|
Name |
Accession |
Description |
Interval |
E-value |
| ChuT |
COG4558 |
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ... |
34-304 |
1.84e-113 |
|
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443619 [Multi-domain] Cd Length: 285 Bit Score: 329.07 E-value: 1.84e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699779 34 LFTAVLALSWAFSVTAAERIVVAGGSLTELIYAMGAGERVVGVDETTSYPPETAKLPHIGYWKQLSSEGILSLRPDSVIT 113
Cdd:COG4558 11 LALAALAAGASVAAAAAERIVSLGGSVTEIVYALGAGDRLVGVDTTSTYPAAAKALPDVGYMRQLSAEGILSLKPTLVLA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699779 114 WQDAGPQIVLDQLRAQKVNVVTLPRvPATLQQMYANIRQLAKTLQVPEQGEALVTQISQRLERVQQNVATKKAPVKAMFI 193
Cdd:COG4558 91 SEGAGPPEVLDQLRAAGVPVVVVPA-APSLEGVLAKIRAVAAALGVPEAGEALAARLEADLAALAARVAAIGKPPRVLFL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699779 194 LSAGGSAPQVAGKGSVADAILSLAGAENVAT-HQQYKSYSAESLIAANPEVIVVTSQMVD--GDINRLRSIAGITHTAAW 270
Cdd:COG4558 170 LSRGGGRPMVAGRGTAADALIRLAGGVNAAAgFEGYKPLSAEALIAAAPDVILVMTRGLEslGGVDGLLALPGLAQTPAG 249
|
250 260 270
....*....|....*....|....*....|....
gi 1447699779 271 KNQRIITVDQNLILGMGPRIADVVESLHQQLWPQ 304
Cdd:COG4558 250 KNKRIVAMDDLLLLGFGPRTPQAALALAQALYPA 283
|
|
| HutB |
cd01149 |
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ... |
50-282 |
1.69e-105 |
|
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: 307.27 E-value: 1.69e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699779 50 AERIVVAGGSLTELIYAMGAGERVVGVDETTSYPPETAKLPHIGYWKQLSSEGILSLRPDSVITWQDAGPQIVLDQLRAQ 129
Cdd:cd01149 1 PERIVSLGGSVTEIVYALGAGDRLVGVDSTSTYPEAAAKLPDVGYMRQLSAEGVLSLKPTLVIASDEAGPPEALDQLRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699779 130 KVNVVTLPRVPaTLQQMYANIRQLAKTLQVPEQGEALVTQISQRLERVQQNVATKKAPVKAMFILSAGGSAPQVAGKGSV 209
Cdd:cd01149 81 GVPVVTVPSTP-TLDGLLTKIRQVAQALGVPEKGEALAQEVRQRLAALRKTVAAHKKPPRVLFLLSHGGGAAMAAGRNTA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1447699779 210 ADAILSLAGAENVA-THQQYKSYSAESLIAANPEVIVVTSQMVD--GDINRLRSIAGITHTAAWKNQRIITVDQNL 282
Cdd:cd01149 160 ADAIIALAGAVNAAaGFRGYKPLSAEALIAAQPDVILVMSRGLDavGGVDGLLKLPGLAQTPAGRNKRILAMDDLL 235
|
|
| PRK03379 |
PRK03379 |
vitamin B12-transporter protein BtuF; Provisional |
37-301 |
3.70e-29 |
|
vitamin B12-transporter protein BtuF; Provisional
Pssm-ID: 179575 [Multi-domain] Cd Length: 260 Bit Score: 112.09 E-value: 3.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699779 37 AVLALSWAF--SVTAAERIVVAGGSLTELIYAMGAGErvVGVDETTSYPPETAKLPHIGYWKQLSSEGILSLRPDSVITW 114
Cdd:PRK03379 2 ALVALLFLAplWLNAAPRVITLSPANTELAFAAGITP--VGVSSYSDYPPQAKKIEQVATWQGMNLERIVALKPDLVLAW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699779 115 QDAGPQIVLDQLRAQKVNVVTLPrvPATLQQMYANIRQLAKTLQVPEQGEALVTQISQRLERVQQNVATKkaPVKAMFiL 194
Cdd:PRK03379 80 RGGNAERQVDQLASLGIKVMWVD--ATSIEQIANALRQLAPWSPQPEKAEQAAQSLLQQYAALKAQYADK--PKKRVF-L 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699779 195 SAGGSAPQVAGKGSVADAILSLAGAENV--ATHQQYKSYSAESLIAANPEVIVVTsqmvdGDINRLRSIAgithtAAWKN 272
Cdd:PRK03379 155 QFGTNPLFTSGKHSIQSQVLSLCGGENIfaDSRVPWPQVSREQVLARKPQAIVIT-----GGPDQIPKIK-----QFWGP 224
|
250 260 270
....*....|....*....|....*....|..
gi 1447699779 273 Q---RIITVDQNLILGMGPRIADVVESLHQQL 301
Cdd:PRK03379 225 QlkiPVIPLNSDWFERASPRIILAAQQLCNAL 256
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
54-281 |
1.91e-28 |
|
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: 109.38 E-value: 1.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699779 54 VVAGGSLTELIYAMGAGERVVGVDETTSYPPETAKLPHI---GYWKQLSSEGILSLRPDSVITWQDAGPQIvLDQLRAQK 130
Cdd:pfam01497 1 AALSPAYTEILYALGATDSIVGVDAYTRDPLKADAVAAIvkvGAYGEINVERLAALKPDLVILSTGYLTDE-AEELLSLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699779 131 VNVVTLPrVPATLQQMYANIRQLAKTLQVPEQGEALVTQISQRLERVQQNVATKKAPVKAMFILSAGGsAPQVAGKGSVA 210
Cdd:pfam01497 80 IPTVIFE-SSSTGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPVLVFGGADGG-GYVVAGSNTYI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1447699779 211 DAILSLAGAENVAT---HQQYKSYSAESLIAANPEVIVVTSQMVDGD--INRLRSIAGITHTAAWKNQRIITVDQN 281
Cdd:pfam01497 158 GDLLRILGIENIAAelsGSEYAPISFEAILSSNPDVIIVSGRDSFTKtgPEFVAANPLWAGLPAVKNGRVYTLPSD 233
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ChuT |
COG4558 |
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ... |
34-304 |
1.84e-113 |
|
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443619 [Multi-domain] Cd Length: 285 Bit Score: 329.07 E-value: 1.84e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699779 34 LFTAVLALSWAFSVTAAERIVVAGGSLTELIYAMGAGERVVGVDETTSYPPETAKLPHIGYWKQLSSEGILSLRPDSVIT 113
Cdd:COG4558 11 LALAALAAGASVAAAAAERIVSLGGSVTEIVYALGAGDRLVGVDTTSTYPAAAKALPDVGYMRQLSAEGILSLKPTLVLA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699779 114 WQDAGPQIVLDQLRAQKVNVVTLPRvPATLQQMYANIRQLAKTLQVPEQGEALVTQISQRLERVQQNVATKKAPVKAMFI 193
Cdd:COG4558 91 SEGAGPPEVLDQLRAAGVPVVVVPA-APSLEGVLAKIRAVAAALGVPEAGEALAARLEADLAALAARVAAIGKPPRVLFL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699779 194 LSAGGSAPQVAGKGSVADAILSLAGAENVAT-HQQYKSYSAESLIAANPEVIVVTSQMVD--GDINRLRSIAGITHTAAW 270
Cdd:COG4558 170 LSRGGGRPMVAGRGTAADALIRLAGGVNAAAgFEGYKPLSAEALIAAAPDVILVMTRGLEslGGVDGLLALPGLAQTPAG 249
|
250 260 270
....*....|....*....|....*....|....
gi 1447699779 271 KNQRIITVDQNLILGMGPRIADVVESLHQQLWPQ 304
Cdd:COG4558 250 KNKRIVAMDDLLLLGFGPRTPQAALALAQALYPA 283
|
|
| HutB |
cd01149 |
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ... |
50-282 |
1.69e-105 |
|
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: 307.27 E-value: 1.69e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699779 50 AERIVVAGGSLTELIYAMGAGERVVGVDETTSYPPETAKLPHIGYWKQLSSEGILSLRPDSVITWQDAGPQIVLDQLRAQ 129
Cdd:cd01149 1 PERIVSLGGSVTEIVYALGAGDRLVGVDSTSTYPEAAAKLPDVGYMRQLSAEGVLSLKPTLVIASDEAGPPEALDQLRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699779 130 KVNVVTLPRVPaTLQQMYANIRQLAKTLQVPEQGEALVTQISQRLERVQQNVATKKAPVKAMFILSAGGSAPQVAGKGSV 209
Cdd:cd01149 81 GVPVVTVPSTP-TLDGLLTKIRQVAQALGVPEKGEALAQEVRQRLAALRKTVAAHKKPPRVLFLLSHGGGAAMAAGRNTA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1447699779 210 ADAILSLAGAENVA-THQQYKSYSAESLIAANPEVIVVTSQMVD--GDINRLRSIAGITHTAAWKNQRIITVDQNL 282
Cdd:cd01149 160 ADAIIALAGAVNAAaGFRGYKPLSAEALIAAQPDVILVMSRGLDavGGVDGLLKLPGLAQTPAGRNKRILAMDDLL 235
|
|
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
52-304 |
7.00e-56 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 181.73 E-value: 7.00e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699779 52 RIVVAGGSLTELIYAMGAGERVVGVDETT--SYPPETAK-LPHIGYWKQLSSEGILSLRPDSVITWQDAGPQIVLDQLRA 128
Cdd:COG0614 2 RIVSLSPSATELLLALGAGDRLVGVSDWGycDYPELELKdLPVVGGTGEPNLEAILALKPDLVLASSSGNDEEDYEQLEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699779 129 QKVNVVTLPrvPATLQQMYANIRQLAKTLQVPEQGEALVTQISQRLERVQQNVATKKAPVKAMFILSAGGSaPQVAGKGS 208
Cdd:COG0614 82 IGIPVVVLD--PRSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGAEERPTVLYEIWSGDP-LYTAGGGS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699779 209 VADAILSLAGAENVA--THQQYKSYSAESLIAANPEVIVVTS-----QMVDGDINRLRSIAGITHTAAWKNQRIITVDQN 281
Cdd:COG0614 159 FIGELLELAGGRNVAadLGGGYPEVSLEQVLALDPDVIILSGggydaETAEEALEALLADPGWQSLPAVKNGRVYVVPGD 238
|
250 260
....*....|....*....|...
gi 1447699779 282 LILGMGPRIADVVESLHQQLWPQ 304
Cdd:COG0614 239 LLSRPGPRLLLALEDLAKALHPE 261
|
|
| BtuF |
cd01144 |
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ... |
51-297 |
3.56e-42 |
|
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: 145.52 E-value: 3.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699779 51 ERIVVAGGSLTELIYAMGAGERVVGVDETTSYPPETAKLPHIGYWKQLSSEGILSLRPDSVITWQDAGPQIVLDQLRAQK 130
Cdd:cd01144 1 MRIVSLAPSATELLYALGLGDQLVGVTDYCDYPPEAKKLPRVGGFYQLDLERVLALKPDLVIAWDDCNVCAVVDQLRAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699779 131 VNVVTLPrvPATLQQMYANIRQLAKTLQVPEQGEALVTQISQRLERVQQnVATKKAPVKAMFILSAggSAPQVAGKGSVA 210
Cdd:cd01144 81 IPVLVSE--PQTLDDILADIRRLGTLAGRPARAEELAEALRRRLAALRK-QYASKPPPRVFYQEWI--DPLMTAGGDWVP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699779 211 DAIlSLAGAENVATH--QQYKSYSAESLIAANPEVIVVTSQMVDGDINRLRSIAGITHTAAWKNQRIITVDQNLILGMGP 288
Cdd:cd01144 156 ELI-ALAGGVNVFADagERSPQVSWEDVLAANPDVIVLSPCGFGFTPAILRKEPAWQALPAVRNGRVYAVDGNWYFRPSP 234
|
....*....
gi 1447699779 289 RIADVVESL 297
Cdd:cd01144 235 RLVDGLEQL 243
|
|
| YvrC |
cd01143 |
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ... |
51-246 |
3.44e-39 |
|
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: 136.25 E-value: 3.44e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699779 51 ERIVVAGGSLTELIYAMGAGERVVGVDETTSYPPETAKLPHIGYWKQLSSEGILSLRPDSVITwQDAGPQIVLDQLRAQK 130
Cdd:cd01143 4 ERIVSLSPSITEILFALGAGDKIVGVDTYSNYPKEVRKKPKVGSYSNPNVEKIVALKPDLVIV-SSSSLAELLEKLKDAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699779 131 VNVVTLPrVPATLQQMYANIRQLAKTLQVPEQGEALVTQISQRLERVQQNVATKKaPVKAMFILSAGGsaPQVAGKGSVA 210
Cdd:cd01143 83 IPVVVLP-AASSLDEIYDQIELIGKITGAEEEAEKLVKEMKQKIDKVKDKGKTIK-KSKVYIEVSLGG--PYTAGKNTFI 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 1447699779 211 DAILSLAGAENVATH-QQYKSYSAESLIAANPEVIVV 246
Cdd:cd01143 159 NELIRLAGAKNIAADsGGWPQVSPEEILKANPDVIIL 195
|
|
| TroA_a |
cd01148 |
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ... |
45-297 |
2.48e-32 |
|
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: 120.91 E-value: 2.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699779 45 FSVT---AAERIVVAGGSLTELIYAMGAGERVVGvdetTSYP---------------PETAKlphigywKQLSSEGILSL 106
Cdd:cd01148 10 RSVTfdkAPQRVVSNDQNTTEMMLALGLQDRMVG----TAGIdnkdlpelkakydkvPELAK-------KYPSKETVLAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699779 107 RPDSVITWQDAG--PQIVL--DQLRAQKVNVVTLP------RVPATLQQMYANIRQLAKTLQVPEQGEALVTQISQRLER 176
Cdd:cd01148 79 RPDLVFGGWSYGfdKGGLGtpDSLAELGIKTYILPescgqrRGEATLDDVYNDIRNLGKIFDVEDRADKLVADLKARLAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699779 177 VQQNVAtKKAPVKAMFILSAGGSAPQVAGKGSVADAILSLAGAENVATHQQyKSY---SAESLIAANPEVIVVTSQMVDG 253
Cdd:cd01148 159 ISAKVK-GDGKKVAVFVYDSGEDKPFTSGRGGIPNAIITAAGGRNVFADVD-ESWttvSWETVIARNPDVIVIIDYGDQN 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1447699779 254 DINR----LRSIAGITHTAAWKNQRIITVDQNLILGmGPRIADVVESL 297
Cdd:cd01148 237 AAEQkikfLKENPALKNVPAVKNNRFIVLPLAEATP-GIRNVDAIEKL 283
|
|
| PRK03379 |
PRK03379 |
vitamin B12-transporter protein BtuF; Provisional |
37-301 |
3.70e-29 |
|
vitamin B12-transporter protein BtuF; Provisional
Pssm-ID: 179575 [Multi-domain] Cd Length: 260 Bit Score: 112.09 E-value: 3.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699779 37 AVLALSWAF--SVTAAERIVVAGGSLTELIYAMGAGErvVGVDETTSYPPETAKLPHIGYWKQLSSEGILSLRPDSVITW 114
Cdd:PRK03379 2 ALVALLFLAplWLNAAPRVITLSPANTELAFAAGITP--VGVSSYSDYPPQAKKIEQVATWQGMNLERIVALKPDLVLAW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699779 115 QDAGPQIVLDQLRAQKVNVVTLPrvPATLQQMYANIRQLAKTLQVPEQGEALVTQISQRLERVQQNVATKkaPVKAMFiL 194
Cdd:PRK03379 80 RGGNAERQVDQLASLGIKVMWVD--ATSIEQIANALRQLAPWSPQPEKAEQAAQSLLQQYAALKAQYADK--PKKRVF-L 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699779 195 SAGGSAPQVAGKGSVADAILSLAGAENV--ATHQQYKSYSAESLIAANPEVIVVTsqmvdGDINRLRSIAgithtAAWKN 272
Cdd:PRK03379 155 QFGTNPLFTSGKHSIQSQVLSLCGGENIfaDSRVPWPQVSREQVLARKPQAIVIT-----GGPDQIPKIK-----QFWGP 224
|
250 260 270
....*....|....*....|....*....|..
gi 1447699779 273 Q---RIITVDQNLILGMGPRIADVVESLHQQL 301
Cdd:PRK03379 225 QlkiPVIPLNSDWFERASPRIILAAQQLCNAL 256
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
54-281 |
1.91e-28 |
|
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: 109.38 E-value: 1.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699779 54 VVAGGSLTELIYAMGAGERVVGVDETTSYPPETAKLPHI---GYWKQLSSEGILSLRPDSVITWQDAGPQIvLDQLRAQK 130
Cdd:pfam01497 1 AALSPAYTEILYALGATDSIVGVDAYTRDPLKADAVAAIvkvGAYGEINVERLAALKPDLVILSTGYLTDE-AEELLSLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699779 131 VNVVTLPrVPATLQQMYANIRQLAKTLQVPEQGEALVTQISQRLERVQQNVATKKAPVKAMFILSAGGsAPQVAGKGSVA 210
Cdd:pfam01497 80 IPTVIFE-SSSTGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPVLVFGGADGG-GYVVAGSNTYI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1447699779 211 DAILSLAGAENVAT---HQQYKSYSAESLIAANPEVIVVTSQMVDGD--INRLRSIAGITHTAAWKNQRIITVDQN 281
Cdd:pfam01497 158 GDLLRILGIENIAAelsGSEYAPISFEAILSSNPDVIIVSGRDSFTKtgPEFVAANPLWAGLPAVKNGRVYTLPSD 233
|
|
| HemV-2 |
cd01147 |
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ... |
51-247 |
6.37e-26 |
|
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: 103.18 E-value: 6.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699779 51 ERIVVAGGSLTELIYAMGAGERVVGVDETTS---------YPPETAKLPHIG---YWKQLSSEGILSLRPDSVITWQDAG 118
Cdd:cd01147 6 ERVVAAGPGALRLLYALAAPDKIVGVDDAEKsdegrpyflASPELKDLPVIGrggRGNTPNYEKIAALKPDVVIDVGSDD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699779 119 PQIVLDQLRAQKVNVVTLPRVPATLQQMYANIRQLAKTLQVPEQGEALVTQISQRLERVQQNVAT-KKAPVKAMFILSAG 197
Cdd:cd01147 86 PTSIADDLQKKTGIPVVVLDGGDSLEDTPEQIRLLGKVLGKEERAEELISFIESILADVEERTKDiPDEEKPTVYFGRIG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1447699779 198 GSAPQV-AGKGSVADAILSLAGAENVA---THQQYKSYSAESLIAANPEVIVVT 247
Cdd:cd01147 166 TKGAAGlESGLAGSIEVFELAGGINVAdglGGGGLKEVSPEQILLWNPDVIFLD 219
|
|
| TroA-like |
cd00636 |
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ... |
51-194 |
2.40e-25 |
|
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: 98.78 E-value: 2.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699779 51 ERIVVAGGSLTELIYAMGAGERVVGVDETTSYPPE----TAKLPHIGYWKQLSSEGILSLRPDSVITWQDAGPQIvLDQL 126
Cdd:cd00636 1 KRVVALDPGATELLLALGGDDKPVGVADPSGYPPEakalLEKVPDVGHGYEPNLEKIAALKPDLIIANGSGLEAW-LDKL 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1447699779 127 RAQKVNVVTLP-RVPATLQQMYANIRQLAKTLQVPEQGEALVTQISQRLERVQQNVATKKAPVKAMFIL 194
Cdd:cd00636 80 SKIAIPVVVVDeASELSLENIKESIRLIGKALGKEENAEELIAELDARLAELRAKLAKIPKKKVSLVVG 148
|
|
| TroA_e |
cd01142 |
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ... |
50-276 |
1.44e-21 |
|
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: 92.03 E-value: 1.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699779 50 AERIVVAGGSLTELIYAMGAGERVVGVDETTSYPPETAKL-PHIGYWKQ------LSSEGILSLRPDSVITWQDAGPQIV 122
Cdd:cd01142 24 VKRIAALWGAGNAVVAALGGGKLIVATTSTVQQEPWLYRLaPSLENVATggtgndVNIEELLALKPDVVIVWSTDGKEAG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699779 123 LDQLRAQKVNvvtLPRVpATLQQMYANIRQLAKTLQVPEQGEALVTQISQRLERVQQnvATKKAPV-KAMFILSAGGSAP 201
Cdd:cd01142 104 KAVLRLLNAL---SLRD-AELEEVKLTIALLGELLGRQEKAEALVAYFDDNLAYVAA--RTKKLPDsERPRVYYAGPDPL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699779 202 QVAGKGSVADAILSLAGAENVATHQQYK---SYSAESLIAANPEVIVVTSQMVDGDI---NRLRSIagithtAAWKNQRI 275
Cdd:cd01142 178 TTDGTGSITNSWIDLAGGINVASEATKKgsgEVSLEQLLKWNPDVIIVGNADTKAAIladPRWQNL------RAVKNGRV 251
|
.
gi 1447699779 276 I 276
Cdd:cd01142 252 Y 252
|
|
| FhuD |
cd01146 |
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ... |
49-288 |
1.16e-16 |
|
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: 77.71 E-value: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699779 49 AAERIVVAGGSLTELIYAMGAgeRVVGVDETTSYPP-------ETAKLPHIGYWKQLSSEGILSLRPDsVITWQDAGPQI 121
Cdd:cd01146 2 KPQRIVALDWGALETLLALGV--KPVGVADTAGYKPwipepalPLEGVVDVGTRGQPNLEAIAALKPD-LILGSASRHDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699779 122 VLDQLrAQKVNVVTLPRVPaTLQQMYANIRQLAKTLQVPEQGEALVTQISQRLERVQQNVATKKAPVKAMFILSAGGSAp 201
Cdd:cd01146 79 IYDQL-SQIAPTVLLDSSP-WLAEWKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKLPDKGPKPVSVVRFSDAGSI- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699779 202 QVAGKGSVADAILSLAG-----AENVATHQQYKSYSAESLIAANPEVIVVTSQMVDGDINRLRSIAGITHTAAWKNQRII 276
Cdd:cd01146 156 RLYGPNSFAGSVLEDLGlqnpwAQETTNDSGFATISLERLAKADADVLFVFTYEDEELAQALQANPLWQNLPAVKNGRVY 235
|
250
....*....|..
gi 1447699779 277 TVDQNLILGMGP 288
Cdd:cd01146 236 VVDDVWWFFGGG 247
|
|
| FatB |
cd01140 |
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ... |
51-301 |
2.17e-15 |
|
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: 74.60 E-value: 2.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699779 51 ERIVVAGGSLTELIYAMGAgeRVVGVDETTSYPP-----ETAKLPHIGYWKQLSSEGILSLRPDSVITWQDAGPQIvlDQ 125
Cdd:cd01140 13 EKVVVFDVGALDTLDALGV--KVVGVPKSSTLPEylkkyKDDKYANVGTLFEPDLEAIAALKPDLIIIGGRLAEKY--DE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699779 126 LR--AQKVNVVTLPRvpATLQQMYANIRQLAKTLQVPEQGEALVTQISQRLERVQQNVATKKapvKAMFILSAGGSApQV 203
Cdd:cd01140 89 LKkiAPTIDLGADLK--NYLESVKQNIETLGKIFGKEEEAKELVAEIDASIAEAKSAAKGKK---KALVVLVNGGKL-SA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699779 204 AGKGSVADAILSLAGAENVATHQ----QYKSYSAESLIAANPEVI-VVTSQMVDGDI---------NRLrsiagITHTAA 269
Cdd:cd01140 163 FGPGSRFGWLHDLLGFEPADENIkassHGQPVSFEYILEANPDWLfVIDRGAAIGAEgssakevldNDL-----VKNTTA 237
|
250 260 270
....*....|....*....|....*....|..
gi 1447699779 270 WKNQRIITVDQNLiLGMGpriADVVESLHQQL 301
Cdd:cd01140 238 WKNGKVIYLDPDL-WYLS---GGGLESLKQMI 265
|
|
| btuF |
PRK09534 |
corrinoid ABC transporter substrate-binding protein; Reviewed |
51-297 |
1.72e-12 |
|
corrinoid ABC transporter substrate-binding protein; Reviewed
Pssm-ID: 236552 [Multi-domain] Cd Length: 359 Bit Score: 66.86 E-value: 1.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699779 51 ERIVVAGGSLTELIYAMGAGERVVGVDETTSYPP--ETAKLPHIGYWKQLSSEGILSLRPDSVItwqdaGPQIVLDQ--- 125
Cdd:PRK09534 61 ERVVTLNPSAAQTMWELGARDRVVGVTQYASYLDgaEERTNVSGGQPFGVNVEAVVGLDPDLVL-----APNAVAGDtvt 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699779 126 -LRAQKVNVVTLPrVPATLQQMYANIRQLAKTLQVPEQGEALVTQISQRLERVQQNVATKKAPVKAMFILSAGgsapQVA 204
Cdd:PRK09534 136 rLREAGITVFHFP-AATSIEDVAEKTATIGRLTGNCEAAAETNAEMRDRVDAVEDRTADVDDRPRVLYPLGDG----YTA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699779 205 GKGSVADAILSLAGAENVA---THQQYKSYSAESLIAANPEVIVVTSqmvdgDINRLRSIAGITHTAAWKNQRIITVDQN 281
Cdd:PRK09534 211 GGNTFIGALIEAAGGHNVAadaTTDGYPQLSEEVIVQQDPDVIVVAT-----ASALVAETEPYASTTAGETGNVVTVNVN 285
|
250
....*....|....*.
gi 1447699779 282 LILGMGPRIADVVESL 297
Cdd:PRK09534 286 HINQPAPRIVESMATM 301
|
|
| TroA_f |
cd01139 |
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ... |
50-248 |
2.98e-12 |
|
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial receptors in the ABC metal ion uptake in eubacteria and archaea. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.
Pssm-ID: 238559 [Multi-domain] Cd Length: 342 Bit Score: 66.18 E-value: 2.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699779 50 AERIVVAGGSLTELIYAM---GAGERVVGVDE------TTSYP------PETAKLPHIGYWKQ--LSSEGILSLRPDSVI 112
Cdd:cd01139 17 VERVLLGEGRQLYALALLegeNPFARIVGWGGdlkkgdPDTYAkykekfPEIADIPLIGSTYNgdFSVEKVLTLKPDLVI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699779 113 --TWQ-DAGPQI-VLDQLRAQKVNVVTLPRVPATLQQMYANIRQLAKTLQVPEQGEALVTQISQRLERVQQNVATKKAPV 188
Cdd:cd01139 97 lnIWAkTTAEESgILEKLEQAGIPVVFVDFRQKPLKNTTPSMRLLGKALGREERAEEFIEFYQERIDRIRDRLAKINEPK 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1447699779 189 KAMFI-LSAGGSAPQV--AGKGSVADaILSLAGAENVATHQ---QYKSYSAESLIAANPEVIVVTS 248
Cdd:cd01139 177 PKVFIeLGAGGPEECCstYGNGNWGE-LVDAAGGDNIADGLipgTSGELNAEYVIAANPEIIIATG 241
|
|
| TroA_d |
cd01141 |
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ... |
50-219 |
2.11e-09 |
|
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: 55.89 E-value: 2.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699779 50 AERIVVAGGSLTELIYAMGAGERVVGVD--ETTSYPPETAKLPH--IGYWKQLSSEGILSLRPDSVITWQDAGPQIVLDQ 125
Cdd:cd01141 8 PKRIVVLSPTHVDLLLALDKADKIVGVSasAYDLNTPAVKERIDiqVGPTGSLNVELIVALKPDLVILYGGFQAQTILDK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699779 126 LRAQKVNVVTLPRVPATLQQ---MYANIRQLAKTLQvpEQGEALVTQISQRLERVQQNVATKKAPVKAMFILSAGGsaPQ 202
Cdd:cd01141 88 LEQLGIPVLYVNEYPSPLGRaewIKFAAAFYGVGKE--DKADEAFAQIAGRYRDLAKKVSNLNKPTVAIGKPVKGL--WY 163
|
170
....*....|....*..
gi 1447699779 203 VAGKGSVADAILSLAGA 219
Cdd:cd01141 164 MPGGNSYVAKMLRDAGG 180
|
|
| PRK14048 |
PRK14048 |
ferrichrome/ferrioxamine B periplasmic transporter; Provisional |
84-248 |
3.46e-09 |
|
ferrichrome/ferrioxamine B periplasmic transporter; Provisional
Pssm-ID: 172540 [Multi-domain] Cd Length: 374 Bit Score: 57.22 E-value: 3.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699779 84 PETAKLPHI--GYWKQLSSEGILSLRPDSVI--TWQ---DAGPQiVLDQLRAQKVNVVTLPRVPATLQQMYANIRQLAKT 156
Cdd:PRK14048 96 PELADVPLIddGSGPGLSFETILTLKADLAIlaNWQadtEAGQR-AIEYLESIGVPVIVVDFNNEALKNTPDNMRLLGKV 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699779 157 LQVPEQGEALVTQISQRLERVQQNVA--TKKAPVKAMFILSAGGSAPQVAGKGSVADAIlSLAGAENVATH---QQYKSY 231
Cdd:PRK14048 175 FEREEQAEDFARFYEERLARIRDRVAkhSEPGPTVLMEAFPAADRCCWAYGRGGLGEFI-ALTGSRNIAEGalpRPGGMM 253
|
170
....*....|....*..
gi 1447699779 232 SAESLIAANPEVIVVTS 248
Cdd:PRK14048 254 NAEAIMAENPDVYIATS 270
|
|
| |
