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Conserved domains on  [gi|167709920|gb|EDS20499|]
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heme ABC transporter, heme-binding protein isdE [Clostridium sp. SS2/1]

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 ...
 19-336 2.53e-153

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: 432.08  E-value: 2.53e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920   19 IFLILLLAISSCFLTGCVNQhpkdskkisqgesvetmleitdpKEKQAVLNAKAKvkalsgNPRIVATSPAVADICDKLD 98
Cdd:TIGR03659   3 ILSLVLLAVLSLGLTGCSSS-----------------------KEKSKVSNKKSK------EERIVATSVAVTEILDKLD 53

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920   99 LDLVGVPKSSvSKIPSRYKKVKKVGLAMSPDMEIVSSLNPDWILAPSSLETDLKPKFEELkNTEYAFLNLRSVQGMYRSV 178
Cdd:TIGR03659  54 LDLVGVPTSQ-KTLPKRYKDVPEVGNPMSPDMEKIKSLKPTVVLSVTTLEEDLGPKFKQL-GVEATFLNLTSVDGMKKSI 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920  179 QELGEIFGKQQEAEKMTKEFTTFYKSYTKRNKNKKHPKVLVLIGLPGSYVIATENSYVGSLVKLAGGENVYQNADKEFLT 258
Cdd:TIGR03659 132 TELGEKYGREEQAEKLVKEINEKEAEVKKKVKGKKKPKVLILMGVPGSYLVATENSYIGDLVKLAGGENVYKGNKQEYLS 211

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167709920  259 VNTEDMKKKEPDIIVRAAHALPDQVTKMFNEDFETNDIWKHFDAVKNKRVYDLTYEYFGMSANFKYKKALSELEKDFY 336
Cdd:TIGR03659 212 SNTEYLLKANPDIILRAAHGMPDEVKKMFDEEFKTNDIWKHFEAVKNNRVYDLDEELFGMTANLKVAEALDELKKILY 289
 
Name Accession Description Interval E-value
IsdE TIGR03659
heme ABC transporter, heme-binding protein isdE; This family of ABC substrate-binding proteins ...
 19-336 2.53e-153

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: 432.08  E-value: 2.53e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920   19 IFLILLLAISSCFLTGCVNQhpkdskkisqgesvetmleitdpKEKQAVLNAKAKvkalsgNPRIVATSPAVADICDKLD 98
Cdd:TIGR03659   3 ILSLVLLAVLSLGLTGCSSS-----------------------KEKSKVSNKKSK------EERIVATSVAVTEILDKLD 53

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920   99 LDLVGVPKSSvSKIPSRYKKVKKVGLAMSPDMEIVSSLNPDWILAPSSLETDLKPKFEELkNTEYAFLNLRSVQGMYRSV 178
Cdd:TIGR03659  54 LDLVGVPTSQ-KTLPKRYKDVPEVGNPMSPDMEKIKSLKPTVVLSVTTLEEDLGPKFKQL-GVEATFLNLTSVDGMKKSI 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920  179 QELGEIFGKQQEAEKMTKEFTTFYKSYTKRNKNKKHPKVLVLIGLPGSYVIATENSYVGSLVKLAGGENVYQNADKEFLT 258
Cdd:TIGR03659 132 TELGEKYGREEQAEKLVKEINEKEAEVKKKVKGKKKPKVLILMGVPGSYLVATENSYIGDLVKLAGGENVYKGNKQEYLS 211

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167709920  259 VNTEDMKKKEPDIIVRAAHALPDQVTKMFNEDFETNDIWKHFDAVKNKRVYDLTYEYFGMSANFKYKKALSELEKDFY 336
Cdd:TIGR03659 212 SNTEYLLKANPDIILRAAHGMPDEVKKMFDEEFKTNDIWKHFEAVKNNRVYDLDEELFGMTANLKVAEALDELKKILY 289
FatB cd01140
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ...
 69-336 2.75e-63

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: 202.49  E-value: 2.75e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920  69 NAKAKVKALSGNPRIVATSPAVADICDKLDLDLVGVPKSSvsKIPSRYKKVKK-----VGLAMSPDMEIVSSLNPDWILA 143
Cdd:cd01140    1 HALGETKVPKNPEKVVVFDVGALDTLDALGVKVVGVPKSS--TLPEYLKKYKDdkyanVGTLFEPDLEAIAALKPDLIII 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920 144 PSSLETDLKPKFEELkNTEYAFLNLR-SVQGMYRSVQELGEIFGKQQEAEKMTKEFTTFYKSYTKRNKNKKhpKVLVLIG 222
Cdd:cd01140   79 GGRLAEKYDELKKIA-PTIDLGADLKnYLESVKQNIETLGKIFGKEEEAKELVAEIDASIAEAKSAAKGKK--KALVVLV 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920 223 LPGSYVIATENSYVGSLVKLAGGENVYQN--ADKEFLTVNTEDMKKKEPDIIVRAAHALPDQVTKMFNEDFETNDIWKHF 300
Cdd:cd01140  156 NGGKLSAFGPGSRFGWLHDLLGFEPADENikASSHGQPVSFEYILEANPDWLFVIDRGAAIGAEGSSAKEVLDNDLVKNT 235

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 167709920 301 DAVKNKRVYDLTYEYFGMSANFkyKKALSELEKDFY 336
Cdd:cd01140  236 TAWKNGKVIYLDPDLWYLSGGG--LESLKQMIDDLK 269
FepB COG0614
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ...
 82-317 1.57e-48

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


Pssm-ID: 440379 [Multi-domain]  Cd Length: 264  Bit Score: 164.02  E-value: 1.57e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920  82 RIVATSPAVADICDKLDLD--LVGVPKSSVSKIPS-RYKKVKKVGLAMSPDMEIVSSLNPDWILAPSS-LETDLKPKFEE 157
Cdd:COG0614    2 RIVSLSPSATELLLALGAGdrLVGVSDWGYCDYPElELKDLPVVGGTGEPNLEAILALKPDLVLASSSgNDEEDYEQLEK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920 158 LkNTEYAFLNLRSVQGMYRSVQELGEIFGKQQEAEKMTKEFTTFYKSYTKRNKN-KKHPKVLVLIGLPGSYVIATENSYV 236
Cdd:COG0614   82 I-GIPVVVLDPRSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGaEERPTVLYEIWSGDPLYTAGGGSFI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920 237 GSLVKLAGGENVYQNADKEFLTVNTEDMKKKEPDIIVRAAHALPDQVTKMFNEDFETNDIWKHFDAVKNKRVYDLTYEYF 316
Cdd:COG0614  161 GELLELAGGRNVAADLGGGYPEVSLEQVLALDPDVIILSGGGYDAETAEEALEALLADPGWQSLPAVKNGRVYVVPGDLL 240


                 .
gi 167709920 317 G 317
Cdd:COG0614  241 S 241
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
 84-311 1.32e-38

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: 137.11  E-value: 1.32e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920   84 VATSPAVADICDKLDLDLVGVPKSSVSKIPSRYKK---VKKVGLAMSPDMEIVSSLNPDWILAPSSLETDLKPKFEELKN 160
Cdd:pfam01497   1 AALSPAYTEILYALGATDSIVGVDAYTRDPLKADAvaaIVKVGAYGEINVERLAALKPDLVILSTGYLTDEAEELLSLII 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920  161 TEYAFLNLRSVQGMYRSVQELGEIFGKQQEAEKMTKEFTTFYKSYTKRNKNKKHPKVLVLIGLP-GSYVIATENSYVGSL 239
Cdd:pfam01497  81 PTVIFESSSTGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPVLVFGGADgGGYVVAGSNTYIGDL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 167709920  240 VKLAGGENVYQNADK-EFLTVNTEDMKKKEPDIIVRAAHALpdqVTKMFNEDFETNDIWKHFDAVKNKRVYDL 311
Cdd:pfam01497 161 LRILGIENIAAELSGsEYAPISFEAILSSNPDVIIVSGRDS---FTKTGPEFVAANPLWAGLPAVKNGRVYTL 230
fecB PRK11411
iron-dicitrate transporter substrate-binding subunit; Provisional
 82-308 2.66e-06

iron-dicitrate transporter substrate-binding subunit; Provisional


Pssm-ID: 183123 [Multi-domain]  Cd Length: 303  Bit Score: 48.52  E-value: 2.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920  82 RIVATSPAVADICDKLDLDLVGV-----PKSSVSKIPSRYKKVKKVGLAMSPDMEIVSSLNPDWILAPSSLETDLkpkFE 156
Cdd:PRK11411  41 RIVVLELSFVDALAAVGVSPVGVaddndAKRILPEVRAHLKPWQSVGTRSQPSLEAIAALKPDLIIADSSRHAGV---YI 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920 157 ELKntEYA---FLNLR--SVQGMYRSVQELGEIFGKQQEAEKMTKEFTTFYKSYTKR-NKNKKhpkvlVLIGLP--GSYV 228
Cdd:PRK11411 118 ALQ--KIAptlLLKSRneTYQENLQSAAIIGEVLGKKREMQARIEQHKERMAQFASQlPKGTR-----VAFGTSreQQFN 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920 229 IATENSYVGSLVKlAGGENV--YQNADKEFLTVNTEDMKKKEPDIIVRAAHALPDQVtkmfnEDFETNDIWKHFDAVKNK 306
Cdd:PRK11411 191 LHSPESYTGSVLA-ALGLNVpkAPMNGAAMPSISLEQLLALNPDWLLVAHYRQESIV-----KRWQQDPLWQMLTAAKKQ 264


                 ..
gi 167709920 307 RV 308
Cdd:PRK11411 265 QV 266
 
Name Accession Description Interval E-value
IsdE TIGR03659
heme ABC transporter, heme-binding protein isdE; This family of ABC substrate-binding proteins ...
 19-336 2.53e-153

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: 432.08  E-value: 2.53e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920   19 IFLILLLAISSCFLTGCVNQhpkdskkisqgesvetmleitdpKEKQAVLNAKAKvkalsgNPRIVATSPAVADICDKLD 98
Cdd:TIGR03659   3 ILSLVLLAVLSLGLTGCSSS-----------------------KEKSKVSNKKSK------EERIVATSVAVTEILDKLD 53

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920   99 LDLVGVPKSSvSKIPSRYKKVKKVGLAMSPDMEIVSSLNPDWILAPSSLETDLKPKFEELkNTEYAFLNLRSVQGMYRSV 178
Cdd:TIGR03659  54 LDLVGVPTSQ-KTLPKRYKDVPEVGNPMSPDMEKIKSLKPTVVLSVTTLEEDLGPKFKQL-GVEATFLNLTSVDGMKKSI 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920  179 QELGEIFGKQQEAEKMTKEFTTFYKSYTKRNKNKKHPKVLVLIGLPGSYVIATENSYVGSLVKLAGGENVYQNADKEFLT 258
Cdd:TIGR03659 132 TELGEKYGREEQAEKLVKEINEKEAEVKKKVKGKKKPKVLILMGVPGSYLVATENSYIGDLVKLAGGENVYKGNKQEYLS 211

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167709920  259 VNTEDMKKKEPDIIVRAAHALPDQVTKMFNEDFETNDIWKHFDAVKNKRVYDLTYEYFGMSANFKYKKALSELEKDFY 336
Cdd:TIGR03659 212 SNTEYLLKANPDIILRAAHGMPDEVKKMFDEEFKTNDIWKHFEAVKNNRVYDLDEELFGMTANLKVAEALDELKKILY 289
FatB cd01140
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ...
 69-336 2.75e-63

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: 202.49  E-value: 2.75e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920  69 NAKAKVKALSGNPRIVATSPAVADICDKLDLDLVGVPKSSvsKIPSRYKKVKK-----VGLAMSPDMEIVSSLNPDWILA 143
Cdd:cd01140    1 HALGETKVPKNPEKVVVFDVGALDTLDALGVKVVGVPKSS--TLPEYLKKYKDdkyanVGTLFEPDLEAIAALKPDLIII 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920 144 PSSLETDLKPKFEELkNTEYAFLNLR-SVQGMYRSVQELGEIFGKQQEAEKMTKEFTTFYKSYTKRNKNKKhpKVLVLIG 222
Cdd:cd01140   79 GGRLAEKYDELKKIA-PTIDLGADLKnYLESVKQNIETLGKIFGKEEEAKELVAEIDASIAEAKSAAKGKK--KALVVLV 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920 223 LPGSYVIATENSYVGSLVKLAGGENVYQN--ADKEFLTVNTEDMKKKEPDIIVRAAHALPDQVTKMFNEDFETNDIWKHF 300
Cdd:cd01140  156 NGGKLSAFGPGSRFGWLHDLLGFEPADENikASSHGQPVSFEYILEANPDWLFVIDRGAAIGAEGSSAKEVLDNDLVKNT 235

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 167709920 301 DAVKNKRVYDLTYEYFGMSANFkyKKALSELEKDFY 336
Cdd:cd01140  236 TAWKNGKVIYLDPDLWYLSGGG--LESLKQMIDDLK 269
FepB COG0614
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ...
 82-317 1.57e-48

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


Pssm-ID: 440379 [Multi-domain]  Cd Length: 264  Bit Score: 164.02  E-value: 1.57e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920  82 RIVATSPAVADICDKLDLD--LVGVPKSSVSKIPS-RYKKVKKVGLAMSPDMEIVSSLNPDWILAPSS-LETDLKPKFEE 157
Cdd:COG0614    2 RIVSLSPSATELLLALGAGdrLVGVSDWGYCDYPElELKDLPVVGGTGEPNLEAILALKPDLVLASSSgNDEEDYEQLEK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920 158 LkNTEYAFLNLRSVQGMYRSVQELGEIFGKQQEAEKMTKEFTTFYKSYTKRNKN-KKHPKVLVLIGLPGSYVIATENSYV 236
Cdd:COG0614   82 I-GIPVVVLDPRSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGaEERPTVLYEIWSGDPLYTAGGGSFI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920 237 GSLVKLAGGENVYQNADKEFLTVNTEDMKKKEPDIIVRAAHALPDQVTKMFNEDFETNDIWKHFDAVKNKRVYDLTYEYF 316
Cdd:COG0614  161 GELLELAGGRNVAADLGGGYPEVSLEQVLALDPDVIILSGGGYDAETAEEALEALLADPGWQSLPAVKNGRVYVVPGDLL 240


                 .
gi 167709920 317 G 317
Cdd:COG0614  241 S 241
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
 84-311 1.32e-38

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: 137.11  E-value: 1.32e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920   84 VATSPAVADICDKLDLDLVGVPKSSVSKIPSRYKK---VKKVGLAMSPDMEIVSSLNPDWILAPSSLETDLKPKFEELKN 160
Cdd:pfam01497   1 AALSPAYTEILYALGATDSIVGVDAYTRDPLKADAvaaIVKVGAYGEINVERLAALKPDLVILSTGYLTDEAEELLSLII 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920  161 TEYAFLNLRSVQGMYRSVQELGEIFGKQQEAEKMTKEFTTFYKSYTKRNKNKKHPKVLVLIGLP-GSYVIATENSYVGSL 239
Cdd:pfam01497  81 PTVIFESSSTGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPVLVFGGADgGGYVVAGSNTYIGDL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 167709920  240 VKLAGGENVYQNADK-EFLTVNTEDMKKKEPDIIVRAAHALpdqVTKMFNEDFETNDIWKHFDAVKNKRVYDL 311
Cdd:pfam01497 161 LRILGIENIAAELSGsEYAPISFEAILSSNPDVIIVSGRDS---FTKTGPEFVAANPLWAGLPAVKNGRVYTL 230
FhuD cd01146
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ...
 79-321 1.53e-28

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: 111.22  E-value: 1.53e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920  79 GNP-RIVATSPAVADICDKLDLDLVGVP-----KSSVSKIPSRYKKVKKVGLAMSPDMEIVSSLNPDWILAPSSLETDLK 152
Cdd:cd01146    1 AKPqRIVALDWGALETLLALGVKPVGVAdtagyKPWIPEPALPLEGVVDVGTRGQPNLEAIAALKPDLILGSASRHDEIY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920 153 PKFEELKNTeyAFLNLRS-VQGMYRSVQELGEIFGKQQEAEKMTKEFTTFYKSYTKRNKNKKHPKVLVL-IGLPGSYVIA 230
Cdd:cd01146   81 DQLSQIAPT--VLLDSSPwLAEWKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKLPDKGPKPVSVVrFSDAGSIRLY 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920 231 TENSYVGSLVKLAG---GENVYQNADKEFLTVNTEDMKKKEPDIIVrAAHALPDQVTKMfnedFETNDIWKHFDAVKNKR 307
Cdd:cd01146  159 GPNSFAGSVLEDLGlqnPWAQETTNDSGFATISLERLAKADADVLF-VFTYEDEELAQA----LQANPLWQNLPAVKNGR 233

                        250
                 ....*....|....*...
gi 167709920 308 VYDLTYEYF----GMSAN 321
Cdd:cd01146  234 VYVVDDVWWffggGLSAA 251
YvrC cd01143
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ...
 82-273 4.99e-27

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: 105.44  E-value: 4.99e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920  82 RIVATSPAVADICDKLDL--DLVGVpkSSVSKIPSRYKKVKKVGLAMSPDMEIVSSLNPDWILAPSSLETDLKPKFEELK 159
Cdd:cd01143    5 RIVSLSPSITEILFALGAgdKIVGV--DTYSNYPKEVRKKPKVGSYSNPNVEKIVALKPDLVIVSSSSLAELLEKLKDAG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920 160 NTEYAFLNLRSVQGMYRSVQELGEIFGKQQEAEKMTKEFTTFYKSYTKRNKNKKHPKVLVLIGLPGSYViATENSYVGSL 239
Cdd:cd01143   83 IPVVVLPAASSLDEIYDQIELIGKITGAEEEAEKLVKEMKQKIDKVKDKGKTIKKSKVYIEVSLGGPYT-AGKNTFINEL 161

                        170       180       190
                 ....*....|....*....|....*....|....
gi 167709920 240 VKLAGGENVYQNAdKEFLTVNTEDMKKKEPDIIV 273
Cdd:cd01143  162 IRLAGAKNIAADS-GGWPQVSPEEILKANPDVII 194
FecB COG4594
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ...
 18-311 6.30e-26

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


Pssm-ID: 443650 [Multi-domain]  Cd Length: 316  Bit Score: 105.39  E-value: 6.30e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920  18 SIFLILLLAISSCFLTGCVNQHPKDSKKISQGESVEtmleITDpkekqavlnAKAKVKaLSGNP-RIVATSPAVADICDK 96
Cdd:COG4594    3 KLLLLLILLLALLLLAACGSSSSDSSSSEAAAGART----VKH---------AMGETT-IPGTPkRVVVLEWSFADALLA 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920  97 LDLDLVGV-----PKSSVSKIPSRYKKVKKVGLAMSPDMEIVSSLNPDWILAPSSLETDLKPKFEELKNTeyAFLNLRSV 171
Cdd:COG4594   69 LGVTPVGIaddndYDRWVPYLRDLIKGVTSVGTRSQPNLEAIAALKPDLIIADKSRHEAIYDQLSKIAPT--VLFKSRNG 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920 172 --QGMYRSVQELGEIFGKQQEAEKMTKEFTTFYKSYTKRNKNKKHP-KVLVLIGLPGSYVIATENSYVGSLVKLAGGENV 248
Cdd:COG4594  147 dyQENLESFKTIAKALGKEEEAEAVLADHDQRIAEAKAKLAAADKGkKVAVGQFRADGLRLYTPNSFAGSVLAALGFENP 226

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 167709920 249 YQNADKE---FLTVNTEDMKKKEPDIIVRAAHALPDQVTKMFNedfetNDIWKHFDAVKNKRVYDL 311
Cdd:COG4594  227 PKQSKDNgygYSEVSLEQLPALDPDVLFIATYDDPSILKEWKN-----NPLWKNLKAVKNGRVYEV 287
BtuF cd01144
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ...
 82-311 9.14e-24

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: 98.14  E-value: 9.14e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920  82 RIVATSPAVADICDKLDLD--LVGVpkSSVSKIPSRYKKVKKVGLAMSPDMEIVSSLNPDWILAPSSLETDLKPKFEELK 159
Cdd:cd01144    2 RIVSLAPSATELLYALGLGdqLVGV--TDYCDYPPEAKKLPRVGGFYQLDLERVLALKPDLVIAWDDCNVCAVVDQLRAA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920 160 NTEYAFLNLRSVQGMYRSVQELGEIFGKQQEAEKMTKEFTTFYKSYTKRNKNKKHPKVLVLIGL-PgsyVIATENSYVGS 238
Cdd:cd01144   80 GIPVLVSEPQTLDDILADIRRLGTLAGRPARAEELAEALRRRLAALRKQYASKPPPRVFYQEWIdP---LMTAGGDWVPE 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 167709920 239 LVKLAGGENVYQNADKEFLTVNTEDMKKKEPDIIVraahaLPDQVTKMFNEDFETNDIWKHFDAVKNKRVYDL 311
Cdd:cd01144  157 LIALAGGVNVFADAGERSPQVSWEDVLAANPDVIV-----LSPCGFGFTPAILRKEPAWQALPAVRNGRVYAV 224
CeuA COG4607
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and ...
 18-313 1.22e-21

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


Pssm-ID: 443657 [Multi-domain]  Cd Length: 310  Bit Score: 93.32  E-value: 1.22e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920  18 SIFLILLLAISSCFLTGCVNqhpkDSKKISQGESVETMlEITDPKEKQAVlnakakvkalSGNP-RIVATSPAVADICDK 96
Cdd:COG4607    3 KTLLAALALAAALALAACGS----SSAAAASAAAAETV-TVEHALGTVEV----------PKNPkRVVVFDNGALDTLDA 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920  97 LDLDLVGVPKSSVSKIPSRYK--KVKKVGLAMSPDMEIVSSLNPDWILApSSLETDlkpKFEELKntEYA---FLNLRS- 170
Cdd:COG4607   68 LGVEVAGVPKGLLPDYLSKYAddKYANVGTLFEPDLEAIAALKPDLIII-GGRSAK---KYDELS--KIAptiDLTVDGe 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920 171 --VQGMYRSVQELGEIFGKQQEAEKMTKEFTTFYKSYTKRNKNKKhpKVLVLIGLPGSYVIATENSYVGSLVKLAGgenv 248
Cdd:COG4607  142 dyLESLKRNTETLGEIFGKEDEAEELVADLDAKIAALKAAAAGKG--TALIVLTNGGKISAYGPGSRFGPIHDVLG---- 215

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167709920 249 YQNADkEFLTVNT-------EDMKKKEPDIIV---RAAHALPDQVTkmfNEDFETNDIWKHFDAVKNKRVY----DLTY 313
Cdd:COG4607  216 FKPAD-EDIEASThgqaisfEFIAEANPDWLFvidRDAAIGGEGPA---AKQVLDNELVKQTTAWKNGQIVyldpDAWY 290
TroA_e cd01142
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ...
 57-309 1.63e-20

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


Pssm-ID: 238562 [Multi-domain]  Cd Length: 289  Bit Score: 90.11  E-value: 1.63e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920  57 EITDPKEKQAVLNAKAKvkalsgnpRIVATSPAVADICDKLDLD--LVGVPKSSVS-----KIPSRYKKVKKVGLAMSPD 129
Cdd:cd01142    9 TITDMAGRKVTIPDEVK--------RIAALWGAGNAVVAALGGGklIVATTSTVQQepwlyRLAPSLENVATGGTGNDVN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920 130 MEIVSSLNPDWILAPSSLETDLKPKFEELKNTEYA-FLNLRSVQgmyRSVQELGEIFGKQQEAEKMTKEFTT---FYKSY 205
Cdd:cd01142   81 IEELLALKPDVVIVWSTDGKEAGKAVLRLLNALSLrDAELEEVK---LTIALLGELLGRQEKAEALVAYFDDnlaYVAAR 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920 206 TKRNKNKKHPKVLVLIGLPGSYviATENSYVGSLVKLAGGENVYQNA-DKEFLTVNTEDMKKKEPDIIVrAAHALPDqvt 284
Cdd:cd01142  158 TKKLPDSERPRVYYAGPDPLTT--DGTGSITNSWIDLAGGINVASEAtKKGSGEVSLEQLLKWNPDVII-VGNADTK--- 231

                        250       260
                 ....*....|....*....|....*
gi 167709920 285 kmfnEDFETNDIWKHFDAVKNKRVY 309
Cdd:cd01142  232 ----AAILADPRWQNLRAVKNGRVY 252
ChuT COG4558
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ...
 81-311 1.44e-18

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


Pssm-ID: 443619 [Multi-domain]  Cd Length: 285  Bit Score: 84.47  E-value: 1.44e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920  81 PRIVATSPAVADICDKLDL--DLVGVPKSSVskIPSRYKKVKKVGLAMSPDMEIVSSLNPDWILApssLETDLKPK-FEE 157
Cdd:COG4558   28 ERIVSLGGSVTEIVYALGAgdRLVGVDTTST--YPAAAKALPDVGYMRQLSAEGILSLKPTLVLA---SEGAGPPEvLDQ 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920 158 LKNTEYAFLNL---RSVQGMYRSVQELGEIFGKQQEAEKMTKEFTT-FYKSYTKRNKNKKHPKVLVLIGL-PGSYVIATE 232
Cdd:COG4558  103 LRAAGVPVVVVpaaPSLEGVLAKIRAVAAALGVPEAGEALAARLEAdLAALAARVAAIGKPPRVLFLLSRgGGRPMVAGR 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920 233 NSYVGSLVKLAGGENVYQNAdKEFLTVNTEDMKKKEPDIIVraahalpdqvtkMFNEDFET----NDIWKH-----FDAV 303
Cdd:COG4558  183 GTAADALIRLAGGVNAAAGF-EGYKPLSAEALIAAAPDVIL------------VMTRGLESlggvDGLLALpglaqTPAG 249


                 ....*...
gi 167709920 304 KNKRVYDL 311
Cdd:COG4558  250 KNKRIVAM 257
TroA-like cd00636
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ...
 81-222 5.14e-18

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: 79.53  E-value: 5.14e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920  81 PRIVATSPAVADICDKLDLD--LVGVPKSSVSKIPSRYK--KVKKVGLAMSPDMEIVSSLNPDWILAPSSLETDLKPKFE 156
Cdd:cd00636    1 KRVVALDPGATELLLALGGDdkPVGVADPSGYPPEAKALleKVPDVGHGYEPNLEKIAALKPDLIIANGSGLEAWLDKLS 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167709920 157 ELKNT--EYAFLNLRSVQGMYRSVQELGEIFGKQQEAEKMTKEFTTFYKSYTKRNKNKKHPKVLVLIG 222
Cdd:cd00636   81 KIAIPvvVVDEASELSLENIKESIRLIGKALGKEENAEELIAELDARLAELRAKLAKIPKKKVSLVVG 148
HemV-2 cd01147
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ...
 82-317 2.12e-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: 80.84  E-value: 2.12e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920  82 RIVATSP-------AVADIcDKLdldlVGVPKSSVSKIPSRYKK----------VKKVGLAMSPDMEIVSSLNPDWILAP 144
Cdd:cd01147    7 RVVAAGPgalrllyALAAP-DKI----VGVDDAEKSDEGRPYFLaspelkdlpvIGRGGRGNTPNYEKIAALKPDVVIDV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920 145 SSLETDLKPkfEELKN-TEYAFLNLR---SVQGMYRSVQELGEIFGKQQEAEKMTKEFTTFYKSYTKRNKN-KKHPKVLV 219
Cdd:cd01147   82 GSDDPTSIA--DDLQKkTGIPVVVLDggdSLEDTPEQIRLLGKVLGKEERAEELISFIESILADVEERTKDiPDEEKPTV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920 220 LIGLPGSYVIA----TENSYVGSLVkLAGGENVYQNAD-KEFLTVNTEDMKKKEPDIIVRAAHALPDQVTkmfnEDFETN 294
Cdd:cd01147  160 YFGRIGTKGAAglesGLAGSIEVFE-LAGGINVADGLGgGGLKEVSPEQILLWNPDVIFLDTGSFYLSLE----GYAKNR 234

                        250       260
                 ....*....|....*....|...
gi 167709920 295 DIWKHFDAVKNKRVYDLTYEYFG 317
Cdd:cd01147  235 PFWQSLKAVKNGRVYLLPALPFN 257
TroA_a cd01148
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ...
 82-315 2.49e-14

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


Pssm-ID: 238568 [Multi-domain]  Cd Length: 284  Bit Score: 72.37  E-value: 2.49e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920  82 RIVATSPAVADICDKLDLD--LVGVPKSSVSKIPSRYKKVKKVG-LAMS-PDMEIVSSLNPDWILA-------------P 144
Cdd:cd01148   20 RVVSNDQNTTEMMLALGLQdrMVGTAGIDNKDLPELKAKYDKVPeLAKKyPSKETVLAARPDLVFGgwsygfdkgglgtP 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920 145 SSLEtDLKPKFEELKNTEYAFLNLRSVQGMYRSVQELGEIFGKQQEAEKMTKEFTTFYKSYTKR-NKNKKHPKVLVLIGL 223
Cdd:cd01148  100 DSLA-ELGIKTYILPESCGQRRGEATLDDVYNDIRNLGKIFDVEDRADKLVADLKARLAEISAKvKGDGKKVAVFVYDSG 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920 224 PGSYVIATENSYVGSLVKLAGGENVYQNADKEFLTVNTEDMKKKEPDIIVraAHALPDQVTKMFNEDF-ETNDIWKHFDA 302
Cdd:cd01148  179 EDKPFTSGRGGIPNAIITAAGGRNVFADVDESWTTVSWETVIARNPDVIV--IIDYGDQNAAEQKIKFlKENPALKNVPA 256

                        250
                 ....*....|...
gi 167709920 303 VKNKRVYDLTYEY 315
Cdd:cd01148  257 VKNNRFIVLPLAE 269
TroA_f cd01139
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ...
 129-336 6.63e-13

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: 68.49  E-value: 6.63e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920 129 DMEIVSSLNPDWILAPSSLET-----DLKPKFEE--------------LKNTEyaflnlrsvqgmyRSVQELGEIFGKQQ 189
Cdd:cd01139   83 SVEKVLTLKPDLVILNIWAKTtaeesGILEKLEQagipvvfvdfrqkpLKNTT-------------PSMRLLGKALGREE 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920 190 EAEkmtkEFTTFYKSYTKR------NKNKKHPKVLVLIGLPGS--YVIATENSYVGSLVKLAGGENVYQNADK-EFLTVN 260
Cdd:cd01139  150 RAE----EFIEFYQERIDRirdrlaKINEPKPKVFIELGAGGPeeCCSTYGNGNWGELVDAAGGDNIADGLIPgTSGELN 225

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920 261 TEDMKKKEPDIIVRAAHA----------LPDQVTKMFNEDFETNDI----WKHFDAVKNKRVYDLTYEYFGMSANFkykK 326
Cdd:cd01139  226 AEYVIAANPEIIIATGGNwakdpsgvslGPDGTTADAKESLLRALLkrpgWSSLQAVKNGRVYALWHQFYRSPYNF---V 302

                        250
                 ....*....|
gi 167709920 327 ALSELEKDFY 336
Cdd:cd01139  303 ALEAFAKWLY 312
FeuA cd01138
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ...
 80-316 3.01e-10

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: 59.65  E-value: 3.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920  80 NPRIVATSPAVADICDKLDLDLVGVPKSSvSKIPSRYKKV--KKVGLAMSPDMEIVSSLNPDWILAPSSLETDLKpKFEE 157
Cdd:cd01138    8 KPKRIVALSGETEGLALLGIKPVGAASIG-GKNPYYKKKTlaKVVGIVDEPNLEKVLELKPDLIIVSSKQEENYE-KLSK 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920 158 LKNTEYAFLNLRSVQGmyrSVQELGEIFGKQQEAEKMTKEFTTFYKSYTKR--NKNKKHPKVLVLIGLPGSYVIATENSY 235
Cdd:cd01138   86 IAPTVPVSYNSSDWEE---QLKEIGKLLNKEDEAEKWLADYKQKAKEAKEKikKKLGNDKSVAVLRGRKQIYVFGEDGRG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920 236 VGSLVK----LAGGENVYQNADK-EFLTVNTEDMKKKEPDIIVRAAHALPDQvtkmfNEDFETNDIWKHFDAVKNKRVY- 309
Cdd:cd01138  163 GGPILYadlgLKAPEKVKEIEDKpGYAAISLEVLPEFDADYIFLLFFTGPEA-----KADFESLPIWKNLPAVKNNHVYi 237


                 ....*...
gi 167709920 310 -DLTYEYF 316
Cdd:cd01138  238 vDAWVFYF 245
TroA_d cd01141
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ...
 81-251 1.63e-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: 56.66  E-value: 1.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920  81 PRIVATSPAVADICDKLD--LDLVGVPKSSVS-KIPS-RYKKVKKVGLAMSPDMEIVSSLNPDWIL--APSSLETDLKpK 154
Cdd:cd01141    9 KRIVVLSPTHVDLLLALDkaDKIVGVSASAYDlNTPAvKERIDIQVGPTGSLNVELIVALKPDLVIlyGGFQAQTILD-K 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920 155 FEELKNTEYAFLNLRSVQGMYRSVQELGEIFGKQQEaEKMTKEFTTFYKSYT---KRNKNKKHPKVLVLIGLPGSYVIAT 231
Cdd:cd01141   88 LEQLGIPVLYVNEYPSPLGRAEWIKFAAAFYGVGKE-DKADEAFAQIAGRYRdlaKKVSNLNKPTVAIGKPVKGLWYMPG 166

                        170       180
                 ....*....|....*....|
gi 167709920 232 ENSYVGSLVKLAGGENVYQN 251
Cdd:cd01141  167 GNSYVAKMLRDAGGRYLSAE 186
HutB cd01149
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ...
 82-273 1.89e-09

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: 57.28  E-value: 1.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920  82 RIVATSPAVADICDKLDLD--LVGVPKSSVskIPSRYKKVKKVGLAMSPDMEIVSSLNPDWILApsslETDLKPKfEELK 159
Cdd:cd01149    3 RIVSLGGSVTEIVYALGAGdrLVGVDSTST--YPEAAAKLPDVGYMRQLSAEGVLSLKPTLVIA----SDEAGPP-EALD 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920 160 NTEYAFLNLRSV------QGMYRSVQELGEIFGKQQEAEKMTKEFTTFYKSYTK-RNKNKKHPKVLVLIGLPGSYV-IAT 231
Cdd:cd01149   76 QLRAAGVPVVTVpstptlDGLLTKIRQVAQALGVPEKGEALAQEVRQRLAALRKtVAAHKKPPRVLFLLSHGGGAAmAAG 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 167709920 232 ENSYVGSLVKLAGGENVYQnADKEFLTVNTEDMKKKEPDIIV 273
Cdd:cd01149  156 RNTAADAIIALAGAVNAAA-GFRGYKPLSAEALIAAQPDVIL 196
fecB PRK11411
iron-dicitrate transporter substrate-binding subunit; Provisional
 82-308 2.66e-06

iron-dicitrate transporter substrate-binding subunit; Provisional


Pssm-ID: 183123 [Multi-domain]  Cd Length: 303  Bit Score: 48.52  E-value: 2.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920  82 RIVATSPAVADICDKLDLDLVGV-----PKSSVSKIPSRYKKVKKVGLAMSPDMEIVSSLNPDWILAPSSLETDLkpkFE 156
Cdd:PRK11411  41 RIVVLELSFVDALAAVGVSPVGVaddndAKRILPEVRAHLKPWQSVGTRSQPSLEAIAALKPDLIIADSSRHAGV---YI 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920 157 ELKntEYA---FLNLR--SVQGMYRSVQELGEIFGKQQEAEKMTKEFTTFYKSYTKR-NKNKKhpkvlVLIGLP--GSYV 228
Cdd:PRK11411 118 ALQ--KIAptlLLKSRneTYQENLQSAAIIGEVLGKKREMQARIEQHKERMAQFASQlPKGTR-----VAFGTSreQQFN 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920 229 IATENSYVGSLVKlAGGENV--YQNADKEFLTVNTEDMKKKEPDIIVRAAHALPDQVtkmfnEDFETNDIWKHFDAVKNK 306
Cdd:PRK11411 191 LHSPESYTGSVLA-ALGLNVpkAPMNGAAMPSISLEQLLALNPDWLLVAHYRQESIV-----KRWQQDPLWQMLTAAKKQ 264


                 ..
gi 167709920 307 RV 308
Cdd:PRK11411 265 QV 266
btuF PRK09534
corrinoid ABC transporter substrate-binding protein; Reviewed
 129-280 1.22e-05

corrinoid ABC transporter substrate-binding protein; Reviewed


Pssm-ID: 236552 [Multi-domain]  Cd Length: 359  Bit Score: 46.44  E-value: 1.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167709920 129 DMEIVSSLNPDWILAPSSLETDLKPKFEELKNTEYAFLNLRSVQGMYRSVQELGEIFGKQQEAEKMTKEFTTFYKSYTKR 208
Cdd:PRK09534 111 NVEAVVGLDPDLVLAPNAVAGDTVTRLREAGITVFHFPAATSIEDVAEKTATIGRLTGNCEAAAETNAEMRDRVDAVEDR 190

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167709920 209 NKN-KKHPKVLVLIGlpGSYViATENSYVGSLVKLAGGENVYQNADKE-FLTVNTEDMKKKEPDIIVRAAHALP 280
Cdd:PRK09534 191 TADvDDRPRVLYPLG--DGYT-AGGNTFIGALIEAAGGHNVAADATTDgYPQLSEEVIVQQDPDVIVVATASAL 261
 
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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