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Conserved domains on  [gi|157683030|gb|ABV64174|]
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heme ABC transporter substrate-binding protein [Bacillus pumilus SAFR-032]

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 ...
 3-293 2.88e-178

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: 492.94  E-value: 2.88e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030    3 HRMLCTLIAALgVCVILSGCSQSAESSAKGKKSAESsERIVATTVAAAEIMDALEVDLVGVPTSQKSLPARYKGLPEVGN 82
Cdd:TIGR03659   1 KKILSLVLLAV-LSLGLTGCSSSKEKSKVSNKKSKE-ERIVATSVAVTEILDKLDLDLVGVPTSQKTLPKRYKDVPEVGN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030   83 PMSPDMEIIQSLQPTDVLSVTTLQYDLETPFQQAGVPATYLNLESMANMEKAITKLGDQYDRKKQAERIVTEFEQKKKDI 162
Cdd:TIGR03659  79 PMSPDMEKIKSLKPTVVLSVTTLEEDLGPKFKQLGVEATFLNLTSVDGMKKSITELGEKYGREEQAEKLVKEINEKEAEV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030  163 QEKTKGKRKPSVLILLGVPGSYLVATEHSYIGDLVRIAGGENIVKGEKMEYLASNTEYLQKANPDIILRAAHGMPDEVVR 242
Cdd:TIGR03659 159 KKKVKGKKKPKVLILMGVPGSYLVATENSYIGDLVKLAGGENVYKGNKQEYLSSNTEYLLKANPDIILRAAHGMPDEVKK 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 157683030  243 MFDQEFKTNDIWKHFHAVKQNRVYDLEESLFGTTGNLKAAEALDELMRMLY 293
Cdd:TIGR03659 239 MFDEEFKTNDIWKHFEAVKNNRVYDLDEELFGMTANLKVAEALDELKKILY 289
 
Name Accession Description Interval E-value
IsdE TIGR03659
heme ABC transporter, heme-binding protein isdE; This family of ABC substrate-binding proteins ...
 3-293 2.88e-178

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: 492.94  E-value: 2.88e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030    3 HRMLCTLIAALgVCVILSGCSQSAESSAKGKKSAESsERIVATTVAAAEIMDALEVDLVGVPTSQKSLPARYKGLPEVGN 82
Cdd:TIGR03659   1 KKILSLVLLAV-LSLGLTGCSSSKEKSKVSNKKSKE-ERIVATSVAVTEILDKLDLDLVGVPTSQKTLPKRYKDVPEVGN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030   83 PMSPDMEIIQSLQPTDVLSVTTLQYDLETPFQQAGVPATYLNLESMANMEKAITKLGDQYDRKKQAERIVTEFEQKKKDI 162
Cdd:TIGR03659  79 PMSPDMEKIKSLKPTVVLSVTTLEEDLGPKFKQLGVEATFLNLTSVDGMKKSITELGEKYGREEQAEKLVKEINEKEAEV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030  163 QEKTKGKRKPSVLILLGVPGSYLVATEHSYIGDLVRIAGGENIVKGEKMEYLASNTEYLQKANPDIILRAAHGMPDEVVR 242
Cdd:TIGR03659 159 KKKVKGKKKPKVLILMGVPGSYLVATENSYIGDLVKLAGGENVYKGNKQEYLSSNTEYLLKANPDIILRAAHGMPDEVKK 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 157683030  243 MFDQEFKTNDIWKHFHAVKQNRVYDLEESLFGTTGNLKAAEALDELMRMLY 293
Cdd:TIGR03659 239 MFDEEFKTNDIWKHFEAVKNNRVYDLDEELFGMTANLKVAEALDELKKILY 289
FatB cd01140
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ...
 40-293 1.00e-62

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: 199.02  E-value: 1.00e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030  40 ERIVATTVAAAEIMDALEVDLVGVPTSqKSLPARYK-----GLPEVGNPMSPDMEIIQSLQPTDVLSVTTLQYDLETPFQ 114
Cdd:cd01140   13 EKVVVFDVGALDTLDALGVKVVGVPKS-STLPEYLKkykddKYANVGTLFEPDLEAIAALKPDLIIIGGRLAEKYDELKK 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030 115 QAGVPATYLNL-ESMANMEKAITKLGDQYDRKKQAERIVTEFEQKKKDIQEKTKGKRKPSVLILLGvpGSYLVATEHSYI 193
Cdd:cd01140   92 IAPTIDLGADLkNYLESVKQNIETLGKIFGKEEEAKELVAEIDASIAEAKSAAKGKKKALVVLVNG--GKLSAFGPGSRF 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030 194 GDLVRIAGGENIVKGEKM--EYLASNTEYLQKANPDIILRAAHGMPDEVVRMFDQEFKTNDIWKHFHAVKQNRVYDLEES 271
Cdd:cd01140  170 GWLHDLLGFEPADENIKAssHGQPVSFEYILEANPDWLFVIDRGAAIGAEGSSAKEVLDNDLVKNTTAWKNGKVIYLDPD 249

                        250       260
                 ....*....|....*....|..
gi 157683030 272 LFGTTGNLKaaEALDELMRMLY 293
Cdd:cd01140  250 LWYLSGGGL--ESLKQMIDDLK 269
FepB COG0614
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ...
 41-294 2.59e-51

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


Pssm-ID: 440379 [Multi-domain]  Cd Length: 264  Bit Score: 169.41  E-value: 2.59e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030  41 RIVATTVAAAEIMDALEVD--LVGVPTSQKSL--PARYKGLPEVGNPMSPDMEIIQSLQPtDV--LSVTTLQYDLETPFQ 114
Cdd:COG0614    2 RIVSLSPSATELLLALGAGdrLVGVSDWGYCDypELELKDLPVVGGTGEPNLEAILALKP-DLvlASSSGNDEEDYEQLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030 115 QAGVPATYLNLESMANMEKAITKLGDQYDRKKQAERIVTEFEQKKKDIQEKTKG-KRKPSVLILLGVPGSYLVATEHSYI 193
Cdd:COG0614   81 KIGIPVVVLDPRSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGaEERPTVLYEIWSGDPLYTAGGGSFI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030 194 GDLVRIAGGENIVKGEKMEYLASNTEYLQKANPDIILRAAHGMPDEVVRMFDQEFKTNDIWKHFHAVKQNRVYDLEESLF 273
Cdd:COG0614  161 GELLELAGGRNVAADLGGGYPEVSLEQVLALDPDVIILSGGGYDAETAEEALEALLADPGWQSLPAVKNGRVYVVPGDLL 240

                        250       260
                 ....*....|....*....|.
gi 157683030 274 GTTGnLKAAEALDELMRMLYP 294
Cdd:COG0614  241 SRPG-PRLLLALEDLAKALHP 260
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
 43-271 9.32e-35

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: 125.56  E-value: 9.32e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030   43 VATTVAAAEIMDAL--EVDLVGVPTSQKSLPARYKG--LPEVGNPMSPDMEIIQSLQPTDVLSVTTLQYDLETPFQQAGV 118
Cdd:pfam01497   1 AALSPAYTEILYALgaTDSIVGVDAYTRDPLKADAVaaIVKVGAYGEINVERLAALKPDLVILSTGYLTDEAEELLSLII 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030  119 PA-TYLNLESMANMEKAITKLGDQYDRKKQAERIVTEFEQKKKDIQEKT-KGKRKPSVLILLGVPGSYLVATEHSYIGDL 196
Cdd:pfam01497  81 PTvIFESSSTGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVpSLTRKPVLVFGGADGGGYVVAGSNTYIGDL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157683030  197 VRIAGGENIVK-GEKMEYLASNTEYLQKANPDIILRAAHGMpdeVVRMFDQEFKTNDIWKHFHAVKQNRVYDLEES 271
Cdd:pfam01497 161 LRILGIENIAAeLSGSEYAPISFEAILSSNPDVIIVSGRDS---FTKTGPEFVAANPLWAGLPAVKNGRVYTLPSD 233
btuF PRK09534
corrinoid ABC transporter substrate-binding protein; Reviewed
 37-232 2.29e-06

corrinoid ABC transporter substrate-binding protein; Reviewed


Pssm-ID: 236552 [Multi-domain]  Cd Length: 359  Bit Score: 48.37  E-value: 2.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030  37 ESSERIVATTVAAAEIMDAL--EVDLVGVPTSQKSLP-ARYKGLPEVGNPMSPDMEIIQSLQPTDVLSVTTLQYDLETPF 113
Cdd:PRK09534  58 ERPERVVTLNPSAAQTMWELgaRDRVVGVTQYASYLDgAEERTNVSGGQPFGVNVEAVVGLDPDLVLAPNAVAGDTVTRL 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030 114 QQAGVPATYL----NLESMANMEKAITKLGDQYDrkkQAERIVTEFEQKKKDIQEKTKG-KRKPSVLILLGvpGSYlVAT 188
Cdd:PRK09534 138 REAGITVFHFpaatSIEDVAEKTATIGRLTGNCE---AAAETNAEMRDRVDAVEDRTADvDDRPRVLYPLG--DGY-TAG 211

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 157683030 189 EHSYIGDLVRIAGGENI-VKGEKMEYLASNTEYLQKANPDIILRA 232
Cdd:PRK09534 212 GNTFIGALIEAAGGHNVaADATTDGYPQLSEEVIVQQDPDVIVVA 256
 
Name Accession Description Interval E-value
IsdE TIGR03659
heme ABC transporter, heme-binding protein isdE; This family of ABC substrate-binding proteins ...
 3-293 2.88e-178

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: 492.94  E-value: 2.88e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030    3 HRMLCTLIAALgVCVILSGCSQSAESSAKGKKSAESsERIVATTVAAAEIMDALEVDLVGVPTSQKSLPARYKGLPEVGN 82
Cdd:TIGR03659   1 KKILSLVLLAV-LSLGLTGCSSSKEKSKVSNKKSKE-ERIVATSVAVTEILDKLDLDLVGVPTSQKTLPKRYKDVPEVGN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030   83 PMSPDMEIIQSLQPTDVLSVTTLQYDLETPFQQAGVPATYLNLESMANMEKAITKLGDQYDRKKQAERIVTEFEQKKKDI 162
Cdd:TIGR03659  79 PMSPDMEKIKSLKPTVVLSVTTLEEDLGPKFKQLGVEATFLNLTSVDGMKKSITELGEKYGREEQAEKLVKEINEKEAEV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030  163 QEKTKGKRKPSVLILLGVPGSYLVATEHSYIGDLVRIAGGENIVKGEKMEYLASNTEYLQKANPDIILRAAHGMPDEVVR 242
Cdd:TIGR03659 159 KKKVKGKKKPKVLILMGVPGSYLVATENSYIGDLVKLAGGENVYKGNKQEYLSSNTEYLLKANPDIILRAAHGMPDEVKK 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 157683030  243 MFDQEFKTNDIWKHFHAVKQNRVYDLEESLFGTTGNLKAAEALDELMRMLY 293
Cdd:TIGR03659 239 MFDEEFKTNDIWKHFEAVKNNRVYDLDEELFGMTANLKVAEALDELKKILY 289
FatB cd01140
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ...
 40-293 1.00e-62

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: 199.02  E-value: 1.00e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030  40 ERIVATTVAAAEIMDALEVDLVGVPTSqKSLPARYK-----GLPEVGNPMSPDMEIIQSLQPTDVLSVTTLQYDLETPFQ 114
Cdd:cd01140   13 EKVVVFDVGALDTLDALGVKVVGVPKS-STLPEYLKkykddKYANVGTLFEPDLEAIAALKPDLIIIGGRLAEKYDELKK 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030 115 QAGVPATYLNL-ESMANMEKAITKLGDQYDRKKQAERIVTEFEQKKKDIQEKTKGKRKPSVLILLGvpGSYLVATEHSYI 193
Cdd:cd01140   92 IAPTIDLGADLkNYLESVKQNIETLGKIFGKEEEAKELVAEIDASIAEAKSAAKGKKKALVVLVNG--GKLSAFGPGSRF 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030 194 GDLVRIAGGENIVKGEKM--EYLASNTEYLQKANPDIILRAAHGMPDEVVRMFDQEFKTNDIWKHFHAVKQNRVYDLEES 271
Cdd:cd01140  170 GWLHDLLGFEPADENIKAssHGQPVSFEYILEANPDWLFVIDRGAAIGAEGSSAKEVLDNDLVKNTTAWKNGKVIYLDPD 249

                        250       260
                 ....*....|....*....|..
gi 157683030 272 LFGTTGNLKaaEALDELMRMLY 293
Cdd:cd01140  250 LWYLSGGGL--ESLKQMIDDLK 269
FepB COG0614
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ...
 41-294 2.59e-51

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


Pssm-ID: 440379 [Multi-domain]  Cd Length: 264  Bit Score: 169.41  E-value: 2.59e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030  41 RIVATTVAAAEIMDALEVD--LVGVPTSQKSL--PARYKGLPEVGNPMSPDMEIIQSLQPtDV--LSVTTLQYDLETPFQ 114
Cdd:COG0614    2 RIVSLSPSATELLLALGAGdrLVGVSDWGYCDypELELKDLPVVGGTGEPNLEAILALKP-DLvlASSSGNDEEDYEQLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030 115 QAGVPATYLNLESMANMEKAITKLGDQYDRKKQAERIVTEFEQKKKDIQEKTKG-KRKPSVLILLGVPGSYLVATEHSYI 193
Cdd:COG0614   81 KIGIPVVVLDPRSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGaEERPTVLYEIWSGDPLYTAGGGSFI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030 194 GDLVRIAGGENIVKGEKMEYLASNTEYLQKANPDIILRAAHGMPDEVVRMFDQEFKTNDIWKHFHAVKQNRVYDLEESLF 273
Cdd:COG0614  161 GELLELAGGRNVAADLGGGYPEVSLEQVLALDPDVIILSGGGYDAETAEEALEALLADPGWQSLPAVKNGRVYVVPGDLL 240

                        250       260
                 ....*....|....*....|.
gi 157683030 274 GTTGnLKAAEALDELMRMLYP 294
Cdd:COG0614  241 SRPG-PRLLLALEDLAKALHP 260
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
 43-271 9.32e-35

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: 125.56  E-value: 9.32e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030   43 VATTVAAAEIMDAL--EVDLVGVPTSQKSLPARYKG--LPEVGNPMSPDMEIIQSLQPTDVLSVTTLQYDLETPFQQAGV 118
Cdd:pfam01497   1 AALSPAYTEILYALgaTDSIVGVDAYTRDPLKADAVaaIVKVGAYGEINVERLAALKPDLVILSTGYLTDEAEELLSLII 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030  119 PA-TYLNLESMANMEKAITKLGDQYDRKKQAERIVTEFEQKKKDIQEKT-KGKRKPSVLILLGVPGSYLVATEHSYIGDL 196
Cdd:pfam01497  81 PTvIFESSSTGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVpSLTRKPVLVFGGADGGGYVVAGSNTYIGDL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157683030  197 VRIAGGENIVK-GEKMEYLASNTEYLQKANPDIILRAAHGMpdeVVRMFDQEFKTNDIWKHFHAVKQNRVYDLEES 271
Cdd:pfam01497 161 LRILGIENIAAeLSGSEYAPISFEAILSSNPDVIIVSGRDS---FTKTGPEFVAANPLWAGLPAVKNGRVYTLPSD 233
YvrC cd01143
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ...
 40-230 1.79e-30

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: 113.14  E-value: 1.79e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030  40 ERIVATTVAAAEIMDAL--EVDLVGVpTSQKSLPARYKGLPEVGNPMSPDMEIIQSLQPTDVLSVTTLQYDLETPFQQAG 117
Cdd:cd01143    4 ERIVSLSPSITEILFALgaGDKIVGV-DTYSNYPKEVRKKPKVGSYSNPNVEKIVALKPDLVIVSSSSLAELLEKLKDAG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030 118 VPATYLNL-ESMANMEKAITKLGDQYDRKKQAERIVTEFEQKKKDIQEKTKGKRKPSVLILLGVPGSYlVATEHSYIGDL 196
Cdd:cd01143   83 IPVVVLPAaSSLDEIYDQIELIGKITGAEEEAEKLVKEMKQKIDKVKDKGKTIKKSKVYIEVSLGGPY-TAGKNTFINEL 161

                        170       180       190
                 ....*....|....*....|....*....|....
gi 157683030 197 VRIAGGENIVkGEKMEYLASNTEYLQKANPDIIL 230
Cdd:cd01143  162 IRLAGAKNIA-ADSGGWPQVSPEEILKANPDVII 194
ChuT COG4558
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ...
 4-294 2.97e-27

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


Pssm-ID: 443619 [Multi-domain]  Cd Length: 285  Bit Score: 107.20  E-value: 2.97e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030   4 RMLCTLIAALGVCVILSGCSqsaessakgkKSAESSERIVATTVAAAEIMDAL--EVDLVGVPTSqkSL-PARYKGLPEV 80
Cdd:COG4558    2 KRLALALLLLALAALAAGAS----------VAAAAAERIVSLGGSVTEIVYALgaGDRLVGVDTT--STyPAAAKALPDV 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030  81 GNPMSPDMEIIQSLQPTDVLSV------TTLQydletPFQQAGVPATYLNLE-SMANMEKAITKLGDQYDRKKQAERIVT 153
Cdd:COG4558   70 GYMRQLSAEGILSLKPTLVLASegagppEVLD-----QLRAAGVPVVVVPAApSLEGVLAKIRAVAAALGVPEAGEALAA 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030 154 EFEQKKKDIQEKTKG-KRKPSVLILLGV-PGSYLVATEHSYIGDLVRIAGGENIVKGEKmEYLASNTEYLQKANPDIILR 231
Cdd:COG4558  145 RLEADLAALAARVAAiGKPPRVLFLLSRgGGRPMVAGRGTAADALIRLAGGVNAAAGFE-GYKPLSAEALIAAAPDVILV 223

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157683030 232 AAHGMpdevvrmfDQEFKTNDIWKH-----FHAVKQNRVYDLEESL---FGttgnLKAAEALDELMRMLYP 294
Cdd:COG4558  224 MTRGL--------ESLGGVDGLLALpglaqTPAGKNKRIVAMDDLLllgFG----PRTPQAALALAQALYP 282
BtuF cd01144
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ...
 40-288 3.99e-26

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: 103.15  E-value: 3.99e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030  40 ERIVATTVAAAEIMDALEVD--LVGVpTSQKSLPARYKGLPEVGNPMSPDMEIIQSLQPTDVLSVTTLQYDLETPF-QQA 116
Cdd:cd01144    1 MRIVSLAPSATELLYALGLGdqLVGV-TDYCDYPPEAKKLPRVGGFYQLDLERVLALKPDLVIAWDDCNVCAVVDQlRAA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030 117 GVPATYLNLESMANMEKAITKLGDQYDRKKQAERIVTEFEQKKKDIQEKTKGKRKPSVLILLGV-PgsyLVATEHSYIGD 195
Cdd:cd01144   80 GIPVLVSEPQTLDDILADIRRLGTLAGRPARAEELAEALRRRLAALRKQYASKPPPRVFYQEWIdP---LMTAGGDWVPE 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030 196 LVRIAGGENIVKGEKMEYLASNTEYLQKANPDIILRAAHGmpdevVRMFDQEFKTNDIWKHFHAVKQNRVYDLEESLFGT 275
Cdd:cd01144  157 LIALAGGVNVFADAGERSPQVSWEDVLAANPDVIVLSPCG-----FGFTPAILRKEPAWQALPAVRNGRVYAVDGNWYFR 231

                        250
                 ....*....|...
gi 157683030 276 TGnLKAAEALDEL 288
Cdd:cd01144  232 PS-PRLVDGLEQL 243
FhuD cd01146
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ...
 40-286 3.81e-24

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: 98.13  E-value: 3.81e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030  40 ERIVATTVAAAEIMDALEVDLVGVPTSQKSLP------ARYKGLPEVGNPMSPDMEIIQSLQPTDVLSVTTLQ---YDLE 110
Cdd:cd01146    4 QRIVALDWGALETLLALGVKPVGVADTAGYKPwipepaLPLEGVVDVGTRGQPNLEAIAALKPDLILGSASRHdeiYDQL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030 111 tpfqQAGVPATYLN-LESMANMEKAITKLGDQYDRKKQAERIVTEFEQKKKDIQEKTKGKRKPSVLIL-LGVPGSYLVAT 188
Cdd:cd01146   84 ----SQIAPTVLLDsSPWLAEWKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKLPDKGPKPVSVVrFSDAGSIRLYG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030 189 EHSYIGDLVRIAGGENIVKGEKME---YLASNTEYLQKANPDIILrAAHGMPDEVVrmfdQEFKTNDIWKHFHAVKQNRV 265
Cdd:cd01146  160 PNSFAGSVLEDLGLQNPWAQETTNdsgFATISLERLAKADADVLF-VFTYEDEELA----QALQANPLWQNLPAVKNGRV 234

                        250       260
                 ....*....|....*....|.
gi 157683030 266 YDLEESLFGTTGNLKAAEALD 286
Cdd:cd01146  235 YVVDDVWWFFGGGLSAARLLL 255
FecB COG4594
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ...
 1-293 4.48e-22

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


Pssm-ID: 443650 [Multi-domain]  Cd Length: 316  Bit Score: 93.83  E-value: 4.48e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030   1 MKHRMLCTLIAALgvCVILSGCSQSAESSAKGKKSAES---------------SERIVATTVAAAEIMDALEVDLVGVPT 65
Cdd:COG4594    1 MKKLLLLLILLLA--LLLLAACGSSSSDSSSSEAAAGArtvkhamgettipgtPKRVVVLEWSFADALLALGVTPVGIAD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030  66 SQKSLP------ARYKGLPEVGNPMSPDMEIIQSLQPTDVLSVTtlqydletpFQQAGVpatYLNLESMA---------- 129
Cdd:COG4594   79 DNDYDRwvpylrDLIKGVTSVGTRSQPNLEAIAALKPDLIIADK---------SRHEAI---YDQLSKIAptvlfksrng 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030 130 ---NMEKAITKLGDQYDRKKQAERIVTEFEQK----KKDIQEKTKGKrkpSVLILLGVPGSYLVATEHSYIGDLVRIAGG 202
Cdd:COG4594  147 dyqENLESFKTIAKALGKEEEAEAVLADHDQRiaeaKAKLAAADKGK---KVAVGQFRADGLRLYTPNSFAGSVLAALGF 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030 203 ENIVKGEKME---YLASNTEYLQKANPDIILRAAHGMPDevvrmFDQEFKTNDIWKHFHAVKQNRVYDLEESLFGTTGNL 279
Cdd:COG4594  224 ENPPKQSKDNgygYSEVSLEQLPALDPDVLFIATYDDPS-----ILKEWKNNPLWKNLKAVKNGRVYEVDGDLWTRGRGP 298

                        330
                 ....*....|....*
gi 157683030 280 KAAEA-LDELMRMLY 293
Cdd:COG4594  299 LAAELmADDLVEILL 313
TroA_e cd01142
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ...
 40-295 1.24e-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: 89.34  E-value: 1.24e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030  40 ERIVATTVAAAEIMDAL--EVDLVGVPTSQKSLPARYKGLPE------VGNPMSPDMEIIQSLQPtDVlsVTTLQYDLET 111
Cdd:cd01142   25 KRIAALWGAGNAVVAALggGKLIVATTSTVQQEPWLYRLAPSlenvatGGTGNDVNIEELLALKP-DV--VIVWSTDGKE 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030 112 PFQQA--GVPATYLNLESMANMEKAITKLGDQYDRKKQAERIVTEFEQKKKDIQEKTKG---KRKPSVLILLGVPGSylV 186
Cdd:cd01142  102 AGKAVlrLLNALSLRDAELEEVKLTIALLGELLGRQEKAEALVAYFDDNLAYVAARTKKlpdSERPRVYYAGPDPLT--T 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030 187 ATEHSYIGDLVRIAGGEN----IVKGEKMEYlasNTEYLQKANPDIILrAAHGMPDEvvrmfdqEFKTNDIWKHFHAVKQ 262
Cdd:cd01142  180 DGTGSITNSWIDLAGGINvaseATKKGSGEV---SLEQLLKWNPDVII-VGNADTKA-------AILADPRWQNLRAVKN 248

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 157683030 263 NRVYDLEESLFgTTGNLKAAEAL--DELMRMLYPS 295
Cdd:cd01142  249 GRVYVNPEGAF-WWDRPSAEEALlgLWLAKTLYPE 282
HemV-2 cd01147
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ...
 40-268 1.41e-19

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: 85.85  E-value: 1.41e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030  40 ERIVATTVAAAEIMDALEV--DLVGVPTSQKS--------LPARYKGLPEVGNPM---SPDMEIIQSLQPtDVLsVTTLQ 106
Cdd:cd01147    6 ERVVAAGPGALRLLYALAApdKIVGVDDAEKSdegrpyflASPELKDLPVIGRGGrgnTPNYEKIAALKP-DVV-IDVGS 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030 107 YD----LETPFQQAGVPATYLNL-ESMANMEKAITKLGDQYDRKKQAERIVTEFEQKKKDIQEKTKG---KRKPSV---- 174
Cdd:cd01147   84 DDptsiADDLQKKTGIPVVVLDGgDSLEDTPEQIRLLGKVLGKEERAEELISFIESILADVEERTKDipdEEKPTVyfgr 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030 175 LILLGVPGsyLVATEHSYIGdLVRIAGGENIVKGEKMEYLAS-NTEYLQKANPDIILRAAHGMPDEVvrmfDQEFKTNDI 253
Cdd:cd01147  164 IGTKGAAG--LESGLAGSIE-VFELAGGINVADGLGGGGLKEvSPEQILLWNPDVIFLDTGSFYLSL----EGYAKNRPF 236

                        250
                 ....*....|....*
gi 157683030 254 WKHFHAVKQNRVYDL 268
Cdd:cd01147  237 WQSLKAVKNGRVYLL 251
TroA-like cd00636
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ...
 40-179 5.13e-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: 78.75  E-value: 5.13e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030  40 ERIVATTVAAAEIMDAL--EVDLVGVPTSQK---SLPARYKGLPEVGNPMSPDMEIIQSLQPTDVLSVTTLQYDLETPFQ 114
Cdd:cd00636    1 KRVVALDPGATELLLALggDDKPVGVADPSGyppEAKALLEKVPDVGHGYEPNLEKIAALKPDLIIANGSGLEAWLDKLS 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157683030 115 QAGVPATYLNLE---SMANMEKAITKLGDQYDRKKQAERIVTEFEQKKKDIQEKTKGKRKPSVLILLG 179
Cdd:cd00636   81 KIAIPVVVVDEAselSLENIKESIRLIGKALGKEENAEELIAELDARLAELRAKLAKIPKKKVSLVVG 148
TroA_f cd01139
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ...
 73-295 1.50e-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: 81.58  E-value: 1.50e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030  73 RYKGLPEVGNPMSPD--MEIIQSLQPtDVLSVTTLQYD------LETPFQQAGVPATY--LNLESMANMEKAITKLGDQY 142
Cdd:cd01139   67 EIADIPLIGSTYNGDfsVEKVLTLKP-DLVILNIWAKTtaeesgILEKLEQAGIPVVFvdFRQKPLKNTTPSMRLLGKAL 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030 143 DRKKQAERIVTEFEQKKKDIQEKTKG--KRKPSVLILLGVPGS--YLVATEHSYIGDLVRIAGGENIVKG-EKMEYLASN 217
Cdd:cd01139  146 GREERAEEFIEFYQERIDRIRDRLAKinEPKPKVFIELGAGGPeeCCSTYGNGNWGELVDAAGGDNIADGlIPGTSGELN 225

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030 218 TEYLQKANPDIILRAAH---GMPDEVVRMFD-------QEFKTNDI----WKHFHAVKQNRVYDLEESLFGTTGNLKAAE 283
Cdd:cd01139  226 AEYVIAANPEIIIATGGnwaKDPSGVSLGPDgttadakESLLRALLkrpgWSSLQAVKNGRVYALWHQFYRSPYNFVALE 305

                        250
                 ....*....|..
gi 157683030 284 ALDELmrmLYPS 295
Cdd:cd01139  306 AFAKW---LYPE 314
TroA_d cd01141
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ...
 40-202 8.34e-15

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: 71.30  E-value: 8.34e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030  40 ERIVATTVAAAEIMDAL--EVDLVGVPTS--QKSLPA-RYKGLPEVGNPMSPDMEIIQSLQPtDV--LSVTTLQYDLETP 112
Cdd:cd01141    9 KRIVVLSPTHVDLLLALdkADKIVGVSASayDLNTPAvKERIDIQVGPTGSLNVELIVALKP-DLviLYGGFQAQTILDK 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030 113 FQQAGVPATYLNLES--MANMEkAITKLGDQYDRKK--QAERIVTEFEQKKKDIQEKTKGKRKPSVLILLGVPGSYLVAT 188
Cdd:cd01141   88 LEQLGIPVLYVNEYPspLGRAE-WIKFAAAFYGVGKedKADEAFAQIAGRYRDLAKKVSNLNKPTVAIGKPVKGLWYMPG 166

                        170
                 ....*....|....
gi 157683030 189 EHSYIGDLVRIAGG 202
Cdd:cd01141  167 GNSYVAKMLRDAGG 180
TroA_a cd01148
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ...
 40-288 2.17e-13

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


Pssm-ID: 238568 [Multi-domain]  Cd Length: 284  Bit Score: 68.90  E-value: 2.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030  40 ERIVATTVAAAEIMDALEVD--LVGVPTSQK----SLPARYKGLPEVGnPMSPDMEIIQSLQPTDVLSVTTLQYDLE--- 110
Cdd:cd01148   19 QRVVSNDQNTTEMMLALGLQdrMVGTAGIDNkdlpELKAKYDKVPELA-KKYPSKETVLAARPDLVFGGWSYGFDKGglg 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030 111 TP--FQQAGVPaTYLNLES---------MANMEKAITKLGDQYDRKKQAERIVTEFEQKKKDIQEKTKG-KRKPSVLIL- 177
Cdd:cd01148   98 TPdsLAELGIK-TYILPEScgqrrgeatLDDVYNDIRNLGKIFDVEDRADKLVADLKARLAEISAKVKGdGKKVAVFVYd 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030 178 LGVPGSYLVATeHSYIGDLVRIAGGENIVKGEKMEYLASNTEYLQKANPD--IILRAAHGMPDEVVRMFdqeFKTNDIWK 255
Cdd:cd01148  177 SGEDKPFTSGR-GGIPNAIITAAGGRNVFADVDESWTTVSWETVIARNPDviVIIDYGDQNAAEQKIKF---LKENPALK 252

                        250       260       270
                 ....*....|....*....|....*....|...
gi 157683030 256 HFHAVKQNRVYDLEesLFGTTGNLKAAEALDEL 288
Cdd:cd01148  253 NVPAVKNNRFIVLP--LAEATPGIRNVDAIEKL 283
FeuA cd01138
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ...
 40-273 1.38e-11

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: 63.12  E-value: 1.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030  40 ERIVATTVAAaEIMDALEVDLVGVPTSQKSLPArYKGLPEVGNP---MSPDMEIIQSLQPTDVLSVTTLQYDLETpFQQA 116
Cdd:cd01138   10 KRIVALSGET-EGLALLGIKPVGAASIGGKNPY-YKKKTLAKVVgivDEPNLEKVLELKPDLIIVSSKQEENYEK-LSKI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030 117 GvPATYLNLESmANMEKAITKLGDQYDRKKQAERIVTEFEQKKKDIQEKTKGKRKP--SVLILLGVPGSYLVATEHSYIG 194
Cdd:cd01138   87 A-PTVPVSYNS-SDWEEQLKEIGKLLNKEDEAEKWLADYKQKAKEAKEKIKKKLGNdkSVAVLRGRKQIYVFGEDGRGGG 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030 195 DLVRIAGG----ENIVKGE-KMEYLASNTEYLQKANPDIILRAAHGMPDEvvrmfDQEFKTNDIWKHFHAVKQNRVYDLE 269
Cdd:cd01138  165 PILYADLGlkapEKVKEIEdKPGYAAISLEVLPEFDADYIFLLFFTGPEA-----KADFESLPIWKNLPAVKNNHVYIVD 239


                 ....
gi 157683030 270 ESLF 273
Cdd:cd01138  240 AWVF 243
btuF PRK09534
corrinoid ABC transporter substrate-binding protein; Reviewed
 37-232 2.29e-06

corrinoid ABC transporter substrate-binding protein; Reviewed


Pssm-ID: 236552 [Multi-domain]  Cd Length: 359  Bit Score: 48.37  E-value: 2.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030  37 ESSERIVATTVAAAEIMDAL--EVDLVGVPTSQKSLP-ARYKGLPEVGNPMSPDMEIIQSLQPTDVLSVTTLQYDLETPF 113
Cdd:PRK09534  58 ERPERVVTLNPSAAQTMWELgaRDRVVGVTQYASYLDgAEERTNVSGGQPFGVNVEAVVGLDPDLVLAPNAVAGDTVTRL 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157683030 114 QQAGVPATYL----NLESMANMEKAITKLGDQYDrkkQAERIVTEFEQKKKDIQEKTKG-KRKPSVLILLGvpGSYlVAT 188
Cdd:PRK09534 138 REAGITVFHFpaatSIEDVAEKTATIGRLTGNCE---AAAETNAEMRDRVDAVEDRTADvDDRPRVLYPLG--DGY-TAG 211

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 157683030 189 EHSYIGDLVRIAGGENI-VKGEKMEYLASNTEYLQKANPDIILRA 232
Cdd:PRK09534 212 GNTFIGALIEAAGGHNVaADATTDGYPQLSEEVIVQQDPDVIVVA 256
 
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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