|
Name |
Accession |
Description |
Interval |
E-value |
| PsaA |
cd01137 |
Metal binding protein PsaA. These proteins have been shown to function as initial receptors ... |
25-309 |
4.92e-122 |
|
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: 351.19 E-value: 4.92e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600122731 25 SSDKSNGKLKVVTTNSILYDMAKNVGGDNVDIHSIVPVGQDPHEYEVKPKDIKKLTDADVILYNGLNLEtgnGWFEKALE 104
Cdd:cd01137 10 SPATAASKLKVVATFSILADIARNIAGDRVNVTSIVPPGADPHEYEPTPSDIKKLSKADLILYNGLNLE---PWLERLVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600122731 105 QAGKslkDKKVIAVSKDVKPIYLngEEGN-KDKQDPHAWLSLDNGIKYVKTIQQTFIDNDKKHKADYEKQGNKYIAQLEK 183
Cdd:cd01137 87 NAGK---DVPVVAVSEGIDPIPL--EEGHyKGKPDPHAWMSPKNAIIYVKNIAKALSEADPANAETYQKNAAAYKAKLKA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600122731 184 LNNDSKDKFNDIPKEQRAMITSEGAFKYFSKQYGITPGYIWEINTEKQGTPEQMRQAIEFVKKHKLKHLLVETSVDKKAM 263
Cdd:cd01137 162 LDEWAKAKFATIPAEKRKLVTSEGAFSYFAKAYGLKEAYLWPINTEEEGTPKQVATLIEQVKKEKVPAVFVESTVNDRLM 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 600122731 264 ESLSEETKKDIFGEVYTDSIGKEGTKGDSYYKMMKSNIETVHGSMK 309
Cdd:cd01137 242 KQVAKETGAKIGGQLYTDSLSEKGGPADTYLDMMEHNLDTIVEGLG 287
|
|
| ZnuA |
COG0803 |
ABC-type Zn uptake system ZnuABC, Zn-binding component ZnuA [Inorganic ion transport and ... |
20-300 |
2.42e-103 |
|
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: 303.70 E-value: 2.42e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600122731 20 TGGKQSSDKSNGKLKVVTTNSILYDMAKNVGGDNVDIHSIVPVGQDPHEYEVKPKDIKKLTDADVILYNGLNLEtgnGWF 99
Cdd:COG0803 17 AGCSAAASSAAGKLKVVATFSPLADLAKQIGGDKVEVTSLVPPGADPHDYEPTPSDIAKLAKADLVVYNGLGLE---GWL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600122731 100 EKALEQAGKslKDKKVIAVSKDVKPIYLNGEEGNkDKQDPHAWLSLDNGIKYVKTIQQTFIDNDKKHKADYEKQGNKYIA 179
Cdd:COG0803 94 DKLLEAAGN--PGVPVVDASEGIDLLELEEGHDH-GEPDPHVWLDPKNAKKVAENIADALAELDPANAAYYEANAAAYLA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600122731 180 QLEKLNNDSKDKFNDIPkeQRAMITSEGAFKYFSKQYGITPGYIWEINTEKQGTPEQMRQAIEFVKKHKLKHLLVETSVD 259
Cdd:COG0803 171 ELDALDAEIKAKLAAIP--GRKLVTSHDAFGYLARAYGLEVVAIQGISPGSEPSPADLAELIDLIKEEGVKAIFVESQVS 248
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 600122731 260 KKAMESLSEETKKDIfgeVYTDSIGKEGTKGDSYYKMMKSN 300
Cdd:COG0803 249 PKLAETLAEETGVKV---LYLDSLGGPGGPGDTYLDMMRHN 286
|
|
| ZnuA |
pfam01297 |
Zinc-uptake complex component A periplasmic; ZnuA includes periplasmic solute binding proteins ... |
35-303 |
2.16e-102 |
|
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: 300.62 E-value: 2.16e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600122731 35 VVTTNSILYDMAKNVGGDNVDIHSIVPVGQDPHEYEVKPKDIKKLTDADVILYNGLNLEtgnGWFEKALEqagkSLKDKK 114
Cdd:pfam01297 1 VVATTYPLADLAKQIGGDRVEVTSLVPPGADPHDYEPTPSDIAALSDADLVVYNGLGLE---PWLDKLLE----ALPNKK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600122731 115 VIAVSKDVKPIYLNGEEGNKDK----QDPHAWLSLDNGIKYVKTIQQTFIDNDKKHKADYEKQGNKYIAQLEKLNNDSKD 190
Cdd:pfam01297 74 VVDASEGVELLDEEGEEEDHDGhdhgYDPHVWLDPKNAKKMAENIADALSELDPANAATYEANAAAYLAELDALDAEIKE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600122731 191 KFNDIPKEQRAMITSEGAFKYFSKQYGITPGYIWEINTEKQGTPEQMRQAIEFVKKHKLKHLLVETSVDKKAMESLSEET 270
Cdd:pfam01297 154 QLASIPEKTRKLVTSHDAFGYLARAYGLEQVGIQGVSPESEPSAADLAELIDLIKEKKVKAIFVEPQVSPKLAETVAKET 233
|
250 260 270
....*....|....*....|....*....|...
gi 600122731 271 KKDIFGEVYTDSIGKEGTkGDSYYKMMKSNIET 303
Cdd:pfam01297 234 GVKVLGPLYTDSLGEPGG-GATYLDLMRHNLDT 265
|
|
| AztC |
NF040870 |
zinc ABC transporter substrate-binding protein AztC; |
35-304 |
4.27e-49 |
|
zinc ABC transporter substrate-binding protein AztC;
Pssm-ID: 468807 [Multi-domain] Cd Length: 277 Bit Score: 164.75 E-value: 4.27e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600122731 35 VVTTNSILYDMAKNVGGDNVDIHSIVPVGQDPHEYEVKPKDIKKLTDADVILYNGLNLETGngwFEKALEQAgkSLKDKK 114
Cdd:NF040870 1 VVVTTNILGDLARNVVGDRAEVTTLMKPDADPHSFEPSAADAAALERADLVVVNGLGLEEG---FLRHLIAA--SATGAP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600122731 115 VIAVSKDVKPI-YLNGEEGNKDKQ----DPHAWLSLDNGIKYVKTIQQTFIDNDKKHKADYEKQGNKYIAQLEKLNNDSK 189
Cdd:NF040870 76 VVEVGDGVDPLpYPEGGHYHFEAGagppDPHFWTDPARARDAVDNIADAFCEADDGDCAAYRANAAAYRAELDELDAEMR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600122731 190 DKFNDIPKEQRAMITSEGAFKYFSKQYGIT------PgyiweintekQGTPEQMRQA------IEFVKKHKLKHLLVETS 257
Cdd:NF040870 156 EAFAAIPADRRTLVTNHHVFGYLAERYGFRvlgaviP----------SGSTLASPSAadlaslARAIREAGVPAIFAESS 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 600122731 258 VDKKAMESLSEETKKDIFG-EVYTDSIGKEGTKGDSYYKMMKSNIETV 304
Cdd:NF040870 226 QPPRLAEVLASEAGLDVGVvELYSESLSEPDGGAATYLDMMRANAEAI 273
|
|
| znuA |
PRK09545 |
zinc ABC transporter substrate-binding protein ZnuA; |
59-271 |
2.54e-11 |
|
zinc ABC transporter substrate-binding protein ZnuA;
Pssm-ID: 236558 [Multi-domain] Cd Length: 311 Bit Score: 63.10 E-value: 2.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600122731 59 IVPVGQDPHEYEVKPKDIKKLTDADVILYNGLNLETgngWFEKALEQagksLKDKKVIAVSK--DVKPIYLNGEEgNKDK 136
Cdd:PRK09545 51 LLPDGASPHDYSLRPSDVKRLQSADLVVWVGPEMEA---FLEKPVSK----LPENKQVTIAQlpDVKPLLMKGAH-DDHH 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600122731 137 QDPHAWLSLDNgikyvktiqqtfiDNDKKHKADYE----------KQGNKYIA-QLEKLNNDSKDK-------FNDIPKE 198
Cdd:PRK09545 123 DDDHDHAGHEK-------------SDEDHHHGEYNmhiwlspeiaRATAVAIHdKLVELMPQSKAKldanlkdFEAQLAQ 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600122731 199 QRAMITSE-------------GAFKYFSKQYGITP-GYiWEINTEKQGTPEQMRQAIEFVKKHKLKHLLVETSVDKKAME 264
Cdd:PRK09545 190 TDKQIGNQlapvkgkgyfvfhDAYGYFEKHYGLTPlGH-FTVNPEIQPGAQRLHEIRTQLVEQKATCVFAEPQFRPAVIE 268
|
....*..
gi 600122731 265 SLSEETK 271
Cdd:PRK09545 269 SVAKGTS 275
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PsaA |
cd01137 |
Metal binding protein PsaA. These proteins have been shown to function as initial receptors ... |
25-309 |
4.92e-122 |
|
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: 351.19 E-value: 4.92e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600122731 25 SSDKSNGKLKVVTTNSILYDMAKNVGGDNVDIHSIVPVGQDPHEYEVKPKDIKKLTDADVILYNGLNLEtgnGWFEKALE 104
Cdd:cd01137 10 SPATAASKLKVVATFSILADIARNIAGDRVNVTSIVPPGADPHEYEPTPSDIKKLSKADLILYNGLNLE---PWLERLVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600122731 105 QAGKslkDKKVIAVSKDVKPIYLngEEGN-KDKQDPHAWLSLDNGIKYVKTIQQTFIDNDKKHKADYEKQGNKYIAQLEK 183
Cdd:cd01137 87 NAGK---DVPVVAVSEGIDPIPL--EEGHyKGKPDPHAWMSPKNAIIYVKNIAKALSEADPANAETYQKNAAAYKAKLKA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600122731 184 LNNDSKDKFNDIPKEQRAMITSEGAFKYFSKQYGITPGYIWEINTEKQGTPEQMRQAIEFVKKHKLKHLLVETSVDKKAM 263
Cdd:cd01137 162 LDEWAKAKFATIPAEKRKLVTSEGAFSYFAKAYGLKEAYLWPINTEEEGTPKQVATLIEQVKKEKVPAVFVESTVNDRLM 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 600122731 264 ESLSEETKKDIFGEVYTDSIGKEGTKGDSYYKMMKSNIETVHGSMK 309
Cdd:cd01137 242 KQVAKETGAKIGGQLYTDSLSEKGGPADTYLDMMEHNLDTIVEGLG 287
|
|
| ZnuA |
COG0803 |
ABC-type Zn uptake system ZnuABC, Zn-binding component ZnuA [Inorganic ion transport and ... |
20-300 |
2.42e-103 |
|
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: 303.70 E-value: 2.42e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600122731 20 TGGKQSSDKSNGKLKVVTTNSILYDMAKNVGGDNVDIHSIVPVGQDPHEYEVKPKDIKKLTDADVILYNGLNLEtgnGWF 99
Cdd:COG0803 17 AGCSAAASSAAGKLKVVATFSPLADLAKQIGGDKVEVTSLVPPGADPHDYEPTPSDIAKLAKADLVVYNGLGLE---GWL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600122731 100 EKALEQAGKslKDKKVIAVSKDVKPIYLNGEEGNkDKQDPHAWLSLDNGIKYVKTIQQTFIDNDKKHKADYEKQGNKYIA 179
Cdd:COG0803 94 DKLLEAAGN--PGVPVVDASEGIDLLELEEGHDH-GEPDPHVWLDPKNAKKVAENIADALAELDPANAAYYEANAAAYLA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600122731 180 QLEKLNNDSKDKFNDIPkeQRAMITSEGAFKYFSKQYGITPGYIWEINTEKQGTPEQMRQAIEFVKKHKLKHLLVETSVD 259
Cdd:COG0803 171 ELDALDAEIKAKLAAIP--GRKLVTSHDAFGYLARAYGLEVVAIQGISPGSEPSPADLAELIDLIKEEGVKAIFVESQVS 248
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 600122731 260 KKAMESLSEETKKDIfgeVYTDSIGKEGTKGDSYYKMMKSN 300
Cdd:COG0803 249 PKLAETLAEETGVKV---LYLDSLGGPGGPGDTYLDMMRHN 286
|
|
| ZnuA |
pfam01297 |
Zinc-uptake complex component A periplasmic; ZnuA includes periplasmic solute binding proteins ... |
35-303 |
2.16e-102 |
|
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: 300.62 E-value: 2.16e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600122731 35 VVTTNSILYDMAKNVGGDNVDIHSIVPVGQDPHEYEVKPKDIKKLTDADVILYNGLNLEtgnGWFEKALEqagkSLKDKK 114
Cdd:pfam01297 1 VVATTYPLADLAKQIGGDRVEVTSLVPPGADPHDYEPTPSDIAALSDADLVVYNGLGLE---PWLDKLLE----ALPNKK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600122731 115 VIAVSKDVKPIYLNGEEGNKDK----QDPHAWLSLDNGIKYVKTIQQTFIDNDKKHKADYEKQGNKYIAQLEKLNNDSKD 190
Cdd:pfam01297 74 VVDASEGVELLDEEGEEEDHDGhdhgYDPHVWLDPKNAKKMAENIADALSELDPANAATYEANAAAYLAELDALDAEIKE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600122731 191 KFNDIPKEQRAMITSEGAFKYFSKQYGITPGYIWEINTEKQGTPEQMRQAIEFVKKHKLKHLLVETSVDKKAMESLSEET 270
Cdd:pfam01297 154 QLASIPEKTRKLVTSHDAFGYLARAYGLEQVGIQGVSPESEPSAADLAELIDLIKEKKVKAIFVEPQVSPKLAETVAKET 233
|
250 260 270
....*....|....*....|....*....|...
gi 600122731 271 KKDIFGEVYTDSIGKEGTkGDSYYKMMKSNIET 303
Cdd:pfam01297 234 GVKVLGPLYTDSLGEPGG-GATYLDLMRHNLDT 265
|
|
| AdcA |
cd01017 |
Metal binding protein AdcA. These proteins have been shown to function in the ABC uptake of ... |
30-309 |
6.34e-59 |
|
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: 190.20 E-value: 6.34e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600122731 30 NGKLKVVTTNSILYDMAKNVGGDNVDIHSIVPVGQDPHEYEVKPKDIKKLTDADVILYNGLNLETgngWFEKALEQAGKs 109
Cdd:cd01017 1 SGKLKVVTTFYPLYEFTKAIGGDKADVKLIIPAGTEPHDFEPSPKDIARIADADVFVYNGLGMET---WAEKVLKSLQN- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600122731 110 lKDKKVIAVSKDVKPI--------YLNGEEGNKDKQDPHAWLSLDNGIKYVKTIQQTFIDNDKKHKADYEKQGNKYIAQL 181
Cdd:cd01017 77 -KKLKVVEASKGIKLLkaggaehdHDHSHSHHHGDYDPHVWLSPVLAIQQVENIKDALIKLDPDNKEYYEKNAAAYAKKL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600122731 182 EKLNNDSKDKFNdiPKEQRAMITSEGAFKYFSKQYGITPGYIWEINTEKQGTPEQMRQAIEFVKKHKLKHLLVETSVDKK 261
Cdd:cd01017 156 EALDQEYRAKLA--KAKGKTFVTQHAAFGYLARRYGLKQIAIVGVSPEVEPSPKQLAELVEFVKKSDVKYIFFEENASSK 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 600122731 262 AMESLSEETKkdifGEVYT----DSIGKEGTK-GDSYYKMMKSNIETVHGSMK 309
Cdd:cd01017 234 IAETLAKETG----AKLLVlnplETLTKEEIDdGKDYFSLMKENLETLKRALK 282
|
|
| TroA |
cd01016 |
Metal binding protein TroA. These proteins have been shown to function as initial receptors in ... |
32-309 |
4.73e-57 |
|
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: 185.26 E-value: 4.73e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600122731 32 KLKVVTTNSILYDMAKNVGGDNVDIHSIVPVGQDPHEYEVKPKDIKKLTDADVILYNGLNLETgngwfeKALEQAGKSLK 111
Cdd:cd01016 1 KPNVVTTTGMIADAVENIGGDHVEVTGLMGPGVDPHLYKATAGDVEKLQNADVVFYNGLHLEG------KMSDVLSKLGS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600122731 112 DKKVIAVSK--DVKPIYLNGEEGNkdkQDPHAWLSLDNGIKYVKTIQQTFIDNDKKHKADYEKQGNKYIAQLEKLNNDSK 189
Cdd:cd01016 75 SKSVIALEDtlDRSQLILDEEEGT---YDPHIWFDVKLWKYAVKAVAEVLSEKLPEHKDEFQANSEAYVEELDSLDAYAK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600122731 190 DKFNDIPKEQRAMITSEGAFKYFSKQYGITPGYIWEINTEKQGTPEQMRQAIEFVKKHKLKHLLVETSVDKKAMESLSEE 269
Cdd:cd01016 152 KKIAEIPEQQRVLVTAHDAFGYFGRAYGFEVKGLQGISTDSEAGLRDINELVDLIVERKIKAIFVESSVNQKSIEALQDA 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 600122731 270 TKKD-----IFGEVYTDSIGKEGTKGDSYYKMMKSNIETVHGSMK 309
Cdd:cd01016 232 VKARghdvqIGGELYSDAMGEEGTSEGTYIGMFKHNVDTIVEALK 276
|
|
| AztC |
NF040870 |
zinc ABC transporter substrate-binding protein AztC; |
35-304 |
4.27e-49 |
|
zinc ABC transporter substrate-binding protein AztC;
Pssm-ID: 468807 [Multi-domain] Cd Length: 277 Bit Score: 164.75 E-value: 4.27e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600122731 35 VVTTNSILYDMAKNVGGDNVDIHSIVPVGQDPHEYEVKPKDIKKLTDADVILYNGLNLETGngwFEKALEQAgkSLKDKK 114
Cdd:NF040870 1 VVVTTNILGDLARNVVGDRAEVTTLMKPDADPHSFEPSAADAAALERADLVVVNGLGLEEG---FLRHLIAA--SATGAP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600122731 115 VIAVSKDVKPI-YLNGEEGNKDKQ----DPHAWLSLDNGIKYVKTIQQTFIDNDKKHKADYEKQGNKYIAQLEKLNNDSK 189
Cdd:NF040870 76 VVEVGDGVDPLpYPEGGHYHFEAGagppDPHFWTDPARARDAVDNIADAFCEADDGDCAAYRANAAAYRAELDELDAEMR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600122731 190 DKFNDIPKEQRAMITSEGAFKYFSKQYGIT------PgyiweintekQGTPEQMRQA------IEFVKKHKLKHLLVETS 257
Cdd:NF040870 156 EAFAAIPADRRTLVTNHHVFGYLAERYGFRvlgaviP----------SGSTLASPSAadlaslARAIREAGVPAIFAESS 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 600122731 258 VDKKAMESLSEETKKDIFG-EVYTDSIGKEGTKGDSYYKMMKSNIETV 304
Cdd:NF040870 226 QPPRLAEVLASEAGLDVGVvELYSESLSEPDGGAATYLDMMRANAEAI 273
|
|
| ZnuA |
cd01019 |
Zinc binding protein ZnuA. These proteins have been shown to function as initial receptors in ... |
34-300 |
3.10e-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: 131.34 E-value: 3.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600122731 34 KVVTTNSILYDMAKNVGGDNVDIHSIVPVGQDPHEYEVKPKDIKKLTDADVILYNGLNLETgngWFEKALEQAGKslkdK 113
Cdd:cd01019 5 SVLTSIKPLGFIAAAIMGGVGEVEVLVPPGASPHDYELRPSDARKLQEADLVVWIGPDLEA---FLDKVLQGRKK----G 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600122731 114 KVIAVSK--DVKPIYLNGEEGNKDKQ----------------DPHAWLSLDNGIKYVKTIQQTFIDNDKKHKADYEKQGN 175
Cdd:cd01019 78 KVLTLAKliDLKTLEDGASHGDHEHDhehahgehdgheegglDPHLWLSPENAAEVAQAVAEKLSALDPDNAATYAANLE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600122731 176 KYIAQLEKLNNDSKDKFNDIpkEQRAMITSEGAFKYFSKQYGITPGYIWEINTEKQGTPEQMRQAIEFVKKHKLKHLLVE 255
Cdd:cd01019 158 AFNARLAELDATIKERLAPV--KTKPFFVFHDAYGYFEKRYGLTQAGVFTIDPEIDPGAKRLAKIRKEIKEKGATCVFAE 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 600122731 256 TSVDKKAMESLSEETKkdIFGEVYTDSIGKEGTKGDSYYKMMKSN 300
Cdd:cd01019 236 PQFHPKIAETLAEGTG--AKVGELDPLGGLIELGKNSYVNFLRNL 278
|
|
| ZntC |
cd01018 |
Metal binding protein ZntC. These proteins are predicted to function as initial receptors in ... |
46-280 |
3.32e-34 |
|
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: 125.55 E-value: 3.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600122731 46 AKNVGGDNVDIHSIVPVGQDPHEYEVKPKDIKKLTDADVILYNGLNLEtgNGWFEKaLEQAGKSLkdkKVIAVSKDVKPI 125
Cdd:cd01018 16 VEKIAGDTVDVVVLVPPGSNPHTYEPKPQQMKKLSEADLYFRIGLGFE--EVWLER-FRSNNPKM---QVVNMSKGITLI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600122731 126 YLNGEEGNKDKQ---------DPHAWLSLDNGIKYVKTIQQTFIDNDKKHKADYEKQGNKYIAQLEKLNNDSKDKFNDIP 196
Cdd:cd01018 90 PMADHHHHHHGEhehhhhgnyDPHIWLSPANAKIMAENIYEALAELDPQNATYYQANLDALLAELDALDSEIRTILSKLK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600122731 197 keQRAMITSEGAFKYFSKQYGITpgyiwEINTEKQG---TPEQMRQAIEFVKKHKLKHLLVETSVDKKAMESLSEEtkkd 273
Cdd:cd01018 170 --QRAFMVYHPAWGYFARDYGLT-----QIPIEEEGkepSPADLKRLIDLAKEKGVRVVFVQPQFSTKSAEAIARE---- 238
|
....*..
gi 600122731 274 IFGEVYT 280
Cdd:cd01018 239 IGAKVVT 245
|
|
| TroA_b |
cd01020 |
Metal binding protein TroA_b. These proteins are predicted to function as initial receptors ... |
31-272 |
6.03e-27 |
|
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: 106.37 E-value: 6.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600122731 31 GKLKVVTTNSILYDMAKNVGGDNVDIHSIVPVG-QDPHEYEVKPKDIKKLTDADVILYNGLNLETgngWFEKALEqagkS 109
Cdd:cd01020 1 GKINVVASTNFWGSVAEAVGGDHVEVTSIITNPdVDPHDFEPTPTDAAKVSTADIVVYNGGGYDP---WMTKLLA----D 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600122731 110 LKDKKVIAVSKDVKpiylngeeGNKDKQDPHAWLSLDNGIKYVKTIQQTFIDNDKKHKADYEKQGNKYIAQLEKLNNdsk 189
Cdd:cd01020 74 TKDVIVIAADLDGH--------DDKEGDNPHLWYDPETMSKVANALADALVKADPDNKKYYQANAKKFVASLKPLAA--- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600122731 190 dKFNDIPK--EQRAMITSEGAFKYFSKQYGIT----PGYIWEINTEKQGTPEQMRQAIEFVKKHKLKHLLVETSVDKKAM 263
Cdd:cd01020 143 -KIAELSAkyKGAPVAATEPVFDYLLDALGMKertpKGYTATTESETEPSPADIAAFQNAIKNRQIDALIVNPQQASSAT 221
|
....*....
gi 600122731 264 ESLSEETKK 272
Cdd:cd01020 222 TNITGLAKR 230
|
|
| TroA_c |
cd01145 |
Periplasmic binding protein TroA_c. These proteins are predicted to function as initial ... |
32-218 |
5.97e-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: 99.50 E-value: 5.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600122731 32 KLKVVTTNSILYDMAKNVGGDNVDIHSIVPVGQDPHEYEVKPKDIKKLTDADVILYNGLNLEtgnGWFEKALEQAGKSLK 111
Cdd:cd01145 2 ALNVVVTFPDLKDLVREVAGDAVIVSALTPPGVDPHQYQLKPSDIAKMRKADLVVTSGHELE---GFEPKLAELSSNSKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600122731 112 DK-KVIAVSKDVKPIYLNGEEGNKD-KQDPHAWLSLDNGIKYVKTIQQTFIDNDKKHKADYEKQGNKYIAQLEKLNNDSK 189
Cdd:cd01145 79 QPgIKILIEDSDTVGMVDRAMGDYHgKGNPHVWLDPNNAPALAKALADALIELDPSEQEEYKENLRVFLAKLNKLLREWE 158
|
170 180
....*....|....*....|....*....
gi 600122731 190 DKFNdiPKEQRAMITSEGAFKYFSKQYGI 218
Cdd:cd01145 159 RQFE--GLKGIQVVAYHPSYQYLADWLGI 185
|
|
| ZnuA |
COG4531 |
ABC-type Zn2+ transport system, periplasmic component/surface adhesin ZnuA [Inorganic ion ... |
34-271 |
2.05e-18 |
|
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: 83.73 E-value: 2.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600122731 34 KVVTtnSI--LYDMAKNVGGDNVDIHSIVPVGQDPHEYEVKPKDIKKLTDADVILYNGLNLETgngWFEKALEQAGKslk 111
Cdd:COG4531 11 RVVT--SIkpLHSLVAAVMDGVGEPELLLPPGASPHDYALRPSDARALQDADLVFWVGPDLEP---FLEKPLETLAP--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600122731 112 DKKVIAVSK--DVKPiyLNGEEGNKDKQ-------------------------DPHAWLSLDNGIKYVKTIQQTFIDNDK 164
Cdd:COG4531 83 DAKVVELLElpGLTL--LPFREGGDFEHhdhhdehhhhhhhhddhhdhhhggyDPHLWLSPENAKAWAAAIADALSELDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600122731 165 KHKADYEKQGNKYIAQLEKLNNDSKDKFNDIpKEQRAMITSEgAFKYFSKQYGITP-GYIwEINTEKQGTPEQMRQAIEF 243
Cdd:COG4531 161 ENAATYQANAAAFEARLDALDAEIAAQLAPV-KGKPFFVFHD-AYQYFEKRFGLNAlGAI-TLNPEIQPGAKRLAEIREK 237
|
250 260
....*....|....*....|....*...
gi 600122731 244 VKKHKLKHLLVETSVDKKAMESLSEETK 271
Cdd:COG4531 238 LKELGAVCVFAEPQFNPALVETVAEGTG 265
|
|
| TroA-like |
cd00636 |
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ... |
33-205 |
4.37e-13 |
|
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: 65.66 E-value: 4.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600122731 33 LKVVTTNSILYDMAKNVGGDNVDIHSIVPVGQD-------------PHEYEVKPKDIKKLtDADVILYNGLNLETgngwF 99
Cdd:cd00636 1 KRVVALDPGATELLLALGGDDKPVGVADPSGYPpeakallekvpdvGHGYEPNLEKIAAL-KPDLIIANGSGLEA----W 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600122731 100 EKALEQAGKslkdkKVIAVSKDVKpiylngeegnkdkqdphawLSLDNGIKYVKTIQQTFidndkkhkaDYEKQGNKYIA 179
Cdd:cd00636 76 LDKLSKIAI-----PVVVVDEASE-------------------LSLENIKESIRLIGKAL---------GKEENAEELIA 122
|
170 180
....*....|....*....|....*.
gi 600122731 180 QLEKLNNDSKDKFNDIPKEQRAMITS 205
Cdd:cd00636 123 ELDARLAELRAKLAKIPKKKVSLVVG 148
|
|
| znuA |
PRK09545 |
zinc ABC transporter substrate-binding protein ZnuA; |
59-271 |
2.54e-11 |
|
zinc ABC transporter substrate-binding protein ZnuA;
Pssm-ID: 236558 [Multi-domain] Cd Length: 311 Bit Score: 63.10 E-value: 2.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600122731 59 IVPVGQDPHEYEVKPKDIKKLTDADVILYNGLNLETgngWFEKALEQagksLKDKKVIAVSK--DVKPIYLNGEEgNKDK 136
Cdd:PRK09545 51 LLPDGASPHDYSLRPSDVKRLQSADLVVWVGPEMEA---FLEKPVSK----LPENKQVTIAQlpDVKPLLMKGAH-DDHH 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600122731 137 QDPHAWLSLDNgikyvktiqqtfiDNDKKHKADYE----------KQGNKYIA-QLEKLNNDSKDK-------FNDIPKE 198
Cdd:PRK09545 123 DDDHDHAGHEK-------------SDEDHHHGEYNmhiwlspeiaRATAVAIHdKLVELMPQSKAKldanlkdFEAQLAQ 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600122731 199 QRAMITSE-------------GAFKYFSKQYGITP-GYiWEINTEKQGTPEQMRQAIEFVKKHKLKHLLVETSVDKKAME 264
Cdd:PRK09545 190 TDKQIGNQlapvkgkgyfvfhDAYGYFEKHYGLTPlGH-FTVNPEIQPGAQRLHEIRTQLVEQKATCVFAEPQFRPAVIE 268
|
....*..
gi 600122731 265 SLSEETK 271
Cdd:PRK09545 269 SVAKGTS 275
|
|
| |
