NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1624566571|ref|WP_136409614|]
View 

metal ABC transporter solute-binding protein, Zn/Mn family [Muribaculum gordoncarteri]

Protein Classification

TroA family protein( domain architecture ID 513)

TroA family protein; most TroA-like proteins are encoded by ABC-type operons and appear to function as periplasmic components of ABC transporters in metal ion uptake.

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
TroA-like super family cl00262
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ...
 32-292 2.40e-95

Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function in the ABC transport of ferric siderophores and metal ions such as Mn2+, Fe3+, Cu2+ and/or Zn2+. Their ligand binding site is formed in the interface between two globular domains linked by a single helix. Many of these proteins also possess a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence). The TroA-like proteins differ in their fold and ligand-binding mechanism from the PBPI and PBPII proteins, but are structurally similar, however, to the beta-subunit of the nitrogenase molybdenum-iron protein MoFe. Most TroA-like proteins are encoded by ABC-type operons and appear to function as periplasmic components of ABC transporters in metal ion uptake.


The actual alignment was detected with superfamily member cd01018:

Pssm-ID: 469696 [Multi-domain]  Cd Length: 266  Bit Score: 281.94  E-value: 2.40e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566571  32 SKPTITVSIQPQKYMLEKIVGDKWEIKCLLSNGANPESYDPSLTHLLNLENSKAYFRIGnVAFESAIINKVQNNNPGLKL 111
Cdd:cd01018     1 DKPTVAVSIEPQKYFVEKIAGDTVDVVVLVPPGSNPHTYEPKPQQMKKLSEADLYFRIG-LGFEEVWLERFRSNNPKMQV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566571 112 FDNSEGISLI--RGTHSHGDVEHA----SDIDPHTWTSVKNAKTIASNMYKAVVDLDPENKAYYSRNFKNFLSSLDSLDR 185
Cdd:cd01018    80 VNMSKGITLIpmADHHHHHHGEHEhhhhGNYDPHIWLSPANAKIMAENIYEALAELDPQNATYYQANLDALLAELDALDS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566571 186 EISQQLQPYRGSAFVVWHPSLSYFARDYGLEQISLSPEGKEASVKMMQSTIDKAIVRDVKTLFFQKDIDSRQAQVANEQI 265
Cdd:cd01018   160 EIRTILSKLKQRAFMVYHPAWGYFARDYGLTQIPIEEEGKEPSPADLKRLIDLAKEKGVRVVFVQPQFSTKSAEAIAREI 239

                         250       260
                  ....*....|....*....|....*..
gi 1624566571 266 KAEIVNINPLNYEWDKEMRSIANAISR 292
Cdd:cd01018   240 GAKVVTIDPLAADWEENLLKVADAFAH 266
 
Name Accession Description Interval E-value
ZntC cd01018
Metal binding protein ZntC. These proteins are predicted to function as initial receptors in ...
 32-292 2.40e-95

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: 281.94  E-value: 2.40e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566571  32 SKPTITVSIQPQKYMLEKIVGDKWEIKCLLSNGANPESYDPSLTHLLNLENSKAYFRIGnVAFESAIINKVQNNNPGLKL 111
Cdd:cd01018     1 DKPTVAVSIEPQKYFVEKIAGDTVDVVVLVPPGSNPHTYEPKPQQMKKLSEADLYFRIG-LGFEEVWLERFRSNNPKMQV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566571 112 FDNSEGISLI--RGTHSHGDVEHA----SDIDPHTWTSVKNAKTIASNMYKAVVDLDPENKAYYSRNFKNFLSSLDSLDR 185
Cdd:cd01018    80 VNMSKGITLIpmADHHHHHHGEHEhhhhGNYDPHIWLSPANAKIMAENIYEALAELDPQNATYYQANLDALLAELDALDS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566571 186 EISQQLQPYRGSAFVVWHPSLSYFARDYGLEQISLSPEGKEASVKMMQSTIDKAIVRDVKTLFFQKDIDSRQAQVANEQI 265
Cdd:cd01018   160 EIRTILSKLKQRAFMVYHPAWGYFARDYGLTQIPIEEEGKEPSPADLKRLIDLAKEKGVRVVFVQPQFSTKSAEAIAREI 239

                         250       260
                  ....*....|....*....|....*..
gi 1624566571 266 KAEIVNINPLNYEWDKEMRSIANAISR 292
Cdd:cd01018   240 GAKVVTIDPLAADWEENLLKVADAFAH 266
ZnuA COG0803
ABC-type Zn uptake system ZnuABC, Zn-binding component ZnuA [Inorganic ion transport and ...
 1-275 2.75e-69

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: 216.26  E-value: 2.75e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566571   1 MKRSIfkyiltsLLIVAALGLFLRSCTSASTS---KPTITVSIQPQKYMLEKIVGDKWEIKCLLSNGANPESYDPSLTHL 77
Cdd:COG0803     1 MKRLL-------LALLLLAALLLAGCSAAASSaagKLKVVATFSPLADLAKQIGGDKVEVTSLVPPGADPHDYEPTPSDI 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566571  78 LNLENSKAYFRIGnVAFESAIINKVQN-NNPGLKLFDNSEGISLIRGTHSHgdveHASDIDPHTWTSVKNAKTIASNMYK 156
Cdd:COG0803    74 AKLAKADLVVYNG-LGLEGWLDKLLEAaGNPGVPVVDASEGIDLLELEEGH----DHGEPDPHVWLDPKNAKKVAENIAD 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566571 157 AVVDLDPENKAYYSRNFKNFLSSLDSLDREISQQLQPYRGSAFVVWHPSLSYFARDYGLEQISLSP--EGKEASVKMMQS 234
Cdd:COG0803   149 ALAELDPANAAYYEANAAAYLAELDALDAEIKAKLAAIPGRKLVTSHDAFGYLARAYGLEVVAIQGisPGSEPSPADLAE 228

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1624566571 235 TIDKAIVRDVKTLFFQKDIDSRQAQVANEQIKAEIVNINPL 275
Cdd:COG0803   229 LIDLIKEEGVKAIFVESQVSPKLAETLAEETGVKVLYLDSL 269
ZnuA pfam01297
Zinc-uptake complex component A periplasmic; ZnuA includes periplasmic solute binding proteins ...
 36-270 1.83e-58

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: 188.15  E-value: 1.83e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566571  36 ITVSIQPQKYMLEKIVGDKWEIKCLLSNGANPESYDPSLTHLLNLENSKAYFRIGnVAFESAIInKVQNNNPGLKLFDNS 115
Cdd:pfam01297   1 VVATTYPLADLAKQIGGDRVEVTSLVPPGADPHDYEPTPSDIAALSDADLVVYNG-LGLEPWLD-KLLEALPNKKVVDAS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566571 116 EGISL-IRGTHSHGDVEHASDIDPHTWTSVKNAKTIASNMYKAVVDLDPENKAYYSRNFKNFLSSLDSLDREISQQLQ-- 192
Cdd:pfam01297  79 EGVELlDEEGEEEDHDGHDHGYDPHVWLDPKNAKKMAENIADALSELDPANAATYEANAAAYLAELDALDAEIKEQLAsi 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566571 193 PYRGSAFVVWHPSLSYFARDYGLEQISLSP--EGKEASVKMMQSTIDKAIVRDVKTLFFQKDIDSRQAQVANEQIKAEIV 270
Cdd:pfam01297 159 PEKTRKLVTSHDAFGYLARAYGLEQVGIQGvsPESEPSAADLAELIDLIKEKKVKAIFVEPQVSPKLAETVAKETGVKVL 238
AztC NF040870
zinc ABC transporter substrate-binding protein AztC;
46-228 8.38e-17

zinc ABC transporter substrate-binding protein AztC;


Pssm-ID: 468807 [Multi-domain]  Cd Length: 277  Bit Score: 78.47  E-value: 8.38e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566571  46 MLEKIVGDKWEIKCLLSNGANPESYDPSLTHLLNLENSKAYFRIGNVAFESAIINKVQNNNPGLKLFDNSEGISLI--RG 123
Cdd:NF040870   11 LARNVVGDRAEVTTLMKPDADPHSFEPSAADAAALERADLVVVNGLGLEEGFLRHLIAASATGAPVVEVGDGVDPLpyPE 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566571 124 THSHGDVEHASDIDPHTWTSVKNAKTIASNMYKAVVDLDPENKAYYSRNFKNFLSSLDSLDREISQQLQ--PYRGSAFVV 201
Cdd:NF040870   91 GGHYHFEAGAGPPDPHFWTDPARARDAVDNIADAFCEADDGDCAAYRANAAAYRAELDELDAEMREAFAaiPADRRTLVT 170

                         170       180
                  ....*....|....*....|....*....
gi 1624566571 202 WHPSLSYFARDYGLEQIS-LSPEGK-EAS 228
Cdd:NF040870  171 NHHVFGYLAERYGFRVLGaVIPSGStLAS 199
znuA PRK09545
zinc ABC transporter substrate-binding protein ZnuA;
14-218 1.34e-12

zinc ABC transporter substrate-binding protein ZnuA;


Pssm-ID: 236558 [Multi-domain]  Cd Length: 311  Bit Score: 66.95  E-value: 1.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566571  14 LIVAALGLFLRSCTSASTSKPTITvSIQPQKYMLEKIVGDKWEIKCLLSNGANPESYDPSLTHLLNLENSKAYFRIGN-- 91
Cdd:PRK09545    6 LLFAALLAALLGGATQAANAAVVT-SIKPLGFIASAIADGVTETEVLLPDGASPHDYSLRPSDVKRLQSADLVVWVGPem 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566571  92 VAFESAIINKVQNNN-------PGLKLFdnsegisLIRGT----------HSHGDVE----HASDIDPHTWTSVKNAKTI 150
Cdd:PRK09545   85 EAFLEKPVSKLPENKqvtiaqlPDVKPL-------LMKGAhddhhdddhdHAGHEKSdedhHHGEYNMHIWLSPEIARAT 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1624566571 151 ASNMYKAVVDLDPENKAYYSRNFKNFLSSLDSLDREISQQLQPYRGSAFVVWHPSLSYFARDYGLEQI 218
Cdd:PRK09545  158 AVAIHDKLVELMPQSKAKLDANLKDFEAQLAQTDKQIGNQLAPVKGKGYFVFHDAYGYFEKHYGLTPL 225
anch_rpt_subst TIGR03772
anchored repeat ABC transporter, substrate-binding protein; Members of this protein family are ...
 123-215 3.78e-12

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: 66.04  E-value: 3.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566571 123 GTHSHGDvehasdIDPHTWTSVKNAKTIASNMYKAVVDLDPENKAYYSRNFKNFLSSLDSLDREISQQLQ--PYRGSAFV 200
Cdd:TIGR03772 302 GKHVHGE------IDPHLWHNVKNAIAYVEVIRDKLIEVDPRGAQAYRSNASAYIHRLERLDTYVRRTIAtiPPSRRHLI 375

                          90
                  ....*....|....*
gi 1624566571 201 VWHPSLSYFARDYGL 215
Cdd:TIGR03772 376 TTHDAYSYLGQAYGL 390
 
Name Accession Description Interval E-value
ZntC cd01018
Metal binding protein ZntC. These proteins are predicted to function as initial receptors in ...
 32-292 2.40e-95

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: 281.94  E-value: 2.40e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566571  32 SKPTITVSIQPQKYMLEKIVGDKWEIKCLLSNGANPESYDPSLTHLLNLENSKAYFRIGnVAFESAIINKVQNNNPGLKL 111
Cdd:cd01018     1 DKPTVAVSIEPQKYFVEKIAGDTVDVVVLVPPGSNPHTYEPKPQQMKKLSEADLYFRIG-LGFEEVWLERFRSNNPKMQV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566571 112 FDNSEGISLI--RGTHSHGDVEHA----SDIDPHTWTSVKNAKTIASNMYKAVVDLDPENKAYYSRNFKNFLSSLDSLDR 185
Cdd:cd01018    80 VNMSKGITLIpmADHHHHHHGEHEhhhhGNYDPHIWLSPANAKIMAENIYEALAELDPQNATYYQANLDALLAELDALDS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566571 186 EISQQLQPYRGSAFVVWHPSLSYFARDYGLEQISLSPEGKEASVKMMQSTIDKAIVRDVKTLFFQKDIDSRQAQVANEQI 265
Cdd:cd01018   160 EIRTILSKLKQRAFMVYHPAWGYFARDYGLTQIPIEEEGKEPSPADLKRLIDLAKEKGVRVVFVQPQFSTKSAEAIAREI 239

                         250       260
                  ....*....|....*....|....*..
gi 1624566571 266 KAEIVNINPLNYEWDKEMRSIANAISR 292
Cdd:cd01018   240 GAKVVTIDPLAADWEENLLKVADAFAH 266
ZnuA COG0803
ABC-type Zn uptake system ZnuABC, Zn-binding component ZnuA [Inorganic ion transport and ...
 1-275 2.75e-69

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: 216.26  E-value: 2.75e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566571   1 MKRSIfkyiltsLLIVAALGLFLRSCTSASTS---KPTITVSIQPQKYMLEKIVGDKWEIKCLLSNGANPESYDPSLTHL 77
Cdd:COG0803     1 MKRLL-------LALLLLAALLLAGCSAAASSaagKLKVVATFSPLADLAKQIGGDKVEVTSLVPPGADPHDYEPTPSDI 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566571  78 LNLENSKAYFRIGnVAFESAIINKVQN-NNPGLKLFDNSEGISLIRGTHSHgdveHASDIDPHTWTSVKNAKTIASNMYK 156
Cdd:COG0803    74 AKLAKADLVVYNG-LGLEGWLDKLLEAaGNPGVPVVDASEGIDLLELEEGH----DHGEPDPHVWLDPKNAKKVAENIAD 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566571 157 AVVDLDPENKAYYSRNFKNFLSSLDSLDREISQQLQPYRGSAFVVWHPSLSYFARDYGLEQISLSP--EGKEASVKMMQS 234
Cdd:COG0803   149 ALAELDPANAAYYEANAAAYLAELDALDAEIKAKLAAIPGRKLVTSHDAFGYLARAYGLEVVAIQGisPGSEPSPADLAE 228

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1624566571 235 TIDKAIVRDVKTLFFQKDIDSRQAQVANEQIKAEIVNINPL 275
Cdd:COG0803   229 LIDLIKEEGVKAIFVESQVSPKLAETLAEETGVKVLYLDSL 269
ZnuA pfam01297
Zinc-uptake complex component A periplasmic; ZnuA includes periplasmic solute binding proteins ...
 36-270 1.83e-58

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: 188.15  E-value: 1.83e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566571  36 ITVSIQPQKYMLEKIVGDKWEIKCLLSNGANPESYDPSLTHLLNLENSKAYFRIGnVAFESAIInKVQNNNPGLKLFDNS 115
Cdd:pfam01297   1 VVATTYPLADLAKQIGGDRVEVTSLVPPGADPHDYEPTPSDIAALSDADLVVYNG-LGLEPWLD-KLLEALPNKKVVDAS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566571 116 EGISL-IRGTHSHGDVEHASDIDPHTWTSVKNAKTIASNMYKAVVDLDPENKAYYSRNFKNFLSSLDSLDREISQQLQ-- 192
Cdd:pfam01297  79 EGVELlDEEGEEEDHDGHDHGYDPHVWLDPKNAKKMAENIADALSELDPANAATYEANAAAYLAELDALDAEIKEQLAsi 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566571 193 PYRGSAFVVWHPSLSYFARDYGLEQISLSP--EGKEASVKMMQSTIDKAIVRDVKTLFFQKDIDSRQAQVANEQIKAEIV 270
Cdd:pfam01297 159 PEKTRKLVTSHDAFGYLARAYGLEQVGIQGvsPESEPSAADLAELIDLIKEKKVKAIFVEPQVSPKLAETVAKETGVKVL 238
AdcA cd01017
Metal binding protein AdcA. These proteins have been shown to function in the ABC uptake of ...
 31-275 1.80e-56

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: 183.26  E-value: 1.80e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566571  31 TSKPTITVSIQPQKYMLEKIVGDKWEIKCLLSNGANPESYDPSLTHLLNLENSKAYFRIGNvAFESaIINKVQNN--NPG 108
Cdd:cd01017     1 SGKLKVVTTFYPLYEFTKAIGGDKADVKLIIPAGTEPHDFEPSPKDIARIADADVFVYNGL-GMET-WAEKVLKSlqNKK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566571 109 LKLFDNSEGISLIRGT-----HSHGDVEHASDIDPHTWTSVKNAKTIASNMYKAVVDLDPENKAYYSRNFKNFLSSLDSL 183
Cdd:cd01017    79 LKVVEASKGIKLLKAGgaehdHDHSHSHHHGDYDPHVWLSPVLAIQQVENIKDALIKLDPDNKEYYEKNAAAYAKKLEAL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566571 184 DREISQQLQPYRGSAFVVWHPSLSYFARDYGLEQIS---LSPEGkEASVKMMQSTIDKAIVRDVKTLFFQKDIDSRQAQV 260
Cdd:cd01017   159 DQEYRAKLAKAKGKTFVTQHAAFGYLARRYGLKQIAivgVSPEV-EPSPKQLAELVEFVKKSDVKYIFFEENASSKIAET 237

                         250
                  ....*....|....*
gi 1624566571 261 ANEQIKAEIVNINPL 275
Cdd:cd01017   238 LAKETGAKLLVLNPL 252
ZnuA cd01019
Zinc binding protein ZnuA. These proteins have been shown to function as initial receptors in ...
 31-275 1.06e-31

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: 119.01  E-value: 1.06e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566571  31 TSKPTITVSIQPQKYMLEKIVGDKWEIKCLLSNGANPESYDPSLTHLLNLENSKAYFRIGNV--AFESAIINK------- 101
Cdd:cd01019     1 AAEASVLTSIKPLGFIAAAIMGGVGEVEVLVPPGASPHDYELRPSDARKLQEADLVVWIGPDleAFLDKVLQGrkkgkvl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566571 102 --VQNNNPGLKLFDNSEGISLIRGTHSHGDVEHAS--DIDPHTWTSVKNAKTIASNMYKAVVDLDPENKAYYSRNFKNFL 177
Cdd:cd01019    81 tlAKLIDLKTLEDGASHGDHEHDHEHAHGEHDGHEegGLDPHLWLSPENAAEVAQAVAEKLSALDPDNAATYAANLEAFN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566571 178 SSLDSLDREISQQLQPYRGSAFVVWHPSLSYFARDYGLEQ---ISLSPEGK--EASVKMMQSTIDKAivrDVKTLFFQKD 252
Cdd:cd01019   161 ARLAELDATIKERLAPVKTKPFFVFHDAYGYFEKRYGLTQagvFTIDPEIDpgAKRLAKIRKEIKEK---GATCVFAEPQ 237

                         250       260
                  ....*....|....*....|...
gi 1624566571 253 IDSRQAQVANEQIKAEIVNINPL 275
Cdd:cd01019   238 FHPKIAETLAEGTGAKVGELDPL 260
PsaA cd01137
Metal binding protein PsaA. These proteins have been shown to function as initial receptors ...
 13-263 4.18e-28

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: 109.29  E-value: 4.18e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566571  13 LLIVAALGlflrSCTSASTSKPTITVSIQPQKYMLEKIVGDKWEIKCLLSNGANPESYDPSLTHLLNLENSKAYFRIGnV 92
Cdd:cd01137     1 LAACASLG----SSPATAASKLKVVATFSILADIARNIAGDRVNVTSIVPPGADPHEYEPTPSDIKKLSKADLILYNG-L 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566571  93 AFESAIINKVQNNNPGLKLFDNSEGISLIR--GTHSHGDVehasdiDPHTWTSVKNAKTIASNMYKAVVDLDPENKAYYS 170
Cdd:cd01137    76 NLEPWLERLVKNAGKDVPVVAVSEGIDPIPleEGHYKGKP------DPHAWMSPKNAIIYVKNIAKALSEADPANAETYQ 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566571 171 RNFKNFLSSLDSLDREISQQLQ--PYRGSAFVVWHPSLSYFARDYGLEQISLSPEG--KEASVKMMQSTIDKAIVRDVKT 246
Cdd:cd01137   150 KNAAAYKAKLKALDEWAKAKFAtiPAEKRKLVTSEGAFSYFAKAYGLKEAYLWPINteEEGTPKQVATLIEQVKKEKVPA 229

                         250
                  ....*....|....*...
gi 1624566571 247 LFFQKDIDSR-QAQVANE 263
Cdd:cd01137   230 VFVESTVNDRlMKQVAKE 247
ZnuA COG4531
ABC-type Zn2+ transport system, periplasmic component/surface adhesin ZnuA [Inorganic ion ...
 27-223 6.42e-28

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: 109.15  E-value: 6.42e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566571  27 TSASTSKPTITVSIQPqkymLEKIV----GDKWEIKCLLSNGANPESYD--PSltHLLNLENSKAYFRIGN--VAFESAI 98
Cdd:COG4531     3 SAAAAAAPRVVTSIKP----LHSLVaavmDGVGEPELLLPPGASPHDYAlrPS--DARALQDADLVFWVGPdlEPFLEKP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566571  99 INKVQNNN--------PGLKLFDNSEGI-----------SLIRGTHSHGDVEHASDIDPHTWTSVKNAKTIASNMYKAVV 159
Cdd:COG4531    77 LETLAPDAkvvellelPGLTLLPFREGGdfehhdhhdehHHHHHHHDDHHDHHHGGYDPHLWLSPENAKAWAAAIADALS 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1624566571 160 DLDPENKAYYSRNFKNFLSSLDSLDREISQQLQPYRGSAFVVWHPSLSYFARDYGLEQ---ISLSPE 223
Cdd:COG4531   157 ELDPENAATYQANAAAFEARLDALDAEIAAQLAPVKGKPFFVFHDAYQYFEKRFGLNAlgaITLNPE 223
TroA cd01016
Metal binding protein TroA. These proteins have been shown to function as initial receptors in ...
 33-260 2.85e-17

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: 79.71  E-value: 2.85e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566571  33 KPTITVSIQPQKYMLEKIVGDKWEIKCLLSNGANPESYDPSLTHLLNLENSKAYFRIGnVAFE---SAIINKVQNNNPGL 109
Cdd:cd01016     1 KPNVVTTTGMIADAVENIGGDHVEVTGLMGPGVDPHLYKATAGDVEKLQNADVVFYNG-LHLEgkmSDVLSKLGSSKSVI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566571 110 KLFDnsegiSLIRGTHSHGDVEHAsdIDPHTWTSVKNAKTIASNMYKAVVDLDPENKAYYSRNFKNFLSSLDSLDREISQ 189
Cdd:cd01016    80 ALED-----TLDRSQLILDEEEGT--YDPHIWFDVKLWKYAVKAVAEVLSEKLPEHKDEFQANSEAYVEELDSLDAYAKK 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566571 190 QLQ--PYRGSAFVVWHPSLSYFARDYGLEQISL---SPEGkEASVKMMQSTIDKAIVRDVKTLFF-----QKDIDSRQAQ 259
Cdd:cd01016   153 KIAeiPEQQRVLVTAHDAFGYFGRAYGFEVKGLqgiSTDS-EAGLRDINELVDLIVERKIKAIFVessvnQKSIEALQDA 231


                  .
gi 1624566571 260 V 260
Cdd:cd01016   232 V 232
AztC NF040870
zinc ABC transporter substrate-binding protein AztC;
46-228 8.38e-17

zinc ABC transporter substrate-binding protein AztC;


Pssm-ID: 468807 [Multi-domain]  Cd Length: 277  Bit Score: 78.47  E-value: 8.38e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566571  46 MLEKIVGDKWEIKCLLSNGANPESYDPSLTHLLNLENSKAYFRIGNVAFESAIINKVQNNNPGLKLFDNSEGISLI--RG 123
Cdd:NF040870   11 LARNVVGDRAEVTTLMKPDADPHSFEPSAADAAALERADLVVVNGLGLEEGFLRHLIAASATGAPVVEVGDGVDPLpyPE 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566571 124 THSHGDVEHASDIDPHTWTSVKNAKTIASNMYKAVVDLDPENKAYYSRNFKNFLSSLDSLDREISQQLQ--PYRGSAFVV 201
Cdd:NF040870   91 GGHYHFEAGAGPPDPHFWTDPARARDAVDNIADAFCEADDGDCAAYRANAAAYRAELDELDAEMREAFAaiPADRRTLVT 170

                         170       180
                  ....*....|....*....|....*....
gi 1624566571 202 WHPSLSYFARDYGLEQIS-LSPEGK-EAS 228
Cdd:NF040870  171 NHHVFGYLAERYGFRVLGaVIPSGStLAS 199
TroA_c cd01145
Periplasmic binding protein TroA_c. These proteins are predicted to function as initial ...
 32-224 3.46e-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: 75.23  E-value: 3.46e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566571  32 SKPTITVSIQPQKYMLEKIVGDKWEIKCLLSNGANPESYDPSLTHLLNLENSKAYFRIGN--VAFESAIINKVQNNN--P 107
Cdd:cd01145     1 AALNVVVTFPDLKDLVREVAGDAVIVSALTPPGVDPHQYQLKPSDIAKMRKADLVVTSGHelEGFEPKLAELSSNSKvqP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566571 108 GLKLFDnSEGISLIRGTHSHGDVeHASDiDPHTWTSVKNAKTIASNMYKAVVDLDPENKAYYSRNFKNFLSSLDSLDREI 187
Cdd:cd01145    81 GIKILI-EDSDTVGMVDRAMGDY-HGKG-NPHVWLDPNNAPALAKALADALIELDPSEQEEYKENLRVFLAKLNKLLREW 157

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1624566571 188 SQQLQPYRGSAFVVWHPSLSYFARDYGLEQI-SLSPEG 224
Cdd:cd01145   158 ERQFEGLKGIQVVAYHPSYQYLADWLGIEVVaSLEPLP 195
znuA PRK09545
zinc ABC transporter substrate-binding protein ZnuA;
14-218 1.34e-12

zinc ABC transporter substrate-binding protein ZnuA;


Pssm-ID: 236558 [Multi-domain]  Cd Length: 311  Bit Score: 66.95  E-value: 1.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566571  14 LIVAALGLFLRSCTSASTSKPTITvSIQPQKYMLEKIVGDKWEIKCLLSNGANPESYDPSLTHLLNLENSKAYFRIGN-- 91
Cdd:PRK09545    6 LLFAALLAALLGGATQAANAAVVT-SIKPLGFIASAIADGVTETEVLLPDGASPHDYSLRPSDVKRLQSADLVVWVGPem 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566571  92 VAFESAIINKVQNNN-------PGLKLFdnsegisLIRGT----------HSHGDVE----HASDIDPHTWTSVKNAKTI 150
Cdd:PRK09545   85 EAFLEKPVSKLPENKqvtiaqlPDVKPL-------LMKGAhddhhdddhdHAGHEKSdedhHHGEYNMHIWLSPEIARAT 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1624566571 151 ASNMYKAVVDLDPENKAYYSRNFKNFLSSLDSLDREISQQLQPYRGSAFVVWHPSLSYFARDYGLEQI 218
Cdd:PRK09545  158 AVAIHDKLVELMPQSKAKLDANLKDFEAQLAQTDKQIGNQLAPVKGKGYFVFHDAYGYFEKHYGLTPL 225
anch_rpt_subst TIGR03772
anchored repeat ABC transporter, substrate-binding protein; Members of this protein family are ...
 123-215 3.78e-12

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: 66.04  E-value: 3.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566571 123 GTHSHGDvehasdIDPHTWTSVKNAKTIASNMYKAVVDLDPENKAYYSRNFKNFLSSLDSLDREISQQLQ--PYRGSAFV 200
Cdd:TIGR03772 302 GKHVHGE------IDPHLWHNVKNAIAYVEVIRDKLIEVDPRGAQAYRSNASAYIHRLERLDTYVRRTIAtiPPSRRHLI 375

                          90
                  ....*....|....*
gi 1624566571 201 VWHPSLSYFARDYGL 215
Cdd:TIGR03772 376 TTHDAYSYLGQAYGL 390
TroA_b cd01020
Metal binding protein TroA_b. These proteins are predicted to function as initial receptors ...
 48-271 3.37e-10

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: 59.38  E-value: 3.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566571  48 EKIVGDKWEIKCLLSNG-ANPESYDPSLTHLLNLenSKAYFRIGNVAFESAIINKvqnnnpglkLFDNSEGISLIR-GTH 125
Cdd:cd01020    17 EAVGGDHVEVTSIITNPdVDPHDFEPTPTDAAKV--STADIVVYNGGGYDPWMTK---------LLADTKDVIVIAaDLD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566571 126 SHGDVEHAsdiDPHTWTSVKNAKTIASNMYKAVVDLDPENKAYYSRNFKNFLSSLDSLDREISQQLQPYRGSAFVVWHPS 205
Cdd:cd01020    86 GHDDKEGD---NPHLWYDPETMSKVANALADALVKADPDNKKYYQANAKKFVASLKPLAAKIAELSAKYKGAPVAATEPV 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1624566571 206 LSYFARDYGLeqISLSPEGKEASvkmMQSTIDKAiVRDVKTlfFQKDIDSRqaqvaneQIKAEIVN 271
Cdd:cd01020   163 FDYLLDALGM--KERTPKGYTAT---TESETEPS-PADIAA--FQNAIKNR-------QIDALIVN 213
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH