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Conserved domains on  [gi|748797196|ref|WP_040045182|]
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MULTISPECIES: zinc ABC transporter substrate-binding protein ZnuA [Hafnia]

Protein Classification

zinc ABC transporter substrate-binding protein( domain architecture ID 10793287)

zinc ABC transporter substrate-binding protein functions as the initial receptor for the active uptake of Zn2+

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
znuA PRK09545
zinc ABC transporter substrate-binding protein ZnuA;
2-334 0e+00

zinc ABC transporter substrate-binding protein ZnuA;


:

Pssm-ID: 236558 [Multi-domain]  Cd Length: 311  Bit Score: 548.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748797196   2 IHKKAWFKRTIIAAALVTSAgiSCAQAAVLTSIRPLGFIASAIADGVTTTEVLLPDGASPHDYALKPSDIKRLREADLVV 81
Cdd:PRK09545   1 LHKKTLLFAALLAALLGGAT--QAANAAVVTSIKPLGFIASAIADGVTETEVLLPDGASPHDYSLRPSDVKRLQSADLVV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748797196  82 WVGPEMEAFLTKPVQQLENNKNLMLTGLPAVHSLLMagdddddhdhkahaaesnveKSEKSATHNVTNGAETGSEEHHDH 161
Cdd:PRK09545  79 WVGPEMEAFLEKPVSKLPENKQVTIAQLPDVKPLLM--------------------KGAHDDHHDDDHDHAGHEKSDEDH 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748797196 162 DHGQYNLHIWLSPAIAKQIAIAIHDKLLLQSPQNKDKLDVNLRKFEEQLEQTEKNVGMMLRPVQGKGYFVFHDAYGYFEK 241
Cdd:PRK09545 139 HHGEYNMHIWLSPEIARATAVAIHDKLVELMPQSKAKLDANLKDFEAQLAQTDKQIGNQLAPVKGKGYFVFHDAYGYFEK 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748797196 242 TFGLTPLGHFTVNPEIQPGAQRLHQIRTQLVEQKAVCVFAEPQFRPAVISAVAQGTKVRQGTLDPLGSAIALGADSYMRF 321
Cdd:PRK09545 219 HYGLTPLGHFTVNPEIQPGAQRLHEIRTQLVEQKATCVFAEPQFRPAVIESVAKGTSVRMGTLDPLGTNIKLGKDSYSEF 298
                        330
                 ....*....|...
gi 748797196 322 LTQLSQQYSSCLN 334
Cdd:PRK09545 299 LSQLANQYASCLK 311
 
Name Accession Description Interval E-value
znuA PRK09545
zinc ABC transporter substrate-binding protein ZnuA;
2-334 0e+00

zinc ABC transporter substrate-binding protein ZnuA;


Pssm-ID: 236558 [Multi-domain]  Cd Length: 311  Bit Score: 548.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748797196   2 IHKKAWFKRTIIAAALVTSAgiSCAQAAVLTSIRPLGFIASAIADGVTTTEVLLPDGASPHDYALKPSDIKRLREADLVV 81
Cdd:PRK09545   1 LHKKTLLFAALLAALLGGAT--QAANAAVVTSIKPLGFIASAIADGVTETEVLLPDGASPHDYSLRPSDVKRLQSADLVV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748797196  82 WVGPEMEAFLTKPVQQLENNKNLMLTGLPAVHSLLMagdddddhdhkahaaesnveKSEKSATHNVTNGAETGSEEHHDH 161
Cdd:PRK09545  79 WVGPEMEAFLEKPVSKLPENKQVTIAQLPDVKPLLM--------------------KGAHDDHHDDDHDHAGHEKSDEDH 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748797196 162 DHGQYNLHIWLSPAIAKQIAIAIHDKLLLQSPQNKDKLDVNLRKFEEQLEQTEKNVGMMLRPVQGKGYFVFHDAYGYFEK 241
Cdd:PRK09545 139 HHGEYNMHIWLSPEIARATAVAIHDKLVELMPQSKAKLDANLKDFEAQLAQTDKQIGNQLAPVKGKGYFVFHDAYGYFEK 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748797196 242 TFGLTPLGHFTVNPEIQPGAQRLHQIRTQLVEQKAVCVFAEPQFRPAVISAVAQGTKVRQGTLDPLGSAIALGADSYMRF 321
Cdd:PRK09545 219 HYGLTPLGHFTVNPEIQPGAQRLHEIRTQLVEQKATCVFAEPQFRPAVIESVAKGTSVRMGTLDPLGTNIKLGKDSYSEF 298
                        330
                 ....*....|...
gi 748797196 322 LTQLSQQYSSCLN 334
Cdd:PRK09545 299 LSQLANQYASCLK 311
ZnuA COG4531
ABC-type Zn2+ transport system, periplasmic component/surface adhesin ZnuA [Inorganic ion ...
19-333 1.10e-155

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: 438.11  E-value: 1.10e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748797196  19 TSAGISCAQAAVLTSIRPLGFIASAIADGVTTTEVLLPDGASPHDYALKPSDIKRLREADLVVWVGPEMEAFLTKPVQQL 98
Cdd:COG4531    1 LASAAAAAAPRVVTSIKPLHSLVAAVMDGVGEPELLLPPGASPHDYALRPSDARALQDADLVFWVGPDLEPFLEKPLETL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748797196  99 -ENNKNLMLTGLPAVHSLLMAGDddddhdhkahaaesnvEKSEKSATHNVTNGAETGSEEHHDHDHGQYNLHIWLSPAIA 177
Cdd:COG4531   81 aPDAKVVELLELPGLTLLPFREG----------------GDFEHHDHHDEHHHHHHHHDDHHDHHHGGYDPHLWLSPENA 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748797196 178 KQIAIAIHDKLLLQSPQNKDKLDVNLRKFEEQLEQTEKNVGMMLRPVQGKGYFVFHDAYGYFEKTFGLTPLGHFTVNPEI 257
Cdd:COG4531  145 KAWAAAIADALSELDPENAATYQANAAAFEARLDALDAEIAAQLAPVKGKPFFVFHDAYQYFEKRFGLNALGAITLNPEI 224
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 748797196 258 QPGAQRLHQIRTQLVEQKAVCVFAEPQFRPAVISAVAQGTKVRQGTLDPLGSAIALGADSYMRFLTQLSQQYSSCL 333
Cdd:COG4531  225 QPGAKRLAEIREKLKELGAVCVFAEPQFNPALVETVAEGTGVRTGVLDPLGADLEPGPDLYFQLLRQLADSLASCL 300
ZnuA cd01019
Zinc binding protein ZnuA. These proteins have been shown to function as initial receptors in ...
26-333 1.38e-114

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: 333.57  E-value: 1.38e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748797196  26 AQAAVLTSIRPLGFIASAIADGVTTTEVLLPDGASPHDYALKPSDIKRLREADLVVWVGPEMEAFLTKPVQQLENNKNLM 105
Cdd:cd01019    2 AEASVLTSIKPLGFIAAAIMGGVGEVEVLVPPGASPHDYELRPSDARKLQEADLVVWIGPDLEAFLDKVLQGRKKGKVLT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748797196 106 LTGLPAVHSLLMAGDddddhdhkahaaESNVEKSEKSATHnvtngaetgseEHHDHDHGQYNLHIWLSPAIAKQIAIAIH 185
Cdd:cd01019   82 LAKLIDLKTLEDGAS------------HGDHEHDHEHAHG-----------EHDGHEEGGLDPHLWLSPENAAEVAQAVA 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748797196 186 DKLLLQSPQNKDKLDVNLRKFEEQLEQTEKNVGMMLRPVQGKGYFVFHDAYGYFEKTFGLTPLGHFTVNPEIQPGAQRLH 265
Cdd:cd01019  139 EKLSALDPDNAATYAANLEAFNARLAELDATIKERLAPVKTKPFFVFHDAYGYFEKRYGLTQAGVFTIDPEIDPGAKRLA 218
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 748797196 266 QIRTQLVEQKAVCVFAEPQFRPAVISAVAQGTKVRQGTLDPLGSAIALGADSYMRFLTQLSQQYSSCL 333
Cdd:cd01019  219 KIRKEIKEKGATCVFAEPQFHPKIAETLAEGTGAKVGELDPLGGLIELGKNSYVNFLRNLADSLASCL 286
ZnuA pfam01297
Zinc-uptake complex component A periplasmic; ZnuA includes periplasmic solute binding proteins ...
30-332 1.18e-67

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: 213.18  E-value: 1.18e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748797196   30 VLTSIRPLGFIASAIADGVTTTEVLLPDGASPHDYALKPSDIKRLREADLVVWVGPEMEAFLTKPVQQLENNKNLMLT-G 108
Cdd:pfam01297   1 VVATTYPLADLAKQIGGDRVEVTSLVPPGADPHDYEPTPSDIAALSDADLVVYNGLGLEPWLDKLLEALPNKKVVDASeG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748797196  109 LPAVHSllmagdddddhdhkahaaesnvekseksathnvtngaETGSEEHHDHDHGqYNLHIWLSPAIAKQIAIAIHDKL 188
Cdd:pfam01297  81 VELLDE-------------------------------------EGEEEDHDGHDHG-YDPHVWLDPKNAKKMAENIADAL 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748797196  189 LLQSPQNKDKLDVNLRKFEEQLEQTEKNVGMMLRPVQGKG--YFVFHDAYGYFEKTFGLTPLGHFTVNPEIQPGAQRLHQ 266
Cdd:pfam01297 123 SELDPANAATYEANAAAYLAELDALDAEIKEQLASIPEKTrkLVTSHDAFGYLARAYGLEQVGIQGVSPESEPSAADLAE 202
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 748797196  267 IRTQLVEQKAVCVFAEPQFRPAVISAVAQGTKVR-QGTLDPLGSAIALGADSYMRFLTQLSQQYSSC 332
Cdd:pfam01297 203 LIDLIKEKKVKAIFVEPQVSPKLAETVAKETGVKvLGPLYTDSLGEPGGGATYLDLMRHNLDTLAEA 269
anch_rpt_subst TIGR03772
anchored repeat ABC transporter, substrate-binding protein; Members of this protein family are ...
161-308 8.65e-10

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: 59.49  E-value: 8.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748797196  161 HDHGQYNLHIWLSPAIAKQIAIAIHDKLLLQSPQNKDKLDVNLRKFEEQLEQTEKNVGMMLR--PVQGKGYFVFHDAYGY 238
Cdd:TIGR03772 304 HVHGEIDPHLWHNVKNAIAYVEVIRDKLIEVDPRGAQAYRSNASAYIHRLERLDTYVRRTIAtiPPSRRHLITTHDAYSY 383
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748797196  239 FEKTFGLTPLGHFTVNPEIQPGAQRLHQIRTQLVEQKAVCVFAEPQfrpavisaVAQGTKVRQGTLDPLG 308
Cdd:TIGR03772 384 LGQAYGLNIAGFVTPNPAVEPSLADRRRLTRTIENLKVPAVFLEPN--------LAARSTTLNEIADELG 445
 
Name Accession Description Interval E-value
znuA PRK09545
zinc ABC transporter substrate-binding protein ZnuA;
2-334 0e+00

zinc ABC transporter substrate-binding protein ZnuA;


Pssm-ID: 236558 [Multi-domain]  Cd Length: 311  Bit Score: 548.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748797196   2 IHKKAWFKRTIIAAALVTSAgiSCAQAAVLTSIRPLGFIASAIADGVTTTEVLLPDGASPHDYALKPSDIKRLREADLVV 81
Cdd:PRK09545   1 LHKKTLLFAALLAALLGGAT--QAANAAVVTSIKPLGFIASAIADGVTETEVLLPDGASPHDYSLRPSDVKRLQSADLVV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748797196  82 WVGPEMEAFLTKPVQQLENNKNLMLTGLPAVHSLLMagdddddhdhkahaaesnveKSEKSATHNVTNGAETGSEEHHDH 161
Cdd:PRK09545  79 WVGPEMEAFLEKPVSKLPENKQVTIAQLPDVKPLLM--------------------KGAHDDHHDDDHDHAGHEKSDEDH 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748797196 162 DHGQYNLHIWLSPAIAKQIAIAIHDKLLLQSPQNKDKLDVNLRKFEEQLEQTEKNVGMMLRPVQGKGYFVFHDAYGYFEK 241
Cdd:PRK09545 139 HHGEYNMHIWLSPEIARATAVAIHDKLVELMPQSKAKLDANLKDFEAQLAQTDKQIGNQLAPVKGKGYFVFHDAYGYFEK 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748797196 242 TFGLTPLGHFTVNPEIQPGAQRLHQIRTQLVEQKAVCVFAEPQFRPAVISAVAQGTKVRQGTLDPLGSAIALGADSYMRF 321
Cdd:PRK09545 219 HYGLTPLGHFTVNPEIQPGAQRLHEIRTQLVEQKATCVFAEPQFRPAVIESVAKGTSVRMGTLDPLGTNIKLGKDSYSEF 298
                        330
                 ....*....|...
gi 748797196 322 LTQLSQQYSSCLN 334
Cdd:PRK09545 299 LSQLANQYASCLK 311
ZnuA COG4531
ABC-type Zn2+ transport system, periplasmic component/surface adhesin ZnuA [Inorganic ion ...
19-333 1.10e-155

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: 438.11  E-value: 1.10e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748797196  19 TSAGISCAQAAVLTSIRPLGFIASAIADGVTTTEVLLPDGASPHDYALKPSDIKRLREADLVVWVGPEMEAFLTKPVQQL 98
Cdd:COG4531    1 LASAAAAAAPRVVTSIKPLHSLVAAVMDGVGEPELLLPPGASPHDYALRPSDARALQDADLVFWVGPDLEPFLEKPLETL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748797196  99 -ENNKNLMLTGLPAVHSLLMAGDddddhdhkahaaesnvEKSEKSATHNVTNGAETGSEEHHDHDHGQYNLHIWLSPAIA 177
Cdd:COG4531   81 aPDAKVVELLELPGLTLLPFREG----------------GDFEHHDHHDEHHHHHHHHDDHHDHHHGGYDPHLWLSPENA 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748797196 178 KQIAIAIHDKLLLQSPQNKDKLDVNLRKFEEQLEQTEKNVGMMLRPVQGKGYFVFHDAYGYFEKTFGLTPLGHFTVNPEI 257
Cdd:COG4531  145 KAWAAAIADALSELDPENAATYQANAAAFEARLDALDAEIAAQLAPVKGKPFFVFHDAYQYFEKRFGLNALGAITLNPEI 224
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 748797196 258 QPGAQRLHQIRTQLVEQKAVCVFAEPQFRPAVISAVAQGTKVRQGTLDPLGSAIALGADSYMRFLTQLSQQYSSCL 333
Cdd:COG4531  225 QPGAKRLAEIREKLKELGAVCVFAEPQFNPALVETVAEGTGVRTGVLDPLGADLEPGPDLYFQLLRQLADSLASCL 300
ZnuA cd01019
Zinc binding protein ZnuA. These proteins have been shown to function as initial receptors in ...
26-333 1.38e-114

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: 333.57  E-value: 1.38e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748797196  26 AQAAVLTSIRPLGFIASAIADGVTTTEVLLPDGASPHDYALKPSDIKRLREADLVVWVGPEMEAFLTKPVQQLENNKNLM 105
Cdd:cd01019    2 AEASVLTSIKPLGFIAAAIMGGVGEVEVLVPPGASPHDYELRPSDARKLQEADLVVWIGPDLEAFLDKVLQGRKKGKVLT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748797196 106 LTGLPAVHSLLMAGDddddhdhkahaaESNVEKSEKSATHnvtngaetgseEHHDHDHGQYNLHIWLSPAIAKQIAIAIH 185
Cdd:cd01019   82 LAKLIDLKTLEDGAS------------HGDHEHDHEHAHG-----------EHDGHEEGGLDPHLWLSPENAAEVAQAVA 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748797196 186 DKLLLQSPQNKDKLDVNLRKFEEQLEQTEKNVGMMLRPVQGKGYFVFHDAYGYFEKTFGLTPLGHFTVNPEIQPGAQRLH 265
Cdd:cd01019  139 EKLSALDPDNAATYAANLEAFNARLAELDATIKERLAPVKTKPFFVFHDAYGYFEKRYGLTQAGVFTIDPEIDPGAKRLA 218
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 748797196 266 QIRTQLVEQKAVCVFAEPQFRPAVISAVAQGTKVRQGTLDPLGSAIALGADSYMRFLTQLSQQYSSCL 333
Cdd:cd01019  219 KIRKEIKEKGATCVFAEPQFHPKIAETLAEGTGAKVGELDPLGGLIELGKNSYVNFLRNLADSLASCL 286
ZnuA pfam01297
Zinc-uptake complex component A periplasmic; ZnuA includes periplasmic solute binding proteins ...
30-332 1.18e-67

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: 213.18  E-value: 1.18e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748797196   30 VLTSIRPLGFIASAIADGVTTTEVLLPDGASPHDYALKPSDIKRLREADLVVWVGPEMEAFLTKPVQQLENNKNLMLT-G 108
Cdd:pfam01297   1 VVATTYPLADLAKQIGGDRVEVTSLVPPGADPHDYEPTPSDIAALSDADLVVYNGLGLEPWLDKLLEALPNKKVVDASeG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748797196  109 LPAVHSllmagdddddhdhkahaaesnvekseksathnvtngaETGSEEHHDHDHGqYNLHIWLSPAIAKQIAIAIHDKL 188
Cdd:pfam01297  81 VELLDE-------------------------------------EGEEEDHDGHDHG-YDPHVWLDPKNAKKMAENIADAL 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748797196  189 LLQSPQNKDKLDVNLRKFEEQLEQTEKNVGMMLRPVQGKG--YFVFHDAYGYFEKTFGLTPLGHFTVNPEIQPGAQRLHQ 266
Cdd:pfam01297 123 SELDPANAATYEANAAAYLAELDALDAEIKEQLASIPEKTrkLVTSHDAFGYLARAYGLEQVGIQGVSPESEPSAADLAE 202
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 748797196  267 IRTQLVEQKAVCVFAEPQFRPAVISAVAQGTKVR-QGTLDPLGSAIALGADSYMRFLTQLSQQYSSC 332
Cdd:pfam01297 203 LIDLIKEKKVKAIFVEPQVSPKLAETVAKETGVKvLGPLYTDSLGEPGGGATYLDLMRHNLDTLAEA 269
ZnuA COG0803
ABC-type Zn uptake system ZnuABC, Zn-binding component ZnuA [Inorganic ion transport and ...
9-318 1.26e-52

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: 175.05  E-value: 1.26e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748797196   9 KRTIIAAALVTSAGIS-CAQAA--------VLTSIRPLGFIASAIA-DGVTTTeVLLPDGASPHDYALKPSDIKRLREAD 78
Cdd:COG0803    2 KRLLLALLLLAALLLAgCSAAAssaagklkVVATFSPLADLAKQIGgDKVEVT-SLVPPGADPHDYEPTPSDIAKLAKAD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748797196  79 LVVWVGPEMEAFLTKPVQQLENNKnlmltgLPAVhsllmagdddddhdhkahaaesnvekseksathNVTNGAETgSEEH 158
Cdd:COG0803   81 LVVYNGLGLEGWLDKLLEAAGNPG------VPVV---------------------------------DASEGIDL-LELE 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748797196 159 HDHDHGQYNLHIWLSPAIAKQIAIAIHDKLLLQSPQNKDKLDVNLRKFEEQLEQTEKNVGMMLRPVQGKGYFVFHDAYGY 238
Cdd:COG0803  121 EGHDHGEPDPHVWLDPKNAKKVAENIADALAELDPANAAYYEANAAAYLAELDALDAEIKAKLAAIPGRKLVTSHDAFGY 200
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748797196 239 FEKTFGLTPLGHFTVNPEIQPGAQRLHQIRTQLVEQKAVCVFAEPQFRPAVISAVAQGTKVRQGTLDPLGSAIAlGADSY 318
Cdd:COG0803  201 LARAYGLEVVAIQGISPGSEPSPADLAELIDLIKEEGVKAIFVESQVSPKLAETLAEETGVKVLYLDSLGGPGG-PGDTY 279
ZntC cd01018
Metal binding protein ZntC. These proteins are predicted to function as initial receptors in ...
30-309 2.81e-36

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: 131.71  E-value: 2.81e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748797196  30 VLTSIRPLGFIASAIADGVTTTEVLLPDGASPHDYALKPSDIKRLREADLVVWVGPEME-AFLTKPVQqleNNKNLMLTG 108
Cdd:cd01018    5 VAVSIEPQKYFVEKIAGDTVDVVVLVPPGSNPHTYEPKPQQMKKLSEADLYFRIGLGFEeVWLERFRS---NNPKMQVVN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748797196 109 LPAvhsllmagdddddhdhkahaaesNVEKSEKSATHNVTNGaetgseEHHDHDHGQYNLHIWLSPAIAKQIAIAIHDKL 188
Cdd:cd01018   82 MSK-----------------------GITLIPMADHHHHHHG------EHEHHHHGNYDPHIWLSPANAKIMAENIYEAL 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748797196 189 LLQSPQNKDKLDVNLRKFEEQLEQTEKNVGMMLRPVQGKGYFVFHDAYGYFEKTFGLTplghfTVNPEIQ---PGAQRLH 265
Cdd:cd01018  133 AELDPQNATYYQANLDALLAELDALDSEIRTILSKLKQRAFMVYHPAWGYFARDYGLT-----QIPIEEEgkePSPADLK 207
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 748797196 266 QIRTQLVEQKAVCVFAEPQFRPAVISAVAQGTKVRQGTLDPLGS 309
Cdd:cd01018  208 RLIDLAKEKGVRVVFVQPQFSTKSAEAIAREIGAKVVTIDPLAA 251
AdcA cd01017
Metal binding protein AdcA. These proteins have been shown to function in the ABC uptake of ...
30-319 2.42e-33

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: 124.33  E-value: 2.42e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748797196  30 VLTSIRPLGFIASAIADGVTTTEVLLPDGASPHDYALKPSDIKRLREADLVVWVGPEMEAFLTKPVQQLEnNKNLMLtgl 109
Cdd:cd01017    6 VVTTFYPLYEFTKAIGGDKADVKLIIPAGTEPHDFEPSPKDIARIADADVFVYNGLGMETWAEKVLKSLQ-NKKLKV--- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748797196 110 pavhsllmagdddddhdhkahaaesnVEKSEKSATHNVTnGAETGSEEHHDHDHGQYNLHIWLSPAIAKQIAIAIHDKLL 189
Cdd:cd01017   82 --------------------------VEASKGIKLLKAG-GAEHDHDHSHSHHHGDYDPHVWLSPVLAIQQVENIKDALI 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748797196 190 LQSPQNKDKLDVNLRKFEEQLEQTEKNVGMMLRPVQGKGYFVFHDAYGYFEKTFGLTPLGHFTVNPEIQPGAQRLHQIRT 269
Cdd:cd01017  135 KLDPDNKEYYEKNAAAYAKKLEALDQEYRAKLAKAKGKTFVTQHAAFGYLARRYGLKQIAIVGVSPEVEPSPKQLAELVE 214
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 748797196 270 QLVEQKAVCVFAEPQFRPAVISAVAQGTKVRQGTLDPLGS---AIALGADSYM 319
Cdd:cd01017  215 FVKKSDVKYIFFEENASSKIAETLAKETGAKLLVLNPLETltkEEIDDGKDYF 267
PsaA cd01137
Metal binding protein PsaA. These proteins have been shown to function as initial receptors ...
12-302 9.98e-21

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: 90.41  E-value: 9.98e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748797196  12 IIAAALVTSAGISCAQAAVLTSIRPLGFIASAIADGVTTTEVLLPDGASPHDYALKPSDIKRLREADLVVWVGPEMEAFL 91
Cdd:cd01137    2 AACASLGSSPATAASKLKVVATFSILADIARNIAGDRVNVTSIVPPGADPHEYEPTPSDIKKLSKADLILYNGLNLEPWL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748797196  92 TKPVQQLENNKnlmltglPAVhsllmagdddddhdhkahaaesnvekseksathNVTNGAETGSEEHHdHDHGQYNLHIW 171
Cdd:cd01137   82 ERLVKNAGKDV-------PVV---------------------------------AVSEGIDPIPLEEG-HYKGKPDPHAW 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748797196 172 LSPAIAKQIAIAIHDKLLLQSPQNKDKLDVNLRKFEEQLEQTEKNVGMMLRPV-QGKGYFVF-HDAYGYFEKTFGLTPLG 249
Cdd:cd01137  121 MSPKNAIIYVKNIAKALSEADPANAETYQKNAAAYKAKLKALDEWAKAKFATIpAEKRKLVTsEGAFSYFAKAYGLKEAY 200
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 748797196 250 HFTVNPEIQPGAQRLHQIRTQLVEQKAVCVFAEPQFRPAVISAVAQGTKVRQG 302
Cdd:cd01137  201 LWPINTEEEGTPKQVATLIEQVKKEKVPAVFVESTVNDRLMKQVAKETGAKIG 253
TroA_c cd01145
Periplasmic binding protein TroA_c. These proteins are predicted to function as initial ...
26-263 7.39e-16

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: 74.84  E-value: 7.39e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748797196  26 AQAAVLTSIRPLGFIASAIADGVTTTEVLLPDGASPHDYALKPSDIKRLREADLVVWVGPEMEAFLTKpVQQLENNknlm 105
Cdd:cd01145    1 AALNVVVTFPDLKDLVREVAGDAVIVSALTPPGVDPHQYQLKPSDIAKMRKADLVVTSGHELEGFEPK-LAELSSN---- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748797196 106 ltglpavhsllmagdddddhdhkahaaeSNVEKSEKSATHNVTNGAETGSEEHHDHDHGqyNLHIWLSPAIAKQIAIAIH 185
Cdd:cd01145   76 ----------------------------SKVQPGIKILIEDSDTVGMVDRAMGDYHGKG--NPHVWLDPNNAPALAKALA 125
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 748797196 186 DKLLLQSPQNKDKLDVNLRKFEEQLEQTEKNVGMMLRPVQGKGYFVFHDAYGYFEKTFGLTPLGHFTVNPEIQPGAQR 263
Cdd:cd01145  126 DALIELDPSEQEEYKENLRVFLAKLNKLLREWERQFEGLKGIQVVAYHPSYQYLADWLGIEVVASLEPLPELPPTSSH 203
TroA cd01016
Metal binding protein TroA. These proteins have been shown to function as initial receptors in ...
30-310 4.31e-12

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: 65.46  E-value: 4.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748797196  30 VLTSIRPLGFIASAIADGVTTTEVLLPDGASPHDYALKPSDIKRLREADLVVWVGPEMEAFLTKPVQQLENNKNLMLtgl 109
Cdd:cd01016    4 VVTTTGMIADAVENIGGDHVEVTGLMGPGVDPHLYKATAGDVEKLQNADVVFYNGLHLEGKMSDVLSKLGSSKSVIA--- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748797196 110 pavhsllmagdddddhdhkahaAESNVEKSEKSathnvtngaetgseehHDHDHGQYNLHIWLSPAIAKQIAIAIHDKLL 189
Cdd:cd01016   81 ----------------------LEDTLDRSQLI----------------LDEEEGTYDPHIWFDVKLWKYAVKAVAEVLS 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748797196 190 LQSPQNKDKLDVNLRKFEEQLEQTEKNVGMMLR--PVQGKGYFVFHDAYGYFEKTFGLTPLGHFTVNPEIQPGAQRLHQI 267
Cdd:cd01016  123 EKLPEHKDEFQANSEAYVEELDSLDAYAKKKIAeiPEQQRVLVTAHDAFGYFGRAYGFEVKGLQGISTDSEAGLRDINEL 202
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 748797196 268 RTQLVEQKAVCVFAEPQFRPAVISAVAQGTKVR------QGTL--DPLGSA 310
Cdd:cd01016  203 VDLIVERKIKAIFVESSVNQKSIEALQDAVKARghdvqiGGELysDAMGEE 253
anch_rpt_subst TIGR03772
anchored repeat ABC transporter, substrate-binding protein; Members of this protein family are ...
161-308 8.65e-10

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: 59.49  E-value: 8.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748797196  161 HDHGQYNLHIWLSPAIAKQIAIAIHDKLLLQSPQNKDKLDVNLRKFEEQLEQTEKNVGMMLR--PVQGKGYFVFHDAYGY 238
Cdd:TIGR03772 304 HVHGEIDPHLWHNVKNAIAYVEVIRDKLIEVDPRGAQAYRSNASAYIHRLERLDTYVRRTIAtiPPSRRHLITTHDAYSY 383
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748797196  239 FEKTFGLTPLGHFTVNPEIQPGAQRLHQIRTQLVEQKAVCVFAEPQfrpavisaVAQGTKVRQGTLDPLG 308
Cdd:TIGR03772 384 LGQAYGLNIAGFVTPNPAVEPSLADRRRLTRTIENLKVPAVFLEPN--------LAARSTTLNEIADELG 445
TroA_b cd01020
Metal binding protein TroA_b. These proteins are predicted to function as initial receptors ...
29-284 1.20e-07

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: 52.06  E-value: 1.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748797196  29 AVLTSIRPLGFIASAIA-DGVTTTEVLLPDGASPHDYALKPSDIKRLREADLVVWVGPEMEAFLTKpvqQLENNKNLMLT 107
Cdd:cd01020    4 NVVASTNFWGSVAEAVGgDHVEVTSIITNPDVDPHDFEPTPTDAAKVSTADIVVYNGGGYDPWMTK---LLADTKDVIVI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748797196 108 GLpavhsllmagdddddhdhkahaaesnvekseksathnvtngaetGSEEHHDHDHGqyNLHIWLSPAIAKQIAIAIHDK 187
Cdd:cd01020   81 AA--------------------------------------------DLDGHDDKEGD--NPHLWYDPETMSKVANALADA 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748797196 188 LLLQSPQNKDKLDVNLRKFEEQLEQTEKNVGMMLRPVQGKGYF----VFH---DAYGYFEKTfglTPLGHFTVNPEIQPG 260
Cdd:cd01020  115 LVKADPDNKKYYQANAKKFVASLKPLAAKIAELSAKYKGAPVAatepVFDyllDALGMKERT---PKGYTATTESETEPS 191
                        250       260
                 ....*....|....*....|....
gi 748797196 261 AQRLHQIRTQLVEQKAVCVFAEPQ 284
Cdd:cd01020  192 PADIAAFQNAIKNRQIDALIVNPQ 215
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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