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Conserved domains on  [gi|2739772249|ref|WP_348657704|]
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metal ABC transporter solute-binding protein, Zn/Mn family, partial [uncultured Sulfitobacter sp.]

Protein Classification

zinc ABC transporter substrate-binding protein( domain architecture ID 10790679)

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 COG4531
ABC-type Zn2+ transport system, periplasmic component/surface adhesin ZnuA [Inorganic ion ...
 1-194 1.90e-82

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: 246.28  E-value: 1.90e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739772249   1 DAGHDAPAPDEGHDDHGHDEAHAHSGVDPHVWLDPQNGQLWLGQIAEALAELDPDNAAQYRENAAAAQAELAALEEDIAE 80
Cdd:COG4531   107 EHHDHHDEHHHHHHHHDDHHDHHHGGYDPHLWLSPENAKAWAAAIADALSELDPENAATYQANAAAFEARLDALDAEIAA 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739772249  81 TLAPVKSRPFIVFHDAYHYFEARFDIEARGAISENDARAPGAARVSELRDLVAESGAKCVFAEPQFNPGLIAAVTEGQGT 160
Cdd:COG4531   187 QLAPVKGKPFFVFHDAYQYFEKRFGLNALGAITLNPEIQPGAKRLAEIREKLKELGAVCVFAEPQFNPALVETVAEGTGV 266

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2739772249 161 GTGTLDPLGADLEPGAALYADLLRGMAENMAACL 194
Cdd:COG4531   267 RTGVLDPLGADLEPGPDLYFQLLRQLADSLASCL 300
 
Name Accession Description Interval E-value
ZnuA COG4531
ABC-type Zn2+ transport system, periplasmic component/surface adhesin ZnuA [Inorganic ion ...
 1-194 1.90e-82

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: 246.28  E-value: 1.90e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739772249   1 DAGHDAPAPDEGHDDHGHDEAHAHSGVDPHVWLDPQNGQLWLGQIAEALAELDPDNAAQYRENAAAAQAELAALEEDIAE 80
Cdd:COG4531   107 EHHDHHDEHHHHHHHHDDHHDHHHGGYDPHLWLSPENAKAWAAAIADALSELDPENAATYQANAAAFEARLDALDAEIAA 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739772249  81 TLAPVKSRPFIVFHDAYHYFEARFDIEARGAISENDARAPGAARVSELRDLVAESGAKCVFAEPQFNPGLIAAVTEGQGT 160
Cdd:COG4531   187 QLAPVKGKPFFVFHDAYQYFEKRFGLNALGAITLNPEIQPGAKRLAEIREKLKELGAVCVFAEPQFNPALVETVAEGTGV 266

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2739772249 161 GTGTLDPLGADLEPGAALYADLLRGMAENMAACL 194
Cdd:COG4531   267 RTGVLDPLGADLEPGPDLYFQLLRQLADSLASCL 300
ZnuA cd01019
Zinc binding protein ZnuA. These proteins have been shown to function as initial receptors in ...
 4-194 1.44e-56

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: 179.87  E-value: 1.44e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739772249   4 HDAPAPDEGHDD---HGHDEAHAHSGVDPHVWLDPQNGQLWLGQIAEALAELDPDNAAQYRENAAAAQAELAALEEDIAE 80
Cdd:cd01019    93 DGASHGDHEHDHehaHGEHDGHEEGGLDPHLWLSPENAAEVAQAVAEKLSALDPDNAATYAANLEAFNARLAELDATIKE 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739772249  81 TLAPVKSRPFIVFHDAYHYFEARFDIEARGAISENDARAPGAARVSELRDLVAESGAKCVFAEPQFNPGLIAAVTEGQGT 160
Cdd:cd01019   173 RLAPVKTKPFFVFHDAYGYFEKRYGLTQAGVFTIDPEIDPGAKRLAKIRKEIKEKGATCVFAEPQFHPKIAETLAEGTGA 252

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2739772249 161 GTGTLDPLGADLEPGAALYADLLRGMAENMAACL 194
Cdd:cd01019   253 KVGELDPLGGLIELGKNSYVNFLRNLADSLASCL 286
ZnuA pfam01297
Zinc-uptake complex component A periplasmic; ZnuA includes periplasmic solute binding proteins ...
 1-193 4.38e-46

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: 152.71  E-value: 4.38e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739772249   1 DAGHDAPAPDEGHDDHGHDEaHAHsGVDPHVWLDPQNGQLWLGQIAEALAELDPDNAAQYRENAAAAQAELAALEEDIAE 80
Cdd:pfam01297  76 DASEGVELLDEEGEEEDHDG-HDH-GYDPHVWLDPKNAKKMAENIADALSELDPANAATYEANAAAYLAELDALDAEIKE 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739772249  81 TLA--PVKSRPFIVFHDAYHYFEARFDIEARGAISENDARAPGAARVSELRDLVAESGAKCVFAEPQFNPGLIAAVTEGQ 158
Cdd:pfam01297 154 QLAsiPEKTRKLVTSHDAFGYLARAYGLEQVGIQGVSPESEPSAADLAELIDLIKEKKVKAIFVEPQVSPKLAETVAKET 233

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2739772249 159 -GTGTGTLDPLGADLEPGAALYADLLRGMAENMAAC 193
Cdd:pfam01297 234 gVKVLGPLYTDSLGEPGGGATYLDLMRHNLDTLAEA 269
znuA PRK09545
zinc ABC transporter substrate-binding protein ZnuA;
9-194 1.79e-40

zinc ABC transporter substrate-binding protein ZnuA;


Pssm-ID: 236558 [Multi-domain]  Cd Length: 311  Bit Score: 139.37  E-value: 1.79e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739772249   9 PDEGHDDHGH------DEAHAHSGVDPHVWLDPQNGQLWLGQIAEALAELDPDNAAQYRENAAAAQAELAALEEDIAETL 82
Cdd:PRK09545  119 DDHHDDDHDHagheksDEDHHHGEYNMHIWLSPEIARATAVAIHDKLVELMPQSKAKLDANLKDFEAQLAQTDKQIGNQL 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739772249  83 APVKSRPFIVFHDAYHYFEARFDIEARGAISENDARAPGAARVSELRDLVAESGAKCVFAEPQFNPGLIAAVTEGQGTGT 162
Cdd:PRK09545  199 APVKGKGYFVFHDAYGYFEKHYGLTPLGHFTVNPEIQPGAQRLHEIRTQLVEQKATCVFAEPQFRPAVIESVAKGTSVRM 278

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2739772249 163 GTLDPLGADLEPGAALYADLLRGMAENMAACL 194
Cdd:PRK09545  279 GTLDPLGTNIKLGKDSYSEFLSQLANQYASCL 310
Zn_bnd_ABC_AdcA NF033605
zinc ABC transporter substrate-binding lipoprotein AdcA;
1-143 2.39e-14

zinc ABC transporter substrate-binding lipoprotein AdcA;


Pssm-ID: 468109 [Multi-domain]  Cd Length: 516  Bit Score: 70.57  E-value: 2.39e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739772249   1 DAGHDAPAPDEGHDDHGHDEAHAHSGVDPHVWLDPQNGQLWLGQIAEALAELDPDNAAQYRENAAAAQAELAALEEDIAE 80
Cdd:NF033605  125 DQHEHGEEHEHEEEGHEHEHHHHHGGYDPHVWLDPKFDQTFAKEIKDELVKKDPKHKDEYEKNYKKLNKDLKGIDKDMKD 204

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2739772249  81 TLAPVKSRPFIVFHDAYHYFEARFDIEARGAISENdARAPGAARVSELRDLVAESGAKCVFAE 143
Cdd:NF033605  205 ITKDKQGNAVFISHESLGYLADRYGFVQKGVQNMN-AEDPSQKELTEIVKEINDSGAKYILYE 266
anch_rpt_subst TIGR03772
anchored repeat ABC transporter, substrate-binding protein; Members of this protein family are ...
 21-195 4.73e-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: 69.51  E-value: 4.73e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739772249  21 AHAHSGVDPHVWLDPQNGQLWLGQIAEALAELDPDNAAQYRENAAAAQAELAALEEDIAETLA--PVKSRPFIVFHDAYH 98
Cdd:TIGR03772 303 KHVHGEIDPHLWHNVKNAIAYVEVIRDKLIEVDPRGAQAYRSNASAYIHRLERLDTYVRRTIAtiPPSRRHLITTHDAYS 382

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739772249  99 YFEARFDIEARGAISENDARAPGAARVSELRDLVAESGAKCVFAEPQFNPGLIAAVTEGQGTGTGTLDPLGADLEPGAAL 178
Cdd:TIGR03772 383 YLGQAYGLNIAGFVTPNPAVEPSLADRRRLTRTIENLKVPAVFLEPNLAARSTTLNEIADELGVRVCAIYGDTFDDDVTN 462

                         170
                  ....*....|....*..
gi 2739772249 179 YADLLRGMAENMAACLS 195
Cdd:TIGR03772 463 YVDLMRFNADSLADCLG 479
 
Name Accession Description Interval E-value
ZnuA COG4531
ABC-type Zn2+ transport system, periplasmic component/surface adhesin ZnuA [Inorganic ion ...
 1-194 1.90e-82

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: 246.28  E-value: 1.90e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739772249   1 DAGHDAPAPDEGHDDHGHDEAHAHSGVDPHVWLDPQNGQLWLGQIAEALAELDPDNAAQYRENAAAAQAELAALEEDIAE 80
Cdd:COG4531   107 EHHDHHDEHHHHHHHHDDHHDHHHGGYDPHLWLSPENAKAWAAAIADALSELDPENAATYQANAAAFEARLDALDAEIAA 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739772249  81 TLAPVKSRPFIVFHDAYHYFEARFDIEARGAISENDARAPGAARVSELRDLVAESGAKCVFAEPQFNPGLIAAVTEGQGT 160
Cdd:COG4531   187 QLAPVKGKPFFVFHDAYQYFEKRFGLNALGAITLNPEIQPGAKRLAEIREKLKELGAVCVFAEPQFNPALVETVAEGTGV 266

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2739772249 161 GTGTLDPLGADLEPGAALYADLLRGMAENMAACL 194
Cdd:COG4531   267 RTGVLDPLGADLEPGPDLYFQLLRQLADSLASCL 300
ZnuA cd01019
Zinc binding protein ZnuA. These proteins have been shown to function as initial receptors in ...
 4-194 1.44e-56

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: 179.87  E-value: 1.44e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739772249   4 HDAPAPDEGHDD---HGHDEAHAHSGVDPHVWLDPQNGQLWLGQIAEALAELDPDNAAQYRENAAAAQAELAALEEDIAE 80
Cdd:cd01019    93 DGASHGDHEHDHehaHGEHDGHEEGGLDPHLWLSPENAAEVAQAVAEKLSALDPDNAATYAANLEAFNARLAELDATIKE 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739772249  81 TLAPVKSRPFIVFHDAYHYFEARFDIEARGAISENDARAPGAARVSELRDLVAESGAKCVFAEPQFNPGLIAAVTEGQGT 160
Cdd:cd01019   173 RLAPVKTKPFFVFHDAYGYFEKRYGLTQAGVFTIDPEIDPGAKRLAKIRKEIKEKGATCVFAEPQFHPKIAETLAEGTGA 252

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2739772249 161 GTGTLDPLGADLEPGAALYADLLRGMAENMAACL 194
Cdd:cd01019   253 KVGELDPLGGLIELGKNSYVNFLRNLADSLASCL 286
ZnuA pfam01297
Zinc-uptake complex component A periplasmic; ZnuA includes periplasmic solute binding proteins ...
 1-193 4.38e-46

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: 152.71  E-value: 4.38e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739772249   1 DAGHDAPAPDEGHDDHGHDEaHAHsGVDPHVWLDPQNGQLWLGQIAEALAELDPDNAAQYRENAAAAQAELAALEEDIAE 80
Cdd:pfam01297  76 DASEGVELLDEEGEEEDHDG-HDH-GYDPHVWLDPKNAKKMAENIADALSELDPANAATYEANAAAYLAELDALDAEIKE 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739772249  81 TLA--PVKSRPFIVFHDAYHYFEARFDIEARGAISENDARAPGAARVSELRDLVAESGAKCVFAEPQFNPGLIAAVTEGQ 158
Cdd:pfam01297 154 QLAsiPEKTRKLVTSHDAFGYLARAYGLEQVGIQGVSPESEPSAADLAELIDLIKEKKVKAIFVEPQVSPKLAETVAKET 233

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2739772249 159 -GTGTGTLDPLGADLEPGAALYADLLRGMAENMAAC 193
Cdd:pfam01297 234 gVKVLGPLYTDSLGEPGGGATYLDLMRHNLDTLAEA 269
znuA PRK09545
zinc ABC transporter substrate-binding protein ZnuA;
9-194 1.79e-40

zinc ABC transporter substrate-binding protein ZnuA;


Pssm-ID: 236558 [Multi-domain]  Cd Length: 311  Bit Score: 139.37  E-value: 1.79e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739772249   9 PDEGHDDHGH------DEAHAHSGVDPHVWLDPQNGQLWLGQIAEALAELDPDNAAQYRENAAAAQAELAALEEDIAETL 82
Cdd:PRK09545  119 DDHHDDDHDHagheksDEDHHHGEYNMHIWLSPEIARATAVAIHDKLVELMPQSKAKLDANLKDFEAQLAQTDKQIGNQL 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739772249  83 APVKSRPFIVFHDAYHYFEARFDIEARGAISENDARAPGAARVSELRDLVAESGAKCVFAEPQFNPGLIAAVTEGQGTGT 162
Cdd:PRK09545  199 APVKGKGYFVFHDAYGYFEKHYGLTPLGHFTVNPEIQPGAQRLHEIRTQLVEQKATCVFAEPQFRPAVIESVAKGTSVRM 278

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2739772249 163 GTLDPLGADLEPGAALYADLLRGMAENMAACL 194
Cdd:PRK09545  279 GTLDPLGTNIKLGKDSYSEFLSQLANQYASCL 310
ZnuA COG0803
ABC-type Zn uptake system ZnuABC, Zn-binding component ZnuA [Inorganic ion transport and ...
 11-184 6.00e-37

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: 129.59  E-value: 6.00e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739772249  11 EGHDDHGHDEAHAHSGVDPHVWLDPQNGQLWLGQIAEALAELDPDNAAQYRENAAAAQAELAALEEDIAETLAPVKSRPF 90
Cdd:COG0803   112 EGIDLLELEEGHDHGEPDPHVWLDPKNAKKVAENIADALAELDPANAAYYEANAAAYLAELDALDAEIKAKLAAIPGRKL 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739772249  91 IVFHDAYHYFEARFDIEARGAISENDARAPGAARVSELRDLVAESGAKCVFAEPQFNPGLIAAVTEGQGTGTGTLDPLGA 170
Cdd:COG0803   192 VTSHDAFGYLARAYGLEVVAIQGISPGSEPSPADLAELIDLIKEEGVKAIFVESQVSPKLAETLAEETGVKVLYLDSLGG 271

                         170
                  ....*....|....
gi 2739772249 171 DLEPGAAlYADLLR 184
Cdd:COG0803   272 PGGPGDT-YLDMMR 284
AdcA cd01017
Metal binding protein AdcA. These proteins have been shown to function in the ABC uptake of ...
 2-148 1.70e-30

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: 112.77  E-value: 1.70e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739772249   2 AGHDAPAPDEGHDDHGHDEAHAHSGVDPHVWLDPQNGQLWLGQIAEALAELDPDNAAQYRENAAAAQAELAALEEDIAET 81
Cdd:cd01017    86 KGIKLLKAGGAEHDHDHSHSHHHGDYDPHVWLSPVLAIQQVENIKDALIKLDPDNKEYYEKNAAAYAKKLEALDQEYRAK 165

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2739772249  82 LAPVKSRPFIVFHDAYHYFEARFDIEARGAISENDARAPGAARVSELRDLVAESGAKCVFAEPQFNP 148
Cdd:cd01017   166 LAKAKGKTFVTQHAAFGYLARRYGLKQIAIVGVSPEVEPSPKQLAELVEFVKKSDVKYIFFEENASS 232
ZntC cd01018
Metal binding protein ZntC. These proteins are predicted to function as initial receptors in ...
 5-173 3.42e-30

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: 111.30  E-value: 3.42e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739772249   5 DAPAPDEGHDDHGHDEAHAHSGVDPHVWLDPQNGQLWLGQIAEALAELDPDNAAQYRENAAAAQAELAALEEDIAETLAP 84
Cdd:cd01018    88 LIPMADHHHHHHGEHEHHHHGNYDPHIWLSPANAKIMAENIYEALAELDPQNATYYQANLDALLAELDALDSEIRTILSK 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739772249  85 VKSRPFIVFHDAYHYFEARFDIEaRGAIsENDARAPGAARVSELRDLVAESGAKCVFAEPQFNPGLIAAVTEGQGTGTGT 164
Cdd:cd01018   168 LKQRAFMVYHPAWGYFARDYGLT-QIPI-EEEGKEPSPADLKRLIDLAKEKGVRVVFVQPQFSTKSAEAIAREIGAKVVT 245


                  ....*....
gi 2739772249 165 LDPLGADLE 173
Cdd:cd01018   246 IDPLAADWE 254
PsaA cd01137
Metal binding protein PsaA. These proteins have been shown to function as initial receptors ...
 19-195 2.77e-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: 88.49  E-value: 2.77e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739772249  19 DEAHAHSGVDPHVWLDPQNGQLWLGQIAEALAELDPDNAAQYRENAAAAQAELAALEEDIAETLA--PVKSRPFIVFHDA 96
Cdd:cd01137   107 EEGHYKGKPDPHAWMSPKNAIIYVKNIAKALSEADPANAETYQKNAAAYKAKLKALDEWAKAKFAtiPAEKRKLVTSEGA 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739772249  97 YHYFEARFDIEARGAISENDARAPGAARVSELRDLVAESGAKCVFAEPQFNPGLIAAVTEGQGTGTGTL---DPLGADLE 173
Cdd:cd01137   187 FSYFAKAYGLKEAYLWPINTEEEGTPKQVATLIEQVKKEKVPAVFVESTVNDRLMKQVAKETGAKIGGQlytDSLSEKGG 266

                         170       180
                  ....*....|....*....|..
gi 2739772249 174 PGAAlYADLLRGMAENMAACLS 195
Cdd:cd01137   267 PADT-YLDMMEHNLDTIVEGLG 287
Zn_bnd_ABC_AdcA NF033605
zinc ABC transporter substrate-binding lipoprotein AdcA;
1-143 2.39e-14

zinc ABC transporter substrate-binding lipoprotein AdcA;


Pssm-ID: 468109 [Multi-domain]  Cd Length: 516  Bit Score: 70.57  E-value: 2.39e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739772249   1 DAGHDAPAPDEGHDDHGHDEAHAHSGVDPHVWLDPQNGQLWLGQIAEALAELDPDNAAQYRENAAAAQAELAALEEDIAE 80
Cdd:NF033605  125 DQHEHGEEHEHEEEGHEHEHHHHHGGYDPHVWLDPKFDQTFAKEIKDELVKKDPKHKDEYEKNYKKLNKDLKGIDKDMKD 204

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2739772249  81 TLAPVKSRPFIVFHDAYHYFEARFDIEARGAISENdARAPGAARVSELRDLVAESGAKCVFAE 143
Cdd:NF033605  205 ITKDKQGNAVFISHESLGYLADRYGFVQKGVQNMN-AEDPSQKELTEIVKEINDSGAKYILYE 266
anch_rpt_subst TIGR03772
anchored repeat ABC transporter, substrate-binding protein; Members of this protein family are ...
 21-195 4.73e-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: 69.51  E-value: 4.73e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739772249  21 AHAHSGVDPHVWLDPQNGQLWLGQIAEALAELDPDNAAQYRENAAAAQAELAALEEDIAETLA--PVKSRPFIVFHDAYH 98
Cdd:TIGR03772 303 KHVHGEIDPHLWHNVKNAIAYVEVIRDKLIEVDPRGAQAYRSNASAYIHRLERLDTYVRRTIAtiPPSRRHLITTHDAYS 382

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739772249  99 YFEARFDIEARGAISENDARAPGAARVSELRDLVAESGAKCVFAEPQFNPGLIAAVTEGQGTGTGTLDPLGADLEPGAAL 178
Cdd:TIGR03772 383 YLGQAYGLNIAGFVTPNPAVEPSLADRRRLTRTIENLKVPAVFLEPNLAARSTTLNEIADELGVRVCAIYGDTFDDDVTN 462

                         170
                  ....*....|....*..
gi 2739772249 179 YADLLRGMAENMAACLS 195
Cdd:TIGR03772 463 YVDLMRFNADSLADCLG 479
TroA cd01016
Metal binding protein TroA. These proteins have been shown to function as initial receptors in ...
 26-181 6.91e-14

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: 68.16  E-value: 6.91e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739772249  26 GVDPHVWLDPqngQLW---LGQIAEALAELDPDNAAQYRENAAAAQAELAALEEDIAETLA--PVKSRPFIVFHDAYHYF 100
Cdd:cd01016    98 TYDPHIWFDV---KLWkyaVKAVAEVLSEKLPEHKDEFQANSEAYVEELDSLDAYAKKKIAeiPEQQRVLVTAHDAFGYF 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739772249 101 EARFDIEARG--AISeNDARApGAARVSELRDLVAESGAKCVFAEPQFNPGLIAAVTEGQGTGtgtldplGADLEPGAAL 178
Cdd:cd01016   175 GRAYGFEVKGlqGIS-TDSEA-GLRDINELVDLIVERKIKAIFVESSVNQKSIEALQDAVKAR-------GHDVQIGGEL 245


                  ...
gi 2739772249 179 YAD 181
Cdd:cd01016   246 YSD 248
TroA_c cd01145
Periplasmic binding protein TroA_c. These proteins are predicted to function as initial ...
 24-107 7.39e-09

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: 53.27  E-value: 7.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739772249  24 HSGVDPHVWLDPQNGQLWLGQIAEALAELDPDNAAQYRENAAAAQAELAALEEDIAETLAPVKSRPFIVFHDAYHYFEAR 103
Cdd:cd01145   103 HGKGNPHVWLDPNNAPALAKALADALIELDPSEQEEYKENLRVFLAKLNKLLREWERQFEGLKGIQVVAYHPSYQYLADW 182


                  ....
gi 2739772249 104 FDIE 107
Cdd:cd01145   183 LGIE 186
TroA_b cd01020
Metal binding protein TroA_b. These proteins are predicted to function as initial receptors ...
 17-145 6.16e-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: 48.20  E-value: 6.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2739772249  17 GHDEAHAHSGVDPHVWLDPQNGQLWLGQIAEALAELDPDNAAQYRENAAAAQAELAALEEDIAETLAPVKSRPFI----V 92
Cdd:cd01020    83 DLDGHDDKEGDNPHLWYDPETMSKVANALADALVKADPDNKKYYQANAKKFVASLKPLAAKIAELSAKYKGAPVAatepV 162

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2739772249  93 FH---DAYHYFEARFDIEARGAISENDaraPGAARVSELRDLVAESGAKCVFAEPQ 145
Cdd:cd01020   163 FDyllDALGMKERTPKGYTATTESETE---PSPADIAAFQNAIKNRQIDALIVNPQ 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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