|
Name |
Accession |
Description |
Interval |
E-value |
| PsaA |
cd01137 |
Metal binding protein PsaA. These proteins have been shown to function as initial receptors ... |
23-292 |
6.98e-155 |
|
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: 433.63 E-value: 6.98e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080584186 23 KFKVVTTFTVIQDIAQNVAGDAAVVESITKPGAEIHDYQPTPQDIAKAQSADLVLWNGLNLERWFERFFQNVRNK-PAVV 101
Cdd:cd01137 17 KLKVVATFSILADIARNIAGDRVNVTSIVPPGADPHEYEPTPSDIKKLSKADLILYNGLNLEPWLERLVKNAGKDvPVVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080584186 102 VTQGITPMSIHEGPYRGQPNPHAWMSTRNALIYVENIKNALIKYDPQNAATYTRNAAAYAQRIRNLDRPLREKLARVPQN 181
Cdd:cd01137 97 VSEGIDPIPLEEGHYKGKPDPHAWMSPKNAIIYVKNIAKALSEADPANAETYQKNAAAYKAKLKALDEWAKAKFATIPAE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080584186 182 QRFLVTSEGAFSYLARDYGFKEVYLWPINAEQQGTPQQVRRVINTVRQNHIPVVFSESTVSPRPMRQVSRETGAKYGGVL 261
Cdd:cd01137 177 KRKLVTSEGAFSYFAKAYGLKEAYLWPINTEEEGTPKQVATLIEQVKKEKVPAVFVESTVNDRLMKQVAKETGAKIGGQL 256
|
250 260 270
....*....|....*....|....*....|.
gi 1080584186 262 YVDSLSAKNGPVPTYLDLLNTTVSTIVRGFG 292
Cdd:cd01137 257 YTDSLSEKGGPADTYLDMMEHNLDTIVEGLG 287
|
|
| ZnuA |
pfam01297 |
Zinc-uptake complex component A periplasmic; ZnuA includes periplasmic solute binding proteins ... |
26-290 |
1.29e-122 |
|
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: 351.47 E-value: 1.29e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080584186 26 VVTTFTVIQDIAQNVAGDAAVVESITKPGAEIHDYQPTPQDIAKAQSADLVLWNGLNLERWFERFFQNVRNKPAVVVTQG 105
Cdd:pfam01297 1 VVATTYPLADLAKQIGGDRVEVTSLVPPGADPHDYEPTPSDIAALSDADLVVYNGLGLEPWLDKLLEALPNKKVVDASEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080584186 106 ITPMsIHEGPYRGQP------NPHAWMSTRNALIYVENIKNALIKYDPQNAATYTRNAAAYAQRIRNLDRPLREKLARVP 179
Cdd:pfam01297 81 VELL-DEEGEEEDHDghdhgyDPHVWLDPKNAKKMAENIADALSELDPANAATYEANAAAYLAELDALDAEIKEQLASIP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080584186 180 QNQRFLVTSEGAFSYLARDYGFKEVYLWPINAEQQGTPQQVRRVINTVRQNHIPVVFSESTVSPRPMRQVSRETGAKYGG 259
Cdd:pfam01297 160 EKTRKLVTSHDAFGYLARAYGLEQVGIQGVSPESEPSAADLAELIDLIKEKKVKAIFVEPQVSPKLAETVAKETGVKVLG 239
|
250 260 270
....*....|....*....|....*....|.
gi 1080584186 260 VLYVDSLSAKNGPVpTYLDLLNTTVSTIVRG 290
Cdd:pfam01297 240 PLYTDSLGEPGGGA-TYLDLMRHNLDTLAEA 269
|
|
| ZnuA |
COG0803 |
ABC-type Zn uptake system ZnuABC, Zn-binding component ZnuA [Inorganic ion transport and ... |
23-281 |
2.21e-122 |
|
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: 351.47 E-value: 2.21e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080584186 23 KFKVVTTFTVIQDIAQNVAGDAAVVESITKPGAEIHDYQPTPQDIAKAQSADLVLWNGLNLERWFERFFQNVRNK--PAV 100
Cdd:COG0803 29 KLKVVATFSPLADLAKQIGGDKVEVTSLVPPGADPHDYEPTPSDIAKLAKADLVVYNGLGLEGWLDKLLEAAGNPgvPVV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080584186 101 VVTQGITPMSIHEGPYRGQPNPHAWMSTRNALIYVENIKNALIKYDPQNAATYTRNAAAYAQRIRNLDRPLREKLARVPq 180
Cdd:COG0803 109 DASEGIDLLELEEGHDHGEPDPHVWLDPKNAKKVAENIADALAELDPANAAYYEANAAAYLAELDALDAEIKAKLAAIP- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080584186 181 nQRFLVTSEGAFSYLARDYGFKEVYLWPINAEQQGTPQQVRRVINTVRQNHIPVVFSESTVSPRPMRQVSRETGAKyggV 260
Cdd:COG0803 188 -GRKLVTSHDAFGYLARAYGLEVVAIQGISPGSEPSPADLAELIDLIKEEGVKAIFVESQVSPKLAETLAEETGVK---V 263
|
250 260
....*....|....*....|.
gi 1080584186 261 LYVDSLSAKNGPVPTYLDLLN 281
Cdd:COG0803 264 LYLDSLGGPGGPGDTYLDMMR 284
|
|
| anch_rpt_subst |
TIGR03772 |
anchored repeat ABC transporter, substrate-binding protein; Members of this protein family are ... |
118-292 |
1.03e-30 |
|
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: 119.97 E-value: 1.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080584186 118 GQPNPHAWMSTRNALIYVENIKNALIKYDPQNAATYTRNAAAYAQRIRNLDRPLREKLARVPQNQRFLVTSEGAFSYLAR 197
Cdd:TIGR03772 307 GEIDPHLWHNVKNAIAYVEVIRDKLIEVDPRGAQAYRSNASAYIHRLERLDTYVRRTIATIPPSRRHLITTHDAYSYLGQ 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080584186 198 DYGFKEVYLWPINAEQQGTPQQVRRVINTVRQNHIPVVFSESTVSPRP--MRQVSRETGAKYGGVlYVDSLsakNGPVPT 275
Cdd:TIGR03772 387 AYGLNIAGFVTPNPAVEPSLADRRRLTRTIENLKVPAVFLEPNLAARSttLNEIADELGVRVCAI-YGDTF---DDDVTN 462
|
170
....*....|....*..
gi 1080584186 276 YLDLLNTTVSTIVRGFG 292
Cdd:TIGR03772 463 YVDLMRFNADSLADCLG 479
|
|
| znuA |
PRK09545 |
zinc ABC transporter substrate-binding protein ZnuA; |
26-258 |
2.58e-12 |
|
zinc ABC transporter substrate-binding protein ZnuA;
Pssm-ID: 236558 [Multi-domain] Cd Length: 311 Bit Score: 65.80 E-value: 2.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080584186 26 VVTTFTVIQDIAQNVAGDAAVVESITKPGAEIHDYQPTPQDIAKAQSADLVLWNGLNLERWFERFFQNVRNKPAVVVTQ- 104
Cdd:PRK09545 27 VVTSIKPLGFIASAIADGVTETEVLLPDGASPHDYSLRPSDVKRLQSADLVVWVGPEMEAFLEKPVSKLPENKQVTIAQl 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080584186 105 -GITPMSI--------------------HEGPYRGQPNPHAWMSTRNALIYVENIKNALIKYDPQNAATYTRNAAAYAQR 163
Cdd:PRK09545 107 pDVKPLLMkgahddhhdddhdhagheksDEDHHHGEYNMHIWLSPEIARATAVAIHDKLVELMPQSKAKLDANLKDFEAQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080584186 164 IRNLDRPLREKLARVpQNQRFLVTSEgAFSYLARDYGFKEVYLWPINAEQQGTPQQVRRVINTVRQNHIPVVFSESTVSP 243
Cdd:PRK09545 187 LAQTDKQIGNQLAPV-KGKGYFVFHD-AYGYFEKHYGLTPLGHFTVNPEIQPGAQRLHEIRTQLVEQKATCVFAEPQFRP 264
|
250
....*....|....*
gi 1080584186 244 RPMRQVSRETGAKYG 258
Cdd:PRK09545 265 AVIESVAKGTSVRMG 279
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PsaA |
cd01137 |
Metal binding protein PsaA. These proteins have been shown to function as initial receptors ... |
23-292 |
6.98e-155 |
|
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: 433.63 E-value: 6.98e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080584186 23 KFKVVTTFTVIQDIAQNVAGDAAVVESITKPGAEIHDYQPTPQDIAKAQSADLVLWNGLNLERWFERFFQNVRNK-PAVV 101
Cdd:cd01137 17 KLKVVATFSILADIARNIAGDRVNVTSIVPPGADPHEYEPTPSDIKKLSKADLILYNGLNLEPWLERLVKNAGKDvPVVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080584186 102 VTQGITPMSIHEGPYRGQPNPHAWMSTRNALIYVENIKNALIKYDPQNAATYTRNAAAYAQRIRNLDRPLREKLARVPQN 181
Cdd:cd01137 97 VSEGIDPIPLEEGHYKGKPDPHAWMSPKNAIIYVKNIAKALSEADPANAETYQKNAAAYKAKLKALDEWAKAKFATIPAE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080584186 182 QRFLVTSEGAFSYLARDYGFKEVYLWPINAEQQGTPQQVRRVINTVRQNHIPVVFSESTVSPRPMRQVSRETGAKYGGVL 261
Cdd:cd01137 177 KRKLVTSEGAFSYFAKAYGLKEAYLWPINTEEEGTPKQVATLIEQVKKEKVPAVFVESTVNDRLMKQVAKETGAKIGGQL 256
|
250 260 270
....*....|....*....|....*....|.
gi 1080584186 262 YVDSLSAKNGPVPTYLDLLNTTVSTIVRGFG 292
Cdd:cd01137 257 YTDSLSEKGGPADTYLDMMEHNLDTIVEGLG 287
|
|
| ZnuA |
pfam01297 |
Zinc-uptake complex component A periplasmic; ZnuA includes periplasmic solute binding proteins ... |
26-290 |
1.29e-122 |
|
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: 351.47 E-value: 1.29e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080584186 26 VVTTFTVIQDIAQNVAGDAAVVESITKPGAEIHDYQPTPQDIAKAQSADLVLWNGLNLERWFERFFQNVRNKPAVVVTQG 105
Cdd:pfam01297 1 VVATTYPLADLAKQIGGDRVEVTSLVPPGADPHDYEPTPSDIAALSDADLVVYNGLGLEPWLDKLLEALPNKKVVDASEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080584186 106 ITPMsIHEGPYRGQP------NPHAWMSTRNALIYVENIKNALIKYDPQNAATYTRNAAAYAQRIRNLDRPLREKLARVP 179
Cdd:pfam01297 81 VELL-DEEGEEEDHDghdhgyDPHVWLDPKNAKKMAENIADALSELDPANAATYEANAAAYLAELDALDAEIKEQLASIP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080584186 180 QNQRFLVTSEGAFSYLARDYGFKEVYLWPINAEQQGTPQQVRRVINTVRQNHIPVVFSESTVSPRPMRQVSRETGAKYGG 259
Cdd:pfam01297 160 EKTRKLVTSHDAFGYLARAYGLEQVGIQGVSPESEPSAADLAELIDLIKEKKVKAIFVEPQVSPKLAETVAKETGVKVLG 239
|
250 260 270
....*....|....*....|....*....|.
gi 1080584186 260 VLYVDSLSAKNGPVpTYLDLLNTTVSTIVRG 290
Cdd:pfam01297 240 PLYTDSLGEPGGGA-TYLDLMRHNLDTLAEA 269
|
|
| ZnuA |
COG0803 |
ABC-type Zn uptake system ZnuABC, Zn-binding component ZnuA [Inorganic ion transport and ... |
23-281 |
2.21e-122 |
|
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: 351.47 E-value: 2.21e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080584186 23 KFKVVTTFTVIQDIAQNVAGDAAVVESITKPGAEIHDYQPTPQDIAKAQSADLVLWNGLNLERWFERFFQNVRNK--PAV 100
Cdd:COG0803 29 KLKVVATFSPLADLAKQIGGDKVEVTSLVPPGADPHDYEPTPSDIAKLAKADLVVYNGLGLEGWLDKLLEAAGNPgvPVV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080584186 101 VVTQGITPMSIHEGPYRGQPNPHAWMSTRNALIYVENIKNALIKYDPQNAATYTRNAAAYAQRIRNLDRPLREKLARVPq 180
Cdd:COG0803 109 DASEGIDLLELEEGHDHGEPDPHVWLDPKNAKKVAENIADALAELDPANAAYYEANAAAYLAELDALDAEIKAKLAAIP- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080584186 181 nQRFLVTSEGAFSYLARDYGFKEVYLWPINAEQQGTPQQVRRVINTVRQNHIPVVFSESTVSPRPMRQVSRETGAKyggV 260
Cdd:COG0803 188 -GRKLVTSHDAFGYLARAYGLEVVAIQGISPGSEPSPADLAELIDLIKEEGVKAIFVESQVSPKLAETLAEETGVK---V 263
|
250 260
....*....|....*....|.
gi 1080584186 261 LYVDSLSAKNGPVPTYLDLLN 281
Cdd:COG0803 264 LYLDSLGGPGGPGDTYLDMMR 284
|
|
| AdcA |
cd01017 |
Metal binding protein AdcA. These proteins have been shown to function in the ABC uptake of ... |
23-292 |
1.83e-77 |
|
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: 237.19 E-value: 1.83e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080584186 23 KFKVVTTFTVIQDIAQNVAGDAAVVESITKPGAEIHDYQPTPQDIAKAQSADLVLWNGLNLERWFERFFQNVRNKPAVVV 102
Cdd:cd01017 3 KLKVVTTFYPLYEFTKAIGGDKADVKLIIPAGTEPHDFEPSPKDIARIADADVFVYNGLGMETWAEKVLKSLQNKKLKVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080584186 103 --TQGITPMS---------IHEGPYRGQPNPHAWMSTRNALIYVENIKNALIKYDPQNAATYTRNAAAYAQRIRNLDRPL 171
Cdd:cd01017 83 eaSKGIKLLKaggaehdhdHSHSHHHGDYDPHVWLSPVLAIQQVENIKDALIKLDPDNKEYYEKNAAAYAKKLEALDQEY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080584186 172 REKLARVPqnQRFLVTSEGAFSYLARDYGFKEVYLWPINAEQQGTPQQVRRVINTVRQNHIPVVFSESTVSPRPMRQVSR 251
Cdd:cd01017 163 RAKLAKAK--GKTFVTQHAAFGYLARRYGLKQIAIVGVSPEVEPSPKQLAELVEFVKKSDVKYIFFEENASSKIAETLAK 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1080584186 252 ETGAKyggVLYVDSLS------AKNGpvPTYLDLLNTTVSTIVRGFG 292
Cdd:cd01017 241 ETGAK---LLVLNPLEtltkeeIDDG--KDYFSLMKENLETLKRALK 282
|
|
| TroA |
cd01016 |
Metal binding protein TroA. These proteins have been shown to function as initial receptors in ... |
23-292 |
5.26e-51 |
|
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: 169.08 E-value: 5.26e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080584186 23 KFKVVTTFTVIQDIAQNVAGDAAVVESITKPGAEIHDYQPTPQDIAKAQSADLVLWNGLNLERWFERFFQNVRN-KPAVV 101
Cdd:cd01016 1 KPNVVTTTGMIADAVENIGGDHVEVTGLMGPGVDPHLYKATAGDVEKLQNADVVFYNGLHLEGKMSDVLSKLGSsKSVIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080584186 102 VTQGITPMSIHEGPYRGQPNPHAWMSTRNALIYVENIKNALIKYDPQNAATYTRNAAAYAQRIRNLDRPLREKLARVPQN 181
Cdd:cd01016 81 LEDTLDRSQLILDEEEGTYDPHIWFDVKLWKYAVKAVAEVLSEKLPEHKDEFQANSEAYVEELDSLDAYAKKKIAEIPEQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080584186 182 QRFLVTSEGAFSYLARDYGFKEVYLWPINAEQQGTPQQVRRVINTVRQNHIPVVFSESTVSPRPMRQVSRETGAK----- 256
Cdd:cd01016 161 QRVLVTAHDAFGYFGRAYGFEVKGLQGISTDSEAGLRDINELVDLIVERKIKAIFVESSVNQKSIEALQDAVKARghdvq 240
|
250 260 270
....*....|....*....|....*....|....*.
gi 1080584186 257 YGGVLYVDSLSAKNGPVPTYLDLLNTTVSTIVRGFG 292
Cdd:cd01016 241 IGGELYSDAMGEEGTSEGTYIGMFKHNVDTIVEALK 276
|
|
| ZntC |
cd01018 |
Metal binding protein ZntC. These proteins are predicted to function as initial receptors in ... |
40-269 |
2.00e-48 |
|
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: 162.15 E-value: 2.00e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080584186 40 VAGDAAVVESITKPGAEIHDYQPTPQDIAKAQSADLVLWNGLNLE-RWFERFFQNVRNKPAVVVTQGIT--PMSIHEG-- 114
Cdd:cd01018 19 IAGDTVDVVVLVPPGSNPHTYEPKPQQMKKLSEADLYFRIGLGFEeVWLERFRSNNPKMQVVNMSKGITliPMADHHHhh 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080584186 115 ------PYRGQPNPHAWMSTRNALIYVENIKNALIKYDPQNAATYTRNAAAYAQRIRNLDRPLREKLARVPQnQRFLVtS 188
Cdd:cd01018 99 hgehehHHHGNYDPHIWLSPANAKIMAENIYEALAELDPQNATYYQANLDALLAELDALDSEIRTILSKLKQ-RAFMV-Y 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080584186 189 EGAFSYLARDYGFKEVylwPInaEQQG---TPQQVRRVINTVRQNHIPVVFSESTVSPRPMRQVSRETGAKyggVLYVDS 265
Cdd:cd01018 177 HPAWGYFARDYGLTQI---PI--EEEGkepSPADLKRLIDLAKEKGVRVVFVQPQFSTKSAEAIAREIGAK---VVTIDP 248
|
....
gi 1080584186 266 LSAK 269
Cdd:cd01018 249 LAAD 252
|
|
| ZnuA |
cd01019 |
Zinc binding protein ZnuA. These proteins have been shown to function as initial receptors in ... |
23-258 |
1.47e-43 |
|
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: 150.21 E-value: 1.47e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080584186 23 KFKVVTTFTVIQDIAQNVAGDAAVVESITKPGAEIHDYQPTPQDIAKAQSADLVLWNGLNLERWFERFFQNVRNKPAVVV 102
Cdd:cd01019 3 EASVLTSIKPLGFIAAAIMGGVGEVEVLVPPGASPHDYELRPSDARKLQEADLVVWIGPDLEAFLDKVLQGRKKGKVLTL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080584186 103 TQGI-------------------TPMSIHEGPYRGQPNPHAWMSTRNALIYVENIKNALIKYDPQNAATYTRNAAAYAQR 163
Cdd:cd01019 83 AKLIdlktledgashgdhehdheHAHGEHDGHEEGGLDPHLWLSPENAAEVAQAVAEKLSALDPDNAATYAANLEAFNAR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080584186 164 IRNLDRPLREKLARVpQNQRFLVTsEGAFSYLARDYGFKEVYLWPINAEQQGTPQQVRRVINTVRQNHIPVVFSESTVSP 243
Cdd:cd01019 163 LAELDATIKERLAPV-KTKPFFVF-HDAYGYFEKRYGLTQAGVFTIDPEIDPGAKRLAKIRKEIKEKGATCVFAEPQFHP 240
|
250
....*....|....*
gi 1080584186 244 RPMRQVSRETGAKYG 258
Cdd:cd01019 241 KIAETLAEGTGAKVG 255
|
|
| ZnuA |
COG4531 |
ABC-type Zn2+ transport system, periplasmic component/surface adhesin ZnuA [Inorganic ion ... |
25-288 |
9.57e-41 |
|
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: 143.05 E-value: 9.57e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080584186 25 KVVTTFTVIQDIAQNVAGDAAVVESITKPGAEIHDYQPTPQDIAKAQSADLVLWNGLNLERWFERFFQNVRNKpAVVVT- 103
Cdd:COG4531 11 RVVTSIKPLHSLVAAVMDGVGEPELLLPPGASPHDYALRPSDARALQDADLVFWVGPDLEPFLEKPLETLAPD-AKVVEl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080584186 104 ---QGITPMSI------------------------HEGPYRGQPNPHAWMSTRNALIYVENIKNALIKYDPQNAATYTRN 156
Cdd:COG4531 90 lelPGLTLLPFreggdfehhdhhdehhhhhhhhddHHDHHHGGYDPHLWLSPENAKAWAAAIADALSELDPENAATYQAN 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080584186 157 AAAYAQRIRNLDRPLREKLARVpQNQRFLVTSEgAFSYLARDYGFKEVYLWPINAEQQGTPQQVRRVINTVRQNHIPVVF 236
Cdd:COG4531 170 AAAFEARLDALDAEIAAQLAPV-KGKPFFVFHD-AYQYFEKRFGLNALGAITLNPEIQPGAKRLAEIREKLKELGAVCVF 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1080584186 237 SESTVSPRPMRQVSRETGAKYgGVLyvDSLSAKNGPVPT-YLDLLNTTVSTIV 288
Cdd:COG4531 248 AEPQFNPALVETVAEGTGVRT-GVL--DPLGADLEPGPDlYFQLLRQLADSLA 297
|
|
| anch_rpt_subst |
TIGR03772 |
anchored repeat ABC transporter, substrate-binding protein; Members of this protein family are ... |
118-292 |
1.03e-30 |
|
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: 119.97 E-value: 1.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080584186 118 GQPNPHAWMSTRNALIYVENIKNALIKYDPQNAATYTRNAAAYAQRIRNLDRPLREKLARVPQNQRFLVTSEGAFSYLAR 197
Cdd:TIGR03772 307 GEIDPHLWHNVKNAIAYVEVIRDKLIEVDPRGAQAYRSNASAYIHRLERLDTYVRRTIATIPPSRRHLITTHDAYSYLGQ 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080584186 198 DYGFKEVYLWPINAEQQGTPQQVRRVINTVRQNHIPVVFSESTVSPRP--MRQVSRETGAKYGGVlYVDSLsakNGPVPT 275
Cdd:TIGR03772 387 AYGLNIAGFVTPNPAVEPSLADRRRLTRTIENLKVPAVFLEPNLAARSttLNEIADELGVRVCAI-YGDTF---DDDVTN 462
|
170
....*....|....*..
gi 1080584186 276 YLDLLNTTVSTIVRGFG 292
Cdd:TIGR03772 463 YVDLMRFNADSLADCLG 479
|
|
| TroA_c |
cd01145 |
Periplasmic binding protein TroA_c. These proteins are predicted to function as initial ... |
26-204 |
6.69e-30 |
|
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: 112.21 E-value: 6.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080584186 26 VVTTFTVIQDIAQNVAGDAAVVESITKPGAEIHDYQPTPQDIAKAQSADLVLWNGLNLERWFERFFQNVRN-------KP 98
Cdd:cd01145 5 VVVTFPDLKDLVREVAGDAVIVSALTPPGVDPHQYQLKPSDIAKMRKADLVVTSGHELEGFEPKLAELSSNskvqpgiKI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080584186 99 AVVVTQGITPMSIHEGPYRGQPNPHAWMSTRNALIYVENIKNALIKYDPQNAATYTRNAAAYAQRIRNLDRPLREKLArv 178
Cdd:cd01145 85 LIEDSDTVGMVDRAMGDYHGKGNPHVWLDPNNAPALAKALADALIELDPSEQEEYKENLRVFLAKLNKLLREWERQFE-- 162
|
170 180
....*....|....*....|....*.
gi 1080584186 179 PQNQRFLVTSEGAFSYLARDYGFKEV 204
Cdd:cd01145 163 GLKGIQVVAYHPSYQYLADWLGIEVV 188
|
|
| TroA_b |
cd01020 |
Metal binding protein TroA_b. These proteins are predicted to function as initial receptors ... |
23-242 |
2.45e-26 |
|
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: 104.06 E-value: 2.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080584186 23 KFKVVTTFTVIQDIAQNVAGDAAVVESI-TKPGAEIHDYQPTPQDIAKAQSADLVLWNGLNLERWFERFFQNvrNKPAVV 101
Cdd:cd01020 2 KINVVASTNFWGSVAEAVGGDHVEVTSIiTNPDVDPHDFEPTPTDAAKVSTADIVVYNGGGYDPWMTKLLAD--TKDVIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080584186 102 VTQGITPMSIHEGpyrgqPNPHAWMSTRNALIYVENIKNALIKYDPQNAATYTRNAAAYaqrIRNLDrPLREKLARVP-- 179
Cdd:cd01020 80 IAADLDGHDDKEG-----DNPHLWYDPETMSKVANALADALVKADPDNKKYYQANAKKF---VASLK-PLAAKIAELSak 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1080584186 180 -QNQRFLVTsEGAFSYLARDYGFKEV----YLWPINAEQQGTPQQVRRVINTVRQNHIPVVFSESTVS 242
Cdd:cd01020 151 yKGAPVAAT-EPVFDYLLDALGMKERtpkgYTATTESETEPSPADIAAFQNAIKNRQIDALIVNPQQA 217
|
|
| TroA-like |
cd00636 |
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ... |
25-188 |
8.16e-15 |
|
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: 70.28 E-value: 8.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080584186 25 KVVTTFTVIQDIAQNVAGDAAVVESITKPGAEI-------------HDYQPTPQDIAKAQsADLVLWNGLNLERWFERFF 91
Cdd:cd00636 2 RVVALDPGATELLLALGGDDKPVGVADPSGYPPeakallekvpdvgHGYEPNLEKIAALK-PDLIIANGSGLEAWLDKLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080584186 92 QNvrNKPAVVVTQGITpmsihegpyrgqpnphawMSTRNALIYVENIKNALIKYDpqnaatytrNAAAYAQRIRNLDRPL 171
Cdd:cd00636 81 KI--AIPVVVVDEASE------------------LSLENIKESIRLIGKALGKEE---------NAEELIAELDARLAEL 131
|
170
....*....|....*..
gi 1080584186 172 REKLARVPQNQRFLVTS 188
Cdd:cd00636 132 RAKLAKIPKKKVSLVVG 148
|
|
| znuA |
PRK09545 |
zinc ABC transporter substrate-binding protein ZnuA; |
26-258 |
2.58e-12 |
|
zinc ABC transporter substrate-binding protein ZnuA;
Pssm-ID: 236558 [Multi-domain] Cd Length: 311 Bit Score: 65.80 E-value: 2.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080584186 26 VVTTFTVIQDIAQNVAGDAAVVESITKPGAEIHDYQPTPQDIAKAQSADLVLWNGLNLERWFERFFQNVRNKPAVVVTQ- 104
Cdd:PRK09545 27 VVTSIKPLGFIASAIADGVTETEVLLPDGASPHDYSLRPSDVKRLQSADLVVWVGPEMEAFLEKPVSKLPENKQVTIAQl 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080584186 105 -GITPMSI--------------------HEGPYRGQPNPHAWMSTRNALIYVENIKNALIKYDPQNAATYTRNAAAYAQR 163
Cdd:PRK09545 107 pDVKPLLMkgahddhhdddhdhagheksDEDHHHGEYNMHIWLSPEIARATAVAIHDKLVELMPQSKAKLDANLKDFEAQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080584186 164 IRNLDRPLREKLARVpQNQRFLVTSEgAFSYLARDYGFKEVYLWPINAEQQGTPQQVRRVINTVRQNHIPVVFSESTVSP 243
Cdd:PRK09545 187 LAQTDKQIGNQLAPV-KGKGYFVFHD-AYGYFEKHYGLTPLGHFTVNPEIQPGAQRLHEIRTQLVEQKATCVFAEPQFRP 264
|
250
....*....|....*
gi 1080584186 244 RPMRQVSRETGAKYG 258
Cdd:PRK09545 265 AVIESVAKGTSVRMG 279
|
|
| |
