|
Name |
Accession |
Description |
Interval |
E-value |
| PsaA |
cd01137 |
Metal binding protein PsaA. These proteins have been shown to function as initial receptors ... |
7-292 |
2.22e-147 |
|
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: 414.75 E-value: 2.22e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528028 7 VVALSSLLVSPLVIAKELNVVASFSVLGDMVSQIGGPYVHVTDLVQPDGDPHEFEPSPKDSKTLAQADVVFVNGLGLEGW 86
Cdd:cd01137 1 LAACASLGSSPATAASKLKVVATFSILADIARNIAGDRVNVTSIVPPGADPHEYEPTPSDIKKLSKADLILYNGLNLEPW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528028 87 LDRLMKASGYRGEVITASNGIDTLKMKE-DGTTITDPHAWNSMKNGIVYAHNIVNGLSKADPEHASDYRKQGDSYIQQLQ 165
Cdd:cd01137 81 LERLVKNAGKDVPVVAVSEGIDPIPLEEgHYKGKPDPHAWMSPKNAIIYVKNIAKALSEADPANAETYQKNAAAYKAKLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528028 166 QLDNYATQTFAAIPREKRKVLTSHDAFGYFAAAYGVRFLSPVGYSTESEASSKNVAKLINQIKREHVKLYFIENQTDPRL 245
Cdd:cd01137 161 ALDEWAKAKFATIPAEKRKLVTSEGAFSYFAKAYGLKEAYLWPINTEEEGTPKQVATLIEQVKKEKVPAVFVESTVNDRL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 24528028 246 VKQIANASGAQAGGELYPEALTDSSGLAATYTAAFKHNVDTLAAGMK 292
Cdd:cd01137 241 MKQVAKETGAKIGGQLYTDSLSEKGGPADTYLDMMEHNLDTIVEGLG 287
|
|
| ZnuA |
COG0803 |
ABC-type Zn uptake system ZnuABC, Zn-binding component ZnuA [Inorganic ion transport and ... |
1-283 |
2.00e-109 |
|
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: 318.34 E-value: 2.00e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528028 1 MKRSILVVALSSLLV------SPLVIAKELNVVASFSVLGDMVSQIGGPYVHVTDLVQPDGDPHEFEPSPKDSKTLAQAD 74
Cdd:COG0803 1 MKRLLLALLLLAALLlagcsaAASSAAGKLKVVATFSPLADLAKQIGGDKVEVTSLVPPGADPHDYEPTPSDIAKLAKAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528028 75 VVFVNGLGLEGWLDRLMKASGYRG-EVITASNGIDTLKMKE-DGTTITDPHAWNSMKNGIVYAHNIVNGLSKADPEHASD 152
Cdd:COG0803 81 LVVYNGLGLEGWLDKLLEAAGNPGvPVVDASEGIDLLELEEgHDHGEPDPHVWLDPKNAKKVAENIADALAELDPANAAY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528028 153 YRKQGDSYIQQLQQLDNYATQTFAAIPRekRKVLTSHDAFGYFAAAYGVRFLSPVGYSTESEASSKNVAKLINQIKREHV 232
Cdd:COG0803 161 YEANAAAYLAELDALDAEIKAKLAAIPG--RKLVTSHDAFGYLARAYGLEVVAIQGISPGSEPSPADLAELIDLIKEEGV 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 24528028 233 KLYFIENQTDPRLVKQIANASGAQAggeLYPEALTDSSGLAATYTAAFKHN 283
Cdd:COG0803 239 KAIFVESQVSPKLAETLAEETGVKV---LYLDSLGGPGGPGDTYLDMMRHN 286
|
|
| ZnuA |
pfam01297 |
Zinc-uptake complex component A periplasmic; ZnuA includes periplasmic solute binding proteins ... |
26-290 |
4.10e-106 |
|
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: 309.48 E-value: 4.10e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528028 26 VVASFSVLGDMVSQIGGPYVHVTDLVQPDGDPHEFEPSPKDSKTLAQADVVFVNGLGLEGWLDRLMKASGyRGEVITASN 105
Cdd:pfam01297 1 VVATTYPLADLAKQIGGDRVEVTSLVPPGADPHDYEPTPSDIAALSDADLVVYNGLGLEPWLDKLLEALP-NKKVVDASE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528028 106 GIDTLKMKEDGTTI------TDPHAWNSMKNGIVYAHNIVNGLSKADPEHASDYRKQGDSYIQQLQQLDNYATQTFAAIP 179
Cdd:pfam01297 80 GVELLDEEGEEEDHdghdhgYDPHVWLDPKNAKKMAENIADALSELDPANAATYEANAAAYLAELDALDAEIKEQLASIP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528028 180 REKRKVLTSHDAFGYFAAAYGVRFLSPVGYSTESEASSKNVAKLINQIKREHVKLYFIENQTDPRLVKQIANASGAQAGG 259
Cdd:pfam01297 160 EKTRKLVTSHDAFGYLARAYGLEQVGIQGVSPESEPSAADLAELIDLIKEKKVKAIFVEPQVSPKLAETVAKETGVKVLG 239
|
250 260 270
....*....|....*....|....*....|.
gi 24528028 260 ELYPEALTDSSGlAATYTAAFKHNVDTLAAG 290
Cdd:pfam01297 240 PLYTDSLGEPGG-GATYLDLMRHNLDTLAEA 269
|
|
| AztC |
NF040870 |
zinc ABC transporter substrate-binding protein AztC; |
26-291 |
5.31e-88 |
|
zinc ABC transporter substrate-binding protein AztC;
Pssm-ID: 468807 [Multi-domain] Cd Length: 277 Bit Score: 263.75 E-value: 5.31e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528028 26 VVASFSVLGDMVSQIGGPYVHVTDLVQPDGDPHEFEPSPKDSKTLAQADVVFVNGLGL-EGWLDRLMKASGYRGEVITAS 104
Cdd:NF040870 1 VVVTTNILGDLARNVVGDRAEVTTLMKPDADPHSFEPSAADAAALERADLVVVNGLGLeEGFLRHLIAASATGAPVVEVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528028 105 NGIDTLKMKEDGTTI-------TDPHAWNSMKNGIVYAHNIVNGLSKADPEHASDYRKQGDSYIQQLQQLDNYATQTFAA 177
Cdd:NF040870 81 DGVDPLPYPEGGHYHfeagagpPDPHFWTDPARARDAVDNIADAFCEADDGDCAAYRANAAAYRAELDELDAEMREAFAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528028 178 IPREKRKVLTSHDAFGYFAAAYGVRFLSPV--GYSTESEASSKNVAKLINQIKREHVKLYFIENQTDPRLVKQIANASGA 255
Cdd:NF040870 161 IPADRRTLVTNHHVFGYLAERYGFRVLGAVipSGSTLASPSAADLASLARAIREAGVPAIFAESSQPPRLAEVLASEAGL 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 24528028 256 QAGG-ELYPEALTDSSGLAATYTAAFKHNVDTLAAGM 291
Cdd:NF040870 241 DVGVvELYSESLSEPDGGAATYLDMMRANAEAIVDGL 277
|
|
| anch_rpt_subst |
TIGR03772 |
anchored repeat ABC transporter, substrate-binding protein; Members of this protein family are ... |
121-288 |
5.83e-28 |
|
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: 112.26 E-value: 5.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528028 121 DPHAWNSMKNGIVYAHNIVNGLSKADPEHASDYRKQGDSYIQQLQQLDNYATQTFAAIPREKRKVLTSHDAFGYFAAAYG 200
Cdd:TIGR03772 310 DPHLWHNVKNAIAYVEVIRDKLIEVDPRGAQAYRSNASAYIHRLERLDTYVRRTIATIPPSRRHLITTHDAYSYLGQAYG 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528028 201 VRFLSPVGYSTESEASSKNVAKLINQIKREHVKLYFIENQTDPR--LVKQIANASGAQAgGELYPEALTDSsglAATYTA 278
Cdd:TIGR03772 390 LNIAGFVTPNPAVEPSLADRRRLTRTIENLKVPAVFLEPNLAARstTLNEIADELGVRV-CAIYGDTFDDD---VTNYVD 465
|
170
....*....|
gi 24528028 279 AFKHNVDTLA 288
Cdd:TIGR03772 466 LMRFNADSLA 475
|
|
| znuA |
PRK09545 |
zinc ABC transporter substrate-binding protein ZnuA; |
2-258 |
1.01e-07 |
|
zinc ABC transporter substrate-binding protein ZnuA;
Pssm-ID: 236558 [Multi-domain] Cd Length: 311 Bit Score: 52.32 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528028 2 KRSILVVALSSLLVSPLVIAKELNVVASFSVLGDMVSQIG-GpyVHVTDLVQPDG-DPHEFEPSPKDSKTLAQADVVFVN 79
Cdd:PRK09545 3 KKTLLFAALLAALLGGATQAANAAVVTSIKPLGFIASAIAdG--VTETEVLLPDGaSPHDYSLRPSDVKRLQSADLVVWV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528028 80 GLGLEGWLDRLMkASGYRGEVITASN--GIDTLKMKEDGTTITDP---------------------HAWNSMKNGIVYAH 136
Cdd:PRK09545 81 GPEMEAFLEKPV-SKLPENKQVTIAQlpDVKPLLMKGAHDDHHDDdhdhagheksdedhhhgeynmHIWLSPEIARATAV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528028 137 NIVNGLSKADPEH----ASDYRKqgdsYIQQLQQLDNYATQTFAaiPREKRKVLTSHDAFGYFAAAYGvrfLSPVGYST- 211
Cdd:PRK09545 160 AIHDKLVELMPQSkaklDANLKD----FEAQLAQTDKQIGNQLA--PVKGKGYFVFHDAYGYFEKHYG---LTPLGHFTv 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 24528028 212 --ESEASSKNVAKLINQIKREHVKLYFIENQTDPRLVKQIANASGAQAG 258
Cdd:PRK09545 231 npEIQPGAQRLHEIRTQLVEQKATCVFAEPQFRPAVIESVAKGTSVRMG 279
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PsaA |
cd01137 |
Metal binding protein PsaA. These proteins have been shown to function as initial receptors ... |
7-292 |
2.22e-147 |
|
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: 414.75 E-value: 2.22e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528028 7 VVALSSLLVSPLVIAKELNVVASFSVLGDMVSQIGGPYVHVTDLVQPDGDPHEFEPSPKDSKTLAQADVVFVNGLGLEGW 86
Cdd:cd01137 1 LAACASLGSSPATAASKLKVVATFSILADIARNIAGDRVNVTSIVPPGADPHEYEPTPSDIKKLSKADLILYNGLNLEPW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528028 87 LDRLMKASGYRGEVITASNGIDTLKMKE-DGTTITDPHAWNSMKNGIVYAHNIVNGLSKADPEHASDYRKQGDSYIQQLQ 165
Cdd:cd01137 81 LERLVKNAGKDVPVVAVSEGIDPIPLEEgHYKGKPDPHAWMSPKNAIIYVKNIAKALSEADPANAETYQKNAAAYKAKLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528028 166 QLDNYATQTFAAIPREKRKVLTSHDAFGYFAAAYGVRFLSPVGYSTESEASSKNVAKLINQIKREHVKLYFIENQTDPRL 245
Cdd:cd01137 161 ALDEWAKAKFATIPAEKRKLVTSEGAFSYFAKAYGLKEAYLWPINTEEEGTPKQVATLIEQVKKEKVPAVFVESTVNDRL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 24528028 246 VKQIANASGAQAGGELYPEALTDSSGLAATYTAAFKHNVDTLAAGMK 292
Cdd:cd01137 241 MKQVAKETGAKIGGQLYTDSLSEKGGPADTYLDMMEHNLDTIVEGLG 287
|
|
| ZnuA |
COG0803 |
ABC-type Zn uptake system ZnuABC, Zn-binding component ZnuA [Inorganic ion transport and ... |
1-283 |
2.00e-109 |
|
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: 318.34 E-value: 2.00e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528028 1 MKRSILVVALSSLLV------SPLVIAKELNVVASFSVLGDMVSQIGGPYVHVTDLVQPDGDPHEFEPSPKDSKTLAQAD 74
Cdd:COG0803 1 MKRLLLALLLLAALLlagcsaAASSAAGKLKVVATFSPLADLAKQIGGDKVEVTSLVPPGADPHDYEPTPSDIAKLAKAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528028 75 VVFVNGLGLEGWLDRLMKASGYRG-EVITASNGIDTLKMKE-DGTTITDPHAWNSMKNGIVYAHNIVNGLSKADPEHASD 152
Cdd:COG0803 81 LVVYNGLGLEGWLDKLLEAAGNPGvPVVDASEGIDLLELEEgHDHGEPDPHVWLDPKNAKKVAENIADALAELDPANAAY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528028 153 YRKQGDSYIQQLQQLDNYATQTFAAIPRekRKVLTSHDAFGYFAAAYGVRFLSPVGYSTESEASSKNVAKLINQIKREHV 232
Cdd:COG0803 161 YEANAAAYLAELDALDAEIKAKLAAIPG--RKLVTSHDAFGYLARAYGLEVVAIQGISPGSEPSPADLAELIDLIKEEGV 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 24528028 233 KLYFIENQTDPRLVKQIANASGAQAggeLYPEALTDSSGLAATYTAAFKHN 283
Cdd:COG0803 239 KAIFVESQVSPKLAETLAEETGVKV---LYLDSLGGPGGPGDTYLDMMRHN 286
|
|
| ZnuA |
pfam01297 |
Zinc-uptake complex component A periplasmic; ZnuA includes periplasmic solute binding proteins ... |
26-290 |
4.10e-106 |
|
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: 309.48 E-value: 4.10e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528028 26 VVASFSVLGDMVSQIGGPYVHVTDLVQPDGDPHEFEPSPKDSKTLAQADVVFVNGLGLEGWLDRLMKASGyRGEVITASN 105
Cdd:pfam01297 1 VVATTYPLADLAKQIGGDRVEVTSLVPPGADPHDYEPTPSDIAALSDADLVVYNGLGLEPWLDKLLEALP-NKKVVDASE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528028 106 GIDTLKMKEDGTTI------TDPHAWNSMKNGIVYAHNIVNGLSKADPEHASDYRKQGDSYIQQLQQLDNYATQTFAAIP 179
Cdd:pfam01297 80 GVELLDEEGEEEDHdghdhgYDPHVWLDPKNAKKMAENIADALSELDPANAATYEANAAAYLAELDALDAEIKEQLASIP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528028 180 REKRKVLTSHDAFGYFAAAYGVRFLSPVGYSTESEASSKNVAKLINQIKREHVKLYFIENQTDPRLVKQIANASGAQAGG 259
Cdd:pfam01297 160 EKTRKLVTSHDAFGYLARAYGLEQVGIQGVSPESEPSAADLAELIDLIKEKKVKAIFVEPQVSPKLAETVAKETGVKVLG 239
|
250 260 270
....*....|....*....|....*....|.
gi 24528028 260 ELYPEALTDSSGlAATYTAAFKHNVDTLAAG 290
Cdd:pfam01297 240 PLYTDSLGEPGG-GATYLDLMRHNLDTLAEA 269
|
|
| AztC |
NF040870 |
zinc ABC transporter substrate-binding protein AztC; |
26-291 |
5.31e-88 |
|
zinc ABC transporter substrate-binding protein AztC;
Pssm-ID: 468807 [Multi-domain] Cd Length: 277 Bit Score: 263.75 E-value: 5.31e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528028 26 VVASFSVLGDMVSQIGGPYVHVTDLVQPDGDPHEFEPSPKDSKTLAQADVVFVNGLGL-EGWLDRLMKASGYRGEVITAS 104
Cdd:NF040870 1 VVVTTNILGDLARNVVGDRAEVTTLMKPDADPHSFEPSAADAAALERADLVVVNGLGLeEGFLRHLIAASATGAPVVEVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528028 105 NGIDTLKMKEDGTTI-------TDPHAWNSMKNGIVYAHNIVNGLSKADPEHASDYRKQGDSYIQQLQQLDNYATQTFAA 177
Cdd:NF040870 81 DGVDPLPYPEGGHYHfeagagpPDPHFWTDPARARDAVDNIADAFCEADDGDCAAYRANAAAYRAELDELDAEMREAFAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528028 178 IPREKRKVLTSHDAFGYFAAAYGVRFLSPV--GYSTESEASSKNVAKLINQIKREHVKLYFIENQTDPRLVKQIANASGA 255
Cdd:NF040870 161 IPADRRTLVTNHHVFGYLAERYGFRVLGAVipSGSTLASPSAADLASLARAIREAGVPAIFAESSQPPRLAEVLASEAGL 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 24528028 256 QAGG-ELYPEALTDSSGLAATYTAAFKHNVDTLAAGM 291
Cdd:NF040870 241 DVGVvELYSESLSEPDGGAATYLDMMRANAEAIVDGL 277
|
|
| AdcA |
cd01017 |
Metal binding protein AdcA. These proteins have been shown to function in the ABC uptake of ... |
21-292 |
9.60e-67 |
|
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: 209.84 E-value: 9.60e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528028 21 AKELNVVASFSVLGDMVSQIGGPYVHVTDLVQPDGDPHEFEPSPKDSKTLAQADVVFVNGLGLEGWLDRLMKASGYRGE- 99
Cdd:cd01017 1 SGKLKVVTTFYPLYEFTKAIGGDKADVKLIIPAGTEPHDFEPSPKDIARIADADVFVYNGLGMETWAEKVLKSLQNKKLk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528028 100 VITASNGIDTLKMKEDGTTIT----------DPHAWNSMKNGIVYAHNIVNGLSKADPEHASDYRKQGDSYIQQLQQLDN 169
Cdd:cd01017 81 VVEASKGIKLLKAGGAEHDHDhshshhhgdyDPHVWLSPVLAIQQVENIKDALIKLDPDNKEYYEKNAAAYAKKLEALDQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528028 170 YATQTFAAIPRekRKVLTSHDAFGYFAAAYGVRFLSPVGYSTESEASSKNVAKLINQIKREHVKLYFIENQTDPRLVKQI 249
Cdd:cd01017 161 EYRAKLAKAKG--KTFVTQHAAFGYLARRYGLKQIAIVGVSPEVEPSPKQLAELVEFVKKSDVKYIFFEENASSKIAETL 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 24528028 250 ANASGAQAGGeLYP-EALTDSSGL-AATYTAAFKHNVDTLAAGMK 292
Cdd:cd01017 239 AKETGAKLLV-LNPlETLTKEEIDdGKDYFSLMKENLETLKRALK 282
|
|
| TroA |
cd01016 |
Metal binding protein TroA. These proteins have been shown to function as initial receptors in ... |
24-292 |
1.91e-62 |
|
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: 198.36 E-value: 1.91e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528028 24 LNVVASFSVLGDMVSQIGGPYVHVTDLVQPDGDPHEFEPSPKDSKTLAQADVVFVNGLGLEGWLDRLMKASGYRGEVITA 103
Cdd:cd01016 2 PNVVTTTGMIADAVENIGGDHVEVTGLMGPGVDPHLYKATAGDVEKLQNADVVFYNGLHLEGKMSDVLSKLGSSKSVIAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528028 104 SNGID-TLKMKEDGTTITDPHAWNSMKNGIVYAHNIVNGLSKADPEHASDYRKQGDSYIQQLQQLDNYATQTFAAIPREK 182
Cdd:cd01016 82 EDTLDrSQLILDEEEGTYDPHIWFDVKLWKYAVKAVAEVLSEKLPEHKDEFQANSEAYVEELDSLDAYAKKKIAEIPEQQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528028 183 RKVLTSHDAFGYFAAAYGVRFLSPVGYSTESEASSKNVAKLINQIKREHVKLYFIENQTDPRLVKQI---ANASG--AQA 257
Cdd:cd01016 162 RVLVTAHDAFGYFGRAYGFEVKGLQGISTDSEAGLRDINELVDLIVERKIKAIFVESSVNQKSIEALqdaVKARGhdVQI 241
|
250 260 270
....*....|....*....|....*....|....*
gi 24528028 258 GGELYPEALTDSSGLAATYTAAFKHNVDTLAAGMK 292
Cdd:cd01016 242 GGELYSDAMGEEGTSEGTYIGMFKHNVDTIVEALK 276
|
|
| ZnuA |
cd01019 |
Zinc binding protein ZnuA. These proteins have been shown to function as initial receptors in ... |
21-271 |
1.22e-44 |
|
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: 152.91 E-value: 1.22e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528028 21 AKELNVVASFSVLGDMVSQIGGPYVHVTDLVQPDGDPHEFEPSPKDSKTLAQADVVFVNGLGLEGWLDRLMKaSGYRGEV 100
Cdd:cd01019 1 AAEASVLTSIKPLGFIAAAIMGGVGEVEVLVPPGASPHDYELRPSDARKLQEADLVVWIGPDLEAFLDKVLQ-GRKKGKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528028 101 ITASNGIDtLKMKEDGTTI---------------------TDPHAWNSMKNGIVYAHNIVNGLSKADPEHASDYRKQGDS 159
Cdd:cd01019 80 LTLAKLID-LKTLEDGASHgdhehdhehahgehdgheeggLDPHLWLSPENAAEVAQAVAEKLSALDPDNAATYAANLEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528028 160 YIQQLQQLDNYATQTFAAIprEKRKVLTSHDAFGYFAAAYGvrfLSPVGYST---ESEASSKNVAKLINQIKREHVKLYF 236
Cdd:cd01019 159 FNARLAELDATIKERLAPV--KTKPFFVFHDAYGYFEKRYG---LTQAGVFTidpEIDPGAKRLAKIRKEIKEKGATCVF 233
|
250 260 270
....*....|....*....|....*....|....*
gi 24528028 237 IENQTDPRLVKQIANASGAQaGGELYPEALTDSSG 271
Cdd:cd01019 234 AEPQFHPKIAETLAEGTGAK-VGELDPLGGLIELG 267
|
|
| ZntC |
cd01018 |
Metal binding protein ZntC. These proteins are predicted to function as initial receptors in ... |
37-289 |
5.63e-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: 145.20 E-value: 5.63e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528028 37 VSQIGGPYVHVTDLVQPDGDPHEFEPSPKDSKTLAQADVVFVNGLGLE-GWLDRLMKASGyRGEVITASNGIDTLKM--- 112
Cdd:cd01018 16 VEKIAGDTVDVVVLVPPGSNPHTYEPKPQQMKKLSEADLYFRIGLGFEeVWLERFRSNNP-KMQVVNMSKGITLIPMadh 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528028 113 -------KEDG-TTITDPHAWNSMKNGIVYAHNIVNGLSKADPEHASDYRKQGDSYIQQLQQLDNYATQTFAAIPRekRK 184
Cdd:cd01018 95 hhhhhgeHEHHhHGNYDPHIWLSPANAKIMAENIYEALAELDPQNATYYQANLDALLAELDALDSEIRTILSKLKQ--RA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528028 185 VLTSHDAFGYFAAAYGvrfLSPVGYSTE-SEASSKNVAKLINQIKREHVKLYFIENQTDPRLVKQIAnasgAQAGGELYP 263
Cdd:cd01018 173 FMVYHPAWGYFARDYG---LTQIPIEEEgKEPSPADLKRLIDLAKEKGVRVVFVQPQFSTKSAEAIA----REIGAKVVT 245
|
250 260
....*....|....*....|....*.
gi 24528028 264 ealTDSsgLAATYTAAFKHNVDTLAA 289
Cdd:cd01018 246 ---IDP--LAADWEENLLKVADAFAH 266
|
|
| ZnuA |
COG4531 |
ABC-type Zn2+ transport system, periplasmic component/surface adhesin ZnuA [Inorganic ion ... |
21-278 |
4.19e-37 |
|
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: 133.42 E-value: 4.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528028 21 AKELNVVASFSVLGDMVSQI----GGPYVhvtdLVQPDGDPHEFEPSPKDSKTLAQADVVFVNGLGLEGWLDRLMKASGY 96
Cdd:COG4531 7 AAAPRVVTSIKPLHSLVAAVmdgvGEPEL----LLPPGASPHDYALRPSDARALQDADLVFWVGPDLEPFLEKPLETLAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528028 97 RGEVITASN--GIDTLKMKEDGT-------------------------TITDPHAWNSMKNGIVYAHNIVNGLSKADPEH 149
Cdd:COG4531 83 DAKVVELLElpGLTLLPFREGGDfehhdhhdehhhhhhhhddhhdhhhGGYDPHLWLSPENAKAWAAAIADALSELDPEN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528028 150 ASDYRKQGDSYIQQLQQLDNYATQTFAAIpREKRKVLTsHDAFGYFAAAYGvrfLSPVGYST---ESEASSKNVAKLINQ 226
Cdd:COG4531 163 AATYQANAAAFEARLDALDAEIAAQLAPV-KGKPFFVF-HDAYQYFEKRFG---LNALGAITlnpEIQPGAKRLAEIREK 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24528028 227 IKREHVKLYFIENQTDPRLVKQIANASGA------------QAGGELYPEALTDssgLAATYTA 278
Cdd:COG4531 238 LKELGAVCVFAEPQFNPALVETVAEGTGVrtgvldplgadlEPGPDLYFQLLRQ---LADSLAS 298
|
|
| TroA_b |
cd01020 |
Metal binding protein TroA_b. These proteins are predicted to function as initial receptors ... |
24-255 |
7.82e-34 |
|
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: 124.09 E-value: 7.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528028 24 LNVVASFSVLGDMVSQIGGPYVHVTDLV-QPDGDPHEFEPSPKDSKTLAQADVVFVNGLGLEGWLDRLMKASGYRgeVIT 102
Cdd:cd01020 3 INVVASTNFWGSVAEAVGGDHVEVTSIItNPDVDPHDFEPTPTDAAKVSTADIVVYNGGGYDPWMTKLLADTKDV--IVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528028 103 ASNgiDTLKMKEDGttiTDPHAWNSMKNGIVYAHNIVNGLSKADPEHASDYRKQGDSYIQQLQQLDNYATQTFAAIPreK 182
Cdd:cd01020 81 AAD--LDGHDDKEG---DNPHLWYDPETMSKVANALADALVKADPDNKKYYQANAKKFVASLKPLAAKIAELSAKYK--G 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24528028 183 RKVLTSHDAFGYFAAAYGVRFLSPVGYS----TESEASSKNVAKLINQIKREHVKLYFIENQTDPRLVKQIANASGA 255
Cdd:cd01020 154 APVAATEPVFDYLLDALGMKERTPKGYTatteSETEPSPADIAAFQNAIKNRQIDALIVNPQQASSATTNITGLAKR 230
|
|
| anch_rpt_subst |
TIGR03772 |
anchored repeat ABC transporter, substrate-binding protein; Members of this protein family are ... |
121-288 |
5.83e-28 |
|
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: 112.26 E-value: 5.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528028 121 DPHAWNSMKNGIVYAHNIVNGLSKADPEHASDYRKQGDSYIQQLQQLDNYATQTFAAIPREKRKVLTSHDAFGYFAAAYG 200
Cdd:TIGR03772 310 DPHLWHNVKNAIAYVEVIRDKLIEVDPRGAQAYRSNASAYIHRLERLDTYVRRTIATIPPSRRHLITTHDAYSYLGQAYG 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528028 201 VRFLSPVGYSTESEASSKNVAKLINQIKREHVKLYFIENQTDPR--LVKQIANASGAQAgGELYPEALTDSsglAATYTA 278
Cdd:TIGR03772 390 LNIAGFVTPNPAVEPSLADRRRLTRTIENLKVPAVFLEPNLAARstTLNEIADELGVRV-CAIYGDTFDDD---VTNYVD 465
|
170
....*....|
gi 24528028 279 AFKHNVDTLA 288
Cdd:TIGR03772 466 LMRFNADSLA 475
|
|
| TroA_c |
cd01145 |
Periplasmic binding protein TroA_c. These proteins are predicted to function as initial ... |
22-202 |
2.58e-19 |
|
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: 83.70 E-value: 2.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528028 22 KELNVVASFSVLGDMVSQIGGPYVHVTDLVQPDGDPHEFEPSPKDSKTLAQADVVFVNGLGLEGWLDRL-MKASGY---R 97
Cdd:cd01145 1 AALNVVVTFPDLKDLVREVAGDAVIVSALTPPGVDPHQYQLKPSDIAKMRKADLVVTSGHELEGFEPKLaELSSNSkvqP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528028 98 GEV--ITASNGIDTLKMKEDGTTIT-DPHAWNSMKNGIVYAHNIVNGLSKADPEHASDYRKQGDSYIQQLQQLDNYATQT 174
Cdd:cd01145 81 GIKilIEDSDTVGMVDRAMGDYHGKgNPHVWLDPNNAPALAKALADALIELDPSEQEEYKENLRVFLAKLNKLLREWERQ 160
|
170 180
....*....|....*....|....*...
gi 24528028 175 FAaiPREKRKVLTSHDAFGYFAAAYGVR 202
Cdd:cd01145 161 FE--GLKGIQVVAYHPSYQYLADWLGIE 186
|
|
| TroA-like |
cd00636 |
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ... |
24-188 |
2.14e-11 |
|
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: 60.65 E-value: 2.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528028 24 LNVVASFSVLGDMVSQIGGPYVHVTDLVQPDGD-------------PHEFEPSPKDSKTLaQADVVFVNGLGLEGWLDRL 90
Cdd:cd00636 1 KRVVALDPGATELLLALGGDDKPVGVADPSGYPpeakallekvpdvGHGYEPNLEKIAAL-KPDLIIANGSGLEAWLDKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528028 91 MKASGyrgevitasngidtlkmkedGTTITDPHAWNSMKNGIVYAHNIVNGLskadpehasDYRKQGDSYIQQLQQLDNY 170
Cdd:cd00636 80 SKIAI--------------------PVVVVDEASELSLENIKESIRLIGKAL---------GKEENAEELIAELDARLAE 130
|
170
....*....|....*...
gi 24528028 171 ATQTFAAIPREKRKVLTS 188
Cdd:cd00636 131 LRAKLAKIPKKKVSLVVG 148
|
|
| znuA |
PRK09545 |
zinc ABC transporter substrate-binding protein ZnuA; |
2-258 |
1.01e-07 |
|
zinc ABC transporter substrate-binding protein ZnuA;
Pssm-ID: 236558 [Multi-domain] Cd Length: 311 Bit Score: 52.32 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528028 2 KRSILVVALSSLLVSPLVIAKELNVVASFSVLGDMVSQIG-GpyVHVTDLVQPDG-DPHEFEPSPKDSKTLAQADVVFVN 79
Cdd:PRK09545 3 KKTLLFAALLAALLGGATQAANAAVVTSIKPLGFIASAIAdG--VTETEVLLPDGaSPHDYSLRPSDVKRLQSADLVVWV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528028 80 GLGLEGWLDRLMkASGYRGEVITASN--GIDTLKMKEDGTTITDP---------------------HAWNSMKNGIVYAH 136
Cdd:PRK09545 81 GPEMEAFLEKPV-SKLPENKQVTIAQlpDVKPLLMKGAHDDHHDDdhdhagheksdedhhhgeynmHIWLSPEIARATAV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528028 137 NIVNGLSKADPEH----ASDYRKqgdsYIQQLQQLDNYATQTFAaiPREKRKVLTSHDAFGYFAAAYGvrfLSPVGYST- 211
Cdd:PRK09545 160 AIHDKLVELMPQSkaklDANLKD----FEAQLAQTDKQIGNQLA--PVKGKGYFVFHDAYGYFEKHYG---LTPLGHFTv 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 24528028 212 --ESEASSKNVAKLINQIKREHVKLYFIENQTDPRLVKQIANASGAQAG 258
Cdd:PRK09545 231 npEIQPGAQRLHEIRTQLVEQKATCVFAEPQFRPAVIESVAKGTSVRMG 279
|
|
| |
