|
Name |
Accession |
Description |
Interval |
E-value |
| CeuA |
COG4607 |
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and ... |
1-303 |
1.13e-85 |
|
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443657 [Multi-domain] Cd Length: 310 Bit Score: 259.73 E-value: 1.13e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582490333 1 MKKIFQ-IMTLTATLAIAAPSLA------------FELEHTTGTINGDKTPERIVSYDLSILDSLNALGIEAVGVPKSNY 67
Cdd:COG4607 1 MKKTLLaALALAAALALAACGSSsaaaasaaaaetVTVEHALGTVEVPKNPKRVVVFDNGALDTLDALGVEVAGVPKGLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582490333 68 KDELAKFA--EAPKVGTLFEPDYEALKALKPDLIFAGGRSASAIPELEKIAPVANLTNRNPEFLADFRTNTLRLAAAFDK 145
Cdd:COG4607 81 PDYLSKYAddKYANVGTLFEPDLEAIAALKPDLIIIGGRSAKKYDELSKIAPTIDLTVDGEDYLESLKRNTETLGEIFGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582490333 146 TKKAEEGLSNIDKDIADLQKLNAGK-TGAFLFVMNGNIIPHVVGDRFGFVYELTGLesvlpaKTAEELAAPATRPAPDSP 224
Cdd:COG4607 161 EDEAEELVADLDAKIAALKAAAAGKgTALIVLTNGGKISAYGPGSRFGPIHDVLGF------KPADEDIEASTHGQAISF 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2582490333 225 EakaaaakraqqikAIAKADPDWLIVFDRAAINGGENAGEKTLAEHPDLSQTSAFKNGRVVYVDPVRWYVITGGLNNLK 303
Cdd:COG4607 235 E-------------FIAEANPDWLFVIDRDAAIGGEGPAAKQVLDNELVKQTTAWKNGQIVYLDPDAWYLAGGGIQSLT 300
|
|
| FatB |
cd01140 |
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ... |
27-303 |
1.12e-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: 199.79 E-value: 1.12e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582490333 27 HTTGTINGDKTPERIVSYDLSILDSLNALGIEAVGVPKSN---YKDELAKFAEAPKVGTLFEPDYEALKALKPDLIFAGG 103
Cdd:cd01140 1 HALGETKVPKNPEKVVVFDVGALDTLDALGVKVVGVPKSStlpEYLKKYKDDKYANVGTLFEPDLEAIAALKPDLIIIGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582490333 104 RSASAIPELEKIAPVANLTNRNPEFLADFRTNTLRLAAAFDKTKKAEEGLSNIDKDIADLQKLNAGK-TGAFLFVMNGNI 182
Cdd:cd01140 81 RLAEKYDELKKIAPTIDLGADLKNYLESVKQNIETLGKIFGKEEEAKELVAEIDASIAEAKSAAKGKkKALVVLVNGGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582490333 183 IPHVVGDRFGFVYELTGLESVLpaktaeELAAPATRPAPDSPEakaaaakraqqikAIAKADPDWLIVFDRAAINGGENA 262
Cdd:cd01140 161 SAFGPGSRFGWLHDLLGFEPAD------ENIKASSHGQPVSFE-------------YILEANPDWLFVIDRGAAIGAEGS 221
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2582490333 263 GEKTLAEHPDLSQTSAFKNGRVVYVDPVRWYVITGGLNNLK 303
Cdd:cd01140 222 SAKEVLDNDLVKNTTAWKNGKVIYLDPDLWYLSGGGLESLK 262
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
42-289 |
2.19e-23 |
|
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: 95.90 E-value: 2.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582490333 42 VSYDLSILDSLNALGIEA--VGVPKSNYKDELAKFAEA-PKVGTLFEPDYEALKALKPDLIFAGGR--SASAIPELEKIA 116
Cdd:pfam01497 1 AALSPAYTEILYALGATDsiVGVDAYTRDPLKADAVAAiVKVGAYGEINVERLAALKPDLVILSTGylTDEAEELLSLII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582490333 117 PVanLTNRNPEFLADFRTNTLRLAAAFDKTKKAEEGLSNIDKDIADLQKLNAGKTG--AFLFVMNGNIIPHVVGD--RFG 192
Cdd:pfam01497 81 PT--VIFESSSTGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRkpVLVFGGADGGGYVVAGSntYIG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582490333 193 FVYELTGLESVLPAKTAEElAAPAtrpapdSPEakaaaakraqqikAIAKADPDWLIVFDRAAINggeNAGEKTLAEHPD 272
Cdd:pfam01497 159 DLLRILGIENIAAELSGSE-YAPI------SFE-------------AILSSNPDVIIVSGRDSFT---KTGPEFVAANPL 215
|
250
....*....|....*..
gi 2582490333 273 LSQTSAFKNGRVVYVDP 289
Cdd:pfam01497 216 WAGLPAVKNGRVYTLPS 232
|
|
| fecB |
PRK11411 |
iron-dicitrate transporter substrate-binding subunit; Provisional |
3-292 |
1.08e-17 |
|
iron-dicitrate transporter substrate-binding subunit; Provisional
Pssm-ID: 183123 [Multi-domain] Cd Length: 303 Bit Score: 81.64 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582490333 3 KIFQIMTLTATLAIAAPSLAFEL----EHTTGTIngDKTPERIVSYDLSILDSLNALGIEAVGVPKSNYKDE-LAKFAEA 77
Cdd:PRK11411 2 LAFIRLLFAGLLLLSGSSHAFAVtvqdEQGTFTL--EKTPQRIVVLELSFVDALAAVGVSPVGVADDNDAKRiLPEVRAH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582490333 78 PK----VGTLFEPDYEALKALKPDLIFA-GGRSASAIPELEKIAPVANLTNRNPEFLADFRTnTLRLAAAFDKTKKAEEG 152
Cdd:PRK11411 80 LKpwqsVGTRSQPSLEAIAALKPDLIIAdSSRHAGVYIALQKIAPTLLLKSRNETYQENLQS-AAIIGEVLGKKREMQAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582490333 153 LSNIDKDIADL-QKLNAGKTGAFLFVMNGNIIPHVVGDRFGFVYELTGLESVLPAKTAEELaapatrpAPDSPEakaaaa 231
Cdd:PRK11411 159 IEQHKERMAQFaSQLPKGTRVAFGTSREQQFNLHSPESYTGSVLAALGLNVPKAPMNGAAM-------PSISLE------ 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2582490333 232 kraqQIKAIakaDPDWLIV--FDRAAInggenagEKTLAEHPDLSQTSAFKNGRVVYVDPVRW 292
Cdd:PRK11411 226 ----QLLAL---NPDWLLVahYRQESI-------VKRWQQDPLWQMLTAAKKQQVASVDSNTW 274
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CeuA |
COG4607 |
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and ... |
1-303 |
1.13e-85 |
|
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443657 [Multi-domain] Cd Length: 310 Bit Score: 259.73 E-value: 1.13e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582490333 1 MKKIFQ-IMTLTATLAIAAPSLA------------FELEHTTGTINGDKTPERIVSYDLSILDSLNALGIEAVGVPKSNY 67
Cdd:COG4607 1 MKKTLLaALALAAALALAACGSSsaaaasaaaaetVTVEHALGTVEVPKNPKRVVVFDNGALDTLDALGVEVAGVPKGLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582490333 68 KDELAKFA--EAPKVGTLFEPDYEALKALKPDLIFAGGRSASAIPELEKIAPVANLTNRNPEFLADFRTNTLRLAAAFDK 145
Cdd:COG4607 81 PDYLSKYAddKYANVGTLFEPDLEAIAALKPDLIIIGGRSAKKYDELSKIAPTIDLTVDGEDYLESLKRNTETLGEIFGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582490333 146 TKKAEEGLSNIDKDIADLQKLNAGK-TGAFLFVMNGNIIPHVVGDRFGFVYELTGLesvlpaKTAEELAAPATRPAPDSP 224
Cdd:COG4607 161 EDEAEELVADLDAKIAALKAAAAGKgTALIVLTNGGKISAYGPGSRFGPIHDVLGF------KPADEDIEASTHGQAISF 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2582490333 225 EakaaaakraqqikAIAKADPDWLIVFDRAAINGGENAGEKTLAEHPDLSQTSAFKNGRVVYVDPVRWYVITGGLNNLK 303
Cdd:COG4607 235 E-------------FIAEANPDWLFVIDRDAAIGGEGPAAKQVLDNELVKQTTAWKNGQIVYLDPDAWYLAGGGIQSLT 300
|
|
| FatB |
cd01140 |
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ... |
27-303 |
1.12e-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: 199.79 E-value: 1.12e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582490333 27 HTTGTINGDKTPERIVSYDLSILDSLNALGIEAVGVPKSN---YKDELAKFAEAPKVGTLFEPDYEALKALKPDLIFAGG 103
Cdd:cd01140 1 HALGETKVPKNPEKVVVFDVGALDTLDALGVKVVGVPKSStlpEYLKKYKDDKYANVGTLFEPDLEAIAALKPDLIIIGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582490333 104 RSASAIPELEKIAPVANLTNRNPEFLADFRTNTLRLAAAFDKTKKAEEGLSNIDKDIADLQKLNAGK-TGAFLFVMNGNI 182
Cdd:cd01140 81 RLAEKYDELKKIAPTIDLGADLKNYLESVKQNIETLGKIFGKEEEAKELVAEIDASIAEAKSAAKGKkKALVVLVNGGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582490333 183 IPHVVGDRFGFVYELTGLESVLpaktaeELAAPATRPAPDSPEakaaaakraqqikAIAKADPDWLIVFDRAAINGGENA 262
Cdd:cd01140 161 SAFGPGSRFGWLHDLLGFEPAD------ENIKASSHGQPVSFE-------------YILEANPDWLFVIDRGAAIGAEGS 221
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2582490333 263 GEKTLAEHPDLSQTSAFKNGRVVYVDPVRWYVITGGLNNLK 303
Cdd:cd01140 222 SAKEVLDNDLVKNTTAWKNGKVIYLDPDLWYLSGGGLESLK 262
|
|
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
40-305 |
1.60e-34 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 126.27 E-value: 1.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582490333 40 RIVSYDLSILDSLNALGIEA--VGVPKSNYKDELA-KFAEAPKVGTLFEPDYEALKALKPDLIFAG--GRSASAIPELEK 114
Cdd:COG0614 2 RIVSLSPSATELLLALGAGDrlVGVSDWGYCDYPElELKDLPVVGGTGEPNLEAILALKPDLVLASssGNDEEDYEQLEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582490333 115 I-APVANLtnrNPEFLADFRTNTLRLAAAFDKTKKAEEGLSNIDKDIADLQKLNAGKTG---AFLFVMNGNIIpHVVGDR 190
Cdd:COG0614 82 IgIPVVVL---DPRSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGAEErptVLYEIWSGDPL-YTAGGG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582490333 191 --FGFVYELTGLESVlpaktaeelAAPATRPAPD-SPEakaaaakraqqikAIAKADPDWLIVFDRAAINGGENAGEKTL 267
Cdd:COG0614 158 sfIGELLELAGGRNV---------AADLGGGYPEvSLE-------------QVLALDPDVIILSGGGYDAETAEEALEAL 215
|
250 260 270
....*....|....*....|....*....|....*...
gi 2582490333 268 AEHPDLSQTSAFKNGRVVYVDPVRWYviTGGLNNLKFL 305
Cdd:COG0614 216 LADPGWQSLPAVKNGRVYVVPGDLLS--RPGPRLLLAL 251
|
|
| FhuD |
cd01146 |
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ... |
36-293 |
2.19e-31 |
|
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: 117.77 E-value: 2.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582490333 36 KTPERIVSYDLSILDSLNALGIEAVGVPKSN-----YKDELAKFAEAPKVGTLFEPDYEALKALKPDLIFA-GGRSASAI 109
Cdd:cd01146 1 AKPQRIVALDWGALETLLALGVKPVGVADTAgykpwIPEPALPLEGVVDVGTRGQPNLEAIAALKPDLILGsASRHDEIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582490333 110 PELEKIAPVANLTNRNPefLADFRTNTLRLAAAFDKTKKAEEGLSNIDKDIADL-QKL--NAGKTGAFLFVM-NGNIIPH 185
Cdd:cd01146 81 DQLSQIAPTVLLDSSPW--LAEWKENLRLIAKALGKEEEAEKLLAEYDQRLAELrQKLpdKGPKPVSVVRFSdAGSIRLY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582490333 186 VVGDRFGFVYELTGLEsvLPAKTAEELAAPAtrpAPDSPEakaaaakraqqikAIAKADPDWLIVFDRAAinggeNAGEK 265
Cdd:cd01146 159 GPNSFAGSVLEDLGLQ--NPWAQETTNDSGF---ATISLE-------------RLAKADADVLFVFTYED-----EELAQ 215
|
250 260
....*....|....*....|....*...
gi 2582490333 266 TLAEHPDLSQTSAFKNGRVVYVDPVRWY 293
Cdd:cd01146 216 ALQANPLWQNLPAVKNGRVYVVDDVWWF 243
|
|
| FecB |
COG4594 |
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ... |
1-292 |
7.00e-29 |
|
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443650 [Multi-domain] Cd Length: 316 Bit Score: 112.71 E-value: 7.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582490333 1 MKKI-FQIMTLTATLAIAAPSL-------------AFELEHTTGTINGDKTPERIVSYDLSILDSLNALGIEAVGVPKSN 66
Cdd:COG4594 1 MKKLlLLLILLLALLLLAACGSsssdsssseaaagARTVKHAMGETTIPGTPKRVVVLEWSFADALLALGVTPVGIADDN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582490333 67 YKD----ELAKFAEAPK-VGTLFEPDYEALKALKPDLIFA-GGRSASAIPELEKIAPVANLTNRN---PEFLADFRTntl 137
Cdd:COG4594 81 DYDrwvpYLRDLIKGVTsVGTRSQPNLEAIAALKPDLIIAdKSRHEAIYDQLSKIAPTVLFKSRNgdyQENLESFKT--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582490333 138 rLAAAFDKTKKAEEGLSNIDKDIAD----LQKLNAGKTGAFLFVMNGNIIPHVVGDRFGFVYELTGLESVLPAKTAEELA 213
Cdd:COG4594 158 -IAKALGKEEEAEAVLADHDQRIAEakakLAAADKGKKVAVGQFRADGLRLYTPNSFAGSVLAALGFENPPKQSKDNGYG 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2582490333 214 APATrpapdSPEakaaaakraqqikAIAKADPDWLIVFdraaiNGGENAGEKTLAEHPDLSQTSAFKNGRVVYVDPVRW 292
Cdd:COG4594 237 YSEV-----SLE-------------QLPALDPDVLFIA-----TYDDPSILKEWKNNPLWKNLKAVKNGRVYEVDGDLW 292
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
42-289 |
2.19e-23 |
|
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: 95.90 E-value: 2.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582490333 42 VSYDLSILDSLNALGIEA--VGVPKSNYKDELAKFAEA-PKVGTLFEPDYEALKALKPDLIFAGGR--SASAIPELEKIA 116
Cdd:pfam01497 1 AALSPAYTEILYALGATDsiVGVDAYTRDPLKADAVAAiVKVGAYGEINVERLAALKPDLVILSTGylTDEAEELLSLII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582490333 117 PVanLTNRNPEFLADFRTNTLRLAAAFDKTKKAEEGLSNIDKDIADLQKLNAGKTG--AFLFVMNGNIIPHVVGD--RFG 192
Cdd:pfam01497 81 PT--VIFESSSTGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRkpVLVFGGADGGGYVVAGSntYIG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582490333 193 FVYELTGLESVLPAKTAEElAAPAtrpapdSPEakaaaakraqqikAIAKADPDWLIVFDRAAINggeNAGEKTLAEHPD 272
Cdd:pfam01497 159 DLLRILGIENIAAELSGSE-YAPI------SFE-------------AILSSNPDVIIVSGRDSFT---KTGPEFVAANPL 215
|
250
....*....|....*..
gi 2582490333 273 LSQTSAFKNGRVVYVDP 289
Cdd:pfam01497 216 WAGLPAVKNGRVYTLPS 232
|
|
| TroA-like |
cd00636 |
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ... |
39-180 |
1.59e-19 |
|
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: 83.38 E-value: 1.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582490333 39 ERIVSYDLSILDSLNALGIEA--VGVPKSNYKDELAKFA--EAPKVGTLFEPDYEALKALKPDLIFAGGRSASAIPE-LE 113
Cdd:cd00636 1 KRVVALDPGATELLLALGGDDkpVGVADPSGYPPEAKALleKVPDVGHGYEPNLEKIAALKPDLIIANGSGLEAWLDkLS 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2582490333 114 KIA-PVANLTNRNPEFLADFRTNTLRLAAAFDKTKKAEEGLSNIDKDIADLQKLNAGKTGAFLFVMNG 180
Cdd:cd00636 81 KIAiPVVVVDEASELSLENIKESIRLIGKALGKEENAEELIAELDARLAELRAKLAKIPKKKVSLVVG 148
|
|
| fecB |
PRK11411 |
iron-dicitrate transporter substrate-binding subunit; Provisional |
3-292 |
1.08e-17 |
|
iron-dicitrate transporter substrate-binding subunit; Provisional
Pssm-ID: 183123 [Multi-domain] Cd Length: 303 Bit Score: 81.64 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582490333 3 KIFQIMTLTATLAIAAPSLAFEL----EHTTGTIngDKTPERIVSYDLSILDSLNALGIEAVGVPKSNYKDE-LAKFAEA 77
Cdd:PRK11411 2 LAFIRLLFAGLLLLSGSSHAFAVtvqdEQGTFTL--EKTPQRIVVLELSFVDALAAVGVSPVGVADDNDAKRiLPEVRAH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582490333 78 PK----VGTLFEPDYEALKALKPDLIFA-GGRSASAIPELEKIAPVANLTNRNPEFLADFRTnTLRLAAAFDKTKKAEEG 152
Cdd:PRK11411 80 LKpwqsVGTRSQPSLEAIAALKPDLIIAdSSRHAGVYIALQKIAPTLLLKSRNETYQENLQS-AAIIGEVLGKKREMQAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582490333 153 LSNIDKDIADL-QKLNAGKTGAFLFVMNGNIIPHVVGDRFGFVYELTGLESVLPAKTAEELaapatrpAPDSPEakaaaa 231
Cdd:PRK11411 159 IEQHKERMAQFaSQLPKGTRVAFGTSREQQFNLHSPESYTGSVLAALGLNVPKAPMNGAAM-------PSISLE------ 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2582490333 232 kraqQIKAIakaDPDWLIV--FDRAAInggenagEKTLAEHPDLSQTSAFKNGRVVYVDPVRW 292
Cdd:PRK11411 226 ----QLLAL---NPDWLLVahYRQESI-------VKRWQQDPLWQMLTAAKKQQVASVDSNTW 274
|
|
| ChuT |
COG4558 |
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ... |
1-289 |
1.46e-17 |
|
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443619 [Multi-domain] Cd Length: 285 Bit Score: 81.01 E-value: 1.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582490333 1 MKKIFQIMTLTATLAIAAPSLAFElehttgtingdKTPERIVSYDLSILDSLNALGIEA--VGVPK-SNYKDELAKfaeA 77
Cdd:COG4558 1 MKRLALALLLLALAALAAGASVAA-----------AAAERIVSLGGSVTEIVYALGAGDrlVGVDTtSTYPAAAKA---L 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582490333 78 PKVGTLFEPDYEALKALKPDLIFAggrSASAIPE--LEKIA----PVANLTNRNPefLADFRTNTLRLAAAFDKTKKAEE 151
Cdd:COG4558 67 PDVGYMRQLSAEGILSLKPTLVLA---SEGAGPPevLDQLRaagvPVVVVPAAPS--LEGVLAKIRAVAAALGVPEAGEA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582490333 152 GLSNIDKDIADLQKLNAGKTGA--FLFVMN-GNIIPHVVGDRfgfvyelTGLESVLPAKTAEELAAPATRPAPDSPEaka 228
Cdd:COG4558 142 LAARLEADLAALAARVAAIGKPprVLFLLSrGGGRPMVAGRG-------TAADALIRLAGGVNAAAGFEGYKPLSAE--- 211
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2582490333 229 aaakraqqikAIAKADPDWLIVFDRaainGGENAG-EKTLAEHPDLSQTSAFKNGRVVYVDP 289
Cdd:COG4558 212 ----------ALIAAAPDVILVMTR----GLESLGgVDGLLALPGLAQTPAGKNKRIVAMDD 259
|
|
| YvrC |
cd01143 |
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ... |
36-250 |
1.13e-14 |
|
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: 71.16 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582490333 36 KTPERIVSYDLSILDSLNALGIE--AVGVPK-SNYKDELAKfaeAPKVGTLFEPDYEALKALKPDLIFA-GGRSASAIPE 111
Cdd:cd01143 1 KEPERIVSLSPSITEILFALGAGdkIVGVDTySNYPKEVRK---KPKVGSYSNPNVEKIVALKPDLVIVsSSSLAELLEK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582490333 112 LEKIA-PVANLtnRNPEFLADFRTNTLRLAAAFDKTKKAEEGLSNIDKDIADLQKLNAGKTGAFLFVMNGNIIPHVVGDR 190
Cdd:cd01143 78 LKDAGiPVVVL--PAASSLDEIYDQIELIGKITGAEEEAEKLVKEMKQKIDKVKDKGKTIKKSKVYIEVSLGGPYTAGKN 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2582490333 191 --FGFVYELTGLESVLPAKTaeelaapaTRPAPdSPEakaaaakraqqikAIAKADPDWLIV 250
Cdd:cd01143 156 tfINELIRLAGAKNIAADSG--------GWPQV-SPE-------------EILKANPDVIIL 195
|
|
| FeuA |
cd01138 |
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ... |
36-289 |
5.65e-14 |
|
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: 70.44 E-value: 5.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582490333 36 KTPERIV-SYDLSILDSLnaLGIEAVGVPKSNYKDELAKFAEAPKVGTL-FEPDYEALKALKPDLIFAGGRSASAIPELE 113
Cdd:cd01138 7 AKPKRIVaLSGETEGLAL--LGIKPVGAASIGGKNPYYKKKTLAKVVGIvDEPNLEKVLELKPDLIIVSSKQEENYEKLS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582490333 114 KIAPVANLTNRNpeflADFRTNTLRLAAAFDKTKKAEEGLSNIDKDIADLQKLNAGKTGAF--LFVMNGNIIPHVVGDRF 191
Cdd:cd01138 85 KIAPTVPVSYNS----SDWEEQLKEIGKLLNKEDEAEKWLADYKQKAKEAKEKIKKKLGNDksVAVLRGRKQIYVFGEDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582490333 192 GF----VYELTGLESvlPAKTAEELAAPATrpAPDSPEakaaaakraqqikAIAKADPDWLIVFDraainggeNAGEKTL 267
Cdd:cd01138 161 RGggpiLYADLGLKA--PEKVKEIEDKPGY--AAISLE-------------VLPEFDADYIFLLF--------FTGPEAK 215
|
250 260
....*....|....*....|....*
gi 2582490333 268 AEHPDLS---QTSAFKNGRVVYVDP 289
Cdd:cd01138 216 ADFESLPiwkNLPAVKNNHVYIVDA 240
|
|
| TroA_d |
cd01141 |
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ... |
36-166 |
2.32e-10 |
|
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: 58.97 E-value: 2.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582490333 36 KTPERIVSYDLSILDSLNALGIEA--VGVPKSNYKDELAKFAEAPK--VGTLFEPDYEALKALKPDLIFAGGR--SASAI 109
Cdd:cd01141 6 VPPKRIVVLSPTHVDLLLALDKADkiVGVSASAYDLNTPAVKERIDiqVGPTGSLNVELIVALKPDLVILYGGfqAQTIL 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582490333 110 PELEKIAPVANLTNRNPEFLAdfRTNTLRLAAAF---DKTKKAEEGLSNIDKDIADLQKL 166
Cdd:cd01141 86 DKLEQLGIPVLYVNEYPSPLG--RAEWIKFAAAFygvGKEDKADEAFAQIAGRYRDLAKK 143
|
|
| BtuF |
cd01144 |
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ... |
39-289 |
5.02e-10 |
|
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: 58.85 E-value: 5.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582490333 39 ERIVSYDLSILDSLNALGIEA--VGVpkSNYKDELAKFAEAPKVGTLFEPDYEALKALKPDLI--FAGGRSASAIPELEK 114
Cdd:cd01144 1 MRIVSLAPSATELLYALGLGDqlVGV--TDYCDYPPEAKKLPRVGGFYQLDLERVLALKPDLViaWDDCNVCAVVDQLRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582490333 115 IAPVANLTNRN--PEFLADFRtntlRLAAAFDKTKKAEEGLSNIDKDIADLQKLNAGKTG--AF-------LFVMNGNII 183
Cdd:cd01144 79 AGIPVLVSEPQtlDDILADIR----RLGTLAGRPARAEELAEALRRRLAALRKQYASKPPprVFyqewidpLMTAGGDWV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582490333 184 PHVVgdrfgfvyELTGLESVLPaktaeELAAPATRPAPDSpeakaaaakraqqikaIAKADPDWLIVFDraainGGENAG 263
Cdd:cd01144 155 PELI--------ALAGGVNVFA-----DAGERSPQVSWED----------------VLAANPDVIVLSP-----CGFGFT 200
|
250 260
....*....|....*....|....*.
gi 2582490333 264 EKTLAEHPDLSQTSAFKNGRVVYVDP 289
Cdd:cd01144 201 PAILRKEPAWQALPAVRNGRVYAVDG 226
|
|
| HutB |
cd01149 |
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ... |
38-289 |
9.16e-10 |
|
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: 58.05 E-value: 9.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582490333 38 PERIVSYDLSILDSLNALGIEA--VGV-PKSNYKDELAKfaeAPKVGTLFEPDYEALKALKPDLIFA--GGRSASAIPEL 112
Cdd:cd01149 1 PERIVSLGGSVTEIVYALGAGDrlVGVdSTSTYPEAAAK---LPDVGYMRQLSAEGVLSLKPTLVIAsdEAGPPEALDQL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582490333 113 EKiAPVANLTNRNPEFLADFRTNTLRLAAAFDKTKKAEEGLSNIDKDIADLQKLNA--GKTGAFLFVM-NGNIIPHVVGd 189
Cdd:cd01149 78 RA-AGVPVVTVPSTPTLDGLLTKIRQVAQALGVPEKGEALAQEVRQRLAALRKTVAahKKPPRVLFLLsHGGGAAMAAG- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582490333 190 rfgfvyELTGLESVLPAKTAEELAAPATRPAPDSPEakaaaakraqqikAIAKADPDWLIVFDRAAINGGENAGektLAE 269
Cdd:cd01149 156 ------RNTAADAIIALAGAVNAAAGFRGYKPLSAE-------------ALIAAQPDVILVMSRGLDAVGGVDG---LLK 213
|
250 260
....*....|....*....|
gi 2582490333 270 HPDLSQTSAFKNGRVVYVDP 289
Cdd:cd01149 214 LPGLAQTPAGRNKRILAMDD 233
|
|
| HemV-2 |
cd01147 |
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ... |
39-290 |
1.92e-09 |
|
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: 57.34 E-value: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582490333 39 ERIVSYDLSILDSLNALGI--EAVGVPKSNYKDELAKF-------AEAPKVGTLF---EPDYEALKALKPDLIFA-GGRS 105
Cdd:cd01147 6 ERVVAAGPGALRLLYALAApdKIVGVDDAEKSDEGRPYflaspelKDLPVIGRGGrgnTPNYEKIAALKPDVVIDvGSDD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582490333 106 ASAIPE-LEKIA--PVANLTNRNpeFLADFRTNTLRLAAAFDKTKKAEEGLSNIDKDIADLQK----LNAGKTGAFLFVM 178
Cdd:cd01147 86 PTSIADdLQKKTgiPVVVLDGGD--SLEDTPEQIRLLGKVLGKEERAEELISFIESILADVEErtkdIPDEEKPTVYFGR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582490333 179 NGNIIPHVV---GDRFGFVYELTGLESVLPAKTAEELAAPatrpapdSPEAkaaaakraqqikaIAKADPDWLIVFDraa 255
Cdd:cd01147 164 IGTKGAAGLesgLAGSIEVFELAGGINVADGLGGGGLKEV-------SPEQ-------------ILLWNPDVIFLDT--- 220
|
250 260 270
....*....|....*....|....*....|....*
gi 2582490333 256 iNGGENAGEKTLAEHPDLSQTSAFKNGRvVYVDPV 290
Cdd:cd01147 221 -GSFYLSLEGYAKNRPFWQSLKAVKNGR-VYLLPA 253
|
|
| TroA_a |
cd01148 |
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ... |
35-300 |
1.73e-08 |
|
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: 54.65 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582490333 35 DKTPERIVSYDLSILDSLNALGIE--AVGVPKSNYKD--EL-AKFAEAPKVGTLfEPDYEALKALKPDLIFAGGRSASAI 109
Cdd:cd01148 15 DKAPQRVVSNDQNTTEMMLALGLQdrMVGTAGIDNKDlpELkAKYDKVPELAKK-YPSKETVLAARPDLVFGGWSYGFDK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582490333 110 PELEKIA-------PVANLTN----RNPEF-LADFRTNTLRLAAAFDKTKKAEEGLSNIDKDIADLQKLNAG---KTGAF 174
Cdd:cd01148 94 GGLGTPDslaelgiKTYILPEscgqRRGEAtLDDVYNDIRNLGKIFDVEDRADKLVADLKARLAEISAKVKGdgkKVAVF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582490333 175 LFVM-NGNIIPHVVGDRFGFVYELTGLESVlpaktaeeLAAPATRPAPDSPEAkaaaakraqqikaIAKADPDWLIVFDR 253
Cdd:cd01148 174 VYDSgEDKPFTSGRGGIPNAIITAAGGRNV--------FADVDESWTTVSWET-------------VIARNPDVIVIIDY 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2582490333 254 AAINGGENAgEKTLAEHPDLSQTSAFKNGRVVYVDPVRWYviTGGLN 300
Cdd:cd01148 233 GDQNAAEQK-IKFLKENPALKNVPAVKNNRFIVLPLAEAT--PGIRN 276
|
|
| PRK10957 |
PRK10957 |
iron-enterobactin transporter periplasmic binding protein; Provisional |
7-118 |
2.51e-07 |
|
iron-enterobactin transporter periplasmic binding protein; Provisional
Pssm-ID: 236806 [Multi-domain] Cd Length: 317 Bit Score: 51.51 E-value: 2.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582490333 7 IMTLTATLAIAAPSLAFE--------LEHTTGTINGDKTPERIVSYDLSILDSLnaLGIEA------VGVPKSNYKDEL- 71
Cdd:PRK10957 5 LALLLLGLLLSGIAAAQAsaagwprtVTDSRGSVTLESKPQRIVSTSVTLTGTL--LAIDApviasgATTPNTRVADDQg 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2582490333 72 -----AKFAEAPKVGTLF--EPDYEALKALKPDLIFA---GGRSASA-IPELEKIAPV 118
Cdd:PRK10957 83 ffrqwSDVAKERGVEVLYigEPDAEAVAAQMPDLIVIsatGGDSALAlYDQLSAIAPT 140
|
|
| PRK10576 |
PRK10576 |
Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD; |
38-178 |
3.98e-04 |
|
Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD;
Pssm-ID: 236719 Cd Length: 292 Bit Score: 41.54 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2582490333 38 PERIVSYDLSILDSLNALGIEAVGVP-KSNYK---DELAKFAEAPKVGTLFEPDYEALKALKPDLIFAggrSASAIPELE 113
Cdd:PRK10576 32 PNRIVALEWLPVELLLALGVTPYGVAdTHNYRlwvSEPALPDSVIDVGLRTEPNLELLTQMKPSLILW---SAGYGPSPE 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2582490333 114 KIAPVA-----NLTNR-NPefLADFRTNTLRLAAAFDKTKKAEEGLSNIDKDIADLQKLNAGKTGAFLFVM 178
Cdd:PRK10576 109 KLARIApgrgfAFSDGkKP--LAVARKSLVELAQRLNLEAAAETHLAQFDDFIASAKPRLAGRGQRPLLLT 177
|
|
| |
