|
Name |
Accession |
Description |
Interval |
E-value |
| PsaA |
cd01137 |
Metal binding protein PsaA. These proteins have been shown to function as initial receptors ... |
8-292 |
9.67e-139 |
|
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: 392.80 E-value: 9.67e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306047 8 FSVLLPLSFATAQAADKLQVVTSFSILDDMTHQVGGDHIQISNMVGPDADAHTYEPTPDDAKALLKAKVIIKNGLGFEPW 87
Cdd:cd01137 1 LAACASLGSSPATAASKLKVVATFSILADIARNIAGDRVNVTSIVPPGADPHEYEPTPSDIKKLSKADLILYNGLNLEPW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306047 88 LDRLVTSTETKATVVTASKGVLSHTMEE-DGETIPDPHAWHNLANTVIYVNNITKALIAADPANKADYEHNSQVYLKEIY 166
Cdd:cd01137 81 LERLVKNAGKDVPVVAVSEGIDPIPLEEgHYKGKPDPHAWMSPKNAIIYVKNIAKALSEADPANAETYQKNAAAYKAKLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306047 167 RLLAEAKAKFGALPPGNRRIVTSHDAFGYLGQAYGIEFLSPQGLSTEREPSAAEVATLITQIRKDKVKAVFMENIKDSRL 246
Cdd:cd01137 161 ALDEWAKAKFATIPAEKRKLVTSEGAFSYFAKAYGLKEAYLWPINTEEEGTPKQVATLIEQVKKEKVPAVFVESTVNDRL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 489306047 247 LQQIADESGAQIGGTLYSDALAAE-GPASTFTGLFEYNLNTLCAALS 292
Cdd:cd01137 241 MKQVAKETGAKIGGQLYTDSLSEKgGPADTYLDMMEHNLDTIVEGLG 287
|
|
| ZnuA |
pfam01297 |
Zinc-uptake complex component A periplasmic; ZnuA includes periplasmic solute binding proteins ... |
27-290 |
1.55e-104 |
|
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: 305.63 E-value: 1.55e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306047 27 VVTSFSILDDMTHQVGGDHIQISNMVGPDADAHTYEPTPDDAKALLKAKVIIKNGLGFEPWLDRLVTSTEtKATVVTASK 106
Cdd:pfam01297 1 VVATTYPLADLAKQIGGDRVEVTSLVPPGADPHDYEPTPSDIAALSDADLVVYNGLGLEPWLDKLLEALP-NKKVVDASE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306047 107 GVLSHTMEEDGETIP------DPHAWHNLANTVIYVNNITKALIAADPANKADYEHNSQVYLKEIYRLLAEAKAKFGALP 180
Cdd:pfam01297 80 GVELLDEEGEEEDHDghdhgyDPHVWLDPKNAKKMAENIADALSELDPANAATYEANAAAYLAELDALDAEIKEQLASIP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306047 181 PGNRRIVTSHDAFGYLGQAYGIEFLSPQGLSTEREPSAAEVATLITQIRKDKVKAVFMENIKDSRLLQQIADESGAQIGG 260
Cdd:pfam01297 160 EKTRKLVTSHDAFGYLARAYGLEQVGIQGVSPESEPSAADLAELIDLIKEKKVKAIFVEPQVSPKLAETVAKETGVKVLG 239
|
250 260 270
....*....|....*....|....*....|
gi 489306047 261 TLYSDALAAEGPASTFTGLFEYNLNTLCAA 290
Cdd:pfam01297 240 PLYTDSLGEPGGGATYLDLMRHNLDTLAEA 269
|
|
| ZnuA |
COG0803 |
ABC-type Zn uptake system ZnuABC, Zn-binding component ZnuA [Inorganic ion transport and ... |
1-283 |
4.55e-104 |
|
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: 304.86 E-value: 4.55e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306047 1 MRALLVLFSVLLPLSFA-----TAQAADKLQVVTSFSILDDMTHQVGGDHIQISNMVGPDADAHTYEPTPDDAKALLKAK 75
Cdd:COG0803 1 MKRLLLALLLLAALLLAgcsaaASSAAGKLKVVATFSPLADLAKQIGGDKVEVTSLVPPGADPHDYEPTPSDIAKLAKAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306047 76 VIIKNGLGFEPWLDRLVTSTE-TKATVVTASKGV-LSHTMEEDGETIPDPHAWHNLANTVIYVNNITKALIAADPANKAD 153
Cdd:COG0803 81 LVVYNGLGLEGWLDKLLEAAGnPGVPVVDASEGIdLLELEEGHDHGEPDPHVWLDPKNAKKVAENIADALAELDPANAAY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306047 154 YEHNSQVYLKEIYRLLAEAKAKFGALPpgNRRIVTSHDAFGYLGQAYGIEFLSPQGLSTEREPSAAEVATLITQIRKDKV 233
Cdd:COG0803 161 YEANAAAYLAELDALDAEIKAKLAAIP--GRKLVTSHDAFGYLARAYGLEVVAIQGISPGSEPSPADLAELIDLIKEEGV 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 489306047 234 KAVFMENIKDSRLLQQIADESGAQIggtLYSDAL-AAEGPASTFTGLFEYN 283
Cdd:COG0803 239 KAIFVESQVSPKLAETLAEETGVKV---LYLDSLgGPGGPGDTYLDMMRHN 286
|
|
| AztC |
NF040870 |
zinc ABC transporter substrate-binding protein AztC; |
27-291 |
1.45e-87 |
|
zinc ABC transporter substrate-binding protein AztC;
Pssm-ID: 468807 [Multi-domain] Cd Length: 277 Bit Score: 262.59 E-value: 1.45e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306047 27 VVTSFSILDDMTHQVGGDHIQISNMVGPDADAHTYEPTPDDAKALLKAKVIIKNGLGF-EPWLDRLVTSTETKATVVTAS 105
Cdd:NF040870 1 VVVTTNILGDLARNVVGDRAEVTTLMKPDADPHSFEPSAADAAALERADLVVVNGLGLeEGFLRHLIAASATGAPVVEVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306047 106 KGVL-------SHTMEEDGETIPDPHAWHNLANTVIYVNNITKALIAADPANKADYEHNSQVYLKEIYRLLAEAKAKFGA 178
Cdd:NF040870 81 DGVDplpypegGHYHFEAGAGPPDPHFWTDPARARDAVDNIADAFCEADDGDCAAYRANAAAYRAELDELDAEMREAFAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306047 179 LPPGNRRIVTSHDAFGYLGQAYGIEFLS---PQGlSTEREPSAAEVATLITQIRKDKVKAVFMENIKDSRLLQQIADESG 255
Cdd:NF040870 161 IPADRRTLVTNHHVFGYLAERYGFRVLGaviPSG-STLASPSAADLASLARAIREAGVPAIFAESSQPPRLAEVLASEAG 239
|
250 260 270
....*....|....*....|....*....|....*...
gi 489306047 256 AQIGGT-LYSDALAAE-GPASTFTGLFEYNLNTLCAAL 291
Cdd:NF040870 240 LDVGVVeLYSESLSEPdGGAATYLDMMRANAEAIVDGL 277
|
|
| anch_rpt_subst |
TIGR03772 |
anchored repeat ABC transporter, substrate-binding protein; Members of this protein family are ... |
122-292 |
7.70e-34 |
|
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: 128.44 E-value: 7.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306047 122 DPHAWHNLANTVIYVNNITKALIAADPANKADYEHNSQVYLKEIYRLLAEAKAKFGALPPGNRRIVTSHDAFGYLGQAYG 201
Cdd:TIGR03772 310 DPHLWHNVKNAIAYVEVIRDKLIEVDPRGAQAYRSNASAYIHRLERLDTYVRRTIATIPPSRRHLITTHDAYSYLGQAYG 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306047 202 IE---FLSPqglSTEREPSAAEVATLITQIRKDKVKAVFMEN--IKDSRLLQQIADESGAQIgGTLYSDALAAEGPasTF 276
Cdd:TIGR03772 390 LNiagFVTP---NPAVEPSLADRRRLTRTIENLKVPAVFLEPnlAARSTTLNEIADELGVRV-CAIYGDTFDDDVT--NY 463
|
170
....*....|....*.
gi 489306047 277 TGLFEYNLNTLCAALS 292
Cdd:TIGR03772 464 VDLMRFNADSLADCLG 479
|
|
| znuA |
PRK09545 |
zinc ABC transporter substrate-binding protein ZnuA; |
5-239 |
4.31e-08 |
|
zinc ABC transporter substrate-binding protein ZnuA;
Pssm-ID: 236558 [Multi-domain] Cd Length: 311 Bit Score: 53.47 E-value: 4.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306047 5 LVLFSVLLPLSFATAQAAdklqVVTSF--------SILDDMTH-QVggdhiqisnMVGPDADAHTYEPTPDDAKALLKAK 75
Cdd:PRK09545 9 AALLAALLGGATQAANAA----VVTSIkplgfiasAIADGVTEtEV---------LLPDGASPHDYSLRPSDVKRLQSAD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306047 76 VIIKNGLGFEPWLDRLVTSTETKATVVTAS----KGVLSHTMEEDGETIPDPHAWHNLA---------NTVIYVN-NITK 141
Cdd:PRK09545 76 LVVWVGPEMEAFLEKPVSKLPENKQVTIAQlpdvKPLLMKGAHDDHHDDDHDHAGHEKSdedhhhgeyNMHIWLSpEIAR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306047 142 A--------LIAADPANKADYEHNsqvyLKEIYRLLAEAKAKFGAL--PPGNRRIVTSHDAFGYLGQAYGiefLSPQGLS 211
Cdd:PRK09545 156 AtavaihdkLVELMPQSKAKLDAN----LKDFEAQLAQTDKQIGNQlaPVKGKGYFVFHDAYGYFEKHYG---LTPLGHF 228
|
250 260 270
....*....|....*....|....*....|.
gi 489306047 212 T---EREPSAAEVATLITQIRKDKVKAVFME 239
Cdd:PRK09545 229 TvnpEIQPGAQRLHEIRTQLVEQKATCVFAE 259
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PsaA |
cd01137 |
Metal binding protein PsaA. These proteins have been shown to function as initial receptors ... |
8-292 |
9.67e-139 |
|
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: 392.80 E-value: 9.67e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306047 8 FSVLLPLSFATAQAADKLQVVTSFSILDDMTHQVGGDHIQISNMVGPDADAHTYEPTPDDAKALLKAKVIIKNGLGFEPW 87
Cdd:cd01137 1 LAACASLGSSPATAASKLKVVATFSILADIARNIAGDRVNVTSIVPPGADPHEYEPTPSDIKKLSKADLILYNGLNLEPW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306047 88 LDRLVTSTETKATVVTASKGVLSHTMEE-DGETIPDPHAWHNLANTVIYVNNITKALIAADPANKADYEHNSQVYLKEIY 166
Cdd:cd01137 81 LERLVKNAGKDVPVVAVSEGIDPIPLEEgHYKGKPDPHAWMSPKNAIIYVKNIAKALSEADPANAETYQKNAAAYKAKLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306047 167 RLLAEAKAKFGALPPGNRRIVTSHDAFGYLGQAYGIEFLSPQGLSTEREPSAAEVATLITQIRKDKVKAVFMENIKDSRL 246
Cdd:cd01137 161 ALDEWAKAKFATIPAEKRKLVTSEGAFSYFAKAYGLKEAYLWPINTEEEGTPKQVATLIEQVKKEKVPAVFVESTVNDRL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 489306047 247 LQQIADESGAQIGGTLYSDALAAE-GPASTFTGLFEYNLNTLCAALS 292
Cdd:cd01137 241 MKQVAKETGAKIGGQLYTDSLSEKgGPADTYLDMMEHNLDTIVEGLG 287
|
|
| ZnuA |
pfam01297 |
Zinc-uptake complex component A periplasmic; ZnuA includes periplasmic solute binding proteins ... |
27-290 |
1.55e-104 |
|
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: 305.63 E-value: 1.55e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306047 27 VVTSFSILDDMTHQVGGDHIQISNMVGPDADAHTYEPTPDDAKALLKAKVIIKNGLGFEPWLDRLVTSTEtKATVVTASK 106
Cdd:pfam01297 1 VVATTYPLADLAKQIGGDRVEVTSLVPPGADPHDYEPTPSDIAALSDADLVVYNGLGLEPWLDKLLEALP-NKKVVDASE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306047 107 GVLSHTMEEDGETIP------DPHAWHNLANTVIYVNNITKALIAADPANKADYEHNSQVYLKEIYRLLAEAKAKFGALP 180
Cdd:pfam01297 80 GVELLDEEGEEEDHDghdhgyDPHVWLDPKNAKKMAENIADALSELDPANAATYEANAAAYLAELDALDAEIKEQLASIP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306047 181 PGNRRIVTSHDAFGYLGQAYGIEFLSPQGLSTEREPSAAEVATLITQIRKDKVKAVFMENIKDSRLLQQIADESGAQIGG 260
Cdd:pfam01297 160 EKTRKLVTSHDAFGYLARAYGLEQVGIQGVSPESEPSAADLAELIDLIKEKKVKAIFVEPQVSPKLAETVAKETGVKVLG 239
|
250 260 270
....*....|....*....|....*....|
gi 489306047 261 TLYSDALAAEGPASTFTGLFEYNLNTLCAA 290
Cdd:pfam01297 240 PLYTDSLGEPGGGATYLDLMRHNLDTLAEA 269
|
|
| ZnuA |
COG0803 |
ABC-type Zn uptake system ZnuABC, Zn-binding component ZnuA [Inorganic ion transport and ... |
1-283 |
4.55e-104 |
|
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: 304.86 E-value: 4.55e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306047 1 MRALLVLFSVLLPLSFA-----TAQAADKLQVVTSFSILDDMTHQVGGDHIQISNMVGPDADAHTYEPTPDDAKALLKAK 75
Cdd:COG0803 1 MKRLLLALLLLAALLLAgcsaaASSAAGKLKVVATFSPLADLAKQIGGDKVEVTSLVPPGADPHDYEPTPSDIAKLAKAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306047 76 VIIKNGLGFEPWLDRLVTSTE-TKATVVTASKGV-LSHTMEEDGETIPDPHAWHNLANTVIYVNNITKALIAADPANKAD 153
Cdd:COG0803 81 LVVYNGLGLEGWLDKLLEAAGnPGVPVVDASEGIdLLELEEGHDHGEPDPHVWLDPKNAKKVAENIADALAELDPANAAY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306047 154 YEHNSQVYLKEIYRLLAEAKAKFGALPpgNRRIVTSHDAFGYLGQAYGIEFLSPQGLSTEREPSAAEVATLITQIRKDKV 233
Cdd:COG0803 161 YEANAAAYLAELDALDAEIKAKLAAIP--GRKLVTSHDAFGYLARAYGLEVVAIQGISPGSEPSPADLAELIDLIKEEGV 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 489306047 234 KAVFMENIKDSRLLQQIADESGAQIggtLYSDAL-AAEGPASTFTGLFEYN 283
Cdd:COG0803 239 KAIFVESQVSPKLAETLAEETGVKV---LYLDSLgGPGGPGDTYLDMMRHN 286
|
|
| AztC |
NF040870 |
zinc ABC transporter substrate-binding protein AztC; |
27-291 |
1.45e-87 |
|
zinc ABC transporter substrate-binding protein AztC;
Pssm-ID: 468807 [Multi-domain] Cd Length: 277 Bit Score: 262.59 E-value: 1.45e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306047 27 VVTSFSILDDMTHQVGGDHIQISNMVGPDADAHTYEPTPDDAKALLKAKVIIKNGLGF-EPWLDRLVTSTETKATVVTAS 105
Cdd:NF040870 1 VVVTTNILGDLARNVVGDRAEVTTLMKPDADPHSFEPSAADAAALERADLVVVNGLGLeEGFLRHLIAASATGAPVVEVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306047 106 KGVL-------SHTMEEDGETIPDPHAWHNLANTVIYVNNITKALIAADPANKADYEHNSQVYLKEIYRLLAEAKAKFGA 178
Cdd:NF040870 81 DGVDplpypegGHYHFEAGAGPPDPHFWTDPARARDAVDNIADAFCEADDGDCAAYRANAAAYRAELDELDAEMREAFAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306047 179 LPPGNRRIVTSHDAFGYLGQAYGIEFLS---PQGlSTEREPSAAEVATLITQIRKDKVKAVFMENIKDSRLLQQIADESG 255
Cdd:NF040870 161 IPADRRTLVTNHHVFGYLAERYGFRVLGaviPSG-STLASPSAADLASLARAIREAGVPAIFAESSQPPRLAEVLASEAG 239
|
250 260 270
....*....|....*....|....*....|....*...
gi 489306047 256 AQIGGT-LYSDALAAE-GPASTFTGLFEYNLNTLCAAL 291
Cdd:NF040870 240 LDVGVVeLYSESLSEPdGGAATYLDMMRANAEAIVDGL 277
|
|
| AdcA |
cd01017 |
Metal binding protein AdcA. These proteins have been shown to function in the ABC uptake of ... |
22-292 |
2.82e-70 |
|
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: 218.70 E-value: 2.82e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306047 22 ADKLQVVTSFSILDDMTHQVGGDHIQISNMVGPDADAHTYEPTPDDAKALLKAKVIIKNGLGFEPWLDRLV-TSTETKAT 100
Cdd:cd01017 1 SGKLKVVTTFYPLYEFTKAIGGDKADVKLIIPAGTEPHDFEPSPKDIARIADADVFVYNGLGMETWAEKVLkSLQNKKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306047 101 VVTASKGVL----------SHTMEEDGETIPDPHAWHNLANTVIYVNNITKALIAADPANKADYEHNSQVYLKEIYRLLA 170
Cdd:cd01017 81 VVEASKGIKllkaggaehdHDHSHSHHHGDYDPHVWLSPVLAIQQVENIKDALIKLDPDNKEYYEKNAAAYAKKLEALDQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306047 171 EAKAKFGALPpgNRRIVTSHDAFGYLGQAYGIEFLSPQGLSTEREPSAAEVATLITQIRKDKVKAVFMENIKDSRLLQQI 250
Cdd:cd01017 161 EYRAKLAKAK--GKTFVTQHAAFGYLARRYGLKQIAIVGVSPEVEPSPKQLAELVEFVKKSDVKYIFFEENASSKIAETL 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 489306047 251 ADESGAQIGG--TLYSDALAAEGPASTFTGLFEYNLNTLCAALS 292
Cdd:cd01017 239 AKETGAKLLVlnPLETLTKEEIDDGKDYFSLMKENLETLKRALK 282
|
|
| TroA |
cd01016 |
Metal binding protein TroA. These proteins have been shown to function as initial receptors in ... |
24-291 |
3.63e-59 |
|
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: 190.27 E-value: 3.63e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306047 24 KLQVVTSFSILDDMTHQVGGDHIQISNMVGPDADAHTYEPTPDDAKALLKAKVIIKNGLGFE----PWLDRLVTSTETKA 99
Cdd:cd01016 1 KPNVVTTTGMIADAVENIGGDHVEVTGLMGPGVDPHLYKATAGDVEKLQNADVVFYNGLHLEgkmsDVLSKLGSSKSVIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306047 100 TVVTASKGVLSHtmeEDGETIPDPHAWHNLANTVIYVNNITKALIAADPANKADYEHNSQVYLKEIYRLLAEAKAKFGAL 179
Cdd:cd01016 81 LEDTLDRSQLIL---DEEEGTYDPHIWFDVKLWKYAVKAVAEVLSEKLPEHKDEFQANSEAYVEELDSLDAYAKKKIAEI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306047 180 PPGNRRIVTSHDAFGYLGQAYGIEFLSPQGLSTEREPSAAEVATLITQIRKDKVKAVFME---NIKDSRLLQQIADESG- 255
Cdd:cd01016 158 PEQQRVLVTAHDAFGYFGRAYGFEVKGLQGISTDSEAGLRDINELVDLIVERKIKAIFVEssvNQKSIEALQDAVKARGh 237
|
250 260 270
....*....|....*....|....*....|....*...
gi 489306047 256 -AQIGGTLYSDALAAEG-PASTFTGLFEYNLNTLCAAL 291
Cdd:cd01016 238 dVQIGGELYSDAMGEEGtSEGTYIGMFKHNVDTIVEAL 275
|
|
| ZntC |
cd01018 |
Metal binding protein ZntC. These proteins are predicted to function as initial receptors in ... |
23-258 |
3.53e-43 |
|
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: 148.66 E-value: 3.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306047 23 DKLQVVTSFSILDDMTHQVGGDHIQISNMVGPDADAHTYEPTPDDAKALLKAKVIIKNGLGFE-PWLDRLVTSTEtKATV 101
Cdd:cd01018 1 DKPTVAVSIEPQKYFVEKIAGDTVDVVVLVPPGSNPHTYEPKPQQMKKLSEADLYFRIGLGFEeVWLERFRSNNP-KMQV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306047 102 VTASKGV----------LSHTMEEDGETIP-DPHAWHNLANTVIYVNNITKALIAADPANKADYEHNSQVYLKEIYRLLA 170
Cdd:cd01018 80 VNMSKGItlipmadhhhHHHGEHEHHHHGNyDPHIWLSPANAKIMAENIYEALAELDPQNATYYQANLDALLAELDALDS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306047 171 EAKAKFGALPpgNRRIVTSHDAFGYLGQAYGIEFLSPQglSTEREPSAAEVATLITQIRKDKVKAVFMENIKDSRLLQQI 250
Cdd:cd01018 160 EIRTILSKLK--QRAFMVYHPAWGYFARDYGLTQIPIE--EEGKEPSPADLKRLIDLAKEKGVRVVFVQPQFSTKSAEAI 235
|
....*...
gi 489306047 251 ADESGAQI 258
Cdd:cd01018 236 AREIGAKV 243
|
|
| ZnuA |
cd01019 |
Zinc binding protein ZnuA. These proteins have been shown to function as initial receptors in ... |
22-291 |
3.56e-38 |
|
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: 135.96 E-value: 3.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306047 22 ADKLQVVTSFSILDDMTHQVGGDHIQISNMVGPDADAHTYEPTPDDAKALLKAKVIIKNGLGFEPWLDRlVTSTETKATV 101
Cdd:cd01019 1 AAEASVLTSIKPLGFIAAAIMGGVGEVEVLVPPGASPHDYELRPSDARKLQEADLVVWIGPDLEAFLDK-VLQGRKKGKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306047 102 VTASKGVLSHTME--------------------EDGETIPDPHAWHNLANTVIYVNNITKALIAADPANKADYEHNsqvy 161
Cdd:cd01019 80 LTLAKLIDLKTLEdgashgdhehdhehahgehdGHEEGGLDPHLWLSPENAAEVAQAVAEKLSALDPDNAATYAAN---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306047 162 LKEIYRLLAEAKAKFGA--LPPGNRRIVTSHDAFGYLGQAYGIEFLSPQGLSTEREPSAAEVATLITQIRKDKVKAVFME 239
Cdd:cd01019 156 LEAFNARLAELDATIKErlAPVKTKPFFVFHDAYGYFEKRYGLTQAGVFTIDPEIDPGAKRLAKIRKEIKEKGATCVFAE 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 489306047 240 NIKDSRLLQQIADESGAQIgGTLYSDALAAEGPASTFTGLFEYNLNTLCAAL 291
Cdd:cd01019 236 PQFHPKIAETLAEGTGAKV-GELDPLGGLIELGKNSYVNFLRNLADSLASCL 286
|
|
| anch_rpt_subst |
TIGR03772 |
anchored repeat ABC transporter, substrate-binding protein; Members of this protein family are ... |
122-292 |
7.70e-34 |
|
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: 128.44 E-value: 7.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306047 122 DPHAWHNLANTVIYVNNITKALIAADPANKADYEHNSQVYLKEIYRLLAEAKAKFGALPPGNRRIVTSHDAFGYLGQAYG 201
Cdd:TIGR03772 310 DPHLWHNVKNAIAYVEVIRDKLIEVDPRGAQAYRSNASAYIHRLERLDTYVRRTIATIPPSRRHLITTHDAYSYLGQAYG 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306047 202 IE---FLSPqglSTEREPSAAEVATLITQIRKDKVKAVFMEN--IKDSRLLQQIADESGAQIgGTLYSDALAAEGPasTF 276
Cdd:TIGR03772 390 LNiagFVTP---NPAVEPSLADRRRLTRTIENLKVPAVFLEPnlAARSTTLNEIADELGVRV-CAIYGDTFDDDVT--NY 463
|
170
....*....|....*.
gi 489306047 277 TGLFEYNLNTLCAALS 292
Cdd:TIGR03772 464 VDLMRFNADSLADCLG 479
|
|
| TroA_b |
cd01020 |
Metal binding protein TroA_b. These proteins are predicted to function as initial receptors ... |
23-255 |
5.71e-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: 119.08 E-value: 5.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306047 23 DKLQVVTSFSILDDMTHQVGGDHIQISNMVG-PDADAHTYEPTPDDAKALLKAKVIIKNGLGFEPWLDRLVTSteTKATV 101
Cdd:cd01020 1 GKINVVASTNFWGSVAEAVGGDHVEVTSIITnPDVDPHDFEPTPTDAAKVSTADIVVYNGGGYDPWMTKLLAD--TKDVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306047 102 VTASKGVLSHTMEEDgetipDPHAWHNLANTVIYVNNITKALIAADPANKADYEHNSQVY---LKEIYRLLAEAKAKFga 178
Cdd:cd01020 79 VIAADLDGHDDKEGD-----NPHLWYDPETMSKVANALADALVKADPDNKKYYQANAKKFvasLKPLAAKIAELSAKY-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306047 179 lppGNRRIVTSHDAFGYLGQAYGIEFLSPQGLS----TEREPSAAEVATLITQIRKDKVKAVFMENIKDSRL---LQQIA 251
Cdd:cd01020 152 ---KGAPVAATEPVFDYLLDALGMKERTPKGYTatteSETEPSPADIAAFQNAIKNRQIDALIVNPQQASSAttnITGLA 228
|
....
gi 489306047 252 DESG 255
Cdd:cd01020 229 KRSG 232
|
|
| ZnuA |
COG4531 |
ABC-type Zn2+ transport system, periplasmic component/surface adhesin ZnuA [Inorganic ion ... |
16-274 |
7.33e-32 |
|
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: 119.93 E-value: 7.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306047 16 FATAQAADKLQVVTSFSILDDMTHQVGGDHIQISNMVGPDADAHTYEPTPDDAKALLKAKVIIKNGLGFEPWLDRLVTST 95
Cdd:COG4531 1 LASAAAAAAPRVVTSIKPLHSLVAAVMDGVGEPELLLPPGASPHDYALRPSDARALQDADLVFWVGPDLEPFLEKPLETL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306047 96 ETKATVVTASK--GVLSHTMEEDGE-------------------------TIPDPHAWHNLANTVIYVNNITKALIAADP 148
Cdd:COG4531 81 APDAKVVELLElpGLTLLPFREGGDfehhdhhdehhhhhhhhddhhdhhhGGYDPHLWLSPENAKAWAAAIADALSELDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306047 149 ANKADYEHNSQVYLKEIYRLLAEAKAKFGALppGNRRIVTSHDAFGYLGQAYGiefLSPQG---LSTEREPSAAEVATLI 225
Cdd:COG4531 161 ENAATYQANAAAFEARLDALDAEIAAQLAPV--KGKPFFVFHDAYQYFEKRFG---LNALGaitLNPEIQPGAKRLAEIR 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 489306047 226 TQIRKDKVKAVFMENIKDSRLLQQIADESGAQIgGTLysDALAAE---GPAS 274
Cdd:COG4531 236 EKLKELGAVCVFAEPQFNPALVETVAEGTGVRT-GVL--DPLGADlepGPDL 284
|
|
| TroA_c |
cd01145 |
Periplasmic binding protein TroA_c. These proteins are predicted to function as initial ... |
24-203 |
3.14e-20 |
|
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: 86.40 E-value: 3.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306047 24 KLQVVTSFSILDDMTHQVGGDHIQISNMVGPDADAHTYEPTPDDAKALLKAKVIIKNGLGFEPWLDRLVTSTE------- 96
Cdd:cd01145 2 ALNVVVTFPDLKDLVREVAGDAVIVSALTPPGVDPHQYQLKPSDIAKMRKADLVVTSGHELEGFEPKLAELSSnskvqpg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306047 97 TKATVVTASKGVLSHTMEEDGETIPDPHAWHNLANTVIYVNNITKALIAADPANKADYEHNSQVYLKEIYRLLAEAKAKF 176
Cdd:cd01145 82 IKILIEDSDTVGMVDRAMGDYHGKGNPHVWLDPNNAPALAKALADALIELDPSEQEEYKENLRVFLAKLNKLLREWERQF 161
|
170 180
....*....|....*....|....*..
gi 489306047 177 GALppGNRRIVTSHDAFGYLGQAYGIE 203
Cdd:cd01145 162 EGL--KGIQVVAYHPSYQYLADWLGIE 186
|
|
| znuA |
PRK09545 |
zinc ABC transporter substrate-binding protein ZnuA; |
5-239 |
4.31e-08 |
|
zinc ABC transporter substrate-binding protein ZnuA;
Pssm-ID: 236558 [Multi-domain] Cd Length: 311 Bit Score: 53.47 E-value: 4.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306047 5 LVLFSVLLPLSFATAQAAdklqVVTSF--------SILDDMTH-QVggdhiqisnMVGPDADAHTYEPTPDDAKALLKAK 75
Cdd:PRK09545 9 AALLAALLGGATQAANAA----VVTSIkplgfiasAIADGVTEtEV---------LLPDGASPHDYSLRPSDVKRLQSAD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306047 76 VIIKNGLGFEPWLDRLVTSTETKATVVTAS----KGVLSHTMEEDGETIPDPHAWHNLA---------NTVIYVN-NITK 141
Cdd:PRK09545 76 LVVWVGPEMEAFLEKPVSKLPENKQVTIAQlpdvKPLLMKGAHDDHHDDDHDHAGHEKSdedhhhgeyNMHIWLSpEIAR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306047 142 A--------LIAADPANKADYEHNsqvyLKEIYRLLAEAKAKFGAL--PPGNRRIVTSHDAFGYLGQAYGiefLSPQGLS 211
Cdd:PRK09545 156 AtavaihdkLVELMPQSKAKLDAN----LKDFEAQLAQTDKQIGNQlaPVKGKGYFVFHDAYGYFEKHYG---LTPLGHF 228
|
250 260 270
....*....|....*....|....*....|.
gi 489306047 212 T---EREPSAAEVATLITQIRKDKVKAVFME 239
Cdd:PRK09545 229 TvnpEIQPGAQRLHEIRTQLVEQKATCVFAE 259
|
|
| TroA-like |
cd00636 |
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ... |
27-189 |
1.02e-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: 50.25 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306047 27 VVTSFSILDDMTHQVGGDHIQISNMVGPDADA-------------HTYEPTPDDAKALlKAKVIIKNGLGFEPWLDRLVT 93
Cdd:cd00636 3 VVALDPGATELLLALGGDDKPVGVADPSGYPPeakallekvpdvgHGYEPNLEKIAAL-KPDLIIANGSGLEAWLDKLSK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306047 94 STETKATVVTASKgvlshtmeedgetipdphawHNLANTVIYVNNITKALiaadpankaDYEHNSQVYLKEIYRLLAEAK 173
Cdd:cd00636 82 IAIPVVVVDEASE--------------------LSLENIKESIRLIGKAL---------GKEENAEELIAELDARLAELR 132
|
170
....*....|....*.
gi 489306047 174 AKFGALPPGNRRIVTS 189
Cdd:cd00636 133 AKLAKIPKKKVSLVVG 148
|
|
| |
