|
Name |
Accession |
Description |
Interval |
E-value |
| znuA |
PRK09545 |
zinc ABC transporter substrate-binding protein ZnuA; |
2-308 |
0e+00 |
|
zinc ABC transporter substrate-binding protein ZnuA;
Pssm-ID: 236558 [Multi-domain] Cd Length: 311 Bit Score: 598.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372873206 2 LHKKTLLFAALSAALWGGATQAADAAVVASLKPVGFIASAIADGVTETEVLLPDGASEHDYSLRPSDVKRLQNADLVVWV 81
Cdd:PRK09545 1 LHKKTLLFAALLAALLGGATQAANAAVVTSIKPLGFIASAIADGVTETEVLLPDGASPHDYSLRPSDVKRLQSADLVVWV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372873206 82 GPEMEAFMQKPVSKLPGAKQVTIAQLEDVKPLLMKSI----HGDDDDHDHAEKSDEDHHHGDFNMHLWLSPEIARATAVA 157
Cdd:PRK09545 81 GPEMEAFLEKPVSKLPENKQVTIAQLPDVKPLLMKGAhddhHDDDHDHAGHEKSDEDHHHGEYNMHIWLSPEIARATAVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372873206 158 IHGKLVELMPQSRAKLDANLKDFEAQLASTETQVGNELAPLKGKGYFVFHDAYGYFEKQFGLTPLGHFTVNPEIQPGAQR 237
Cdd:PRK09545 161 IHDKLVELMPQSKAKLDANLKDFEAQLAQTDKQIGNQLAPVKGKGYFVFHDAYGYFEKHYGLTPLGHFTVNPEIQPGAQR 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1372873206 238 LHEIRTQLVEQKATCVFAEPQFRPAVVESVARGTSVRMGTLDPLGTNIKLGKTSYSEFLSQLANQYASCLK 308
Cdd:PRK09545 241 LHEIRTQLVEQKATCVFAEPQFRPAVIESVAKGTSVRMGTLDPLGTNIKLGKDSYSEFLSQLANQYASCLK 311
|
|
| ZnuA |
COG4531 |
ABC-type Zn2+ transport system, periplasmic component/surface adhesin ZnuA [Inorganic ion ... |
17-307 |
4.32e-169 |
|
ABC-type Zn2+ transport system, periplasmic component/surface adhesin ZnuA [Inorganic ion transport and metabolism];
Pssm-ID: 443599 [Multi-domain] Cd Length: 300 Bit Score: 470.85 E-value: 4.32e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372873206 17 WGGATQAADAAVVASLKPVGFIASAIADGVTETEVLLPDGASEHDYSLRPSDVKRLQNADLVVWVGPEMEAFMQKPVSKL 96
Cdd:COG4531 1 LASAAAAAAPRVVTSIKPLHSLVAAVMDGVGEPELLLPPGASPHDYALRPSDARALQDADLVFWVGPDLEPFLEKPLETL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372873206 97 -PGAKQVTIAQLEDVKPLLMKSI--------HGDDDDHDHAEKSDEDHHHGDFNMHLWLSPEIARATAVAIHGKLVELMP 167
Cdd:COG4531 81 aPDAKVVELLELPGLTLLPFREGgdfehhdhHDEHHHHHHHHDDHHDHHHGGYDPHLWLSPENAKAWAAAIADALSELDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372873206 168 QSRAKLDANLKDFEAQLASTETQVGNELAPLKGKGYFVFHDAYGYFEKQFGLTPLGHFTVNPEIQPGAQRLHEIRTQLVE 247
Cdd:COG4531 161 ENAATYQANAAAFEARLDALDAEIAAQLAPVKGKPFFVFHDAYQYFEKRFGLNALGAITLNPEIQPGAKRLAEIREKLKE 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372873206 248 QKATCVFAEPQFRPAVVESVARGTSVRMGTLDPLGTNIKLGKTSYSEFLSQLANQYASCL 307
Cdd:COG4531 241 LGAVCVFAEPQFNPALVETVAEGTGVRTGVLDPLGADLEPGPDLYFQLLRQLADSLASCL 300
|
|
| ZnuA |
cd01019 |
Zinc binding protein ZnuA. These proteins have been shown to function as initial receptors in ... |
23-307 |
3.01e-145 |
|
Zinc binding protein ZnuA. These proteins have been shown to function as initial receptors in the ABC uptake of Zn2+. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. They are comprised of two globular subdomains connected by a single helix and bind their specific ligands in the cleft between these domains. 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: 238501 [Multi-domain] Cd Length: 286 Bit Score: 410.22 E-value: 3.01e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372873206 23 AADAAVVASLKPVGFIASAIADGVTETEVLLPDGASEHDYSLRPSDVKRLQNADLVVWVGPEMEAFMQKPVSKLPGAKQV 102
Cdd:cd01019 1 AAEASVLTSIKPLGFIAAAIMGGVGEVEVLVPPGASPHDYELRPSDARKLQEADLVVWIGPDLEAFLDKVLQGRKKGKVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372873206 103 TIAQLEDVKPLLMKSIH-GDDDDHDHAEKSDEDHHHGDFNMHLWLSPEIARATAVAIHGKLVELMPQSRAKLDANLKDFE 181
Cdd:cd01019 81 TLAKLIDLKTLEDGASHgDHEHDHEHAHGEHDGHEEGGLDPHLWLSPENAAEVAQAVAEKLSALDPDNAATYAANLEAFN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372873206 182 AQLASTETQVGNELAPLKGKGYFVFHDAYGYFEKQFGLTPLGHFTVNPEIQPGAQRLHEIRTQLVEQKATCVFAEPQFRP 261
Cdd:cd01019 161 ARLAELDATIKERLAPVKTKPFFVFHDAYGYFEKRYGLTQAGVFTIDPEIDPGAKRLAKIRKEIKEKGATCVFAEPQFHP 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1372873206 262 AVVESVARGTSVRMGTLDPLGTNIKLGKTSYSEFLSQLANQYASCL 307
Cdd:cd01019 241 KIAETLAEGTGAKVGELDPLGGLIELGKNSYVNFLRNLADSLASCL 286
|
|
| ZnuA |
pfam01297 |
Zinc-uptake complex component A periplasmic; ZnuA includes periplasmic solute binding proteins ... |
28-306 |
1.70e-81 |
|
Zinc-uptake complex component A periplasmic; ZnuA includes periplasmic solute binding proteins such as TroA that interacts with an ATP-binding cassette transport system in Treponema pallidum. ZnuA is part of the bacterial zinc-uptake complex ZnuABC, whose components are the following families, ZinT, pfam09223, pfam00950, pfam00005, all of which are regulated by the transcription-regulator family FUR, pfam01475. ZinT acts as a Zn2+-buffering protein that delivers Zn2+ to ZnuA (TroA), a high-affinity zinc-uptake protein. In Gram-negative bacteria the ZnuABC transporter system ensures an adequate import of zinc in Zn2+-poor environments, such as those encountered by pathogens within the infected host.
Pssm-ID: 460151 [Multi-domain] Cd Length: 269 Bit Score: 247.47 E-value: 1.70e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372873206 28 VVASLKPVGFIASAIADGVTETEVLLPDGASEHDYSLRPSDVKRLQNADLVVWVGPEMEAFMQKPVSKLPGAKQVTIAQl 107
Cdd:pfam01297 1 VVATTYPLADLAKQIGGDRVEVTSLVPPGADPHDYEPTPSDIAALSDADLVVYNGLGLEPWLDKLLEALPNKKVVDASE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372873206 108 edvkpllmksihGDDDDHDHAEKSDEDHHHGDFNMHLWLSPEIARATAVAIHGKLVELMPQSRAKLDANLKDFEAQLAST 187
Cdd:pfam01297 80 ------------GVELLDEEGEEEDHDGHDHGYDPHVWLDPKNAKKMAENIADALSELDPANAATYEANAAAYLAELDAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372873206 188 ETQVGNELAPLKGKG--YFVFHDAYGYFEKQFGLTPLGHFTVNPEIQPGAQRLHEIRTQLVEQKATCVFAEPQFRPAVVE 265
Cdd:pfam01297 148 DAEIKEQLASIPEKTrkLVTSHDAFGYLARAYGLEQVGIQGVSPESEPSAADLAELIDLIKEKKVKAIFVEPQVSPKLAE 227
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1372873206 266 SVARGTSVRM-GTLDPLGTNIKLGKTSYSEFLSQLANQYASC 306
Cdd:pfam01297 228 TVAKETGVKVlGPLYTDSLGEPGGGATYLDLMRHNLDTLAEA 269
|
|
| anch_rpt_subst |
TIGR03772 |
anchored repeat ABC transporter, substrate-binding protein; Members of this protein family are ... |
135-307 |
2.57e-15 |
|
anchored repeat ABC transporter, substrate-binding protein; Members of this protein family are ABC transporter permease subunits as identified by pfam00950, but additionally contain the Actinobacterial insert domain described by TIGR03769. Some homologs (lacking the insert) have been described as transporters of manganese or of chelated iron. Members of this family typically are found along with an ATP-binding cassette protein, a permease, and an LPXTG-anchored protein with two or three copies of the TIGR03769 insert that occurs just once in this protein family. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163484 [Multi-domain] Cd Length: 479 Bit Score: 76.05 E-value: 2.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372873206 135 HHHGDFNMHLWLSPEIARATAVAIHGKLVELMPQSRAKLDANLKDFEAQLASTETQVGNELA--PLKGKGYFVFHDAYGY 212
Cdd:TIGR03772 304 HVHGEIDPHLWHNVKNAIAYVEVIRDKLIEVDPRGAQAYRSNASAYIHRLERLDTYVRRTIAtiPPSRRHLITTHDAYSY 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372873206 213 FEKQFGLTPLGHFTVNPEIQPGAQRLHEIRTQLVEQKATCVFAEPQF--RPAVVESVARGTSVRMGTL--DPLGTNIklg 288
Cdd:TIGR03772 384 LGQAYGLNIAGFVTPNPAVEPSLADRRRLTRTIENLKVPAVFLEPNLaaRSTTLNEIADELGVRVCAIygDTFDDDV--- 460
|
170
....*....|....*....
gi 1372873206 289 kTSYSEFLSQLANQYASCL 307
Cdd:TIGR03772 461 -TNYVDLMRFNADSLADCL 478
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| znuA |
PRK09545 |
zinc ABC transporter substrate-binding protein ZnuA; |
2-308 |
0e+00 |
|
zinc ABC transporter substrate-binding protein ZnuA;
Pssm-ID: 236558 [Multi-domain] Cd Length: 311 Bit Score: 598.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372873206 2 LHKKTLLFAALSAALWGGATQAADAAVVASLKPVGFIASAIADGVTETEVLLPDGASEHDYSLRPSDVKRLQNADLVVWV 81
Cdd:PRK09545 1 LHKKTLLFAALLAALLGGATQAANAAVVTSIKPLGFIASAIADGVTETEVLLPDGASPHDYSLRPSDVKRLQSADLVVWV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372873206 82 GPEMEAFMQKPVSKLPGAKQVTIAQLEDVKPLLMKSI----HGDDDDHDHAEKSDEDHHHGDFNMHLWLSPEIARATAVA 157
Cdd:PRK09545 81 GPEMEAFLEKPVSKLPENKQVTIAQLPDVKPLLMKGAhddhHDDDHDHAGHEKSDEDHHHGEYNMHIWLSPEIARATAVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372873206 158 IHGKLVELMPQSRAKLDANLKDFEAQLASTETQVGNELAPLKGKGYFVFHDAYGYFEKQFGLTPLGHFTVNPEIQPGAQR 237
Cdd:PRK09545 161 IHDKLVELMPQSKAKLDANLKDFEAQLAQTDKQIGNQLAPVKGKGYFVFHDAYGYFEKHYGLTPLGHFTVNPEIQPGAQR 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1372873206 238 LHEIRTQLVEQKATCVFAEPQFRPAVVESVARGTSVRMGTLDPLGTNIKLGKTSYSEFLSQLANQYASCLK 308
Cdd:PRK09545 241 LHEIRTQLVEQKATCVFAEPQFRPAVIESVAKGTSVRMGTLDPLGTNIKLGKDSYSEFLSQLANQYASCLK 311
|
|
| ZnuA |
COG4531 |
ABC-type Zn2+ transport system, periplasmic component/surface adhesin ZnuA [Inorganic ion ... |
17-307 |
4.32e-169 |
|
ABC-type Zn2+ transport system, periplasmic component/surface adhesin ZnuA [Inorganic ion transport and metabolism];
Pssm-ID: 443599 [Multi-domain] Cd Length: 300 Bit Score: 470.85 E-value: 4.32e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372873206 17 WGGATQAADAAVVASLKPVGFIASAIADGVTETEVLLPDGASEHDYSLRPSDVKRLQNADLVVWVGPEMEAFMQKPVSKL 96
Cdd:COG4531 1 LASAAAAAAPRVVTSIKPLHSLVAAVMDGVGEPELLLPPGASPHDYALRPSDARALQDADLVFWVGPDLEPFLEKPLETL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372873206 97 -PGAKQVTIAQLEDVKPLLMKSI--------HGDDDDHDHAEKSDEDHHHGDFNMHLWLSPEIARATAVAIHGKLVELMP 167
Cdd:COG4531 81 aPDAKVVELLELPGLTLLPFREGgdfehhdhHDEHHHHHHHHDDHHDHHHGGYDPHLWLSPENAKAWAAAIADALSELDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372873206 168 QSRAKLDANLKDFEAQLASTETQVGNELAPLKGKGYFVFHDAYGYFEKQFGLTPLGHFTVNPEIQPGAQRLHEIRTQLVE 247
Cdd:COG4531 161 ENAATYQANAAAFEARLDALDAEIAAQLAPVKGKPFFVFHDAYQYFEKRFGLNALGAITLNPEIQPGAKRLAEIREKLKE 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372873206 248 QKATCVFAEPQFRPAVVESVARGTSVRMGTLDPLGTNIKLGKTSYSEFLSQLANQYASCL 307
Cdd:COG4531 241 LGAVCVFAEPQFNPALVETVAEGTGVRTGVLDPLGADLEPGPDLYFQLLRQLADSLASCL 300
|
|
| ZnuA |
cd01019 |
Zinc binding protein ZnuA. These proteins have been shown to function as initial receptors in ... |
23-307 |
3.01e-145 |
|
Zinc binding protein ZnuA. These proteins have been shown to function as initial receptors in the ABC uptake of Zn2+. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. They are comprised of two globular subdomains connected by a single helix and bind their specific ligands in the cleft between these domains. 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: 238501 [Multi-domain] Cd Length: 286 Bit Score: 410.22 E-value: 3.01e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372873206 23 AADAAVVASLKPVGFIASAIADGVTETEVLLPDGASEHDYSLRPSDVKRLQNADLVVWVGPEMEAFMQKPVSKLPGAKQV 102
Cdd:cd01019 1 AAEASVLTSIKPLGFIAAAIMGGVGEVEVLVPPGASPHDYELRPSDARKLQEADLVVWIGPDLEAFLDKVLQGRKKGKVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372873206 103 TIAQLEDVKPLLMKSIH-GDDDDHDHAEKSDEDHHHGDFNMHLWLSPEIARATAVAIHGKLVELMPQSRAKLDANLKDFE 181
Cdd:cd01019 81 TLAKLIDLKTLEDGASHgDHEHDHEHAHGEHDGHEEGGLDPHLWLSPENAAEVAQAVAEKLSALDPDNAATYAANLEAFN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372873206 182 AQLASTETQVGNELAPLKGKGYFVFHDAYGYFEKQFGLTPLGHFTVNPEIQPGAQRLHEIRTQLVEQKATCVFAEPQFRP 261
Cdd:cd01019 161 ARLAELDATIKERLAPVKTKPFFVFHDAYGYFEKRYGLTQAGVFTIDPEIDPGAKRLAKIRKEIKEKGATCVFAEPQFHP 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1372873206 262 AVVESVARGTSVRMGTLDPLGTNIKLGKTSYSEFLSQLANQYASCL 307
Cdd:cd01019 241 KIAETLAEGTGAKVGELDPLGGLIELGKNSYVNFLRNLADSLASCL 286
|
|
| ZnuA |
pfam01297 |
Zinc-uptake complex component A periplasmic; ZnuA includes periplasmic solute binding proteins ... |
28-306 |
1.70e-81 |
|
Zinc-uptake complex component A periplasmic; ZnuA includes periplasmic solute binding proteins such as TroA that interacts with an ATP-binding cassette transport system in Treponema pallidum. ZnuA is part of the bacterial zinc-uptake complex ZnuABC, whose components are the following families, ZinT, pfam09223, pfam00950, pfam00005, all of which are regulated by the transcription-regulator family FUR, pfam01475. ZinT acts as a Zn2+-buffering protein that delivers Zn2+ to ZnuA (TroA), a high-affinity zinc-uptake protein. In Gram-negative bacteria the ZnuABC transporter system ensures an adequate import of zinc in Zn2+-poor environments, such as those encountered by pathogens within the infected host.
Pssm-ID: 460151 [Multi-domain] Cd Length: 269 Bit Score: 247.47 E-value: 1.70e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372873206 28 VVASLKPVGFIASAIADGVTETEVLLPDGASEHDYSLRPSDVKRLQNADLVVWVGPEMEAFMQKPVSKLPGAKQVTIAQl 107
Cdd:pfam01297 1 VVATTYPLADLAKQIGGDRVEVTSLVPPGADPHDYEPTPSDIAALSDADLVVYNGLGLEPWLDKLLEALPNKKVVDASE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372873206 108 edvkpllmksihGDDDDHDHAEKSDEDHHHGDFNMHLWLSPEIARATAVAIHGKLVELMPQSRAKLDANLKDFEAQLAST 187
Cdd:pfam01297 80 ------------GVELLDEEGEEEDHDGHDHGYDPHVWLDPKNAKKMAENIADALSELDPANAATYEANAAAYLAELDAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372873206 188 ETQVGNELAPLKGKG--YFVFHDAYGYFEKQFGLTPLGHFTVNPEIQPGAQRLHEIRTQLVEQKATCVFAEPQFRPAVVE 265
Cdd:pfam01297 148 DAEIKEQLASIPEKTrkLVTSHDAFGYLARAYGLEQVGIQGVSPESEPSAADLAELIDLIKEKKVKAIFVEPQVSPKLAE 227
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1372873206 266 SVARGTSVRM-GTLDPLGTNIKLGKTSYSEFLSQLANQYASC 306
Cdd:pfam01297 228 TVAKETGVKVlGPLYTDSLGEPGGGATYLDLMRHNLDTLAEA 269
|
|
| ZnuA |
COG0803 |
ABC-type Zn uptake system ZnuABC, Zn-binding component ZnuA [Inorganic ion transport and ... |
18-290 |
1.04e-60 |
|
ABC-type Zn uptake system ZnuABC, Zn-binding component ZnuA [Inorganic ion transport and metabolism];
Pssm-ID: 440566 [Multi-domain] Cd Length: 286 Bit Score: 195.08 E-value: 1.04e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372873206 18 GGATQAADAA--VVASLKPVGFIASAIA-DGVtETEVLLPDGASEHDYSLRPSDVKRLQNADLVVWVGPEMEAFMQKPVS 94
Cdd:COG0803 20 SAAASSAAGKlkVVATFSPLADLAKQIGgDKV-EVTSLVPPGADPHDYEPTPSDIAKLAKADLVVYNGLGLEGWLDKLLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372873206 95 KLPGAKQVTIAQLEDVKPLlmksihgddddhdhaeKSDEDHHHGDFNMHLWLSPEIARATAVAIHGKLVELMPQSRAKLD 174
Cdd:COG0803 99 AAGNPGVPVVDASEGIDLL----------------ELEEGHDHGEPDPHVWLDPKNAKKVAENIADALAELDPANAAYYE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372873206 175 ANLKDFEAQLASTETQVGNELAPLKGKGYFVFHDAYGYFEKQFGLTPLGHFTVNPEIQPGAQRLHEIRTQLVEQKATCVF 254
Cdd:COG0803 163 ANAAAYLAELDALDAEIKAKLAAIPGRKLVTSHDAFGYLARAYGLEVVAIQGISPGSEPSPADLAELIDLIKEEGVKAIF 242
|
250 260 270
....*....|....*....|....*....|....*.
gi 1372873206 255 AEPQFRPAVVESVARGTSVRMGTLDPLGTNIKLGKT 290
Cdd:COG0803 243 VESQVSPKLAETLAEETGVKVLYLDSLGGPGGPGDT 278
|
|
| AdcA |
cd01017 |
Metal binding protein AdcA. These proteins have been shown to function in the ABC uptake of ... |
28-297 |
2.23e-42 |
|
Metal binding protein AdcA. These proteins have been shown to function in the ABC uptake of Zn2+ and Mn2+ and in competence for genetic transformation and adhesion. The AdcA proteins belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. They are comprised of two globular subdomains connected by a long alpha helix and they bind their ligand in the cleft between these domains. In addition, many of these proteins have a low complexity region containing metal binding histidine-rich motif (repetitive HDH sequence).
Pssm-ID: 238499 [Multi-domain] Cd Length: 282 Bit Score: 147.44 E-value: 2.23e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372873206 28 VVASLKPVGFIASAIADGVTETEVLLPDGASEHDYSLRPSDVKRLQNADLVVWVGPEMEAFMQKPVSKLPGAKQVTIAQL 107
Cdd:cd01017 6 VVTTFYPLYEFTKAIGGDKADVKLIIPAGTEPHDFEPSPKDIARIADADVFVYNGLGMETWAEKVLKSLQNKKLKVVEAS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372873206 108 EDVKPLlmKSIHGDDDdhdhaEKSDEDHHHGDFNMHLWLSPEIARATAVAIHGKLVELMPQSRAKLDANLKDFEAQLAST 187
Cdd:cd01017 86 KGIKLL--KAGGAEHD-----HDHSHSHHHGDYDPHVWLSPVLAIQQVENIKDALIKLDPDNKEYYEKNAAAYAKKLEAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372873206 188 ETQVGNELAPLKGKGYFVFHDAYGYFEKQFGLTPLGHFTVNPEIQPGAQRLHEIRTQLVEQKATCVFAEPQFRPAVVESV 267
Cdd:cd01017 159 DQEYRAKLAKAKGKTFVTQHAAFGYLARRYGLKQIAIVGVSPEVEPSPKQLAELVEFVKKSDVKYIFFEENASSKIAETL 238
|
250 260 270
....*....|....*....|....*....|
gi 1372873206 268 ARGTSVRMGTLDPLGTNIKLGKTSYSEFLS 297
Cdd:cd01017 239 AKETGAKLLVLNPLETLTKEEIDDGKDYFS 268
|
|
| ZntC |
cd01018 |
Metal binding protein ZntC. These proteins are predicted to function as initial receptors in ... |
24-284 |
6.79e-42 |
|
Metal binding protein ZntC. 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. They are comprised of two globular subdomains connected by a long alpha helix and bind their specific ligands in the cleft between these domains. In addition, many of these proteins possess a metal-binding histidine-rich motif (repetitive HDH sequence).
Pssm-ID: 238500 [Multi-domain] Cd Length: 266 Bit Score: 145.58 E-value: 6.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372873206 24 ADAAVVASLKPVGFIASAIADGVTETEVLLPDGASEHDYSLRPSDVKRLQNADLVVWVGPEME-AFMQKPVSKLPGAKQV 102
Cdd:cd01018 1 DKPTVAVSIEPQKYFVEKIAGDTVDVVVLVPPGSNPHTYEPKPQQMKKLSEADLYFRIGLGFEeVWLERFRSNNPKMQVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372873206 103 TIAQleDVKPLLMKSIHGDdddhdhAEKSDEDHHHGDFNMHLWLSPEIARATAVAIHGKLVELMPQSRAKLDANLKDFEA 182
Cdd:cd01018 81 NMSK--GITLIPMADHHHH------HHGEHEHHHHGNYDPHIWLSPANAKIMAENIYEALAELDPQNATYYQANLDALLA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372873206 183 QLASTETQVGNELAPLKGKGYFVFHDAYGYFEKQFGLTplghfTVNPEIQ---PGAQRLHEIRTQLVEQKATCVFAEPQF 259
Cdd:cd01018 153 ELDALDSEIRTILSKLKQRAFMVYHPAWGYFARDYGLT-----QIPIEEEgkePSPADLKRLIDLAKEKGVRVVFVQPQF 227
|
250 260
....*....|....*....|....*
gi 1372873206 260 RPAVVESVARGTSVRMGTLDPLGTN 284
Cdd:cd01018 228 STKSAEAIAREIGAKVVTIDPLAAD 252
|
|
| PsaA |
cd01137 |
Metal binding protein PsaA. These proteins have been shown to function as initial receptors ... |
20-298 |
5.75e-30 |
|
Metal binding protein PsaA. These proteins have been shown to function as initial receptors in ABC transport of Mn2+ and as surface adhesins 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 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: 238557 [Multi-domain] Cd Length: 287 Bit Score: 114.68 E-value: 5.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372873206 20 ATQAADAAVVASLKPVGFIASAIADGVTETEVLLPDGASEHDYSLRPSDVKRLQNADLVVWVGPEMEAFMQKPVSKLpGA 99
Cdd:cd01137 12 ATAASKLKVVATFSILADIARNIAGDRVNVTSIVPPGADPHEYEPTPSDIKKLSKADLILYNGLNLEPWLERLVKNA-GK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372873206 100 KQVTIAQLEDVKPLLMksihgddddhdhaeksDEDHHHGDFNMHLWLSPEIARATAVAIHGKLVELMPQSRAKLDANLKD 179
Cdd:cd01137 91 DVPVVAVSEGIDPIPL----------------EEGHYKGKPDPHAWMSPKNAIIYVKNIAKALSEADPANAETYQKNAAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372873206 180 FEAQLASTETQVGNELAPL-KGKGYFVF-HDAYGYFEKQFGLTPLGHFTVNPEIQPGAQRLHEIRTQLVEQKATCVFAEP 257
Cdd:cd01137 155 YKAKLKALDEWAKAKFATIpAEKRKLVTsEGAFSYFAKAYGLKEAYLWPINTEEEGTPKQVATLIEQVKKEKVPAVFVES 234
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1372873206 258 QFRPAVVESVARgtsvrmgtldplGTNIKLGKTSYSEFLSQ 298
Cdd:cd01137 235 TVNDRLMKQVAK------------ETGAKIGGQLYTDSLSE 263
|
|
| TroA |
cd01016 |
Metal binding protein TroA. These proteins have been shown to function as initial receptors in ... |
28-294 |
1.11e-20 |
|
Metal binding protein TroA. These proteins have been shown to function as initial receptors in ABC transport of Zn2+ and possibly Fe3+ in many eubacterial species. The TroA proteins 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. In addition, these proteins sometimes have a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence).
Pssm-ID: 238498 [Multi-domain] Cd Length: 276 Bit Score: 89.34 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372873206 28 VVASLKPVGFIASAIADGVTETEVLLPDGASEHDYSLRPSDVKRLQNADLVVWVGPEMEAFMQKPVSKLPGAKQV-TIAQ 106
Cdd:cd01016 4 VVTTTGMIADAVENIGGDHVEVTGLMGPGVDPHLYKATAGDVEKLQNADVVFYNGLHLEGKMSDVLSKLGSSKSViALED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372873206 107 LEDVKPLLMksihgddddhdhaekSDEDhhhGDFNMHLWLSPEIARATAVAIHGKLVELMPQSRAKLDANLKDFEAQLAS 186
Cdd:cd01016 84 TLDRSQLIL---------------DEEE---GTYDPHIWFDVKLWKYAVKAVAEVLSEKLPEHKDEFQANSEAYVEELDS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372873206 187 TETQVGNELAPL-KGKGYFVF-HDAYGYFEKQFGLTPLGHFTVNPEIQPGAQRLHEIRTQLVEQKATCVFAEPQFRPAVV 264
Cdd:cd01016 146 LDAYAKKKIAEIpEQQRVLVTaHDAFGYFGRAYGFEVKGLQGISTDSEAGLRDINELVDLIVERKIKAIFVESSVNQKSI 225
|
250 260 270
....*....|....*....|....*....|
gi 1372873206 265 ESVARGTSVRmgtldplGTNIKLGKTSYSE 294
Cdd:cd01016 226 EALQDAVKAR-------GHDVQIGGELYSD 248
|
|
| TroA_c |
cd01145 |
Periplasmic binding protein TroA_c. These proteins are predicted to function as initial ... |
28-237 |
3.90e-18 |
|
Periplasmic binding protein TroA_c. 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: 238565 [Multi-domain] Cd Length: 203 Bit Score: 81.01 E-value: 3.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372873206 28 VVASLKPVGFIASAIADGVTETEVLLPDGASEHDYSLRPSDVKRLQNADLVVWVGPEMEAFMQKPVSKLPGAKQVTIAQL 107
Cdd:cd01145 5 VVVTFPDLKDLVREVAGDAVIVSALTPPGVDPHQYQLKPSDIAKMRKADLVVTSGHELEGFEPKLAELSSNSKVQPGIKI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372873206 108 EDVKPLlmksihgdddDHDHAEKSDEDHHHGDfNMHLWLSPEIARATAVAIHGKLVELMPQSRAKLDANLKDFEAQLAST 187
Cdd:cd01145 85 LIEDSD----------TVGMVDRAMGDYHGKG-NPHVWLDPNNAPALAKALADALIELDPSEQEEYKENLRVFLAKLNKL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1372873206 188 ETQVGNELAPLKGKGYFVFHDAYGYFEKQFGLTPLGHFTVNPEIQPGAQR 237
Cdd:cd01145 154 LREWERQFEGLKGIQVVAYHPSYQYLADWLGIEVVASLEPLPELPPTSSH 203
|
|
| TroA_b |
cd01020 |
Metal binding protein TroA_b. These proteins are predicted to function as initial receptors ... |
27-258 |
1.52e-15 |
|
Metal binding protein TroA_b. 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: 238502 [Multi-domain] Cd Length: 264 Bit Score: 74.78 E-value: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372873206 27 AVVASLKPVGFIASAIA-DGVTETEVLLPDGASEHDYSLRPSDVKRLQNADLVVWVGPemeafmqkpvsklpgakqvtia 105
Cdd:cd01020 4 NVVASTNFWGSVAEAVGgDHVEVTSIITNPDVDPHDFEPTPTDAAKVSTADIVVYNGG---------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372873206 106 qleDVKPLLMKSIHGDDDDHDHAEKSDEDHHHGDFNMHLWLSPEIARATAVAIHGKLVELMPQSRAKLDANLKDFEAQLA 185
Cdd:cd01020 62 ---GYDPWMTKLLADTKDVIVIAADLDGHDDKEGDNPHLWYDPETMSKVANALADALVKADPDNKKYYQANAKKFVASLK 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1372873206 186 STETQVGNELAPLKGKGYFVFHDAYGYFEKQFGL---TPLGHF-TVNPEIQPGAQRLHEIRTQLVEQKATCVFAEPQ 258
Cdd:cd01020 139 PLAAKIAELSAKYKGAPVAATEPVFDYLLDALGMkerTPKGYTaTTESETEPSPADIAAFQNAIKNRQIDALIVNPQ 215
|
|
| anch_rpt_subst |
TIGR03772 |
anchored repeat ABC transporter, substrate-binding protein; Members of this protein family are ... |
135-307 |
2.57e-15 |
|
anchored repeat ABC transporter, substrate-binding protein; Members of this protein family are ABC transporter permease subunits as identified by pfam00950, but additionally contain the Actinobacterial insert domain described by TIGR03769. Some homologs (lacking the insert) have been described as transporters of manganese or of chelated iron. Members of this family typically are found along with an ATP-binding cassette protein, a permease, and an LPXTG-anchored protein with two or three copies of the TIGR03769 insert that occurs just once in this protein family. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163484 [Multi-domain] Cd Length: 479 Bit Score: 76.05 E-value: 2.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372873206 135 HHHGDFNMHLWLSPEIARATAVAIHGKLVELMPQSRAKLDANLKDFEAQLASTETQVGNELA--PLKGKGYFVFHDAYGY 212
Cdd:TIGR03772 304 HVHGEIDPHLWHNVKNAIAYVEVIRDKLIEVDPRGAQAYRSNASAYIHRLERLDTYVRRTIAtiPPSRRHLITTHDAYSY 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372873206 213 FEKQFGLTPLGHFTVNPEIQPGAQRLHEIRTQLVEQKATCVFAEPQF--RPAVVESVARGTSVRMGTL--DPLGTNIklg 288
Cdd:TIGR03772 384 LGQAYGLNIAGFVTPNPAVEPSLADRRRLTRTIENLKVPAVFLEPNLaaRSTTLNEIADELGVRVCAIygDTFDDDV--- 460
|
170
....*....|....*....
gi 1372873206 289 kTSYSEFLSQLANQYASCL 307
Cdd:TIGR03772 461 -TNYVDLMRFNADSLADCL 478
|
|
| |
