|
Name |
Accession |
Description |
Interval |
E-value |
| IsdE |
TIGR03659 |
heme ABC transporter, heme-binding protein isdE; This family of ABC substrate-binding proteins ... |
2-288 |
1.58e-151 |
|
heme ABC transporter, heme-binding protein isdE; This family of ABC substrate-binding proteins is observed primarily in close proximity with proteins localized to the cell wall and bearing the NEAT (NEAr Transporter, pfam05031) heme-binding domain. IsdE has been shown to bind heme and is involved in the process of scavenging heme for the purpose of obtaining iron.
Pssm-ID: 274706 [Multi-domain] Cd Length: 289 Bit Score: 425.15 E-value: 1.58e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925900502 2 RIIKYLTILVISVVILT---SCQSSSSQESTKSGEFRIVPTTVALTMTLDKLDLPIVGKPTSYKTLPNRYKDVPEIGQPM 78
Cdd:TIGR03659 1 KKILSLVLLAVLSLGLTgcsSSKEKSKVSNKKSKEERIVATSVAVTEILDKLDLDLVGVPTSQKTLPKRYKDVPEVGNPM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925900502 79 EPNVEAVKKLKPTHVLSVSTIKDEMQPFYKQLNMKGYFYDFDSLKGMQKSITQLGDQFNRKAQAKELNDHLNSVKQKIEN 158
Cdd:TIGR03659 81 SPDMEKIKSLKPTVVLSVTTLEEDLGPKFKQLGVEATFLNLTSVDGMKKSITELGEKYGREEQAEKLVKEINEKEAEVKK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925900502 159 KAAKQKKhPKVLILMGVPGSYLVATDKSYIGDLVKIAGGENVIKVKDRQYISSNTENLLNINPDIILRLPHGMPEEVKKM 238
Cdd:TIGR03659 161 KVKGKKK-PKVLILMGVPGSYLVATENSYIGDLVKLAGGENVYKGNKQEYLSSNTEYLLKANPDIILRAAHGMPDEVKKM 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 925900502 239 FQKEFKQNDIWKHFKAVKNNHVYDLEEVPFGITANVDADKAMTQLYDLFY 288
Cdd:TIGR03659 240 FDEEFKTNDIWKHFEAVKNNRVYDLDEELFGMTANLKVAEALDELKKILY 289
|
|
| FatB |
cd01140 |
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ... |
35-289 |
2.17e-52 |
|
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type initial receptors in the siderophore-mediated iron uptake in some eubacterial species. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.
Pssm-ID: 238560 [Multi-domain] Cd Length: 270 Bit Score: 172.44 E-value: 2.17e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925900502 35 RIVPTTVALTMTLDKLDLPIVGKPTSyKTLPNRYKDV-----PEIGQPMEPNVEAVKKLKPTHVLSVSTikdeMQPFYKQ 109
Cdd:cd01140 14 KVVVFDVGALDTLDALGVKVVGVPKS-STLPEYLKKYkddkyANVGTLFEPDLEAIAALKPDLIIIGGR----LAEKYDE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925900502 110 L----NMKGYFYDFD-SLKGMQKSITQLGDQFNRKAQAKELNDHLNSVKQKIENKAAKQKKhPKVLILMGvpGSYLVATD 184
Cdd:cd01140 89 LkkiaPTIDLGADLKnYLESVKQNIETLGKIFGKEEEAKELVAEIDASIAEAKSAAKGKKK-ALVVLVNG--GKLSAFGP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925900502 185 KSYIGDLVKIAGGENVIKVK--DRQYISSNTENLLNINPDIILRLPHGMPEEVKKMFQKEFKQNDIWKHFKAVKNNHVYD 262
Cdd:cd01140 166 GSRFGWLHDLLGFEPADENIkaSSHGQPVSFEYILEANPDWLFVIDRGAAIGAEGSSAKEVLDNDLVKNTTAWKNGKVIY 245
|
250 260
....*....|....*....|....*..
gi 925900502 263 LEEVPFGITANVdaDKAMTQLYDLFYK 289
Cdd:cd01140 246 LDPDLWYLSGGG--LESLKQMIDDLKK 270
|
|
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
35-291 |
9.35e-50 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 165.56 E-value: 9.35e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925900502 35 RIVPTTVALTMTLDKLDLP--IVGKP-TSYKTLP-NRYKDVPEIGQPMEPNVEAVKKLKPTHVL-SVSTIKDEMQPFYKQ 109
Cdd:COG0614 2 RIVSLSPSATELLLALGAGdrLVGVSdWGYCDYPeLELKDLPVVGGTGEPNLEAILALKPDLVLaSSSGNDEEDYEQLEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925900502 110 LNMKGYFYDFDSLKGMQKSITQLGDQFNRKAQAKELNDHLNSVKQKIENKAAKQKKHPKVLILMGVPGSYLVATDKSYIG 189
Cdd:COG0614 82 IGIPVVVLDPRSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGAEERPTVLYEIWSGDPLYTAGGGSFIG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925900502 190 DLVKIAGGENVIKVKDRQYISSNTENLLNINPDIILRLPHGMPEEVKKMFQKEFKQNDIWKHFKAVKNNHVYDLEEVpFG 269
Cdd:COG0614 162 ELLELAGGRNVAADLGGGYPEVSLEQVLALDPDVIILSGGGYDAETAEEALEALLADPGWQSLPAVKNGRVYVVPGD-LL 240
|
250 260
....*....|....*....|..
gi 925900502 270 ITANVDADKAMTQLYDLFYKDK 291
Cdd:COG0614 241 SRPGPRLLLALEDLAKALHPEL 262
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
46-263 |
1.49e-37 |
|
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding proteins, several of which are involved in iron and cobalamin transport. Among its ligands are siderophores bacillibactin, enterobactin and iron(III)-hydroxamates (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1 https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 426291 [Multi-domain] Cd Length: 233 Bit Score: 132.88 E-value: 1.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925900502 46 TLDKLDL--PIVGKP--TSYKTLPNRYKDVPEIGQPMEPNVEAVKKLKPTHVLSVSTIKDEmqPFYKQL--NMKGYFYDF 119
Cdd:pfam01497 10 ILYALGAtdSIVGVDayTRDPLKADAVAAIVKVGAYGEINVERLAALKPDLVILSTGYLTD--EAEELLslIIPTVIFES 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925900502 120 DSLK-GMQKSITQLGDQFNRKAQAKELNDHLNSVKQKIENKAAKQKKHPKVLILMGVPGSYLVATDKSYIGDLVKIAGGE 198
Cdd:pfam01497 88 SSTGeSLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPVLVFGGADGGGYVVAGSNTYIGDLLRILGIE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 925900502 199 NVIKVKDR-QYISSNTENLLNINPDIILRLPHGMpeeVKKMFQKEFKQNDIWKHFKAVKNNHVYDL 263
Cdd:pfam01497 168 NIAAELSGsEYAPISFEAILSSNPDVIIVSGRDS---FTKTGPEFVAANPLWAGLPAVKNGRVYTL 230
|
|
| btuF |
PRK09534 |
corrinoid ABC transporter substrate-binding protein; Reviewed |
75-225 |
3.76e-09 |
|
corrinoid ABC transporter substrate-binding protein; Reviewed
Pssm-ID: 236552 [Multi-domain] Cd Length: 359 Bit Score: 56.84 E-value: 3.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925900502 75 GQPMEPNVEAVKKLKPTHVLSVSTIKDEMQPFYKQLNMKGYFYDF-DSLKGMQKSITQLGDQFNRKAQAKELNDHLNSVK 153
Cdd:PRK09534 105 GQPFGVNVEAVVGLDPDLVLAPNAVAGDTVTRLREAGITVFHFPAaTSIEDVAEKTATIGRLTGNCEAAAETNAEMRDRV 184
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 925900502 154 QKIENKAAKQKKHPKVLILMGvpGSYlVATDKSYIGDLVKIAGGENVIKVKD-RQYISSNTENLLNINPDIIL 225
Cdd:PRK09534 185 DAVEDRTADVDDRPRVLYPLG--DGY-TAGGNTFIGALIEAAGGHNVAADATtDGYPQLSEEVIVQQDPDVIV 254
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| IsdE |
TIGR03659 |
heme ABC transporter, heme-binding protein isdE; This family of ABC substrate-binding proteins ... |
2-288 |
1.58e-151 |
|
heme ABC transporter, heme-binding protein isdE; This family of ABC substrate-binding proteins is observed primarily in close proximity with proteins localized to the cell wall and bearing the NEAT (NEAr Transporter, pfam05031) heme-binding domain. IsdE has been shown to bind heme and is involved in the process of scavenging heme for the purpose of obtaining iron.
Pssm-ID: 274706 [Multi-domain] Cd Length: 289 Bit Score: 425.15 E-value: 1.58e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925900502 2 RIIKYLTILVISVVILT---SCQSSSSQESTKSGEFRIVPTTVALTMTLDKLDLPIVGKPTSYKTLPNRYKDVPEIGQPM 78
Cdd:TIGR03659 1 KKILSLVLLAVLSLGLTgcsSSKEKSKVSNKKSKEERIVATSVAVTEILDKLDLDLVGVPTSQKTLPKRYKDVPEVGNPM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925900502 79 EPNVEAVKKLKPTHVLSVSTIKDEMQPFYKQLNMKGYFYDFDSLKGMQKSITQLGDQFNRKAQAKELNDHLNSVKQKIEN 158
Cdd:TIGR03659 81 SPDMEKIKSLKPTVVLSVTTLEEDLGPKFKQLGVEATFLNLTSVDGMKKSITELGEKYGREEQAEKLVKEINEKEAEVKK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925900502 159 KAAKQKKhPKVLILMGVPGSYLVATDKSYIGDLVKIAGGENVIKVKDRQYISSNTENLLNINPDIILRLPHGMPEEVKKM 238
Cdd:TIGR03659 161 KVKGKKK-PKVLILMGVPGSYLVATENSYIGDLVKLAGGENVYKGNKQEYLSSNTEYLLKANPDIILRAAHGMPDEVKKM 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 925900502 239 FQKEFKQNDIWKHFKAVKNNHVYDLEEVPFGITANVDADKAMTQLYDLFY 288
Cdd:TIGR03659 240 FDEEFKTNDIWKHFEAVKNNRVYDLDEELFGMTANLKVAEALDELKKILY 289
|
|
| FatB |
cd01140 |
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ... |
35-289 |
2.17e-52 |
|
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type initial receptors in the siderophore-mediated iron uptake in some eubacterial species. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.
Pssm-ID: 238560 [Multi-domain] Cd Length: 270 Bit Score: 172.44 E-value: 2.17e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925900502 35 RIVPTTVALTMTLDKLDLPIVGKPTSyKTLPNRYKDV-----PEIGQPMEPNVEAVKKLKPTHVLSVSTikdeMQPFYKQ 109
Cdd:cd01140 14 KVVVFDVGALDTLDALGVKVVGVPKS-STLPEYLKKYkddkyANVGTLFEPDLEAIAALKPDLIIIGGR----LAEKYDE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925900502 110 L----NMKGYFYDFD-SLKGMQKSITQLGDQFNRKAQAKELNDHLNSVKQKIENKAAKQKKhPKVLILMGvpGSYLVATD 184
Cdd:cd01140 89 LkkiaPTIDLGADLKnYLESVKQNIETLGKIFGKEEEAKELVAEIDASIAEAKSAAKGKKK-ALVVLVNG--GKLSAFGP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925900502 185 KSYIGDLVKIAGGENVIKVK--DRQYISSNTENLLNINPDIILRLPHGMPEEVKKMFQKEFKQNDIWKHFKAVKNNHVYD 262
Cdd:cd01140 166 GSRFGWLHDLLGFEPADENIkaSSHGQPVSFEYILEANPDWLFVIDRGAAIGAEGSSAKEVLDNDLVKNTTAWKNGKVIY 245
|
250 260
....*....|....*....|....*..
gi 925900502 263 LEEVPFGITANVdaDKAMTQLYDLFYK 289
Cdd:cd01140 246 LDPDLWYLSGGG--LESLKQMIDDLKK 270
|
|
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
35-291 |
9.35e-50 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 165.56 E-value: 9.35e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925900502 35 RIVPTTVALTMTLDKLDLP--IVGKP-TSYKTLP-NRYKDVPEIGQPMEPNVEAVKKLKPTHVL-SVSTIKDEMQPFYKQ 109
Cdd:COG0614 2 RIVSLSPSATELLLALGAGdrLVGVSdWGYCDYPeLELKDLPVVGGTGEPNLEAILALKPDLVLaSSSGNDEEDYEQLEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925900502 110 LNMKGYFYDFDSLKGMQKSITQLGDQFNRKAQAKELNDHLNSVKQKIENKAAKQKKHPKVLILMGVPGSYLVATDKSYIG 189
Cdd:COG0614 82 IGIPVVVLDPRSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGAEERPTVLYEIWSGDPLYTAGGGSFIG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925900502 190 DLVKIAGGENVIKVKDRQYISSNTENLLNINPDIILRLPHGMPEEVKKMFQKEFKQNDIWKHFKAVKNNHVYDLEEVpFG 269
Cdd:COG0614 162 ELLELAGGRNVAADLGGGYPEVSLEQVLALDPDVIILSGGGYDAETAEEALEALLADPGWQSLPAVKNGRVYVVPGD-LL 240
|
250 260
....*....|....*....|..
gi 925900502 270 ITANVDADKAMTQLYDLFYKDK 291
Cdd:COG0614 241 SRPGPRLLLALEDLAKALHPEL 262
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
46-263 |
1.49e-37 |
|
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding proteins, several of which are involved in iron and cobalamin transport. Among its ligands are siderophores bacillibactin, enterobactin and iron(III)-hydroxamates (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1 https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 426291 [Multi-domain] Cd Length: 233 Bit Score: 132.88 E-value: 1.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925900502 46 TLDKLDL--PIVGKP--TSYKTLPNRYKDVPEIGQPMEPNVEAVKKLKPTHVLSVSTIKDEmqPFYKQL--NMKGYFYDF 119
Cdd:pfam01497 10 ILYALGAtdSIVGVDayTRDPLKADAVAAIVKVGAYGEINVERLAALKPDLVILSTGYLTD--EAEELLslIIPTVIFES 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925900502 120 DSLK-GMQKSITQLGDQFNRKAQAKELNDHLNSVKQKIENKAAKQKKHPKVLILMGVPGSYLVATDKSYIGDLVKIAGGE 198
Cdd:pfam01497 88 SSTGeSLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPVLVFGGADGGGYVVAGSNTYIGDLLRILGIE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 925900502 199 NVIKVKDR-QYISSNTENLLNINPDIILRLPHGMpeeVKKMFQKEFKQNDIWKHFKAVKNNHVYDL 263
Cdd:pfam01497 168 NIAAELSGsEYAPISFEAILSSNPDVIIVSGRDS---FTKTGPEFVAANPLWAGLPAVKNGRVYTL 230
|
|
| FecB |
COG4594 |
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ... |
61-291 |
1.03e-24 |
|
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443650 [Multi-domain] Cd Length: 316 Bit Score: 100.77 E-value: 1.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925900502 61 YKTLPNRYKDVPEIGQPMEPNVEAVKKLKPTHVLSVstiKDEMQPFYKQLN-------MKGYFYDFdslKGMQKSITQLG 133
Cdd:COG4594 86 VPYLRDLIKGVTSVGTRSQPNLEAIAALKPDLIIAD---KSRHEAIYDQLSkiaptvlFKSRNGDY---QENLESFKTIA 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925900502 134 DQFNRKAQAKE-LNDH---LNSVKQKIENKAAKQKkhpkVLILMGVPGSYLVATDKSYIGDLVKIAGGENVIKVKDRQ-- 207
Cdd:COG4594 160 KALGKEEEAEAvLADHdqrIAEAKAKLAAADKGKK----VAVGQFRADGLRLYTPNSFAGSVLAALGFENPPKQSKDNgy 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925900502 208 -YISSNTENLLNINPDIILRLPHGMPEevkkmFQKEFKQNDIWKHFKAVKNNHVYDLEEV--PFG---ITANVDADkamt 281
Cdd:COG4594 236 gYSEVSLEQLPALDPDVLFIATYDDPS-----ILKEWKNNPLWKNLKAVKNGRVYEVDGDlwTRGrgpLAAELMAD---- 306
|
250
....*....|
gi 925900502 282 QLYDLFYKDK 291
Cdd:COG4594 307 DLVEILLKKK 316
|
|
| YvrC |
cd01143 |
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ... |
35-225 |
1.26e-22 |
|
Periplasmic binding protein YvrC. These proteins are predicted to function as initial receptors in ABC transport of metal ions in eubacteria and archaea. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains.
Pssm-ID: 238563 [Multi-domain] Cd Length: 195 Bit Score: 92.34 E-value: 1.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925900502 35 RIVPTTVALTMTLDKLDL--PIVGKpTSYKTLPNRYKDVPEIGQPMEPNVEAVKKLKPTHVLSVSTIKDEMqpfYKQLNM 112
Cdd:cd01143 5 RIVSLSPSITEILFALGAgdKIVGV-DTYSNYPKEVRKKPKVGSYSNPNVEKIVALKPDLVIVSSSSLAEL---LEKLKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925900502 113 KG----YFYDFDSLKGMQKSITQLGDQFNRKAQAKELNDHLNSVKQKIEnKAAKQKKHPKVLILMGVPGSYlVATDKSYI 188
Cdd:cd01143 81 AGipvvVLPAASSLDEIYDQIELIGKITGAEEEAEKLVKEMKQKIDKVK-DKGKTIKKSKVYIEVSLGGPY-TAGKNTFI 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 925900502 189 GDLVKIAGGENVIKvKDRQYISSNTENLLNINPDIIL 225
Cdd:cd01143 159 NELIRLAGAKNIAA-DSGGWPQVSPEEILKANPDVII 194
|
|
| TroA_e |
cd01142 |
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ... |
35-270 |
1.13e-21 |
|
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial receptors in the ABC metal ion uptake in eubacteria and archaea. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.
Pssm-ID: 238562 [Multi-domain] Cd Length: 289 Bit Score: 92.03 E-value: 1.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925900502 35 RIVPTTVALTMTLDKLDLP--IVGKPTSYKTLPN------RYKDVPEIGQPMEPNVEAVKKLKPTHVLSVSTIKDEMQpf 106
Cdd:cd01142 26 RIAALWGAGNAVVAALGGGklIVATTSTVQQEPWlyrlapSLENVATGGTGNDVNIEELLALKPDVVIVWSTDGKEAG-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925900502 107 YKQLNMKGY-FYDFDSLKGMQKSITQLGDQFNRKAQAKELN----DHLNSVKQKIENKAAKQKkhPKVLILMGVPGSylV 181
Cdd:cd01142 104 KAVLRLLNAlSLRDAELEEVKLTIALLGELLGRQEKAEALVayfdDNLAYVAARTKKLPDSER--PRVYYAGPDPLT--T 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925900502 182 ATDKSYIGDLVKIAGGENVIKVK-DRQYISSNTENLLNINPDIILrLPHGMPEevkkmfqKEFKQNDIWKHFKAVKNNHV 260
Cdd:cd01142 180 DGTGSITNSWIDLAGGINVASEAtKKGSGEVSLEQLLKWNPDVII-VGNADTK-------AAILADPRWQNLRAVKNGRV 251
|
250
....*....|
gi 925900502 261 YdleEVPFGI 270
Cdd:cd01142 252 Y---VNPEGA 258
|
|
| FhuD |
cd01146 |
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ... |
35-278 |
4.89e-20 |
|
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial receptors in ABC transport of Fe3+-siderophores in many eubacterial species. They belong to the TroA-like superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA-like protein is comprised of two globular subdomains connected by a long alpha helix and binds its specific ligands in the cleft between these domains.
Pssm-ID: 238566 [Multi-domain] Cd Length: 256 Bit Score: 86.96 E-value: 4.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925900502 35 RIVPTTVALTMTLDKLDLPIVG------KPTSYKTLPNRYKDVPEIGQPMEPNVEAVKKLKPTHVLSVSTIKDEMqpfYK 108
Cdd:cd01146 5 RIVALDWGALETLLALGVKPVGvadtagYKPWIPEPALPLEGVVDVGTRGQPNLEAIAALKPDLILGSASRHDEI---YD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925900502 109 QLN-------MKGYFYDFDslkgMQKSITQLGDQFNRKAQAKEL----NDHLNSVKQKIENKAAKqkkhPKVLILMGVPG 177
Cdd:cd01146 82 QLSqiaptvlLDSSPWLAE----WKENLRLIAKALGKEEEAEKLlaeyDQRLAELRQKLPDKGPK----PVSVVRFSDAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925900502 178 SYLVATDKSYIGDLVKIAGGENVIKVK---DRQYISSNTENLLNINPDIILRLPHGMPEevkkmFQKEFKQNDIWKHFKA 254
Cdd:cd01146 154 SIRLYGPNSFAGSVLEDLGLQNPWAQEttnDSGFATISLERLAKADADVLFVFTYEDEE-----LAQALQANPLWQNLPA 228
|
250 260
....*....|....*....|....*...
gi 925900502 255 VKNNHVYDLEEVPF----GITANVDADK 278
Cdd:cd01146 229 VKNGRVYVVDDVWWffggGLSAARLLLD 256
|
|
| BtuF |
cd01144 |
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ... |
54-265 |
3.94e-18 |
|
Cobalamin binding protein BtuF. These proteins have been shown to function as initial receptors in ABC transport of vitamin B12 (cobalamin) in eubacterial and some archaeal species. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains. In addition, these proteins sometimes have a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence).
Pssm-ID: 238564 [Multi-domain] Cd Length: 245 Bit Score: 81.58 E-value: 3.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925900502 54 IVGKpTSYKTLPNRYKDVPEIGQPMEPNVEAVKKLKPTHVLSVSTIkdEMQPFYKQLNMKG---YFYDFDSLKGMQKSIT 130
Cdd:cd01144 23 LVGV-TDYCDYPPEAKKLPRVGGFYQLDLERVLALKPDLVIAWDDC--NVCAVVDQLRAAGipvLVSEPQTLDDILADIR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925900502 131 QLGDQFNRKAQAKELNdhlNSVKQKIEN--KAAKQKKHPKVLILMGV-PgsyLVATDKSYIGDLVKIAGGENVIKVKDRQ 207
Cdd:cd01144 100 RLGTLAGRPARAEELA---EALRRRLAAlrKQYASKPPPRVFYQEWIdP---LMTAGGDWVPELIALAGGVNVFADAGER 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 925900502 208 YISSNTENLLNINPDIILRLPHGmpeevKKMFQKEFKQNDIWKHFKAVKNNHVYDLEE 265
Cdd:cd01144 174 SPQVSWEDVLAANPDVIVLSPCG-----FGFTPAILRKEPAWQALPAVRNGRVYAVDG 226
|
|
| HemV-2 |
cd01147 |
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ... |
35-269 |
1.13e-17 |
|
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors in ABC transport of metal ions. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains. In addition, these proteins sometimes have a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence).
Pssm-ID: 238567 [Multi-domain] Cd Length: 262 Bit Score: 80.46 E-value: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925900502 35 RIVPT---TVALTMTLDKLDLpIVG---KPTS-----YKTLPNRYKDVPEIGQPM---EPNVEAVKKLKPTHVLSVST-- 98
Cdd:cd01147 7 RVVAAgpgALRLLYALAAPDK-IVGvddAEKSdegrpYFLASPELKDLPVIGRGGrgnTPNYEKIAALKPDVVIDVGSdd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925900502 99 ---IKDEMQpfyKQLNMKG-YFYDFDSLKGMQKSITQLGDQFNRKAQAKELNDHLNSVKQKIENKAAKQKKHPKVLILMG 174
Cdd:cd01147 86 ptsIADDLQ---KKTGIPVvVLDGGDSLEDTPEQIRLLGKVLGKEERAEELISFIESILADVEERTKDIPDEEKPTVYFG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925900502 175 VPGSY----LVATDKSYIGDLVkIAGGENVIKVKDRQYISS-NTENLLNINPDIILRLPHGMPEEVKKmfqkEFKQNDIW 249
Cdd:cd01147 163 RIGTKgaagLESGLAGSIEVFE-LAGGINVADGLGGGGLKEvSPEQILLWNPDVIFLDTGSFYLSLEG----YAKNRPFW 237
|
250 260
....*....|....*....|
gi 925900502 250 KHFKAVKNNHVYDLEEVPFG 269
Cdd:cd01147 238 QSLKAVKNGRVYLLPALPFN 257
|
|
| TroA_f |
cd01139 |
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ... |
67-263 |
6.00e-17 |
|
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial receptors in the ABC metal ion uptake in eubacteria and archaea. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.
Pssm-ID: 238559 [Multi-domain] Cd Length: 342 Bit Score: 79.66 E-value: 6.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925900502 67 RYKDVPEIGQPMEP--NVEAVKKLKPTHVLSVSTIKD-----EMQPFYKQLNMKGYFYDF--DSLKGMQKSITQLGDQFN 137
Cdd:cd01139 67 EIADIPLIGSTYNGdfSVEKVLTLKPDLVILNIWAKTtaeesGILEKLEQAGIPVVFVDFrqKPLKNTTPSMRLLGKALG 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925900502 138 RKAQAKELNDHLNSVKQKIENKAAKQK-KHPKVLILMGVPGS--YLVATDKSYIGDLVKIAGGENVIK-VKDRQYISSNT 213
Cdd:cd01139 147 REERAEEFIEFYQERIDRIRDRLAKINePKPKVFIELGAGGPeeCCSTYGNGNWGELVDAAGGDNIADgLIPGTSGELNA 226
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 925900502 214 ENLLNINPDIILR--------------LPHGMPEEVKKMFQKEFKQNDIWKHFKAVKNNHVYDL 263
Cdd:cd01139 227 EYVIAANPEIIIAtggnwakdpsgvslGPDGTTADAKESLLRALLKRPGWSSLQAVKNGRVYAL 290
|
|
| TroA-like |
cd00636 |
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ... |
35-173 |
1.27e-13 |
|
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function in the ABC transport of ferric siderophores and metal ions such as Mn2+, Fe3+, Cu2+ and/or Zn2+. Their ligand binding site is formed in the interface between two globular domains linked by a single helix. Many of these proteins also possess a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence). The TroA-like proteins differ in their fold and ligand-binding mechanism from the PBPI and PBPII proteins, but are structurally similar, however, to the beta-subunit of the nitrogenase molybdenum-iron protein MoFe. Most TroA-like proteins are encoded by ABC-type operons and appear to function as periplasmic components of ABC transporters in metal ion uptake.
Pssm-ID: 238347 [Multi-domain] Cd Length: 148 Bit Score: 66.81 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925900502 35 RIVPTTVALTMTLDKLDL--PIVG---KPTSYKTLPNRYKDVPEIGQPMEPNVEAVKKLKPTHVLSVSTIKDEMQPFYKQ 109
Cdd:cd00636 2 RVVALDPGATELLLALGGddKPVGvadPSGYPPEAKALLEKVPDVGHGYEPNLEKIAALKPDLIIANGSGLEAWLDKLSK 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 925900502 110 LNMKGYFYDFD---SLKGMQKSITQLGDQFNRKAQAKELNDHLNSVKQKIENKAAKQKKHPKVLILM 173
Cdd:cd00636 82 IAIPVVVVDEAselSLENIKESIRLIGKALGKEENAEELIAELDARLAELRAKLAKIPKKKVSLVVG 148
|
|
| FeuA |
cd01138 |
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ... |
43-268 |
6.36e-12 |
|
Periplasmic binding protein FeuA. These proteins have predicted to function as initial receptors in ABC transport of metal ions in some eubacterial species. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.
Pssm-ID: 238558 [Multi-domain] Cd Length: 248 Bit Score: 64.28 E-value: 6.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925900502 43 LTMTLDKLDLPIVGKPTSYKTLPNRYKDVP--EIGQPMEPNVEAVKKLKPTHVLSVSTIKDEmqpfYKQLN--MKGYFYD 118
Cdd:cd01138 18 ETEGLALLGIKPVGAASIGGKNPYYKKKTLakVVGIVDEPNLEKVLELKPDLIIVSSKQEEN----YEKLSkiAPTVPVS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925900502 119 FDSlKGMQKSITQLGDQFNRKAQAKE-LNDH---LNSVKQKIENKAAKQKKhpkVLILMGVPGSYLVATDKSYIGDLVKI 194
Cdd:cd01138 94 YNS-SDWEEQLKEIGKLLNKEDEAEKwLADYkqkAKEAKEKIKKKLGNDKS---VAVLRGRKQIYVFGEDGRGGGPILYA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925900502 195 AGG-------ENVIKVKDRQYISSntENLLNINPDIILRLPHGMPEEvkkmfQKEFKQNDIWKHFKAVKNNHVY--DLEE 265
Cdd:cd01138 170 DLGlkapekvKEIEDKPGYAAISL--EVLPEFDADYIFLLFFTGPEA-----KADFESLPIWKNLPAVKNNHVYivDAWV 242
|
...
gi 925900502 266 VPF 268
Cdd:cd01138 243 FYF 245
|
|
| TroA_a |
cd01148 |
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ... |
35-276 |
5.35e-11 |
|
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors in ABC transport of metal ions in eubacteria. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains.
Pssm-ID: 238568 [Multi-domain] Cd Length: 284 Bit Score: 61.97 E-value: 5.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925900502 35 RIVPTTVALTMTLDKLDLP--IVGKPTSYK----TLPNRYKDVPEIGqPMEPNVEAVKKLKP-------------THVLS 95
Cdd:cd01148 20 RVVSNDQNTTEMMLALGLQdrMVGTAGIDNkdlpELKAKYDKVPELA-KKYPSKETVLAARPdlvfggwsygfdkGGLGT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925900502 96 VSTIKDEMQPFYKQLNMKGYFYDFDSLKGMQKSITQLGDQFNRKAQAKELNDHLNSVKQKIENKAAKQKKHPKVLIlmgv 175
Cdd:cd01148 99 PDSLAELGIKTYILPESCGQRRGEATLDDVYNDIRNLGKIFDVEDRADKLVADLKARLAEISAKVKGDGKKVAVFV---- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925900502 176 pgsYLVATDKSYI-------GDLVKIAGGENVIKVKDRQYISSNTENLLNINPDIILRLPHGMPEEVKKMfQKEFKQNDI 248
Cdd:cd01148 175 ---YDSGEDKPFTsgrggipNAIITAAGGRNVFADVDESWTTVSWETVIARNPDVIVIIDYGDQNAAEQK-IKFLKENPA 250
|
250 260 270
....*....|....*....|....*....|
gi 925900502 249 WKHFKAVKNNH--VYDLEEVPFGItANVDA 276
Cdd:cd01148 251 LKNVPAVKNNRfiVLPLAEATPGI-RNVDA 279
|
|
| HutB |
cd01149 |
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ... |
35-225 |
7.88e-11 |
|
Hemin binding protein HutB. These proteins have been shown to function as initial receptors in ABC transport of hemin and hemoproteins in many eubacterial species. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains.
Pssm-ID: 238569 [Multi-domain] Cd Length: 235 Bit Score: 60.74 E-value: 7.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925900502 35 RIVPTTVALTMTLDKLDLP--IVGKPTSyKTLPNRYKDVPEIGQPMEPNVEAVKKLKPTHVLSVstikDEMQP--FYKQL 110
Cdd:cd01149 3 RIVSLGGSVTEIVYALGAGdrLVGVDST-STYPEAAAKLPDVGYMRQLSAEGVLSLKPTLVIAS----DEAGPpeALDQL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925900502 111 NMKG----YFYDFDSLKGMQKSITQLGDQFNRKAQAKELndhLNSVKQKIE---NKAAKQKKHPKVLILMGVPGSYLVAT 183
Cdd:cd01149 78 RAAGvpvvTVPSTPTLDGLLTKIRQVAQALGVPEKGEAL---AQEVRQRLAalrKTVAAHKKPPRVLFLLSHGGGAAMAA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 925900502 184 DKSYIGD-LVKIAGGENVIKvKDRQYISSNTENLLNINPDIIL 225
Cdd:cd01149 155 GRNTAADaIIALAGAVNAAA-GFRGYKPLSAEALIAAQPDVIL 196
|
|
| btuF |
PRK09534 |
corrinoid ABC transporter substrate-binding protein; Reviewed |
75-225 |
3.76e-09 |
|
corrinoid ABC transporter substrate-binding protein; Reviewed
Pssm-ID: 236552 [Multi-domain] Cd Length: 359 Bit Score: 56.84 E-value: 3.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925900502 75 GQPMEPNVEAVKKLKPTHVLSVSTIKDEMQPFYKQLNMKGYFYDF-DSLKGMQKSITQLGDQFNRKAQAKELNDHLNSVK 153
Cdd:PRK09534 105 GQPFGVNVEAVVGLDPDLVLAPNAVAGDTVTRLREAGITVFHFPAaTSIEDVAEKTATIGRLTGNCEAAAETNAEMRDRV 184
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 925900502 154 QKIENKAAKQKKHPKVLILMGvpGSYlVATDKSYIGDLVKIAGGENVIKVKD-RQYISSNTENLLNINPDIIL 225
Cdd:PRK09534 185 DAVEDRTADVDDRPRVLYPLG--DGY-TAGGNTFIGALIEAAGGHNVAADATtDGYPQLSEEVIVQQDPDVIV 254
|
|
| TroA_d |
cd01141 |
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ... |
35-197 |
4.80e-09 |
|
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial receptors in the ABC metal ion uptake in eubacteria and archaea. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.
Pssm-ID: 238561 [Multi-domain] Cd Length: 186 Bit Score: 54.73 E-value: 4.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925900502 35 RIV---PTTVALTMTLDKLDlPIVGKPTSYKTLPN---RYKDVPEIGQPMEPNVEAVKKLKPTHV-LSVSTIKDEMQPFY 107
Cdd:cd01141 10 RIVvlsPTHVDLLLALDKAD-KIVGVSASAYDLNTpavKERIDIQVGPTGSLNVELIVALKPDLViLYGGFQAQTILDKL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925900502 108 KQLNMK-GYFYDFDSLKGMQKSITQLGDQFNRKAQAK--ELNDHLNSVKQKIENKAAKQKKhPKVLILMGVPGSYLVATD 184
Cdd:cd01141 89 EQLGIPvLYVNEYPSPLGRAEWIKFAAAFYGVGKEDKadEAFAQIAGRYRDLAKKVSNLNK-PTVAIGKPVKGLWYMPGG 167
|
170
....*....|...
gi 925900502 185 KSYIGDLVKIAGG 197
Cdd:cd01141 168 NSYVAKMLRDAGG 180
|
|
| PRK10957 |
PRK10957 |
iron-enterobactin transporter periplasmic binding protein; Provisional |
35-263 |
2.23e-05 |
|
iron-enterobactin transporter periplasmic binding protein; Provisional
Pssm-ID: 236806 [Multi-domain] Cd Length: 317 Bit Score: 45.35 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925900502 35 RIVPTTVALTMTLDKLDLPIVGkptSYKTLPN-----------RYKDVPE--------IGqpmEPNVEAVKKLKPTHVLS 95
Cdd:PRK10957 46 RIVSTSVTLTGTLLAIDAPVIA---SGATTPNtrvaddqgffrQWSDVAKergvevlyIG---EPDAEAVAAQMPDLIVI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925900502 96 VSTIKDEMQPFYKQLNMKG--YFYDFDSlKGMQKSITQLGDQFNRKAQA----KELNDHLNSVKQKIenKAAKQKKhpKV 169
Cdd:PRK10957 120 SATGGDSALALYDQLSAIAptLVIDYDD-KSWQELATQLGEATGLEKQAaaviAQFDAQLAEVKAKI--TLPPQPV--SA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925900502 170 LILMGVPGSYLVATDKSYIGDLVK------------IAGGENVIKVKDRQYISSntENLL-NINPDIILRLPhGMPEEVK 236
Cdd:PRK10957 195 LVYNGAGHSANLWTPESAQGQLLEqlgftlaelpagLQASTSQGKRHDIIQLGG--ENLAaGLNGETLFLFA-GDDKDAD 271
|
250 260
....*....|....*....|....*..
gi 925900502 237 KmfqkeFKQNDIWKHFKAVKNNHVYDL 263
Cdd:PRK10957 272 A-----FLADPLLANLPAVQNKQVYAL 293
|
|
| fecB |
PRK11411 |
iron-dicitrate transporter substrate-binding subunit; Provisional |
65-277 |
1.65e-04 |
|
iron-dicitrate transporter substrate-binding subunit; Provisional
Pssm-ID: 183123 [Multi-domain] Cd Length: 303 Bit Score: 42.35 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925900502 65 PNR-YKDVPEIGQPME-------PNVEAVKKLKPTHVLSVS----TIKDEMQPFYKQLNMK--GYFYDfDSLKGMQKsit 130
Cdd:PRK11411 69 AKRiLPEVRAHLKPWQsvgtrsqPSLEAIAALKPDLIIADSsrhaGVYIALQKIAPTLLLKsrNETYQ-ENLQSAAI--- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925900502 131 qLGDQFNRKAQAK-ELNDHlnsvKQKIENKAAKQKKHPKVLILMGVPGSYLVATDKSYIGDLVKIAGGENVIKVKDRQ-Y 208
Cdd:PRK11411 145 -IGEVLGKKREMQaRIEQH----KERMAQFASQLPKGTRVAFGTSREQQFNLHSPESYTGSVLAALGLNVPKAPMNGAaM 219
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 925900502 209 ISSNTENLLNINPDIILRLPHGMPEEVKKmfqkeFKQNDIWKHFKAVKNNHVydleevpfgitANVDAD 277
Cdd:PRK11411 220 PSISLEQLLALNPDWLLVAHYRQESIVKR-----WQQDPLWQMLTAAKKQQV-----------ASVDSN 272
|
|
| |
