|
Name |
Accession |
Description |
Interval |
E-value |
| znuA |
PRK09545 |
zinc ABC transporter substrate-binding protein ZnuA; |
2-320 |
1.14e-167 |
|
zinc ABC transporter substrate-binding protein ZnuA;
Pssm-ID: 236558 [Multi-domain] Cd Length: 311 Bit Score: 468.33 E-value: 1.14e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621387588 2 KTILKMSAISTALLTLPMMANADVLASVKPLGFIASAVANGVTDTQILVPAGASPHDYSLKLSDIQKVKSADLVLWVGED 81
Cdd:PRK09545 4 KTLLFAALLAALLGGATQAANAAVVTSIKPLGFIASAIADGVTETEVLLPDGASPHDYSLRPSDVKRLQSADLVVWVGPE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621387588 82 VDSFLEKPLSQIDRQKVITIADLAEVKPLLIQAHHEHFHEEGEHDHKHDHKHEHKSGHEhdhdhenheglsTNWHVWYSP 161
Cdd:PRK09545 84 MEAFLEKPVSKLPENKQVTIAQLPDVKPLLMKGAHDDHHDDDHDHAGHEKSDEDHHHGE------------YNMHIWLSP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621387588 162 AVSQIVAQKVADKLTVQFPNKKELIAKNLADFNRTLAERSDKIKAQLAPFKEKGFFVFHDAYGYFNDAYGLKQTGYFTIN 241
Cdd:PRK09545 152 EIARATAVAIHDKLVELMPQSKAKLDANLKDFEAQLAQTDKQIGNQLAPVKGKGYFVFHDAYGYFEKHYGLTPLGHFTVN 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1621387588 242 PLVAPGAKTLAHIKEEIAEHRVNCLFAEPQFTPKVIESLAKGTAVNVGRLDPIGDGVELGANSYANFLQATADSYAQCL 320
Cdd:PRK09545 232 PEIQPGAQRLHEIRTQLVEQKATCVFAEPQFRPAVIESVAKGTSVRMGTLDPLGTNIKLGKDSYSEFLSQLANQYASCL 310
|
|
| ZnuA |
COG4531 |
ABC-type Zn2+ transport system, periplasmic component/surface adhesin ZnuA [Inorganic ion ... |
14-320 |
1.72e-127 |
|
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: 366.08 E-value: 1.72e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621387588 14 LLTLPMMANADVLASVKPLGFIASAVANGVTDTQILVPAGASPHDYSLKLSDIQKVKSADLVLWVGEDVDSFLEKPLSQI 93
Cdd:COG4531 1 LASAAAAAAPRVVTSIKPLHSLVAAVMDGVGEPELLLPPGASPHDYALRPSDARALQDADLVFWVGPDLEPFLEKPLETL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621387588 94 -DRQKVITIADLAEVKPLLIQAHHEHFHEEGEHDHKHDHKHEHKSGHEHDHdhenheglSTNWHVWYSPAVSQIVAQKVA 172
Cdd:COG4531 81 aPDAKVVELLELPGLTLLPFREGGDFEHHDHHDEHHHHHHHHDDHHDHHHG--------GYDPHLWLSPENAKAWAAAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621387588 173 DKLTVQFPNKKELIAKNLADFNRTLAERSDKIKAQLAPFKEKGFFVFHDAYGYFNDAYGLKQTGYFTINPLVAPGAKTLA 252
Cdd:COG4531 153 DALSELDPENAATYQANAAAFEARLDALDAEIAAQLAPVKGKPFFVFHDAYQYFEKRFGLNALGAITLNPEIQPGAKRLA 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1621387588 253 HIKEEIAEHRVNCLFAEPQFTPKVIESLAKGTAVNVGRLDPIGDGVELGANSYANFLQATADSYAQCL 320
Cdd:COG4531 233 EIREKLKELGAVCVFAEPQFNPALVETVAEGTGVRTGVLDPLGADLEPGPDLYFQLLRQLADSLASCL 300
|
|
| ZnuA |
cd01019 |
Zinc binding protein ZnuA. These proteins have been shown to function as initial receptors in ... |
20-320 |
7.98e-125 |
|
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: 358.99 E-value: 7.98e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621387588 20 MANADVLASVKPLGFIASAVANGVTDTQILVPAGASPHDYSLKLSDIQKVKSADLVLWVGEDVDSFLEKPLSQIDRQKVI 99
Cdd:cd01019 1 AAEASVLTSIKPLGFIAAAIMGGVGEVEVLVPPGASPHDYELRPSDARKLQEADLVVWIGPDLEAFLDKVLQGRKKGKVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621387588 100 TIADLAEVKPLLIQAHHEHFHEEGEHDHKHDHKHEhksghehdhdhenheGLSTNWHVWYSPAVSQIVAQKVADKLTVQF 179
Cdd:cd01019 81 TLAKLIDLKTLEDGASHGDHEHDHEHAHGEHDGHE---------------EGGLDPHLWLSPENAAEVAQAVAEKLSALD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621387588 180 PNKKELIAKNLADFNRTLAERSDKIKAQLAPFKEKGFFVFHDAYGYFNDAYGLKQTGYFTINPLVAPGAKTLAHIKEEIA 259
Cdd:cd01019 146 PDNAATYAANLEAFNARLAELDATIKERLAPVKTKPFFVFHDAYGYFEKRYGLTQAGVFTIDPEIDPGAKRLAKIRKEIK 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1621387588 260 EHRVNCLFAEPQFTPKVIESLAKGTAVNVGRLDPIGDGVELGANSYANFLQATADSYAQCL 320
Cdd:cd01019 226 EKGATCVFAEPQFHPKIAETLAEGTGAKVGELDPLGGLIELGKNSYVNFLRNLADSLASCL 286
|
|
| ZnuA |
pfam01297 |
Zinc-uptake complex component A periplasmic; ZnuA includes periplasmic solute binding proteins ... |
25-319 |
8.01e-70 |
|
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: 218.19 E-value: 8.01e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621387588 25 VLASVKPLGFIASAVANGVTDTQILVPAGASPHDYSLKLSDIQKVKSADLVLWVGEDVDSFLEKPLSQIDRQKVITIADl 104
Cdd:pfam01297 1 VVATTYPLADLAKQIGGDRVEVTSLVPPGADPHDYEPTPSDIAALSDADLVVYNGLGLEPWLDKLLEALPNKKVVDASE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621387588 105 aEVKPLLiqahhehfheegehdhkhdhkhehksgHEHDHDHENHEGLSTNWHVWYSPAVSQIVAQKVADKLTVQFPNKKE 184
Cdd:pfam01297 80 -GVELLD---------------------------EEGEEEDHDGHDHGYDPHVWLDPKNAKKMAENIADALSELDPANAA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621387588 185 LIAKNLADFNRTLAERSDKIKAQLAPFKEKG--FFVFHDAYGYFNDAYGLKQTGYFTINPLVAPGAKTLAHIKEEIAEHR 262
Cdd:pfam01297 132 TYEANAAAYLAELDALDAEIKEQLASIPEKTrkLVTSHDAFGYLARAYGLEQVGIQGVSPESEPSAADLAELIDLIKEKK 211
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1621387588 263 VNCLFAEPQFTPKVIESLAKGTAVNVGR-LDPIGDGVELGANSYANFLQATADSYAQC 319
Cdd:pfam01297 212 VKAIFVEPQVSPKLAETVAKETGVKVLGpLYTDSLGEPGGGATYLDLMRHNLDTLAEA 269
|
|
| anch_rpt_subst |
TIGR03772 |
anchored repeat ABC transporter, substrate-binding protein; Members of this protein family are ... |
156-321 |
1.65e-14 |
|
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: 73.74 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621387588 156 HVWYSPAVSQIVAQKVADKLTVQFPNKKELIAKNLADFNRTLAERSDKIKAQLA--PFKEKGFFVFHDAYGYFNDAYGLK 233
Cdd:TIGR03772 312 HLWHNVKNAIAYVEVIRDKLIEVDPRGAQAYRSNASAYIHRLERLDTYVRRTIAtiPPSRRHLITTHDAYSYLGQAYGLN 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621387588 234 QTGYFTINPLVAPGAKTLAHIKEEIAEHRVNCLFAEPQFTPK--VIESLAKGTAVNVGRLdpIGDGVELGANSYANFLQA 311
Cdd:TIGR03772 392 IAGFVTPNPAVEPSLADRRRLTRTIENLKVPAVFLEPNLAARstTLNEIADELGVRVCAI--YGDTFDDDVTNYVDLMRF 469
|
170
....*....|
gi 1621387588 312 TADSYAQCLS 321
Cdd:TIGR03772 470 NADSLADCLG 479
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| znuA |
PRK09545 |
zinc ABC transporter substrate-binding protein ZnuA; |
2-320 |
1.14e-167 |
|
zinc ABC transporter substrate-binding protein ZnuA;
Pssm-ID: 236558 [Multi-domain] Cd Length: 311 Bit Score: 468.33 E-value: 1.14e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621387588 2 KTILKMSAISTALLTLPMMANADVLASVKPLGFIASAVANGVTDTQILVPAGASPHDYSLKLSDIQKVKSADLVLWVGED 81
Cdd:PRK09545 4 KTLLFAALLAALLGGATQAANAAVVTSIKPLGFIASAIADGVTETEVLLPDGASPHDYSLRPSDVKRLQSADLVVWVGPE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621387588 82 VDSFLEKPLSQIDRQKVITIADLAEVKPLLIQAHHEHFHEEGEHDHKHDHKHEHKSGHEhdhdhenheglsTNWHVWYSP 161
Cdd:PRK09545 84 MEAFLEKPVSKLPENKQVTIAQLPDVKPLLMKGAHDDHHDDDHDHAGHEKSDEDHHHGE------------YNMHIWLSP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621387588 162 AVSQIVAQKVADKLTVQFPNKKELIAKNLADFNRTLAERSDKIKAQLAPFKEKGFFVFHDAYGYFNDAYGLKQTGYFTIN 241
Cdd:PRK09545 152 EIARATAVAIHDKLVELMPQSKAKLDANLKDFEAQLAQTDKQIGNQLAPVKGKGYFVFHDAYGYFEKHYGLTPLGHFTVN 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1621387588 242 PLVAPGAKTLAHIKEEIAEHRVNCLFAEPQFTPKVIESLAKGTAVNVGRLDPIGDGVELGANSYANFLQATADSYAQCL 320
Cdd:PRK09545 232 PEIQPGAQRLHEIRTQLVEQKATCVFAEPQFRPAVIESVAKGTSVRMGTLDPLGTNIKLGKDSYSEFLSQLANQYASCL 310
|
|
| ZnuA |
COG4531 |
ABC-type Zn2+ transport system, periplasmic component/surface adhesin ZnuA [Inorganic ion ... |
14-320 |
1.72e-127 |
|
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: 366.08 E-value: 1.72e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621387588 14 LLTLPMMANADVLASVKPLGFIASAVANGVTDTQILVPAGASPHDYSLKLSDIQKVKSADLVLWVGEDVDSFLEKPLSQI 93
Cdd:COG4531 1 LASAAAAAAPRVVTSIKPLHSLVAAVMDGVGEPELLLPPGASPHDYALRPSDARALQDADLVFWVGPDLEPFLEKPLETL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621387588 94 -DRQKVITIADLAEVKPLLIQAHHEHFHEEGEHDHKHDHKHEHKSGHEHDHdhenheglSTNWHVWYSPAVSQIVAQKVA 172
Cdd:COG4531 81 aPDAKVVELLELPGLTLLPFREGGDFEHHDHHDEHHHHHHHHDDHHDHHHG--------GYDPHLWLSPENAKAWAAAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621387588 173 DKLTVQFPNKKELIAKNLADFNRTLAERSDKIKAQLAPFKEKGFFVFHDAYGYFNDAYGLKQTGYFTINPLVAPGAKTLA 252
Cdd:COG4531 153 DALSELDPENAATYQANAAAFEARLDALDAEIAAQLAPVKGKPFFVFHDAYQYFEKRFGLNALGAITLNPEIQPGAKRLA 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1621387588 253 HIKEEIAEHRVNCLFAEPQFTPKVIESLAKGTAVNVGRLDPIGDGVELGANSYANFLQATADSYAQCL 320
Cdd:COG4531 233 EIREKLKELGAVCVFAEPQFNPALVETVAEGTGVRTGVLDPLGADLEPGPDLYFQLLRQLADSLASCL 300
|
|
| ZnuA |
cd01019 |
Zinc binding protein ZnuA. These proteins have been shown to function as initial receptors in ... |
20-320 |
7.98e-125 |
|
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: 358.99 E-value: 7.98e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621387588 20 MANADVLASVKPLGFIASAVANGVTDTQILVPAGASPHDYSLKLSDIQKVKSADLVLWVGEDVDSFLEKPLSQIDRQKVI 99
Cdd:cd01019 1 AAEASVLTSIKPLGFIAAAIMGGVGEVEVLVPPGASPHDYELRPSDARKLQEADLVVWIGPDLEAFLDKVLQGRKKGKVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621387588 100 TIADLAEVKPLLIQAHHEHFHEEGEHDHKHDHKHEhksghehdhdhenheGLSTNWHVWYSPAVSQIVAQKVADKLTVQF 179
Cdd:cd01019 81 TLAKLIDLKTLEDGASHGDHEHDHEHAHGEHDGHE---------------EGGLDPHLWLSPENAAEVAQAVAEKLSALD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621387588 180 PNKKELIAKNLADFNRTLAERSDKIKAQLAPFKEKGFFVFHDAYGYFNDAYGLKQTGYFTINPLVAPGAKTLAHIKEEIA 259
Cdd:cd01019 146 PDNAATYAANLEAFNARLAELDATIKERLAPVKTKPFFVFHDAYGYFEKRYGLTQAGVFTIDPEIDPGAKRLAKIRKEIK 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1621387588 260 EHRVNCLFAEPQFTPKVIESLAKGTAVNVGRLDPIGDGVELGANSYANFLQATADSYAQCL 320
Cdd:cd01019 226 EKGATCVFAEPQFHPKIAETLAEGTGAKVGELDPLGGLIELGKNSYVNFLRNLADSLASCL 286
|
|
| ZnuA |
pfam01297 |
Zinc-uptake complex component A periplasmic; ZnuA includes periplasmic solute binding proteins ... |
25-319 |
8.01e-70 |
|
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: 218.19 E-value: 8.01e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621387588 25 VLASVKPLGFIASAVANGVTDTQILVPAGASPHDYSLKLSDIQKVKSADLVLWVGEDVDSFLEKPLSQIDRQKVITIADl 104
Cdd:pfam01297 1 VVATTYPLADLAKQIGGDRVEVTSLVPPGADPHDYEPTPSDIAALSDADLVVYNGLGLEPWLDKLLEALPNKKVVDASE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621387588 105 aEVKPLLiqahhehfheegehdhkhdhkhehksgHEHDHDHENHEGLSTNWHVWYSPAVSQIVAQKVADKLTVQFPNKKE 184
Cdd:pfam01297 80 -GVELLD---------------------------EEGEEEDHDGHDHGYDPHVWLDPKNAKKMAENIADALSELDPANAA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621387588 185 LIAKNLADFNRTLAERSDKIKAQLAPFKEKG--FFVFHDAYGYFNDAYGLKQTGYFTINPLVAPGAKTLAHIKEEIAEHR 262
Cdd:pfam01297 132 TYEANAAAYLAELDALDAEIKEQLASIPEKTrkLVTSHDAFGYLARAYGLEQVGIQGVSPESEPSAADLAELIDLIKEKK 211
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1621387588 263 VNCLFAEPQFTPKVIESLAKGTAVNVGR-LDPIGDGVELGANSYANFLQATADSYAQC 319
Cdd:pfam01297 212 VKAIFVEPQVSPKLAETVAKETGVKVLGpLYTDSLGEPGGGATYLDLMRHNLDTLAEA 269
|
|
| ZnuA |
COG0803 |
ABC-type Zn uptake system ZnuABC, Zn-binding component ZnuA [Inorganic ion transport and ... |
2-312 |
9.63e-56 |
|
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: 182.37 E-value: 9.63e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621387588 2 KTILKMSAISTALLTLPMMANAD------VLASVKPLGFIASAVANGVTDTQILVPAGASPHDYSLKLSDIQKVKSADLV 75
Cdd:COG0803 3 RLLLALLLLAALLLAGCSAAASSaagklkVVATFSPLADLAKQIGGDKVEVTSLVPPGADPHDYEPTPSDIAKLAKADLV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621387588 76 LWVGEDVDSFLEKPLSQIDRQKVITIADLAEVKPLLIQAHHEHFheegehdhkhdhkhehksghehdhdhenheglSTNW 155
Cdd:COG0803 83 VYNGLGLEGWLDKLLEAAGNPGVPVVDASEGIDLLELEEGHDHG--------------------------------EPDP 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621387588 156 HVWYSPAVSQIVAQKVADKLTVQFPNKKELIAKNLADFNRTLAERSDKIKAQLAPFKEKGFFVFHDAYGYFNDAYGLKQT 235
Cdd:COG0803 131 HVWLDPKNAKKVAENIADALAELDPANAAYYEANAAAYLAELDALDAEIKAKLAAIPGRKLVTSHDAFGYLARAYGLEVV 210
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1621387588 236 GYFTINPLVAPGAKTLAHIKEEIAEHRVNCLFAEPQFTPKVIESLAKGTAVNVGRLDPIGDGVElGANSYANFLQAT 312
Cdd:COG0803 211 AIQGISPGSEPSPADLAELIDLIKEEGVKAIFVESQVSPKLAETLAEETGVKVLYLDSLGGPGG-PGDTYLDMMRHN 286
|
|
| AdcA |
cd01017 |
Metal binding protein AdcA. These proteins have been shown to function in the ABC uptake of ... |
25-314 |
3.27e-38 |
|
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: 137.04 E-value: 3.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621387588 25 VLASVKPLGFIASAVANGVTDTQILVPAGASPHDYSLKLSDIQKVKSADLVLWVGEDVDSFLEKPLSQIDRQKVITIADL 104
Cdd:cd01017 6 VVTTFYPLYEFTKAIGGDKADVKLIIPAGTEPHDFEPSPKDIARIADADVFVYNGLGMETWAEKVLKSLQNKKLKVVEAS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621387588 105 AEVKPLliqahhehfheegehdhkhdhkhEHKSGHEHDHDHENHEGLSTNWHVWYSPAVSQIVAQKVADKLTVQFPNKKE 184
Cdd:cd01017 86 KGIKLL-----------------------KAGGAEHDHDHSHSHHHGDYDPHVWLSPVLAIQQVENIKDALIKLDPDNKE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621387588 185 LIAKNLADFNRTLAERSDKIKAQLAPFKEKGFFVFHDAYGYFNDAYGLKQTGYFTINPLVAPGAKTLAHIKEEIAEHRVN 264
Cdd:cd01017 143 YYEKNAAAYAKKLEALDQEYRAKLAKAKGKTFVTQHAAFGYLARRYGLKQIAIVGVSPEVEPSPKQLAELVEFVKKSDVK 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1621387588 265 CLFAEPQFTPKVIESLAKGTAVNVGRLDPIGDGVELGANSYANFLQATAD 314
Cdd:cd01017 223 YIFFEENASSKIAETLAKETGAKLLVLNPLETLTKEEIDDGKDYFSLMKE 272
|
|
| ZntC |
cd01018 |
Metal binding protein ZntC. These proteins are predicted to function as initial receptors in ... |
21-318 |
2.66e-28 |
|
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: 110.14 E-value: 2.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621387588 21 ANADVLASVKPLGFIASAVANGVTDTQILVPAGASPHDYSLKLSDIQKVKSADLVLWVGEDVDS-FLEKPLS------QI 93
Cdd:cd01018 1 DKPTVAVSIEPQKYFVEKIAGDTVDVVVLVPPGSNPHTYEPKPQQMKKLSEADLYFRIGLGFEEvWLERFRSnnpkmqVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621387588 94 DRQKVITIADLAEVKplliqahhehfheegehdhkhdhkhehksgheHDHDHENHEGLSTNW--HVWYSPAVSQIVAQKV 171
Cdd:cd01018 81 NMSKGITLIPMADHH--------------------------------HHHHGEHEHHHHGNYdpHIWLSPANAKIMAENI 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621387588 172 ADKLTVQFPNKKELIAKNLADFNRTLAERSDKIKAQLAPFKEKGFFVFHDAYGYFNDAYGLKQtgyFTINPL-VAPGAKT 250
Cdd:cd01018 129 YEALAELDPQNATYYQANLDALLAELDALDSEIRTILSKLKQRAFMVYHPAWGYFARDYGLTQ---IPIEEEgKEPSPAD 205
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1621387588 251 LAHIKEEIAEHRVNCLFAEPQFTPKVIESLAKGTAVNVGRLDPIgdgvelgANSYANFLQATADSYAQ 318
Cdd:cd01018 206 LKRLIDLAKEKGVRVVFVQPQFSTKSAEAIAREIGAKVVTIDPL-------AADWEENLLKVADAFAH 266
|
|
| PsaA |
cd01137 |
Metal binding protein PsaA. These proteins have been shown to function as initial receptors ... |
10-321 |
1.87e-25 |
|
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: 103.13 E-value: 1.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621387588 10 ISTALLTLPMMANAD---VLASVKPLGFIASAVANGVTDTQILVPAGASPHDYSLKLSDIQKVKSADLVLWVGEDVDSFL 86
Cdd:cd01137 2 AACASLGSSPATAASklkVVATFSILADIARNIAGDRVNVTSIVPPGADPHEYEPTPSDIKKLSKADLILYNGLNLEPWL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621387588 87 EKPLSQIDRQKVITIADlAEVKPLLIQahhehfheegehdhkhdhkHEHKSGHehdhdhenheglsTNWHVWYSPAVSQI 166
Cdd:cd01137 82 ERLVKNAGKDVPVVAVS-EGIDPIPLE-------------------EGHYKGK-------------PDPHAWMSPKNAII 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621387588 167 VAQKVADKLTVQFPNKKELIAKNLADFNRTLAERSDKIKAQLA--PfKEKGFFVF-HDAYGYFNDAYGLKQTGYFTINPL 243
Cdd:cd01137 129 YVKNIAKALSEADPANAETYQKNAAAYKAKLKALDEWAKAKFAtiP-AEKRKLVTsEGAFSYFAKAYGLKEAYLWPINTE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621387588 244 VAPGAKTLAHIKEEIAEHRVNCLFAEPQFTPKVIESLAKGTAVNVGRL---DPIGDGVElGANSYANFLQATADSYAQCL 320
Cdd:cd01137 208 EEGTPKQVATLIEQVKKEKVPAVFVESTVNDRLMKQVAKETGAKIGGQlytDSLSEKGG-PADTYLDMMEHNLDTIVEGL 286
|
.
gi 1621387588 321 S 321
Cdd:cd01137 287 G 287
|
|
| TroA_c |
cd01145 |
Periplasmic binding protein TroA_c. These proteins are predicted to function as initial ... |
21-247 |
3.79e-21 |
|
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: 89.48 E-value: 3.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621387588 21 ANADVLASVKPLGFIASAVANGVTDTQILVPAGASPHDYSLKLSDIQKVKSADLVLWVGEDVDSFLEKPLSQIDRQKVIT 100
Cdd:cd01145 1 AALNVVVTFPDLKDLVREVAGDAVIVSALTPPGVDPHQYQLKPSDIAKMRKADLVVTSGHELEGFEPKLAELSSNSKVQP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621387588 101 IADLAEVKPLLIQAHHEHFHEEGEhdhkhdhkhehksghehdhdhenheglSTNWHVWYSPAVSQIVAQKVADKLTVQFP 180
Cdd:cd01145 81 GIKILIEDSDTVGMVDRAMGDYHG---------------------------KGNPHVWLDPNNAPALAKALADALIELDP 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1621387588 181 NKKELIAKNLADFNRTLAERSDKIKAQLAPFKEKGFFVFHDAYGYFNDAYGLKQTGYFTINPLVAPG 247
Cdd:cd01145 134 SEQEEYKENLRVFLAKLNKLLREWERQFEGLKGIQVVAYHPSYQYLADWLGIEVVASLEPLPELPPT 200
|
|
| anch_rpt_subst |
TIGR03772 |
anchored repeat ABC transporter, substrate-binding protein; Members of this protein family are ... |
156-321 |
1.65e-14 |
|
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: 73.74 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621387588 156 HVWYSPAVSQIVAQKVADKLTVQFPNKKELIAKNLADFNRTLAERSDKIKAQLA--PFKEKGFFVFHDAYGYFNDAYGLK 233
Cdd:TIGR03772 312 HLWHNVKNAIAYVEVIRDKLIEVDPRGAQAYRSNASAYIHRLERLDTYVRRTIAtiPPSRRHLITTHDAYSYLGQAYGLN 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621387588 234 QTGYFTINPLVAPGAKTLAHIKEEIAEHRVNCLFAEPQFTPK--VIESLAKGTAVNVGRLdpIGDGVELGANSYANFLQA 311
Cdd:TIGR03772 392 IAGFVTPNPAVEPSLADRRRLTRTIENLKVPAVFLEPNLAARstTLNEIADELGVRVCAI--YGDTFDDDVTNYVDLMRF 469
|
170
....*....|
gi 1621387588 312 TADSYAQCLS 321
Cdd:TIGR03772 470 NADSLADCLG 479
|
|
| TroA_b |
cd01020 |
Metal binding protein TroA_b. These proteins are predicted to function as initial receptors ... |
25-288 |
3.14e-14 |
|
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: 71.32 E-value: 3.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621387588 25 VLASVKPLGFIASAVA-NGVTDTQILVPAGASPHDYSLKLSDIQKVKSADLVLWVGEDVDSFLEKPLSQIDRQKVITiAD 103
Cdd:cd01020 5 VVASTNFWGSVAEAVGgDHVEVTSIITNPDVDPHDFEPTPTDAAKVSTADIVVYNGGGYDPWMTKLLADTKDVIVIA-AD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621387588 104 LAEvkplliqahhehfheegehdhkhdhkHEHKSGHehdhdhenheglstNWHVWYSPAVSQIVAQKVADKLTVQFPNKK 183
Cdd:cd01020 84 LDG--------------------------HDDKEGD--------------NPHLWYDPETMSKVANALADALVKADPDNK 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621387588 184 ELIAKNLADFNRTLAERSDKIKAQLAPFKEKGFFVFHDAYGYFNDAYGLK---QTGYF-TINPLVAPGAKTLAHIKEEIA 259
Cdd:cd01020 124 KYYQANAKKFVASLKPLAAKIAELSAKYKGAPVAATEPVFDYLLDALGMKertPKGYTaTTESETEPSPADIAAFQNAIK 203
|
250 260 270
....*....|....*....|....*....|..
gi 1621387588 260 EHRVNCLFAEPQFTPKV---IESLAKGTAVNV 288
Cdd:cd01020 204 NRQIDALIVNPQQASSAttnITGLAKRSGVPV 235
|
|
| TroA |
cd01016 |
Metal binding protein TroA. These proteins have been shown to function as initial receptors in ... |
32-289 |
8.46e-13 |
|
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: 67.39 E-value: 8.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621387588 32 LGFIASAVANGVTD---TQILVPAGASPHDYSLKLSDIQKVKSADLVLWVGEDVDSFLEKPLSQIDRQK-VITIADLAEV 107
Cdd:cd01016 8 TGMIADAVENIGGDhveVTGLMGPGVDPHLYKATAGDVEKLQNADVVFYNGLHLEGKMSDVLSKLGSSKsVIALEDTLDR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621387588 108 KPLLIQAHHEHFheegehdhkhdhkhehksghehdhdhenheglstNWHVWYSPAVSQIVAQKVADKLTVQFPNKKELIA 187
Cdd:cd01016 88 SQLILDEEEGTY----------------------------------DPHIWFDVKLWKYAVKAVAEVLSEKLPEHKDEFQ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621387588 188 KNLADFNRTLAERSDKIKAQLA--PFKEKGFFVFHDAYGYFNDAYGLKQTGYFTINPLVAPGAKTLAHIKEEIAEHRVNC 265
Cdd:cd01016 134 ANSEAYVEELDSLDAYAKKKIAeiPEQQRVLVTAHDAFGYFGRAYGFEVKGLQGISTDSEAGLRDINELVDLIVERKIKA 213
|
250 260
....*....|....*....|....*....
gi 1621387588 266 LFAEPQFTPKVIESL-----AKGTAVNVG 289
Cdd:cd01016 214 IFVESSVNQKSIEALqdavkARGHDVQIG 242
|
|
| |
