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Conserved domains on  [gi|1816544345|ref|WP_163536509|]
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ABC transporter substrate-binding protein [Gracilibacillus sp. YIM 98692]

Protein Classification

FecB family protein( domain architecture ID 11468466)

FecB family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FecB COG4594
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ...
 52-342 6.86e-109

ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and metabolism];


:

Pssm-ID: 443650 [Multi-domain]  Cd Length: 316  Bit Score: 320.33  E-value: 6.86e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345  52 SITVSDVYGEQTFDEVPEKIVVLEWVYAENLLALGVQPVGMADIEGYHSWVNIEPELDESVEDVGTRQEPSLEAIHALDP 131
Cdd:COG4594    36 ARTVKHAMGETTIPGTPKRVVVLEWSFADALLALGVTPVGIADDNDYDRWVPYLRDLIKGVTSVGTRSQPNLEAIAALKP 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345 132 DLIITAQSRHEDILDSLKDIAPTLVYNAYPEegegtQYEEMVSTFNEMAKLVQKQDEAEQVLSDIEETYETAKTEIEEAG 211
Cdd:COG4594   116 DLIIADKSRHEAIYDQLSKIAPTVLFKSRNG-----DYQENLESFKTIAKALGKEEEAEAVLADHDQRIAEAKAKLAAAD 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345 212 iENKLFALSQAYSSDnspvIRLFKDNAMATEIMTKMGLENAYESEGFQLYGFDQTNVEALQtAQEAHFFYIVQEDDNIFT 291
Cdd:COG4594   191 -KGKKVAVGQFRADG----LRLYTPNSFAGSVLAALGFENPPKQSKDNGYGYSEVSLEQLP-ALDPDVLFIATYDDPSIL 264

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1816544345 292 EQLAGNPAWEELEFVKEDRTYQLPGDTWTFG-GPLSAEVFANQIKEALVQEK 342
Cdd:COG4594   265 KEWKNNPLWKNLKAVKNGRVYEVDGDLWTRGrGPLAAELMADDLVEILLKKK 316
 
Name Accession Description Interval E-value
FecB COG4594
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ...
 52-342 6.86e-109

ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 443650 [Multi-domain]  Cd Length: 316  Bit Score: 320.33  E-value: 6.86e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345  52 SITVSDVYGEQTFDEVPEKIVVLEWVYAENLLALGVQPVGMADIEGYHSWVNIEPELDESVEDVGTRQEPSLEAIHALDP 131
Cdd:COG4594    36 ARTVKHAMGETTIPGTPKRVVVLEWSFADALLALGVTPVGIADDNDYDRWVPYLRDLIKGVTSVGTRSQPNLEAIAALKP 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345 132 DLIITAQSRHEDILDSLKDIAPTLVYNAYPEegegtQYEEMVSTFNEMAKLVQKQDEAEQVLSDIEETYETAKTEIEEAG 211
Cdd:COG4594   116 DLIIADKSRHEAIYDQLSKIAPTVLFKSRNG-----DYQENLESFKTIAKALGKEEEAEAVLADHDQRIAEAKAKLAAAD 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345 212 iENKLFALSQAYSSDnspvIRLFKDNAMATEIMTKMGLENAYESEGFQLYGFDQTNVEALQtAQEAHFFYIVQEDDNIFT 291
Cdd:COG4594   191 -KGKKVAVGQFRADG----LRLYTPNSFAGSVLAALGFENPPKQSKDNGYGYSEVSLEQLP-ALDPDVLFIATYDDPSIL 264

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1816544345 292 EQLAGNPAWEELEFVKEDRTYQLPGDTWTFG-GPLSAEVFANQIKEALVQEK 342
Cdd:COG4594   265 KEWKNNPLWKNLKAVKNGRVYEVDGDLWTRGrGPLAAELMADDLVEILLKKK 316
FhuD cd01146
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ...
 66-333 2.65e-74

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: 229.87  E-value: 2.65e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345  66 EVPEKIVVLEWVYAENLLALGVQPVGMADIEGYHSWVNIEPELDESVEDVGTRQEPSLEAIHALDPDLIITAQSRHEDIL 145
Cdd:cd01146     1 AKPQRIVALDWGALETLLALGVKPVGVADTAGYKPWIPEPALPLEGVVDVGTRGQPNLEAIAALKPDLILGSASRHDEIY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345 146 DSLKDIAPTLVYNAYPeegegtQYEEMVSTFNEMAKLVQKQDEAEQVLSDIEETYETAKTEIeeAGIENKLFALSQAYSS 225
Cdd:cd01146    81 DQLSQIAPTVLLDSSP------WLAEWKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKL--PDKGPKPVSVVRFSDA 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345 226 DNspvIRLFKDNAMATEIMTKMGLENAYESEGFQLYGFDQTNVEALqTAQEAHFFYIVQEDDNIFTEQLAGNPAWEELEF 305
Cdd:cd01146   153 GS---IRLYGPNSFAGSVLEDLGLQNPWAQETTNDSGFATISLERL-AKADADVLFVFTYEDEELAQALQANPLWQNLPA 228

                         250       260
                  ....*....|....*....|....*...
gi 1816544345 306 VKEDRTYQLPGDTWTFGGPLSAEVFANQ 333
Cdd:cd01146   229 VKNGRVYVVDDVWWFFGGGLSAARLLLD 256
PRK10576 PRK10576
Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD;
68-338 4.18e-32

Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD;


Pssm-ID: 236719  Cd Length: 292  Bit Score: 121.66  E-value: 4.18e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345  68 PEKIVVLEWVYAENLLALGVQPVGMADIEGYHSWVNiEPELDESVEDVGTRQEPSLEAIHALDPDLIITAQSRHEDIlDS 147
Cdd:PRK10576   32 PNRIVALEWLPVELLLALGVTPYGVADTHNYRLWVS-EPALPDSVIDVGLRTEPNLELLTQMKPSLILWSAGYGPSP-EK 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345 148 LKDIAPTLVYnAYPEEGEGTQYEEmvSTFNEMAKLVQKQDEAEQVLSDIEETYETAKTEIEEAGiENKLFALSQAyssDN 227
Cdd:PRK10576  110 LARIAPGRGF-AFSDGKKPLAVAR--KSLVELAQRLNLEAAAETHLAQFDDFIASAKPRLAGRG-QRPLLLTSLI---DP 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345 228 SPVIrLFKDNAMATEIMTKMGLENAYESE-GFqlYGFDQTNVEALQTAQEAHFFYIVQEDDNIFTeQLAGNPAWEELEFV 306
Cdd:PRK10576  183 RHAL-VFGPNSLFQEVLDELGIENAWQGEtNF--WGSTVVGIERLAAYKDADVICFDHGNSKDMQ-QLMATPLWQAMPFV 258

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1816544345 307 KEDRTYQLPGdTWTFGGPLSAEVFANQIKEAL 338
Cdd:PRK10576  259 RAGRFQRVPA-VWFYGATLSAMHFVRVLDNAL 289
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
 72-317 8.28e-26

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: 103.22  E-value: 8.28e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345  72 VVLEWVYAENLLALGVqPVGMADIEGYHSWVNIEPELDESVEdVGTRQEPSLEAIHALDPDLIITAQSRH-EDILDSLKD 150
Cdd:pfam01497   1 AALSPAYTEILYALGA-TDSIVGVDAYTRDPLKADAVAAIVK-VGAYGEINVERLAALKPDLVILSTGYLtDEAEELLSL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345 151 IAPTLVYNaYPEEGEGtqYEEMVSTfneMAKLVQKQDEAEQVLSDIEETYETAKTEIEEAGIENKLFalsqaYSSDNSPV 230
Cdd:pfam01497  79 IIPTVIFE-SSSTGES--LKEQIKQ---LGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPVLV-----FGGADGGG 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345 231 IRLFKDNAMATEIMTKMGLENAYESEGFQlyGFDQTNVEALQTAQEAHFFYIVQEDDN-IFTEQLAGNPAWEELEFVKED 309
Cdd:pfam01497 148 YVVAGSNTYIGDLLRILGIENIAAELSGS--EYAPISFEAILSSNPDVIIVSGRDSFTkTGPEFVAANPLWAGLPAVKNG 225


                  ....*...
gi 1816544345 310 RTYQLPGD 317
Cdd:pfam01497 226 RVYTLPSD 233
 
Name Accession Description Interval E-value
FecB COG4594
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ...
 52-342 6.86e-109

ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 443650 [Multi-domain]  Cd Length: 316  Bit Score: 320.33  E-value: 6.86e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345  52 SITVSDVYGEQTFDEVPEKIVVLEWVYAENLLALGVQPVGMADIEGYHSWVNIEPELDESVEDVGTRQEPSLEAIHALDP 131
Cdd:COG4594    36 ARTVKHAMGETTIPGTPKRVVVLEWSFADALLALGVTPVGIADDNDYDRWVPYLRDLIKGVTSVGTRSQPNLEAIAALKP 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345 132 DLIITAQSRHEDILDSLKDIAPTLVYNAYPEegegtQYEEMVSTFNEMAKLVQKQDEAEQVLSDIEETYETAKTEIEEAG 211
Cdd:COG4594   116 DLIIADKSRHEAIYDQLSKIAPTVLFKSRNG-----DYQENLESFKTIAKALGKEEEAEAVLADHDQRIAEAKAKLAAAD 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345 212 iENKLFALSQAYSSDnspvIRLFKDNAMATEIMTKMGLENAYESEGFQLYGFDQTNVEALQtAQEAHFFYIVQEDDNIFT 291
Cdd:COG4594   191 -KGKKVAVGQFRADG----LRLYTPNSFAGSVLAALGFENPPKQSKDNGYGYSEVSLEQLP-ALDPDVLFIATYDDPSIL 264

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1816544345 292 EQLAGNPAWEELEFVKEDRTYQLPGDTWTFG-GPLSAEVFANQIKEALVQEK 342
Cdd:COG4594   265 KEWKNNPLWKNLKAVKNGRVYEVDGDLWTRGrGPLAAELMADDLVEILLKKK 316
FhuD cd01146
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ...
 66-333 2.65e-74

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: 229.87  E-value: 2.65e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345  66 EVPEKIVVLEWVYAENLLALGVQPVGMADIEGYHSWVNIEPELDESVEDVGTRQEPSLEAIHALDPDLIITAQSRHEDIL 145
Cdd:cd01146     1 AKPQRIVALDWGALETLLALGVKPVGVADTAGYKPWIPEPALPLEGVVDVGTRGQPNLEAIAALKPDLILGSASRHDEIY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345 146 DSLKDIAPTLVYNAYPeegegtQYEEMVSTFNEMAKLVQKQDEAEQVLSDIEETYETAKTEIeeAGIENKLFALSQAYSS 225
Cdd:cd01146    81 DQLSQIAPTVLLDSSP------WLAEWKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKL--PDKGPKPVSVVRFSDA 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345 226 DNspvIRLFKDNAMATEIMTKMGLENAYESEGFQLYGFDQTNVEALqTAQEAHFFYIVQEDDNIFTEQLAGNPAWEELEF 305
Cdd:cd01146   153 GS---IRLYGPNSFAGSVLEDLGLQNPWAQETTNDSGFATISLERL-AKADADVLFVFTYEDEELAQALQANPLWQNLPA 228

                         250       260
                  ....*....|....*....|....*...
gi 1816544345 306 VKEDRTYQLPGDTWTFGGPLSAEVFANQ 333
Cdd:cd01146   229 VKNGRVYVVDDVWWFFGGGLSAARLLLD 256
FepB COG0614
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ...
 70-334 2.07e-39

ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 440379 [Multi-domain]  Cd Length: 264  Bit Score: 140.13  E-value: 2.07e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345  70 KIVVLEWVYAENLLALGVQP--VGMADIegyhSWVNIEPELDESVEDVGTRQEPSLEAIHALDPDLIITAQS-RHEDILD 146
Cdd:COG0614     2 RIVSLSPSATELLLALGAGDrlVGVSDW----GYCDYPELELKDLPVVGGTGEPNLEAILALKPDLVLASSSgNDEEDYE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345 147 SLKDI-APTLVYNAYPeegegtqYEEMVSTFNEMAKLVQKQDEAEQVLSDIEETYETAKTEIeeAGIENKLFALSQAYSS 225
Cdd:COG0614    78 QLEKIgIPVVVLDPRS-------LEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARL--AGAEERPTVLYEIWSG 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345 226 DNspvIRLFKDNAMATEIMTKMGLENAYESEGFqlyGFDQTNVEALQTAQEAHFFY----IVQEDDNIFTEQLAGNPAWE 301
Cdd:COG0614   149 DP---LYTAGGGSFIGELLELAGGRNVAADLGG---GYPEVSLEQVLALDPDVIILsgggYDAETAEEALEALLADPGWQ 222

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1816544345 302 ELEFVKEDRTYQLPGDTWTFGGPL---SAEVFANQI 334
Cdd:COG0614   223 SLPAVKNGRVYVVPGDLLSRPGPRlllALEDLAKAL 258
PRK10576 PRK10576
Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD;
68-338 4.18e-32

Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD;


Pssm-ID: 236719  Cd Length: 292  Bit Score: 121.66  E-value: 4.18e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345  68 PEKIVVLEWVYAENLLALGVQPVGMADIEGYHSWVNiEPELDESVEDVGTRQEPSLEAIHALDPDLIITAQSRHEDIlDS 147
Cdd:PRK10576   32 PNRIVALEWLPVELLLALGVTPYGVADTHNYRLWVS-EPALPDSVIDVGLRTEPNLELLTQMKPSLILWSAGYGPSP-EK 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345 148 LKDIAPTLVYnAYPEEGEGTQYEEmvSTFNEMAKLVQKQDEAEQVLSDIEETYETAKTEIEEAGiENKLFALSQAyssDN 227
Cdd:PRK10576  110 LARIAPGRGF-AFSDGKKPLAVAR--KSLVELAQRLNLEAAAETHLAQFDDFIASAKPRLAGRG-QRPLLLTSLI---DP 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345 228 SPVIrLFKDNAMATEIMTKMGLENAYESE-GFqlYGFDQTNVEALQTAQEAHFFYIVQEDDNIFTeQLAGNPAWEELEFV 306
Cdd:PRK10576  183 RHAL-VFGPNSLFQEVLDELGIENAWQGEtNF--WGSTVVGIERLAAYKDADVICFDHGNSKDMQ-QLMATPLWQAMPFV 258

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1816544345 307 KEDRTYQLPGdTWTFGGPLSAEVFANQIKEAL 338
Cdd:PRK10576  259 RAGRFQRVPA-VWFYGATLSAMHFVRVLDNAL 289
CeuA COG4607
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and ...
 51-338 4.66e-30

ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 443657 [Multi-domain]  Cd Length: 310  Bit Score: 116.43  E-value: 4.66e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345  51 TSITVSDVYGEQTFDEVPEKIVVLEWVYAENLLALGVQPVGMADiegyhswVNIEPEL----DESVEDVGTRQEPSLEAI 126
Cdd:COG4607    34 ETVTVEHALGTVEVPKNPKRVVVFDNGALDTLDALGVEVAGVPK-------GLLPDYLskyaDDKYANVGTLFEPDLEAI 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345 127 HALDPDLIITAQsRHEDILDSLKDIAPTLVYNAypeegEGTQY-EEMVSTFNEMAKLVQKQDEAEQVLSDIEETYETAKt 205
Cdd:COG4607   107 AALKPDLIIIGG-RSAKKYDELSKIAPTIDLTV-----DGEDYlESLKRNTETLGEIFGKEDEAEELVADLDAKIAALK- 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345 206 eieeagienklfalsQAYSSDnspvirlfkDNAMAteIMTKMGLENAYESEG-----FQLYGFDQTnVEALQTA---QEA 277
Cdd:COG4607   180 ---------------AAAAGK---------GTALI--VLTNGGKISAYGPGSrfgpiHDVLGFKPA-DEDIEASthgQAI 232

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1816544345 278 HFFYIVQED-DNIF--------------TEQLAGNPAWEELEFVKEDRTYQLPGDTW--TFGGPLSAEVFANQIKEAL 338
Cdd:COG4607   233 SFEFIAEANpDWLFvidrdaaiggegpaAKQVLDNELVKQTTAWKNGQIVYLDPDAWylAGGGIQSLTEMLDEVADAL 310
fecB PRK11411
iron-dicitrate transporter substrate-binding subunit; Provisional
 53-342 1.78e-27

iron-dicitrate transporter substrate-binding subunit; Provisional


Pssm-ID: 183123 [Multi-domain]  Cd Length: 303  Bit Score: 109.38  E-value: 1.78e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345  53 ITVSDVYGEQTFDEVPEKIVVLEWVYAENLLALGVQPVGMADIEGYHswvNIEPELDESV---EDVGTRQEPSLEAIHAL 129
Cdd:PRK11411   24 VTVQDEQGTFTLEKTPQRIVVLELSFVDALAAVGVSPVGVADDNDAK---RILPEVRAHLkpwQSVGTRSQPSLEAIAAL 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345 130 DPDLIITAQSRHEDILDSLKDIAPTLVYNAypeegEGTQYEEMVSTFNEMAKLVQKQDEAEQVLSDIEETYETAKTEIEE 209
Cdd:PRK11411  101 KPDLIIADSSRHAGVYIALQKIAPTLLLKS-----RNETYQENLQSAAIIGEVLGKKREMQARIEQHKERMAQFASQLPK 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345 210 AgiENKLFALSQAYSsdnspvIRLFKDNAMATEIMTKMGLENAYESEGFQLYGFdqTNVEALQTAQEAHFFYIVQEDDNI 289
Cdd:PRK11411  176 G--TRVAFGTSREQQ------FNLHSPESYTGSVLAALGLNVPKAPMNGAAMPS--ISLEQLLALNPDWLLVAHYRQESI 245

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1816544345 290 fTEQLAGNPAWEELEFVKEDRTYQLPGDTWTFG-GPLSAEVFANQIKEALVQEK 342
Cdd:PRK11411  246 -VKRWQQDPLWQMLTAAKKQQVASVDSNTWARMrGIFAAERIAKDTVKIFHHQP 298
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
 72-317 8.28e-26

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: 103.22  E-value: 8.28e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345  72 VVLEWVYAENLLALGVqPVGMADIEGYHSWVNIEPELDESVEdVGTRQEPSLEAIHALDPDLIITAQSRH-EDILDSLKD 150
Cdd:pfam01497   1 AALSPAYTEILYALGA-TDSIVGVDAYTRDPLKADAVAAIVK-VGAYGEINVERLAALKPDLVILSTGYLtDEAEELLSL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345 151 IAPTLVYNaYPEEGEGtqYEEMVSTfneMAKLVQKQDEAEQVLSDIEETYETAKTEIEEAGIENKLFalsqaYSSDNSPV 230
Cdd:pfam01497  79 IIPTVIFE-SSSTGES--LKEQIKQ---LGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPVLV-----FGGADGGG 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345 231 IRLFKDNAMATEIMTKMGLENAYESEGFQlyGFDQTNVEALQTAQEAHFFYIVQEDDN-IFTEQLAGNPAWEELEFVKED 309
Cdd:pfam01497 148 YVVAGSNTYIGDLLRILGIENIAAELSGS--EYAPISFEAILSSNPDVIIVSGRDSFTkTGPEFVAANPLWAGLPAVKNG 225


                  ....*...
gi 1816544345 310 RTYQLPGD 317
Cdd:pfam01497 226 RVYTLPSD 233
FatB cd01140
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ...
 60-323 2.09e-25

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: 103.11  E-value: 2.09e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345  60 GEQTFDEVPEKIVVLEWVYAENLLALGVQPVGMADiegyhswVNIEPEL-----DESVEDVGTRQEPSLEAIHALDPDLI 134
Cdd:cd01140     4 GETKVPKNPEKVVVFDVGALDTLDALGVKVVGVPK-------SSTLPEYlkkykDDKYANVGTLFEPDLEAIAALKPDLI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345 135 ITAQsRHEDILDSLKDIAPTLVYNAYPEEgegtQYEEMVSTFNEMAKLVQKQDEAEQVLSDIEETYETAKTEIEEAGieN 214
Cdd:cd01140    77 IIGG-RLAEKYDELKKIAPTIDLGADLKN----YLESVKQNIETLGKIFGKEEEAKELVAEIDASIAEAKSAAKGKK--K 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345 215 KLFALSqayssdNSPVIRLFKDNAMATEIMTKMGLENAYESEGFQLYGfDQTNVEALQTAQEAHFFYI----VQEDDNIF 290
Cdd:cd01140   150 ALVVLV------NGGKLSAFGPGSRFGWLHDLLGFEPADENIKASSHG-QPVSFEYILEANPDWLFVIdrgaAIGAEGSS 222

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1816544345 291 TEQLAGNPAWEELEFVKEDRTYQLPGDTWTFGG 323
Cdd:cd01140   223 AKEVLDNDLVKNTTAWKNGKVIYLDPDLWYLSG 255
TroA-like cd00636
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ...
 69-220 1.04e-23

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: 94.93  E-value: 1.04e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345  69 EKIVVLEWVYAENLLALG--VQPVGMADIEGYHSWVNiepELDESVEDVGTRQEPSLEAIHALDPDLIITAQSRHEDILD 146
Cdd:cd00636     1 KRVVALDPGATELLLALGgdDKPVGVADPSGYPPEAK---ALLEKVPDVGHGYEPNLEKIAALKPDLIIANGSGLEAWLD 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1816544345 147 SLKDIA-PTLVYNaypeEGEGTQYEEMVSTFNEMAKLVQKQDEAEQVLSDIEETYETAKTEIEEAGIENKLFALS 220
Cdd:cd00636    78 KLSKIAiPVVVVD----EASELSLENIKESIRLIGKALGKEENAEELIAELDARLAELRAKLAKIPKKKVSLVVG 148
FeuA cd01138
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ...
 68-321 7.77e-19

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: 84.31  E-value: 7.77e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345  68 PEKIVVLEWVYaENLLALGVQPVGMADiegyHSWVNiePELDESVEDVGTRQ--EPSLEAIHALDPDLIItAQSRHEDIL 145
Cdd:cd01138     9 PKRIVALSGET-EGLALLGIKPVGAAS----IGGKN--PYYKKKTLAKVVGIvdEPNLEKVLELKPDLII-VSSKQEENY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345 146 DSLKDIAPTLVYNAypeegEGTQYEEMVStfnEMAKLVQKQDEAEQVLSDIEETYETAKTEIEEAGIENKlfALSQAYSS 225
Cdd:cd01138    81 EKLSKIAPTVPVSY-----NSSDWEEQLK---EIGKLLNKEDEAEKWLADYKQKAKEAKEKIKKKLGNDK--SVAVLRGR 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345 226 DNspvIRLFKDN--AMATEIMTKMGLE-NAYESEGFQLYGFDQTNVEALQTAQEAHFFyIVQEDDNIFTEQLAGNPAWEE 302
Cdd:cd01138   151 KQ---IYVFGEDgrGGGPILYADLGLKaPEKVKEIEDKPGYAAISLEVLPEFDADYIF-LLFFTGPEAKADFESLPIWKN 226

                         250
                  ....*....|....*....
gi 1816544345 303 LEFVKEDRTYQLpgDTWTF 321
Cdd:cd01138   227 LPAVKNNHVYIV--DAWVF 243
TroA_a cd01148
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ...
 53-323 3.50e-13

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: 68.90  E-value: 3.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345  53 ITVSDVYGEQTFDEVPEKIVVLEWVYAENLLALGVQP--VGMADIEgyhswVNIEPELD---ESVEDVGTRqEPSLEAIH 127
Cdd:cd01148     3 LTVENCGRSVTFDKAPQRVVSNDQNTTEMMLALGLQDrmVGTAGID-----NKDLPELKakyDKVPELAKK-YPSKETVL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345 128 ALDPDLIITAQS---RHEDIL--DSLKDI-APTLVYNAY-PEEGEGTQYEEMVSTFNEMAKLVQKQDEAEQVLSDIEETY 200
Cdd:cd01148    77 AARPDLVFGGWSygfDKGGLGtpDSLAELgIKTYILPEScGQRRGEATLDDVYNDIRNLGKIFDVEDRADKLVADLKARL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345 201 ETAKTEIEEAGIENKLFALSqaySSDNSPVIrlFKDNAMATEIMTKMGLENAYESEGFQlygFDQTNVEALqTAQEAHFF 280
Cdd:cd01148   157 AEISAKVKGDGKKVAVFVYD---SGEDKPFT--SGRGGIPNAIITAAGGRNVFADVDES---WTTVSWETV-IARNPDVI 227

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1816544345 281 YIVQEDDNIFTEQ----LAGNPAWEELEFVKEDRTYQLPGDTWTFGG 323
Cdd:cd01148   228 VIIDYGDQNAAEQkikfLKENPALKNVPAVKNNRFIVLPLAEATPGI 274
YvrC cd01143
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ...
 68-271 9.52e-11

Periplasmic binding protein YvrC. These proteins are predicted to function as initial receptors in ABC transport of metal ions in eubacteria and archaea. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains.


Pssm-ID: 238563 [Multi-domain]  Cd Length: 195  Bit Score: 60.37  E-value: 9.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345  68 PEKIVVLEWVYAENLLALGV--QPVGMADIEGYhswvniePELDESVEDVGTRQEPSLEAIHALDPDLIITAQSRHEDIL 145
Cdd:cd01143     3 PERIVSLSPSITEILFALGAgdKIVGVDTYSNY-------PKEVRKKPKVGSYSNPNVEKIVALKPDLVIVSSSSLAELL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345 146 DSLKDIAPTLVYNaypeeGEGTQYEEMVSTFNEMAKLVQKQDEAEQVLSDIeetyetaKTEIEEAGIENK-LFALSQAYS 224
Cdd:cd01143    76 EKLKDAGIPVVVL-----PAASSLDEIYDQIELIGKITGAEEEAEKLVKEM-------KQKIDKVKDKGKtIKKSKVYIE 143

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1816544345 225 SDNSPVIRLFKDNAMAtEIMTKMGLENAYESEGfqlyGFDQTNVEAL 271
Cdd:cd01143   144 VSLGGPYTAGKNTFIN-ELIRLAGAKNIAADSG----GWPQVSPEEI 185
FepB COG4592
ABC-type Fe2+-enterobactin transport system, periplasmic component [Inorganic ion transport ...
 54-321 3.31e-10

ABC-type Fe2+-enterobactin transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 443649 [Multi-domain]  Cd Length: 330  Bit Score: 60.34  E-value: 3.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345  54 TVSDVYGEQTFDEVPEKIVVLEWVYAENLLALGVQPVG--------MADIEGYHS-WVniepelDESVEDvGTRQ----- 119
Cdd:COG4592    43 TVTTEKGTVTLPAKPQRIVSTSVTLTGSLLAIDAPVVAsgattpnnVTDDQGFFRqWA------DVAKER-GVKRlyigl 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345 120 EPSLEAIHALDPDLIITAQSRHE---DILDSLKDIAPTLVYNaYPEEGEGTQYEemvstfnEMAKLVQKQDEAEQVLSDI 196
Cdd:COG4592   116 EPNAEAIAAAAPDLIIGSATGGDsalDLYDQLSAIAPTLVVN-YDDKSWQELAT-------QLGEATGHEAQADAVIAAF 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345 197 EETYETAKTEIEEAgiENKLFALsqAYSSDNSPviRLFKDNAMATEIMTKMG--LENAYESEGF-QLYG----FDQTNVE 269
Cdd:COG4592   188 DARVAEVKAAITLP--PQPVSAL--VYNEDGGA--NLWTPESAQGQLLQALGftLAPLPAELATsTSQGkrgdIVQLSGE 261

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1816544345 270 ALQTA--QEAHFFYIVQEDDnifTEQLAGNPAWEELEFVKEDRTYQLPgdTWTF 321
Cdd:COG4592   262 NLAAAltGPTLFLFAADDKD---VDALKADPLLAHLPAVQAGRVYALG--PDSF 310
TroA_e cd01142
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ...
 54-326 6.58e-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: 53.13  E-value: 6.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345  54 TVSDVYGEQ-TFDEVPEKIVVLEWVYAENLLALGVQPVGMADIegyHSWVNIE------PELDEsVEDVGTRQEPSLEAI 126
Cdd:cd01142     9 TITDMAGRKvTIPDEVKRIAALWGAGNAVVAALGGGKLIVATT---STVQQEPwlyrlaPSLEN-VATGGTGNDVNIEEL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345 127 HALDPDLIITAQSRHEDILDSLKDIAPTLvynaYPEEGEGTQYEEmvsTFNEMAKLVQKQDEAEQVLSDIEET--YETAK 204
Cdd:cd01142    85 LALKPDVVIVWSTDGKEAGKAVLRLLNAL----SLRDAELEEVKL---TIALLGELLGRQEKAEALVAYFDDNlaYVAAR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345 205 TEIEEAGIENKLF-ALSQAYSSDNSPVIrlfkdnamATEIMTKMGLENAYESEGFQlyGFDQTNVEALQTAQEAhfFYIV 283
Cdd:cd01142   158 TKKLPDSERPRVYyAGPDPLTTDGTGSI--------TNSWIDLAGGINVASEATKK--GSGEVSLEQLLKWNPD--VIIV 225

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1816544345 284 QEDDNifTEQLAGNPAWEELEFVKEDRTYQLPGDTWTFGGPLS 326
Cdd:cd01142   226 GNADT--KAAILADPRWQNLRAVKNGRVYVNPEGAFWWDRPSA 266
PRK10957 PRK10957
iron-enterobactin transporter periplasmic binding protein; Provisional
 54-318 2.27e-07

iron-enterobactin transporter periplasmic binding protein; Provisional


Pssm-ID: 236806 [Multi-domain]  Cd Length: 317  Bit Score: 51.51  E-value: 2.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345  54 TVSDVYGEQTFDEVPEKIVVLEWVYAENLLALGVqPV----------GMADIEGYHS-WVNIEPELDESVEDVGtrqEPS 122
Cdd:PRK10957   30 TVTDSRGSVTLESKPQRIVSTSVTLTGTLLAIDA-PViasgattpntRVADDQGFFRqWSDVAKERGVEVLYIG---EPD 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345 123 LEAIHALDPDLII---TAQSRHEDILDSLKDIAPTLVYNaYpeegeGTQYEEMVSTfnEMAKLVQKQDEAEQVLSDIEET 199
Cdd:PRK10957  106 AEAVAAQMPDLIVisaTGGDSALALYDQLSAIAPTLVID-Y-----DDKSWQELAT--QLGEATGLEKQAAAVIAQFDAQ 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345 200 YETAKTEIEEAgiENKLFALSqaYSSDNSPViRLFKDNAMATEIMTKMGLENAYESEGFQ-------LYGFDQTNVEALQ 272
Cdd:PRK10957  178 LAEVKAKITLP--PQPVSALV--YNGAGHSA-NLWTPESAQGQLLEQLGFTLAELPAGLQastsqgkRHDIIQLGGENLA 252

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1816544345 273 TAQEAHFFYIVQEDDNIfTEQLAGNPAWEELEFVKEDRTYQLPGDT 318
Cdd:PRK10957  253 AGLNGETLFLFAGDDKD-ADAFLADPLLANLPAVQNKQVYALGTDT 297
ChuT COG4558
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ...
 60-275 1.44e-06

ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 443619 [Multi-domain]  Cd Length: 285  Bit Score: 49.03  E-value: 1.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345  60 GEQTFDEVPEKIVVL-----EWVYAenllaLGVQP--VGmADIEGYHswvniePELDESVEDVGTRQEPSLEAIHALDPD 132
Cdd:COG4558    19 GASVAAAAAERIVSLggsvtEIVYA-----LGAGDrlVG-VDTTSTY------PAAAKALPDVGYMRQLSAEGILSLKPT 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345 133 LII-TAQSRHEDILDSLKD--IAPTLVYNAYPEEGegtqyeeMVSTFNEMAKLVQKQDEAEQVLSDIEETYETAKTEIEE 209
Cdd:COG4558    87 LVLaSEGAGPPEVLDQLRAagVPVVVVPAAPSLEG-------VLAKIRAVAAALGVPEAGEALAARLEADLAALAARVAA 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1816544345 210 AGIENK-LFALSQAyssdnSPVIRLFKDNAMATEIMTKMGLENAYesEGFQlyGFDQTNVEALQTAQ 275
Cdd:COG4558   160 IGKPPRvLFLLSRG-----GGRPMVAGRGTAADALIRLAGGVNAA--AGFE--GYKPLSAEALIAAA 217
TroA_d cd01141
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ...
 68-201 1.73e-06

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: 47.80  E-value: 1.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345  68 PEKIVVLEWVYAENLLALGVQpVGMADIEGYHSWVNIEPELDESVEDVGTRQEPSLEAIHALDPDLIITAQ-SRHEDILD 146
Cdd:cd01141     8 PKRIVVLSPTHVDLLLALDKA-DKIVGVSASAYDLNTPAVKERIDIQVGPTGSLNVELIVALKPDLVILYGgFQAQTILD 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1816544345 147 SLKDIAPTLVYNaYPEEGEGTQYEEMVSTFNEMAklVQKQDEAEQVLSDIEETYE 201
Cdd:cd01141    87 KLEQLGIPVLYV-NEYPSPLGRAEWIKFAAAFYG--VGKEDKADEAFAQIAGRYR 138
HemV-2 cd01147
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ...
 69-315 2.62e-06

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: 48.10  E-value: 2.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345  69 EKIVVLEWVYAENLLALGVQP--VGMADIE----GYHSWVnIEPELDE--SVEDVGTRQEPSLEAIHALDPDLII----T 136
Cdd:cd01147     6 ERVVAAGPGALRLLYALAAPDkiVGVDDAEksdeGRPYFL-ASPELKDlpVIGRGGRGNTPNYEKIAALKPDVVIdvgsD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345 137 AQSRHEDILDSLKDIAPTLVYNaypeegeGTQYEEMVSTFNEMAKLVQKQDEAEQVLSDIEETYETakteieeagIENKL 216
Cdd:cd01147    85 DPTSIADDLQKKTGIPVVVLDG-------GDSLEDTPEQIRLLGKVLGKEERAEELISFIESILAD---------VEERT 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345 217 FALSqayssdNSPVIRLFkdnAMATEIMTKMGLENAYES--EGFQLYGFdqTNVEALQTAqEAHFF----YIVQED-DNI 289
Cdd:cd01147   149 KDIP------DEEKPTVY---FGRIGTKGAAGLESGLAGsiEVFELAGG--INVADGLGG-GGLKEvspeQILLWNpDVI 216

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1816544345 290 FT----------EQLAGNPAWEELEFVKEDRTYQLP 315
Cdd:cd01147   217 FLdtgsfylsleGYAKNRPFWQSLKAVKNGRVYLLP 252
HutB cd01149
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ...
 68-275 2.81e-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: 41.87  E-value: 2.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345  68 PEKIVVL-----EWVYAenlLALGVQPVGMaDIEGYHswvniePELDESVEDVGTRQEPSLEAIHALDPDLII-TAQSRH 141
Cdd:cd01149     1 PERIVSLggsvtEIVYA---LGAGDRLVGV-DSTSTY------PEAAAKLPDVGYMRQLSAEGVLSLKPTLVIaSDEAGP 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816544345 142 EDILDSLKDIA-PTLVYNAYPEEgegtqyEEMVSTFNEMAKLVQKQDEAEQVLSDIEETYETAKTEIEEAGIENK-LFal 219
Cdd:cd01149    71 PEALDQLRAAGvPVVTVPSTPTL------DGLLTKIRQVAQALGVPEKGEALAQEVRQRLAALRKTVAAHKKPPRvLF-- 142

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1816544345 220 sqAYSSDNSPVIRLFKDNAmATEIMTKMGLENAyeseGFQLYGFDQTNVEALQTAQ 275
Cdd:cd01149   143 --LLSHGGGAAMAAGRNTA-ADAIIALAGAVNA----AAGFRGYKPLSAEALIAAQ 191
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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