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Conserved domains on  [gi|1080980409|gb|OFR38126|]
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zinc ABC transporter substrate-binding protein [Staphylococcus sp. HMSC063F02]

Protein Classification

metal ABC transporter substrate-binding protein( domain architecture ID 11435238)

metal ABC transporter substrate-binding protein functions as the initial receptor for the active uptake of metals such as Zn(2+)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ZnuA COG0803
ABC-type Zn uptake system ZnuABC, Zn-binding component ZnuA [Inorganic ion transport and ...
1-307 5.66e-105

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: 308.33  E-value: 5.66e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080980409   1 MKKVILFLFTITLsVVLAACSNGDKDGDsdkelesvdkDKIKVVTSFSMIDDMVKEIGGEHVEVKNLVPTGTDPHDYDPK 80
Cdd:COG0803     1 MKRLLLALLLLAA-LLLAGCSAAASSAA----------GKLKVVATFSPLADLAKQIGGDKVEVTSLVPPGADPHDYEPT 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080980409  81 PDDIKHISSADLVFYNGLNLEggskGWLFKALESSDFSKENAIKTSEGVKPKYIKDEDGKKEVNPHAFIDPKVGEKMIKN 160
Cdd:COG0803    70 PSDIAKLAKADLVVYNGLGLE----GWLDKLLEAAGNPGVPVVDASEGIDLLELEEGHDHGEPDPHVWLDPKNAKKVAEN 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080980409 161 ITKSLSERNPKNKDYYKENEKAYLKKLHNIEDDYEKQLGDIPKkdRVFVASEQAFQYLTDRYDLKEGYIWAIDTDENGSP 240
Cdd:COG0803   146 IADALAELDPANAAYYEANAAAYLAELDALDAEIKAKLAAIPG--RKLVTSHDAFGYLARAYGLEVVAIQGISPGSEPSP 223
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1080980409 241 EQIKDLVKFIDKNEPSHLFVESNVDKRPMETVSKESGVsiykKPIYSDEISKEGGVADTYLKYLEYN 307
Cdd:COG0803   224 ADLAELIDLIKEEGVKAIFVESQVSPKLAETLAEETGV----KVLYLDSLGGPGGPGDTYLDMMRHN 286
 
Name Accession Description Interval E-value
ZnuA COG0803
ABC-type Zn uptake system ZnuABC, Zn-binding component ZnuA [Inorganic ion transport and ...
1-307 5.66e-105

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: 308.33  E-value: 5.66e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080980409   1 MKKVILFLFTITLsVVLAACSNGDKDGDsdkelesvdkDKIKVVTSFSMIDDMVKEIGGEHVEVKNLVPTGTDPHDYDPK 80
Cdd:COG0803     1 MKRLLLALLLLAA-LLLAGCSAAASSAA----------GKLKVVATFSPLADLAKQIGGDKVEVTSLVPPGADPHDYEPT 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080980409  81 PDDIKHISSADLVFYNGLNLEggskGWLFKALESSDFSKENAIKTSEGVKPKYIKDEDGKKEVNPHAFIDPKVGEKMIKN 160
Cdd:COG0803    70 PSDIAKLAKADLVVYNGLGLE----GWLDKLLEAAGNPGVPVVDASEGIDLLELEEGHDHGEPDPHVWLDPKNAKKVAEN 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080980409 161 ITKSLSERNPKNKDYYKENEKAYLKKLHNIEDDYEKQLGDIPKkdRVFVASEQAFQYLTDRYDLKEGYIWAIDTDENGSP 240
Cdd:COG0803   146 IADALAELDPANAAYYEANAAAYLAELDALDAEIKAKLAAIPG--RKLVTSHDAFGYLARAYGLEVVAIQGISPGSEPSP 223
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1080980409 241 EQIKDLVKFIDKNEPSHLFVESNVDKRPMETVSKESGVsiykKPIYSDEISKEGGVADTYLKYLEYN 307
Cdd:COG0803   224 ADLAELIDLIKEEGVKAIFVESQVSPKLAETLAEETGV----KVLYLDSLGGPGGPGDTYLDMMRHN 286
PsaA cd01137
Metal binding protein PsaA. These proteins have been shown to function as initial receptors ...
17-315 2.40e-101

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: 299.19  E-value: 2.40e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080980409  17 LAACSNGDKDgdsdkelESVDKDKIKVVTSFSMIDDMVKEIGGEHVEVKNLVPTGTDPHDYDPKPDDIKHISSADLVFYN 96
Cdd:cd01137     1 LAACASLGSS-------PATAASKLKVVATFSILADIARNIAGDRVNVTSIVPPGADPHEYEPTPSDIKKLSKADLILYN 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080980409  97 GLNLEGgskgWLFKALESSDFSKEnAIKTSEGVKPKYIKDEDGKKEVNPHAFIDPKVGEKMIKNITKSLSERNPKNKDYY 176
Cdd:cd01137    74 GLNLEP----WLERLVKNAGKDVP-VVAVSEGIDPIPLEEGHYKGKPDPHAWMSPKNAIIYVKNIAKALSEADPANAETY 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080980409 177 KENEKAYLKKLHNIEDDYEKQLGDIPKKDRVFVASEQAFQYLTDRYDLKEGYIWAIDTDENGSPEQIKDLVKFIDKNEPS 256
Cdd:cd01137   149 QKNAAAYKAKLKALDEWAKAKFATIPAEKRKLVTSEGAFSYFAKAYGLKEAYLWPINTEEEGTPKQVATLIEQVKKEKVP 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1080980409 257 HLFVESNVDKRPMETVSKESGVSIYKKpIYSDEISKEGGVADTYLKYLEYNLDVLTDGL 315
Cdd:cd01137   229 AVFVESTVNDRLMKQVAKETGAKIGGQ-LYTDSLSEKGGPADTYLDMMEHNLDTIVEGL 286
ZnuA pfam01297
Zinc-uptake complex component A periplasmic; ZnuA includes periplasmic solute binding proteins ...
43-314 1.02e-92

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: 276.36  E-value: 1.02e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080980409  43 VVTSFSMIDDMVKEIGGEHVEVKNLVPTGTDPHDYDPKPDDIKHISSADLVFYNGLNLEGgskgWLFKALESSDfsKENA 122
Cdd:pfam01297   1 VVATTYPLADLAKQIGGDRVEVTSLVPPGADPHDYEPTPSDIAALSDADLVVYNGLGLEP----WLDKLLEALP--NKKV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080980409 123 IKTSEGVKPKYIKDEDGKKE-----VNPHAFIDPKVGEKMIKNITKSLSERNPKNKDYYKENEKAYLKKLHNIEDDYEKQ 197
Cdd:pfam01297  75 VDASEGVELLDEEGEEEDHDghdhgYDPHVWLDPKNAKKMAENIADALSELDPANAATYEANAAAYLAELDALDAEIKEQ 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080980409 198 LGDIPKKDRVFVASEQAFQYLTDRYDLKEGYIWAIDTDENGSPEQIKDLVKFIDKNEPSHLFVESNVDKRPMETVSKESG 277
Cdd:pfam01297 155 LASIPEKTRKLVTSHDAFGYLARAYGLEQVGIQGVSPESEPSAADLAELIDLIKEKKVKAIFVEPQVSPKLAETVAKETG 234
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1080980409 278 VSIYkKPIYSDEISKEGGvADTYLKYLEYNLDVLTDG 314
Cdd:pfam01297 235 VKVL-GPLYTDSLGEPGG-GATYLDLMRHNLDTLAEA 269
AztC NF040870
zinc ABC transporter substrate-binding protein AztC;
43-315 6.45e-54

zinc ABC transporter substrate-binding protein AztC;


Pssm-ID: 468807 [Multi-domain]  Cd Length: 277  Bit Score: 177.46  E-value: 6.45e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080980409  43 VVTSFSMIDDMVKEIGGEHVEVKNLVPTGTDPHDYDPKPDDIKHISSADLVFYNGLNLEGGskgwLFKALESSDFSKENA 122
Cdd:NF040870    1 VVVTTNILGDLARNVVGDRAEVTTLMKPDADPHSFEPSAADAAALERADLVVVNGLGLEEG----FLRHLIAASATGAPV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080980409 123 IKTSEGVKP-KYIKDEDGKKEV-----NPHAFIDPKVGEKMIKNITKSLSERNPKNKDYYKENEKAYLKKLHNIEDDYEK 196
Cdd:NF040870   77 VEVGDGVDPlPYPEGGHYHFEAgagppDPHFWTDPARARDAVDNIADAFCEADDGDCAAYRANAAAYRAELDELDAEMRE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080980409 197 QLGDIPKKDRVFVASEQAFQYLTDRYDLKegYIWAID----TDENGSPEQIKDLVKFIDKNEPSHLFVESNVDKRPMETV 272
Cdd:NF040870  157 AFAAIPADRRTLVTNHHVFGYLAERYGFR--VLGAVIpsgsTLASPSAADLASLARAIREAGVPAIFAESSQPPRLAEVL 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1080980409 273 SKESGVSIYKKPIYSDEISKEGGVADTYLKYLEYNLDVLTDGL 315
Cdd:NF040870  235 ASEAGLDVGVVELYSESLSEPDGGAATYLDMMRANAEAIVDGL 277
znuA PRK09545
zinc ABC transporter substrate-binding protein ZnuA;
43-225 6.81e-14

zinc ABC transporter substrate-binding protein ZnuA;


Pssm-ID: 236558 [Multi-domain]  Cd Length: 311  Bit Score: 70.81  E-value: 6.81e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080980409  43 VVTSF-------SMIDDMVKEiggehVEVknLVPTGTDPHDYDPKPDDIKHISSADLVFYNGLNLEggskGWLFKALESS 115
Cdd:PRK09545   27 VVTSIkplgfiaSAIADGVTE-----TEV--LLPDGASPHDYSLRPSDVKRLQSADLVVWVGPEME----AFLEKPVSKL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080980409 116 DFSKENAIKTSEGVKPKYIKDEDGKK--------------------EVNPHAFIDPKVGEKMIKNITKSLSERNPKNKDY 175
Cdd:PRK09545   96 PENKQVTIAQLPDVKPLLMKGAHDDHhdddhdhagheksdedhhhgEYNMHIWLSPEIARATAVAIHDKLVELMPQSKAK 175
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1080980409 176 YKENEKAYLKKLHNIEDDYEKQLGdiPKKDRVFVASEQAFQYLTDRYDLK 225
Cdd:PRK09545  176 LDANLKDFEAQLAQTDKQIGNQLA--PVKGKGYFVFHDAYGYFEKHYGLT 223
 
Name Accession Description Interval E-value
ZnuA COG0803
ABC-type Zn uptake system ZnuABC, Zn-binding component ZnuA [Inorganic ion transport and ...
1-307 5.66e-105

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: 308.33  E-value: 5.66e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080980409   1 MKKVILFLFTITLsVVLAACSNGDKDGDsdkelesvdkDKIKVVTSFSMIDDMVKEIGGEHVEVKNLVPTGTDPHDYDPK 80
Cdd:COG0803     1 MKRLLLALLLLAA-LLLAGCSAAASSAA----------GKLKVVATFSPLADLAKQIGGDKVEVTSLVPPGADPHDYEPT 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080980409  81 PDDIKHISSADLVFYNGLNLEggskGWLFKALESSDFSKENAIKTSEGVKPKYIKDEDGKKEVNPHAFIDPKVGEKMIKN 160
Cdd:COG0803    70 PSDIAKLAKADLVVYNGLGLE----GWLDKLLEAAGNPGVPVVDASEGIDLLELEEGHDHGEPDPHVWLDPKNAKKVAEN 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080980409 161 ITKSLSERNPKNKDYYKENEKAYLKKLHNIEDDYEKQLGDIPKkdRVFVASEQAFQYLTDRYDLKEGYIWAIDTDENGSP 240
Cdd:COG0803   146 IADALAELDPANAAYYEANAAAYLAELDALDAEIKAKLAAIPG--RKLVTSHDAFGYLARAYGLEVVAIQGISPGSEPSP 223
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1080980409 241 EQIKDLVKFIDKNEPSHLFVESNVDKRPMETVSKESGVsiykKPIYSDEISKEGGVADTYLKYLEYN 307
Cdd:COG0803   224 ADLAELIDLIKEEGVKAIFVESQVSPKLAETLAEETGV----KVLYLDSLGGPGGPGDTYLDMMRHN 286
PsaA cd01137
Metal binding protein PsaA. These proteins have been shown to function as initial receptors ...
17-315 2.40e-101

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: 299.19  E-value: 2.40e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080980409  17 LAACSNGDKDgdsdkelESVDKDKIKVVTSFSMIDDMVKEIGGEHVEVKNLVPTGTDPHDYDPKPDDIKHISSADLVFYN 96
Cdd:cd01137     1 LAACASLGSS-------PATAASKLKVVATFSILADIARNIAGDRVNVTSIVPPGADPHEYEPTPSDIKKLSKADLILYN 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080980409  97 GLNLEGgskgWLFKALESSDFSKEnAIKTSEGVKPKYIKDEDGKKEVNPHAFIDPKVGEKMIKNITKSLSERNPKNKDYY 176
Cdd:cd01137    74 GLNLEP----WLERLVKNAGKDVP-VVAVSEGIDPIPLEEGHYKGKPDPHAWMSPKNAIIYVKNIAKALSEADPANAETY 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080980409 177 KENEKAYLKKLHNIEDDYEKQLGDIPKKDRVFVASEQAFQYLTDRYDLKEGYIWAIDTDENGSPEQIKDLVKFIDKNEPS 256
Cdd:cd01137   149 QKNAAAYKAKLKALDEWAKAKFATIPAEKRKLVTSEGAFSYFAKAYGLKEAYLWPINTEEEGTPKQVATLIEQVKKEKVP 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1080980409 257 HLFVESNVDKRPMETVSKESGVSIYKKpIYSDEISKEGGVADTYLKYLEYNLDVLTDGL 315
Cdd:cd01137   229 AVFVESTVNDRLMKQVAKETGAKIGGQ-LYTDSLSEKGGPADTYLDMMEHNLDTIVEGL 286
ZnuA pfam01297
Zinc-uptake complex component A periplasmic; ZnuA includes periplasmic solute binding proteins ...
43-314 1.02e-92

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: 276.36  E-value: 1.02e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080980409  43 VVTSFSMIDDMVKEIGGEHVEVKNLVPTGTDPHDYDPKPDDIKHISSADLVFYNGLNLEGgskgWLFKALESSDfsKENA 122
Cdd:pfam01297   1 VVATTYPLADLAKQIGGDRVEVTSLVPPGADPHDYEPTPSDIAALSDADLVVYNGLGLEP----WLDKLLEALP--NKKV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080980409 123 IKTSEGVKPKYIKDEDGKKE-----VNPHAFIDPKVGEKMIKNITKSLSERNPKNKDYYKENEKAYLKKLHNIEDDYEKQ 197
Cdd:pfam01297  75 VDASEGVELLDEEGEEEDHDghdhgYDPHVWLDPKNAKKMAENIADALSELDPANAATYEANAAAYLAELDALDAEIKEQ 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080980409 198 LGDIPKKDRVFVASEQAFQYLTDRYDLKEGYIWAIDTDENGSPEQIKDLVKFIDKNEPSHLFVESNVDKRPMETVSKESG 277
Cdd:pfam01297 155 LASIPEKTRKLVTSHDAFGYLARAYGLEQVGIQGVSPESEPSAADLAELIDLIKEKKVKAIFVEPQVSPKLAETVAKETG 234
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1080980409 278 VSIYkKPIYSDEISKEGGvADTYLKYLEYNLDVLTDG 314
Cdd:pfam01297 235 VKVL-GPLYTDSLGEPGG-GATYLDLMRHNLDTLAEA 269
AdcA cd01017
Metal binding protein AdcA. These proteins have been shown to function in the ABC uptake of ...
38-315 2.20e-66

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: 209.46  E-value: 2.20e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080980409  38 KDKIKVVTSFSMIDDMVKEIGGEHVEVKNLVPTGTDPHDYDPKPDDIKHISSADLVFYNGLNLEggskGWLFKALESSDF 117
Cdd:cd01017     1 SGKLKVVTTFYPLYEFTKAIGGDKADVKLIIPAGTEPHDFEPSPKDIARIADADVFVYNGLGME----TWAEKVLKSLQN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080980409 118 SKENAIKTSEGVKP---------KYIKDEDGKKEVNPHAFIDPKVGEKMIKNITKSLSERNPKNKDYYKENEKAYLKKLH 188
Cdd:cd01017    77 KKLKVVEASKGIKLlkaggaehdHDHSHSHHHGDYDPHVWLSPVLAIQQVENIKDALIKLDPDNKEYYEKNAAAYAKKLE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080980409 189 NIEDDYEKQLGDIPKKDrvFVASEQAFQYLTDRYDLKEGYIWAIDTDENGSPEQIKDLVKFIDKNEPSHLFVESNVDKRP 268
Cdd:cd01017   157 ALDQEYRAKLAKAKGKT--FVTQHAAFGYLARRYGLKQIAIVGVSPEVEPSPKQLAELVEFVKKSDVKYIFFEENASSKI 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1080980409 269 METVSKESGVSIYK-KPIYSDEiSKEGGVADTYLKYLEYNLDVLTDGL 315
Cdd:cd01017   235 AETLAKETGAKLLVlNPLETLT-KEEIDDGKDYFSLMKENLETLKRAL 281
TroA cd01016
Metal binding protein TroA. These proteins have been shown to function as initial receptors in ...
40-315 1.99e-55

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: 181.41  E-value: 1.99e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080980409  40 KIKVVTSFSMIDDMVKEIGGEHVEVKNLVPTGTDPHDYDPKPDDIKHISSADLVFYNGLNLEGgSKGWLFKALESSdfsk 119
Cdd:cd01016     1 KPNVVTTTGMIADAVENIGGDHVEVTGLMGPGVDPHLYKATAGDVEKLQNADVVFYNGLHLEG-KMSDVLSKLGSS---- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080980409 120 ENAIKTSEGVKPKYIKDEDGKKEVNPHAFIDPKVGEKMIKNITKSLSERNPKNKDYYKENEKAYLKKLHNIEDDYEKQLG 199
Cdd:cd01016    76 KSVIALEDTLDRSQLILDEEEGTYDPHIWFDVKLWKYAVKAVAEVLSEKLPEHKDEFQANSEAYVEELDSLDAYAKKKIA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080980409 200 DIPKKDRVFVASEQAFQYLTDRYDLKEGYIWAIDTDENGSPEQIKDLVKFIDKNEPSHLFVESNVDKRPMETV---SKES 276
Cdd:cd01016   156 EIPEQQRVLVTAHDAFGYFGRAYGFEVKGLQGISTDSEAGLRDINELVDLIVERKIKAIFVESSVNQKSIEALqdaVKAR 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1080980409 277 GVSI-YKKPIYSDEISKEGGVADTYLKYLEYNLDVLTDGL 315
Cdd:cd01016   236 GHDVqIGGELYSDAMGEEGTSEGTYIGMFKHNVDTIVEAL 275
AztC NF040870
zinc ABC transporter substrate-binding protein AztC;
43-315 6.45e-54

zinc ABC transporter substrate-binding protein AztC;


Pssm-ID: 468807 [Multi-domain]  Cd Length: 277  Bit Score: 177.46  E-value: 6.45e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080980409  43 VVTSFSMIDDMVKEIGGEHVEVKNLVPTGTDPHDYDPKPDDIKHISSADLVFYNGLNLEGGskgwLFKALESSDFSKENA 122
Cdd:NF040870    1 VVVTTNILGDLARNVVGDRAEVTTLMKPDADPHSFEPSAADAAALERADLVVVNGLGLEEG----FLRHLIAASATGAPV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080980409 123 IKTSEGVKP-KYIKDEDGKKEV-----NPHAFIDPKVGEKMIKNITKSLSERNPKNKDYYKENEKAYLKKLHNIEDDYEK 196
Cdd:NF040870   77 VEVGDGVDPlPYPEGGHYHFEAgagppDPHFWTDPARARDAVDNIADAFCEADDGDCAAYRANAAAYRAELDELDAEMRE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080980409 197 QLGDIPKKDRVFVASEQAFQYLTDRYDLKegYIWAID----TDENGSPEQIKDLVKFIDKNEPSHLFVESNVDKRPMETV 272
Cdd:NF040870  157 AFAAIPADRRTLVTNHHVFGYLAERYGFR--VLGAVIpsgsTLASPSAADLASLARAIREAGVPAIFAESSQPPRLAEVL 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1080980409 273 SKESGVSIYKKPIYSDEISKEGGVADTYLKYLEYNLDVLTDGL 315
Cdd:NF040870  235 ASEAGLDVGVVELYSESLSEPDGGAATYLDMMRANAEAIVDGL 277
ZnuA cd01019
Zinc binding protein ZnuA. These proteins have been shown to function as initial receptors in ...
39-311 1.00e-36

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: 132.88  E-value: 1.00e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080980409  39 DKIKVVTSFSMIDDMVKEIGGEHVEVKNLVPTGTDPHDYDPKPDDIKHISSADLVFYNGLNLEggskGWLFKALESSDFS 118
Cdd:cd01019     2 AEASVLTSIKPLGFIAAAIMGGVGEVEVLVPPGASPHDYELRPSDARKLQEADLVVWIGPDLE----AFLDKVLQGRKKG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080980409 119 KENAIKTSEGVKPKYIKDEDGKKEV-----------------NPHAFIDPKVGEKMIKNITKSLSERNPKNKDYYKENEK 181
Cdd:cd01019    78 KVLTLAKLIDLKTLEDGASHGDHEHdhehahgehdgheegglDPHLWLSPENAAEVAQAVAEKLSALDPDNAATYAANLE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080980409 182 AYLKKLHNIEDDYEKQLGDIpkKDRVFVASEQAFQYLTDRYDLKEGYIWAIDTDENGSPEQIKDLVKFIDKNEPSHLFVE 261
Cdd:cd01019   158 AFNARLAELDATIKERLAPV--KTKPFFVFHDAYGYFEKRYGLTQAGVFTIDPEIDPGAKRLAKIRKEIKEKGATCVFAE 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1080980409 262 SNVDKRPMETVSKESGVsiyKKPIYSDEISKEGGVADTYLKYLEYNLDVL 311
Cdd:cd01019   236 PQFHPKIAETLAEGTGA---KVGELDPLGGLIELGKNSYVNFLRNLADSL 282
TroA_b cd01020
Metal binding protein TroA_b. These proteins are predicted to function as initial receptors ...
39-262 1.44e-32

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: 121.39  E-value: 1.44e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080980409  39 DKIKVVTSFSMIDDMVKEIGGEHVEVKNLV-PTGTDPHDYDPKPDDIKHISSADLVFYNGlnleGGSKGWLFKALESSDf 117
Cdd:cd01020     1 GKINVVASTNFWGSVAEAVGGDHVEVTSIItNPDVDPHDFEPTPTDAAKVSTADIVVYNG----GGYDPWMTKLLADTK- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080980409 118 skeNAIKTSEGVKPKYIKDEDgkkevNPHAFIDPKVGEKMIKNITKSLSERNPKNKDYYKENEKAYLKKLhnieDDYEKQ 197
Cdd:cd01020    76 ---DVIVIAADLDGHDDKEGD-----NPHLWYDPETMSKVANALADALVKADPDNKKYYQANAKKFVASL----KPLAAK 143
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1080980409 198 LGDIPKK--DRVFVASEQAFQYLTDRYDLKE----GYIWAIDTDENGSPEQIKDLVKFIDKNEPSHLFVES 262
Cdd:cd01020   144 IAELSAKykGAPVAATEPVFDYLLDALGMKErtpkGYTATTESETEPSPADIAAFQNAIKNRQIDALIVNP 214
ZntC cd01018
Metal binding protein ZntC. These proteins are predicted to function as initial receptors in ...
39-282 9.49e-31

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: 116.69  E-value: 9.49e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080980409  39 DKIKVVTSFSMIDDMVKEIGGEHVEVKNLVPTGTDPHDYDPKPDDIKHISSADLVFYNGLnleGGSKGWLFKALesSDFS 118
Cdd:cd01018     1 DKPTVAVSIEPQKYFVEKIAGDTVDVVVLVPPGSNPHTYEPKPQQMKKLSEADLYFRIGL---GFEEVWLERFR--SNNP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080980409 119 KENAIKTSEGVKPKYIKDEDGKKEV----------NPHAFIDPKVGEKMIKNITKSLSERNPKNKDYYKENEKAYLKKLH 188
Cdd:cd01018    76 KMQVVNMSKGITLIPMADHHHHHHGehehhhhgnyDPHIWLSPANAKIMAENIYEALAELDPQNATYYQANLDALLAELD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080980409 189 NIEDDYEKQLGdiPKKDRVFVASEQAFQYLTDRYDLKEgyiwaIDTDENG---SPEQIKDLVKFIDKNEPSHLFVESNVD 265
Cdd:cd01018   156 ALDSEIRTILS--KLKQRAFMVYHPAWGYFARDYGLTQ-----IPIEEEGkepSPADLKRLIDLAKEKGVRVVFVQPQFS 228
                         250
                  ....*....|....*..
gi 1080980409 266 KRPMETVSKESGVSIYK 282
Cdd:cd01018   229 TKSAEAIAREIGAKVVT 245
TroA_c cd01145
Periplasmic binding protein TroA_c. These proteins are predicted to function as initial ...
43-225 1.56e-27

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: 106.43  E-value: 1.56e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080980409  43 VVTSFSMIDDMVKEIGGEHVEVKNLVPTGTDPHDYDPKPDDIKHISSADLVFYNGLNLEggskGWLFKALE-SSDFSKEN 121
Cdd:cd01145     5 VVVTFPDLKDLVREVAGDAVIVSALTPPGVDPHQYQLKPSDIAKMRKADLVVTSGHELE----GFEPKLAElSSNSKVQP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080980409 122 AIKTSEGVKPKYIKDE----DGKKEVNPHAFIDPKVGEKMIKNITKSLSERNPKNKDYYKENEKAYLKKLHNIEDDYEKQ 197
Cdd:cd01145    81 GIKILIEDSDTVGMVDramgDYHGKGNPHVWLDPNNAPALAKALADALIELDPSEQEEYKENLRVFLAKLNKLLREWERQ 160
                         170       180
                  ....*....|....*....|....*...
gi 1080980409 198 LGdiPKKDRVFVASEQAFQYLTDRYDLK 225
Cdd:cd01145   161 FE--GLKGIQVVAYHPSYQYLADWLGIE 186
ZnuA COG4531
ABC-type Zn2+ transport system, periplasmic component/surface adhesin ZnuA [Inorganic ion ...
42-280 1.90e-23

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: 97.59  E-value: 1.90e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080980409  42 KVVTSFSMIDDMVKEIGGEHVEVKNLVPTGTDPHDYDPKPDDIKHISSADLVFYNGLNLEggskGWLFKALESSDFSKEN 121
Cdd:COG4531    11 RVVTSIKPLHSLVAAVMDGVGEPELLLPPGASPHDYALRPSDARALQDADLVFWVGPDLE----PFLEKPLETLAPDAKV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080980409 122 -AIKTSEGVKPKYIK------------------------DEDGKKEVNPHAFIDPKVGEKMIKNITKSLSERNPKNKDYY 176
Cdd:COG4531    87 vELLELPGLTLLPFReggdfehhdhhdehhhhhhhhddhHDHHHGGYDPHLWLSPENAKAWAAAIADALSELDPENAATY 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080980409 177 KENEKAYLKKLHNIEDDYEKQLGdiPKKDRVFVASEQAFQYLTDRYDLK-EGYIwAIDTDENGSPEQIKDLVKFIDKNEP 255
Cdd:COG4531   167 QANAAAFEARLDALDAEIAAQLA--PVKGKPFFVFHDAYQYFEKRFGLNaLGAI-TLNPEIQPGAKRLAEIREKLKELGA 243
                         250       260
                  ....*....|....*....|....*
gi 1080980409 256 SHLFVESNVDKRPMETVSKESGVSI 280
Cdd:COG4531   244 VCVFAEPQFNPALVETVAEGTGVRT 268
znuA PRK09545
zinc ABC transporter substrate-binding protein ZnuA;
43-225 6.81e-14

zinc ABC transporter substrate-binding protein ZnuA;


Pssm-ID: 236558 [Multi-domain]  Cd Length: 311  Bit Score: 70.81  E-value: 6.81e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080980409  43 VVTSF-------SMIDDMVKEiggehVEVknLVPTGTDPHDYDPKPDDIKHISSADLVFYNGLNLEggskGWLFKALESS 115
Cdd:PRK09545   27 VVTSIkplgfiaSAIADGVTE-----TEV--LLPDGASPHDYSLRPSDVKRLQSADLVVWVGPEME----AFLEKPVSKL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080980409 116 DFSKENAIKTSEGVKPKYIKDEDGKK--------------------EVNPHAFIDPKVGEKMIKNITKSLSERNPKNKDY 175
Cdd:PRK09545   96 PENKQVTIAQLPDVKPLLMKGAHDDHhdddhdhagheksdedhhhgEYNMHIWLSPEIARATAVAIHDKLVELMPQSKAK 175
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1080980409 176 YKENEKAYLKKLHNIEDDYEKQLGdiPKKDRVFVASEQAFQYLTDRYDLK 225
Cdd:PRK09545  176 LDANLKDFEAQLAQTDKQIGNQLA--PVKGKGYFVFHDAYGYFEKHYGLT 223
TroA-like cd00636
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ...
42-211 5.84e-07

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


Pssm-ID: 238347 [Multi-domain]  Cd Length: 148  Bit Score: 48.32  E-value: 5.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080980409  42 KVVTSFSMIDDMVKEIGGEHVEVKNLVPTGTD-------------PHDYDPKPDDIKHIsSADLVFYNGLNLEggskGWL 108
Cdd:cd00636     2 RVVALDPGATELLLALGGDDKPVGVADPSGYPpeakallekvpdvGHGYEPNLEKIAAL-KPDLIIANGSGLE----AWL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080980409 109 fkalessDFSKENAIKTsegvkpkyikdedgkKEVNPHAFIDPKVGEKMIKNITKSLSernpknkdyYKENEKAYLKKLH 188
Cdd:cd00636    77 -------DKLSKIAIPV---------------VVVDEASELSLENIKESIRLIGKALG---------KEENAEELIAELD 125
                         170       180
                  ....*....|....*....|...
gi 1080980409 189 NIEDDYEKQLGDIPKKDRVFVAS 211
Cdd:cd00636   126 ARLAELRAKLAKIPKKKVSLVVG 148
NlpA COG1464
ABC-type metal ion transport system, periplasmic component/surface antigen [Inorganic ion ...
1-57 5.09e-03

ABC-type metal ion transport system, periplasmic component/surface antigen [Inorganic ion transport and metabolism];


Pssm-ID: 441073 [Multi-domain]  Cd Length: 270  Bit Score: 37.78  E-value: 5.09e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1080980409   1 MKKVILFLFTITLSVVLAACSNGDKDGDSDkelesvDKDKIKVVTSFSMIDDMVKEI 57
Cdd:COG1464     1 MKKLLALLLALALALALAACGSSSAAAAAA------DKKTIKVGATPGPHAEILEVV 51
 
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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