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Conserved domains on  [gi|81705852|sp|Q7A652|]
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RecName: Full=High-affinity heme uptake system protein IsdE; AltName: Full=Iron-regulated surface determinant protein E; AltName: Full=Staphylococcal iron-regulated protein F; Flags: Precursor

Protein Classification

heme ABC transporter substrate-binding protein IsdE( domain architecture ID 11497308)

heme ABC transporter substrate-binding protein IsdE binds Fe(2+) and Fe(3+) heme, and may function in relaying heme-iron from cell wall-anchored isd proteins receptors to the probable permease IsdF

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
IsdE TIGR03659
heme ABC transporter, heme-binding protein isdE; This family of ABC substrate-binding proteins ...
 2-288 1.58e-151

heme ABC transporter, heme-binding protein isdE; This family of ABC substrate-binding proteins is observed primarily in close proximity with proteins localized to the cell wall and bearing the NEAT (NEAr Transporter, pfam05031) heme-binding domain. IsdE has been shown to bind heme and is involved in the process of scavenging heme for the purpose of obtaining iron.


:

Pssm-ID: 274706 [Multi-domain]  Cd Length: 289  Bit Score: 425.15  E-value: 1.58e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852     2 RIIKYLTILVISVVILT---SCQSSSSQESTKSGEFRIVPTTVALTMTLDKLDLPIVGKPTSYKTLPNRYKDVPEIGQPM 78
Cdd:TIGR03659   1 KKILSLVLLAVLSLGLTgcsSSKEKSKVSNKKSKEERIVATSVAVTEILDKLDLDLVGVPTSQKTLPKRYKDVPEVGNPM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852    79 EPNVEAVKKLKPTHVLSVSTIKDEMQPFYKQLNMKGYFYDFDSLKGMQKSITQLGDQFNRKAQAKELNDHLNSVKQKIEN 158
Cdd:TIGR03659  81 SPDMEKIKSLKPTVVLSVTTLEEDLGPKFKQLGVEATFLNLTSVDGMKKSITELGEKYGREEQAEKLVKEINEKEAEVKK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852   159 KAAKQKKhPKVLILMGVPGSYLVATDKSYIGDLVKIAGGENVIKVKDRQYISSNTENLLNINPDIILRLPHGMPEEVKKM 238
Cdd:TIGR03659 161 KVKGKKK-PKVLILMGVPGSYLVATENSYIGDLVKLAGGENVYKGNKQEYLSSNTEYLLKANPDIILRAAHGMPDEVKKM 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 81705852   239 FQKEFKQNDIWKHFKAVKNNHVYDLEEVPFGITANVDADKAMTQLYDLFY 288
Cdd:TIGR03659 240 FDEEFKTNDIWKHFEAVKNNRVYDLDEELFGMTANLKVAEALDELKKILY 289
 
Name Accession Description Interval E-value
IsdE TIGR03659
heme ABC transporter, heme-binding protein isdE; This family of ABC substrate-binding proteins ...
 2-288 1.58e-151

heme ABC transporter, heme-binding protein isdE; This family of ABC substrate-binding proteins is observed primarily in close proximity with proteins localized to the cell wall and bearing the NEAT (NEAr Transporter, pfam05031) heme-binding domain. IsdE has been shown to bind heme and is involved in the process of scavenging heme for the purpose of obtaining iron.


Pssm-ID: 274706 [Multi-domain]  Cd Length: 289  Bit Score: 425.15  E-value: 1.58e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852     2 RIIKYLTILVISVVILT---SCQSSSSQESTKSGEFRIVPTTVALTMTLDKLDLPIVGKPTSYKTLPNRYKDVPEIGQPM 78
Cdd:TIGR03659   1 KKILSLVLLAVLSLGLTgcsSSKEKSKVSNKKSKEERIVATSVAVTEILDKLDLDLVGVPTSQKTLPKRYKDVPEVGNPM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852    79 EPNVEAVKKLKPTHVLSVSTIKDEMQPFYKQLNMKGYFYDFDSLKGMQKSITQLGDQFNRKAQAKELNDHLNSVKQKIEN 158
Cdd:TIGR03659  81 SPDMEKIKSLKPTVVLSVTTLEEDLGPKFKQLGVEATFLNLTSVDGMKKSITELGEKYGREEQAEKLVKEINEKEAEVKK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852   159 KAAKQKKhPKVLILMGVPGSYLVATDKSYIGDLVKIAGGENVIKVKDRQYISSNTENLLNINPDIILRLPHGMPEEVKKM 238
Cdd:TIGR03659 161 KVKGKKK-PKVLILMGVPGSYLVATENSYIGDLVKLAGGENVYKGNKQEYLSSNTEYLLKANPDIILRAAHGMPDEVKKM 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 81705852   239 FQKEFKQNDIWKHFKAVKNNHVYDLEEVPFGITANVDADKAMTQLYDLFY 288
Cdd:TIGR03659 240 FDEEFKTNDIWKHFEAVKNNRVYDLDEELFGMTANLKVAEALDELKKILY 289
FatB cd01140
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ...
 35-289 2.17e-52

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: 172.44  E-value: 2.17e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852  35 RIVPTTVALTMTLDKLDLPIVGKPTSyKTLPNRYKDV-----PEIGQPMEPNVEAVKKLKPTHVLSVSTikdeMQPFYKQ 109
Cdd:cd01140  14 KVVVFDVGALDTLDALGVKVVGVPKS-STLPEYLKKYkddkyANVGTLFEPDLEAIAALKPDLIIIGGR----LAEKYDE 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852 110 L----NMKGYFYDFD-SLKGMQKSITQLGDQFNRKAQAKELNDHLNSVKQKIENKAAKQKKhPKVLILMGvpGSYLVATD 184
Cdd:cd01140  89 LkkiaPTIDLGADLKnYLESVKQNIETLGKIFGKEEEAKELVAEIDASIAEAKSAAKGKKK-ALVVLVNG--GKLSAFGP 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852 185 KSYIGDLVKIAGGENVIKVK--DRQYISSNTENLLNINPDIILRLPHGMPEEVKKMFQKEFKQNDIWKHFKAVKNNHVYD 262
Cdd:cd01140 166 GSRFGWLHDLLGFEPADENIkaSSHGQPVSFEYILEANPDWLFVIDRGAAIGAEGSSAKEVLDNDLVKNTTAWKNGKVIY 245

                       250       260
                ....*....|....*....|....*..
gi 81705852 263 LEEVPFGITANVdaDKAMTQLYDLFYK 289
Cdd:cd01140 246 LDPDLWYLSGGG--LESLKQMIDDLKK 270
FepB COG0614
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ...
 35-291 9.35e-50

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


Pssm-ID: 440379 [Multi-domain]  Cd Length: 264  Bit Score: 165.56  E-value: 9.35e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852  35 RIVPTTVALTMTLDKLDLP--IVGKP-TSYKTLP-NRYKDVPEIGQPMEPNVEAVKKLKPTHVL-SVSTIKDEMQPFYKQ 109
Cdd:COG0614   2 RIVSLSPSATELLLALGAGdrLVGVSdWGYCDYPeLELKDLPVVGGTGEPNLEAILALKPDLVLaSSSGNDEEDYEQLEK 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852 110 LNMKGYFYDFDSLKGMQKSITQLGDQFNRKAQAKELNDHLNSVKQKIENKAAKQKKHPKVLILMGVPGSYLVATDKSYIG 189
Cdd:COG0614  82 IGIPVVVLDPRSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGAEERPTVLYEIWSGDPLYTAGGGSFIG 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852 190 DLVKIAGGENVIKVKDRQYISSNTENLLNINPDIILRLPHGMPEEVKKMFQKEFKQNDIWKHFKAVKNNHVYDLEEVpFG 269
Cdd:COG0614 162 ELLELAGGRNVAADLGGGYPEVSLEQVLALDPDVIILSGGGYDAETAEEALEALLADPGWQSLPAVKNGRVYVVPGD-LL 240

                       250       260
                ....*....|....*....|..
gi 81705852 270 ITANVDADKAMTQLYDLFYKDK 291
Cdd:COG0614 241 SRPGPRLLLALEDLAKALHPEL 262
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
 46-263 1.49e-37

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: 132.88  E-value: 1.49e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852    46 TLDKLDL--PIVGKP--TSYKTLPNRYKDVPEIGQPMEPNVEAVKKLKPTHVLSVSTIKDEmqPFYKQL--NMKGYFYDF 119
Cdd:pfam01497  10 ILYALGAtdSIVGVDayTRDPLKADAVAAIVKVGAYGEINVERLAALKPDLVILSTGYLTD--EAEELLslIIPTVIFES 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852   120 DSLK-GMQKSITQLGDQFNRKAQAKELNDHLNSVKQKIENKAAKQKKHPKVLILMGVPGSYLVATDKSYIGDLVKIAGGE 198
Cdd:pfam01497  88 SSTGeSLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPVLVFGGADGGGYVVAGSNTYIGDLLRILGIE 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 81705852   199 NVIKVKDR-QYISSNTENLLNINPDIILRLPHGMpeeVKKMFQKEFKQNDIWKHFKAVKNNHVYDL 263
Cdd:pfam01497 168 NIAAELSGsEYAPISFEAILSSNPDVIIVSGRDS---FTKTGPEFVAANPLWAGLPAVKNGRVYTL 230
btuF PRK09534
corrinoid ABC transporter substrate-binding protein; Reviewed
 75-225 3.76e-09

corrinoid ABC transporter substrate-binding protein; Reviewed


Pssm-ID: 236552 [Multi-domain]  Cd Length: 359  Bit Score: 56.84  E-value: 3.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852   75 GQPMEPNVEAVKKLKPTHVLSVSTIKDEMQPFYKQLNMKGYFYDF-DSLKGMQKSITQLGDQFNRKAQAKELNDHLNSVK 153
Cdd:PRK09534 105 GQPFGVNVEAVVGLDPDLVLAPNAVAGDTVTRLREAGITVFHFPAaTSIEDVAEKTATIGRLTGNCEAAAETNAEMRDRV 184

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 81705852  154 QKIENKAAKQKKHPKVLILMGvpGSYlVATDKSYIGDLVKIAGGENVIKVKD-RQYISSNTENLLNINPDIIL 225
Cdd:PRK09534 185 DAVEDRTADVDDRPRVLYPLG--DGY-TAGGNTFIGALIEAAGGHNVAADATtDGYPQLSEEVIVQQDPDVIV 254
 
Name Accession Description Interval E-value
IsdE TIGR03659
heme ABC transporter, heme-binding protein isdE; This family of ABC substrate-binding proteins ...
 2-288 1.58e-151

heme ABC transporter, heme-binding protein isdE; This family of ABC substrate-binding proteins is observed primarily in close proximity with proteins localized to the cell wall and bearing the NEAT (NEAr Transporter, pfam05031) heme-binding domain. IsdE has been shown to bind heme and is involved in the process of scavenging heme for the purpose of obtaining iron.


Pssm-ID: 274706 [Multi-domain]  Cd Length: 289  Bit Score: 425.15  E-value: 1.58e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852     2 RIIKYLTILVISVVILT---SCQSSSSQESTKSGEFRIVPTTVALTMTLDKLDLPIVGKPTSYKTLPNRYKDVPEIGQPM 78
Cdd:TIGR03659   1 KKILSLVLLAVLSLGLTgcsSSKEKSKVSNKKSKEERIVATSVAVTEILDKLDLDLVGVPTSQKTLPKRYKDVPEVGNPM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852    79 EPNVEAVKKLKPTHVLSVSTIKDEMQPFYKQLNMKGYFYDFDSLKGMQKSITQLGDQFNRKAQAKELNDHLNSVKQKIEN 158
Cdd:TIGR03659  81 SPDMEKIKSLKPTVVLSVTTLEEDLGPKFKQLGVEATFLNLTSVDGMKKSITELGEKYGREEQAEKLVKEINEKEAEVKK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852   159 KAAKQKKhPKVLILMGVPGSYLVATDKSYIGDLVKIAGGENVIKVKDRQYISSNTENLLNINPDIILRLPHGMPEEVKKM 238
Cdd:TIGR03659 161 KVKGKKK-PKVLILMGVPGSYLVATENSYIGDLVKLAGGENVYKGNKQEYLSSNTEYLLKANPDIILRAAHGMPDEVKKM 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 81705852   239 FQKEFKQNDIWKHFKAVKNNHVYDLEEVPFGITANVDADKAMTQLYDLFY 288
Cdd:TIGR03659 240 FDEEFKTNDIWKHFEAVKNNRVYDLDEELFGMTANLKVAEALDELKKILY 289
FatB cd01140
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ...
 35-289 2.17e-52

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: 172.44  E-value: 2.17e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852  35 RIVPTTVALTMTLDKLDLPIVGKPTSyKTLPNRYKDV-----PEIGQPMEPNVEAVKKLKPTHVLSVSTikdeMQPFYKQ 109
Cdd:cd01140  14 KVVVFDVGALDTLDALGVKVVGVPKS-STLPEYLKKYkddkyANVGTLFEPDLEAIAALKPDLIIIGGR----LAEKYDE 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852 110 L----NMKGYFYDFD-SLKGMQKSITQLGDQFNRKAQAKELNDHLNSVKQKIENKAAKQKKhPKVLILMGvpGSYLVATD 184
Cdd:cd01140  89 LkkiaPTIDLGADLKnYLESVKQNIETLGKIFGKEEEAKELVAEIDASIAEAKSAAKGKKK-ALVVLVNG--GKLSAFGP 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852 185 KSYIGDLVKIAGGENVIKVK--DRQYISSNTENLLNINPDIILRLPHGMPEEVKKMFQKEFKQNDIWKHFKAVKNNHVYD 262
Cdd:cd01140 166 GSRFGWLHDLLGFEPADENIkaSSHGQPVSFEYILEANPDWLFVIDRGAAIGAEGSSAKEVLDNDLVKNTTAWKNGKVIY 245

                       250       260
                ....*....|....*....|....*..
gi 81705852 263 LEEVPFGITANVdaDKAMTQLYDLFYK 289
Cdd:cd01140 246 LDPDLWYLSGGG--LESLKQMIDDLKK 270
FepB COG0614
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ...
 35-291 9.35e-50

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


Pssm-ID: 440379 [Multi-domain]  Cd Length: 264  Bit Score: 165.56  E-value: 9.35e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852  35 RIVPTTVALTMTLDKLDLP--IVGKP-TSYKTLP-NRYKDVPEIGQPMEPNVEAVKKLKPTHVL-SVSTIKDEMQPFYKQ 109
Cdd:COG0614   2 RIVSLSPSATELLLALGAGdrLVGVSdWGYCDYPeLELKDLPVVGGTGEPNLEAILALKPDLVLaSSSGNDEEDYEQLEK 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852 110 LNMKGYFYDFDSLKGMQKSITQLGDQFNRKAQAKELNDHLNSVKQKIENKAAKQKKHPKVLILMGVPGSYLVATDKSYIG 189
Cdd:COG0614  82 IGIPVVVLDPRSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGAEERPTVLYEIWSGDPLYTAGGGSFIG 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852 190 DLVKIAGGENVIKVKDRQYISSNTENLLNINPDIILRLPHGMPEEVKKMFQKEFKQNDIWKHFKAVKNNHVYDLEEVpFG 269
Cdd:COG0614 162 ELLELAGGRNVAADLGGGYPEVSLEQVLALDPDVIILSGGGYDAETAEEALEALLADPGWQSLPAVKNGRVYVVPGD-LL 240

                       250       260
                ....*....|....*....|..
gi 81705852 270 ITANVDADKAMTQLYDLFYKDK 291
Cdd:COG0614 241 SRPGPRLLLALEDLAKALHPEL 262
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
 46-263 1.49e-37

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: 132.88  E-value: 1.49e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852    46 TLDKLDL--PIVGKP--TSYKTLPNRYKDVPEIGQPMEPNVEAVKKLKPTHVLSVSTIKDEmqPFYKQL--NMKGYFYDF 119
Cdd:pfam01497  10 ILYALGAtdSIVGVDayTRDPLKADAVAAIVKVGAYGEINVERLAALKPDLVILSTGYLTD--EAEELLslIIPTVIFES 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852   120 DSLK-GMQKSITQLGDQFNRKAQAKELNDHLNSVKQKIENKAAKQKKHPKVLILMGVPGSYLVATDKSYIGDLVKIAGGE 198
Cdd:pfam01497  88 SSTGeSLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPVLVFGGADGGGYVVAGSNTYIGDLLRILGIE 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 81705852   199 NVIKVKDR-QYISSNTENLLNINPDIILRLPHGMpeeVKKMFQKEFKQNDIWKHFKAVKNNHVYDL 263
Cdd:pfam01497 168 NIAAELSGsEYAPISFEAILSSNPDVIIVSGRDS---FTKTGPEFVAANPLWAGLPAVKNGRVYTL 230
FecB COG4594
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ...
 61-291 1.03e-24

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


Pssm-ID: 443650 [Multi-domain]  Cd Length: 316  Bit Score: 100.77  E-value: 1.03e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852  61 YKTLPNRYKDVPEIGQPMEPNVEAVKKLKPTHVLSVstiKDEMQPFYKQLN-------MKGYFYDFdslKGMQKSITQLG 133
Cdd:COG4594  86 VPYLRDLIKGVTSVGTRSQPNLEAIAALKPDLIIAD---KSRHEAIYDQLSkiaptvlFKSRNGDY---QENLESFKTIA 159

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852 134 DQFNRKAQAKE-LNDH---LNSVKQKIENKAAKQKkhpkVLILMGVPGSYLVATDKSYIGDLVKIAGGENVIKVKDRQ-- 207
Cdd:COG4594 160 KALGKEEEAEAvLADHdqrIAEAKAKLAAADKGKK----VAVGQFRADGLRLYTPNSFAGSVLAALGFENPPKQSKDNgy 235

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852 208 -YISSNTENLLNINPDIILRLPHGMPEevkkmFQKEFKQNDIWKHFKAVKNNHVYDLEEV--PFG---ITANVDADkamt 281
Cdd:COG4594 236 gYSEVSLEQLPALDPDVLFIATYDDPS-----ILKEWKNNPLWKNLKAVKNGRVYEVDGDlwTRGrgpLAAELMAD---- 306

                       250
                ....*....|
gi 81705852 282 QLYDLFYKDK 291
Cdd:COG4594 307 DLVEILLKKK 316
YvrC cd01143
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ...
 35-225 1.26e-22

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: 92.34  E-value: 1.26e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852  35 RIVPTTVALTMTLDKLDL--PIVGKpTSYKTLPNRYKDVPEIGQPMEPNVEAVKKLKPTHVLSVSTIKDEMqpfYKQLNM 112
Cdd:cd01143   5 RIVSLSPSITEILFALGAgdKIVGV-DTYSNYPKEVRKKPKVGSYSNPNVEKIVALKPDLVIVSSSSLAEL---LEKLKD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852 113 KG----YFYDFDSLKGMQKSITQLGDQFNRKAQAKELNDHLNSVKQKIEnKAAKQKKHPKVLILMGVPGSYlVATDKSYI 188
Cdd:cd01143  81 AGipvvVLPAASSLDEIYDQIELIGKITGAEEEAEKLVKEMKQKIDKVK-DKGKTIKKSKVYIEVSLGGPY-TAGKNTFI 158

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 81705852 189 GDLVKIAGGENVIKvKDRQYISSNTENLLNINPDIIL 225
Cdd:cd01143 159 NELIRLAGAKNIAA-DSGGWPQVSPEEILKANPDVII 194
TroA_e cd01142
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ...
 35-270 1.13e-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: 1.13e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852  35 RIVPTTVALTMTLDKLDLP--IVGKPTSYKTLPN------RYKDVPEIGQPMEPNVEAVKKLKPTHVLSVSTIKDEMQpf 106
Cdd:cd01142  26 RIAALWGAGNAVVAALGGGklIVATTSTVQQEPWlyrlapSLENVATGGTGNDVNIEELLALKPDVVIVWSTDGKEAG-- 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852 107 YKQLNMKGY-FYDFDSLKGMQKSITQLGDQFNRKAQAKELN----DHLNSVKQKIENKAAKQKkhPKVLILMGVPGSylV 181
Cdd:cd01142 104 KAVLRLLNAlSLRDAELEEVKLTIALLGELLGRQEKAEALVayfdDNLAYVAARTKKLPDSER--PRVYYAGPDPLT--T 179

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852 182 ATDKSYIGDLVKIAGGENVIKVK-DRQYISSNTENLLNINPDIILrLPHGMPEevkkmfqKEFKQNDIWKHFKAVKNNHV 260
Cdd:cd01142 180 DGTGSITNSWIDLAGGINVASEAtKKGSGEVSLEQLLKWNPDVII-VGNADTK-------AAILADPRWQNLRAVKNGRV 251

                       250
                ....*....|
gi 81705852 261 YdleEVPFGI 270
Cdd:cd01142 252 Y---VNPEGA 258
FhuD cd01146
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ...
 35-278 4.89e-20

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: 86.96  E-value: 4.89e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852  35 RIVPTTVALTMTLDKLDLPIVG------KPTSYKTLPNRYKDVPEIGQPMEPNVEAVKKLKPTHVLSVSTIKDEMqpfYK 108
Cdd:cd01146   5 RIVALDWGALETLLALGVKPVGvadtagYKPWIPEPALPLEGVVDVGTRGQPNLEAIAALKPDLILGSASRHDEI---YD 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852 109 QLN-------MKGYFYDFDslkgMQKSITQLGDQFNRKAQAKEL----NDHLNSVKQKIENKAAKqkkhPKVLILMGVPG 177
Cdd:cd01146  82 QLSqiaptvlLDSSPWLAE----WKENLRLIAKALGKEEEAEKLlaeyDQRLAELRQKLPDKGPK----PVSVVRFSDAG 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852 178 SYLVATDKSYIGDLVKIAGGENVIKVK---DRQYISSNTENLLNINPDIILRLPHGMPEevkkmFQKEFKQNDIWKHFKA 254
Cdd:cd01146 154 SIRLYGPNSFAGSVLEDLGLQNPWAQEttnDSGFATISLERLAKADADVLFVFTYEDEE-----LAQALQANPLWQNLPA 228

                       250       260
                ....*....|....*....|....*...
gi 81705852 255 VKNNHVYDLEEVPF----GITANVDADK 278
Cdd:cd01146 229 VKNGRVYVVDDVWWffggGLSAARLLLD 256
BtuF cd01144
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ...
 54-265 3.94e-18

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: 81.58  E-value: 3.94e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852  54 IVGKpTSYKTLPNRYKDVPEIGQPMEPNVEAVKKLKPTHVLSVSTIkdEMQPFYKQLNMKG---YFYDFDSLKGMQKSIT 130
Cdd:cd01144  23 LVGV-TDYCDYPPEAKKLPRVGGFYQLDLERVLALKPDLVIAWDDC--NVCAVVDQLRAAGipvLVSEPQTLDDILADIR 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852 131 QLGDQFNRKAQAKELNdhlNSVKQKIEN--KAAKQKKHPKVLILMGV-PgsyLVATDKSYIGDLVKIAGGENVIKVKDRQ 207
Cdd:cd01144 100 RLGTLAGRPARAEELA---EALRRRLAAlrKQYASKPPPRVFYQEWIdP---LMTAGGDWVPELIALAGGVNVFADAGER 173

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 81705852 208 YISSNTENLLNINPDIILRLPHGmpeevKKMFQKEFKQNDIWKHFKAVKNNHVYDLEE 265
Cdd:cd01144 174 SPQVSWEDVLAANPDVIVLSPCG-----FGFTPAILRKEPAWQALPAVRNGRVYAVDG 226
HemV-2 cd01147
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ...
 35-269 1.13e-17

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: 80.46  E-value: 1.13e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852  35 RIVPT---TVALTMTLDKLDLpIVG---KPTS-----YKTLPNRYKDVPEIGQPM---EPNVEAVKKLKPTHVLSVST-- 98
Cdd:cd01147   7 RVVAAgpgALRLLYALAAPDK-IVGvddAEKSdegrpYFLASPELKDLPVIGRGGrgnTPNYEKIAALKPDVVIDVGSdd 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852  99 ---IKDEMQpfyKQLNMKG-YFYDFDSLKGMQKSITQLGDQFNRKAQAKELNDHLNSVKQKIENKAAKQKKHPKVLILMG 174
Cdd:cd01147  86 ptsIADDLQ---KKTGIPVvVLDGGDSLEDTPEQIRLLGKVLGKEERAEELISFIESILADVEERTKDIPDEEKPTVYFG 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852 175 VPGSY----LVATDKSYIGDLVkIAGGENVIKVKDRQYISS-NTENLLNINPDIILRLPHGMPEEVKKmfqkEFKQNDIW 249
Cdd:cd01147 163 RIGTKgaagLESGLAGSIEVFE-LAGGINVADGLGGGGLKEvSPEQILLWNPDVIFLDTGSFYLSLEG----YAKNRPFW 237

                       250       260
                ....*....|....*....|
gi 81705852 250 KHFKAVKNNHVYDLEEVPFG 269
Cdd:cd01147 238 QSLKAVKNGRVYLLPALPFN 257
TroA_f cd01139
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ...
 67-263 6.00e-17

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: 79.66  E-value: 6.00e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852  67 RYKDVPEIGQPMEP--NVEAVKKLKPTHVLSVSTIKD-----EMQPFYKQLNMKGYFYDF--DSLKGMQKSITQLGDQFN 137
Cdd:cd01139  67 EIADIPLIGSTYNGdfSVEKVLTLKPDLVILNIWAKTtaeesGILEKLEQAGIPVVFVDFrqKPLKNTTPSMRLLGKALG 146

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852 138 RKAQAKELNDHLNSVKQKIENKAAKQK-KHPKVLILMGVPGS--YLVATDKSYIGDLVKIAGGENVIK-VKDRQYISSNT 213
Cdd:cd01139 147 REERAEEFIEFYQERIDRIRDRLAKINePKPKVFIELGAGGPeeCCSTYGNGNWGELVDAAGGDNIADgLIPGTSGELNA 226

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 81705852 214 ENLLNINPDIILR--------------LPHGMPEEVKKMFQKEFKQNDIWKHFKAVKNNHVYDL 263
Cdd:cd01139 227 EYVIAANPEIIIAtggnwakdpsgvslGPDGTTADAKESLLRALLKRPGWSSLQAVKNGRVYAL 290
TroA-like cd00636
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ...
 35-173 1.27e-13

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: 66.81  E-value: 1.27e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852  35 RIVPTTVALTMTLDKLDL--PIVG---KPTSYKTLPNRYKDVPEIGQPMEPNVEAVKKLKPTHVLSVSTIKDEMQPFYKQ 109
Cdd:cd00636   2 RVVALDPGATELLLALGGddKPVGvadPSGYPPEAKALLEKVPDVGHGYEPNLEKIAALKPDLIIANGSGLEAWLDKLSK 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 81705852 110 LNMKGYFYDFD---SLKGMQKSITQLGDQFNRKAQAKELNDHLNSVKQKIENKAAKQKKHPKVLILM 173
Cdd:cd00636  82 IAIPVVVVDEAselSLENIKESIRLIGKALGKEENAEELIAELDARLAELRAKLAKIPKKKVSLVVG 148
FeuA cd01138
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ...
 43-268 6.36e-12

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: 64.28  E-value: 6.36e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852  43 LTMTLDKLDLPIVGKPTSYKTLPNRYKDVP--EIGQPMEPNVEAVKKLKPTHVLSVSTIKDEmqpfYKQLN--MKGYFYD 118
Cdd:cd01138  18 ETEGLALLGIKPVGAASIGGKNPYYKKKTLakVVGIVDEPNLEKVLELKPDLIIVSSKQEEN----YEKLSkiAPTVPVS 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852 119 FDSlKGMQKSITQLGDQFNRKAQAKE-LNDH---LNSVKQKIENKAAKQKKhpkVLILMGVPGSYLVATDKSYIGDLVKI 194
Cdd:cd01138  94 YNS-SDWEEQLKEIGKLLNKEDEAEKwLADYkqkAKEAKEKIKKKLGNDKS---VAVLRGRKQIYVFGEDGRGGGPILYA 169

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852 195 AGG-------ENVIKVKDRQYISSntENLLNINPDIILRLPHGMPEEvkkmfQKEFKQNDIWKHFKAVKNNHVY--DLEE 265
Cdd:cd01138 170 DLGlkapekvKEIEDKPGYAAISL--EVLPEFDADYIFLLFFTGPEA-----KADFESLPIWKNLPAVKNNHVYivDAWV 242


                ...
gi 81705852 266 VPF 268
Cdd:cd01138 243 FYF 245
TroA_a cd01148
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ...
 35-276 5.35e-11

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: 61.97  E-value: 5.35e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852  35 RIVPTTVALTMTLDKLDLP--IVGKPTSYK----TLPNRYKDVPEIGqPMEPNVEAVKKLKP-------------THVLS 95
Cdd:cd01148  20 RVVSNDQNTTEMMLALGLQdrMVGTAGIDNkdlpELKAKYDKVPELA-KKYPSKETVLAARPdlvfggwsygfdkGGLGT 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852  96 VSTIKDEMQPFYKQLNMKGYFYDFDSLKGMQKSITQLGDQFNRKAQAKELNDHLNSVKQKIENKAAKQKKHPKVLIlmgv 175
Cdd:cd01148  99 PDSLAELGIKTYILPESCGQRRGEATLDDVYNDIRNLGKIFDVEDRADKLVADLKARLAEISAKVKGDGKKVAVFV---- 174

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852 176 pgsYLVATDKSYI-------GDLVKIAGGENVIKVKDRQYISSNTENLLNINPDIILRLPHGMPEEVKKMfQKEFKQNDI 248
Cdd:cd01148 175 ---YDSGEDKPFTsgrggipNAIITAAGGRNVFADVDESWTTVSWETVIARNPDVIVIIDYGDQNAAEQK-IKFLKENPA 250

                       250       260       270
                ....*....|....*....|....*....|
gi 81705852 249 WKHFKAVKNNH--VYDLEEVPFGItANVDA 276
Cdd:cd01148 251 LKNVPAVKNNRfiVLPLAEATPGI-RNVDA 279
HutB cd01149
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ...
 35-225 7.88e-11

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: 60.74  E-value: 7.88e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852  35 RIVPTTVALTMTLDKLDLP--IVGKPTSyKTLPNRYKDVPEIGQPMEPNVEAVKKLKPTHVLSVstikDEMQP--FYKQL 110
Cdd:cd01149   3 RIVSLGGSVTEIVYALGAGdrLVGVDST-STYPEAAAKLPDVGYMRQLSAEGVLSLKPTLVIAS----DEAGPpeALDQL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852 111 NMKG----YFYDFDSLKGMQKSITQLGDQFNRKAQAKELndhLNSVKQKIE---NKAAKQKKHPKVLILMGVPGSYLVAT 183
Cdd:cd01149  78 RAAGvpvvTVPSTPTLDGLLTKIRQVAQALGVPEKGEAL---AQEVRQRLAalrKTVAAHKKPPRVLFLLSHGGGAAMAA 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 81705852 184 DKSYIGD-LVKIAGGENVIKvKDRQYISSNTENLLNINPDIIL 225
Cdd:cd01149 155 GRNTAADaIIALAGAVNAAA-GFRGYKPLSAEALIAAQPDVIL 196
btuF PRK09534
corrinoid ABC transporter substrate-binding protein; Reviewed
 75-225 3.76e-09

corrinoid ABC transporter substrate-binding protein; Reviewed


Pssm-ID: 236552 [Multi-domain]  Cd Length: 359  Bit Score: 56.84  E-value: 3.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852   75 GQPMEPNVEAVKKLKPTHVLSVSTIKDEMQPFYKQLNMKGYFYDF-DSLKGMQKSITQLGDQFNRKAQAKELNDHLNSVK 153
Cdd:PRK09534 105 GQPFGVNVEAVVGLDPDLVLAPNAVAGDTVTRLREAGITVFHFPAaTSIEDVAEKTATIGRLTGNCEAAAETNAEMRDRV 184

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 81705852  154 QKIENKAAKQKKHPKVLILMGvpGSYlVATDKSYIGDLVKIAGGENVIKVKD-RQYISSNTENLLNINPDIIL 225
Cdd:PRK09534 185 DAVEDRTADVDDRPRVLYPLG--DGY-TAGGNTFIGALIEAAGGHNVAADATtDGYPQLSEEVIVQQDPDVIV 254
TroA_d cd01141
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ...
 35-197 4.80e-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: 54.73  E-value: 4.80e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852  35 RIV---PTTVALTMTLDKLDlPIVGKPTSYKTLPN---RYKDVPEIGQPMEPNVEAVKKLKPTHV-LSVSTIKDEMQPFY 107
Cdd:cd01141  10 RIVvlsPTHVDLLLALDKAD-KIVGVSASAYDLNTpavKERIDIQVGPTGSLNVELIVALKPDLViLYGGFQAQTILDKL 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852 108 KQLNMK-GYFYDFDSLKGMQKSITQLGDQFNRKAQAK--ELNDHLNSVKQKIENKAAKQKKhPKVLILMGVPGSYLVATD 184
Cdd:cd01141  89 EQLGIPvLYVNEYPSPLGRAEWIKFAAAFYGVGKEDKadEAFAQIAGRYRDLAKKVSNLNK-PTVAIGKPVKGLWYMPGG 167

                       170
                ....*....|...
gi 81705852 185 KSYIGDLVKIAGG 197
Cdd:cd01141 168 NSYVAKMLRDAGG 180
PRK10957 PRK10957
iron-enterobactin transporter periplasmic binding protein; Provisional
 35-263 2.23e-05

iron-enterobactin transporter periplasmic binding protein; Provisional


Pssm-ID: 236806 [Multi-domain]  Cd Length: 317  Bit Score: 45.35  E-value: 2.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852   35 RIVPTTVALTMTLDKLDLPIVGkptSYKTLPN-----------RYKDVPE--------IGqpmEPNVEAVKKLKPTHVLS 95
Cdd:PRK10957  46 RIVSTSVTLTGTLLAIDAPVIA---SGATTPNtrvaddqgffrQWSDVAKergvevlyIG---EPDAEAVAAQMPDLIVI 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852   96 VSTIKDEMQPFYKQLNMKG--YFYDFDSlKGMQKSITQLGDQFNRKAQA----KELNDHLNSVKQKIenKAAKQKKhpKV 169
Cdd:PRK10957 120 SATGGDSALALYDQLSAIAptLVIDYDD-KSWQELATQLGEATGLEKQAaaviAQFDAQLAEVKAKI--TLPPQPV--SA 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852  170 LILMGVPGSYLVATDKSYIGDLVK------------IAGGENVIKVKDRQYISSntENLL-NINPDIILRLPhGMPEEVK 236
Cdd:PRK10957 195 LVYNGAGHSANLWTPESAQGQLLEqlgftlaelpagLQASTSQGKRHDIIQLGG--ENLAaGLNGETLFLFA-GDDKDAD 271

                        250       260
                 ....*....|....*....|....*..
gi 81705852  237 KmfqkeFKQNDIWKHFKAVKNNHVYDL 263
Cdd:PRK10957 272 A-----FLADPLLANLPAVQNKQVYAL 293
fecB PRK11411
iron-dicitrate transporter substrate-binding subunit; Provisional
 65-277 1.65e-04

iron-dicitrate transporter substrate-binding subunit; Provisional


Pssm-ID: 183123 [Multi-domain]  Cd Length: 303  Bit Score: 42.35  E-value: 1.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852   65 PNR-YKDVPEIGQPME-------PNVEAVKKLKPTHVLSVS----TIKDEMQPFYKQLNMK--GYFYDfDSLKGMQKsit 130
Cdd:PRK11411  69 AKRiLPEVRAHLKPWQsvgtrsqPSLEAIAALKPDLIIADSsrhaGVYIALQKIAPTLLLKsrNETYQ-ENLQSAAI--- 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81705852  131 qLGDQFNRKAQAK-ELNDHlnsvKQKIENKAAKQKKHPKVLILMGVPGSYLVATDKSYIGDLVKIAGGENVIKVKDRQ-Y 208
Cdd:PRK11411 145 -IGEVLGKKREMQaRIEQH----KERMAQFASQLPKGTRVAFGTSREQQFNLHSPESYTGSVLAALGLNVPKAPMNGAaM 219

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 81705852  209 ISSNTENLLNINPDIILRLPHGMPEEVKKmfqkeFKQNDIWKHFKAVKNNHVydleevpfgitANVDAD 277
Cdd:PRK11411 220 PSISLEQLLALNPDWLLVAHYRQESIVKR-----WQQDPLWQMLTAAKKQQV-----------ASVDSN 272
 
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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