|
Name |
Accession |
Description |
Interval |
E-value |
| PsaA |
cd01137 |
Metal binding protein PsaA. These proteins have been shown to function as initial receptors ... |
8-292 |
8.30e-130 |
|
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: 370.07 E-value: 8.30e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992520 8 LALALGLASHGVMAKTLNVVSSFSVLGDMVQQIGGEHVHVDTLVGPDGDPHTFEPSPKDSALLNNADVVVVNGLGLEGWL 87
Cdd:cd01137 2 AACASLGSSPATAASKLKVVATFSILADIARNIAGDRVNVTSIVPPGADPHEYEPTPSDIKKLSKADLILYNGLNLEPWL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992520 88 DRLIKASGFKGELVVASRGVKTHTLEE-DGATVTDPHAWNSAANGALYAQNILNGLVKADPEDKLALEASGKRYISQLNE 166
Cdd:cd01137 82 ERLVKNAGKDVPVVAVSEGIDPIPLEEgHYKGKPDPHAWMSPKNAIIYVKNIAKALSEADPANAETYQKNAAAYKAKLKA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992520 167 IDRWAKSQFTAIPQAKRKVLTSHDAFGYFGRAYGVTFLAPQGLSSESEASAAQVAALIRQIKADEVHTWFMENQLDPRLV 246
Cdd:cd01137 162 LDEWAKAKFATIPAEKRKLVTSEGAFSYFAKAYGLKEAYLWPINTEEEGTPKQVATLIEQVKKEKVPAVFVESTVNDRLM 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 503992520 247 KQIASATGAQPGGELYPEALSQPGGVADSYVKMLRHNVELIAASMK 292
Cdd:cd01137 242 KQVAKETGAKIGGQLYTDSLSEKGGPADTYLDMMEHNLDTIVEGLG 287
|
|
| ZnuA |
COG0803 |
ABC-type Zn uptake system ZnuABC, Zn-binding component ZnuA [Inorganic ion transport and ... |
1-283 |
4.18e-107 |
|
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: 312.56 E-value: 4.18e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992520 1 MKRTGIWLALALGLA------SHGVMAKTLNVVSSFSVLGDMVQQIGGEHVHVDTLVGPDGDPHTFEPSPKDSALLNNAD 74
Cdd:COG0803 1 MKRLLLALLLLAALLlagcsaAASSAAGKLKVVATFSPLADLAKQIGGDKVEVTSLVPPGADPHDYEPTPSDIAKLAKAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992520 75 VVVVNGLGLEGWLDRLIKASGFKG-ELVVASRGVKTHTLEE-DGATVTDPHAWNSAANGALYAQNILNGLVKADPEDKLA 152
Cdd:COG0803 81 LVVYNGLGLEGWLDKLLEAAGNPGvPVVDASEGIDLLELEEgHDHGEPDPHVWLDPKNAKKVAENIADALAELDPANAAY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992520 153 LEASGKRYISQLNEIDRWAKSQFTAIPQakRKVLTSHDAFGYFGRAYGVTFLAPQGLSSESEASAAQVAALIRQIKADEV 232
Cdd:COG0803 161 YEANAAAYLAELDALDAEIKAKLAAIPG--RKLVTSHDAFGYLARAYGLEVVAIQGISPGSEPSPADLAELIDLIKEEGV 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 503992520 233 HTWFMENQLDPRLVKQIASATGAQPggeLYPEALSQPGGVADSYVKMLRHN 283
Cdd:COG0803 239 KAIFVESQVSPKLAETLAEETGVKV---LYLDSLGGPGGPGDTYLDMMRHN 286
|
|
| ZnuA |
pfam01297 |
Zinc-uptake complex component A periplasmic; ZnuA includes periplasmic solute binding proteins ... |
26-289 |
3.16e-105 |
|
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: 307.17 E-value: 3.16e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992520 26 VVSSFSVLGDMVQQIGGEHVHVDTLVGPDGDPHTFEPSPKDSALLNNADVVVVNGLGLEGWLDRLIKASGfKGELVVASR 105
Cdd:pfam01297 1 VVATTYPLADLAKQIGGDRVEVTSLVPPGADPHDYEPTPSDIAALSDADLVVYNGLGLEPWLDKLLEALP-NKKVVDASE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992520 106 GVKTHTLEEDGATV------TDPHAWNSAANGALYAQNILNGLVKADPEDKLALEASGKRYISQLNEIDRWAKSQFTAIP 179
Cdd:pfam01297 80 GVELLDEEGEEEDHdghdhgYDPHVWLDPKNAKKMAENIADALSELDPANAATYEANAAAYLAELDALDAEIKEQLASIP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992520 180 QAKRKVLTSHDAFGYFGRAYGVTFLAPQGLSSESEASAAQVAALIRQIKADEVHTWFMENQLDPRLVKQIASATGAQPGG 259
Cdd:pfam01297 160 EKTRKLVTSHDAFGYLARAYGLEQVGIQGVSPESEPSAADLAELIDLIKEKKVKAIFVEPQVSPKLAETVAKETGVKVLG 239
|
250 260 270
....*....|....*....|....*....|
gi 503992520 260 ELYPEALSQPGGVADsYVKMLRHNVELIAA 289
Cdd:pfam01297 240 PLYTDSLGEPGGGAT-YLDLMRHNLDTLAE 268
|
|
| AztC |
NF040870 |
zinc ABC transporter substrate-binding protein AztC; |
26-289 |
1.33e-91 |
|
zinc ABC transporter substrate-binding protein AztC;
Pssm-ID: 468807 [Multi-domain] Cd Length: 277 Bit Score: 272.99 E-value: 1.33e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992520 26 VVSSFSVLGDMVQQIGGEHVHVDTLVGPDGDPHTFEPSPKDSALLNNADVVVVNGLGL-EGWLDRLIKASGFKGELVVAS 104
Cdd:NF040870 1 VVVTTNILGDLARNVVGDRAEVTTLMKPDADPHSFEPSAADAAALERADLVVVNGLGLeEGFLRHLIAASATGAPVVEVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992520 105 RGVKT-------HTLEEDGATVTDPHAWNSAANGALYAQNILNGLVKADPEDKLALEASGKRYISQLNEIDRWAKSQFTA 177
Cdd:NF040870 81 DGVDPlpypeggHYHFEAGAGPPDPHFWTDPARARDAVDNIADAFCEADDGDCAAYRANAAAYRAELDELDAEMREAFAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992520 178 IPQAKRKVLTSHDAFGYFGRAYGVTFLA---PQGlSSESEASAAQVAALIRQIKADEVHTWFMENQLDPRLVKQIASATG 254
Cdd:NF040870 161 IPADRRTLVTNHHVFGYLAERYGFRVLGaviPSG-STLASPSAADLASLARAIREAGVPAIFAESSQPPRLAEVLASEAG 239
|
250 260 270
....*....|....*....|....*....|....*.
gi 503992520 255 AQPGG-ELYPEALSQPGGVADSYVKMLRHNVELIAA 289
Cdd:NF040870 240 LDVGVvELYSESLSEPDGGAATYLDMMRANAEAIVD 275
|
|
| anch_rpt_subst |
TIGR03772 |
anchored repeat ABC transporter, substrate-binding protein; Members of this protein family are ... |
121-288 |
7.03e-23 |
|
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: 97.63 E-value: 7.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992520 121 DPHAWNSAANGALYAQNILNGLVKADPEDKLALEASGKRYISQLNEIDRWAKSQFTAIPQAKRKVLTSHDAFGYFGRAYG 200
Cdd:TIGR03772 310 DPHLWHNVKNAIAYVEVIRDKLIEVDPRGAQAYRSNASAYIHRLERLDTYVRRTIATIPPSRRHLITTHDAYSYLGQAYG 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992520 201 VT---FLAPqglSSESEASAAQVAALIRQIKADEVHTWFMENQLDPR--LVKQIASATGAQPgGELYPEALSQPggvADS 275
Cdd:TIGR03772 390 LNiagFVTP---NPAVEPSLADRRRLTRTIENLKVPAVFLEPNLAARstTLNEIADELGVRV-CAIYGDTFDDD---VTN 462
|
170
....*....|...
gi 503992520 276 YVKMLRHNVELIA 288
Cdd:TIGR03772 463 YVDLMRFNADSLA 475
|
|
| znuA |
PRK09545 |
zinc ABC transporter substrate-binding protein ZnuA; |
2-280 |
1.05e-12 |
|
zinc ABC transporter substrate-binding protein ZnuA;
Pssm-ID: 236558 [Multi-domain] Cd Length: 311 Bit Score: 66.95 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992520 2 KRTGIWLALALGLASHGVMAKTLNVVSSFSVLGDMVQQIGGEHVHVDTLVgPDG-DPHTFEPSPKDSALLNNADVVVVNG 80
Cdd:PRK09545 3 KKTLLFAALLAALLGGATQAANAAVVTSIKPLGFIASAIADGVTETEVLL-PDGaSPHDYSLRPSDVKRLQSADLVVWVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992520 81 LGLEGWLDRLIKASGFKGELVVAS-RGVKT----------HTLEEDGATVTDP-----------HAWNSAANGALYAQNI 138
Cdd:PRK09545 82 PEMEAFLEKPVSKLPENKQVTIAQlPDVKPllmkgahddhHDDDHDHAGHEKSdedhhhgeynmHIWLSPEIARATAVAI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992520 139 LNGLVKADPEDKLALEASGKRYISQLNEIDRWAKSQFTaiPQAKRKVLTSHDAFGYFGRAYGVTFLAPQGLSSESeASAA 218
Cdd:PRK09545 162 HDKLVELMPQSKAKLDANLKDFEAQLAQTDKQIGNQLA--PVKGKGYFVFHDAYGYFEKHYGLTPLGHFTVNPEI-QPGA 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503992520 219 QVAALIR-QIKADEVHTWFMENQLDPRLVKQIASATGA------------QPGGELYPEALSQpggVADSYVKML 280
Cdd:PRK09545 239 QRLHEIRtQLVEQKATCVFAEPQFRPAVIESVAKGTSVrmgtldplgtniKLGKDSYSEFLSQ---LANQYASCL 310
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PsaA |
cd01137 |
Metal binding protein PsaA. These proteins have been shown to function as initial receptors ... |
8-292 |
8.30e-130 |
|
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: 370.07 E-value: 8.30e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992520 8 LALALGLASHGVMAKTLNVVSSFSVLGDMVQQIGGEHVHVDTLVGPDGDPHTFEPSPKDSALLNNADVVVVNGLGLEGWL 87
Cdd:cd01137 2 AACASLGSSPATAASKLKVVATFSILADIARNIAGDRVNVTSIVPPGADPHEYEPTPSDIKKLSKADLILYNGLNLEPWL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992520 88 DRLIKASGFKGELVVASRGVKTHTLEE-DGATVTDPHAWNSAANGALYAQNILNGLVKADPEDKLALEASGKRYISQLNE 166
Cdd:cd01137 82 ERLVKNAGKDVPVVAVSEGIDPIPLEEgHYKGKPDPHAWMSPKNAIIYVKNIAKALSEADPANAETYQKNAAAYKAKLKA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992520 167 IDRWAKSQFTAIPQAKRKVLTSHDAFGYFGRAYGVTFLAPQGLSSESEASAAQVAALIRQIKADEVHTWFMENQLDPRLV 246
Cdd:cd01137 162 LDEWAKAKFATIPAEKRKLVTSEGAFSYFAKAYGLKEAYLWPINTEEEGTPKQVATLIEQVKKEKVPAVFVESTVNDRLM 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 503992520 247 KQIASATGAQPGGELYPEALSQPGGVADSYVKMLRHNVELIAASMK 292
Cdd:cd01137 242 KQVAKETGAKIGGQLYTDSLSEKGGPADTYLDMMEHNLDTIVEGLG 287
|
|
| ZnuA |
COG0803 |
ABC-type Zn uptake system ZnuABC, Zn-binding component ZnuA [Inorganic ion transport and ... |
1-283 |
4.18e-107 |
|
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: 312.56 E-value: 4.18e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992520 1 MKRTGIWLALALGLA------SHGVMAKTLNVVSSFSVLGDMVQQIGGEHVHVDTLVGPDGDPHTFEPSPKDSALLNNAD 74
Cdd:COG0803 1 MKRLLLALLLLAALLlagcsaAASSAAGKLKVVATFSPLADLAKQIGGDKVEVTSLVPPGADPHDYEPTPSDIAKLAKAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992520 75 VVVVNGLGLEGWLDRLIKASGFKG-ELVVASRGVKTHTLEE-DGATVTDPHAWNSAANGALYAQNILNGLVKADPEDKLA 152
Cdd:COG0803 81 LVVYNGLGLEGWLDKLLEAAGNPGvPVVDASEGIDLLELEEgHDHGEPDPHVWLDPKNAKKVAENIADALAELDPANAAY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992520 153 LEASGKRYISQLNEIDRWAKSQFTAIPQakRKVLTSHDAFGYFGRAYGVTFLAPQGLSSESEASAAQVAALIRQIKADEV 232
Cdd:COG0803 161 YEANAAAYLAELDALDAEIKAKLAAIPG--RKLVTSHDAFGYLARAYGLEVVAIQGISPGSEPSPADLAELIDLIKEEGV 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 503992520 233 HTWFMENQLDPRLVKQIASATGAQPggeLYPEALSQPGGVADSYVKMLRHN 283
Cdd:COG0803 239 KAIFVESQVSPKLAETLAEETGVKV---LYLDSLGGPGGPGDTYLDMMRHN 286
|
|
| ZnuA |
pfam01297 |
Zinc-uptake complex component A periplasmic; ZnuA includes periplasmic solute binding proteins ... |
26-289 |
3.16e-105 |
|
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: 307.17 E-value: 3.16e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992520 26 VVSSFSVLGDMVQQIGGEHVHVDTLVGPDGDPHTFEPSPKDSALLNNADVVVVNGLGLEGWLDRLIKASGfKGELVVASR 105
Cdd:pfam01297 1 VVATTYPLADLAKQIGGDRVEVTSLVPPGADPHDYEPTPSDIAALSDADLVVYNGLGLEPWLDKLLEALP-NKKVVDASE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992520 106 GVKTHTLEEDGATV------TDPHAWNSAANGALYAQNILNGLVKADPEDKLALEASGKRYISQLNEIDRWAKSQFTAIP 179
Cdd:pfam01297 80 GVELLDEEGEEEDHdghdhgYDPHVWLDPKNAKKMAENIADALSELDPANAATYEANAAAYLAELDALDAEIKEQLASIP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992520 180 QAKRKVLTSHDAFGYFGRAYGVTFLAPQGLSSESEASAAQVAALIRQIKADEVHTWFMENQLDPRLVKQIASATGAQPGG 259
Cdd:pfam01297 160 EKTRKLVTSHDAFGYLARAYGLEQVGIQGVSPESEPSAADLAELIDLIKEKKVKAIFVEPQVSPKLAETVAKETGVKVLG 239
|
250 260 270
....*....|....*....|....*....|
gi 503992520 260 ELYPEALSQPGGVADsYVKMLRHNVELIAA 289
Cdd:pfam01297 240 PLYTDSLGEPGGGAT-YLDLMRHNLDTLAE 268
|
|
| AztC |
NF040870 |
zinc ABC transporter substrate-binding protein AztC; |
26-289 |
1.33e-91 |
|
zinc ABC transporter substrate-binding protein AztC;
Pssm-ID: 468807 [Multi-domain] Cd Length: 277 Bit Score: 272.99 E-value: 1.33e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992520 26 VVSSFSVLGDMVQQIGGEHVHVDTLVGPDGDPHTFEPSPKDSALLNNADVVVVNGLGL-EGWLDRLIKASGFKGELVVAS 104
Cdd:NF040870 1 VVVTTNILGDLARNVVGDRAEVTTLMKPDADPHSFEPSAADAAALERADLVVVNGLGLeEGFLRHLIAASATGAPVVEVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992520 105 RGVKT-------HTLEEDGATVTDPHAWNSAANGALYAQNILNGLVKADPEDKLALEASGKRYISQLNEIDRWAKSQFTA 177
Cdd:NF040870 81 DGVDPlpypeggHYHFEAGAGPPDPHFWTDPARARDAVDNIADAFCEADDGDCAAYRANAAAYRAELDELDAEMREAFAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992520 178 IPQAKRKVLTSHDAFGYFGRAYGVTFLA---PQGlSSESEASAAQVAALIRQIKADEVHTWFMENQLDPRLVKQIASATG 254
Cdd:NF040870 161 IPADRRTLVTNHHVFGYLAERYGFRVLGaviPSG-STLASPSAADLASLARAIREAGVPAIFAESSQPPRLAEVLASEAG 239
|
250 260 270
....*....|....*....|....*....|....*.
gi 503992520 255 AQPGG-ELYPEALSQPGGVADSYVKMLRHNVELIAA 289
Cdd:NF040870 240 LDVGVvELYSESLSEPDGGAATYLDMMRANAEAIVD 275
|
|
| AdcA |
cd01017 |
Metal binding protein AdcA. These proteins have been shown to function in the ABC uptake of ... |
24-292 |
1.28e-63 |
|
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: 201.75 E-value: 1.28e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992520 24 LNVVSSFSVLGDMVQQIGGEHVHVDTLVGPDGDPHTFEPSPKDSALLNNADVVVVNGLGLEGWLDRLIKASGFKGELVV- 102
Cdd:cd01017 4 LKVVTTFYPLYEFTKAIGGDKADVKLIIPAGTEPHDFEPSPKDIARIADADVFVYNGLGMETWAEKVLKSLQNKKLKVVe 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992520 103 ASRGVK----------THTLEEDGATVTDPHAWNSAANGALYAQNILNGLVKADPEDKLALEASGKRYISQLNEIDRWAK 172
Cdd:cd01017 84 ASKGIKllkaggaehdHDHSHSHHHGDYDPHVWLSPVLAIQQVENIKDALIKLDPDNKEYYEKNAAAYAKKLEALDQEYR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992520 173 SQFTAIPQakRKVLTSHDAFGYFGRAYGVTFLAPQGLSSESEASAAQVAALIRQIKADEVHTWFMENQLDPRLVKQIASA 252
Cdd:cd01017 164 AKLAKAKG--KTFVTQHAAFGYLARRYGLKQIAIVGVSPEVEPSPKQLAELVEFVKKSDVKYIFFEENASSKIAETLAKE 241
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 503992520 253 TGAQPGGeLYP-EALSQPGGV-ADSYVKMLRHNVELIAASMK 292
Cdd:cd01017 242 TGAKLLV-LNPlETLTKEEIDdGKDYFSLMKENLETLKRALK 282
|
|
| TroA |
cd01016 |
Metal binding protein TroA. These proteins have been shown to function as initial receptors in ... |
24-292 |
4.20e-63 |
|
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: 200.28 E-value: 4.20e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992520 24 LNVVSSFSVLGDMVQQIGGEHVHVDTLVGPDGDPHTFEPSPKDSALLNNADVVVVNGLGLEGWL-DRLIKASGFKGELVV 102
Cdd:cd01016 2 PNVVTTTGMIADAVENIGGDHVEVTGLMGPGVDPHLYKATAGDVEKLQNADVVFYNGLHLEGKMsDVLSKLGSSKSVIAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992520 103 ASRGVKTHTLEEDGATVTDPHAWNSAANGALYAQNILNGLVKADPEDKLALEASGKRYISQLNEIDRWAKSQFTAIPQAK 182
Cdd:cd01016 82 EDTLDRSQLILDEEEGTYDPHIWFDVKLWKYAVKAVAEVLSEKLPEHKDEFQANSEAYVEELDSLDAYAKKKIAEIPEQQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992520 183 RKVLTSHDAFGYFGRAYGVTFLAPQGLSSESEASAAQVAALIRQIKADEVHTWFMENQLDPRLVKQIASATGA-----QP 257
Cdd:cd01016 162 RVLVTAHDAFGYFGRAYGFEVKGLQGISTDSEAGLRDINELVDLIVERKIKAIFVESSVNQKSIEALQDAVKArghdvQI 241
|
250 260 270
....*....|....*....|....*....|....*
gi 503992520 258 GGELYPEALSQPGGVADSYVKMLRHNVELIAASMK 292
Cdd:cd01016 242 GGELYSDAMGEEGTSEGTYIGMFKHNVDTIVEALK 276
|
|
| ZnuA |
cd01019 |
Zinc binding protein ZnuA. These proteins have been shown to function as initial receptors in ... |
25-283 |
4.80e-46 |
|
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: 156.38 E-value: 4.80e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992520 25 NVVSSFSVLGDMVQQIGGEHVHVDTLVGPDGDPHTFEPSPKDSALLNNADVVVVNGLGLEGWLDRLIKaSGFKGELVVAS 104
Cdd:cd01019 5 SVLTSIKPLGFIAAAIMGGVGEVEVLVPPGASPHDYELRPSDARKLQEADLVVWIGPDLEAFLDKVLQ-GRKKGKVLTLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992520 105 RGVKTHTLEEDGA--------------------TVTDPHAWNSAANGALYAQNILNGLVKADPEDKLALEASGKRYISQL 164
Cdd:cd01019 84 KLIDLKTLEDGAShgdhehdhehahgehdgheeGGLDPHLWLSPENAAEVAQAVAEKLSALDPDNAATYAANLEAFNARL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992520 165 NEIDRWAKSQFTAIpqAKRKVLTSHDAFGYFGRAYGVTFLAPQGLSSESEASAAQVAALIRQIKADEVHTWFMENQLDPR 244
Cdd:cd01019 164 AELDATIKERLAPV--KTKPFFVFHDAYGYFEKRYGLTQAGVFTIDPEIDPGAKRLAKIRKEIKEKGATCVFAEPQFHPK 241
|
250 260 270
....*....|....*....|....*....|....*....
gi 503992520 245 LVKQIASATGAQpGGELYPEALSQPGGvADSYVKMLRHN 283
Cdd:cd01019 242 IAETLAEGTGAK-VGELDPLGGLIELG-KNSYVNFLRNL 278
|
|
| ZntC |
cd01018 |
Metal binding protein ZntC. These proteins are predicted to function as initial receptors in ... |
37-257 |
8.05e-35 |
|
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: 126.71 E-value: 8.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992520 37 VQQIGGEHVHVDTLVGPDGDPHTFEPSPKDSALLNNADVVVVNGLGLE-GWLDRlIKASGFKGELVVASRGVK------- 108
Cdd:cd01018 16 VEKIAGDTVDVVVLVPPGSNPHTYEPKPQQMKKLSEADLYFRIGLGFEeVWLER-FRSNNPKMQVVNMSKGITlipmadh 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992520 109 ---THTLEEDGA-TVTDPHAWNSAANGALYAQNILNGLVKADPEDKLALEASGKRYISQLNEIDRWAKSQFTAIPQakRK 184
Cdd:cd01018 95 hhhHHGEHEHHHhGNYDPHIWLSPANAKIMAENIYEALAELDPQNATYYQANLDALLAELDALDSEIRTILSKLKQ--RA 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503992520 185 VLTSHDAFGYFGRAYGVTFLAPQglSSESEASAAQVAALIRQIKADEVHTWFMENQLDPRLVKQIASATGAQP 257
Cdd:cd01018 173 FMVYHPAWGYFARDYGLTQIPIE--EEGKEPSPADLKRLIDLAKEKGVRVVFVQPQFSTKSAEAIAREIGAKV 243
|
|
| TroA_b |
cd01020 |
Metal binding protein TroA_b. These proteins are predicted to function as initial receptors ... |
24-252 |
7.03e-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: 7.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992520 24 LNVVSSFSVLGDMVQQIGGEHVHVDTLVG-PDGDPHTFEPSPKDSALLNNADVVVVNGLGLEGWLDRLIKasgfkgelvv 102
Cdd:cd01020 3 INVVASTNFWGSVAEAVGGDHVEVTSIITnPDVDPHDFEPTPTDAAKVSTADIVVYNGGGYDPWMTKLLA---------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992520 103 ASRGVKTHTLEEDGA---TVTDPHAWNSAANGALYAQNILNGLVKADPEDKLALEASGKRYISQLNEIDRWAKsQFTAIP 179
Cdd:cd01020 73 DTKDVIVIAADLDGHddkEGDNPHLWYDPETMSKVANALADALVKADPDNKKYYQANAKKFVASLKPLAAKIA-ELSAKY 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503992520 180 QAKRkVLTSHDAFGYFGRAYGVTFLAPQGLS----SESEASAAQVAALIRQIKADEVHTWFMENQLDPRLVKQIASA 252
Cdd:cd01020 152 KGAP-VAATEPVFDYLLDALGMKERTPKGYTatteSETEPSPADIAAFQNAIKNRQIDALIVNPQQASSATTNITGL 227
|
|
| ZnuA |
COG4531 |
ABC-type Zn2+ transport system, periplasmic component/surface adhesin ZnuA [Inorganic ion ... |
20-277 |
7.75e-30 |
|
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: 114.16 E-value: 7.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992520 20 MAKTLNVVSSFSVLGDMVQQIGGEHVHVDTLVGPDGDPHTFEPSPKDSALLNNADVVVVNGLGLEGWLDRLIKASGFKGE 99
Cdd:COG4531 6 AAAAPRVVTSIKPLHSLVAAVMDGVGEPELLLPPGASPHDYALRPSDARALQDADLVFWVGPDLEPFLEKPLETLAPDAK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992520 100 LV-------VASRGVKTHTLEEDGATV--------------------TDPHAWNSAANGALYAQNILNGLVKADPEDKLA 152
Cdd:COG4531 86 VVellelpgLTLLPFREGGDFEHHDHHdehhhhhhhhddhhdhhhggYDPHLWLSPENAKAWAAAIADALSELDPENAAT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992520 153 LEASGKRYISQLNEIDRWAKSQFTaiPQAKRKVLTSHDAFGYFGRAYGvtfLAPQG---LSSESEASAAQVAALIRQIKA 229
Cdd:COG4531 166 YQANAAAFEARLDALDAEIAAQLA--PVKGKPFFVFHDAYQYFEKRFG---LNALGaitLNPEIQPGAKRLAEIREKLKE 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992520 230 DEVHTWFMENQLDPRLVKQIASATGA------------QPGGELYPEALSQpggVADSYV 277
Cdd:COG4531 241 LGAVCVFAEPQFNPALVETVAEGTGVrtgvldplgadlEPGPDLYFQLLRQ---LADSLA 297
|
|
| TroA_c |
cd01145 |
Periplasmic binding protein TroA_c. These proteins are predicted to function as initial ... |
24-205 |
9.98e-26 |
|
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: 101.04 E-value: 9.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992520 24 LNVVSSFSVLGDMVQQIGGEHVHVDTLVGPDGDPHTFEPSPKDSALLNNADVVVVNGLGLEGWLDRLIKAS-------GF 96
Cdd:cd01145 3 LNVVVTFPDLKDLVREVAGDAVIVSALTPPGVDPHQYQLKPSDIAKMRKADLVVTSGHELEGFEPKLAELSsnskvqpGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992520 97 KGELVVASRGVKTHTLEEDGATVTDPHAWNSAANGALYAQNILNGLVKADPEDKLALEASGKRYISQLNEIDRWAKSQFT 176
Cdd:cd01145 83 KILIEDSDTVGMVDRAMGDYHGKGNPHVWLDPNNAPALAKALADALIELDPSEQEEYKENLRVFLAKLNKLLREWERQFE 162
|
170 180
....*....|....*....|....*....
gi 503992520 177 aiPQAKRKVLTSHDAFGYFGRAYGVTFLA 205
Cdd:cd01145 163 --GLKGIQVVAYHPSYQYLADWLGIEVVA 189
|
|
| anch_rpt_subst |
TIGR03772 |
anchored repeat ABC transporter, substrate-binding protein; Members of this protein family are ... |
121-288 |
7.03e-23 |
|
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: 97.63 E-value: 7.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992520 121 DPHAWNSAANGALYAQNILNGLVKADPEDKLALEASGKRYISQLNEIDRWAKSQFTAIPQAKRKVLTSHDAFGYFGRAYG 200
Cdd:TIGR03772 310 DPHLWHNVKNAIAYVEVIRDKLIEVDPRGAQAYRSNASAYIHRLERLDTYVRRTIATIPPSRRHLITTHDAYSYLGQAYG 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992520 201 VT---FLAPqglSSESEASAAQVAALIRQIKADEVHTWFMENQLDPR--LVKQIASATGAQPgGELYPEALSQPggvADS 275
Cdd:TIGR03772 390 LNiagFVTP---NPAVEPSLADRRRLTRTIENLKVPAVFLEPNLAARstTLNEIADELGVRV-CAIYGDTFDDD---VTN 462
|
170
....*....|...
gi 503992520 276 YVKMLRHNVELIA 288
Cdd:TIGR03772 463 YVDLMRFNADSLA 475
|
|
| znuA |
PRK09545 |
zinc ABC transporter substrate-binding protein ZnuA; |
2-280 |
1.05e-12 |
|
zinc ABC transporter substrate-binding protein ZnuA;
Pssm-ID: 236558 [Multi-domain] Cd Length: 311 Bit Score: 66.95 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992520 2 KRTGIWLALALGLASHGVMAKTLNVVSSFSVLGDMVQQIGGEHVHVDTLVgPDG-DPHTFEPSPKDSALLNNADVVVVNG 80
Cdd:PRK09545 3 KKTLLFAALLAALLGGATQAANAAVVTSIKPLGFIASAIADGVTETEVLL-PDGaSPHDYSLRPSDVKRLQSADLVVWVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992520 81 LGLEGWLDRLIKASGFKGELVVAS-RGVKT----------HTLEEDGATVTDP-----------HAWNSAANGALYAQNI 138
Cdd:PRK09545 82 PEMEAFLEKPVSKLPENKQVTIAQlPDVKPllmkgahddhHDDDHDHAGHEKSdedhhhgeynmHIWLSPEIARATAVAI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992520 139 LNGLVKADPEDKLALEASGKRYISQLNEIDRWAKSQFTaiPQAKRKVLTSHDAFGYFGRAYGVTFLAPQGLSSESeASAA 218
Cdd:PRK09545 162 HDKLVELMPQSKAKLDANLKDFEAQLAQTDKQIGNQLA--PVKGKGYFVFHDAYGYFEKHYGLTPLGHFTVNPEI-QPGA 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503992520 219 QVAALIR-QIKADEVHTWFMENQLDPRLVKQIASATGA------------QPGGELYPEALSQpggVADSYVKML 280
Cdd:PRK09545 239 QRLHEIRtQLVEQKATCVFAEPQFRPAVIESVAKGTSVrmgtldplgtniKLGKDSYSEFLSQ---LANQYASCL 310
|
|
| TroA-like |
cd00636 |
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ... |
24-188 |
5.15e-10 |
|
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: 56.80 E-value: 5.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992520 24 LNVVSSFSVLGDMVQQIGGEHVHVDTLVGPDGD-------------PHTFEPSPKDSALLNnADVVVVNGLGLEGWLDRL 90
Cdd:cd00636 1 KRVVALDPGATELLLALGGDDKPVGVADPSGYPpeakallekvpdvGHGYEPNLEKIAALK-PDLIIANGSGLEAWLDKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503992520 91 IKAsgfkgelvvasrGVKTHTLEEDGAtvtdphawNSAANGALYAQNILNGLVKadpedklalEASGKRYISQLNEIDRW 170
Cdd:cd00636 80 SKI------------AIPVVVVDEASE--------LSLENIKESIRLIGKALGK---------EENAEELIAELDARLAE 130
|
170
....*....|....*...
gi 503992520 171 AKSQFTAIPQAKRKVLTS 188
Cdd:cd00636 131 LRAKLAKIPKKKVSLVVG 148
|
|
| |
