|
Name |
Accession |
Description |
Interval |
E-value |
| CeuA |
COG4607 |
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and ... |
36-342 |
6.52e-117 |
|
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443657 [Multi-domain] Cd Length: 310 Bit Score: 340.62 E-value: 6.52e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 36 SKETVTIKNsfeasgkeNNGsdkkkisnTVEVPKNPKNAVVLDYGALDVLKELGVadKVKGLPKcennQSLPKFLDEFKD 115
Cdd:COG4607 32 AAETVTVEH--------ALG--------TVEVPKNPKRVVVFDNGALDTLDALGV--EVAGVPK----GLLPDYLSKYAD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 116 DKYINTGNLKEVNFDKVASAKPDVIFISGRTAnqKNLDEFKKAAPkakVVYVGTSDDNLIKDMKKNTENLGKIYDKEDKA 195
Cdd:COG4607 90 DKYANVGTLFEPDLEAIAALKPDLIIIGGRSA--KKYDELSKIAP---TIDLTVDGEDYLESLKRNTETLGEIFGKEDEA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 196 KKINKDLDRKISDMKDKTKDfNKKVMYLLVNEGELSTFGPGGRFGgLVFDTLGFKPADKKVSKSPHGQNINNEYINKQNP 275
Cdd:COG4607 165 EELVADLDAKIAALKAAAAG-KGTALIVLTNGGKISAYGPGSRFG-PIHDVLGFKPADEDIEASTHGQAISFEFIAEANP 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092757762 276 DVILAMDRGSVVGGKATTN-QVLKNKVIKNVKAVKSNHIYELDPKLWYFSSGSSTTTIKQIDELNEVV 342
Cdd:COG4607 243 DWLFVIDRDAAIGGEGPAAkQVLDNELVKQTTAWKNGQIVYLDPDAWYLAGGGIQSLTEMLDEVADAL 310
|
|
| FatB |
cd01140 |
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ... |
62-338 |
1.61e-92 |
|
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: 277.22 E-value: 1.61e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 62 SNTVEVPKNPKNAVVLDYGALDVLKELGVadKVKGLPKCENnqsLPKFLDEFKDDKYINTGNLKEVNFDKVASAKPDVIF 141
Cdd:cd01140 3 LGETKVPKNPEKVVVFDVGALDTLDALGV--KVVGVPKSST---LPEYLKKYKDDKYANVGTLFEPDLEAIAALKPDLII 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 142 ISGRTanQKNLDEFKKAAPKakvVYVGTSDDNLIKDMKKNTENLGKIYDKEDKAKKINKDLDRKISDMKDKTKdFNKKVM 221
Cdd:cd01140 78 IGGRL--AEKYDELKKIAPT---IDLGADLKNYLESVKQNIETLGKIFGKEEEAKELVAEIDASIAEAKSAAK-GKKKAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 222 YLLVNEGELSTFGPGGRFGgLVFDTLGFKPADKKVSKSPHGQNINNEYINKQNPDVILAMDRGSVVG-GKATTNQVLKNK 300
Cdd:cd01140 152 VVLVNGGKLSAFGPGSRFG-WLHDLLGFEPADENIKASSHGQPVSFEYILEANPDWLFVIDRGAAIGaEGSSAKEVLDND 230
|
250 260 270
....*....|....*....|....*....|....*...
gi 1092757762 301 VIKNVKAVKSNHIYELDPKLWYFSSGSSTTTIKQIDEL 338
Cdd:cd01140 231 LVKNTTAWKNGKVIYLDPDLWYLSGGGLESLKQMIDDL 268
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
75-318 |
1.24e-31 |
|
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: 118.62 E-value: 1.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 75 VVLDYGALDVLKELGVADKVKGlpkCENNQSLPKFLDEFKDDKYINTGNlkEVNFDKVASAKPDVIFISGRTANQKnldE 154
Cdd:pfam01497 1 AALSPAYTEILYALGATDSIVG---VDAYTRDPLKADAVAAIVKVGAYG--EINVERLAALKPDLVILSTGYLTDE---A 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 155 FKKAAPKAKVVYVGTSDDNL-IKDMkknTENLGKIYDKEDKAKKINKDLDRKISDMKDK--TKDFNKKVMYLLVNEGELS 231
Cdd:pfam01497 73 EELLSLIIPTVIFESSSTGEsLKEQ---IKQLGELLGLEDEAEELVAEIDSALAAAKKAvpSLTRKPVLVFGGADGGGYV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 232 TFGPGGRFGGLvFDTLGFKPADKKVSKSpHGQNINNEYINKQNPDVILAMDRGSVVggKATTNQVLKNKVIKNVKAVKSN 311
Cdd:pfam01497 150 VAGSNTYIGDL-LRILGIENIAAELSGS-EYAPISFEAILSSNPDVIIVSGRDSFT--KTGPEFVAANPLWAGLPAVKNG 225
|
....*..
gi 1092757762 312 HIYELDP 318
Cdd:pfam01497 226 RVYTLPS 232
|
|
| btuF |
PRK09534 |
corrinoid ABC transporter substrate-binding protein; Reviewed |
64-322 |
1.06e-08 |
|
corrinoid ABC transporter substrate-binding protein; Reviewed
Pssm-ID: 236552 [Multi-domain] Cd Length: 359 Bit Score: 56.07 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 64 TVEVPKNPKNAVVLDYGALDVLKELGVADKVKGLPKcennqsLPKFLDEFKDDKYINTGNLKEVNFDKVASAKPDVIFIS 143
Cdd:PRK09534 53 EITLDERPERVVTLNPSAAQTMWELGARDRVVGVTQ------YASYLDGAEERTNVSGGQPFGVNVEAVVGLDPDLVLAP 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 144 GRTANQkNLDEFKKAAPKAKVVYVGTSddnlIKDMKKNTENLGKIYDKEDKAKKINKDLDRKISDMKDKTKDFNKK--VM 221
Cdd:PRK09534 127 NAVAGD-TVTRLREAGITVFHFPAATS----IEDVAEKTATIGRLTGNCEAAAETNAEMRDRVDAVEDRTADVDDRprVL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 222 YLLvneGELSTFGpGGRFGGLVFDTLGFK--PADKKVSKSPHgqnINNEYINKQNPDVILAMDRGSVVGGK---ATTNQV 296
Cdd:PRK09534 202 YPL---GDGYTAG-GNTFIGALIEAAGGHnvAADATTDGYPQ---LSEEVIVQQDPDVIVVATASALVAETepyASTTAG 274
|
250 260
....*....|....*....|....*.
gi 1092757762 297 LKNkvikNVKAVKSNHIYELDPKLWY 322
Cdd:PRK09534 275 ETG----NVVTVNVNHINQPAPRIVE 296
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CeuA |
COG4607 |
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and ... |
36-342 |
6.52e-117 |
|
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443657 [Multi-domain] Cd Length: 310 Bit Score: 340.62 E-value: 6.52e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 36 SKETVTIKNsfeasgkeNNGsdkkkisnTVEVPKNPKNAVVLDYGALDVLKELGVadKVKGLPKcennQSLPKFLDEFKD 115
Cdd:COG4607 32 AAETVTVEH--------ALG--------TVEVPKNPKRVVVFDNGALDTLDALGV--EVAGVPK----GLLPDYLSKYAD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 116 DKYINTGNLKEVNFDKVASAKPDVIFISGRTAnqKNLDEFKKAAPkakVVYVGTSDDNLIKDMKKNTENLGKIYDKEDKA 195
Cdd:COG4607 90 DKYANVGTLFEPDLEAIAALKPDLIIIGGRSA--KKYDELSKIAP---TIDLTVDGEDYLESLKRNTETLGEIFGKEDEA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 196 KKINKDLDRKISDMKDKTKDfNKKVMYLLVNEGELSTFGPGGRFGgLVFDTLGFKPADKKVSKSPHGQNINNEYINKQNP 275
Cdd:COG4607 165 EELVADLDAKIAALKAAAAG-KGTALIVLTNGGKISAYGPGSRFG-PIHDVLGFKPADEDIEASTHGQAISFEFIAEANP 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092757762 276 DVILAMDRGSVVGGKATTN-QVLKNKVIKNVKAVKSNHIYELDPKLWYFSSGSSTTTIKQIDELNEVV 342
Cdd:COG4607 243 DWLFVIDRDAAIGGEGPAAkQVLDNELVKQTTAWKNGQIVYLDPDAWYLAGGGIQSLTEMLDEVADAL 310
|
|
| FatB |
cd01140 |
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ... |
62-338 |
1.61e-92 |
|
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: 277.22 E-value: 1.61e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 62 SNTVEVPKNPKNAVVLDYGALDVLKELGVadKVKGLPKCENnqsLPKFLDEFKDDKYINTGNLKEVNFDKVASAKPDVIF 141
Cdd:cd01140 3 LGETKVPKNPEKVVVFDVGALDTLDALGV--KVVGVPKSST---LPEYLKKYKDDKYANVGTLFEPDLEAIAALKPDLII 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 142 ISGRTanQKNLDEFKKAAPKakvVYVGTSDDNLIKDMKKNTENLGKIYDKEDKAKKINKDLDRKISDMKDKTKdFNKKVM 221
Cdd:cd01140 78 IGGRL--AEKYDELKKIAPT---IDLGADLKNYLESVKQNIETLGKIFGKEEEAKELVAEIDASIAEAKSAAK-GKKKAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 222 YLLVNEGELSTFGPGGRFGgLVFDTLGFKPADKKVSKSPHGQNINNEYINKQNPDVILAMDRGSVVG-GKATTNQVLKNK 300
Cdd:cd01140 152 VVLVNGGKLSAFGPGSRFG-WLHDLLGFEPADENIKASSHGQPVSFEYILEANPDWLFVIDRGAAIGaEGSSAKEVLDND 230
|
250 260 270
....*....|....*....|....*....|....*...
gi 1092757762 301 VIKNVKAVKSNHIYELDPKLWYFSSGSSTTTIKQIDEL 338
Cdd:cd01140 231 LVKNTTAWKNGKVIYLDPDLWYLSGGGLESLKQMIDDL 268
|
|
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
75-325 |
4.07e-41 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 144.76 E-value: 4.07e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 75 VVLDYGALDVLKELGVADKVKGLPKcennqslPKFLD--EFKDDKYINTGNLKEVNFDKVASAKPDVIFISGRTANQKNL 152
Cdd:COG0614 4 VSLSPSATELLLALGAGDRLVGVSD-------WGYCDypELELKDLPVVGGTGEPNLEAILALKPDLVLASSSGNDEEDY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 153 DEFKKAapKAKVVYVGTSDdnlIKDMKKNTENLGKIYDKEDKAKKINKDLDRKISDMKDKTKDFNKK--VMYLLVNEGEL 230
Cdd:COG0614 77 EQLEKI--GIPVVVLDPRS---LEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGAEERptVLYEIWSGDPL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 231 STFGPGGrFGGLVFDTLGFKPADKKVSKspHGQNINNEYINKQNPDVILAMDRGSVVGG-KATTNQVLKNKVIKNVKAVK 309
Cdd:COG0614 152 YTAGGGS-FIGELLELAGGRNVAADLGG--GYPEVSLEQVLALDPDVIILSGGGYDAETaEEALEALLADPGWQSLPAVK 228
|
250
....*....|....*.
gi 1092757762 310 SNHIYELDPKLWYFSS 325
Cdd:COG0614 229 NGRVYVVPGDLLSRPG 244
|
|
| FecB |
COG4594 |
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ... |
64-338 |
1.77e-32 |
|
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443650 [Multi-domain] Cd Length: 316 Bit Score: 123.11 E-value: 1.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 64 TVEVPKNPKNAVVLDYGALDVLKELGV-----ADKvkglpkcENNQSLPKFLDEfKDDKYINTGNLKEVNFDKVASAKPD 138
Cdd:COG4594 45 ETTIPGTPKRVVVLEWSFADALLALGVtpvgiADD-------NDYDRWVPYLRD-LIKGVTSVGTRSQPNLEAIAALKPD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 139 VIfISGRTANQKNLDEFKKAAPkakVVYVGTSDDNLiKDMKKNTENLGKIYDKEDKAKKINKDLDRKISDMKDKTKDF-- 216
Cdd:COG4594 117 LI-IADKSRHEAIYDQLSKIAP---TVLFKSRNGDY-QENLESFKTIAKALGKEEEAEAVLADHDQRIAEAKAKLAAAdk 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 217 NKKVMYLLVNEGELSTFGPGGrFGGLVFDTLGFKPADKKVSKSPHGQN-INNEYINKQNPDVILAMdrgsVVGGKATTNQ 295
Cdd:COG4594 192 GKKVAVGQFRADGLRLYTPNS-FAGSVLAALGFENPPKQSKDNGYGYSeVSLEQLPALDPDVLFIA----TYDDPSILKE 266
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1092757762 296 VLKNKVIKNVKAVKSNHIYELDPKLWYFSSG--SSTTTIKQIDEL 338
Cdd:COG4594 267 WKNNPLWKNLKAVKNGRVYEVDGDLWTRGRGplAAELMADDLVEI 311
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
75-318 |
1.24e-31 |
|
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: 118.62 E-value: 1.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 75 VVLDYGALDVLKELGVADKVKGlpkCENNQSLPKFLDEFKDDKYINTGNlkEVNFDKVASAKPDVIFISGRTANQKnldE 154
Cdd:pfam01497 1 AALSPAYTEILYALGATDSIVG---VDAYTRDPLKADAVAAIVKVGAYG--EINVERLAALKPDLVILSTGYLTDE---A 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 155 FKKAAPKAKVVYVGTSDDNL-IKDMkknTENLGKIYDKEDKAKKINKDLDRKISDMKDK--TKDFNKKVMYLLVNEGELS 231
Cdd:pfam01497 73 EELLSLIIPTVIFESSSTGEsLKEQ---IKQLGELLGLEDEAEELVAEIDSALAAAKKAvpSLTRKPVLVFGGADGGGYV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 232 TFGPGGRFGGLvFDTLGFKPADKKVSKSpHGQNINNEYINKQNPDVILAMDRGSVVggKATTNQVLKNKVIKNVKAVKSN 311
Cdd:pfam01497 150 VAGSNTYIGDL-LRILGIENIAAELSGS-EYAPISFEAILSSNPDVIIVSGRDSFT--KTGPEFVAANPLWAGLPAVKNG 225
|
....*..
gi 1092757762 312 HIYELDP 318
Cdd:pfam01497 226 RVYTLPS 232
|
|
| FhuD |
cd01146 |
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ... |
69-328 |
2.34e-31 |
|
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: 118.54 E-value: 2.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 69 KNPKNAVVLDYGALDVLKELGVadKVKGLPKCENNQSLPKFLDEFKDDkYINTGNLKEVNFDKVASAKPDVIFISgRTAN 148
Cdd:cd01146 1 AKPQRIVALDWGALETLLALGV--KPVGVADTAGYKPWIPEPALPLEG-VVDVGTRGQPNLEAIAALKPDLILGS-ASRH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 149 QKNLDEFKKAAPkakVVYVGTSDDnlIKDMKKNTENLGKIYDKEDKAKKINKDLDRKISDMKDKTKDFNKKVMYLLV--N 226
Cdd:cd01146 77 DEIYDQLSQIAP---TVLLDSSPW--LAEWKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKLPDKGPKPVSVVRfsD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 227 EGELSTFGPGGRFGGLVFDtLGFKPAdKKVSKSPHG--QNINNEYINKQNPDVILAMdrgsVVGGKATTNQVLKNKVIKN 304
Cdd:cd01146 152 AGSIRLYGPNSFAGSVLED-LGLQNP-WAQETTNDSgfATISLERLAKADADVLFVF----TYEDEELAQALQANPLWQN 225
|
250 260
....*....|....*....|....
gi 1092757762 305 VKAVKSNHIYELDPKLWYFSSGSS 328
Cdd:cd01146 226 LPAVKNGRVYVVDDVWWFFGGGLS 249
|
|
| FeuA |
cd01138 |
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ... |
63-326 |
2.17e-22 |
|
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: 94.32 E-value: 2.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 63 NTVEVPKNPKNAVVLDYGALDVLKE----LGVADKVKGLPkcennqslpkflDEFKDDKYINTGNLKEVNFDKVASAKPD 138
Cdd:cd01138 1 GEVEIPAKPKRIVALSGETEGLALLgikpVGAASIGGKNP------------YYKKKTLAKVVGIVDEPNLEKVLELKPD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 139 VIFISgrTANQKNLDEFKKAAPkakVVYVgtSDDNliKDMKKNTENLGKIYDKEDKAKKINKDLDRKISDMKDKTKDFNK 218
Cdd:cd01138 69 LIIVS--SKQEENYEKLSKIAP---TVPV--SYNS--SDWEEQLKEIGKLLNKEDEAEKWLADYKQKAKEAKEKIKKKLG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 219 KVMYLLVNE--GELSTFGPGGRFGGLVFD-TLGFKPAD--KKVSKSPHGQNINNEYINKQNPD-VILAMDRGSvvggkAT 292
Cdd:cd01138 140 NDKSVAVLRgrKQIYVFGEDGRGGGPILYaDLGLKAPEkvKEIEDKPGYAAISLEVLPEFDADyIFLLFFTGP-----EA 214
|
250 260 270
....*....|....*....|....*....|....
gi 1092757762 293 TNQVLKNKVIKNVKAVKSNHIYELDPKLWYFSSG 326
Cdd:cd01138 215 KADFESLPIWKNLPAVKNNHVYIVDAWVFYFADG 248
|
|
| TroA-like |
cd00636 |
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ... |
72-225 |
7.97e-22 |
|
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: 89.93 E-value: 7.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 72 KNAVVLDYGALDVLKELGVADKVKGLPKCENnqslPKFLDEFKDDKYINTGNLKEVNFDKVASAKPDVIFISGRTANQkN 151
Cdd:cd00636 1 KRVVALDPGATELLLALGGDDKPVGVADPSG----YPPEAKALLEKVPDVGHGYEPNLEKIAALKPDLIIANGSGLEA-W 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1092757762 152 LDEFKKAApkAKVVYVGTSDDNLIKDMKKNTENLGKIYDKEDKAKKINKDLDRKISDMKDKTKDFNKKVMYLLV 225
Cdd:cd00636 76 LDKLSKIA--IPVVVVDEASELSLENIKESIRLIGKALGKEENAEELIAELDARLAELRAKLAKIPKKKVSLVV 147
|
|
| TroA_a |
cd01148 |
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ... |
69-335 |
1.34e-20 |
|
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: 90.09 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 69 KNPKNAVVLDYGALDVLKELGVADKVKGLPKCENNQsLPKFldefkDDKYINTGNL--KEVNFDKVASAKPDVIFISGRT 146
Cdd:cd01148 16 KAPQRVVSNDQNTTEMMLALGLQDRMVGTAGIDNKD-LPEL-----KAKYDKVPELakKYPSKETVLAARPDLVFGGWSY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 147 ANQKNLDEFKKAAPKAKV-VYVGTSD------DNLIKDMKKNTENLGKIYDKEDKAKKINKDLDRKISDMKDKTKDFNKK 219
Cdd:cd01148 90 GFDKGGLGTPDSLAELGIkTYILPEScgqrrgEATLDDVYNDIRNLGKIFDVEDRADKLVADLKARLAEISAKVKGDGKK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 220 VMYLLVNEGELSTFgPGGRFG--GLVFDTLGFKPADKKVSKSphGQNINNEYINKQNPDVILAMDRGSVVGGKATTNQVL 297
Cdd:cd01148 170 VAVFVYDSGEDKPF-TSGRGGipNAIITAAGGRNVFADVDES--WTTVSWETVIARNPDVIVIIDYGDQNAAEQKIKFLK 246
|
250 260 270
....*....|....*....|....*....|....*...
gi 1092757762 298 KNKVIKNVKAVKSNHIYELDPKLWYfSSGSSTTTIKQI 335
Cdd:cd01148 247 ENPALKNVPAVKNNRFIVLPLAEAT-PGIRNVDAIEKL 283
|
|
| YvrC |
cd01143 |
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ... |
69-279 |
2.62e-20 |
|
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: 87.33 E-value: 2.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 69 KNPKNAVVLDYGALDVLKELGVADKVKGLPKCENnqsLPKfldEFKDDKYIntGNLKEVNFDKVASAKPDVIFISGRTAN 148
Cdd:cd01143 1 KEPERIVSLSPSITEILFALGAGDKIVGVDTYSN---YPK---EVRKKPKV--GSYSNPNVEKIVALKPDLVIVSSSSLA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 149 QkNLDEFKKAAPKakVVYVGtsDDNLIKDMKKNTENLGKIYDKEDKAKKINKDLDRKISDMKDKTKDFNKKVMYLLVNEG 228
Cdd:cd01143 73 E-LLEKLKDAGIP--VVVLP--AASSLDEIYDQIELIGKITGAEEEAEKLVKEMKQKIDKVKDKGKTIKKSKVYIEVSLG 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1092757762 229 ELSTFGPGgRFGGLVFDTLGFK-PADKKVSKSPhgqnINNEYINKQNPDVIL 279
Cdd:cd01143 148 GPYTAGKN-TFINELIRLAGAKnIAADSGGWPQ----VSPEEILKANPDVII 194
|
|
| TroA_e |
cd01142 |
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ... |
64-322 |
8.94e-20 |
|
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: 87.80 E-value: 8.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 64 TVEVPKNPKNAVVLDYGALDVLKELGVADK-VKGLPKCENNQSLPKFLDEFKDDKYINTGNlkEVNFDKVASAKPDVIFI 142
Cdd:cd01142 17 KVTIPDEVKRIAALWGAGNAVVAALGGGKLiVATTSTVQQEPWLYRLAPSLENVATGGTGN--DVNIEELLALKPDVVIV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 143 SGRTANQKNLDefkkaapKAKVVYVGTSDDNLIKDMKKNTENLGKIYDKEDKAKKINKDLDRKISDMKDKTKD----FNK 218
Cdd:cd01142 95 WSTDGKEAGKA-------VLRLLNALSLRDAELEEVKLTIALLGELLGRQEKAEALVAYFDDNLAYVAARTKKlpdsERP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 219 KVMYllVNEGELSTFGPgGRFGGLVFDTLGFKPADKKVSKSPHGQnINNEYINKQNPDVILAMDRGSVVGgkattnqVLK 298
Cdd:cd01142 168 RVYY--AGPDPLTTDGT-GSITNSWIDLAGGINVASEATKKGSGE-VSLEQLLKWNPDVIIVGNADTKAA-------ILA 236
|
250 260
....*....|....*....|....
gi 1092757762 299 NKVIKNVKAVKSNHIYeLDPKLWY 322
Cdd:cd01142 237 DPRWQNLRAVKNGRVY-VNPEGAF 259
|
|
| HemV-2 |
cd01147 |
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ... |
67-323 |
4.32e-18 |
|
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: 82.77 E-value: 4.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 67 VPKNPKNAVVLDYGALDVLKELGVADKVKGLP---KCENNQSLPKFLDEFKDDKYINTGNL-KEVNFDKVASAKPDVIFI 142
Cdd:cd01147 1 VPKPVERVVAAGPGALRLLYALAAPDKIVGVDdaeKSDEGRPYFLASPELKDLPVIGRGGRgNTPNYEKIAALKPDVVID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 143 SGRTANQKNLDEFKKAA--PKAkVVYVGTSDDNLIKDMKKntenLGKIYDKEDKAKKINKDLDRKISDMKDKTKDF---N 217
Cdd:cd01147 81 VGSDDPTSIADDLQKKTgiPVV-VLDGGDSLEDTPEQIRL----LGKVLGKEERAEELISFIESILADVEERTKDIpdeE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 218 KKVMYLlvneGELSTFGPGGRFGGL-----VFDTLGFKP-ADKKVSKSphGQNINNEYINKQNPDVILAMDRGS--VVGG 289
Cdd:cd01147 156 KPTVYF----GRIGTKGAAGLESGLagsieVFELAGGINvADGLGGGG--LKEVSPEQILLWNPDVIFLDTGSFylSLEG 229
|
250 260 270
....*....|....*....|....*....|....*.
gi 1092757762 290 KATTNQVLknkviKNVKAVKSNHIYEL--DPKLWYF 323
Cdd:cd01147 230 YAKNRPFW-----QSLKAVKNGRVYLLpaLPFNWYD 260
|
|
| ChuT |
COG4558 |
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ... |
122-347 |
2.22e-12 |
|
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443619 [Multi-domain] Cd Length: 285 Bit Score: 66.37 E-value: 2.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 122 GNLKEVNFDKVASAKPDVIFISGRTANQKNLDEFKKAapKAKVVYVGTSDDnlIKDMKKNTENLGKIYDKEDKAKKINKD 201
Cdd:COG4558 70 GYMRQLSAEGILSLKPTLVLASEGAGPPEVLDQLRAA--GVPVVVVPAAPS--LEGVLAKIRAVAAALGVPEAGEALAAR 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 202 LDRKISDMKDKTKDF--NKKVMYLLVNE-GELSTFGPGGRFGGL--------VFDTL-GFKPadkkvsksphgqnINNEY 269
Cdd:COG4558 146 LEADLAALAARVAAIgkPPRVLFLLSRGgGRPMVAGRGTAADALirlaggvnAAAGFeGYKP-------------LSAEA 212
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1092757762 270 INKQNPDVILAMDRG-SVVGGKAttnQVLKNKVIKNVKAVKSNHIYELDPKLwyfSSGSSTTTIKQIDELNEVVEKVEK 347
Cdd:COG4558 213 LIAAAPDVILVMTRGlESLGGVD---GLLALPGLAQTPAGKNKRIVAMDDLL---LLGFGPRTPQAALALAQALYPAAA 285
|
|
| BtuF |
cd01144 |
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ... |
122-326 |
4.09e-11 |
|
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: 62.32 E-value: 4.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 122 GNLKEVNFDKVASAKPDVIfISGRTAN-QKNLDEFKKAAPKakvVYVgtSDDNLIKDMKKNTENLGKIYDKEDKAKKINK 200
Cdd:cd01144 43 GGFYQLDLERVLALKPDLV-IAWDDCNvCAVVDQLRAAGIP---VLV--SEPQTLDDILADIRRLGTLAGRPARAEELAE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 201 DLDRKISDMKDKTKD-FNKKVMYLlvnEGELSTFGPGGRF--------GGL-VFDTLGfkpadkkvSKSPHgqnINNEYI 270
Cdd:cd01144 117 ALRRRLAALRKQYASkPPPRVFYQ---EWIDPLMTAGGDWvpelialaGGVnVFADAG--------ERSPQ---VSWEDV 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1092757762 271 NKQNPDVILAMDrgsvVGGKATTNQVLKNKVIKNVKAVKSNHIYELDPKlWYFSSG 326
Cdd:cd01144 183 LAANPDVIVLSP----CGFGFTPAILRKEPAWQALPAVRNGRVYAVDGN-WYFRPS 233
|
|
| TroA_f |
cd01139 |
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ... |
64-316 |
8.34e-11 |
|
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial receptors in the ABC metal ion uptake in eubacteria and archaea. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.
Pssm-ID: 238559 [Multi-domain] Cd Length: 342 Bit Score: 62.32 E-value: 8.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 64 TVEVPKNPKNAVVLDYGALDVLKEL---GVADKVKGLP---KCENNQSLPKFLDEFKD-DKYINTGNLKE--VNFDKVAS 134
Cdd:cd01139 10 KVTLDAPVERVLLGEGRQLYALALLegeNPFARIVGWGgdlKKGDPDTYAKYKEKFPEiADIPLIGSTYNgdFSVEKVLT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 135 AKPDVIF--ISGRTANQKNLDEFKKAAPKAKVVYV---GTSDDNLIKDMKKntenLGKIYDKEDKAKKINKDLDRKISDM 209
Cdd:cd01139 90 LKPDLVIlnIWAKTTAEESGILEKLEQAGIPVVFVdfrQKPLKNTTPSMRL----LGKALGREERAEEFIEFYQERIDRI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 210 KDKTKDFNK---KVMYLLVNEGE---LSTFGPGGrFGGLVFDTLGFKPADKKVSKSPhgQNINNEYINKQNPDVILA--- 280
Cdd:cd01139 166 RDRLAKINEpkpKVFIELGAGGPeecCSTYGNGN-WGELVDAAGGDNIADGLIPGTS--GELNAEYVIAANPEIIIAtgg 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1092757762 281 ----MDRGSVVGGKATTNQ--------VLKNKVIKNVKAVKSNHIYEL 316
Cdd:cd01139 243 nwakDPSGVSLGPDGTTADakesllraLLKRPGWSSLQAVKNGRVYAL 290
|
|
| TroA_d |
cd01141 |
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ... |
64-218 |
2.29e-10 |
|
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: 58.97 E-value: 2.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 64 TVEVPknPKNAVVLDYGALDVLKELGVADKVKGLPKCENNQSLPKFLDEFKddkyINTGNLKEVNFDKVASAKPDVIFIS 143
Cdd:cd01141 3 TIKVP--PKRIVVLSPTHVDLLLALDKADKIVGVSASAYDLNTPAVKERID----IQVGPTGSLNVELIVALKPDLVILY 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1092757762 144 GRTANQKNLDEFKKAAPKAKVVYVGTSDDNLIKDMKKNTENLGKiyDKEDKAKKINKDLDRKISDMKDKTKDFNK 218
Cdd:cd01141 77 GGFQAQTILDKLEQLGIPVLYVNEYPSPLGRAEWIKFAAAFYGV--GKEDKADEAFAQIAGRYRDLAKKVSNLNK 149
|
|
| btuF |
PRK09534 |
corrinoid ABC transporter substrate-binding protein; Reviewed |
64-322 |
1.06e-08 |
|
corrinoid ABC transporter substrate-binding protein; Reviewed
Pssm-ID: 236552 [Multi-domain] Cd Length: 359 Bit Score: 56.07 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 64 TVEVPKNPKNAVVLDYGALDVLKELGVADKVKGLPKcennqsLPKFLDEFKDDKYINTGNLKEVNFDKVASAKPDVIFIS 143
Cdd:PRK09534 53 EITLDERPERVVTLNPSAAQTMWELGARDRVVGVTQ------YASYLDGAEERTNVSGGQPFGVNVEAVVGLDPDLVLAP 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 144 GRTANQkNLDEFKKAAPKAKVVYVGTSddnlIKDMKKNTENLGKIYDKEDKAKKINKDLDRKISDMKDKTKDFNKK--VM 221
Cdd:PRK09534 127 NAVAGD-TVTRLREAGITVFHFPAATS----IEDVAEKTATIGRLTGNCEAAAETNAEMRDRVDAVEDRTADVDDRprVL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 222 YLLvneGELSTFGpGGRFGGLVFDTLGFK--PADKKVSKSPHgqnINNEYINKQNPDVILAMDRGSVVGGK---ATTNQV 296
Cdd:PRK09534 202 YPL---GDGYTAG-GNTFIGALIEAAGGHnvAADATTDGYPQ---LSEEVIVQQDPDVIVVATASALVAETepyASTTAG 274
|
250 260
....*....|....*....|....*.
gi 1092757762 297 LKNkvikNVKAVKSNHIYELDPKLWY 322
Cdd:PRK09534 275 ETG----NVVTVNVNHINQPAPRIVE 296
|
|
| HutB |
cd01149 |
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ... |
122-320 |
3.20e-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: 41.48 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 122 GNLKEVNFDKVASAKPDVIFISGRTANQKNLDEFKKAapKAKVVYVGTSDDnlIKDMKKNTENLGKIYDKEDKAKKINKD 201
Cdd:cd01149 44 GYMRQLSAEGVLSLKPTLVIASDEAGPPEALDQLRAA--GVPVVTVPSTPT--LDGLLTKIRQVAQALGVPEKGEALAQE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 202 LDRKISDMKDK--TKDFNKKVMYLLVNEG-ELSTFGPGGRFGGLVfdTL-----------GFKPadkkvsksphgqnINN 267
Cdd:cd01149 120 VRQRLAALRKTvaAHKKPPRVLFLLSHGGgAAMAAGRNTAADAII--ALagavnaaagfrGYKP-------------LSA 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1092757762 268 EYINKQNPDVILAMDRG-SVVGGkatTNQVLKNKVIKNVKAVKSNHIYELDPKL 320
Cdd:cd01149 185 EALIAAQPDVILVMSRGlDAVGG---VDGLLKLPGLAQTPAGRNKRILAMDDLL 235
|
|
| fecB |
PRK11411 |
iron-dicitrate transporter substrate-binding subunit; Provisional |
64-321 |
3.84e-04 |
|
iron-dicitrate transporter substrate-binding subunit; Provisional
Pssm-ID: 183123 [Multi-domain] Cd Length: 303 Bit Score: 41.58 E-value: 3.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 64 TVEVPKNPKNAVVLDYGALDVLKEL-----GVADkvkglpkcENNQS--LPKFLDEFKddKYINTGNLKEVNFDKVASAK 136
Cdd:PRK11411 32 TFTLEKTPQRIVVLELSFVDALAAVgvspvGVAD--------DNDAKriLPEVRAHLK--PWQSVGTRSQPSLEAIAALK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 137 PDVIfISGRTANQKNLDEFKKAAPKAkvvyvgtsddnLIK----DMKKNTENLGKIYDKEDKAKKINKDLDRKISDMKDK 212
Cdd:PRK11411 102 PDLI-IADSSRHAGVYIALQKIAPTL-----------LLKsrneTYQENLQSAAIIGEVLGKKREMQARIEQHKERMAQF 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092757762 213 TKDFNK--KVMYLLVNEGELSTFGPGGRFGGlVFDTLGFKpadkkVSKSPHGQ----NINNEYINKQNPD-VILAMDRG- 284
Cdd:PRK11411 170 ASQLPKgtRVAFGTSREQQFNLHSPESYTGS-VLAALGLN-----VPKAPMNGaampSISLEQLLALNPDwLLVAHYRQe 243
|
250 260 270
....*....|....*....|....*....|....*....
gi 1092757762 285 SVVGG--KATTNQVLKnkviknvkAVKSNHIYELDPKLW 321
Cdd:PRK11411 244 SIVKRwqQDPLWQMLT--------AAKKQQVASVDSNTW 274
|
|
| |
