDKTDKYVKELRDRLNKIEEKTSKVKNKKKVLILGDkNKGE 243
Cdd:pfam01497 77 --SLIIPTVIFES------SSTGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPVLVFGGA-DGGG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411745 244 FRLYGKNDLVGDMVLKAGGENLGEKSGT-----MSLENIVSANPDAIVFIHYGDEKeihdAELAKEFTENKALANVNAIK 318
Cdd:pfam01497 148 YVVAGSNTYIGDLLRILGIENIAAELSGseyapISFEAILSSNPDVIIVSGRDSFT----KTGPEFVAANPLWAGLPAVK 223
|
....*...
gi 499411745 319 NKKIIITG 326
Cdd:pfam01497 224 NGRVYTLP 231
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| TroA_a |
cd01148 |
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ... |
59-345 |
1.93e-99 |
|
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: 295.40 E-value: 1.93e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411745 59 YPVTITNynfagEEIKVIFDKTPEKVLTTNQTTIELMLDLGLEKYLVGTCYLDNPILDRLADKYKKVNVVSEKYPTKEQV 138
Cdd:cd01148 1 YPLTVEN-----CGRSVTFDKAPQRVVSNDQNTTEMMLALGLQDRMVGTAGIDNKDLPELKAKYDKVPELAKKYPSKETV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411745 139 LALQPDLIFGWKSVFADKT-LGDVKEWNDRNVKTFAQRNTVKT-VGNYTIENGFKDINDLGTIFNIKDKTDKYVKELRDR 216
Cdd:cd01148 76 LAARPDLVFGGWSYGFDKGgLGTPDSLAELGIKTYILPESCGQrRGEATLDDVYNDIRNLGKIFDVEDRADKLVADLKAR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411745 217 LNKIEEKTSKVKNKKKVL--ILGDKNKGEfrlYGKNDLVGDMVLKAGGENLG----EKSGTMSLENIVSANPDAIVFIHY 290
Cdd:cd01148 156 LAEISAKVKGDGKKVAVFvyDSGEDKPFT---SGRGGIPNAIITAAGGRNVFadvdESWTTVSWETVIARNPDVIVIIDY 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 499411745 291 GDEKEihDAELAKEFTENKALANVNAIKNKKIIITGLAETWAGGvRTVDAVERYA 345
Cdd:cd01148 233 GDQNA--AEQKIKFLKENPALKNVPAVKNNRFIVLPLAEATPGI-RNVDAIEKLA 284
|
|
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
83-354 |
2.67e-48 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 163.63 E-value: 2.67e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411745 83 KVLTTNQTTIELMLDLGLEKYLVGTCylDNPILDRLADKYKKVNVV-SEKYPTKEQVLALQPDLIFGWKSVFADKtlgDV 161
Cdd:COG0614 2 RIVSLSPSATELLLALGAGDRLVGVS--DWGYCDYPELELKDLPVVgGTGEPNLEAILALKPDLVLASSSGNDEE---DY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411745 162 KEWNDRNVKTFAqrntvktVGNYTIENGFKDINDLGTIFNIKDKTDKYVKELRDRLNKIEEKTSKVKNKKKVLILGDKNK 241
Cdd:COG0614 77 EQLEKIGIPVVV-------LDPRSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGAEERPTVLYEIWSGD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411745 242 GeFRLYGKNDLVGDMVLKAGGEN----LGEKSGTMSLENIVSANPDAIVFIHYGDEKEIHDaELAKEFTENKALANVNAI 317
Cdd:COG0614 150 P-LYTAGGGSFIGELLELAGGRNvaadLGGGYPEVSLEQVLALDPDVIILSGGGYDAETAE-EALEALLADPGWQSLPAV 227
|
250 260 270
....*....|....*....|....*....|....*..
gi 499411745 318 KNKKIIITGLAETWAGGVRTVDAVERYAKELYPELFK 354
Cdd:COG0614 228 KNGRVYVVPGDLLSRPGPRLLLALEDLAKALHPELFA 264
|
|
| TroA_e |
cd01142 |
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ... |
61-354 |
1.19e-22 |
|
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: 95.88 E-value: 1.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411745 61 VTITNYnfAGEEIKVifDKTPEKVLTTNQTTIELMLDLGLEKYLVGTCY--LDNPILDRLADKYKKVN-VVSEKYPTKEQ 137
Cdd:cd01142 8 RTITDM--AGRKVTI--PDEVKRIAALWGAGNAVVAALGGGKLIVATTStvQQEPWLYRLAPSLENVAtGGTGNDVNIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411745 138 VLALQPDLIFGWKSvfADKTLGDVKewnDRNVKTFAQRNTVKTVGNYTIENgfkdindLGTIFNIKDKTDKYVKELRDRL 217
Cdd:cd01142 84 LLALKPDVVIVWST--DGKEAGKAV---LRLLNALSLRDAELEEVKLTIAL-------LGELLGRQEKAEALVAYFDDNL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411745 218 NKIEEKTSKvknkkkvliLGDKNKgeFRLY----------GKNDLVGDMVLKAGGENL-----GEKSGTMSLENIVSANP 282
Cdd:cd01142 152 AYVAARTKK---------LPDSER--PRVYyagpdplttdGTGSITNSWIDLAGGINVaseatKKGSGEVSLEQLLKWNP 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499411745 283 DAIVFIHYGDEKEIhdaelakefTENKALANVNAIKNKKIIITGLAETWAGGVRTVDAVERY--AKELYPELFK 354
Cdd:cd01142 221 DVIIVGNADTKAAI---------LADPRWQNLRAVKNGRVYVNPEGAFWWDRPSAEEALLGLwlAKTLYPERFT 285
|
|
| ChuT |
COG4558 |
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ... |
81-352 |
7.12e-19 |
|
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443619 [Multi-domain] Cd Length: 285 Bit Score: 85.24 E-value: 7.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411745 81 PEKVLTTNQTTIELMLDLGLEKYLVGTcylD-----NPILDRLAD--KYKKVNVvsekyptkEQVLALQPDLIFGWKSVF 153
Cdd:COG4558 27 AERIVSLGGSVTEIVYALGAGDRLVGV---DttstyPAAAKALPDvgYMRQLSA--------EGILSLKPTLVLASEGAG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411745 154 ADKTLGDVKEwNDRNVKTFAQRNTVKTVGnytiengfKDINDLGTIFNIKDKTDKYVKELRDRLNKIEEKTSKVKNKKKV 233
Cdd:COG4558 96 PPEVLDQLRA-AGVPVVVVPAAPSLEGVL--------AKIRAVAAALGVPEAGEALAARLEADLAALAARVAAIGKPPRV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411745 234 LILGDKNKGEFRLYGKNDLVGDMVLKAGGENLGEK-SGT--MSLENIVSANPDAIVFIHYGDEKEIHDAELAKefteNKA 310
Cdd:COG4558 167 LFLLSRGGGRPMVAGRGTAADALIRLAGGVNAAAGfEGYkpLSAEALIAAAPDVILVMTRGLESLGGVDGLLA----LPG 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 499411745 311 LANVNAIKNKKII------ITGLaetwagGVRTVDAVERYAKELYPEL 352
Cdd:COG4558 243 LAQTPAGKNKRIVamddllLLGF------GPRTPQAALALAQALYPAA 284
|
|
| FecB |
COG4594 |
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ... |
12-349 |
4.36e-18 |
|
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443650 [Multi-domain] Cd Length: 316 Bit Score: 83.82 E-value: 4.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411745 12 KLILGVIAVSMVASLSACSGNDSSKNGESANKNNIETSGKKGdkqshypvtitnynfageEIKVifDKTPEKVLTTNQTT 91
Cdd:COG4594 3 KLLLLLILLLALLLLAACGSSSSDSSSSEAAAGARTVKHAMG------------------ETTI--PGTPKRVVVLEWSF 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411745 92 IELMLDLGLEKylVGtcYLD----NPILDRLADKYKKVNVV-SEKYPTKEQVLALQPDLIFGWKSvfadktlgdvkewnd 166
Cdd:COG4594 63 ADALLALGVTP--VG--IADdndyDRWVPYLRDLIKGVTSVgTRSQPNLEAIAALKPDLIIADKS--------------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411745 167 RNVKTFAQRN----TVKT-VGNYTIENGFKDINDLGTIFNIKDKTDKYVKELRDRLNKIEEKTSKVKNKKKVLILGDkNK 241
Cdd:COG4594 124 RHEAIYDQLSkiapTVLFkSRNGDYQENLESFKTIAKALGKEEEAEAVLADHDQRIAEAKAKLAAADKGKKVAVGQF-RA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411745 242 GEFRLYGKNDLVGDmVLKAGGENLGEKSG--------TMSLENIVSANPDAIVFIHYGDEKeihdaeLAKEFTENKALAN 313
Cdd:COG4594 203 DGLRLYTPNSFAGS-VLAALGFENPPKQSkdngygysEVSLEQLPALDPDVLFIATYDDPS------ILKEWKNNPLWKN 275
|
330 340 350
....*....|....*....|....*....|....*.
gi 499411745 314 VNAIKNKKIIITGlAETWAGGvRTVDAVERYAKELY 349
Cdd:COG4594 276 LKAVKNGRVYEVD-GDLWTRG-RGPLAAELMADDLV 309
|
|
| BtuF |
cd01144 |
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ... |
93-346 |
5.02e-18 |
|
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: 82.35 E-value: 5.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411745 93 ELMLDLGLEKYLVG-TCYLDNPildrlADKYKKVNVVSEKYPTKEQVLALQPDLIFGWKSVFADKTLGDVKEwndRNVKT 171
Cdd:cd01144 12 ELLYALGLGDQLVGvTDYCDYP-----PEAKKLPRVGGFYQLDLERVLALKPDLVIAWDDCNVCAVVDQLRA---AGIPV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411745 172 FAQRNTvktvgnyTIENGFKDINDLGTIFNIKDKTDKYVKELRDRLNKIEEKTSKVKNKKKVLILGDKnkgEFrLYGKND 251
Cdd:cd01144 84 LVSEPQ-------TLDDILADIRRLGTLAGRPARAEELAEALRRRLAALRKQYASKPPPRVFYQEWID---PL-MTAGGD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411745 252 LVGDMVLKAGGENL----GEKSGTMSLENIVSANPDAIVFIHYGDEKEihDAELAKEftenKALANVNAIKNKKIIitGL 327
Cdd:cd01144 153 WVPELIALAGGVNVfadaGERSPQVSWEDVLAANPDVIVLSPCGFGFT--PAILRKE----PAWQALPAVRNGRVY--AV 224
|
250 260
....*....|....*....|.
gi 499411745 328 AETWAG--GVRTVDAVERYAK 346
Cdd:cd01144 225 DGNWYFrpSPRLVDGLEQLAA 245
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
86-326 |
3.41e-16 |
|
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: 76.64 E-value: 3.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411745 86 TTNQTTIELMLDLGLEKYLVG--TCYLDNPILDRLADKyKKVNVVSEkyPTKEQVLALQPDLIFGwkSVFADKTLGDVKE 163
Cdd:pfam01497 2 ALSPAYTEILYALGATDSIVGvdAYTRDPLKADAVAAI-VKVGAYGE--INVERLAALKPDLVIL--STGYLTDEAEELL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411745 164 wnDRNVKTFAQRNtvktvgNYTIENGFKDINDLGTIFNIKDKTDKYVKELRDRLNKIEEKTSKVKNKKKVLILGDkNKGE 243
Cdd:pfam01497 77 --SLIIPTVIFES------SSTGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPVLVFGGA-DGGG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411745 244 FRLYGKNDLVGDMVLKAGGENLGEKSGT-----MSLENIVSANPDAIVFIHYGDEKeihdAELAKEFTENKALANVNAIK 318
Cdd:pfam01497 148 YVVAGSNTYIGDLLRILGIENIAAELSGseyapISFEAILSSNPDVIIVSGRDSFT----KTGPEFVAANPLWAGLPAVK 223
|
....*...
gi 499411745 319 NKKIIITG 326
Cdd:pfam01497 224 NGRVYTLP 231
|
|
| TroA-like |
cd00636 |
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ... |
82-237 |
1.87e-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: 72.59 E-value: 1.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411745 82 EKVLTTNQTTIELMLDLGLEKYLVGTCYLDNPILDRLADKYKKVNVVSEKYPTKEQVLALQPDLIFGWKSVFADktlgdv 161
Cdd:cd00636 1 KRVVALDPGATELLLALGGDDKPVGVADPSGYPPEAKALLEKVPDVGHGYEPNLEKIAALKPDLIIANGSGLEA------ 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499411745 162 keWNDRNVKTFAQRNTVKTVGNYTIENGFKDINDLGTIFNIKDKTDKYVKELRDRLNKIEEKTSKVKNKKKVLILG 237
Cdd:cd00636 75 --WLDKLSKIAIPVVVVDEASELSLENIKESIRLIGKALGKEENAEELIAELDARLAELRAKLAKIPKKKVSLVVG 148
|
|
| FhuD |
cd01146 |
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ... |
79-334 |
1.76e-14 |
|
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: 72.32 E-value: 1.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411745 79 KTPEKVLTTNQTTIELMLDLGLEkyLVGTCYLDN--PILDRLADKYKKVNVVSEKY-PTKEQVLALQPDLIFGwksvfad 155
Cdd:cd01146 1 AKPQRIVALDWGALETLLALGVK--PVGVADTAGykPWIPEPALPLEGVVDVGTRGqPNLEAIAALKPDLILG------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411745 156 ktlgdVKEWNDRNVKTFAQrnTVKTVG--NYTIENGFKD-INDLGTIFNIKDK-------TDKYVKELRDRLNKIEEkts 225
Cdd:cd01146 72 -----SASRHDEIYDQLSQ--IAPTVLldSSPWLAEWKEnLRLIAKALGKEEEaekllaeYDQRLAELRQKLPDKGP--- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411745 226 kvknkKKVLILGDKNKGEFRLYGKNDLVGDMVLKAG-----GENLGEKSG--TMSLENIVSANPDAIVFIHYGDEkeihd 298
Cdd:cd01146 142 -----KPVSVVRFSDAGSIRLYGPNSFAGSVLEDLGlqnpwAQETTNDSGfaTISLERLAKADADVLFVFTYEDE----- 211
|
250 260 270
....*....|....*....|....*....|....*.
gi 499411745 299 aELAKEFTENKALANVNAIKNKKIIITGlAETWAGG 334
Cdd:cd01146 212 -ELAQALQANPLWQNLPAVKNGRVYVVD-DVWWFFG 245
|
|
| CeuA |
COG4607 |
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and ... |
12-323 |
5.32e-14 |
|
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443657 [Multi-domain] Cd Length: 310 Bit Score: 71.75 E-value: 5.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411745 12 KLILGVIAVSMVASLSACSGNDSSKNGESANKnnietsgkkgdkqshyPVTITNYNfaGEeikVIFDKTPEKVLTTNQTT 91
Cdd:COG4607 3 KTLLAALALAAALALAACGSSSAAAASAAAAE----------------TVTVEHAL--GT---VEVPKNPKRVVVFDNGA 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411745 92 IELMLDLGLEkyLVGTcyldnP---ILDRLAdKYKK---VNVVSEKYPTKEQVLALQPDLIF--GWKSVFADK------T 157
Cdd:COG4607 62 LDTLDALGVE--VAGV-----PkglLPDYLS-KYADdkyANVGTLFEPDLEAIAALKPDLIIigGRSAKKYDElskiapT 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411745 158 LgDVKEWNDRNVKTFAQRntvktvgnytiengfkdINDLGTIFNIKDKTDKYVKELRDrlnKIEEKTSKVKNKKKVLILg 237
Cdd:COG4607 134 I-DLTVDGEDYLESLKRN-----------------TETLGEIFGKEDEAEELVADLDA---KIAALKAAAAGKGTALIV- 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411745 238 DKNKGEFRLYGKN-------DLVGdmvLKAGGENLgeKSGT----MSLENIVSANPDaIVFIhygdekeI-------HDA 299
Cdd:COG4607 192 LTNGGKISAYGPGsrfgpihDVLG---FKPADEDI--EASThgqaISFEFIAEANPD-WLFV-------IdrdaaigGEG 258
|
330 340
....*....|....*....|....
gi 499411745 300 ELAKEFTENKALANVNAIKNKKII 323
Cdd:COG4607 259 PAAKQVLDNELVKQTTAWKNGQIV 282
|
|
| FatB |
cd01140 |
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ... |
74-323 |
8.85e-14 |
|
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: 70.36 E-value: 8.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411745 74 KVIFDKTPEKVLTTNQTTIELMLDLGLEkyLVGTCylDNPILDRLADKYKK---VNVVSEKYPTKEQVLALQPDLIFGWK 150
Cdd:cd01140 5 ETKVPKNPEKVVVFDVGALDTLDALGVK--VVGVP--KSSTLPEYLKKYKDdkyANVGTLFEPDLEAIAALKPDLIIIGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411745 151 SvFADKtLGDVKEWNDRNVKTFAQRNTVKTVgnytiengFKDINDLGTIFNIKDKTDKYVKELRDRLNKIEEKTSKVKNK 230
Cdd:cd01140 81 R-LAEK-YDELKKIAPTIDLGADLKNYLESV--------KQNIETLGKIFGKEEEAKELVAEIDASIAEAKSAAKGKKKA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411745 231 KKVLIlgdkNKGEFRLYGKNDLVGDMVLKAGGENLGEKSGT------MSLENIVSANPDaIVFIHYGDEKEIHDAELAKE 304
Cdd:cd01140 151 LVVLV----NGGKLSAFGPGSRFGWLHDLLGFEPADENIKAsshgqpVSFEYILEANPD-WLFVIDRGAAIGAEGSSAKE 225
|
250
....*....|....*....
gi 499411745 305 FTENKALANVNAIKNKKII 323
Cdd:cd01140 226 VLDNDLVKNTTAWKNGKVI 244
|
|
| HutB |
cd01149 |
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ... |
81-323 |
1.61e-13 |
|
Hemin binding protein HutB. These proteins have been shown to function as initial receptors in ABC transport of hemin and hemoproteins in many eubacterial species. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains.
Pssm-ID: 238569 [Multi-domain] Cd Length: 235 Bit Score: 69.22 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411745 81 PEKVLTTNQTTIELMLDLGLEKYLVGTcylDN-----PILDRLAD--KYKKVNVvsekyptkEQVLALQPDLIFGWKSVF 153
Cdd:cd01149 1 PERIVSLGGSVTEIVYALGAGDRLVGV---DStstypEAAAKLPDvgYMRQLSA--------EGVLSLKPTLVIASDEAG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411745 154 ADKTLGDVKEwndRNVKtfaqrntVKTVGNYTIENGFKD-INDLGTIFNIKDKTDKYVKELRDRLNKIEEKTSKVKNKKK 232
Cdd:cd01149 70 PPEALDQLRA---AGVP-------VVTVPSTPTLDGLLTkIRQVAQALGVPEKGEALAQEVRQRLAALRKTVAAHKKPPR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411745 233 VLILGDKNKGEFRLYGKNDLVGDMVLKAGGENLGEK-SG--TMSLENIVSANPDAIVFIHYGDEKEIHDAELAKefteNK 309
Cdd:cd01149 140 VLFLLSHGGGAAMAAGRNTAADAIIALAGAVNAAAGfRGykPLSAEALIAAQPDVILVMSRGLDAVGGVDGLLK----LP 215
|
250
....*....|....
gi 499411745 310 ALANVNAIKNKKII 323
Cdd:cd01149 216 GLAQTPAGRNKRIL 229
|
|
| YvrC |
cd01143 |
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ... |
79-287 |
3.66e-12 |
|
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: 64.61 E-value: 3.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411745 79 KTPEKVLTTNQTTIELMLDLGLEKYLVGTCYLDNpildRLADKYKKVNVVSEKYPTKEQVLALQPDLIFGWKSvfADKTL 158
Cdd:cd01143 1 KEPERIVSLSPSITEILFALGAGDKIVGVDTYSN----YPKEVRKKPKVGSYSNPNVEKIVALKPDLVIVSSS--SLAEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411745 159 gdVKEWNDRNVKTFAQRNTVktvgnyTIENGFKDINDLGTIFNIKDKTDKYVKELRDRLNKIEEKTSKVKNKKKVLILGD 238
Cdd:cd01143 75 --LEKLKDAGIPVVVLPAAS------SLDEIYDQIELIGKITGAEEEAEKLVKEMKQKIDKVKDKGKTIKKSKVYIEVSL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499411745 239 knkGEFRLYGKNDLVGDMVLKAGGENLGEKSG---TMSLENIVSANPDAIVF 287
Cdd:cd01143 147 ---GGPYTAGKNTFINELIRLAGAKNIAADSGgwpQVSPEEILKANPDVIIL 195
|
|
| TroA_f |
cd01139 |
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ... |
136-354 |
3.42e-11 |
|
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: 63.48 E-value: 3.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411745 136 EQVLALQPDLIfgwksVFAdktLGDVKEWNDRNVKTFAQRNTVKTV----GNYTIENGFKDINDLGTIFNIKDKT----- 206
Cdd:cd01139 85 EKVLTLKPDLV-----ILN---IWAKTTAEESGILEKLEQAGIPVVfvdfRQKPLKNTTPSMRLLGKALGREERAeefie 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411745 207 --DKYVKELRDRLNKIEEKTSKvknkkkVLI-LGDKNKGEF-RLYGKNDLvGDMVLKAGGENLGEK-----SGTMSLENI 277
Cdd:cd01139 157 fyQERIDRIRDRLAKINEPKPK------VFIeLGAGGPEECcSTYGNGNW-GELVDAAGGDNIADGlipgtSGELNAEYV 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411745 278 VSANPDAIV----------------FIHYGDEKEihdAELAKEFTENKALANVNAIKNKKIIitglaETWAGGVRT---V 338
Cdd:cd01139 230 IAANPEIIIatggnwakdpsgvslgPDGTTADAK---ESLLRALLKRPGWSSLQAVKNGRVY-----ALWHQFYRSpynF 301
|
250
....*....|....*.
gi 499411745 339 DAVERYAKELYPELFK 354
Cdd:cd01139 302 VALEAFAKWLYPELFK 317
|
|
| HemV-2 |
cd01147 |
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ... |
82-322 |
1.27e-07 |
|
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: 52.34 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411745 82 EKVLTTNQTTIELMLDLGLEKYLVGTCYLDNPILDR----LADKYKKVNVVSEKYPTK----EQVLALQPDLIFGWKSVf 153
Cdd:cd01147 6 ERVVAAGPGALRLLYALAAPDKIVGVDDAEKSDEGRpyflASPELKDLPVIGRGGRGNtpnyEKIAALKPDVVIDVGSD- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411745 154 adktlGDVKEWNDRNVKTfaQRNTVKTVGNYTIENGFKDINDLGTIFNIKDKTDKYVKELRDRLNKIEEKTSK--VKNKK 231
Cdd:cd01147 85 -----DPTSIADDLQKKT--GIPVVVLDGGDSLEDTPEQIRLLGKVLGKEERAEELISFIESILADVEERTKDipDEEKP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411745 232 KVLILGDKNKGEFRLYGKNDLVGDMVLKAGGENL-----GEKSGTMSLENIVSANPDaIVFIhygDEKEIHDAeLAKEFT 306
Cdd:cd01147 158 TVYFGRIGTKGAAGLESGLAGSIEVFELAGGINVadglgGGGLKEVSPEQILLWNPD-VIFL---DTGSFYLS-LEGYAK 232
|
250
....*....|....*.
gi 499411745 307 ENKALANVNAIKNKKI 322
Cdd:cd01147 233 NRPFWQSLKAVKNGRV 248
|
|
| FeuA |
cd01138 |
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ... |
79-324 |
4.21e-05 |
|
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: 44.25 E-value: 4.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411745 79 KTPEKVLTTNQTTIELMLdLGLEKYLVGTCYLDNPILDrladKYKKVNVVSEKYPTK-EQVLALQPDLIFGWksvfaDKT 157
Cdd:cd01138 7 AKPKRIVALSGETEGLAL-LGIKPVGAASIGGKNPYYK----KKTLAKVVGIVDEPNlEKVLELKPDLIIVS-----SKQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411745 158 LGDVKEWNdRNVKTFaqrntvktVGNYTIENGFKDINDLGTIFNIKDKTDKYVKELRDRLNKIEEKTSKVKNKKKVLILG 237
Cdd:cd01138 77 EENYEKLS-KIAPTV--------PVSYNSSDWEEQLKEIGKLLNKEDEAEKWLADYKQKAKEAKEKIKKKLGNDKSVAVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411745 238 DKNKgEFRLYGKNDLVGDMVLKAG----------GENLGEKSGTMSLENIVSANPDAIVFIHYGDEKEIhdaelaKEFTE 307
Cdd:cd01138 148 RGRK-QIYVFGEDGRGGGPILYADlglkapekvkEIEDKPGYAAISLEVLPEFDADYIFLLFFTGPEAK------ADFES 220
|
250
....*....|....*..
gi 499411745 308 NKALANVNAIKNKKIII 324
Cdd:cd01138 221 LPIWKNLPAVKNNHVYI 237
|
|
| |
