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Conserved domains on  [gi|446477776|ref|WP_000555630|]
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MULTISPECIES: iron/manganese ABC transporter substrate-binding protein SitA [Enterobacteriaceae]

Protein Classification

metal ABC transporter substrate-binding protein( domain architecture ID 10100136)

metal ABC transporter substrate-binding lipoprotein functions as the initial receptor in ABC transport of metal ions and as surface adhesin in some eubacterial species

Gene Ontology:  GO:0046872|GO:0030001

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PsaA cd01137
Metal binding protein PsaA. These proteins have been shown to function as initial receptors ...
 14-298 1.26e-149

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: 420.92  E-value: 1.26e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446477776  14 LALTCSIAFQASATEKFKVITTFTIIADMAKNVAGDAAEVSSITKPGAEIHEYQPTPGDIKRAQGAQLILANGMNLELWF 93
Cdd:cd01137    2 AACASLGSSPATAASKLKVVATFSILADIARNIAGDRVNVTSIVPPGADPHEYEPTPSDIKKLSKADLILYNGLNLEPWL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446477776  94 QRFYQHLNG-VPEVIVSSGVTPVGITEGPYEGKPNPHAWMSPDNALIYVDNIRDALIKYDPANAQTYQRNADTYKAKITQ 172
Cdd:cd01137   82 ERLVKNAGKdVPVVAVSEGIDPIPLEEGHYKGKPDPHAWMSPKNAIIYVKNIAKALSEADPANAETYQKNAAAYKAKLKA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446477776 173 TLAPLRKQITELPENQRWMVTSEGAFSYLARDLGLKELYLWPINADQQGTPQQVRKVVDIVKKNHIPAVFSESTISDKPA 252
Cdd:cd01137  162 LDEWAKAKFATIPAEKRKLVTSEGAFSYFAKAYGLKEAYLWPINTEEEGTPKQVATLIEQVKKEKVPAVFVESTVNDRLM 241

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 446477776 253 RQVARETGAHYGGVLYVDSLSTENGPVPTYIDLLKVTTSTLVQGIK 298
Cdd:cd01137  242 KQVAKETGAKIGGQLYTDSLSEKGGPADTYLDMMEHNLDTIVEGLG 287
 
Name Accession Description Interval E-value
PsaA cd01137
Metal binding protein PsaA. These proteins have been shown to function as initial receptors ...
 14-298 1.26e-149

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: 420.92  E-value: 1.26e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446477776  14 LALTCSIAFQASATEKFKVITTFTIIADMAKNVAGDAAEVSSITKPGAEIHEYQPTPGDIKRAQGAQLILANGMNLELWF 93
Cdd:cd01137    2 AACASLGSSPATAASKLKVVATFSILADIARNIAGDRVNVTSIVPPGADPHEYEPTPSDIKKLSKADLILYNGLNLEPWL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446477776  94 QRFYQHLNG-VPEVIVSSGVTPVGITEGPYEGKPNPHAWMSPDNALIYVDNIRDALIKYDPANAQTYQRNADTYKAKITQ 172
Cdd:cd01137   82 ERLVKNAGKdVPVVAVSEGIDPIPLEEGHYKGKPDPHAWMSPKNAIIYVKNIAKALSEADPANAETYQKNAAAYKAKLKA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446477776 173 TLAPLRKQITELPENQRWMVTSEGAFSYLARDLGLKELYLWPINADQQGTPQQVRKVVDIVKKNHIPAVFSESTISDKPA 252
Cdd:cd01137  162 LDEWAKAKFATIPAEKRKLVTSEGAFSYFAKAYGLKEAYLWPINTEEEGTPKQVATLIEQVKKEKVPAVFVESTVNDRLM 241

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 446477776 253 RQVARETGAHYGGVLYVDSLSTENGPVPTYIDLLKVTTSTLVQGIK 298
Cdd:cd01137  242 KQVAKETGAKIGGQLYTDSLSEKGGPADTYLDMMEHNLDTIVEGLG 287
ZnuA COG0803
ABC-type Zn uptake system ZnuABC, Zn-binding component ZnuA [Inorganic ion transport and ...
 1-289 5.13e-118

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: 340.68  E-value: 5.13e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446477776   1 MHSIKKVTMLLGGLALTCSIAFQASATEKFKVITTFTIIADMAKNVAGDAAEVSSITKPGAEIHEYQPTPGDIKRAQGAQ 80
Cdd:COG0803    1 MKRLLLALLLLAALLLAGCSAAASSAAGKLKVVATFSPLADLAKQIGGDKVEVTSLVPPGADPHDYEPTPSDIAKLAKAD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446477776  81 LILANGMNLELWFQRFYQHLN--GVPEVIVSSGVTPVGITEGPYEGKPNPHAWMSPDNALIYVDNIRDALIKYDPANAQT 158
Cdd:COG0803   81 LVVYNGLGLEGWLDKLLEAAGnpGVPVVDASEGIDLLELEEGHDHGEPDPHVWLDPKNAKKVAENIADALAELDPANAAY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446477776 159 YQRNADTYKAKITQTLAPLRKQITELPenQRWMVTSEGAFSYLARDLGLKELYLWPINADQQGTPQQVRKVVDIVKKNHI 238
Cdd:COG0803  161 YEANAAAYLAELDALDAEIKAKLAAIP--GRKLVTSHDAFGYLARAYGLEVVAIQGISPGSEPSPADLAELIDLIKEEGV 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446477776 239 PAVFSESTISDKPARQVARETGAHyggVLYVDSLSTENGPVPTYIDLLKVT 289
Cdd:COG0803  239 KAIFVESQVSPKLAETLAEETGVK---VLYLDSLGGPGGPGDTYLDMMRHN 286
ZnuA pfam01297
Zinc-uptake complex component A periplasmic; ZnuA includes periplasmic solute binding proteins ...
 32-296 4.82e-111

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: 322.58  E-value: 4.82e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446477776   32 VITTFTIIADMAKNVAGDAAEVSSITKPGAEIHEYQPTPGDIKRAQGAQLILANGMNLELWFQRFYQHLNGVPEVIVSSG 111
Cdd:pfam01297   1 VVATTYPLADLAKQIGGDRVEVTSLVPPGADPHDYEPTPSDIAALSDADLVVYNGLGLEPWLDKLLEALPNKKVVDASEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446477776  112 VTPvGITEGPYEGKP------NPHAWMSPDNALIYVDNIRDALIKYDPANAQTYQRNADTYKAKITQTLAPLRKQITELP 185
Cdd:pfam01297  81 VEL-LDEEGEEEDHDghdhgyDPHVWLDPKNAKKMAENIADALSELDPANAATYEANAAAYLAELDALDAEIKEQLASIP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446477776  186 ENQRWMVTSEGAFSYLARDLGLKELYLWPINADQQGTPQQVRKVVDIVKKNHIPAVFSESTISDKPARQVARETGAHYGG 265
Cdd:pfam01297 160 EKTRKLVTSHDAFGYLARAYGLEQVGIQGVSPESEPSAADLAELIDLIKEKKVKAIFVEPQVSPKLAETVAKETGVKVLG 239

                         250       260       270
                  ....*....|....*....|....*....|.
gi 446477776  266 VLYVDSLSTENGPVpTYIDLLKVTTSTLVQG 296
Cdd:pfam01297 240 PLYTDSLGEPGGGA-TYLDLMRHNLDTLAEA 269
anch_rpt_subst TIGR03772
anchored repeat ABC transporter, substrate-binding protein; Members of this protein family are ...
 124-293 4.19e-27

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: 109.95  E-value: 4.19e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446477776  124 GKPNPHAWMSPDNALIYVDNIRDALIKYDPANAQTYQRNADTYKAKITQTLAPLRKQITELPENQRWMVTSEGAFSYLAR 203
Cdd:TIGR03772 307 GEIDPHLWHNVKNAIAYVEVIRDKLIEVDPRGAQAYRSNASAYIHRLERLDTYVRRTIATIPPSRRHLITTHDAYSYLGQ 386

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446477776  204 DLGLKELYLWPINADQQGTPQQVRKVVDIVKKNHIPAVFSESTISDKPA--RQVARETGAHYGGVlYVDSLSTEngpVPT 281
Cdd:TIGR03772 387 AYGLNIAGFVTPNPAVEPSLADRRRLTRTIENLKVPAVFLEPNLAARSTtlNEIADELGVRVCAI-YGDTFDDD---VTN 462

                         170
                  ....*....|..
gi 446477776  282 YIDLLKVTTSTL 293
Cdd:TIGR03772 463 YVDLMRFNADSL 474
znuA PRK09545
zinc ABC transporter substrate-binding protein ZnuA;
1-264 2.75e-07

zinc ABC transporter substrate-binding protein ZnuA;


Pssm-ID: 236558 [Multi-domain]  Cd Length: 311  Bit Score: 51.16  E-value: 2.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446477776   1 MHSIKKVTMLLGGLALTCSIAfQASATekfkVITTFTIIADMAKNVAGDAAEVSSITKPGAEIHEYQPTPGDIKRAQGAQ 80
Cdd:PRK09545   1 LHKKTLLFAALLAALLGGATQ-AANAA----VVTSIKPLGFIASAIADGVTETEVLLPDGASPHDYSLRPSDVKRLQSAD 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446477776  81 LILANGMNLELWFQRFYQHL--NGVPEVIVSSGVTPVGIT--------------------EGPYEGKPNPHAWMSPDNAL 138
Cdd:PRK09545  76 LVVWVGPEMEAFLEKPVSKLpeNKQVTIAQLPDVKPLLMKgahddhhdddhdhagheksdEDHHHGEYNMHIWLSPEIAR 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446477776 139 IYVDNIRDALIKYDPANAQTYQRNADTYKAKITQTlaplRKQITelpeNQRWMVTSEG------AFSYLARDLGLKELYL 212
Cdd:PRK09545 156 ATAVAIHDKLVELMPQSKAKLDANLKDFEAQLAQT----DKQIG----NQLAPVKGKGyfvfhdAYGYFEKHYGLTPLGH 227

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446477776 213 WPINADQQGTPQ---QVRKVVDIVKKNhipAVFSESTISDKPARQVARETGAHYG 264
Cdd:PRK09545 228 FTVNPEIQPGAQrlhEIRTQLVEQKAT---CVFAEPQFRPAVIESVAKGTSVRMG 279
 
Name Accession Description Interval E-value
PsaA cd01137
Metal binding protein PsaA. These proteins have been shown to function as initial receptors ...
 14-298 1.26e-149

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: 420.92  E-value: 1.26e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446477776  14 LALTCSIAFQASATEKFKVITTFTIIADMAKNVAGDAAEVSSITKPGAEIHEYQPTPGDIKRAQGAQLILANGMNLELWF 93
Cdd:cd01137    2 AACASLGSSPATAASKLKVVATFSILADIARNIAGDRVNVTSIVPPGADPHEYEPTPSDIKKLSKADLILYNGLNLEPWL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446477776  94 QRFYQHLNG-VPEVIVSSGVTPVGITEGPYEGKPNPHAWMSPDNALIYVDNIRDALIKYDPANAQTYQRNADTYKAKITQ 172
Cdd:cd01137   82 ERLVKNAGKdVPVVAVSEGIDPIPLEEGHYKGKPDPHAWMSPKNAIIYVKNIAKALSEADPANAETYQKNAAAYKAKLKA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446477776 173 TLAPLRKQITELPENQRWMVTSEGAFSYLARDLGLKELYLWPINADQQGTPQQVRKVVDIVKKNHIPAVFSESTISDKPA 252
Cdd:cd01137  162 LDEWAKAKFATIPAEKRKLVTSEGAFSYFAKAYGLKEAYLWPINTEEEGTPKQVATLIEQVKKEKVPAVFVESTVNDRLM 241

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 446477776 253 RQVARETGAHYGGVLYVDSLSTENGPVPTYIDLLKVTTSTLVQGIK 298
Cdd:cd01137  242 KQVAKETGAKIGGQLYTDSLSEKGGPADTYLDMMEHNLDTIVEGLG 287
ZnuA COG0803
ABC-type Zn uptake system ZnuABC, Zn-binding component ZnuA [Inorganic ion transport and ...
 1-289 5.13e-118

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: 340.68  E-value: 5.13e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446477776   1 MHSIKKVTMLLGGLALTCSIAFQASATEKFKVITTFTIIADMAKNVAGDAAEVSSITKPGAEIHEYQPTPGDIKRAQGAQ 80
Cdd:COG0803    1 MKRLLLALLLLAALLLAGCSAAASSAAGKLKVVATFSPLADLAKQIGGDKVEVTSLVPPGADPHDYEPTPSDIAKLAKAD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446477776  81 LILANGMNLELWFQRFYQHLN--GVPEVIVSSGVTPVGITEGPYEGKPNPHAWMSPDNALIYVDNIRDALIKYDPANAQT 158
Cdd:COG0803   81 LVVYNGLGLEGWLDKLLEAAGnpGVPVVDASEGIDLLELEEGHDHGEPDPHVWLDPKNAKKVAENIADALAELDPANAAY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446477776 159 YQRNADTYKAKITQTLAPLRKQITELPenQRWMVTSEGAFSYLARDLGLKELYLWPINADQQGTPQQVRKVVDIVKKNHI 238
Cdd:COG0803  161 YEANAAAYLAELDALDAEIKAKLAAIP--GRKLVTSHDAFGYLARAYGLEVVAIQGISPGSEPSPADLAELIDLIKEEGV 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446477776 239 PAVFSESTISDKPARQVARETGAHyggVLYVDSLSTENGPVPTYIDLLKVT 289
Cdd:COG0803  239 KAIFVESQVSPKLAETLAEETGVK---VLYLDSLGGPGGPGDTYLDMMRHN 286
ZnuA pfam01297
Zinc-uptake complex component A periplasmic; ZnuA includes periplasmic solute binding proteins ...
 32-296 4.82e-111

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: 322.58  E-value: 4.82e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446477776   32 VITTFTIIADMAKNVAGDAAEVSSITKPGAEIHEYQPTPGDIKRAQGAQLILANGMNLELWFQRFYQHLNGVPEVIVSSG 111
Cdd:pfam01297   1 VVATTYPLADLAKQIGGDRVEVTSLVPPGADPHDYEPTPSDIAALSDADLVVYNGLGLEPWLDKLLEALPNKKVVDASEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446477776  112 VTPvGITEGPYEGKP------NPHAWMSPDNALIYVDNIRDALIKYDPANAQTYQRNADTYKAKITQTLAPLRKQITELP 185
Cdd:pfam01297  81 VEL-LDEEGEEEDHDghdhgyDPHVWLDPKNAKKMAENIADALSELDPANAATYEANAAAYLAELDALDAEIKEQLASIP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446477776  186 ENQRWMVTSEGAFSYLARDLGLKELYLWPINADQQGTPQQVRKVVDIVKKNHIPAVFSESTISDKPARQVARETGAHYGG 265
Cdd:pfam01297 160 EKTRKLVTSHDAFGYLARAYGLEQVGIQGVSPESEPSAADLAELIDLIKEKKVKAIFVEPQVSPKLAETVAKETGVKVLG 239

                         250       260       270
                  ....*....|....*....|....*....|.
gi 446477776  266 VLYVDSLSTENGPVpTYIDLLKVTTSTLVQG 296
Cdd:pfam01297 240 PLYTDSLGEPGGGA-TYLDLMRHNLDTLAEA 269
AdcA cd01017
Metal binding protein AdcA. These proteins have been shown to function in the ABC uptake of ...
 27-298 2.79e-63

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: 201.37  E-value: 2.79e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446477776  27 TEKFKVITTFTIIADMAKNVAGDAAEVSSITKPGAEIHEYQPTPGDIKRAQGAQLILANGMNLELWFQRFYQHLNGvPEV 106
Cdd:cd01017    1 SGKLKVVTTFYPLYEFTKAIGGDKADVKLIIPAGTEPHDFEPSPKDIARIADADVFVYNGLGMETWAEKVLKSLQN-KKL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446477776 107 IV---SSGVTPVGITEGPYE---------GKPNPHAWMSPDNALIYVDNIRDALIKYDPANAQTYQRNADTYKAKITQtl 174
Cdd:cd01017   80 KVveaSKGIKLLKAGGAEHDhdhshshhhGDYDPHVWLSPVLAIQQVENIKDALIKLDPDNKEYYEKNAAAYAKKLEA-- 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446477776 175 apLRKQITELPEN--QRWMVTSEGAFSYLARDLGLKELYLWPINADQQGTPQQVRKVVDIVKKNHIPAVFSESTISDKPA 252
Cdd:cd01017  158 --LDQEYRAKLAKakGKTFVTQHAAFGYLARRYGLKQIAIVGVSPEVEPSPKQLAELVEFVKKSDVKYIFFEENASSKIA 235

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 446477776 253 RQVARETGAHyggVLYVDSLST----ENGPVPTYIDLLKVTTSTLVQGIK 298
Cdd:cd01017  236 ETLAKETGAK---LLVLNPLETltkeEIDDGKDYFSLMKENLETLKRALK 282
TroA cd01016
Metal binding protein TroA. These proteins have been shown to function as initial receptors in ...
 29-298 9.24e-46

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: 155.98  E-value: 9.24e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446477776  29 KFKVITTFTIIADMAKNVAGDAAEVSSITKPGAEIHEYQPTPGDIKRAQGAQLILANGMNLELWFQRFYQHLNGVPEVI- 107
Cdd:cd01016    1 KPNVVTTTGMIADAVENIGGDHVEVTGLMGPGVDPHLYKATAGDVEKLQNADVVFYNGLHLEGKMSDVLSKLGSSKSVIa 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446477776 108 VSSGVTPVGITEGPYEGKPNPHAWMSPDNALIYVDNIRDALIKYDPANAQTYQRNADTYKAKITQTLAPLRKQITELPEN 187
Cdd:cd01016   81 LEDTLDRSQLILDEEEGTYDPHIWFDVKLWKYAVKAVAEVLSEKLPEHKDEFQANSEAYVEELDSLDAYAKKKIAEIPEQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446477776 188 QRWMVTSEGAFSYLARDLGLKELYLWPINADQQGTPQQVRKVVDIVKKNHIPAVFSESTISDKPARQV---ARETG--AH 262
Cdd:cd01016  161 QRVLVTAHDAFGYFGRAYGFEVKGLQGISTDSEAGLRDINELVDLIVERKIKAIFVESSVNQKSIEALqdaVKARGhdVQ 240

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 446477776 263 YGGVLYVDSLSTENGPVPTYIDLLKVTTSTLVQGIK 298
Cdd:cd01016  241 IGGELYSDAMGEEGTSEGTYIGMFKHNVDTIVEALK 276
ZntC cd01018
Metal binding protein ZntC. These proteins are predicted to function as initial receptors in ...
 43-273 9.11e-40

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: 139.80  E-value: 9.11e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446477776  43 AKNVAGDAAEVSSITKPGAEIHEYQPTPGDIKRAQGAQLILANGMNLE-LWFQRFYQHLNGVPEVIVSSGVTPVGIT--- 118
Cdd:cd01018   16 VEKIAGDTVDVVVLVPPGSNPHTYEPKPQQMKKLSEADLYFRIGLGFEeVWLERFRSNNPKMQVVNMSKGITLIPMAdhh 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446477776 119 -------EGPYEGKPNPHAWMSPDNALIYVDNIRDALIKYDPANAQTYQRNADTYKAKITQTLAPLRKQITELPenQRWM 191
Cdd:cd01018   96 hhhhgehEHHHHGNYDPHIWLSPANAKIMAENIYEALAELDPQNATYYQANLDALLAELDALDSEIRTILSKLK--QRAF 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446477776 192 VTSEGAFSYLARDLGLKELylwPINAD-QQGTPQQVRKVVDIVKKNHIPAVFSESTISDKPARQVARETGAHyggVLYVD 270
Cdd:cd01018  174 MVYHPAWGYFARDYGLTQI---PIEEEgKEPSPADLKRLIDLAKEKGVRVVFVQPQFSTKSAEAIAREIGAK---VVTID 247


                 ...
gi 446477776 271 SLS 273
Cdd:cd01018  248 PLA 250
ZnuA cd01019
Zinc binding protein ZnuA. These proteins have been shown to function as initial receptors in ...
 27-261 3.91e-34

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: 125.56  E-value: 3.91e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446477776  27 TEKFKVITTFTIIADMAKNVAGDAAEVSSITKPGAEIHEYQPTPGDIKRAQGAQLILANGMNLELWFQRFYQHLNGVpEV 106
Cdd:cd01019    1 AAEASVLTSIKPLGFIAAAIMGGVGEVEVLVPPGASPHDYELRPSDARKLQEADLVVWIGPDLEAFLDKVLQGRKKG-KV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446477776 107 IVSSGVTPV-----GITEGPYEGKP---------------NPHAWMSPDNALIYVDNIRDALIKYDPANAQTYQRNADTY 166
Cdd:cd01019   80 LTLAKLIDLktledGASHGDHEHDHehahgehdgheegglDPHLWLSPENAAEVAQAVAEKLSALDPDNAATYAANLEAF 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446477776 167 KAKitqtLAPLRKQITE--LPENQRWMVTSEGAFSYLARDLGLKELYLWPINADQQGTPQQVRKVVDIVKKNHIPAVFSE 244
Cdd:cd01019  160 NAR----LAELDATIKErlAPVKTKPFFVFHDAYGYFEKRYGLTQAGVFTIDPEIDPGAKRLAKIRKEIKEKGATCVFAE 235

                        250
                 ....*....|....*..
gi 446477776 245 STISDKPARQVARETGA 261
Cdd:cd01019  236 PQFHPKIAETLAEGTGA 252
anch_rpt_subst TIGR03772
anchored repeat ABC transporter, substrate-binding protein; Members of this protein family are ...
 124-293 4.19e-27

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: 109.95  E-value: 4.19e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446477776  124 GKPNPHAWMSPDNALIYVDNIRDALIKYDPANAQTYQRNADTYKAKITQTLAPLRKQITELPENQRWMVTSEGAFSYLAR 203
Cdd:TIGR03772 307 GEIDPHLWHNVKNAIAYVEVIRDKLIEVDPRGAQAYRSNASAYIHRLERLDTYVRRTIATIPPSRRHLITTHDAYSYLGQ 386

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446477776  204 DLGLKELYLWPINADQQGTPQQVRKVVDIVKKNHIPAVFSESTISDKPA--RQVARETGAHYGGVlYVDSLSTEngpVPT 281
Cdd:TIGR03772 387 AYGLNIAGFVTPNPAVEPSLADRRRLTRTIENLKVPAVFLEPNLAARSTtlNEIADELGVRVCAI-YGDTFDDD---VTN 462

                         170
                  ....*....|..
gi 446477776  282 YIDLLKVTTSTL 293
Cdd:TIGR03772 463 YVDLMRFNADSL 474
ZnuA COG4531
ABC-type Zn2+ transport system, periplasmic component/surface adhesin ZnuA [Inorganic ion ...
 19-264 1.08e-26

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: 106.07  E-value: 1.08e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446477776  19 SIAFQASAtekfKVITTFTIIADMAKNVAGDAAEVSSITKPGAEIHEYQPTPGDIKRAQGAQLILANGMNLELWFQRFYQ 98
Cdd:COG4531    3 SAAAAAAP----RVVTSIKPLHSLVAAVMDGVGEPELLLPPGASPHDYALRPSDARALQDADLVFWVGPDLEPFLEKPLE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446477776  99 HLNG---VPEVIVSSGVTPVGITEGP------------------------YEGKPNPHAWMSPDNALIYVDNIRDALIKY 151
Cdd:COG4531   79 TLAPdakVVELLELPGLTLLPFREGGdfehhdhhdehhhhhhhhddhhdhHHGGYDPHLWLSPENAKAWAAAIADALSEL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446477776 152 DPANAQTYQRNADTYKAKITQT-------LAPLRkqitelpeNQRWMVTSEgAFSYLARDLGLKELYLWPINADQQGTPQ 224
Cdd:COG4531  159 DPENAATYQANAAAFEARLDALdaeiaaqLAPVK--------GKPFFVFHD-AYQYFEKRFGLNALGAITLNPEIQPGAK 229

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 446477776 225 QVRKVVDIVKKNHIPAVFSESTISDKPARQVARETGAHYG 264
Cdd:COG4531  230 RLAEIREKLKELGAVCVFAEPQFNPALVETVAEGTGVRTG 269
TroA_b cd01020
Metal binding protein TroA_b. These proteins are predicted to function as initial receptors ...
 29-250 2.81e-26

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: 104.44  E-value: 2.81e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446477776  29 KFKVITTFTIIADMAKNVAGDAAEVSSI-TKPGAEIHEYQPTPGDIKRAQGAQLILANGMNLELWfqrFYQHLNGVPEVI 107
Cdd:cd01020    2 KINVVASTNFWGSVAEAVGGDHVEVTSIiTNPDVDPHDFEPTPTDAAKVSTADIVVYNGGGYDPW---MTKLLADTKDVI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446477776 108 VSSgvtpVGITEGPYEGKPNPHAWMSPDNALIYVDNIRDALIKYDPANAQTYQRNADTYKAKitqtLAPLRKQITELP-- 185
Cdd:cd01020   79 VIA----ADLDGHDDKEGDNPHLWYDPETMSKVANALADALVKADPDNKKYYQANAKKFVAS----LKPLAAKIAELSak 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446477776 186 -ENQRWMVTsEGAFSYLARDLGLKE----LYLWPINADQQGTPQQVRKVVDIVKKNHIPAVFSESTISDK 250
Cdd:cd01020  151 yKGAPVAAT-EPVFDYLLDALGMKErtpkGYTATTESETEPSPADIAAFQNAIKNRQIDALIVNPQQASS 219
TroA_c cd01145
Periplasmic binding protein TroA_c. These proteins are predicted to function as initial ...
 32-210 1.74e-25

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: 100.65  E-value: 1.74e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446477776  32 VITTFTIIADMAKNVAGDAAEVSSITKPGAEIHEYQPTPGDIKRAQGAQLILANGMNLELWFQRFyQHLNGVPEVI---- 107
Cdd:cd01145    5 VVVTFPDLKDLVREVAGDAVIVSALTPPGVDPHQYQLKPSDIAKMRKADLVVTSGHELEGFEPKL-AELSSNSKVQpgik 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446477776 108 ----VSSGVTPVGITEGPYEGKPNPHAWMSPDNALIYVDNIRDALIKYDPANAQTYQRNADTYKAKItQTLAPLRKQITE 183
Cdd:cd01145   84 ilieDSDTVGMVDRAMGDYHGKGNPHVWLDPNNAPALAKALADALIELDPSEQEEYKENLRVFLAKL-NKLLREWERQFE 162

                        170       180
                 ....*....|....*....|....*..
gi 446477776 184 lPENQRWMVTSEGAFSYLARDLGLKEL 210
Cdd:cd01145  163 -GLKGIQVVAYHPSYQYLADWLGIEVV 188
TroA-like cd00636
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ...
 31-194 3.61e-10

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: 57.57  E-value: 3.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446477776  31 KVITTFTIIADMAKNVAGDAAEVSSITKPGAEI-------------HEYQPTPGDIKRAQgAQLILANGMNLELWFQRFY 97
Cdd:cd00636    2 RVVALDPGATELLLALGGDDKPVGVADPSGYPPeakallekvpdvgHGYEPNLEKIAALK-PDLIIANGSGLEAWLDKLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446477776  98 QhlNGVPEVIVSSGVTpvgitegpyegkpnphawMSPDNALIYVDNIRDALIkydpanaqtYQRNADTYKAKITQTLAPL 177
Cdd:cd00636   81 K--IAIPVVVVDEASE------------------LSLENIKESIRLIGKALG---------KEENAEELIAELDARLAEL 131

                        170
                 ....*....|....*..
gi 446477776 178 RKQITELPENQRWMVTS 194
Cdd:cd00636  132 RAKLAKIPKKKVSLVVG 148
znuA PRK09545
zinc ABC transporter substrate-binding protein ZnuA;
1-264 2.75e-07

zinc ABC transporter substrate-binding protein ZnuA;


Pssm-ID: 236558 [Multi-domain]  Cd Length: 311  Bit Score: 51.16  E-value: 2.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446477776   1 MHSIKKVTMLLGGLALTCSIAfQASATekfkVITTFTIIADMAKNVAGDAAEVSSITKPGAEIHEYQPTPGDIKRAQGAQ 80
Cdd:PRK09545   1 LHKKTLLFAALLAALLGGATQ-AANAA----VVTSIKPLGFIASAIADGVTETEVLLPDGASPHDYSLRPSDVKRLQSAD 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446477776  81 LILANGMNLELWFQRFYQHL--NGVPEVIVSSGVTPVGIT--------------------EGPYEGKPNPHAWMSPDNAL 138
Cdd:PRK09545  76 LVVWVGPEMEAFLEKPVSKLpeNKQVTIAQLPDVKPLLMKgahddhhdddhdhagheksdEDHHHGEYNMHIWLSPEIAR 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446477776 139 IYVDNIRDALIKYDPANAQTYQRNADTYKAKITQTlaplRKQITelpeNQRWMVTSEG------AFSYLARDLGLKELYL 212
Cdd:PRK09545 156 ATAVAIHDKLVELMPQSKAKLDANLKDFEAQLAQT----DKQIG----NQLAPVKGKGyfvfhdAYGYFEKHYGLTPLGH 227

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446477776 213 WPINADQQGTPQ---QVRKVVDIVKKNhipAVFSESTISDKPARQVARETGAHYG 264
Cdd:PRK09545 228 FTVNPEIQPGAQrlhEIRTQLVEQKAT---CVFAEPQFRPAVIESVAKGTSVRMG 279
 
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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