|
Name |
Accession |
Description |
Interval |
E-value |
| CeuA |
COG4607 |
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and ... |
8-330 |
3.13e-108 |
|
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443657 [Multi-domain] Cd Length: 310 Bit Score: 317.89 E-value: 3.13e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 8 RTATAVLTAVPLALVLAACGADTESQAGETTGGgeprTVTIEDNHGSVEVPVDPARVVALDNHVFETLSAWDVPLAAAPK 87
Cdd:COG4607 2 KKTLLAALALAAALALAACGSSSAAAASAAAAE----TVTVEHALGTVEVPKNPKRVVVFDNGALDTLDALGVEVAGVPK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 88 GIMGDGLwPEYTDDDaVLDVGMHREPNLESIVAAEPDLIIGGYRFSDSYDDIKAQNPdavVIEIApREGEDQAAELARQT 167
Cdd:COG4607 78 GLLPDYL-SKYADDK-YANVGTLFEPDLEAIAALKPDLIIIGGRSAKKYDELSKIAP---TIDLT-VDGEDYLESLKRNT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 168 EILGEIFDRQDEAAAIVADYDAAVDAARTAYDGQSTVVGLITSGGEISYSAPvtGRSIGVLFPALGLQPAIEQAAEDTsH 247
Cdd:COG4607 152 ETLGEIFGKEDEAEELVADLDAKIAALKAAAAGKGTALIVLTNGGKISAYGP--GSRFGPIHDVLGFKPADEDIEAST-H 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 248 GDDISVEAIASANPDWIIVLDRDgAGVGEGEyrPAKELIEGSEALASVTAVAEQQVVYLDPD-FYLTE-DIQAYTALYEQ 325
Cdd:COG4607 229 GQAISFEFIAEANPDWLFVIDRD-AAIGGEG--PAAKQVLDNELVKQTTAWKNGQIVYLDPDaWYLAGgGIQSLTEMLDE 305
|
....*
gi 502628837 326 IAQAF 330
Cdd:COG4607 306 VADAL 310
|
|
| FatB |
cd01140 |
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ... |
50-327 |
2.12e-61 |
|
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: 197.10 E-value: 2.12e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 50 DNHGSVEVPVDPARVVALDNHVFETLSAWDVPLAAAPKgimgDGLWPEYTD---DDAVLDVGMHREPNLESIVAAEPDLI 126
Cdd:cd01140 1 HALGETKVPKNPEKVVVFDVGALDTLDALGVKVVGVPK----SSTLPEYLKkykDDKYANVGTLFEPDLEAIAALKPDLI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 127 IGGYRFSDSYDDIKAQNPdAVVIEIAPRegeDQAAELARQTEILGEIFDRQDEAAAIVADYDAAVDAARTAYDGQSTVVG 206
Cdd:cd01140 77 IIGGRLAEKYDELKKIAP-TIDLGADLK---NYLESVKQNIETLGKIFGKEEEAKELVAEIDASIAEAKSAAKGKKKALV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 207 LITSGGEISYSAPvtGRSIGVLFPALGLQPAIEQaAEDTSHGDDISVEAIASANPDWIIVLDRDgAGVGEGEyRPAKELI 286
Cdd:cd01140 153 VLVNGGKLSAFGP--GSRFGWLHDLLGFEPADEN-IKASSHGQPVSFEYILEANPDWLFVIDRG-AAIGAEG-SSAKEVL 227
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 502628837 287 EgSEALASVTAVAEQQVVYLDPD-FYLTED-IQAYTALYEQIA 327
Cdd:cd01140 228 D-NDLVKNTTAWKNGKVIYLDPDlWYLSGGgLESLKQMIDDLK 269
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
65-309 |
1.04e-27 |
|
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: 108.22 E-value: 1.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 65 VALDNHVFETLSAWDVPLAAAPKgIMGDGLWPEYTDDDAVLDVGMHREPNLESIVAAEPDLIIGGYRFSDSyDDIKAQNP 144
Cdd:pfam01497 1 AALSPAYTEILYALGATDSIVGV-DAYTRDPLKADAVAAIVKVGAYGEINVERLAALKPDLVILSTGYLTD-EAEELLSL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 145 DAVVIEIAPREgedQAAELARQTEILGEIFDRQDEAAAIVADYDAAVDAARTAYD--GQSTVVgLITSGGEISYSAPVTG 222
Cdd:pfam01497 79 IIPTVIFESSS---TGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPslTRKPVL-VFGGADGGGYVVAGSN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 223 RSIGVLFPALGLQPAIeqAAEDTSHGDDISVEAIASANPDWIIVLDRDgagvgeGEYRPAKELIEGSEALASVTAVAEQQ 302
Cdd:pfam01497 155 TYIGDLLRILGIENIA--AELSGSEYAPISFEAILSSNPDVIIVSGRD------SFTKTGPEFVAANPLWAGLPAVKNGR 226
|
....*..
gi 502628837 303 VVYLDPD 309
Cdd:pfam01497 227 VYTLPSD 233
|
|
| fecB |
PRK11411 |
iron-dicitrate transporter substrate-binding subunit; Provisional |
45-309 |
4.01e-13 |
|
iron-dicitrate transporter substrate-binding subunit; Provisional
Pssm-ID: 183123 [Multi-domain] Cd Length: 303 Bit Score: 68.93 E-value: 4.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 45 TVTIEDNHGSVEVPVDPARVVALDNHVFETLSAWDVplaaAPKGIMGDGlwpeytDDDAVL-----------DVGMHREP 113
Cdd:PRK11411 23 AVTVQDEQGTFTLEKTPQRIVVLELSFVDALAAVGV----SPVGVADDN------DAKRILpevrahlkpwqSVGTRSQP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 114 NLESIVAAEPDLIIG-GYRFSDSYDDIKaqnpdavviEIAP-----REGEDQAAELaRQTEILGEIFDRQDEAAA-IVAD 186
Cdd:PRK11411 93 SLEAIAALKPDLIIAdSSRHAGVYIALQ---------KIAPtlllkSRNETYQENL-QSAAIIGEVLGKKREMQArIEQH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 187 YDAAVDAARTAYDGQSTVVGLITSGG-EISYSAPVTGrsiGVLfPALGLQPAIeqAAEDTSHGDDISVEAIASANPDWII 265
Cdd:PRK11411 163 KERMAQFASQLPKGTRVAFGTSREQQfNLHSPESYTG---SVL-AALGLNVPK--APMNGAAMPSISLEQLLALNPDWLL 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 502628837 266 VldrdgagvgeGEYRpaKELIEGS---EALASV-TAVAEQQVVYLDPD 309
Cdd:PRK11411 237 V----------AHYR--QESIVKRwqqDPLWQMlTAAKKQQVASVDSN 272
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CeuA |
COG4607 |
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and ... |
8-330 |
3.13e-108 |
|
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443657 [Multi-domain] Cd Length: 310 Bit Score: 317.89 E-value: 3.13e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 8 RTATAVLTAVPLALVLAACGADTESQAGETTGGgeprTVTIEDNHGSVEVPVDPARVVALDNHVFETLSAWDVPLAAAPK 87
Cdd:COG4607 2 KKTLLAALALAAALALAACGSSSAAAASAAAAE----TVTVEHALGTVEVPKNPKRVVVFDNGALDTLDALGVEVAGVPK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 88 GIMGDGLwPEYTDDDaVLDVGMHREPNLESIVAAEPDLIIGGYRFSDSYDDIKAQNPdavVIEIApREGEDQAAELARQT 167
Cdd:COG4607 78 GLLPDYL-SKYADDK-YANVGTLFEPDLEAIAALKPDLIIIGGRSAKKYDELSKIAP---TIDLT-VDGEDYLESLKRNT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 168 EILGEIFDRQDEAAAIVADYDAAVDAARTAYDGQSTVVGLITSGGEISYSAPvtGRSIGVLFPALGLQPAIEQAAEDTsH 247
Cdd:COG4607 152 ETLGEIFGKEDEAEELVADLDAKIAALKAAAAGKGTALIVLTNGGKISAYGP--GSRFGPIHDVLGFKPADEDIEAST-H 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 248 GDDISVEAIASANPDWIIVLDRDgAGVGEGEyrPAKELIEGSEALASVTAVAEQQVVYLDPD-FYLTE-DIQAYTALYEQ 325
Cdd:COG4607 229 GQAISFEFIAEANPDWLFVIDRD-AAIGGEG--PAAKQVLDNELVKQTTAWKNGQIVYLDPDaWYLAGgGIQSLTEMLDE 305
|
....*
gi 502628837 326 IAQAF 330
Cdd:COG4607 306 VADAL 310
|
|
| FatB |
cd01140 |
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ... |
50-327 |
2.12e-61 |
|
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: 197.10 E-value: 2.12e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 50 DNHGSVEVPVDPARVVALDNHVFETLSAWDVPLAAAPKgimgDGLWPEYTD---DDAVLDVGMHREPNLESIVAAEPDLI 126
Cdd:cd01140 1 HALGETKVPKNPEKVVVFDVGALDTLDALGVKVVGVPK----SSTLPEYLKkykDDKYANVGTLFEPDLEAIAALKPDLI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 127 IGGYRFSDSYDDIKAQNPdAVVIEIAPRegeDQAAELARQTEILGEIFDRQDEAAAIVADYDAAVDAARTAYDGQSTVVG 206
Cdd:cd01140 77 IIGGRLAEKYDELKKIAP-TIDLGADLK---NYLESVKQNIETLGKIFGKEEEAKELVAEIDASIAEAKSAAKGKKKALV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 207 LITSGGEISYSAPvtGRSIGVLFPALGLQPAIEQaAEDTSHGDDISVEAIASANPDWIIVLDRDgAGVGEGEyRPAKELI 286
Cdd:cd01140 153 VLVNGGKLSAFGP--GSRFGWLHDLLGFEPADEN-IKASSHGQPVSFEYILEANPDWLFVIDRG-AAIGAEG-SSAKEVL 227
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 502628837 287 EgSEALASVTAVAEQQVVYLDPD-FYLTED-IQAYTALYEQIA 327
Cdd:cd01140 228 D-NDLVKNTTAWKNGKVIYLDPDlWYLSGGgLESLKQMIDDLK 269
|
|
| FecB |
COG4594 |
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ... |
8-309 |
1.96e-30 |
|
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443650 [Multi-domain] Cd Length: 316 Bit Score: 117.33 E-value: 1.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 8 RTATAVLTAVPLALVLAACGADTESQAGETTGGGeprTVTIEDNHGSVEVPVDPARVVALDNHVFETLSAWDVplaaAPK 87
Cdd:COG4594 2 KKLLLLLILLLALLLLAACGSSSSDSSSSEAAAG---ARTVKHAMGETTIPGTPKRVVVLEWSFADALLALGV----TPV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 88 GIMGDG---LWPEYTDD--DAVLDVGMHREPNLESIVAAEPDLIIG-GYRFSDSYDDIKAqnpdavvieIAP----REGE 157
Cdd:COG4594 75 GIADDNdydRWVPYLRDliKGVTSVGTRSQPNLEAIAALKPDLIIAdKSRHEAIYDQLSK---------IAPtvlfKSRN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 158 DQAAELARQTEILGEIFDRQDEAAAIVADYDAAVDAART----AYDGQSTVVGLITSGG-----EISYSapvtgrsiGVL 228
Cdd:COG4594 146 GDYQENLESFKTIAKALGKEEEAEAVLADHDQRIAEAKAklaaADKGKKVAVGQFRADGlrlytPNSFA--------GSV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 229 FPALGLQPAIEQAAEDTSHGDDISVEAIASANPDWIIVL-DRDGAGVGEgeyrpakelIEGSEALASVTAVAEQQVVYLD 307
Cdd:COG4594 218 LAALGFENPPKQSKDNGYGYSEVSLEQLPALDPDVLFIAtYDDPSILKE---------WKNNPLWKNLKAVKNGRVYEVD 288
|
..
gi 502628837 308 PD 309
Cdd:COG4594 289 GD 290
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
65-309 |
1.04e-27 |
|
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: 108.22 E-value: 1.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 65 VALDNHVFETLSAWDVPLAAAPKgIMGDGLWPEYTDDDAVLDVGMHREPNLESIVAAEPDLIIGGYRFSDSyDDIKAQNP 144
Cdd:pfam01497 1 AALSPAYTEILYALGATDSIVGV-DAYTRDPLKADAVAAIVKVGAYGEINVERLAALKPDLVILSTGYLTD-EAEELLSL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 145 DAVVIEIAPREgedQAAELARQTEILGEIFDRQDEAAAIVADYDAAVDAARTAYD--GQSTVVgLITSGGEISYSAPVTG 222
Cdd:pfam01497 79 IIPTVIFESSS---TGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPslTRKPVL-VFGGADGGGYVVAGSN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 223 RSIGVLFPALGLQPAIeqAAEDTSHGDDISVEAIASANPDWIIVLDRDgagvgeGEYRPAKELIEGSEALASVTAVAEQQ 302
Cdd:pfam01497 155 TYIGDLLRILGIENIA--AELSGSEYAPISFEAILSSNPDVIIVSGRD------SFTKTGPEFVAANPLWAGLPAVKNGR 226
|
....*..
gi 502628837 303 VVYLDPD 309
Cdd:pfam01497 227 VYTLPSD 233
|
|
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
63-334 |
1.12e-25 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 103.54 E-value: 1.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 63 RVVALDNHVFETLSAWDVP--LAAAPKGIMGDGLWPEYtddDAVLDVGMHREPNLESIVAAEPDLIIGGY--RFSDSYDD 138
Cdd:COG0614 2 RIVSLSPSATELLLALGAGdrLVGVSDWGYCDYPELEL---KDLPVVGGTGEPNLEAILALKPDLVLASSsgNDEEDYEQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 139 IKAQNPDAVVIEIAPREgedqaaELARQTEILGEIFDRQDEAAAIVADYDAAVDAARTAYDGQS---TVVGLITSGGEIS 215
Cdd:COG0614 79 LEKIGIPVVVLDPRSLE------DLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGAEerpTVLYEIWSGDPLY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 216 YSAPvtGRSIGVLFPALGLQPAieqAAEDTSHGDDISVEAIASANPDWIIVLDrdgAGVGEGEYRPAKELIEGSEALASV 295
Cdd:COG0614 153 TAGG--GSFIGELLELAGGRNV---AADLGGGYPEVSLEQVLALDPDVIILSG---GGYDAETAEEALEALLADPGWQSL 224
|
250 260 270
....*....|....*....|....*....|....*....
gi 502628837 296 TAVAEQQVVYLDPDFYLTEDIQAYTALyEQIAQAFEAAA 334
Cdd:COG0614 225 PAVKNGRVYVVPGDLLSRPGPRLLLAL-EDLAKALHPEL 262
|
|
| FhuD |
cd01146 |
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ... |
60-309 |
4.83e-22 |
|
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: 93.12 E-value: 4.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 60 DPARVVALDNHVFETLSAWDVPLAAAPKgIMGDGLWPEYT--DDDAVLDVGMHREPNLESIVAAEPDLIIG-GYRFSDSY 136
Cdd:cd01146 2 KPQRIVALDWGALETLLALGVKPVGVAD-TAGYKPWIPEPalPLEGVVDVGTRGQPNLEAIAALKPDLILGsASRHDEIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 137 DDIKAqnpdavvieIAP---REGEDQAAELARQTEILGEIFDRQDEAAAIVADYDAAVDAARTAYDGQS-TVVGLITSGG 212
Cdd:cd01146 81 DQLSQ---------IAPtvlLDSSPWLAEWKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKLPDKGpKPVSVVRFSD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 213 EISYSAPVTGRSIGVLFPALGLQPAIEQAAEDTSHGDDISVEAIASANPDWIIVLDRDGAgvgegeyrPAKELIEGSEAL 292
Cdd:cd01146 152 AGSIRLYGPNSFAGSVLEDLGLQNPWAQETTNDSGFATISLERLAKADADVLFVFTYEDE--------ELAQALQANPLW 223
|
250
....*....|....*..
gi 502628837 293 ASVTAVAEQQVVYLDPD 309
Cdd:cd01146 224 QNLPAVKNGRVYVVDDV 240
|
|
| FeuA |
cd01138 |
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ... |
53-313 |
1.08e-15 |
|
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: 75.45 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 53 GSVEVPVDPARVVALdNHVFETLSAWDV-PLAAAPKGimgdGLWPEYTDDDAVLDVGMHREPNLESIVAAEPDLIIGGYR 131
Cdd:cd01138 1 GEVEIPAKPKRIVAL-SGETEGLALLGIkPVGAASIG----GKNPYYKKKTLAKVVGIVDEPNLEKVLELKPDLIIVSSK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 132 FSDSYDDIKAQNPdAVVIEIAPREGEDQAAElarqteiLGEIFDRQDEAAAIVADYDAAVDAART---AYDGQSTVVGLI 208
Cdd:cd01138 76 QEENYEKLSKIAP-TVPVSYNSSDWEEQLKE-------IGKLLNKEDEAEKWLADYKQKAKEAKEkikKKLGNDKSVAVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 209 TSGGEIsYSAPVTGRSIG-VLFPALGLQ-PAIEQAAEDTSHGDDISVEAIASANPDWIIVLDRDGAGvgegeyrpAKELI 286
Cdd:cd01138 148 RGRKQI-YVFGEDGRGGGpILYADLGLKaPEKVKEIEDKPGYAAISLEVLPEFDADYIFLLFFTGPE--------AKADF 218
|
250 260
....*....|....*....|....*...
gi 502628837 287 EGSEALASVTAVAEQQVVYLDPD-FYLT 313
Cdd:cd01138 219 ESLPIWKNLPAVKNNHVYIVDAWvFYFA 246
|
|
| TroA_a |
cd01148 |
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ... |
45-327 |
1.26e-14 |
|
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: 73.14 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 45 TVTIEDNHGSVEVPVDPARVVALDNHVFETLSAwdvpLAAAPKgIMGDGLW-----PEYTDDDAVLDVGMHREPNLESIV 119
Cdd:cd01148 2 PLTVENCGRSVTFDKAPQRVVSNDQNTTEMMLA----LGLQDR-MVGTAGIdnkdlPELKAKYDKVPELAKKYPSKETVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 120 AAEPDLIIGG--YRFSDSYD-DIKAQNPDAVVIEIAP-----REGEDQAAELARQTEILGEIFDRQDEAAAIVAD--YDA 189
Cdd:cd01148 77 AARPDLVFGGwsYGFDKGGLgTPDSLAELGIKTYILPescgqRRGEATLDDVYNDIRNLGKIFDVEDRADKLVADlkARL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 190 AVDAARTAYDGQSTVVGLITSGGEISYSApVTGRSIGVLFPALGLQPAIeqAAEDTSHGdDISVEAIASANPDWIIVLDR 269
Cdd:cd01148 157 AEISAKVKGDGKKVAVFVYDSGEDKPFTS-GRGGIPNAIITAAGGRNVF--ADVDESWT-TVSWETVIARNPDVIVIIDY 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 502628837 270 DgagvGEGEYRPAKELIEGSEALASVTAVAEQQVVYLdPDFYLTEDIQAYTALyEQIA 327
Cdd:cd01148 233 G----DQNAAEQKIKFLKENPALKNVPAVKNNRFIVL-PLAEATPGIRNVDAI-EKLA 284
|
|
| fecB |
PRK11411 |
iron-dicitrate transporter substrate-binding subunit; Provisional |
45-309 |
4.01e-13 |
|
iron-dicitrate transporter substrate-binding subunit; Provisional
Pssm-ID: 183123 [Multi-domain] Cd Length: 303 Bit Score: 68.93 E-value: 4.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 45 TVTIEDNHGSVEVPVDPARVVALDNHVFETLSAWDVplaaAPKGIMGDGlwpeytDDDAVL-----------DVGMHREP 113
Cdd:PRK11411 23 AVTVQDEQGTFTLEKTPQRIVVLELSFVDALAAVGV----SPVGVADDN------DAKRILpevrahlkpwqSVGTRSQP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 114 NLESIVAAEPDLIIG-GYRFSDSYDDIKaqnpdavviEIAP-----REGEDQAAELaRQTEILGEIFDRQDEAAA-IVAD 186
Cdd:PRK11411 93 SLEAIAALKPDLIIAdSSRHAGVYIALQ---------KIAPtlllkSRNETYQENL-QSAAIIGEVLGKKREMQArIEQH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 187 YDAAVDAARTAYDGQSTVVGLITSGG-EISYSAPVTGrsiGVLfPALGLQPAIeqAAEDTSHGDDISVEAIASANPDWII 265
Cdd:PRK11411 163 KERMAQFASQLPKGTRVAFGTSREQQfNLHSPESYTG---SVL-AALGLNVPK--APMNGAAMPSISLEQLLALNPDWLL 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 502628837 266 VldrdgagvgeGEYRpaKELIEGS---EALASV-TAVAEQQVVYLDPD 309
Cdd:PRK11411 237 V----------AHYR--QESIVKRwqqDPLWQMlTAAKKQQVASVDSN 272
|
|
| TroA-like |
cd00636 |
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ... |
63-183 |
3.08e-11 |
|
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: 60.65 E-value: 3.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 63 RVVALDNHVFETLSAwdVPLAAAPKGIMGDGLWPEYTD--DDAVLDVGMHREPNLESIVAAEPDLIIG-GYRFSDSYDDI 139
Cdd:cd00636 2 RVVALDPGATELLLA--LGGDDKPVGVADPSGYPPEAKalLEKVPDVGHGYEPNLEKIAALKPDLIIAnGSGLEAWLDKL 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 502628837 140 KAQNPDAVVIEIAPREGEDQAAELARqteILGEIFDRQDEAAAI 183
Cdd:cd00636 80 SKIAIPVVVVDEASELSLENIKESIR---LIGKALGKEENAEEL 120
|
|
| PRK10957 |
PRK10957 |
iron-enterobactin transporter periplasmic binding protein; Provisional |
12-183 |
4.32e-11 |
|
iron-enterobactin transporter periplasmic binding protein; Provisional
Pssm-ID: 236806 [Multi-domain] Cd Length: 317 Bit Score: 63.07 E-value: 4.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 12 AVLTAVPLALVLAACGADTESQAGEttgggePRTVTieDNHGSVEVPVDPARVVALDNHVFETLSAWDVPL----AAAPK 87
Cdd:PRK10957 3 YRLALLLLGLLLSGIAAAQASAAGW------PRTVT--DSRGSVTLESKPQRIVSTSVTLTGTLLAIDAPViasgATTPN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 88 GIMGD--GL---WPEYTDDD--AVLDVGmhrEPNLESIVAAEPDLIIGGYRFSDS----YDDIKAQNPDAVVieiapREG 156
Cdd:PRK10957 75 TRVADdqGFfrqWSDVAKERgvEVLYIG---EPDAEAVAAQMPDLIVISATGGDSalalYDQLSAIAPTLVI-----DYD 146
|
170 180
....*....|....*....|....*..
gi 502628837 157 EDQAAELARQteiLGEIFDRQDEAAAI 183
Cdd:PRK10957 147 DKSWQELATQ---LGEATGLEKQAAAV 170
|
|
| TroA_e |
cd01142 |
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ... |
45-305 |
4.19e-08 |
|
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: 53.51 E-value: 4.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 45 TVTIEDNHGS-VEVPVDPARVVALD---NHVFETLSAWDVpLAAAPKGIMGDGLWPE-YTDDDAVLDVGMHREPNLESIV 119
Cdd:cd01142 7 TRTITDMAGRkVTIPDEVKRIAALWgagNAVVAALGGGKL-IVATTSTVQQEPWLYRlAPSLENVATGGTGNDVNIEELL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 120 AAEPDLIIGGyrfsdSYDDIKAQnpDAVVIEI---APREGEDQAAELArqTEILGEIFDRQDEAAAIVADYDAAVDAART 196
Cdd:cd01142 86 ALKPDVVIVW-----STDGKEAG--KAVLRLLnalSLRDAELEEVKLT--IALLGELLGRQEKAEALVAYFDDNLAYVAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 197 AY----DGQSTVV------GLITSGGEiSYSAPVTGRSIGVlfpalglqpaieQAAEDTSHGDDISV--EAIASANPDWI 264
Cdd:cd01142 157 RTkklpDSERPRVyyagpdPLTTDGTG-SITNSWIDLAGGI------------NVASEATKKGSGEVslEQLLKWNPDVI 223
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 502628837 265 IVLDRDGagvgegeyrpaKELIEGSEALASVTAVAEQQVVY 305
Cdd:cd01142 224 IVGNADT-----------KAAILADPRWQNLRAVKNGRVYV 253
|
|
| HemV-2 |
cd01147 |
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ... |
57-308 |
1.69e-07 |
|
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors in ABC transport of metal ions. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains. In addition, these proteins sometimes have a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence).
Pssm-ID: 238567 [Multi-domain] Cd Length: 262 Bit Score: 51.57 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 57 VPVDPARVVALDNHVFETLSAWDVP-----LAAAPKGIMGDGLW---PEYTDDDAVLDVGMHREPNLESIVAAEPDLII- 127
Cdd:cd01147 1 VPKPVERVVAAGPGALRLLYALAAPdkivgVDDAEKSDEGRPYFlasPELKDLPVIGRGGRGNTPNYEKIAALKPDVVId 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 128 -GGYRFSDSYDDIKAQ--NPDAVVieiaprEGEDQAAELARQTEILGEIFDRQDEAAAIVADYDAAVDAAR--------- 195
Cdd:cd01147 81 vGSDDPTSIADDLQKKtgIPVVVL------DGGDSLEDTPEQIRLLGKVLGKEERAEELISFIESILADVEertkdipde 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 196 ---TAYDGQSTVVGL--ITSGGEISYSAPVTGRSIGVlfpalglqpaieqAAEDTSHG-DDISVEAIASANPDWIIVLDR 269
Cdd:cd01147 155 ekpTVYFGRIGTKGAagLESGLAGSIEVFELAGGINV-------------ADGLGGGGlKEVSPEQILLWNPDVIFLDTG 221
|
250 260 270
....*....|....*....|....*....|....*....
gi 502628837 270 DGagvgegeYRPAKELIEGSEALASVTAVAEQQvVYLDP 308
Cdd:cd01147 222 SF-------YLSLEGYAKNRPFWQSLKAVKNGR-VYLLP 252
|
|
| ChuT |
COG4558 |
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ... |
60-312 |
1.70e-06 |
|
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443619 [Multi-domain] Cd Length: 285 Bit Score: 48.65 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 60 DPARVVALDNHVFETLSAwdvpLAAAPKGIMGD--GLWPEytDDDAVLDVGMHREPNLESIVAAEPDLIIGgyrfsdsyd 137
Cdd:COG4558 26 AAERIVSLGGSVTEIVYA----LGAGDRLVGVDttSTYPA--AAKALPDVGYMRQLSAEGILSLKPTLVLA--------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 138 DIKAQNPDAV---------VIEIAPREGEDQAAELARQteiLGEIFDRQDEAAAIVADYDAAVDAARTAYDGQST---VV 205
Cdd:COG4558 91 SEGAGPPEVLdqlraagvpVVVVPAAPSLEGVLAKIRA---VAAALGVPEAGEALAARLEADLAALAARVAAIGKpprVL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 206 GLITSGGEISYSApvtGR--SIGVLFPALGLQPAieqaAEDTSHGDDISVEAIASANPDWIIVLDRDGAGVGegeyrpAK 283
Cdd:COG4558 168 FLLSRGGGRPMVA---GRgtAADALIRLAGGVNA----AAGFEGYKPLSAEALIAAAPDVILVMTRGLESLG------GV 234
|
250 260
....*....|....*....|....*....
gi 502628837 284 ELIEGSEALASVTAVAEQQVVYLDPDFYL 312
Cdd:COG4558 235 DGLLALPGLAQTPAGKNKRIVAMDDLLLL 263
|
|
| YvrC |
cd01143 |
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ... |
61-266 |
2.98e-06 |
|
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: 47.27 E-value: 2.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 61 PARVVALDNHVFETLSAwdvpLAAAPKgIMGDGlwpEYTDD--DAV--LDVGMHREPNLESIVAAEPDLIIG-GYRFSDS 135
Cdd:cd01143 3 PERIVSLSPSITEILFA----LGAGDK-IVGVD---TYSNYpkEVRkkPKVGSYSNPNVEKIVALKPDLVIVsSSSLAEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 136 YDDIKAQNPDAVVIeiaprEGEDQAAELARQTEILGEIFDRQDEAAAIVADYDAAVDAARTAYDGQSTVVGLItsggEIS 215
Cdd:cd01143 75 LEKLKDAGIPVVVL-----PAASSLDEIYDQIELIGKITGAEEEAEKLVKEMKQKIDKVKDKGKTIKKSKVYI----EVS 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502628837 216 YSAPVT---GRSIGVLFPALGlqpaIEQAAEDTSHGDDISVEAIASANPDWIIV 266
Cdd:cd01143 146 LGGPYTagkNTFINELIRLAG----AKNIAADSGGWPQVSPEEILKANPDVIIL 195
|
|
| PRK10576 |
PRK10576 |
Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD; |
58-182 |
6.05e-06 |
|
Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD;
Pssm-ID: 236719 Cd Length: 292 Bit Score: 47.31 E-value: 6.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 58 PVDPARVVALDNHVFETLSAWDV-PLAAAPkgIMGDGLWPEYTD-DDAVLDVGMHREPNLESIVAAEPDLIIggyrFSDS 135
Cdd:PRK10576 29 AIDPNRIVALEWLPVELLLALGVtPYGVAD--THNYRLWVSEPAlPDSVIDVGLRTEPNLELLTQMKPSLIL----WSAG 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 502628837 136 YDDIKAQnpdavVIEIAPREG---EDQAAELARQTEILGEIFDRQD-EAAA 182
Cdd:PRK10576 103 YGPSPEK-----LARIAPGRGfafSDGKKPLAVARKSLVELAQRLNlEAAA 148
|
|
| TroA_f |
cd01139 |
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ... |
46-330 |
1.59e-03 |
|
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: 39.98 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 46 VTIEDNHG-SVEVPVDPARVV-----------ALD-NHVFETLSAWDVPL-AAAPKGimgdglWPEYTDD----DAVLDV 107
Cdd:cd01139 1 ITVTDVAGrKVTLDAPVERVLlgegrqlyalaLLEgENPFARIVGWGGDLkKGDPDT------YAKYKEKfpeiADIPLI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 108 GM--HREPNLESIVAAEPDLIIggyrFSDSYDDIKAQNPDAVVIEIA---------PREGEDQAAELARqteILGEIFDR 176
Cdd:cd01139 75 GStyNGDFSVEKVLTLKPDLVI----LNIWAKTTAEESGILEKLEQAgipvvfvdfRQKPLKNTTPSMR---LLGKALGR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 177 QDEAAAIVADYDAAVDAAR---TAYDGQSTVVGLitsggEISYSAP-VTGRSIGVLfpalGLQPAIEQAAED-------T 245
Cdd:cd01139 148 EERAEEFIEFYQERIDRIRdrlAKINEPKPKVFI-----ELGAGGPeECCSTYGNG----NWGELVDAAGGDniadgliP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 246 SHGDDISVEAIASANPDWIIVLDRDGA----GVGEG-EYRPAKEL------IEGSEALASVTAVAEQQVVYLDPDFYLTe 314
Cdd:cd01139 219 GTSGELNAEYVIAANPEIIIATGGNWAkdpsGVSLGpDGTTADAKesllraLLKRPGWSSLQAVKNGRVYALWHQFYRS- 297
|
330
....*....|....*.
gi 502628837 315 dIQAYTALyEQIAQAF 330
Cdd:cd01139 298 -PYNFVAL-EAFAKWL 311
|
|
| TroA_d |
cd01141 |
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ... |
106-133 |
3.26e-03 |
|
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: 38.17 E-value: 3.26e-03
10 20
....*....|....*....|....*...
gi 502628837 106 DVGMHREPNLESIVAAEPDLIIGGYRFS 133
Cdd:cd01141 53 QVGPTGSLNVELIVALKPDLVILYGGFQ 80
|
|
| BtuF |
cd01144 |
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ... |
107-311 |
4.87e-03 |
|
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: 38.05 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 107 VGMHREPNLESIVAAEPDLIIgGYRFSDSYDDIKA-QNPDAVVIEIAPREGEDQAAELARqteiLGEIFDRQDEAAAIVA 185
Cdd:cd01144 42 VGGFYQLDLERVLALKPDLVI-AWDDCNVCAVVDQlRAAGIPVLVSEPQTLDDILADIRR----LGTLAGRPARAEELAE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502628837 186 DYDAAVDAARTAYDG--QSTVVG------LITSGGEIsysapvtgrsIGVLFPALGLQPAIEQAAEDTSHgddISVEAIA 257
Cdd:cd01144 117 ALRRRLAALRKQYASkpPPRVFYqewidpLMTAGGDW----------VPELIALAGGVNVFADAGERSPQ---VSWEDVL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502628837 258 SANPDWIIvldrdgagVGEGEYRPAKELIEGSEALASVTAVAEQQVVYLDPDFY 311
Cdd:cd01144 184 AANPDVIV--------LSPCGFGFTPAILRKEPAWQALPAVRNGRVYAVDGNWY 229
|
|
| |
