|
Name |
Accession |
Description |
Interval |
E-value |
| CeuA |
COG4607 |
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and ... |
1-335 |
1.04e-126 |
|
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443657 [Multi-domain] Cd Length: 310 Bit Score: 364.89 E-value: 1.04e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 1 MKKTMLLklvSILAIFTLMLVACSDSSKETSKATKdngsdkPKTVEITDAHGKVTVPVNPKNVVALDNRTFETLADWGIK 80
Cdd:COG4607 1 MKKTLLA---ALALAAALALAACGSSSAAAASAAA------AETVTVEHALGTVEVPKNPKRVVVFDNGALDTLDALGVE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 81 LAAAPKDIMPADSAYKKDEKVQNIGNHREPNLEIIAAANPDLVIVGQRFADHYEEIKKLVPnaaVIDLNFDvsekatkpG 160
Cdd:COG4607 72 VAGVPKGLLPDYLSKYADDKYANVGTLFEPDLEAIAALKPDLIIIGGRSAKKYDELSKIAP---TIDLTVD--------G 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 161 ENLVKGLKDSTTTLGKIFAKDKEAKQLVADFDKSIEKAKSAYNGKDKVMSVIVTGGNIGFAAPhsGRVWGPMYEIFGWTP 240
Cdd:COG4607 141 EDYLESLKRNTETLGEIFGKEDEAEELVADLDAKIAALKAAAAGKGTALIVLTNGGKISAYGP--GSRFGPIHDVLGFKP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 241 ALEVSnSTAGHkGDDVSVEAIAQTNPDWIFVLDRDAATSdaaKSTPAKDVISKSPALQNTTAVSKKQVIYA-PEDTYTNE 319
Cdd:COG4607 219 ADEDI-EASTH-GQAISFEFIAEANPDWLFVIDRDAAIG---GEGPAAKQVLDNELVKQTTAWKNGQIVYLdPDAWYLAG 293
|
330
....*....|....*..
gi 446676110 320 -SIQTYIELFGNMAKTL 335
Cdd:COG4607 294 gGIQSLTEMLDEVADAL 310
|
|
| FatB |
cd01140 |
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ... |
49-337 |
2.23e-91 |
|
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: 273.75 E-value: 2.23e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 49 DAHGKVTVPVNPKNVVALDNRTFETLADWGIKLAAAPKD-IMPADSAYKKDEKVQNIGNHREPNLEIIAAANPDLVIVGQ 127
Cdd:cd01140 1 HALGETKVPKNPEKVVVFDVGALDTLDALGVKVVGVPKSsTLPEYLKKYKDDKYANVGTLFEPDLEAIAALKPDLIIIGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 128 RFADHYEEIKKLVPNaavIDLNFDVSekatkpgeNLVKGLKDSTTTLGKIFAKDKEAKQLVADFDKSIEKAKSAYNGKDK 207
Cdd:cd01140 81 RLAEKYDELKKIAPT---IDLGADLK--------NYLESVKQNIETLGKIFGKEEEAKELVAEIDASIAEAKSAAKGKKK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 208 VMSVIVTGGNIGFAAPHSgrVWGPMYEIFGWTPALEVSNstAGHKGDDVSVEAIAQTNPDWIFVLDRDAATSdaAKSTPA 287
Cdd:cd01140 150 ALVVLVNGGKLSAFGPGS--RFGWLHDLLGFEPADENIK--ASSHGQPVSFEYILEANPDWLFVIDRGAAIG--AEGSSA 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 446676110 288 KDVISKSPaLQNTTAVSKKQVIYAPEDTYTNESIQTyiELFGNMAKTLAK 337
Cdd:cd01140 224 KEVLDNDL-VKNTTAWKNGKVIYLDPDLWYLSGGGL--ESLKQMIDDLKK 270
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
64-314 |
1.07e-34 |
|
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: 126.71 E-value: 1.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 64 VALDNRTFETLADWGIKLAAAPKDIMPAD-SAYKKDEKVQNIGNHREPNLEIIAAANPDLVIVGQRFADHyEEIKKLVPN 142
Cdd:pfam01497 1 AALSPAYTEILYALGATDSIVGVDAYTRDpLKADAVAAIVKVGAYGEINVERLAALKPDLVILSTGYLTD-EAEELLSLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 143 AAVIDLNFDvsekatkpgeNLVKGLKDSTTTLGKIFAKDKEAKQLVADFDKSIEKAKSAYN-GKDKVMSVIVTGGNIGFA 221
Cdd:pfam01497 80 IPTVIFESS----------STGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPsLTRKPVLVFGGADGGGYV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 222 APHSGRVWGPMYEIFGWTPALEVSNstaGHKGDDVSVEAIAQTNPDWIFVLDRDAATSDAAkstpakDVISKSPALQNTT 301
Cdd:pfam01497 150 VAGSNTYIGDLLRILGIENIAAELS---GSEYAPISFEAILSSNPDVIIVSGRDSFTKTGP------EFVAANPLWAGLP 220
|
250
....*....|...
gi 446676110 302 AVSKKQVIYAPED 314
Cdd:pfam01497 221 AVKNGRVYTLPSD 233
|
|
| PRK10957 |
PRK10957 |
iron-enterobactin transporter periplasmic binding protein; Provisional |
13-316 |
1.49e-18 |
|
iron-enterobactin transporter periplasmic binding protein; Provisional
Pssm-ID: 236806 [Multi-domain] Cd Length: 317 Bit Score: 84.64 E-value: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 13 LAIFTLMLVACSDSSKETSkatkdngsDKPKTVeiTDAHGKVTVPVNPKNVVAldnrTFETLAdwGIKLA---------- 82
Cdd:PRK10957 7 LLLLGLLLSGIAAAQASAA--------GWPRTV--TDSRGSVTLESKPQRIVS----TSVTLT--GTLLAidapviasga 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 83 AAPKDIMP---------ADSAYKKDEKVQNIGnhrEPNLEIIAAANPDLVIV----GQRFADHYEEIKKLVPnaaVIDLN 149
Cdd:PRK10957 71 TTPNTRVAddqgffrqwSDVAKERGVEVLYIG---EPDAEAVAAQMPDLIVIsatgGDSALALYDQLSAIAP---TLVID 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 150 FDvsekatkpgenlVKGLKDSTTTLGKIFAKDKEAKQLVADFDKSIEKAKSAYNGKDKVMSVIVTGGnigfaAPHSGRVW 229
Cdd:PRK10957 145 YD------------DKSWQELATQLGEATGLEKQAAAVIAQFDAQLAEVKAKITLPPQPVSALVYNG-----AGHSANLW 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 230 ------GPMYEIFGWT----PALEVSNSTAGHKGD--DVSVEAIAQ-TNPDWIFVLdrdAATSDAAkstpakDVISKSPA 296
Cdd:PRK10957 208 tpesaqGQLLEQLGFTlaelPAGLQASTSQGKRHDiiQLGGENLAAgLNGETLFLF---AGDDKDA------DAFLADPL 278
|
330 340
....*....|....*....|
gi 446676110 297 LQNTTAVSKKQVIYAPEDTY 316
Cdd:PRK10957 279 LANLPAVQNKQVYALGTDTF 298
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CeuA |
COG4607 |
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and ... |
1-335 |
1.04e-126 |
|
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443657 [Multi-domain] Cd Length: 310 Bit Score: 364.89 E-value: 1.04e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 1 MKKTMLLklvSILAIFTLMLVACSDSSKETSKATKdngsdkPKTVEITDAHGKVTVPVNPKNVVALDNRTFETLADWGIK 80
Cdd:COG4607 1 MKKTLLA---ALALAAALALAACGSSSAAAASAAA------AETVTVEHALGTVEVPKNPKRVVVFDNGALDTLDALGVE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 81 LAAAPKDIMPADSAYKKDEKVQNIGNHREPNLEIIAAANPDLVIVGQRFADHYEEIKKLVPnaaVIDLNFDvsekatkpG 160
Cdd:COG4607 72 VAGVPKGLLPDYLSKYADDKYANVGTLFEPDLEAIAALKPDLIIIGGRSAKKYDELSKIAP---TIDLTVD--------G 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 161 ENLVKGLKDSTTTLGKIFAKDKEAKQLVADFDKSIEKAKSAYNGKDKVMSVIVTGGNIGFAAPhsGRVWGPMYEIFGWTP 240
Cdd:COG4607 141 EDYLESLKRNTETLGEIFGKEDEAEELVADLDAKIAALKAAAAGKGTALIVLTNGGKISAYGP--GSRFGPIHDVLGFKP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 241 ALEVSnSTAGHkGDDVSVEAIAQTNPDWIFVLDRDAATSdaaKSTPAKDVISKSPALQNTTAVSKKQVIYA-PEDTYTNE 319
Cdd:COG4607 219 ADEDI-EASTH-GQAISFEFIAEANPDWLFVIDRDAAIG---GEGPAAKQVLDNELVKQTTAWKNGQIVYLdPDAWYLAG 293
|
330
....*....|....*..
gi 446676110 320 -SIQTYIELFGNMAKTL 335
Cdd:COG4607 294 gGIQSLTEMLDEVADAL 310
|
|
| FatB |
cd01140 |
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ... |
49-337 |
2.23e-91 |
|
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: 273.75 E-value: 2.23e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 49 DAHGKVTVPVNPKNVVALDNRTFETLADWGIKLAAAPKD-IMPADSAYKKDEKVQNIGNHREPNLEIIAAANPDLVIVGQ 127
Cdd:cd01140 1 HALGETKVPKNPEKVVVFDVGALDTLDALGVKVVGVPKSsTLPEYLKKYKDDKYANVGTLFEPDLEAIAALKPDLIIIGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 128 RFADHYEEIKKLVPNaavIDLNFDVSekatkpgeNLVKGLKDSTTTLGKIFAKDKEAKQLVADFDKSIEKAKSAYNGKDK 207
Cdd:cd01140 81 RLAEKYDELKKIAPT---IDLGADLK--------NYLESVKQNIETLGKIFGKEEEAKELVAEIDASIAEAKSAAKGKKK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 208 VMSVIVTGGNIGFAAPHSgrVWGPMYEIFGWTPALEVSNstAGHKGDDVSVEAIAQTNPDWIFVLDRDAATSdaAKSTPA 287
Cdd:cd01140 150 ALVVLVNGGKLSAFGPGS--RFGWLHDLLGFEPADENIK--ASSHGQPVSFEYILEANPDWLFVIDRGAAIG--AEGSSA 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 446676110 288 KDVISKSPaLQNTTAVSKKQVIYAPEDTYTNESIQTyiELFGNMAKTLAK 337
Cdd:cd01140 224 KEVLDNDL-VKNTTAWKNGKVIYLDPDLWYLSGGGL--ESLKQMIDDLKK 270
|
|
| FecB |
COG4594 |
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ... |
1-317 |
3.78e-36 |
|
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443650 [Multi-domain] Cd Length: 316 Bit Score: 132.74 E-value: 3.78e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 1 MKKTMLLklvSILAIFTLMLVACSDSSKETSKATKDNGsdkpkTVEITDAHGKVTVPVNPKNVVALDNRTFETLADWGIK 80
Cdd:COG4594 1 MKKLLLL---LILLLALLLLAACGSSSSDSSSSEAAAG-----ARTVKHAMGETTIPGTPKRVVVLEWSFADALLALGVT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 81 LAAA-----PKDIMPADSayKKDEKVQNIGNHREPNLEIIAAANPDLVI-VGQRFADHYEEIKKLVPNAAVIDLNFDVSE 154
Cdd:COG4594 73 PVGIaddndYDRWVPYLR--DLIKGVTSVGTRSQPNLEAIAALKPDLIIaDKSRHEAIYDQLSKIAPTVLFKSRNGDYQE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 155 KAtkpgenlvkglkDSTTTLGKIFAKDKEAKQLVADFDKSIEKAKSAYNGKDKVMSVIVTggniGFAAPHSgRVWGP--- 231
Cdd:COG4594 151 NL------------ESFKTIAKALGKEEEAEAVLADHDQRIAEAKAKLAAADKGKKVAVG----QFRADGL-RLYTPnsf 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 232 ---MYEIFGWTPALEVSNSTA-GHKGddVSVEAIAQTNPDWIFVldrdAATSDAAkstpAKDVISKSPALQNTTAVSKKQ 307
Cdd:COG4594 214 agsVLAALGFENPPKQSKDNGyGYSE--VSLEQLPALDPDVLFI----ATYDDPS----ILKEWKNNPLWKNLKAVKNGR 283
|
330
....*....|
gi 446676110 308 VIYAPEDTYT 317
Cdd:COG4594 284 VYEVDGDLWT 293
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
64-314 |
1.07e-34 |
|
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: 126.71 E-value: 1.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 64 VALDNRTFETLADWGIKLAAAPKDIMPAD-SAYKKDEKVQNIGNHREPNLEIIAAANPDLVIVGQRFADHyEEIKKLVPN 142
Cdd:pfam01497 1 AALSPAYTEILYALGATDSIVGVDAYTRDpLKADAVAAIVKVGAYGEINVERLAALKPDLVILSTGYLTD-EAEELLSLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 143 AAVIDLNFDvsekatkpgeNLVKGLKDSTTTLGKIFAKDKEAKQLVADFDKSIEKAKSAYN-GKDKVMSVIVTGGNIGFA 221
Cdd:pfam01497 80 IPTVIFESS----------STGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPsLTRKPVLVFGGADGGGYV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 222 APHSGRVWGPMYEIFGWTPALEVSNstaGHKGDDVSVEAIAQTNPDWIFVLDRDAATSDAAkstpakDVISKSPALQNTT 301
Cdd:pfam01497 150 VAGSNTYIGDLLRILGIENIAAELS---GSEYAPISFEAILSSNPDVIIVSGRDSFTKTGP------EFVAANPLWAGLP 220
|
250
....*....|...
gi 446676110 302 AVSKKQVIYAPED 314
Cdd:pfam01497 221 AVKNGRVYTLPSD 233
|
|
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
63-314 |
9.39e-32 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 119.72 E-value: 9.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 63 VVALDNRTFETLADWGI--KLAAAPKDIMpADSAYKKDEKVQNIGNHREPNLEIIAAANPDLVIVG--QRFADHYEEIKK 138
Cdd:COG0614 3 IVSLSPSATELLLALGAgdRLVGVSDWGY-CDYPELELKDLPVVGGTGEPNLEAILALKPDLVLASssGNDEEDYEQLEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 139 LvpNAAVIDLNFdvsekatkpgeNLVKGLKDSTTTLGKIFAKDKEAKQLVADFDKSIEKAKSAYNGKDKVMSVIV---TG 215
Cdd:COG0614 82 I--GIPVVVLDP-----------RSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGAEERPTVLYeiwSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 216 GNIGFAAPHSGrvWGPMYEIFGWTPALEVSNSTAGhkgdDVSVEAIAQTNPDWIFVLDRDAATSDAAKstpAKDVISKSP 295
Cdd:COG0614 149 DPLYTAGGGSF--IGELLELAGGRNVAADLGGGYP----EVSLEQVLALDPDVIILSGGGYDAETAEE---ALEALLADP 219
|
250
....*....|....*....
gi 446676110 296 ALQNTTAVSKKQVIYAPED 314
Cdd:COG0614 220 GWQSLPAVKNGRVYVVPGD 238
|
|
| FhuD |
cd01146 |
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ... |
59-315 |
7.13e-25 |
|
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: 101.21 E-value: 7.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 59 NPKNVVALDNRTFETLADWGIKLAAAPKDI-MPADSAYKKD--EKVQNIGNHREPNLEIIAAANPDLVIVGQRFADH-YE 134
Cdd:cd01146 2 KPQRIVALDWGALETLLALGVKPVGVADTAgYKPWIPEPALplEGVVDVGTRGQPNLEAIAALKPDLILGSASRHDEiYD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 135 EIKKLVPNAAVidlnfdvsekatkPGENLVKGLKDSTTTLGKIFAKDKEAKQLVADFDKSIEKAKSAYNGK-DKVMSViv 213
Cdd:cd01146 82 QLSQIAPTVLL-------------DSSPWLAEWKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKLPDKgPKPVSV-- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 214 tggnIGFAAPHSGRVWGPMYEIFGWTPALEVSNSTAGHKGDD-----VSVEAIAQTNPDWIFVLDRDAAtsdaakstPAK 288
Cdd:cd01146 147 ----VRFSDAGSIRLYGPNSFAGSVLEDLGLQNPWAQETTNDsgfatISLERLAKADADVLFVFTYEDE--------ELA 214
|
250 260
....*....|....*....|....*..
gi 446676110 289 DVISKSPALQNTTAVSKKQVIYAPEDT 315
Cdd:cd01146 215 QALQANPLWQNLPAVKNGRVYVVDDVW 241
|
|
| FeuA |
cd01138 |
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ... |
52-309 |
4.89e-23 |
|
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: 95.86 E-value: 4.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 52 GKVTVPVNPKNVVALdNRTFETLADWGIKLAAAPkDIMPADSAYKKDEKVQNIGNHREPNLEIIAAANPDLVIVGQRFAD 131
Cdd:cd01138 1 GEVEIPAKPKRIVAL-SGETEGLALLGIKPVGAA-SIGGKNPYYKKKTLAKVVGIVDEPNLEKVLELKPDLIIVSSKQEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 132 HYEEIKKLVPNAAVIDLNFDVSEKatkpgenlvkgLKDstttLGKIFAKDKEAKQLVADFDKSIEKAKSAYNGK---DKV 208
Cdd:cd01138 79 NYEKLSKIAPTVPVSYNSSDWEEQ-----------LKE----IGKLLNKEDEAEKWLADYKQKAKEAKEKIKKKlgnDKS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 209 MSVIVTGGNIgFAAPHSGRVWGPMYEIFGWTPALEVSNSTAGHKG-DDVSVEAIAQTNPDWIFVLDrdaatsdaAKSTPA 287
Cdd:cd01138 144 VAVLRGRKQI-YVFGEDGRGGGPILYADLGLKAPEKVKEIEDKPGyAAISLEVLPEFDADYIFLLF--------FTGPEA 214
|
250 260
....*....|....*....|..
gi 446676110 288 KDVISKSPALQNTTAVSKKQVI 309
Cdd:cd01138 215 KADFESLPIWKNLPAVKNNHVY 236
|
|
| PRK10957 |
PRK10957 |
iron-enterobactin transporter periplasmic binding protein; Provisional |
13-316 |
1.49e-18 |
|
iron-enterobactin transporter periplasmic binding protein; Provisional
Pssm-ID: 236806 [Multi-domain] Cd Length: 317 Bit Score: 84.64 E-value: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 13 LAIFTLMLVACSDSSKETSkatkdngsDKPKTVeiTDAHGKVTVPVNPKNVVAldnrTFETLAdwGIKLA---------- 82
Cdd:PRK10957 7 LLLLGLLLSGIAAAQASAA--------GWPRTV--TDSRGSVTLESKPQRIVS----TSVTLT--GTLLAidapviasga 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 83 AAPKDIMP---------ADSAYKKDEKVQNIGnhrEPNLEIIAAANPDLVIV----GQRFADHYEEIKKLVPnaaVIDLN 149
Cdd:PRK10957 71 TTPNTRVAddqgffrqwSDVAKERGVEVLYIG---EPDAEAVAAQMPDLIVIsatgGDSALALYDQLSAIAP---TLVID 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 150 FDvsekatkpgenlVKGLKDSTTTLGKIFAKDKEAKQLVADFDKSIEKAKSAYNGKDKVMSVIVTGGnigfaAPHSGRVW 229
Cdd:PRK10957 145 YD------------DKSWQELATQLGEATGLEKQAAAVIAQFDAQLAEVKAKITLPPQPVSALVYNG-----AGHSANLW 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 230 ------GPMYEIFGWT----PALEVSNSTAGHKGD--DVSVEAIAQ-TNPDWIFVLdrdAATSDAAkstpakDVISKSPA 296
Cdd:PRK10957 208 tpesaqGQLLEQLGFTlaelPAGLQASTSQGKRHDiiQLGGENLAAgLNGETLFLF---AGDDKDA------DAFLADPL 278
|
330 340
....*....|....*....|
gi 446676110 297 LQNTTAVSKKQVIYAPEDTY 316
Cdd:PRK10957 279 LANLPAVQNKQVYALGTDTF 298
|
|
| TroA-like |
cd00636 |
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ... |
61-215 |
1.97e-18 |
|
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: 80.68 E-value: 1.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 61 KNVVALDNRTFETLADWG--IKLAAAPKDIMPADSAYKKDEKVQNIGNHREPNLEIIAAANPDLVIVGQRFADHYEEIKK 138
Cdd:cd00636 1 KRVVALDPGATELLLALGgdDKPVGVADPSGYPPEAKALLEKVPDVGHGYEPNLEKIAALKPDLIIANGSGLEAWLDKLS 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446676110 139 lvpNAAVIDLNFDVSEKATkpgenlVKGLKDSTTTLGKIFAKDKEAKQLVADFDKSIEKAKSAYNGKDKVMSVIVTG 215
Cdd:cd00636 81 ---KIAIPVVVVDEASELS------LENIKESIRLIGKALGKEENAEELIAELDARLAELRAKLAKIPKKKVSLVVG 148
|
|
| TroA_a |
cd01148 |
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ... |
60-312 |
8.30e-16 |
|
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: 76.22 E-value: 8.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 60 PKNVVALDNRTFETLADWGIK-----LAAAPKDIMPA-DSAYKKDEKVqnigNHREPNLEIIAAANPDLVIVG-QRFADh 132
Cdd:cd01148 18 PQRVVSNDQNTTEMMLALGLQdrmvgTAGIDNKDLPElKAKYDKVPEL----AKKYPSKETVLAARPDLVFGGwSYGFD- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 133 yeeIKKLVPNAAVIDLNFDVSEK----ATKPGENLVKGLKDSTTTLGKIFAKDKEAKQLVADFDKSIEKAKSAYNGKDKV 208
Cdd:cd01148 93 ---KGGLGTPDSLAELGIKTYILpescGQRRGEATLDDVYNDIRNLGKIFDVEDRADKLVADLKARLAEISAKVKGDGKK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 209 MSVIV----TGGNI---GFAAPHsgrvwgPMYEIFGWTPALEVSNSTAGhkgdDVSVEAIAQTNPDWIFVLDRDAATSDA 281
Cdd:cd01148 170 VAVFVydsgEDKPFtsgRGGIPN------AIITAAGGRNVFADVDESWT----TVSWETVIARNPDVIVIIDYGDQNAAE 239
|
250 260 270
....*....|....*....|....*....|.
gi 446676110 282 AKstpaKDVISKSPALQNTTAVSKKQVIYAP 312
Cdd:cd01148 240 QK----IKFLKENPALKNVPAVKNNRFIVLP 266
|
|
| TroA_e |
cd01142 |
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ... |
44-316 |
1.78e-15 |
|
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: 75.47 E-value: 1.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 44 TVEITDAHG-KVTVPVNPKNVVALDNRTFETLADWGI-KLAAAPKDIMPADSAYKK----DEKVQNIGNHREPNLEIIAA 117
Cdd:cd01142 7 TRTITDMAGrKVTIPDEVKRIAALWGAGNAVVAALGGgKLIVATTSTVQQEPWLYRlapsLENVATGGTGNDVNIEELLA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 118 ANPDLVIVGQRFADhyEEIKKLVPNaavidLNFDVSEKATKpgenlvKGLKDSTTTLGKIFAKDKEAKQLVADFDKSIEK 197
Cdd:cd01142 87 LKPDVVIVWSTDGK--EAGKAVLRL-----LNALSLRDAEL------EEVKLTIALLGELLGRQEKAEALVAYFDDNLAY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 198 AKSAYNG--KDKVMSVIVTGGNIGFAAPhSGRVWGPMYEIFGWTPALEVsnstAGHKGD-DVSVEAIAQTNPDWIFVLDR 274
Cdd:cd01142 154 VAARTKKlpDSERPRVYYAGPDPLTTDG-TGSITNSWIDLAGGINVASE----ATKKGSgEVSLEQLLKWNPDVIIVGNA 228
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 446676110 275 DaatsdaakstpAKDVISKSPALQNTTAVSKKQVIYAPEDTY 316
Cdd:cd01142 229 D-----------TKAAILADPRWQNLRAVKNGRVYVNPEGAF 259
|
|
| fecB |
PRK11411 |
iron-dicitrate transporter substrate-binding subunit; Provisional |
38-309 |
6.34e-14 |
|
iron-dicitrate transporter substrate-binding subunit; Provisional
Pssm-ID: 183123 [Multi-domain] Cd Length: 303 Bit Score: 71.24 E-value: 6.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 38 GSDKPKTVEITDAHGKVTVPVNPKNVVALDNRTFETLADWGIK-LAAA----PKDIMPAdsAYKKDEKVQNIGNHREPNL 112
Cdd:PRK11411 17 GSSHAFAVTVQDEQGTFTLEKTPQRIVVLELSFVDALAAVGVSpVGVAddndAKRILPE--VRAHLKPWQSVGTRSQPSL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 113 EIIAAANPDLVIV-GQRFADHYEEIKKLVPnaaVIDLNfdvSEKATKPgENLvkglkDSTTTLGKIFAKDKEAKQLVADF 191
Cdd:PRK11411 95 EAIAALKPDLIIAdSSRHAGVYIALQKIAP---TLLLK---SRNETYQ-ENL-----QSAAIIGEVLGKKREMQARIEQH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 192 DKSIEKAKSAYNGKDKVmsVIVTGGNIGFAAPHSGRVWGPMYEIFGwtpaLEVSNSTAGHKG-DDVSVEAIAQTNPDWIF 270
Cdd:PRK11411 163 KERMAQFASQLPKGTRV--AFGTSREQQFNLHSPESYTGSVLAALG----LNVPKAPMNGAAmPSISLEQLLALNPDWLL 236
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 446676110 271 VldrdaatsdAAKSTPA-KDVISKSPALQNTTAVSKKQVI 309
Cdd:PRK11411 237 V---------AHYRQESiVKRWQQDPLWQMLTAAKKQQVA 267
|
|
| ChuT |
COG4558 |
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ... |
99-309 |
2.93e-11 |
|
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443619 [Multi-domain] Cd Length: 285 Bit Score: 63.29 E-value: 2.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 99 EKVQNIGNHREPNLEIIAAANPDLVIVGQRfADHYEEIKKLvpNAAVIDLNFdVSEKATkpgenlVKGLKDSTTTLGKIF 178
Cdd:COG4558 64 KALPDVGYMRQLSAEGILSLKPTLVLASEG-AGPPEVLDQL--RAAGVPVVV-VPAAPS------LEGVLAKIRAVAAAL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 179 AKDKEAKQLVADFDKSIEKAKSAYNGKD---KVMSVIVTGGNIGFAAphsGRVWGP--MYEIFGwtpaleVSNSTAGHKG 253
Cdd:COG4558 134 GVPEAGEALAARLEADLAALAARVAAIGkppRVLFLLSRGGGRPMVA---GRGTAAdaLIRLAG------GVNAAAGFEG 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446676110 254 -DDVSVEAIAQTNPDWIFVLDRDaatsdaAKSTPAKDVISKSPALQNTTAVSKKQVI 309
Cdd:COG4558 205 yKPLSAEALIAAAPDVILVMTRG------LESLGGVDGLLALPGLAQTPAGKNKRIV 255
|
|
| YvrC |
cd01143 |
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ... |
59-271 |
6.93e-11 |
|
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: 60.75 E-value: 6.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 59 NPKNVVALDNRTFETLADWGiklaaAPKDIMPAD--SAYKKD-EKVQNIGNHREPNLEIIAAANPDLVIVGQRFADH-YE 134
Cdd:cd01143 2 EPERIVSLSPSITEILFALG-----AGDKIVGVDtySNYPKEvRKKPKVGSYSNPNVEKIVALKPDLVIVSSSSLAElLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 135 EIKKLVPNAAVIdlnfdvsekatkPGENLVKGLKDSTTTLGKIFAKDKEAKQLVADFDKSIEKAKSAYNGKDKvMSV--- 211
Cdd:cd01143 77 KLKDAGIPVVVL------------PAASSLDEIYDQIELIGKITGAEEEAEKLVKEMKQKIDKVKDKGKTIKK-SKVyie 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446676110 212 -----IVTGGNIGFAaphsgrvwGPMYEIFGwtpALEVSNSTAGHKgdDVSVEAIAQTNPDWIFV 271
Cdd:cd01143 144 vslggPYTAGKNTFI--------NELIRLAG---AKNIAADSGGWP--QVSPEEILKANPDVIIL 195
|
|
| HemV-2 |
cd01147 |
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ... |
56-312 |
5.67e-10 |
|
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: 58.89 E-value: 5.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 56 VPVNPKNVVALDNRTFETLAdwgikLAAAPKDIMPADSAYKKDEKVQNIGNHRE---------------PNLEIIAAANP 120
Cdd:cd01147 1 VPKPVERVVAAGPGALRLLY-----ALAAPDKIVGVDDAEKSDEGRPYFLASPElkdlpvigrggrgntPNYEKIAALKP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 121 DLVI--VGQRFADHYEEIKKLVpNAAVIDLNfdvsekatkpGENLVKGLKDSTTTLGKIFAKDKEAKQLVADFDKSIEKA 198
Cdd:cd01147 76 DVVIdvGSDDPTSIADDLQKKT-GIPVVVLD----------GGDSLEDTPEQIRLLGKVLGKEERAEELISFIESILADV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 199 KSAYNGKDKVMSVIVTGGNIGFAAPHsGRVWG--PMYEIFGWTPALEVSNSTAGHKGDDVSVEAIAQTNPDWIFVldRDA 276
Cdd:cd01147 145 EERTKDIPDEEKPTVYFGRIGTKGAA-GLESGlaGSIEVFELAGGINVADGLGGGGLKEVSPEQILLWNPDVIFL--DTG 221
|
250 260 270
....*....|....*....|....*....|....*.
gi 446676110 277 ATSDaakstPAKDVISKSPALQNTTAVSKKQVIYAP 312
Cdd:cd01147 222 SFYL-----SLEGYAKNRPFWQSLKAVKNGRVYLLP 252
|
|
| TroA_f |
cd01139 |
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ... |
45-309 |
2.02e-09 |
|
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: 58.09 E-value: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 45 VEITDAHG-KVTVPVNPKNVV-----------ALD-NRTFETLADWGIKLAAAPKDIMPAdsaYKKD----EKVQNIGN- 106
Cdd:cd01139 1 ITVTDVAGrKVTLDAPVERVLlgegrqlyalaLLEgENPFARIVGWGGDLKKGDPDTYAK---YKEKfpeiADIPLIGSt 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 107 -HREPNLEIIAAANPDLVIVGQRFADHYEE---IKKL----VPnAAVIDLNFDVsEKATKPgenlvkglkdSTTTLGKIF 178
Cdd:cd01139 78 yNGDFSVEKVLTLKPDLVILNIWAKTTAEEsgiLEKLeqagIP-VVFVDFRQKP-LKNTTP----------SMRLLGKAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 179 AKDKEAKQLVADFDKSIEKAKS---AYNG-KDKVMsvIVTGGNigfAAPHSGRV-----WGPMYEIFGwtpALEVSNSTA 249
Cdd:cd01139 146 GREERAEEFIEFYQERIDRIRDrlaKINEpKPKVF--IELGAG---GPEECCSTygngnWGELVDAAG---GDNIADGLI 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446676110 250 GHKGDDVSVEAIAQTNPDWIFVLDRDAAT-----SDAAKSTPAK------DVISKSPALQNTTAVSKKQVI 309
Cdd:cd01139 218 PGTSGELNAEYVIAANPEIIIATGGNWAKdpsgvSLGPDGTTADakesllRALLKRPGWSSLQAVKNGRVY 288
|
|
| BtuF |
cd01144 |
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ... |
100-316 |
1.29e-06 |
|
Cobalamin binding protein BtuF. These proteins have been shown to function as initial receptors in ABC transport of vitamin B12 (cobalamin) in eubacterial and some archaeal species. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains. In addition, these proteins sometimes have a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence).
Pssm-ID: 238564 [Multi-domain] Cd Length: 245 Bit Score: 48.84 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 100 KVQNIGNHREPNLEIIAAANPDLVIVgQRFADHYEEIKKLVpnAAVIDLNfdVSEKATkpgenlVKGLKDSTTTLGKIFA 179
Cdd:cd01144 38 KLPRVGGFYQLDLERVLALKPDLVIA-WDDCNVCAVVDQLR--AAGIPVL--VSEPQT------LDDILADIRRLGTLAG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 180 KDKEAKQLVADFDKSIEKAKSAYNGKDKVMSVIVTGGNIGFAAphsGRVWGP-MYEIFGWTPALevsnSTAGHKGDDVSV 258
Cdd:cd01144 107 RPARAEELAEALRRRLAALRKQYASKPPPRVFYQEWIDPLMTA---GGDWVPeLIALAGGVNVF----ADAGERSPQVSW 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446676110 259 EAIAQTNPDWIFVldrdaatSDAAKSTPAKDVIsKSPALQNTTAVSKKQVIYAPEDTY 316
Cdd:cd01144 180 EDVLAANPDVIVL-------SPCGFGFTPAILR-KEPAWQALPAVRNGRVYAVDGNWY 229
|
|
| HutB |
cd01149 |
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ... |
100-309 |
1.96e-04 |
|
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: 42.25 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 100 KVQNIGNHREPNLEIIAAANPDLVIvGQRFADHYEEIKKLvpNAAVIDLNFdVSEKATKpgenlvKGLKDSTTTLGKIFA 179
Cdd:cd01149 39 KLPDVGYMRQLSAEGVLSLKPTLVI-ASDEAGPPEALDQL--RAAGVPVVT-VPSTPTL------DGLLTKIRQVAQALG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 180 KDKEAKQLVADFDKSIEKA---KSAYNGKDKVMSVIVTGGNIGFAA-PHSGRVWgpMYEIFGWTpalevsNSTAGHKG-D 254
Cdd:cd01149 109 VPEKGEALAQEVRQRLAALrktVAAHKKPPRVLFLLSHGGGAAMAAgRNTAADA--IIALAGAV------NAAAGFRGyK 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446676110 255 DVSVEAIAQTNPDWIFVLDRdaatsdAAKSTPAKDVISKSPALQNTTAVSKKQVI 309
Cdd:cd01149 181 PLSAEALIAAQPDVILVMSR------GLDAVGGVDGLLKLPGLAQTPAGRNKRIL 229
|
|
| TroA_d |
cd01141 |
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ... |
54-139 |
3.36e-04 |
|
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: 40.87 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446676110 54 VTVPVNPKNVVALDNRTFETLADwgikLAAAPKDIMPADSAY-KKDEKVQN-----IGNHREPNLEIIAAANPDLVIVGQ 127
Cdd:cd01141 2 KTIKVPPKRIVVLSPTHVDLLLA----LDKADKIVGVSASAYdLNTPAVKEridiqVGPTGSLNVELIVALKPDLVILYG 77
|
90
....*....|..
gi 446676110 128 RFADHyEEIKKL 139
Cdd:cd01141 78 GFQAQ-TILDKL 88
|
|
| |
