|
Name |
Accession |
Description |
Interval |
E-value |
| TroA_f |
cd01139 |
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ... |
27-364 |
4.26e-105 |
|
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: 312.70 E-value: 4.26e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 27 VTITDTDGQKITLKHEPKRVVLQDGRDILTLALLDRNNPFERVVAWNNNLKKSDPQTVSLLEQKWKsNINSIPDMGFNDK 106
Cdd:cd01139 1 ITVTDVAGRKVTLDAPVERVLLGEGRQLYALALLEGENPFARIVGWGGDLKKGDPDTYAKYKEKFP-EIADIPLIGSTYN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 107 GEVNAEQVIAQQPDVVIAQLRAKPALEGSGVVSILKEANIPIIYVDTFLEPVKNTKESVELLGIILNKESEAKEYTDFYQ 186
Cdd:cd01139 80 GDFSVEKVLTLKPDLVILNIWAKTTAEESGILEKLEQAGIPVVFVDFRQKPLKNTTPSMRLLGKALGREERAEEFIEFYQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 187 QHLDSIKNKTQEIK-NKPRVFVEAKAGAnGDGCCFTHNNAGWGGLIQAVGGDNIGSHFLPGASGVISLEQVISTKPDVYI 265
Cdd:cd01139 160 ERIDRIRDRLAKINePKPKVFIELGAGG-PEECCSTYGNGNWGELVDAAGGDNIADGLIPGTSGELNAEYVIAANPEIII 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 266 VTGSRWINKNSiAAPFGYGVSSKETQEGFKR-LKSRIGFNQIAAVENGQLYGIYHNFYNHPYNIVGLEYLATFIYPEQFA 344
Cdd:cd01139 239 ATGGNWAKDPS-GVSLGPDGTTADAKESLLRaLLKRPGWSSLQAVKNGRVYALWHQFYRSPYNFVALEAFAKWLYPELFK 317
|
330 340
....*....|....*....|
gi 1114044858 345 ELKPENTYKEIIEKYTTLPS 364
Cdd:cd01139 318 DLDPEATLQEFHRQFLPVDY 337
|
|
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
45-344 |
3.58e-54 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 179.42 E-value: 3.58e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 45 RVVLQDGRDILTLALLDRNnpfERVVAWNNNLKKSDPQTVslleqkwksnINSIPDMGfnDKGEVNAEQVIAQQPDVVIA 124
Cdd:COG0614 2 RIVSLSPSATELLLALGAG---DRLVGVSDWGYCDYPELE----------LKDLPVVG--GTGEPNLEAILALKPDLVLA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 125 QlrakPALEGSGVVSILKEANIPIIYVDTflEPVKNTKESVELLGIILNKESEAKEYTDFYQQHLDSIKNKTQEIKNKPR 204
Cdd:COG0614 67 S----SSGNDEEDYEQLEKIGIPVVVLDP--RSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGAEERPT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 205 VFVEAkagANGDGCCFTHNNAGWGGLIQAVGGDNIGSHfLPGASGVISLEQVISTKPDVYIVTgsrwinknsiaapfGYG 284
Cdd:COG0614 141 VLYEI---WSGDPLYTAGGGSFIGELLELAGGRNVAAD-LGGGYPEVSLEQVLALDPDVIILS--------------GGG 202
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1114044858 285 VSSKETQEGFKRLKSRIGFNQIAAVENGQLYGIYHNF--YNHPYNIVGLEYLATFIYPEQFA 344
Cdd:COG0614 203 YDAETAEEALEALLADPGWQSLPAVKNGRVYVVPGDLlsRPGPRLLLALEDLAKALHPELFA 264
|
|
| PRK14048 |
PRK14048 |
ferrichrome/ferrioxamine B periplasmic transporter; Provisional |
17-369 |
4.12e-50 |
|
ferrichrome/ferrioxamine B periplasmic transporter; Provisional
Pssm-ID: 172540 [Multi-domain] Cd Length: 374 Bit Score: 172.39 E-value: 4.12e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 17 PFSALA-TTYPVTITDTDGQKITLKHEPKRVVLQDGRDILTLALLdRNNPFERVVAWNNNLKKSDPQTVSLLEQKWKSnI 95
Cdd:PRK14048 21 ALSALAeVQWPMTVTDAVGREVTIPAPPKAVLLGSGFNLIALSLI-HPDPVSLLAGWSGDMKGDNPEIYESFLRKFPE-L 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 96 NSIPDMGFNDKGEVNAEQVIAQQPDVVIAQLRAKPALEGSGVVSILKEANIPIIYVDTFLEPVKNTKESVELLGIILNKE 175
Cdd:PRK14048 99 ADVPLIDDGSGPGLSFETILTLKADLAILANWQADTEAGQRAIEYLESIGVPVIVVDFNNEALKNTPDNMRLLGKVFERE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 176 SEAKEYTDFYQQHLDSIKNKTQEIKNK-PRVFVEAKAGAngDGCCFTHNNAGWGGLIQAVGGDNIGSHFLPGASGVISLE 254
Cdd:PRK14048 179 EQAEDFARFYEERLARIRDRVAKHSEPgPTVLMEAFPAA--DRCCWAYGRGGLGEFIALTGSRNIAEGALPRPGGMMNAE 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 255 QVISTKPDVYIVTGSRWINKNSIAapFGYGVSSKETQEGFKRLKSRIGFNQIAAVENGQLYGIYhNFYNH-PYNIVGLEY 333
Cdd:PRK14048 257 AIMAENPDVYIATSSPGGKYSGFS--IGPGVSAEEAETTLANVVDKPVMASIAAVRDGRVHGLW-NFFNAvPLNIVAAEA 333
|
330 340 350
....*....|....*....|....*....|....*.
gi 1114044858 334 LATFIYPEQFAELKPENTYKEIIEKYTTLPSAKFLW 369
Cdd:PRK14048 334 FASWLRPELFADIDPAATLAEINRRFAAVPFEGSYW 369
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
107-317 |
8.56e-22 |
|
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: 92.82 E-value: 8.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 107 GEVNAEQVIAQQPDVVIAQLRAKPALEgsgvvsILKEANIPIIYVDTFLEPVKNTKESVELLGIILNKESEAKEYTDFYQ 186
Cdd:pfam01497 46 GEINVERLAALKPDLVILSTGYLTDEA------EELLSLIIPTVIFESSSTGESLKEQIKQLGELLGLEDEAEELVAEID 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 187 QHLDSIKNKTQEIKNKPRVFVEakaGANGDGCCFTHNNAGWGGLIQAVGGDNIGSHFLPGASGVISLEQVISTKPDVYIV 266
Cdd:pfam01497 120 SALAAAKKAVPSLTRKPVLVFG---GADGGGYVVAGSNTYIGDLLRILGIENIAAELSGSEYAPISFEAILSSNPDVIIV 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1114044858 267 TGSRWinknsiaapfgygvsskETQEGFKRLKSRIGFNQIAAVENGQLYGI 317
Cdd:pfam01497 197 SGRDS-----------------FTKTGPEFVAANPLWAGLPAVKNGRVYTL 230
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| TroA_f |
cd01139 |
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ... |
27-364 |
4.26e-105 |
|
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: 312.70 E-value: 4.26e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 27 VTITDTDGQKITLKHEPKRVVLQDGRDILTLALLDRNNPFERVVAWNNNLKKSDPQTVSLLEQKWKsNINSIPDMGFNDK 106
Cdd:cd01139 1 ITVTDVAGRKVTLDAPVERVLLGEGRQLYALALLEGENPFARIVGWGGDLKKGDPDTYAKYKEKFP-EIADIPLIGSTYN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 107 GEVNAEQVIAQQPDVVIAQLRAKPALEGSGVVSILKEANIPIIYVDTFLEPVKNTKESVELLGIILNKESEAKEYTDFYQ 186
Cdd:cd01139 80 GDFSVEKVLTLKPDLVILNIWAKTTAEESGILEKLEQAGIPVVFVDFRQKPLKNTTPSMRLLGKALGREERAEEFIEFYQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 187 QHLDSIKNKTQEIK-NKPRVFVEAKAGAnGDGCCFTHNNAGWGGLIQAVGGDNIGSHFLPGASGVISLEQVISTKPDVYI 265
Cdd:cd01139 160 ERIDRIRDRLAKINePKPKVFIELGAGG-PEECCSTYGNGNWGELVDAAGGDNIADGLIPGTSGELNAEYVIAANPEIII 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 266 VTGSRWINKNSiAAPFGYGVSSKETQEGFKR-LKSRIGFNQIAAVENGQLYGIYHNFYNHPYNIVGLEYLATFIYPEQFA 344
Cdd:cd01139 239 ATGGNWAKDPS-GVSLGPDGTTADAKESLLRaLLKRPGWSSLQAVKNGRVYALWHQFYRSPYNFVALEAFAKWLYPELFK 317
|
330 340
....*....|....*....|
gi 1114044858 345 ELKPENTYKEIIEKYTTLPS 364
Cdd:cd01139 318 DLDPEATLQEFHRQFLPVDY 337
|
|
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
45-344 |
3.58e-54 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 179.42 E-value: 3.58e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 45 RVVLQDGRDILTLALLDRNnpfERVVAWNNNLKKSDPQTVslleqkwksnINSIPDMGfnDKGEVNAEQVIAQQPDVVIA 124
Cdd:COG0614 2 RIVSLSPSATELLLALGAG---DRLVGVSDWGYCDYPELE----------LKDLPVVG--GTGEPNLEAILALKPDLVLA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 125 QlrakPALEGSGVVSILKEANIPIIYVDTflEPVKNTKESVELLGIILNKESEAKEYTDFYQQHLDSIKNKTQEIKNKPR 204
Cdd:COG0614 67 S----SSGNDEEDYEQLEKIGIPVVVLDP--RSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGAEERPT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 205 VFVEAkagANGDGCCFTHNNAGWGGLIQAVGGDNIGSHfLPGASGVISLEQVISTKPDVYIVTgsrwinknsiaapfGYG 284
Cdd:COG0614 141 VLYEI---WSGDPLYTAGGGSFIGELLELAGGRNVAAD-LGGGYPEVSLEQVLALDPDVIILS--------------GGG 202
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1114044858 285 VSSKETQEGFKRLKSRIGFNQIAAVENGQLYGIYHNF--YNHPYNIVGLEYLATFIYPEQFA 344
Cdd:COG0614 203 YDAETAEEALEALLADPGWQSLPAVKNGRVYVVPGDLlsRPGPRLLLALEDLAKALHPELFA 264
|
|
| PRK14048 |
PRK14048 |
ferrichrome/ferrioxamine B periplasmic transporter; Provisional |
17-369 |
4.12e-50 |
|
ferrichrome/ferrioxamine B periplasmic transporter; Provisional
Pssm-ID: 172540 [Multi-domain] Cd Length: 374 Bit Score: 172.39 E-value: 4.12e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 17 PFSALA-TTYPVTITDTDGQKITLKHEPKRVVLQDGRDILTLALLdRNNPFERVVAWNNNLKKSDPQTVSLLEQKWKSnI 95
Cdd:PRK14048 21 ALSALAeVQWPMTVTDAVGREVTIPAPPKAVLLGSGFNLIALSLI-HPDPVSLLAGWSGDMKGDNPEIYESFLRKFPE-L 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 96 NSIPDMGFNDKGEVNAEQVIAQQPDVVIAQLRAKPALEGSGVVSILKEANIPIIYVDTFLEPVKNTKESVELLGIILNKE 175
Cdd:PRK14048 99 ADVPLIDDGSGPGLSFETILTLKADLAILANWQADTEAGQRAIEYLESIGVPVIVVDFNNEALKNTPDNMRLLGKVFERE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 176 SEAKEYTDFYQQHLDSIKNKTQEIKNK-PRVFVEAKAGAngDGCCFTHNNAGWGGLIQAVGGDNIGSHFLPGASGVISLE 254
Cdd:PRK14048 179 EQAEDFARFYEERLARIRDRVAKHSEPgPTVLMEAFPAA--DRCCWAYGRGGLGEFIALTGSRNIAEGALPRPGGMMNAE 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 255 QVISTKPDVYIVTGSRWINKNSIAapFGYGVSSKETQEGFKRLKSRIGFNQIAAVENGQLYGIYhNFYNH-PYNIVGLEY 333
Cdd:PRK14048 257 AIMAENPDVYIATSSPGGKYSGFS--IGPGVSAEEAETTLANVVDKPVMASIAAVRDGRVHGLW-NFFNAvPLNIVAAEA 333
|
330 340 350
....*....|....*....|....*....|....*.
gi 1114044858 334 LATFIYPEQFAELKPENTYKEIIEKYTTLPSAKFLW 369
Cdd:PRK14048 334 FASWLRPELFADIDPAATLAEINRRFAAVPFEGSYW 369
|
|
| TroA_e |
cd01142 |
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ... |
19-346 |
7.62e-28 |
|
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: 110.52 E-value: 7.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 19 SALATTypVTITDTDGQKITLKHEPKRVVLQDG---RDILTLALLDRNNPFERVVAWNNNLKKSDPQtvslleqkwksnI 95
Cdd:cd01142 2 AATAAT--RTITDMAGRKVTIPDEVKRIAALWGagnAVVAALGGGKLIVATTSTVQQEPWLYRLAPS------------L 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 96 NSIPDMGFNDkgEVNAEQVIAQQPDVVIAqlrakpalegsgVVSILKEANIPIIYVDTFLEPVKNTKESVEL----LGII 171
Cdd:cd01142 68 ENVATGGTGN--DVNIEELLALKPDVVIV------------WSTDGKEAGKAVLRLLNALSLRDAELEEVKLtialLGEL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 172 LNKESEAKEYTDFYQQHLDSIKNKTQEIKN--KPRVFVEAKAGANGDGccfTHNNAGWggLIQAVGGDNIGSHFLPGASG 249
Cdd:cd01142 134 LGRQEKAEALVAYFDDNLAYVAARTKKLPDseRPRVYYAGPDPLTTDG---TGSITNS--WIDLAGGINVASEATKKGSG 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 250 VISLEQVISTKPDVYIVtgsrwinknsiaapfgYGVSSKETQEGFKRLKSrigfnqIAAVENGQLYGI-YHNFYNHPY-- 326
Cdd:cd01142 209 EVSLEQLLKWNPDVIIV----------------GNADTKAAILADPRWQN------LRAVKNGRVYVNpEGAFWWDRPsa 266
|
330 340
....*....|....*....|.
gi 1114044858 327 -NIVGLEYLATFIYPEQFAEL 346
Cdd:cd01142 267 eEALLGLWLAKTLYPERFTDD 287
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
107-317 |
8.56e-22 |
|
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: 92.82 E-value: 8.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 107 GEVNAEQVIAQQPDVVIAQLRAKPALEgsgvvsILKEANIPIIYVDTFLEPVKNTKESVELLGIILNKESEAKEYTDFYQ 186
Cdd:pfam01497 46 GEINVERLAALKPDLVILSTGYLTDEA------EELLSLIIPTVIFESSSTGESLKEQIKQLGELLGLEDEAEELVAEID 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 187 QHLDSIKNKTQEIKNKPRVFVEakaGANGDGCCFTHNNAGWGGLIQAVGGDNIGSHFLPGASGVISLEQVISTKPDVYIV 266
Cdd:pfam01497 120 SALAAAKKAVPSLTRKPVLVFG---GADGGGYVVAGSNTYIGDLLRILGIENIAAELSGSEYAPISFEAILSSNPDVIIV 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1114044858 267 TGSRWinknsiaapfgygvsskETQEGFKRLKSRIGFNQIAAVENGQLYGI 317
Cdd:pfam01497 197 SGRDS-----------------FTKTGPEFVAANPLWAGLPAVKNGRVYTL 230
|
|
| HemV-2 |
cd01147 |
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ... |
46-315 |
3.63e-20 |
|
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: 88.93 E-value: 3.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 46 VVLQDGRDILTLALLDRnnpfERVVAWNNNLKkSDPQTVSLLEQKWKSNINSIPDMGFNDkgEVNAEQVIAQQPDVVIAQ 125
Cdd:cd01147 9 VAAGPGALRLLYALAAP----DKIVGVDDAEK-SDEGRPYFLASPELKDLPVIGRGGRGN--TPNYEKIAALKPDVVIDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 126 LRAKPALEGSgvvSILKEANIPIIYVDTFlEPVKNTKESVELLGIILNKESEAKEYTDFYQQHLDSIKNKTQEIKN--KP 203
Cdd:cd01147 82 GSDDPTSIAD---DLQKKTGIPVVVLDGG-DSLEDTPEQIRLLGKVLGKEERAEELISFIESILADVEERTKDIPDeeKP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 204 RVFVEAKAGANGDGccFTHNNAGWGGLIQAVGGDNIGSHFLPGASGVISLEQVISTKPDVYIVTGSRWINKNSiaapfgy 283
Cdd:cd01147 158 TVYFGRIGTKGAAG--LESGLAGSIEVFELAGGINVADGLGGGGLKEVSPEQILLWNPDVIFLDTGSFYLSLE------- 228
|
250 260 270
....*....|....*....|....*....|..
gi 1114044858 284 gvssketqegfKRLKSRIGFNQIAAVENGQLY 315
Cdd:cd01147 229 -----------GYAKNRPFWQSLKAVKNGRVY 249
|
|
| TroA_a |
cd01148 |
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ... |
25-266 |
6.90e-18 |
|
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: 82.77 E-value: 6.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 25 YPVTItDTDGQKITLKHEPKRVVLQDGRDI---LTLALLDRnnpferVVAWNNNLKKSDPqtvsLLEQKWKSninsIPDM 101
Cdd:cd01148 1 YPLTV-ENCGRSVTFDKAPQRVVSNDQNTTemmLALGLQDR------MVGTAGIDNKDLP----ELKAKYDK----VPEL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 102 GfndKGEVNAEQVIAQQPDVVIAQLRAKPALEGSGVVSILKEANIPiiyvdTFLEP-----------VKNTKESVELLGI 170
Cdd:cd01148 66 A---KKYPSKETVLAARPDLVFGGWSYGFDKGGLGTPDSLAELGIK-----TYILPescgqrrgeatLDDVYNDIRNLGK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 171 ILNKESEAKEYTDFYQQHLDSIKNKTQEIKNKPRVFVEakagANGDGCCFThnnAGWGG----LIQAVGGDNIGSHfLPG 246
Cdd:cd01148 138 IFDVEDRADKLVADLKARLAEISAKVKGDGKKVAVFVY----DSGEDKPFT---SGRGGipnaIITAAGGRNVFAD-VDE 209
|
250 260
....*....|....*....|
gi 1114044858 247 ASGVISLEQVISTKPDVYIV 266
Cdd:cd01148 210 SWTTVSWETVIARNPDVIVI 229
|
|
| TroA-like |
cd00636 |
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ... |
44-207 |
6.90e-16 |
|
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: 74.13 E-value: 6.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 44 KRVVLQDGRDILTLALLDrnnPFERVVAWnnnlkkSDPQTVSLLEQKWKSNINSIPDMGfndkgEVNAEQVIAQQPDVVI 123
Cdd:cd00636 1 KRVVALDPGATELLLALG---GDDKPVGV------ADPSGYPPEAKALLEKVPDVGHGY-----EPNLEKIAALKPDLII 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 124 AQlrakpALEGSGVVSILKEANIPIIYVDTFLE-PVKNTKESVELLGIILNKESEAKEYTDFYQQHLDSIKNKTQEIKNK 202
Cdd:cd00636 67 AN-----GSGLEAWLDKLSKIAIPVVVVDEASElSLENIKESIRLIGKALGKEENAEELIAELDARLAELRAKLAKIPKK 141
|
....*
gi 1114044858 203 PRVFV 207
Cdd:cd00636 142 KVSLV 146
|
|
| ChuT |
COG4558 |
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ... |
95-315 |
2.17e-14 |
|
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443619 [Multi-domain] Cd Length: 285 Bit Score: 72.53 E-value: 2.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 95 INSIPDMGFNdkGEVNAEQVIAQQPDVVIAQLRAKPALegsgVVSILKEANIPIIYVDTflEP-VKNTKESVELLGIILN 173
Cdd:COG4558 63 AKALPDVGYM--RQLSAEGILSLKPTLVLASEGAGPPE----VLDQLRAAGVPVVVVPA--APsLEGVLAKIRAVAAALG 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 174 KESEAKEYTDFYQQHLDSIKNKTQEIKNKPRV-FVEAKAGAN----GDGccfthnnAGWGGLIQAVGGDNIGSHFlpgaS 248
Cdd:COG4558 135 VPEAGEALAARLEADLAALAARVAAIGKPPRVlFLLSRGGGRpmvaGRG-------TAADALIRLAGGVNAAAGF----E 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1114044858 249 GV--ISLEQVISTKPDVYIVTGSrwinknsiaapfgyGVSSKETQEGFKRLKsriGFNQIAAVENGQLY 315
Cdd:COG4558 204 GYkpLSAEALIAAAPDVILVMTR--------------GLESLGGVDGLLALP---GLAQTPAGKNKRIV 255
|
|
| btuF |
PRK09534 |
corrinoid ABC transporter substrate-binding protein; Reviewed |
22-267 |
5.44e-13 |
|
corrinoid ABC transporter substrate-binding protein; Reviewed
Pssm-ID: 236552 [Multi-domain] Cd Length: 359 Bit Score: 69.55 E-value: 5.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 22 ATTYPVTITDTDGQKITLKHEPKRVVLQDGRDILTL-ALLDRnnpfERVVAWNnnlkksdPQTVSLLEQKWKSNINSIPD 100
Cdd:PRK09534 39 ACSFPVTETDATGTEITLDERPERVVTLNPSAAQTMwELGAR----DRVVGVT-------QYASYLDGAEERTNVSGGQP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 101 MGfndkgeVNAEQVIAQQPDVVIAqlrakPALEGSGVVSILKEANIpIIYVDTFLEPVKNTKESVELLGIILNKESEAKE 180
Cdd:PRK09534 108 FG------VNVEAVVGLDPDLVLA-----PNAVAGDTVTRLREAGI-TVFHFPAATSIEDVAEKTATIGRLTGNCEAAAE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 181 YTDFYQQHLDSIKNKTQEIKNKPRVFVEAKAGANGDGCCFThnnagwGGLIQAVGGDNIGSHFLPGASGVISLEQVISTK 260
Cdd:PRK09534 176 TNAEMRDRVDAVEDRTADVDDRPRVLYPLGDGYTAGGNTFI------GALIEAAGGHNVAADATTDGYPQLSEEVIVQQD 249
|
....*..
gi 1114044858 261 PDVYIVT 267
Cdd:PRK09534 250 PDVIVVA 256
|
|
| BtuF |
cd01144 |
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ... |
109-325 |
3.06e-12 |
|
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: 65.78 E-value: 3.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 109 VNAEQVIAQQPDVVIAQlrakPALEGSGVVSILKEANIPIIYVD--TFLEPVkntkESVELLGIILNKESEAKEYTDFYQ 186
Cdd:cd01144 48 LDLERVLALKPDLVIAW----DDCNVCAVVDQLRAAGIPVLVSEpqTLDDIL----ADIRRLGTLAGRPARAEELAEALR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 187 QHLDSIKNKTQEiKNKPRVFVEAkaganGDGCCFTHNNAGWGGLIQAVGGDNIGSHfLPGASGVISLEQVISTKPDVYIV 266
Cdd:cd01144 120 RRLAALRKQYAS-KPPPRVFYQE-----WIDPLMTAGGDWVPELIALAGGVNVFAD-AGERSPQVSWEDVLAANPDVIVL 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1114044858 267 tgsrwinknsiaAPFGYGVSsketqegFKRLKSRIGFNQIAAVENGQLYGIYHNFYNHP 325
Cdd:cd01144 193 ------------SPCGFGFT-------PAILRKEPAWQALPAVRNGRVYAVDGNWYFRP 232
|
|
| YvrC |
cd01143 |
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ... |
107-266 |
3.73e-11 |
|
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: 61.91 E-value: 3.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 107 GEVNAEQVIAQQPDVVIAQlrakpALEGSGVVSILKEANIPIIYVDTfLEPVKNTKESVELLGIILNKESEAKEYTDFYQ 186
Cdd:cd01143 49 SNPNVEKIVALKPDLVIVS-----SSSLAELLEKLKDAGIPVVVLPA-ASSLDEIYDQIELIGKITGAEEEAEKLVKEMK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 187 QHLDSIKNKTQEIKnKPRVFVEAKAGANgdgccFTHNNAGW-GGLIQAVGGDNIgshfLPGASG--VISLEQVISTKPDV 263
Cdd:cd01143 123 QKIDKVKDKGKTIK-KSKVYIEVSLGGP-----YTAGKNTFiNELIRLAGAKNI----AADSGGwpQVSPEEILKANPDV 192
|
...
gi 1114044858 264 YIV 266
Cdd:cd01143 193 IIL 195
|
|
| HutB |
cd01149 |
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ... |
91-270 |
2.24e-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: 60.36 E-value: 2.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 91 WKSNINSIPDMGFNDkgEVNAEQVIAQQPDVVIAQLRAKPALegsgVVSILKEANIPIIYVDTflEPVKNT-KESVELLG 169
Cdd:cd01149 33 YPEAAAKLPDVGYMR--QLSAEGVLSLKPTLVIASDEAGPPE----ALDQLRAAGVPVVTVPS--TPTLDGlLTKIRQVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 170 IILNKESEAKEYTDFYQQHLDSIKNKTQEIKNKPRV-FVEAKAG--ANGDGccfthNNAGWGGLIQAVGGDNIGSHFLPG 246
Cdd:cd01149 105 QALGVPEKGEALAQEVRQRLAALRKTVAAHKKPPRVlFLLSHGGgaAMAAG-----RNTAADAIIALAGAVNAAAGFRGY 179
|
170 180
....*....|....*....|....
gi 1114044858 247 ASgvISLEQVISTKPDVyIVTGSR 270
Cdd:cd01149 180 KP--LSAEALIAAQPDV-ILVMSR 200
|
|
| FatB |
cd01140 |
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ... |
108-266 |
6.14e-09 |
|
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: 56.50 E-value: 6.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 108 EVNAEQVIAQQPDVVIAQLRAKPALEgsgvvSILKEANIPIIYVDTfLEPVKNTKESVELLGIILNKESEAKEYTDFYQQ 187
Cdd:cd01140 62 EPDLEAIAALKPDLIIIGGRLAEKYD-----ELKKIAPTIDLGADL-KNYLESVKQNIETLGKIFGKEEEAKELVAEIDA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 188 HLDSIKNKTqeiKNKPRVFV----EAKAGANGDGCCFthnnaGW----GGLIQAVGGDNIGSHFLPgasgvISLEQVIST 259
Cdd:cd01140 136 SIAEAKSAA---KGKKKALVvlvnGGKLSAFGPGSRF-----GWlhdlLGFEPADENIKASSHGQP-----VSFEYILEA 202
|
....*..
gi 1114044858 260 KPDVYIV 266
Cdd:cd01140 203 NPDWLFV 209
|
|
| fecB |
PRK11411 |
iron-dicitrate transporter substrate-binding subunit; Provisional |
18-314 |
1.19e-06 |
|
iron-dicitrate transporter substrate-binding subunit; Provisional
Pssm-ID: 183123 [Multi-domain] Cd Length: 303 Bit Score: 49.67 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 18 FSALATTYPVTITDTDGQkITLKHEPKRVVlqdgrdILTLALLDrnnPFERV------VAWNNNLKKSDPQTVSLLEQkW 91
Cdd:PRK11411 15 LSGSSHAFAVTVQDEQGT-FTLEKTPQRIV------VLELSFVD---ALAAVgvspvgVADDNDAKRILPEVRAHLKP-W 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 92 KS-NINSIPDMgfndkgevnaEQVIAQQPDVVIAQLRAKpalegSGVVSILKEAnIPIIYVDTFLEPVKNTKESVELLGI 170
Cdd:PRK11411 84 QSvGTRSQPSL----------EAIAALKPDLIIADSSRH-----AGVYIALQKI-APTLLLKSRNETYQENLQSAAIIGE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 171 ILNKESEAKEYTDFYQQHLDSIKnkTQEIKNKPRVF-VEAKAGANgdgccfTHNNAGW-GGLIQAVGgdnIGSHFLPGAS 248
Cdd:PRK11411 148 VLGKKREMQARIEQHKERMAQFA--SQLPKGTRVAFgTSREQQFN------LHSPESYtGSVLAALG---LNVPKAPMNG 216
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1114044858 249 GV---ISLEQVISTKPDVYIVTGSRwinKNSIAapfgygvssketqegfKRLKSRIGFNQIAAVENGQL 314
Cdd:PRK11411 217 AAmpsISLEQLLALNPDWLLVAHYR---QESIV----------------KRWQQDPLWQMLTAAKKQQV 266
|
|
| FecB |
COG4594 |
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ... |
26-315 |
3.84e-06 |
|
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443650 [Multi-domain] Cd Length: 316 Bit Score: 47.99 E-value: 3.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 26 PVTITDTDGqKITLKHEPKRVVLQDGRDILTLALL--------DRNNPfERVVAWnnnlkksdpqtvslleqkWKSNINS 97
Cdd:COG4594 36 ARTVKHAMG-ETTIPGTPKRVVVLEWSFADALLALgvtpvgiaDDNDY-DRWVPY------------------LRDLIKG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 98 IPDMGFNdkGEVNAEQVIAQQPDVVIA-QLRAKpalegsGVVSILKEanI-PIIYVDTFLEPVKNTKESVELLGIILNKE 175
Cdd:COG4594 96 VTSVGTR--SQPNLEAIAALKPDLIIAdKSRHE------AIYDQLSK--IaPTVLFKSRNGDYQENLESFKTIAKALGKE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 176 SEAKEYTDFYQQHLDSIKNKTQEIKNKPRVFVeakAGANGDGCCFTHNNAGWGGLIQAVGGDNIGSHFLPGASGV--ISL 253
Cdd:COG4594 166 EEAEAVLADHDQRIAEAKAKLAAADKGKKVAV---GQFRADGLRLYTPNSFAGSVLAALGFENPPKQSKDNGYGYseVSL 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1114044858 254 EQVISTKPDVYIVTGSRwinKNSIaapfgygVSSKETQEGFKRLKsrigfnqiaAVENGQLY 315
Cdd:COG4594 243 EQLPALDPDVLFIATYD---DPSI-------LKEWKNNPLWKNLK---------AVKNGRVY 285
|
|
| TroA_d |
cd01141 |
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ... |
83-207 |
3.91e-05 |
|
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: 43.95 E-value: 3.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 83 TVSLLEQKWKSN-INSIPDMGFNDKGEVNAEQVIAQQPDVVIAQLRAKPAlegsGVVSILKEANIPIIYVDTFLEPVKNT 161
Cdd:cd01141 33 GVSASAYDLNTPaVKERIDIQVGPTGSLNVELIVALKPDLVILYGGFQAQ----TILDKLEQLGIPVLYVNEYPSPLGRA 108
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1114044858 162 KESVELLGI-ILNKESEAKEYTDFYQQHLDSIKNKTQEiKNKPRVFV 207
Cdd:cd01141 109 EWIKFAAAFyGVGKEDKADEAFAQIAGRYRDLAKKVSN-LNKPTVAI 154
|
|
| FeuA |
cd01138 |
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ... |
100-207 |
3.83e-04 |
|
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: 41.55 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1114044858 100 DMGFNDKGEVNAEQVIAQQPDVVIAQLRAKPALEgsgvvsilKEANI-PIIYVDTFLepvKNTKESVELLGIILNKESEA 178
Cdd:cd01138 48 AKVVGIVDEPNLEKVLELKPDLIIVSSKQEENYE--------KLSKIaPTVPVSYNS---SDWEEQLKEIGKLLNKEDEA 116
|
90 100 110
....*....|....*....|....*....|
gi 1114044858 179 KEYTDFYQQHLDSIKNKTQ-EIKNKPRVFV 207
Cdd:cd01138 117 EKWLADYKQKAKEAKEKIKkKLGNDKSVAV 146
|
|
| |
