|
Name |
Accession |
Description |
Interval |
E-value |
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
47-299 |
8.88e-62 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 197.14 E-value: 8.88e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 47 RVVSLAPNLTEIAHAAGAGDRLVAITSSG--DHPP-SVDTLPHV-SALPVDFEAVAAQEPDLVLATDQINAPGDTDTFEA 122
Cdd:COG0614 2 RIVSLSPSATELLLALGAGDRLVGVSDWGycDYPElELKDLPVVgGTGEPNLEAILALKPDLVLASSSGNDEEDYEQLEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 123 LNVPIYFFSFGSVGDILTSIETMGQLLGTEAAAADSAAALQSSLDALRARTGSlpDAERPRVLVLVG-DDTLYSFGRGSY 201
Cdd:COG0614 82 IGIPVVVLDPRSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAG--AEERPTVLYEIWsGDPLYTAGGGSF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 202 VHTLVRAAGGTSITADIENQAPTLSDEYVLQEKPDVILgLWGRDYDPDRLLDL------HPTWDVVPAVQNDRVLSLPTS 275
Cdd:COG0614 160 IGELLELAGGRNVAADLGGGYPEVSLEQVLALDPDVII-LSGGGYDAETAEEAleallaDPGWQSLPAVKNGRVYVVPGD 238
|
250 260
....*....|....*....|....
gi 2293840735 276 LIARPGPRVLQGARRLARHLHPDR 299
Cdd:COG0614 239 LLSRPGPRLLLALEDLAKALHPEL 262
|
|
| BtuF |
cd01144 |
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ... |
46-293 |
2.51e-51 |
|
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: 169.79 E-value: 2.51e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 46 QRVVSLAPNLTEIAHAAGAGDRLVAITSSGDHPPSVDTLPHVSA-LPVDFEAVAAQEPDLVLATDQINAPGDTDTFEALN 124
Cdd:cd01144 1 MRIVSLAPSATELLYALGLGDQLVGVTDYCDYPPEAKKLPRVGGfYQLDLERVLALKPDLVIAWDDCNVCAVVDQLRAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 125 VPIYFFSFGSVGDILTSIETMGQLLGTEAAAADSAAALQSSLDALRARTgslPDAERPRVLVLVGDDTLYSFGRGsYVHT 204
Cdd:cd01144 81 IPVLVSEPQTLDDILADIRRLGTLAGRPARAEELAEALRRRLAALRKQY---ASKPPPRVFYQEWIDPLMTAGGD-WVPE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 205 LVRAAGGTSITADIENQAPTLSDEYVLQEKPDVILGLWGRDYDPDRLLDLHPTWDVVPAVQNDRVLSLPTSLIARPGPRV 284
Cdd:cd01144 157 LIALAGGVNVFADAGERSPQVSWEDVLAANPDVIVLSPCGFGFTPAILRKEPAWQALPAVRNGRVYAVDGNWYFRPSPRL 236
|
....*....
gi 2293840735 285 LQGARRLAR 293
Cdd:cd01144 237 VDGLEQLAA 245
|
|
| peripla_PGF_1 |
TIGR04281 |
putative ABC transporter PGF-CTERM-modified substrate-binding protein; Members of this ... |
28-309 |
2.44e-29 |
|
putative ABC transporter PGF-CTERM-modified substrate-binding protein; Members of this archaeal protein family resemble periplasmic substrate-binding proteins of ABC transporters and appear in gene neighborhoods with permease and ATP-binding cassette proteins. Notably, essentially all members also have the PGF-CTERM putative protein-sorting domain at the C-terminus, while more distant homologs (excluded by the trusted cutoff) instead have what appear to be lipoprotein signal peptides at the N-terminus.
Pssm-ID: 275101 [Multi-domain] Cd Length: 330 Bit Score: 114.38 E-value: 2.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 28 PRTVTDALDRTVALDPTVQRVVSLAPNLTEIAHAAGAGDRLVAITSSGDHPPSVDTLPHVSA---LPVDFEAVAAQEPDL 104
Cdd:TIGR04281 4 PVTETDATGTEVTLEEEPERVVTLNPSAAQTMWEIGARDKVVGVSQYTDYLDGADERTNVSGddgLTVNVEAVVDLDPDL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 105 VLATDQINApGDTDTFEALNVPIYFFSFG-SVGDILTSIETMGQLLGTEAAAADSAAALQSSLDALRARtgsLPDAERPR 183
Cdd:TIGR04281 84 VLAPNTAND-DTVEQLRDAGLTVYVFPAAtSIDDVAEKTETTGRLTGECEGAAETVDWMDDRLEAVEEA---LADEDRPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 184 VLVLVGDDtlYSFGRGSYVHTLVRAAGGTSITADIENQA-PTLSDEYVLQEKPDVILGLWGRDYDPDrlldlhPTWDVVP 262
Cdd:TIGR04281 160 VLYAMGDG--YTAGSGTFIHDIITTAGGENVAAEAGITGyPQISEEVVVEQDPEWIVYPDTAEVPPT------PAYESTT 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2293840735 263 AVQNDRVLSLPTSLIARPGPRVLQGARRLARHLHPDRVSAPSDSAGP 309
Cdd:TIGR04281 232 AVEEGNVVAVNANYLSQPAPRVVEAVETLAEAFHPEAYEEAETADTE 278
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
49-273 |
8.13e-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: 102.83 E-value: 8.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 49 VSLAPNLTEIAHAAGAGDRLVAITSSGDHPPSVDTLPHV----SALPVDFEAVAAQEPDLVLATDQINaPGDTDTFEALN 124
Cdd:pfam01497 1 AALSPAYTEILYALGATDSIVGVDAYTRDPLKADAVAAIvkvgAYGEINVERLAALKPDLVILSTGYL-TDEAEELLSLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 125 VPIYFFSFGSVGD-ILTSIETMGQLLGTEAAAADSAAALQSSLDALRARTGSLPDAERPrVLVLVGDDTLYSFGRGSYVH 203
Cdd:pfam01497 80 IPTVIFESSSTGEsLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPVL-VFGGADGGGYVVAGSNTYIG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2293840735 204 TLVRAAGGTSITADI-ENQAPTLSDEYVLQEKPDVILGLW---GRDYDPDRLLDlHPTWDVVPAVQNDRVLSLP 273
Cdd:pfam01497 159 DLLRILGIENIAAELsGSEYAPISFEAILSSNPDVIIVSGrdsFTKTGPEFVAA-NPLWAGLPAVKNGRVYTLP 231
|
|
| btuF |
PRK09534 |
corrinoid ABC transporter substrate-binding protein; Reviewed |
21-304 |
1.63e-21 |
|
corrinoid ABC transporter substrate-binding protein; Reviewed
Pssm-ID: 236552 [Multi-domain] Cd Length: 359 Bit Score: 93.43 E-value: 1.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 21 DPAPDDG----PRTVTDALDRTVALDPTVQRVVSLAPNLTEIAHAAGAGDRLVAITSSGDHPPSVDTLPHVSALP---VD 93
Cdd:PRK09534 32 QHADADRacsfPVTETDATGTEITLDERPERVVTLNPSAAQTMWELGARDRVVGVTQYASYLDGAEERTNVSGGQpfgVN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 94 FEAVAAQEPDLVLATDQInaPGDTDT-FEALNVPIYFFSFG-SVGDILTSIETMGQLLGTEAAAADSAAALQSSLDALRA 171
Cdd:PRK09534 112 VEAVVGLDPDLVLAPNAV--AGDTVTrLREAGITVFHFPAAtSIEDVAEKTATIGRLTGNCEAAAETNAEMRDRVDAVED 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 172 RTGSLPDaeRPRVLVLVGDDtlYSFGRGSYVHTLVRAAGGTSITADIE-NQAPTLSDEYVLQEKPDVILGLwgrdyDPDR 250
Cdd:PRK09534 190 RTADVDD--RPRVLYPLGDG--YTAGGNTFIGALIEAAGGHNVAADATtDGYPQLSEEVIVQQDPDVIVVA-----TASA 260
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2293840735 251 LLDLHPTWDVVPAVQNDRVLSLPTSLIARPGPRVLQGARRLARHLH-PDRVSAPS 304
Cdd:PRK09534 261 LVAETEPYASTTAGETGNVVTVNVNHINQPAPRIVESMATMATAFHnTTTNDTLD 315
|
|
| TroA_like |
NF038402 |
helical backbone metal receptor; |
47-239 |
1.12e-08 |
|
helical backbone metal receptor;
Pssm-ID: 439691 Cd Length: 219 Bit Score: 54.55 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 47 RVVSLAPNLTEiAHAAGAGDRLVAITSSGDHPPSVDtLPHVSAL--PvDFEAVAAQEPDLVLATDQINAPGDTDTFEALN 124
Cdd:NF038402 1 RVVSLVPSLTE-AIAATAPELLVGATDWCTHPADLD-VARVRGTknP-DRAAIAALRPDLVVANQEENRELDVDRLRAAG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 125 VPIYFFSFGSVGDILTSIETM-GQLLGTEAAaadsaaalqSSLDALRARTGSLPDAERPRVLVLVGDDTLYSFGRGSYVH 203
Cdd:NF038402 78 VPVWVTRIETVDEALASLRRLfTEALGVPVP---------GWLDEAEREWAAPAPAPRRRAVVPIWRDPWMVVGRDTFTG 148
|
170 180 190
....*....|....*....|....*....|....*.
gi 2293840735 204 TLVRAAGGTSITADIENQAPTLSDEYVLQEKPDVIL 239
Cdd:NF038402 149 DLLARLGLRNVFADHPERYPHVDLDELDAAGPDLVL 184
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
47-299 |
8.88e-62 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 197.14 E-value: 8.88e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 47 RVVSLAPNLTEIAHAAGAGDRLVAITSSG--DHPP-SVDTLPHV-SALPVDFEAVAAQEPDLVLATDQINAPGDTDTFEA 122
Cdd:COG0614 2 RIVSLSPSATELLLALGAGDRLVGVSDWGycDYPElELKDLPVVgGTGEPNLEAILALKPDLVLASSSGNDEEDYEQLEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 123 LNVPIYFFSFGSVGDILTSIETMGQLLGTEAAAADSAAALQSSLDALRARTGSlpDAERPRVLVLVG-DDTLYSFGRGSY 201
Cdd:COG0614 82 IGIPVVVLDPRSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAG--AEERPTVLYEIWsGDPLYTAGGGSF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 202 VHTLVRAAGGTSITADIENQAPTLSDEYVLQEKPDVILgLWGRDYDPDRLLDL------HPTWDVVPAVQNDRVLSLPTS 275
Cdd:COG0614 160 IGELLELAGGRNVAADLGGGYPEVSLEQVLALDPDVII-LSGGGYDAETAEEAleallaDPGWQSLPAVKNGRVYVVPGD 238
|
250 260
....*....|....*....|....
gi 2293840735 276 LIARPGPRVLQGARRLARHLHPDR 299
Cdd:COG0614 239 LLSRPGPRLLLALEDLAKALHPEL 262
|
|
| BtuF |
cd01144 |
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ... |
46-293 |
2.51e-51 |
|
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: 169.79 E-value: 2.51e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 46 QRVVSLAPNLTEIAHAAGAGDRLVAITSSGDHPPSVDTLPHVSA-LPVDFEAVAAQEPDLVLATDQINAPGDTDTFEALN 124
Cdd:cd01144 1 MRIVSLAPSATELLYALGLGDQLVGVTDYCDYPPEAKKLPRVGGfYQLDLERVLALKPDLVIAWDDCNVCAVVDQLRAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 125 VPIYFFSFGSVGDILTSIETMGQLLGTEAAAADSAAALQSSLDALRARTgslPDAERPRVLVLVGDDTLYSFGRGsYVHT 204
Cdd:cd01144 81 IPVLVSEPQTLDDILADIRRLGTLAGRPARAEELAEALRRRLAALRKQY---ASKPPPRVFYQEWIDPLMTAGGD-WVPE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 205 LVRAAGGTSITADIENQAPTLSDEYVLQEKPDVILGLWGRDYDPDRLLDLHPTWDVVPAVQNDRVLSLPTSLIARPGPRV 284
Cdd:cd01144 157 LIALAGGVNVFADAGERSPQVSWEDVLAANPDVIVLSPCGFGFTPAILRKEPAWQALPAVRNGRVYAVDGNWYFRPSPRL 236
|
....*....
gi 2293840735 285 LQGARRLAR 293
Cdd:cd01144 237 VDGLEQLAA 245
|
|
| ChuT |
COG4558 |
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ... |
34-298 |
3.45e-42 |
|
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443619 [Multi-domain] Cd Length: 285 Bit Score: 147.26 E-value: 3.45e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 34 ALDRTVALDPTvQRVVSLAPNLTEIAHAAGAGDRLVAITSSGDHPPSVDTLPHV---SALPVdfEAVAAQEPDLVLATDQ 110
Cdd:COG4558 17 AAGASVAAAAA-ERIVSLGGSVTEIVYALGAGDRLVGVDTTSTYPAAAKALPDVgymRQLSA--EGILSLKPTLVLASEG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 111 INAPGDTDTFEALNVPIYFFSFG-SVGDILTSIETMGQLLGTEAAAADSAAALQSSLDALRARTGSLPdaERPRVLVLV- 188
Cdd:COG4558 94 AGPPEVLDQLRAAGVPVVVVPAApSLEGVLAKIRAVAAALGVPEAGEALAARLEADLAALAARVAAIG--KPPRVLFLLs 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 189 -GDDTLYSFGRGSYVHTLVRAAGGTSITADIENQAPtLSDEYVLQEKPDVIL----GLwGRDYDPDRLLDLhPTWDVVPA 263
Cdd:COG4558 172 rGGGRPMVAGRGTAADALIRLAGGVNAAAGFEGYKP-LSAEALIAAAPDVILvmtrGL-ESLGGVDGLLAL-PGLAQTPA 248
|
250 260 270
....*....|....*....|....*....|....*
gi 2293840735 264 VQNDRVLSLPTSLIARPGPRVLQGARRLARHLHPD 298
Cdd:COG4558 249 GKNKRIVAMDDLLLLGFGPRTPQAALALAQALYPA 283
|
|
| YvrC |
cd01143 |
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ... |
46-240 |
1.52e-34 |
|
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: 124.70 E-value: 1.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 46 QRVVSLAPNLTEIAHAAGAGDRLVAITSSGDHPPSVDTLPHVSAL-PVDFEAVAAQEPDLVLATDqINAPGDTDTFEALN 124
Cdd:cd01143 4 ERIVSLSPSITEILFALGAGDKIVGVDTYSNYPKEVRKKPKVGSYsNPNVEKIVALKPDLVIVSS-SSLAELLEKLKDAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 125 VP-IYFFSFGSVGDILTSIETMGQLLGTEAAAADSAAALQSSLDALRARTgslPDAERPRVLVLVGDDTLYSFGRGSYVH 203
Cdd:cd01143 83 IPvVVLPAASSLDEIYDQIELIGKITGAEEEAEKLVKEMKQKIDKVKDKG---KTIKKSKVYIEVSLGGPYTAGKNTFIN 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 2293840735 204 TLVRAAGGTSITADiENQAPTLSDEYVLQEKPDVILG 240
Cdd:cd01143 160 ELIRLAGAKNIAAD-SGGWPQVSPEEILKANPDVIIL 195
|
|
| TroA_a |
cd01148 |
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ... |
28-292 |
1.30e-33 |
|
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: 124.76 E-value: 1.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 28 PRTVtDALDRTVALDPTVQRVVSLAPNLTEIAHAAGAGDRLVAIT--SSGDHPP---SVDTLPHVSALPVDFEAVAAQEP 102
Cdd:cd01148 2 PLTV-ENCGRSVTFDKAPQRVVSNDQNTTEMMLALGLQDRMVGTAgiDNKDLPElkaKYDKVPELAKKYPSKETVLAARP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 103 DLVLATDQ----INAPGDTDTFEALNVPIYFFSFG--------SVGDILTSIETMGQLLGTEAAAADSAAALQSSLDALR 170
Cdd:cd01148 81 DLVFGGWSygfdKGGLGTPDSLAELGIKTYILPEScgqrrgeaTLDDVYNDIRNLGKIFDVEDRADKLVADLKARLAEIS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 171 ARTGSlpDAERPRVLVL-VGDDTLYSFGRGSYVHTLVRAAGGTSITADIENQAPTLSDEYVLQEKPDVILGLwgrDYDPD 249
Cdd:cd01148 161 AKVKG--DGKKVAVFVYdSGEDKPFTSGRGGIPNAIITAAGGRNVFADVDESWTTVSWETVIARNPDVIVII---DYGDQ 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2293840735 250 -------RLLDLHPTWDVVPAVQNDRVLSLPTSLiARPGPRVLQGARRLA 292
Cdd:cd01148 236 naaeqkiKFLKENPALKNVPAVKNNRFIVLPLAE-ATPGIRNVDAIEKLA 284
|
|
| TroA_e |
cd01142 |
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ... |
29-300 |
2.19e-32 |
|
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: 121.69 E-value: 2.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 29 RTVTDALDRTVALDPTVQRVVSLAPNLTEIAHAAGAGDRLVAITSS---GDHPPSVDTLPHVSALPVDF-----EAVAAQ 100
Cdd:cd01142 8 RTITDMAGRKVTIPDEVKRIAALWGAGNAVVAALGGGKLIVATTSTvqqEPWLYRLAPSLENVATGGTGndvniEELLAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 101 EPDLVLATdqinapgDTDTFEALNVPIYFFSFGSVGDILTS-----IETMGQLLGTEAAAADSAAALQSSLDALRARTGS 175
Cdd:cd01142 88 KPDVVIVW-------STDGKEAGKAVLRLLNALSLRDAELEevkltIALLGELLGRQEKAEALVAYFDDNLAYVAARTKK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 176 LPDAERPRVLVlVGDDTLYSFGRGSYVHTLVRAAGGTSITADIEN---QAPTLsdEYVLQEKPDVILglwGRDYDPDRLL 252
Cdd:cd01142 161 LPDSERPRVYY-AGPDPLTTDGTGSITNSWIDLAGGINVASEATKkgsGEVSL--EQLLKWNPDVII---VGNADTKAAI 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2293840735 253 DLHPTWDVVPAVQNDRVLSLPTSLIARPGPRVLQGARR--LARHLHPDRV 300
Cdd:cd01142 235 LADPRWQNLRAVKNGRVYVNPEGAFWWDRPSAEEALLGlwLAKTLYPERF 284
|
|
| peripla_PGF_1 |
TIGR04281 |
putative ABC transporter PGF-CTERM-modified substrate-binding protein; Members of this ... |
28-309 |
2.44e-29 |
|
putative ABC transporter PGF-CTERM-modified substrate-binding protein; Members of this archaeal protein family resemble periplasmic substrate-binding proteins of ABC transporters and appear in gene neighborhoods with permease and ATP-binding cassette proteins. Notably, essentially all members also have the PGF-CTERM putative protein-sorting domain at the C-terminus, while more distant homologs (excluded by the trusted cutoff) instead have what appear to be lipoprotein signal peptides at the N-terminus.
Pssm-ID: 275101 [Multi-domain] Cd Length: 330 Bit Score: 114.38 E-value: 2.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 28 PRTVTDALDRTVALDPTVQRVVSLAPNLTEIAHAAGAGDRLVAITSSGDHPPSVDTLPHVSA---LPVDFEAVAAQEPDL 104
Cdd:TIGR04281 4 PVTETDATGTEVTLEEEPERVVTLNPSAAQTMWEIGARDKVVGVSQYTDYLDGADERTNVSGddgLTVNVEAVVDLDPDL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 105 VLATDQINApGDTDTFEALNVPIYFFSFG-SVGDILTSIETMGQLLGTEAAAADSAAALQSSLDALRARtgsLPDAERPR 183
Cdd:TIGR04281 84 VLAPNTAND-DTVEQLRDAGLTVYVFPAAtSIDDVAEKTETTGRLTGECEGAAETVDWMDDRLEAVEEA---LADEDRPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 184 VLVLVGDDtlYSFGRGSYVHTLVRAAGGTSITADIENQA-PTLSDEYVLQEKPDVILGLWGRDYDPDrlldlhPTWDVVP 262
Cdd:TIGR04281 160 VLYAMGDG--YTAGSGTFIHDIITTAGGENVAAEAGITGyPQISEEVVVEQDPEWIVYPDTAEVPPT------PAYESTT 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2293840735 263 AVQNDRVLSLPTSLIARPGPRVLQGARRLARHLHPDRVSAPSDSAGP 309
Cdd:TIGR04281 232 AVEEGNVVAVNANYLSQPAPRVVEAVETLAEAFHPEAYEEAETADTE 278
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
49-273 |
8.13e-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: 102.83 E-value: 8.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 49 VSLAPNLTEIAHAAGAGDRLVAITSSGDHPPSVDTLPHV----SALPVDFEAVAAQEPDLVLATDQINaPGDTDTFEALN 124
Cdd:pfam01497 1 AALSPAYTEILYALGATDSIVGVDAYTRDPLKADAVAAIvkvgAYGEINVERLAALKPDLVILSTGYL-TDEAEELLSLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 125 VPIYFFSFGSVGD-ILTSIETMGQLLGTEAAAADSAAALQSSLDALRARTGSLPDAERPrVLVLVGDDTLYSFGRGSYVH 203
Cdd:pfam01497 80 IPTVIFESSSTGEsLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPVL-VFGGADGGGYVVAGSNTYIG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2293840735 204 TLVRAAGGTSITADI-ENQAPTLSDEYVLQEKPDVILGLW---GRDYDPDRLLDlHPTWDVVPAVQNDRVLSLP 273
Cdd:pfam01497 159 DLLRILGIENIAAELsGSEYAPISFEAILSSNPDVIIVSGrdsFTKTGPEFVAA-NPLWAGLPAVKNGRVYTLP 231
|
|
| HemV-2 |
cd01147 |
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ... |
45-274 |
1.68e-24 |
|
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: 99.72 E-value: 1.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 45 VQRVVSLAPNLTEIAHAAGAGDRLVAITSSGDHP---PSVDTLPHVSALPV----------DFEAVAAQEPDLVLATDQI 111
Cdd:cd01147 5 VERVVAAGPGALRLLYALAAPDKIVGVDDAEKSDegrPYFLASPELKDLPVigrggrgntpNYEKIAALKPDVVIDVGSD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 112 NAPGDTDT-FEALNVP-IYFFSFGSVGDILTSIETMGQLLGTEAAAADSAAALQSSLDALRARTGSLPDAERPRV----L 185
Cdd:cd01147 85 DPTSIADDlQKKTGIPvVVLDGGDSLEDTPEQIRLLGKVLGKEERAEELISFIESILADVEERTKDIPDEEKPTVyfgrI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 186 VLVGDDTLYSFGRGSYvhTLVRAAGGTSITADI-ENQAPTLSDEYVLQEKPDVILGLWGRDYDPDRLLDLH-PTWDVVPA 263
Cdd:cd01147 165 GTKGAAGLESGLAGSI--EVFELAGGINVADGLgGGGLKEVSPEQILLWNPDVIFLDTGSFYLSLEGYAKNrPFWQSLKA 242
|
250
....*....|.
gi 2293840735 264 VQNDRVLSLPT 274
Cdd:cd01147 243 VKNGRVYLLPA 253
|
|
| HutB |
cd01149 |
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ... |
45-272 |
1.17e-22 |
|
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: 94.25 E-value: 1.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 45 VQRVVSLAPNLTEIAHAAGAGDRLVAITSSGDHPPSVDTLPHVS---ALPVdfEAVAAQEPDLVLATDQINAPGDTDTFE 121
Cdd:cd01149 1 PERIVSLGGSVTEIVYALGAGDRLVGVDSTSTYPEAAAKLPDVGymrQLSA--EGVLSLKPTLVIASDEAGPPEALDQLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 122 ALNVPIYFF-SFGSVGDILTSIETMGQLLGTEAAAADSAAALQSSLDALRARTGSLPdaERPRVLVLV--GDDTLYSFGR 198
Cdd:cd01149 79 AAGVPVVTVpSTPTLDGLLTKIRQVAQALGVPEKGEALAQEVRQRLAALRKTVAAHK--KPPRVLFLLshGGGAAMAAGR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2293840735 199 GSYVHTLVRAAGGTSITADIENQAPtLSDEYVLQEKPDVILGL---WGRDYDPDRLLDLhPTWDVVPAVQNDRVLSL 272
Cdd:cd01149 157 NTAADAIIALAGAVNAAAGFRGYKP-LSAEALIAAQPDVILVMsrgLDAVGGVDGLLKL-PGLAQTPAGRNKRILAM 231
|
|
| btuF |
PRK09534 |
corrinoid ABC transporter substrate-binding protein; Reviewed |
21-304 |
1.63e-21 |
|
corrinoid ABC transporter substrate-binding protein; Reviewed
Pssm-ID: 236552 [Multi-domain] Cd Length: 359 Bit Score: 93.43 E-value: 1.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 21 DPAPDDG----PRTVTDALDRTVALDPTVQRVVSLAPNLTEIAHAAGAGDRLVAITSSGDHPPSVDTLPHVSALP---VD 93
Cdd:PRK09534 32 QHADADRacsfPVTETDATGTEITLDERPERVVTLNPSAAQTMWELGARDRVVGVTQYASYLDGAEERTNVSGGQpfgVN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 94 FEAVAAQEPDLVLATDQInaPGDTDT-FEALNVPIYFFSFG-SVGDILTSIETMGQLLGTEAAAADSAAALQSSLDALRA 171
Cdd:PRK09534 112 VEAVVGLDPDLVLAPNAV--AGDTVTrLREAGITVFHFPAAtSIEDVAEKTATIGRLTGNCEAAAETNAEMRDRVDAVED 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 172 RTGSLPDaeRPRVLVLVGDDtlYSFGRGSYVHTLVRAAGGTSITADIE-NQAPTLSDEYVLQEKPDVILGLwgrdyDPDR 250
Cdd:PRK09534 190 RTADVDD--RPRVLYPLGDG--YTAGGNTFIGALIEAAGGHNVAADATtDGYPQLSEEVIVQQDPDVIVVA-----TASA 260
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2293840735 251 LLDLHPTWDVVPAVQNDRVLSLPTSLIARPGPRVLQGARRLARHLH-PDRVSAPS 304
Cdd:PRK09534 261 LVAETEPYASTTAGETGNVVTVNVNHINQPAPRIVESMATMATAFHnTTTNDTLD 315
|
|
| PRK03379 |
PRK03379 |
vitamin B12-transporter protein BtuF; Provisional |
46-296 |
7.23e-20 |
|
vitamin B12-transporter protein BtuF; Provisional
Pssm-ID: 179575 [Multi-domain] Cd Length: 260 Bit Score: 87.05 E-value: 7.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 46 QRVVSLAPNLTEIAHAAGAGDrlVAITSSGDHPPSVDTLPHVSALP-VDFEAVAAQEPDLVLATDQINAPGDTDTFEALN 124
Cdd:PRK03379 18 PRVITLSPANTELAFAAGITP--VGVSSYSDYPPQAKKIEQVATWQgMNLERIVALKPDLVLAWRGGNAERQVDQLASLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 125 VPIYFFSFGSVGDILTSIETMGQLLGTEAAAADSAAALQSSLDALRARtgsLPDAERPRVLVLVGDDTLYSFGRGSYVHT 204
Cdd:PRK03379 96 IKVMWVDATSIEQIANALRQLAPWSPQPEKAEQAAQSLLQQYAALKAQ---YADKPKKRVFLQFGTNPLFTSGKHSIQSQ 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 205 LVRAAGGTSITADIENQAPTLSDEYVLQEKPDVILgLWGrdyDPDRLLDLHPTWD---VVPavqndrVLSLPTSLIARPG 281
Cdd:PRK03379 173 VLSLCGGENIFADSRVPWPQVSREQVLARKPQAIV-ITG---GPDQIPKIKQFWGpqlKIP------VIPLNSDWFERAS 242
|
250
....*....|....*
gi 2293840735 282 PRVLQGARRLARHLH 296
Cdd:PRK03379 243 PRIILAAQQLCNALS 257
|
|
| FhuD |
cd01146 |
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ... |
46-293 |
1.57e-19 |
|
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: 86.19 E-value: 1.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 46 QRVVSLAPNLTEIAHAAGAgdRLVAITSSGDHPPSVDTLPHVSALPVD--------FEAVAAQEPDLVLATdQINAPGDT 117
Cdd:cd01146 4 QRIVALDWGALETLLALGV--KPVGVADTAGYKPWIPEPALPLEGVVDvgtrgqpnLEAIAALKPDLILGS-ASRHDEIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 118 DTFEALnVP-IYFFSFGSVGDILTSIETMGQLLGTEAAAADSAAALQSSLDALRARtgsLPDAERPRVLVLV--GDDTLY 194
Cdd:cd01146 81 DQLSQI-APtVLLDSSPWLAEWKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQK---LPDKGPKPVSVVRfsDAGSIR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 195 SFGRGSYVHTLVRAAG---GTSITADIENQAPTLSDEYVLQEKPDVILGLWGRDYDPDRLLDLHPTWDVVPAVQNDRVLS 271
Cdd:cd01146 157 LYGPNSFAGSVLEDLGlqnPWAQETTNDSGFATISLERLAKADADVLFVFTYEDEELAQALQANPLWQNLPAVKNGRVYV 236
|
250 260
....*....|....*....|..
gi 2293840735 272 LPTSLIARPGPrvLQGARRLAR 293
Cdd:cd01146 237 VDDVWWFFGGG--LSAARLLLD 256
|
|
| TroA-like |
cd00636 |
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ... |
46-189 |
1.19e-16 |
|
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function in the ABC transport of ferric siderophores and metal ions such as Mn2+, Fe3+, Cu2+ and/or Zn2+. Their ligand binding site is formed in the interface between two globular domains linked by a single helix. Many of these proteins also possess a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence). The TroA-like proteins differ in their fold and ligand-binding mechanism from the PBPI and PBPII proteins, but are structurally similar, however, to the beta-subunit of the nitrogenase molybdenum-iron protein MoFe. Most TroA-like proteins are encoded by ABC-type operons and appear to function as periplasmic components of ABC transporters in metal ion uptake.
Pssm-ID: 238347 [Multi-domain] Cd Length: 148 Bit Score: 75.67 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 46 QRVVSLAPNLTEIAHAAGAGDRLVAITSSGDHPPSVDTLPHVSALP-----VDFEAVAAQEPDLVLATDqINAPGDTDTF 120
Cdd:cd00636 1 KRVVALDPGATELLLALGGDDKPVGVADPSGYPPEAKALLEKVPDVghgyePNLEKIAALKPDLIIANG-SGLEAWLDKL 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2293840735 121 EALNVPIYFFSFG---SVGDILTSIETMGQLLGTEAAAADSAAALQSSLDALRARtgsLPDAERPRVLVLVG 189
Cdd:cd00636 80 SKIAIPVVVVDEAselSLENIKESIRLIGKALGKEENAEELIAELDARLAELRAK---LAKIPKKKVSLVVG 148
|
|
| TroA_f |
cd01139 |
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ... |
30-290 |
1.30e-15 |
|
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: 76.19 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 30 TVTDALDRTVALDPTVQRVV-SLAPNLTEIA--HAAGAGDRLVAitSSGD----HP----------PSVDTLP---HVSA 89
Cdd:cd01139 2 TVTDVAGRKVTLDAPVERVLlGEGRQLYALAllEGENPFARIVG--WGGDlkkgDPdtyakykekfPEIADIPligSTYN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 90 LPVDFEAVAAQEPDLVL----ATDQINAPGDTDTFEALNVPIYFFSFGSVGD--ILTSIETMGQLLGTEAAAADSAAALQ 163
Cdd:cd01139 80 GDFSVEKVLTLKPDLVIlniwAKTTAEESGILEKLEQAGIPVVFVDFRQKPLknTTPSMRLLGKALGREERAEEFIEFYQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 164 SSLDALRARTGSLpDAERPRVLV----LVGDDTLYSFGRGSYvHTLVRAAGGTSITADIENQAP-TLSDEYVLQEKPDVI 238
Cdd:cd01139 160 ERIDRIRDRLAKI-NEPKPKVFIelgaGGPEECCSTYGNGNW-GELVDAAGGDNIADGLIPGTSgELNAEYVIAANPEII 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2293840735 239 L---GLWGRDYDPDRLLdlhptWDVVPAvqnDRVLSLPTSLIARPGPRVLQGARR 290
Cdd:cd01139 238 IatgGNWAKDPSGVSLG-----PDGTTA---DAKESLLRALLKRPGWSSLQAVKN 284
|
|
| FecB |
COG4594 |
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ... |
18-273 |
1.14e-13 |
|
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443650 [Multi-domain] Cd Length: 316 Bit Score: 70.33 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 18 GCGDPAPDD-------GPRTVTDALDrTVALDPTVQRVVSLAPNLTEIAHAAG----------AGDRLVA-ITSSGDHPP 79
Cdd:COG4594 19 ACGSSSSDSssseaaaGARTVKHAMG-ETTIPGTPKRVVVLEWSFADALLALGvtpvgiaddnDYDRWVPyLRDLIKGVT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 80 SVDTLPHVSalpvdFEAVAAQEPDLVLAT--------DQIN--APgdTDTFEALNvpiyffsfGSVGDILTSIETMGQLL 149
Cdd:COG4594 98 SVGTRSQPN-----LEAIAALKPDLIIADksrheaiyDQLSkiAP--TVLFKSRN--------GDYQENLESFKTIAKAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 150 GTEAAAADSAAALQSSLDALRARtgsLPDAERPR-VLVLVG-DDTLYSFGRGSYVHTLVRAAGGTSITADIENQAP---T 224
Cdd:COG4594 163 GKEEEAEAVLADHDQRIAEAKAK---LAAADKGKkVAVGQFrADGLRLYTPNSFAGSVLAALGFENPPKQSKDNGYgysE 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2293840735 225 LSDEYVLQEKPDVILGLWGRDYDPDRLLDLHPTWDVVPAVQNDRVLSLP 273
Cdd:COG4594 240 VSLEQLPALDPDVLFIATYDDPSILKEWKNNPLWKNLKAVKNGRVYEVD 288
|
|
| FatB |
cd01140 |
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ... |
46-273 |
1.40e-12 |
|
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: 66.51 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 46 QRVVSLAPNLTEIAHAAGAgdRLVAITSSGDHPPSVDTLPHVSALPV------DFEAVAAQEPDLVLATDQINApgDTDT 119
Cdd:cd01140 13 EKVVVFDVGALDTLDALGV--KVVGVPKSSTLPEYLKKYKDDKYANVgtlfepDLEAIAALKPDLIIIGGRLAE--KYDE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 120 FEALNVPIYFF--SFGSVGDILTSIETMGQLLGTEAAAADSAAALQSSLDALRARTGSLPDAerprVLVLVGDDTLYSFG 197
Cdd:cd01140 89 LKKIAPTIDLGadLKNYLESVKQNIETLGKIFGKEEEAKELVAEIDASIAEAKSAAKGKKKA----LVVLVNGGKLSAFG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 198 RGSYVHTLVRAAGGTSITADIENQAP--TLSDEYVLQEKPDVILGL-----WGRDYDPDR-LLDlHPTWDVVPAVQNDRV 269
Cdd:cd01140 165 PGSRFGWLHDLLGFEPADENIKASSHgqPVSFEYILEANPDWLFVIdrgaaIGAEGSSAKeVLD-NDLVKNTTAWKNGKV 243
|
....
gi 2293840735 270 LSLP 273
Cdd:cd01140 244 IYLD 247
|
|
| TroA_like |
NF038402 |
helical backbone metal receptor; |
47-239 |
1.12e-08 |
|
helical backbone metal receptor;
Pssm-ID: 439691 Cd Length: 219 Bit Score: 54.55 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 47 RVVSLAPNLTEiAHAAGAGDRLVAITSSGDHPPSVDtLPHVSAL--PvDFEAVAAQEPDLVLATDQINAPGDTDTFEALN 124
Cdd:NF038402 1 RVVSLVPSLTE-AIAATAPELLVGATDWCTHPADLD-VARVRGTknP-DRAAIAALRPDLVVANQEENRELDVDRLRAAG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 125 VPIYFFSFGSVGDILTSIETM-GQLLGTEAAaadsaaalqSSLDALRARTGSLPDAERPRVLVLVGDDTLYSFGRGSYVH 203
Cdd:NF038402 78 VPVWVTRIETVDEALASLRRLfTEALGVPVP---------GWLDEAEREWAAPAPAPRRRAVVPIWRDPWMVVGRDTFTG 148
|
170 180 190
....*....|....*....|....*....|....*.
gi 2293840735 204 TLVRAAGGTSITADIENQAPTLSDEYVLQEKPDVIL 239
Cdd:NF038402 149 DLLARLGLRNVFADHPERYPHVDLDELDAAGPDLVL 184
|
|
| CeuA |
COG4607 |
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and ... |
17-273 |
1.70e-07 |
|
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443657 [Multi-domain] Cd Length: 310 Bit Score: 51.72 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 17 GGCGDPAPDDG------PRTVTDAL-DRTVALDPtvQRVVSLAPNLTEIAHAAGAGdrLVAITSsgDHPPsvDTLPHVSA 89
Cdd:COG4607 18 AACGSSSAAAAsaaaaeTVTVEHALgTVEVPKNP--KRVVVFDNGALDTLDALGVE--VAGVPK--GLLP--DYLSKYAD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 90 LPV---------DFEAVAAQEPDLVlatdqINAPGDTDTFEALN--VPIYFFSFGS---VGDILTSIETMGQLLGTEAAA 155
Cdd:COG4607 90 DKYanvgtlfepDLEAIAALKPDLI-----IIGGRSAKKYDELSkiAPTIDLTVDGedyLESLKRNTETLGEIFGKEDEA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 156 ADSAAALQSSLDALRARTGSLPDAerprVLVLVGDDTLYSFGRGS---YVHTL--VRAAgGTSITADIENQAptLSDEYV 230
Cdd:COG4607 165 EELVADLDAKIAALKAAAAGKGTA----LIVLTNGGKISAYGPGSrfgPIHDVlgFKPA-DEDIEASTHGQA--ISFEFI 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2293840735 231 LQEKPDVILGL-----WGRDYDPDRLLDLHPTWDVVPAVQNDRVLSLP 273
Cdd:COG4607 238 AEANPDWLFVIdrdaaIGGEGPAAKQVLDNELVKQTTAWKNGQIVYLD 285
|
|
| TroA_d |
cd01141 |
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ... |
44-217 |
6.53e-07 |
|
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: 48.96 E-value: 6.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 44 TVQRVVSLAPNLTEIAHAAGAGDRLVAITSSGDHP--PSVDTLPHVS---ALPVDFEAVAAQEPDLVLATDQINAPGDTD 118
Cdd:cd01141 7 PPKRIVVLSPTHVDLLLALDKADKIVGVSASAYDLntPAVKERIDIQvgpTGSLNVELIVALKPDLVILYGGFQAQTILD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 119 TFEALNVPiyFFSFGSVGDILTSIETMGQLLgtEAAAADSAAALQSSLDALRARTGSL----PDAERPRVLV-LVGDDTL 193
Cdd:cd01141 87 KLEQLGIP--VLYVNEYPSPLGRAEWIKFAA--AFYGVGKEDKADEAFAQIAGRYRDLakkvSNLNKPTVAIgKPVKGLW 162
|
170 180
....*....|....*....|....
gi 2293840735 194 YSFGRGSYVHTLVRAAGGTSITAD 217
Cdd:cd01141 163 YMPGGNSYVAKMLRDAGGRYLSAE 186
|
|
| FeuA |
cd01138 |
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ... |
46-269 |
1.58e-04 |
|
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: 42.32 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 46 QRVVSLApNLTEIAHAAGAgdRLVAITSSGDHPPS----VDTLPHVSALPVDFEAVAAQEPDLVLATDQInaPGDTDTFE 121
Cdd:cd01138 10 KRIVALS-GETEGLALLGI--KPVGAASIGGKNPYykkkTLAKVVGIVDEPNLEKVLELKPDLIIVSSKQ--EENYEKLS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293840735 122 --ALNVPIYFFSfgsvGDILTSIETMGQLLGTEAAAADSAAALQSSLDALRARTGSLPDAERpRVLVLVGDDTLYSFG-R 198
Cdd:cd01138 85 kiAPTVPVSYNS----SDWEEQLKEIGKLLNKEDEAEKWLADYKQKAKEAKEKIKKKLGNDK-SVAVLRGRKQIYVFGeD 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2293840735 199 GSYVHTLVRAAGGTSITADIENQAPTLSDEYVLQEK-----PD-VILGLWGRDYDpDRLLDLHPTWDVVPAVQNDRV 269
Cdd:cd01138 160 GRGGGPILYADLGLKAPEKVKEIEDKPGYAAISLEVlpefdADyIFLLFFTGPEA-KADFESLPIWKNLPAVKNNHV 235
|
|
| |
