|
Name |
Accession |
Description |
Interval |
E-value |
| CeuA |
COG4607 |
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and ... |
1-316 |
1.01e-153 |
|
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443657 [Multi-domain] Cd Length: 310 Bit Score: 432.68 E-value: 1.01e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 1 MKKKFLAMMAVSMMglLMLSACQTNKKTADSATKETTakteVTVKDTNGQLTVPKNPQKVVVFDNGSLDTMDALGVGdrV 80
Cdd:COG4607 1 MKKTLLAALALAAA--LALAACGSSSAAAASAAAAET----VTVEHALGTVEVPKNPKRVVVFDNGALDTLDALGVE--V 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 81 VGAPTKNIPAYLKKYQ--KVESAGGIKEPDLEKINQLKPDLIIISGRQQDYQEQLKAIAPTIYLAVDAKNPWASTKQNIE 158
Cdd:COG4607 73 AGVPKGLLPDYLSKYAddKYANVGTLFEPDLEAIAALKPDLIIIGGRSAKKYDELSKIAPTIDLTVDGEDYLESLKRNTE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 159 TLGTIFDKEEVAKEKITGLEKEIADVKKQAeASANDALVVLVNEGQLSAYGKGSRFGLIHDTFGFKAADDKIEASTHGQS 238
Cdd:COG4607 153 TLGEIFGKEDEAEELVADLDAKIAALKAAA-AGKGTALIVLTNGGKISAYGPGSRFGPIHDVLGFKPADEDIEASTHGQA 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488283756 239 VSYEYVLEKNPGILFVVDRTKAIGGDD-SKDNVAANELIQKTDAGKNDKVIMLQPDVWYLSGGGLESMHLMIEDVKKGL 316
Cdd:COG4607 232 ISFEFIAEANPDWLFVIDRDAAIGGEGpAAKQVLDNELVKQTTAWKNGQIVYLDPDAWYLAGGGIQSLTEMLDEVADAL 310
|
|
| FatB |
cd01140 |
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ... |
46-314 |
7.34e-122 |
|
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: 350.40 E-value: 7.34e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 46 DTNGQLTVPKNPQKVVVFDNGSLDTMDALGVgdRVVGAPT-KNIPAYLKKYQ--KVESAGGIKEPDLEKINQLKPDLIII 122
Cdd:cd01140 1 HALGETKVPKNPEKVVVFDVGALDTLDALGV--KVVGVPKsSTLPEYLKKYKddKYANVGTLFEPDLEAIAALKPDLIII 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 123 SGRQQDYQEQLKAIAPTIYLAVDAKNPWASTKQNIETLGTIFDKEEVAKEKITGLEKEIADVKKQAEASANdALVVLVNE 202
Cdd:cd01140 79 GGRLAEKYDELKKIAPTIDLGADLKNYLESVKQNIETLGKIFGKEEEAKELVAEIDASIAEAKSAAKGKKK-ALVVLVNG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 203 GQLSAYGKGSRFGLIHDTFGFKAADDKIEASTHGQSVSYEYVLEKNPGILFVVDRTKAIGGDD-SKDNVAANELIQKTDA 281
Cdd:cd01140 158 GKLSAFGPGSRFGWLHDLLGFEPADENIKASSHGQPVSFEYILEANPDWLFVIDRGAAIGAEGsSAKEVLDNDLVKNTTA 237
|
250 260 270
....*....|....*....|....*....|...
gi 488283756 282 GKNDKVIMLQPDVWYLSGGGLESMHLMIEDVKK 314
Cdd:cd01140 238 WKNGKVIYLDPDLWYLSGGGLESLKQMIDDLKK 270
|
|
| FecB |
COG4594 |
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ... |
1-317 |
2.00e-51 |
|
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443650 [Multi-domain] Cd Length: 316 Bit Score: 172.03 E-value: 2.00e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 1 MKKkfLAMMAVSMMGLLMLSACQTNkktADSATKETTAKTEVTVKDTNGQLTVPKNPQKVVVFDNGSLDTMDALGV---- 76
Cdd:COG4594 1 MKK--LLLLLILLLALLLLAACGSS---SSDSSSSEAAAGARTVKHAMGETTIPGTPKRVVVLEWSFADALLALGVtpvg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 77 ------GDRVVGAPTKNIPAylkkyqkVESAGGIKEPDLEKINQLKPDLIIISG-RQQDYQEQLKAIAPTIYLAvDAKNP 149
Cdd:COG4594 76 iaddndYDRWVPYLRDLIKG-------VTSVGTRSQPNLEAIAALKPDLIIADKsRHEAIYDQLSKIAPTVLFK-SRNGD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 150 WASTKQNIETLGTIFDKEEVAKEKITGLEKEIADVKKQAEASAND--ALVVLVNEGQLSAYGKGSRFGLIHDTFGFKAAD 227
Cdd:COG4594 148 YQENLESFKTIAKALGKEEEAEAVLADHDQRIAEAKAKLAAADKGkkVAVGQFRADGLRLYTPNSFAGSVLAALGFENPP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 228 DKIEASTHGQS-VSYEYVLEKNPGILFVVdrtkAIGGDDSKDNVAANELIQKTDAGKNDKVIMLQPDVWyLSGGGLESMH 306
Cdd:COG4594 228 KQSKDNGYGYSeVSLEQLPALDPDVLFIA----TYDDPSILKEWKNNPLWKNLKAVKNGRVYEVDGDLW-TRGRGPLAAE 302
|
330
....*....|.
gi 488283756 307 LMIEDVKKGLE 317
Cdd:COG4594 303 LMADDLVEILL 313
|
|
| FhuD |
cd01146 |
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ... |
55-308 |
8.62e-41 |
|
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: 142.81 E-value: 8.62e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 55 KNPQKVVVFDNGSLDTMDALGVgdRVVGAP-TKNIPAYLKKYQK----VESAGGIKEPDLEKINQLKPDLIII--SGRQQ 127
Cdd:cd01146 1 AKPQRIVALDWGALETLLALGV--KPVGVAdTAGYKPWIPEPALplegVVDVGTRGQPNLEAIAALKPDLILGsaSRHDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 128 DYqEQLKAIAPTIylAVDAKNPWASTKQNIETLGTIFDKEEVAKEKITGLEKEIADVKKQAEASANDALVVLV--NEGQL 205
Cdd:cd01146 79 IY-DQLSQIAPTV--LLDSSPWLAEWKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKLPDKGPKPVSVVRfsDAGSI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 206 SAYGKGSRFGLIHDTFGFK--AADDKIEASTHgQSVSYEYVLEKNPGILFVVdrtkAIGGDDSKDNVAANELIQKTDAGK 283
Cdd:cd01146 156 RLYGPNSFAGSVLEDLGLQnpWAQETTNDSGF-ATISLERLAKADADVLFVF----TYEDEELAQALQANPLWQNLPAVK 230
|
250 260
....*....|....*....|....*
gi 488283756 284 NDKVIMLQPDVWYLsGGGLESMHLM 308
Cdd:cd01146 231 NGRVYVVDDVWWFF-GGGLSAARLL 254
|
|
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
59-299 |
6.64e-40 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 140.52 E-value: 6.64e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 59 KVVVFDNGSLDTMDALGVGDRVVGAPTKNIPAYLK-KYQKVESAGGIKEPDLEKINQLKPDLIIIS--GRQQDYQEQLKA 135
Cdd:COG0614 2 RIVSLSPSATELLLALGAGDRLVGVSDWGYCDYPElELKDLPVVGGTGEPNLEAILALKPDLVLASssGNDEEDYEQLEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 136 I-APTIYLAVdakNPWASTKQNIETLGTIFDKEEVAKEKITGLEKEIADVKKQAEASAND--ALVVLVNEGQLSAYGKGS 212
Cdd:COG0614 82 IgIPVVVLDP---RSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGAEERptVLYEIWSGDPLYTAGGGS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 213 RFGLIHDTFGFKAADDkiEASTHGQSVSYEYVLEKNPGILFVVDRTK-AIGGDDSKDNVAANELIQKTDAGKNDKVIMLQ 291
Cdd:COG0614 159 FIGELLELAGGRNVAA--DLGGGYPEVSLEQVLALDPDVIILSGGGYdAETAEEALEALLADPGWQSLPAVKNGRVYVVP 236
|
....*...
gi 488283756 292 PDVWYLSG 299
Cdd:COG0614 237 GDLLSRPG 244
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
61-293 |
3.48e-30 |
|
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: 114.39 E-value: 3.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 61 VVFDNGSLDTMDALGVGDRVVGAPTK-NIPAYLKKYQKVESAGGIKEPDLEKINQLKPDLIIIS---GRQQDYQeQLKAI 136
Cdd:pfam01497 1 AALSPAYTEILYALGATDSIVGVDAYtRDPLKADAVAAIVKVGAYGEINVERLAALKPDLVILStgyLTDEAEE-LLSLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 137 APTIYLAVDakNPWASTKQNIETLGTIFDKEEVAKEKITGLEKEIADVKKQAEASANDALVVLV--NEGQLSAYGKGSRF 214
Cdd:pfam01497 80 IPTVIFESS--STGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPVLVFGgaDGGGYVVAGSNTYI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 215 GLIHDTFGFKAAddkIEASTHGQS--VSYEYVLEKNPGILFVVDRTKaiGGDDSKDNVAANELIQKTDAGKNDKVIMLQP 292
Cdd:pfam01497 158 GDLLRILGIENI---AAELSGSEYapISFEAILSSNPDVIIVSGRDS--FTKTGPEFVAANPLWAGLPAVKNGRVYTLPS 232
|
.
gi 488283756 293 D 293
Cdd:pfam01497 233 D 233
|
|
| FeuA |
cd01138 |
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ... |
49-300 |
1.53e-28 |
|
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: 110.12 E-value: 1.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 49 GQLTVPKNPQKVVVfdnGSLDTMDALGVGDRVVGAPTKNIP-AYLKKYQKVESAGGIKEPDLEKINQLKPDLIIISGRQQ 127
Cdd:cd01138 1 GEVEIPAKPKRIVA---LSGETEGLALLGIKPVGAASIGGKnPYYKKKTLAKVVGIVDEPNLEKVLELKPDLIIVSSKQE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 128 DYQEQLKAIAPTIYLAVDAKNPwastKQNIETLGTIFDKEEVAKEKITGLEKEIADVKKQ-AEASANDALV-VLVNEGQL 205
Cdd:cd01138 78 ENYEKLSKIAPTVPVSYNSSDW----EEQLKEIGKLLNKEDEAEKWLADYKQKAKEAKEKiKKKLGNDKSVaVLRGRKQI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 206 SAYGK-GSRFGLIHDTF-GFKAAD--DKIEASTHGQSVSYEYVLEKNPGILFVVDRTkaigGDDSKDNVAANELIQKTDA 281
Cdd:cd01138 154 YVFGEdGRGGGPILYADlGLKAPEkvKEIEDKPGYAAISLEVLPEFDADYIFLLFFT----GPEAKADFESLPIWKNLPA 229
|
250
....*....|....*....
gi 488283756 282 GKNDKVIMLQPDVWYLSGG 300
Cdd:cd01138 230 VKNNHVYIVDAWVFYFADG 248
|
|
| TroA-like |
cd00636 |
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ... |
58-200 |
4.72e-26 |
|
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: 100.71 E-value: 4.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 58 QKVVVFDNGSLDTMDALGVGDRVVGA--PTKNIPAYLKKYQKVESAGGIKEPDLEKINQLKPDLIIISGRQQD-YQEQLK 134
Cdd:cd00636 1 KRVVALDPGATELLLALGGDDKPVGVadPSGYPPEAKALLEKVPDVGHGYEPNLEKIAALKPDLIIANGSGLEaWLDKLS 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488283756 135 AIA-PTIYLAVDAKNPWASTKQNIETLGTIFDKEEVAKEKITGLEKEIADVKKQAEASANDALVVLV 200
Cdd:cd00636 81 KIAiPVVVVDEASELSLENIKESIRLIGKALGKEENAEELIAELDARLAELRAKLAKIPKKKVSLVV 147
|
|
| TroA_a |
cd01148 |
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ... |
42-300 |
4.84e-24 |
|
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: 98.95 E-value: 4.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 42 VTVKDTNGQLTVPKNPQKVVVFDNGSLDTMDALGVGDRVVG--APTKNIPAYLKKYQKVESAGGIKEPDLEKINQLKPDL 119
Cdd:cd01148 3 LTVENCGRSVTFDKAPQRVVSNDQNTTEMMLALGLQDRMVGtaGIDNKDLPELKAKYDKVPELAKKYPSKETVLAARPDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 120 IIISGrqqDYQ---------EQLKAIAPTIYL------AVDAKNPWASTKQNIETLGTIFDKEEVAKEKITGLEKEIADV 184
Cdd:cd01148 83 VFGGW---SYGfdkgglgtpDSLAELGIKTYIlpescgQRRGEATLDDVYNDIRNLGKIFDVEDRADKLVADLKARLAEI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 185 KKQAEASANDALVVLVNEGQLSAYGKGsRFGLIHDTF----GFKAADDKIEASTHgqsVSYEYVLEKNPGILFVVDRTKA 260
Cdd:cd01148 160 SAKVKGDGKKVAVFVYDSGEDKPFTSG-RGGIPNAIItaagGRNVFADVDESWTT---VSWETVIARNPDVIVIIDYGDQ 235
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 488283756 261 IGGDDSKDNVAANELIQKTDAGKNDKVIMLqPDVWYLSGG 300
Cdd:cd01148 236 NAAEQKIKFLKENPALKNVPAVKNNRFIVL-PLAEATPGI 274
|
|
| YvrC |
cd01143 |
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ... |
55-254 |
2.50e-23 |
|
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: 95.04 E-value: 2.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 55 KNPQKVVVFDNGSLDTMDALGVGDRVVG-APTKNIPAYLKKYQKVesaGGIKEPDLEKINQLKPDLII-ISGRQQDYQEQ 132
Cdd:cd01143 1 KEPERIVSLSPSITEILFALGAGDKIVGvDTYSNYPKEVRKKPKV---GSYSNPNVEKIVALKPDLVIvSSSSLAELLEK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 133 LKAIAPTiYLAVDAKNPWASTKQNIETLGTIFDKEEVAKEKITGLEKEIADVKKQAEASANDALVVLVNEGQLSAYGKGS 212
Cdd:cd01143 78 LKDAGIP-VVVLPAASSLDEIYDQIELIGKITGAEEEAEKLVKEMKQKIDKVKDKGKTIKKSKVYIEVSLGGPYTAGKNT 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488283756 213 RFGLIHDTFGFK-AADDKIEASThgqsVSYEYVLEKNPGILFV 254
Cdd:cd01143 157 FINELIRLAGAKnIAADSGGWPQ----VSPEEILKANPDVIIL 195
|
|
| fecB |
PRK11411 |
iron-dicitrate transporter substrate-binding subunit; Provisional |
41-300 |
4.06e-23 |
|
iron-dicitrate transporter substrate-binding subunit; Provisional
Pssm-ID: 183123 [Multi-domain] Cd Length: 303 Bit Score: 97.05 E-value: 4.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 41 EVTVKDTNGQLTVPKNPQKVVVFDNGSLDTMDALGVGDrvVGA-----PTKNIPAYLKKYQKVESAGGIKEPDLEKINQL 115
Cdd:PRK11411 23 AVTVQDEQGTFTLEKTPQRIVVLELSFVDALAAVGVSP--VGVaddndAKRILPEVRAHLKPWQSVGTRSQPSLEAIAAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 116 KPDLIII-SGRQQDYQEQLKAIAPTIYLavDAKNpwASTKQNIET---LGTIFDKEEVAKEKITGLEKEIADVKKQAEAS 191
Cdd:PRK11411 101 KPDLIIAdSSRHAGVYIALQKIAPTLLL--KSRN--ETYQENLQSaaiIGEVLGKKREMQARIEQHKERMAQFASQLPKG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 192 ANDALVVlVNEGQLSAYGKGSRFGLIHDTFGFKAADDKIEASTHgQSVSYEYVLEKNPGILFVVD-RTKAIGGDDSKDnv 270
Cdd:PRK11411 177 TRVAFGT-SREQQFNLHSPESYTGSVLAALGLNVPKAPMNGAAM-PSISLEQLLALNPDWLLVAHyRQESIVKRWQQD-- 252
|
250 260 270
....*....|....*....|....*....|
gi 488283756 271 aanELIQKTDAGKNDKVIMLQPDVWYLSGG 300
Cdd:PRK11411 253 ---PLWQMLTAAKKQQVASVDSNTWARMRG 279
|
|
| FepB |
COG4592 |
ABC-type Fe2+-enterobactin transport system, periplasmic component [Inorganic ion transport ... |
1-294 |
5.97e-22 |
|
ABC-type Fe2+-enterobactin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443649 [Multi-domain] Cd Length: 330 Bit Score: 94.24 E-value: 5.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 1 MKKKFLAMMAVSMMGLLMLSACQTNKKTADSATKETTAKTEVTVKDTNGQLTVPKNPQKVVVFD---NGSLDTMDA--LG 75
Cdd:COG4592 1 MARRRLAAAAALLAAALLLAGCSSADSTASGTSTAAAGGWPRTVTTEKGTVTLPAKPQRIVSTSvtlTGSLLAIDApvVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 76 VGDRVVGAPTKNiPAYLKKYQKVESAGGIK------EPDLEKINQLKPDLIIISGRQQDYQ----EQLKAIAPTIYLAVD 145
Cdd:COG4592 81 SGATTPNNVTDD-QGFFRQWADVAKERGVKrlyiglEPNAEAIAAAAPDLIIGSATGGDSAldlyDQLSAIAPTLVVNYD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 146 AKNpWastKQNIETLGTIFDKEEVAKEKITGLEKEIADVKKQAEASAND-ALVVLVNEGQLSAYGKGSRFGLIHDTFGFK 224
Cdd:COG4592 160 DKS-W---QELATQLGEATGHEAQADAVIAAFDARVAEVKAAITLPPQPvSALVYNEDGGANLWTPESAQGQLLQALGFT 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488283756 225 AAD--DKIEASTHGQS------VSYEYVLEKNPG-ILFVVDrtkaiGGDDSKDNVAANELIQKTDAGKNDKVIMLQPDV 294
Cdd:COG4592 236 LAPlpAELATSTSQGKrgdivqLSGENLAAALTGpTLFLFA-----ADDKDVDALKADPLLAHLPAVQAGRVYALGPDS 309
|
|
| HemV-2 |
cd01147 |
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ... |
53-287 |
8.46e-21 |
|
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: 89.70 E-value: 8.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 53 VPKNPQKVVVFDNGSLDTMDALGVGDRVVGAPTKNIPAY----------LKKYQKVESAGGIKEPDLEKINQLKPDLIII 122
Cdd:cd01147 1 VPKPVERVVAAGPGALRLLYALAAPDKIVGVDDAEKSDEgrpyflaspeLKDLPVIGRGGRGNTPNYEKIAALKPDVVID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 123 SGRQ--QDYQEQLKAIAPTIYLAVDAKNPWASTKQNIETLGTIFDKEEVAKEKITGLEKEIADVKKQAEASANDALVVLV 200
Cdd:cd01147 81 VGSDdpTSIADDLQKKTGIPVVVLDGGDSLEDTPEQIRLLGKVLGKEERAEELISFIESILADVEERTKDIPDEEKPTVY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 201 NEGQLSAYGKGSRFGLIHDTFGFKAAD-----DKIEASTHGQsVSYEYVLEKNPGILFVVDrtkaIGGDDSKDNVAAN-E 274
Cdd:cd01147 161 FGRIGTKGAAGLESGLAGSIEVFELAGginvaDGLGGGGLKE-VSPEQILLWNPDVIFLDT----GSFYLSLEGYAKNrP 235
|
250
....*....|...
gi 488283756 275 LIQKTDAGKNDKV 287
Cdd:cd01147 236 FWQSLKAVKNGRV 248
|
|
| TroA_e |
cd01142 |
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ... |
35-309 |
6.27e-17 |
|
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: 79.32 E-value: 6.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 35 ETTAKTEVTVKDTNG-QLTVPKNPQKVVVFDNGSLDTMDALGVGDRVVGAPT--KNIPAYLK---KYQKVESAGGIKEPD 108
Cdd:cd01142 1 PAATAATRTITDMAGrKVTIPDEVKRIAALWGAGNAVVAALGGGKLIVATTStvQQEPWLYRlapSLENVATGGTGNDVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 109 LEKINQLKPDLII-ISGRQQDYQEQLKAIAPTIYLAVDAKNpwaSTKQNIETLGTIFDKEEVAKEKITGLEKEIADVKKQ 187
Cdd:cd01142 81 IEELLALKPDVVIvWSTDGKEAGKAVLRLLNALSLRDAELE---EVKLTIALLGELLGRQEKAEALVAYFDDNLAYVAAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 188 AEASANDALVVLVNEG--QLSAYGKGSRFGLIHDTFGFK--AADDKIEASthgQSVSYEYVLEKNPGILFVvdrtkaiGG 263
Cdd:cd01142 158 TKKLPDSERPRVYYAGpdPLTTDGTGSITNSWIDLAGGInvASEATKKGS---GEVSLEQLLKWNPDVIIV-------GN 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 488283756 264 DDSKDNVAANELIQKTDAGKNDKVImLQPDVWYLSGGGLESMHLMI 309
Cdd:cd01142 228 ADTKAAILADPRWQNLRAVKNGRVY-VNPEGAFWWDRPSAEEALLG 272
|
|
| ChuT |
COG4558 |
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ... |
57-302 |
9.17e-17 |
|
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443619 [Multi-domain] Cd Length: 285 Bit Score: 78.69 E-value: 9.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 57 PQKVVVFdNGSL-DTMDALGVGDRVVGAP-TKNIPAYLKKYQKVesaGGIKEPDLEKINQLKPDLIIISgrqQDYQ---- 130
Cdd:COG4558 27 AERIVSL-GGSVtEIVYALGAGDRLVGVDtTSTYPAAAKALPDV---GYMRQLSAEGILSLKPTLVLAS---EGAGppev 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 131 -EQLKAiAPTIYLAVDAKNPWASTKQNIETLGTIFDKEEVAKEKITGLEKEIADVKKQAEASAND--ALVVLVNE-GQLS 206
Cdd:COG4558 100 lDQLRA-AGVPVVVVPAAPSLEGVLAKIRAVAAALGVPEAGEALAARLEADLAALAARVAAIGKPprVLFLLSRGgGRPM 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 207 AYGKGSrfglihdtfgfkAADDKIEAS---------THGQSVSYEYVLEKNPGILFVVDRT-KAIGGddsKDNVAANELI 276
Cdd:COG4558 179 VAGRGT------------AADALIRLAggvnaaagfEGYKPLSAEALIAAAPDVILVMTRGlESLGG---VDGLLALPGL 243
|
250 260
....*....|....*....|....*.
gi 488283756 277 QKTDAGKNDKVIMLQPDvwYLSGGGL 302
Cdd:COG4558 244 AQTPAGKNKRIVAMDDL--LLLGFGP 267
|
|
| PRK10957 |
PRK10957 |
iron-enterobactin transporter periplasmic binding protein; Provisional |
16-293 |
1.31e-16 |
|
iron-enterobactin transporter periplasmic binding protein; Provisional
Pssm-ID: 236806 [Multi-domain] Cd Length: 317 Bit Score: 78.86 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 16 LLMLSACqtnkktadSATKETTAKTEVTVKDTNGQLTVPKNPQKVV---VFDNGSLDTMDALGVGDrvvGAPTKNIP--- 89
Cdd:PRK10957 11 GLLLSGI--------AAAQASAAGWPRTVTDSRGSVTLESKPQRIVstsVTLTGTLLAIDAPVIAS---GATTPNTRvad 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 90 --AYLKKYQKVESAGGIK-----EPDLEKINQLKPDLIIISGRQQD----YQEQLKAIAPTIYLAVDAKNpWastkQNIE 158
Cdd:PRK10957 80 dqGFFRQWSDVAKERGVEvlyigEPDAEAVAAQMPDLIVISATGGDsalaLYDQLSAIAPTLVIDYDDKS-W----QELA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 159 T-LGTIFDKEEVAKEKITGLEKEIADVKKQAEASANDALVVLVNEG--------QLSAYGKgsrfgLIHDtFGFKAAD-- 227
Cdd:PRK10957 155 TqLGEATGLEKQAAAVIAQFDAQLAEVKAKITLPPQPVSALVYNGAghsanlwtPESAQGQ-----LLEQ-LGFTLAElp 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488283756 228 DKIEASTHG------QSVSYEYVLEK-NPGILFVVdrtkaIGGDDSKDNVAANELIQKTDAGKNDKVIMLQPD 293
Cdd:PRK10957 229 AGLQASTSQgkrhdiIQLGGENLAAGlNGETLFLF-----AGDDKDADAFLADPLLANLPAVQNKQVYALGTD 296
|
|
| BtuF |
cd01144 |
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ... |
73-302 |
1.72e-13 |
|
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: 68.87 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 73 ALGVGDRVVGAPTK-NIPAYLKKyqkVESAGGIKEPDLEKINQLKPDLII--ISGRQQDYQEQLKAIAPTIYLaVDAKNP 149
Cdd:cd01144 16 ALGLGDQLVGVTDYcDYPPEAKK---LPRVGGFYQLDLERVLALKPDLVIawDDCNVCAVVDQLRAAGIPVLV-SEPQTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 150 wASTKQNIETLGTIFDKEEVAKEKITGLEKEIADVKKQAEASANDALVVLVNEGQLsaygkgsrFGLIHDTFgfkaaDDK 229
Cdd:cd01144 92 -DDILADIRRLGTLAGRPARAEELAEALRRRLAALRKQYASKPPPRVFYQEWIDPL--------MTAGGDWV-----PEL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 230 IEA-------STHGQ---SVSYEYVLEKNPGILFVVDrtkaIGGDDSKDNVAANELIQKTDAGKNDKVIMLQPDVWYLSG 299
Cdd:cd01144 158 IALaggvnvfADAGErspQVSWEDVLAANPDVIVLSP----CGFGFTPAILRKEPAWQALPAVRNGRVYAVDGNWYFRPS 233
|
...
gi 488283756 300 GGL 302
Cdd:cd01144 234 PRL 236
|
|
| TroA_f |
cd01139 |
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ... |
42-268 |
9.25e-12 |
|
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: 65.02 E-value: 9.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 42 VTVKDTNG-QLTVPKNPQKVVVfdnGSLDTMDALGVGD------RVVGAPT---KNIP----AYLKKYQKVES---AGGI 104
Cdd:cd01139 1 ITVTDVAGrKVTLDAPVERVLL---GEGRQLYALALLEgenpfaRIVGWGGdlkKGDPdtyaKYKEKFPEIADiplIGST 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 105 KEPD--LEKINQLKPDLIIIS------GRQQDYQEQL-KAIAPTIYlaVDAKN-PWASTKQNIETLGTIFDKEEVAKEKI 174
Cdd:cd01139 78 YNGDfsVEKVLTLKPDLVILNiwakttAEESGILEKLeQAGIPVVF--VDFRQkPLKNTTPSMRLLGKALGREERAEEFI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 175 TGLEKEIADVKKQAEASANDALVVLVNEGQL------SAYGKGSrFGLIHDTFGFKAADDKIEASTHGQsVSYEYVLEKN 248
Cdd:cd01139 156 EFYQERIDRIRDRLAKINEPKPKVFIELGAGgpeeccSTYGNGN-WGELVDAAGGDNIADGLIPGTSGE-LNAEYVIAAN 233
|
250 260
....*....|....*....|
gi 488283756 249 PGILFvvdrtkAIGGDDSKD 268
Cdd:cd01139 234 PEIII------ATGGNWAKD 247
|
|
| TroA_d |
cd01141 |
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ... |
50-198 |
1.53e-11 |
|
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: 62.05 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 50 QLTVPKNPQKVVVFDNGSLDTMDALGVGDRVVGAP----TKNIPAYlkKYQKVESAGGIKEPDLEKINQLKPDLIIISGR 125
Cdd:cd01141 1 AKTIKVPPKRIVVLSPTHVDLLLALDKADKIVGVSasayDLNTPAV--KERIDIQVGPTGSLNVELIVALKPDLVILYGG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 126 QQDYQ--EQLKAIAptiyLAVDAKNPWASTKQNIETLG-----TIFDKEEVAKEKITGLEKEIADVKKQAeASANDALVV 198
Cdd:cd01141 79 FQAQTilDKLEQLG----IPVLYVNEYPSPLGRAEWIKfaaafYGVGKEDKADEAFAQIAGRYRDLAKKV-SNLNKPTVA 153
|
|
| PRK10576 |
PRK10576 |
Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD; |
106-226 |
1.15e-10 |
|
Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD;
Pssm-ID: 236719 Cd Length: 292 Bit Score: 61.18 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 106 EPDLEKINQLKPDLIIISgrqQDY---QEQLKAIAPTIYLAV-DAKNPWASTKQNIETLGTIFDKEEVAKEKITGLEKEI 181
Cdd:PRK10576 83 EPNLELLTQMKPSLILWS---AGYgpsPEKLARIAPGRGFAFsDGKKPLAVARKSLVELAQRLNLEAAAETHLAQFDDFI 159
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 488283756 182 ADVKKQAEASANDALVV--LVNEGQLSAYGKGSRFGLIHDTFGFKAA 226
Cdd:PRK10576 160 ASAKPRLAGRGQRPLLLtsLIDPRHALVFGPNSLFQEVLDELGIENA 206
|
|
| HutB |
cd01149 |
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ... |
73-288 |
9.15e-09 |
|
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: 54.96 E-value: 9.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 73 ALGVGDRVVGA-PTKNIPAYLKKYQKVesaGGIKEPDLEKINQLKPDLIIISGRQQDYQ--EQLKAIAPTIyLAVDAKNP 149
Cdd:cd01149 17 ALGAGDRLVGVdSTSTYPEAAAKLPDV---GYMRQLSAEGVLSLKPTLVIASDEAGPPEalDQLRAAGVPV-VTVPSTPT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 150 WASTKQNIETLGTIFDKEEVAKEKITGLEKEIADVKKQAEAS--ANDALVVLVNEG-QLSAYGKGSRFGLIHDTFGFKAA 226
Cdd:cd01149 93 LDGLLTKIRQVAQALGVPEKGEALAQEVRQRLAALRKTVAAHkkPPRVLFLLSHGGgAAMAAGRNTAADAIIALAGAVNA 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488283756 227 DDKIEASThgqSVSYEYVLEKNPGILFVVDRT-KAIGGDdskDNVAANELIQKTDAGKNDKVI 288
Cdd:cd01149 173 AAGFRGYK---PLSAEALIAAQPDVILVMSRGlDAVGGV---DGLLKLPGLAQTPAGRNKRIL 229
|
|
| PRK14048 |
PRK14048 |
ferrichrome/ferrioxamine B periplasmic transporter; Provisional |
15-251 |
9.75e-07 |
|
ferrichrome/ferrioxamine B periplasmic transporter; Provisional
Pssm-ID: 172540 [Multi-domain] Cd Length: 374 Bit Score: 49.90 E-value: 9.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 15 GLLMLSACQTNKKTADSATKEttAKTEVTVKDTNG-QLTVPKNPQKVVVFDNGSLDTM-----DALGV-----GDrVVGA 83
Cdd:PRK14048 7 SLVRLVAFLAIAFLALSALAE--VQWPMTVTDAVGrEVTIPAPPKAVLLGSGFNLIALslihpDPVSLlagwsGD-MKGD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 84 PTKNIPAYLKKYQKVESAGGIKEPD-----LEKINQLKPDLIIISGRQQDYQEQLKAIA-------PTIylAVDAKN-PW 150
Cdd:PRK14048 84 NPEIYESFLRKFPELADVPLIDDGSgpglsFETILTLKADLAILANWQADTEAGQRAIEylesigvPVI--VVDFNNeAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 151 ASTKQNIETLGTIFDKEEVAKEKITGLEKEIADVKKQAEASANDALVVLV----NEGQLS-AYGKGSRFGLIHDTFGFKA 225
Cdd:PRK14048 162 KNTPDNMRLLGKVFEREEQAEDFARFYEERLARIRDRVAKHSEPGPTVLMeafpAADRCCwAYGRGGLGEFIALTGSRNI 241
|
250 260
....*....|....*....|....*.
gi 488283756 226 ADDKIEASthGQSVSYEYVLEKNPGI 251
Cdd:PRK14048 242 AEGALPRP--GGMMNAEAIMAENPDV 265
|
|
| btuF |
PRK09534 |
corrinoid ABC transporter substrate-binding protein; Reviewed |
1-291 |
7.51e-05 |
|
corrinoid ABC transporter substrate-binding protein; Reviewed
Pssm-ID: 236552 [Multi-domain] Cd Length: 359 Bit Score: 43.74 E-value: 7.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 1 MKKKFLAMMAVSMMGLLMlSACQTNKKTADSATKETTAKTEVTVKD-TNGQLTVPKNPQKVVVFDNGSLDTMDALGVGDR 79
Cdd:PRK09534 4 MRFRSLVIVALAVTMTAA-GGALAPAPAAQHADADRACSFPVTETDaTGTEITLDERPERVVTLNPSAAQTMWELGARDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 80 VVGapTKNIPAYLKKYQKVE--SAGGIKEPDLEKINQLKPDLIII-SGRQQDYQEQLKAIAPTIYlavdaKNPWASTKQN 156
Cdd:PRK09534 83 VVG--VTQYASYLDGAEERTnvSGGQPFGVNVEAVVGLDPDLVLApNAVAGDTVTRLREAGITVF-----HFPAATSIED 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 157 I----ETLGTIFDKEEVAKEKITGLEKEIADVkKQAEASANDALVVLVNEGQLSAYGKGSRFGLIHDTfgfkAADDKIEA 232
Cdd:PRK09534 156 VaektATIGRLTGNCEAAAETNAEMRDRVDAV-EDRTADVDDRPRVLYPLGDGYTAGGNTFIGALIEA----AGGHNVAA 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488283756 233 STHGQS---VSYEYVLEKNPGILFVVDRTKAiggddskdnVAANELIQKTDAGKNDKVIMLQ 291
Cdd:PRK09534 231 DATTDGypqLSEEVIVQQDPDVIVVATASAL---------VAETEPYASTTAGETGNVVTVN 283
|
|
| PRK03379 |
PRK03379 |
vitamin B12-transporter protein BtuF; Provisional |
73-192 |
7.82e-04 |
|
vitamin B12-transporter protein BtuF; Provisional
Pssm-ID: 179575 [Multi-domain] Cd Length: 260 Bit Score: 40.44 E-value: 7.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488283756 73 ALGVGDRVVGAPTkNIPAYLKKYQKVESAGGIkepDLEKINQLKPDLIII--SGRQQDYQEQLKAIA-PTIYlaVDAKNp 149
Cdd:PRK03379 33 AAGITPVGVSSYS-DYPPQAKKIEQVATWQGM---NLERIVALKPDLVLAwrGGNAERQVDQLASLGiKVMW--VDATS- 105
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 488283756 150 WASTKQNIETLGTIFDKEEVAKEKITGLEKEIADVKKQAEASA 192
Cdd:PRK03379 106 IEQIANALRQLAPWSPQPEKAEQAAQSLLQQYAALKAQYADKP 148
|
|
| |
