|
Name |
Accession |
Description |
Interval |
E-value |
| PsaA |
cd01137 |
Metal binding protein PsaA. These proteins have been shown to function as initial receptors ... |
27-297 |
7.27e-145 |
|
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: 408.97 E-value: 7.27e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004419 27 QEKFRVITTFTVIADMAQNVAGDAAVVSSITKPGAEIHDYQPTPGDIKRAQGAQLILSNGLNLERWFARFYQHLQG-VPE 105
Cdd:cd01137 15 ASKLKVVATFSILADIARNIAGDRVNVTSIVPPGADPHEYEPTPSDIKKLSKADLILYNGLNLEPWLERLVKNAGKdVPV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004419 106 VVVSEGIQPMGISAGPYSGKPNPHAWMSADNALIYVDNIRDALVKYDPPHADTYRRNAEAYKEKIRQTMAPLQARLAQLP 185
Cdd:cd01137 95 VAVSEGIDPIPLEEGHYKGKPDPHAWMSPKNAIIYVKNIAKALSEADPANAETYQKNAAAYKAKLKALDEWAKAKFATIP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004419 186 ADKRWLVTSEGAFSYLARDYGLRELYLWPINADQQGTPQQVRKVIDTMKKERIPTIFSESTISDKPARQVAREAGAHYGG 265
Cdd:cd01137 175 AEKRKLVTSEGAFSYFAKAYGLKEAYLWPINTEEEGTPKQVATLIEQVKKEKVPAVFVESTVNDRLMKQVAKETGAKIGG 254
|
250 260 270
....*....|....*....|....*....|..
gi 489004419 266 VLYVDSLSAADGPVPTWLDLLRVTTETIVNGI 297
Cdd:cd01137 255 QLYTDSLSEKGGPADTYLDMMEHNLDTIVEGL 286
|
|
| ZnuA |
COG0803 |
ABC-type Zn uptake system ZnuABC, Zn-binding component ZnuA [Inorganic ion transport and ... |
27-289 |
8.59e-115 |
|
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: 332.59 E-value: 8.59e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004419 27 QEKFRVITTFTVIADMAQNVAGDAAVVSSITKPGAEIHDYQPTPGDIKRAQGAQLILSNGLNLERWFARFYQHLQ--GVP 104
Cdd:COG0803 27 AGKLKVVATFSPLADLAKQIGGDKVEVTSLVPPGADPHDYEPTPSDIAKLAKADLVVYNGLGLEGWLDKLLEAAGnpGVP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004419 105 EVVVSEGIQPMGISAGPYSGKPNPHAWMSADNALIYVDNIRDALVKYDPPHADTYRRNAEAYKEKIRQTMAPLQARLAQL 184
Cdd:COG0803 107 VVDASEGIDLLELEEGHDHGEPDPHVWLDPKNAKKVAENIADALAELDPANAAYYEANAAAYLAELDALDAEIKAKLAAI 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004419 185 PadKRWLVTSEGAFSYLARDYGLRELYLWPINADQQGTPQQVRKVIDTMKKERIPTIFSESTISDKPARQVAREAGAHyg 264
Cdd:COG0803 187 P--GRKLVTSHDAFGYLARAYGLEVVAIQGISPGSEPSPADLAELIDLIKEEGVKAIFVESQVSPKLAETLAEETGVK-- 262
|
250 260
....*....|....*....|....*
gi 489004419 265 gVLYVDSLSAADGPVPTWLDLLRVT 289
Cdd:COG0803 263 -VLYLDSLGGPGGPGDTYLDMMRHN 286
|
|
| ZnuA |
pfam01297 |
Zinc-uptake complex component A periplasmic; ZnuA includes periplasmic solute binding proteins ... |
32-296 |
3.89e-110 |
|
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: 320.27 E-value: 3.89e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004419 32 VITTFTVIADMAQNVAGDAAVVSSITKPGAEIHDYQPTPGDIKRAQGAQLILSNGLNLERWFARFYQHLQGVPEVVVSEG 111
Cdd:pfam01297 1 VVATTYPLADLAKQIGGDRVEVTSLVPPGADPHDYEPTPSDIAALSDADLVVYNGLGLEPWLDKLLEALPNKKVVDASEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004419 112 IQPMGISAGP-----YSGKPNPHAWMSADNALIYVDNIRDALVKYDPPHADTYRRNAEAYKEKIRQTMAPLQARLAQLPA 186
Cdd:pfam01297 81 VELLDEEGEEedhdgHDHGYDPHVWLDPKNAKKMAENIADALSELDPANAATYEANAAAYLAELDALDAEIKEQLASIPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004419 187 DKRWLVTSEGAFSYLARDYGLRELYLWPINADQQGTPQQVRKVIDTMKKERIPTIFSESTISDKPARQVAREAGAHYGGV 266
Cdd:pfam01297 161 KTRKLVTSHDAFGYLARAYGLEQVGIQGVSPESEPSAADLAELIDLIKEKKVKAIFVEPQVSPKLAETVAKETGVKVLGP 240
|
250 260 270
....*....|....*....|....*....|
gi 489004419 267 LYVDSLSAADGPVpTWLDLLRVTTETIVNG 296
Cdd:pfam01297 241 LYTDSLGEPGGGA-TYLDLMRHNLDTLAEA 269
|
|
| anch_rpt_subst |
TIGR03772 |
anchored repeat ABC transporter, substrate-binding protein; Members of this protein family are ... |
124-295 |
1.29e-24 |
|
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: 103.02 E-value: 1.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004419 124 GKPNPHAWMSADNALIYVDNIRDALVKYDPPHADTYRRNAEAYKEKIRQTMAPLQARLAQLPADKRWLVTSEGAFSYLAR 203
Cdd:TIGR03772 307 GEIDPHLWHNVKNAIAYVEVIRDKLIEVDPRGAQAYRSNASAYIHRLERLDTYVRRTIATIPPSRRHLITTHDAYSYLGQ 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004419 204 DYGLRELYLWPINADQQGTPQQVRKVIDTMKKERIPTIFSESTISDKPA--RQVAREAGAHYGGVlYVDSLsaaDGPVPT 281
Cdd:TIGR03772 387 AYGLNIAGFVTPNPAVEPSLADRRRLTRTIENLKVPAVFLEPNLAARSTtlNEIADELGVRVCAI-YGDTF---DDDVTN 462
|
170
....*....|....
gi 489004419 282 WLDLLRVTTETIVN 295
Cdd:TIGR03772 463 YVDLMRFNADSLAD 476
|
|
| znuA |
PRK09545 |
zinc ABC transporter substrate-binding protein ZnuA; |
32-216 |
3.54e-05 |
|
zinc ABC transporter substrate-binding protein ZnuA;
Pssm-ID: 236558 [Multi-domain] Cd Length: 311 Bit Score: 44.61 E-value: 3.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004419 32 VITTFTVIADMAQNVAGDAAVVSSItKP---------------------GAEIHDYQPTPGDIKRAQGAQLILSNGLNLE 90
Cdd:PRK09545 7 LFAALLAALLGGATQAANAAVVTSI-KPlgfiasaiadgvtetevllpdGASPHDYSLRPSDVKRLQSADLVVWVGPEME 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004419 91 RWFARFYQHLQGVPEVVVSE--GIQPMGISA--------------------GPYSGKPNPHAWMSADNALIYVDNIRDAL 148
Cdd:PRK09545 86 AFLEKPVSKLPENKQVTIAQlpDVKPLLMKGahddhhdddhdhagheksdeDHHHGEYNMHIWLSPEIARATAVAIHDKL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489004419 149 VKYDPPHAD-------TYRRNAEAYKEKIRQTMAPLQarlaqlpaDKRWLVTSEgAFSYLARDYGLRELYLWPIN 216
Cdd:PRK09545 166 VELMPQSKAkldanlkDFEAQLAQTDKQIGNQLAPVK--------GKGYFVFHD-AYGYFEKHYGLTPLGHFTVN 231
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PsaA |
cd01137 |
Metal binding protein PsaA. These proteins have been shown to function as initial receptors ... |
27-297 |
7.27e-145 |
|
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: 408.97 E-value: 7.27e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004419 27 QEKFRVITTFTVIADMAQNVAGDAAVVSSITKPGAEIHDYQPTPGDIKRAQGAQLILSNGLNLERWFARFYQHLQG-VPE 105
Cdd:cd01137 15 ASKLKVVATFSILADIARNIAGDRVNVTSIVPPGADPHEYEPTPSDIKKLSKADLILYNGLNLEPWLERLVKNAGKdVPV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004419 106 VVVSEGIQPMGISAGPYSGKPNPHAWMSADNALIYVDNIRDALVKYDPPHADTYRRNAEAYKEKIRQTMAPLQARLAQLP 185
Cdd:cd01137 95 VAVSEGIDPIPLEEGHYKGKPDPHAWMSPKNAIIYVKNIAKALSEADPANAETYQKNAAAYKAKLKALDEWAKAKFATIP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004419 186 ADKRWLVTSEGAFSYLARDYGLRELYLWPINADQQGTPQQVRKVIDTMKKERIPTIFSESTISDKPARQVAREAGAHYGG 265
Cdd:cd01137 175 AEKRKLVTSEGAFSYFAKAYGLKEAYLWPINTEEEGTPKQVATLIEQVKKEKVPAVFVESTVNDRLMKQVAKETGAKIGG 254
|
250 260 270
....*....|....*....|....*....|..
gi 489004419 266 VLYVDSLSAADGPVPTWLDLLRVTTETIVNGI 297
Cdd:cd01137 255 QLYTDSLSEKGGPADTYLDMMEHNLDTIVEGL 286
|
|
| ZnuA |
COG0803 |
ABC-type Zn uptake system ZnuABC, Zn-binding component ZnuA [Inorganic ion transport and ... |
27-289 |
8.59e-115 |
|
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: 332.59 E-value: 8.59e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004419 27 QEKFRVITTFTVIADMAQNVAGDAAVVSSITKPGAEIHDYQPTPGDIKRAQGAQLILSNGLNLERWFARFYQHLQ--GVP 104
Cdd:COG0803 27 AGKLKVVATFSPLADLAKQIGGDKVEVTSLVPPGADPHDYEPTPSDIAKLAKADLVVYNGLGLEGWLDKLLEAAGnpGVP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004419 105 EVVVSEGIQPMGISAGPYSGKPNPHAWMSADNALIYVDNIRDALVKYDPPHADTYRRNAEAYKEKIRQTMAPLQARLAQL 184
Cdd:COG0803 107 VVDASEGIDLLELEEGHDHGEPDPHVWLDPKNAKKVAENIADALAELDPANAAYYEANAAAYLAELDALDAEIKAKLAAI 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004419 185 PadKRWLVTSEGAFSYLARDYGLRELYLWPINADQQGTPQQVRKVIDTMKKERIPTIFSESTISDKPARQVAREAGAHyg 264
Cdd:COG0803 187 P--GRKLVTSHDAFGYLARAYGLEVVAIQGISPGSEPSPADLAELIDLIKEEGVKAIFVESQVSPKLAETLAEETGVK-- 262
|
250 260
....*....|....*....|....*
gi 489004419 265 gVLYVDSLSAADGPVPTWLDLLRVT 289
Cdd:COG0803 263 -VLYLDSLGGPGGPGDTYLDMMRHN 286
|
|
| ZnuA |
pfam01297 |
Zinc-uptake complex component A periplasmic; ZnuA includes periplasmic solute binding proteins ... |
32-296 |
3.89e-110 |
|
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: 320.27 E-value: 3.89e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004419 32 VITTFTVIADMAQNVAGDAAVVSSITKPGAEIHDYQPTPGDIKRAQGAQLILSNGLNLERWFARFYQHLQGVPEVVVSEG 111
Cdd:pfam01297 1 VVATTYPLADLAKQIGGDRVEVTSLVPPGADPHDYEPTPSDIAALSDADLVVYNGLGLEPWLDKLLEALPNKKVVDASEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004419 112 IQPMGISAGP-----YSGKPNPHAWMSADNALIYVDNIRDALVKYDPPHADTYRRNAEAYKEKIRQTMAPLQARLAQLPA 186
Cdd:pfam01297 81 VELLDEEGEEedhdgHDHGYDPHVWLDPKNAKKMAENIADALSELDPANAATYEANAAAYLAELDALDAEIKEQLASIPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004419 187 DKRWLVTSEGAFSYLARDYGLRELYLWPINADQQGTPQQVRKVIDTMKKERIPTIFSESTISDKPARQVAREAGAHYGGV 266
Cdd:pfam01297 161 KTRKLVTSHDAFGYLARAYGLEQVGIQGVSPESEPSAADLAELIDLIKEKKVKAIFVEPQVSPKLAETVAKETGVKVLGP 240
|
250 260 270
....*....|....*....|....*....|
gi 489004419 267 LYVDSLSAADGPVpTWLDLLRVTTETIVNG 296
Cdd:pfam01297 241 LYTDSLGEPGGGA-TYLDLMRHNLDTLAEA 269
|
|
| AdcA |
cd01017 |
Metal binding protein AdcA. These proteins have been shown to function in the ABC uptake of ... |
27-298 |
3.21e-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: 200.98 E-value: 3.21e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004419 27 QEKFRVITTFTVIADMAQNVAGDAAVVSSITKPGAEIHDYQPTPGDIKRAQGAQLILSNGLNLERWFARFYQHLQGvPEV 106
Cdd:cd01017 1 SGKLKVVTTFYPLYEFTKAIGGDKADVKLIIPAGTEPHDFEPSPKDIARIADADVFVYNGLGMETWAEKVLKSLQN-KKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004419 107 VV---SEGIQPM---------GISAGPYSGKPNPHAWMSADNALIYVDNIRDALVKYDPPHADTYRRNAEAYKEKIRQTM 174
Cdd:cd01017 80 KVveaSKGIKLLkaggaehdhDHSHSHHHGDYDPHVWLSPVLAIQQVENIKDALIKLDPDNKEYYEKNAAAYAKKLEALD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004419 175 APLQARLAQLPADKrwLVTSEGAFSYLARDYGLRELYLWPINADQQGTPQQVRKVIDTMKKERIPTIFSESTISDKPARQ 254
Cdd:cd01017 160 QEYRAKLAKAKGKT--FVTQHAAFGYLARRYGLKQIAIVGVSPEVEPSPKQLAELVEFVKKSDVKYIFFEENASSKIAET 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 489004419 255 VAREAGA------HYGGVLYVDSLSAADgpvptWLDLLRVTTETIVNGIQ 298
Cdd:cd01017 238 LAKETGAkllvlnPLETLTKEEIDDGKD-----YFSLMKENLETLKRALK 282
|
|
| TroA |
cd01016 |
Metal binding protein TroA. These proteins have been shown to function as initial receptors in ... |
29-295 |
1.03e-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: 158.30 E-value: 1.03e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004419 29 KFRVITTFTVIADMAQNVAGDAAVVSSITKPGAEIHDYQPTPGDIKRAQGAQLILSNGLNLERWFARFYQHL-QGVPEVV 107
Cdd:cd01016 1 KPNVVTTTGMIADAVENIGGDHVEVTGLMGPGVDPHLYKATAGDVEKLQNADVVFYNGLHLEGKMSDVLSKLgSSKSVIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004419 108 VSEGIQPMGISAGPYSGKPNPHAWMSADNALIYVDNIRDALVKYDPPHADTYRRNAEAYKEKIRQTMAPLQARLAQLPAD 187
Cdd:cd01016 81 LEDTLDRSQLILDEEEGTYDPHIWFDVKLWKYAVKAVAEVLSEKLPEHKDEFQANSEAYVEELDSLDAYAKKKIAEIPEQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004419 188 KRWLVTSEGAFSYLARDYGLRELYLWPINADQQGTPQQVRKVIDTMKKERIPTIFSESTISDKP--ARQVAREAGAH--- 262
Cdd:cd01016 161 QRVLVTAHDAFGYFGRAYGFEVKGLQGISTDSEAGLRDINELVDLIVERKIKAIFVESSVNQKSieALQDAVKARGHdvq 240
|
250 260 270
....*....|....*....|....*....|...
gi 489004419 263 YGGVLYVDSLSAADGPVPTWLDLLRVTTETIVN 295
Cdd:cd01016 241 IGGELYSDAMGEEGTSEGTYIGMFKHNVDTIVE 273
|
|
| ZntC |
cd01018 |
Metal binding protein ZntC. These proteins are predicted to function as initial receptors in ... |
46-295 |
4.58e-41 |
|
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: 143.27 E-value: 4.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004419 46 VAGDAAVVSSITKPGAEIHDYQPTPGDIKRAQGAQLILSNGLNLE-RWFARFYQHLQGVPEVVVSEGIQPMGISAGPYS- 123
Cdd:cd01018 19 IAGDTVDVVVLVPPGSNPHTYEPKPQQMKKLSEADLYFRIGLGFEeVWLERFRSNNPKMQVVNMSKGITLIPMADHHHHh 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004419 124 ---------GKPNPHAWMSADNALIYVDNIRDALVKYDPPHADTYRRNAEAYKEKIRQTMAPLQARLAQLPaDKRWLVtS 194
Cdd:cd01018 99 hgehehhhhGNYDPHIWLSPANAKIMAENIYEALAELDPQNATYYQANLDALLAELDALDSEIRTILSKLK-QRAFMV-Y 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004419 195 EGAFSYLARDYGLRELylwPINAD-QQGTPQQVRKVIDTMKKERIPTIFSESTISDKPARQVAREAGAHyggVLYVDSLS 273
Cdd:cd01018 177 HPAWGYFARDYGLTQI---PIEEEgKEPSPADLKRLIDLAKEKGVRVVFVQPQFSTKSAEAIAREIGAK---VVTIDPLA 250
|
250 260
....*....|....*....|..
gi 489004419 274 AadgpvpTWLDLLRVTTETIVN 295
Cdd:cd01018 251 A------DWEENLLKVADAFAH 266
|
|
| ZnuA |
cd01019 |
Zinc binding protein ZnuA. These proteins have been shown to function as initial receptors in ... |
27-261 |
4.13e-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: 4.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004419 27 QEKFRVITTFTVIADMAQNVAGDAAVVSSITKPGAEIHDYQPTPGDIKRAQGAQLILSNGLNLERWFARFYQHLQGVPEV 106
Cdd:cd01019 1 AAEASVLTSIKPLGFIAAAIMGGVGEVEVLVPPGASPHDYELRPSDARKLQEADLVVWIGPDLEAFLDKVLQGRKKGKVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004419 107 VVSEGI----QPMGISAGPYSGKP---------------NPHAWMSADNALIYVDNIRDALVKYDPPHADTYRRNAEAYK 167
Cdd:cd01019 81 TLAKLIdlktLEDGASHGDHEHDHehahgehdgheegglDPHLWLSPENAAEVAQAVAEKLSALDPDNAATYAANLEAFN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004419 168 EKIRQTMAPLQARLAqlPADKRWLVTSEGAFSYLARDYGLRELYLWPINADQQGTPQQVRKVIDTMKKERIPTIFSESTI 247
Cdd:cd01019 161 ARLAELDATIKERLA--PVKTKPFFVFHDAYGYFEKRYGLTQAGVFTIDPEIDPGAKRLAKIRKEIKEKGATCVFAEPQF 238
|
250
....*....|....
gi 489004419 248 SDKPARQVAREAGA 261
Cdd:cd01019 239 HPKIAETLAEGTGA 252
|
|
| ZnuA |
COG4531 |
ABC-type Zn2+ transport system, periplasmic component/surface adhesin ZnuA [Inorganic ion ... |
31-264 |
4.25e-25 |
|
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: 101.83 E-value: 4.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004419 31 RVITTFTVIADMAQNVAGDAAVVSSITKPGAEIHDYQPTPGDIKRAQGAQLILSNGLNLERWFARFYQHLQGVPEVVV-- 108
Cdd:COG4531 11 RVVTSIKPLHSLVAAVMDGVGEPELLLPPGASPHDYALRPSDARALQDADLVFWVGPDLEPFLEKPLETLAPDAKVVEll 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004419 109 -SEGIQPMGISAGPYS------------------------GKPNPHAWMSADNALIYVDNIRDALVKYDPPHADTYRRNA 163
Cdd:COG4531 91 eLPGLTLLPFREGGDFehhdhhdehhhhhhhhddhhdhhhGGYDPHLWLSPENAKAWAAAIADALSELDPENAATYQANA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004419 164 EAYKEKIRQTMAPLQARLAQLpADKRWLVTSEgAFSYLARDYGLRELYLWPINADQQGTPQQVRKVIDTMKKERIPTIFS 243
Cdd:COG4531 171 AAFEARLDALDAEIAAQLAPV-KGKPFFVFHD-AYQYFEKRFGLNALGAITLNPEIQPGAKRLAEIREKLKELGAVCVFA 248
|
250 260
....*....|....*....|.
gi 489004419 244 ESTISDKPARQVAREAGAHYG 264
Cdd:COG4531 249 EPQFNPALVETVAEGTGVRTG 269
|
|
| anch_rpt_subst |
TIGR03772 |
anchored repeat ABC transporter, substrate-binding protein; Members of this protein family are ... |
124-295 |
1.29e-24 |
|
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: 103.02 E-value: 1.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004419 124 GKPNPHAWMSADNALIYVDNIRDALVKYDPPHADTYRRNAEAYKEKIRQTMAPLQARLAQLPADKRWLVTSEGAFSYLAR 203
Cdd:TIGR03772 307 GEIDPHLWHNVKNAIAYVEVIRDKLIEVDPRGAQAYRSNASAYIHRLERLDTYVRRTIATIPPSRRHLITTHDAYSYLGQ 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004419 204 DYGLRELYLWPINADQQGTPQQVRKVIDTMKKERIPTIFSESTISDKPA--RQVAREAGAHYGGVlYVDSLsaaDGPVPT 281
Cdd:TIGR03772 387 AYGLNIAGFVTPNPAVEPSLADRRRLTRTIENLKVPAVFLEPNLAARSTtlNEIADELGVRVCAI-YGDTF---DDDVTN 462
|
170
....*....|....
gi 489004419 282 WLDLLRVTTETIVN 295
Cdd:TIGR03772 463 YVDLMRFNADSLAD 476
|
|
| TroA_b |
cd01020 |
Metal binding protein TroA_b. These proteins are predicted to function as initial receptors ... |
29-262 |
2.78e-24 |
|
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: 99.05 E-value: 2.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004419 29 KFRVITTFTVIADMAQNVAGDAAVVSSI-TKPGAEIHDYQPTPGDIKRAQGAQLILSNGLNLERWfarFYQHLQGVPEVV 107
Cdd:cd01020 2 KINVVASTNFWGSVAEAVGGDHVEVTSIiTNPDVDPHDFEPTPTDAAKVSTADIVVYNGGGYDPW---MTKLLADTKDVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004419 108 VSEgiqpMGISAGPYSGKPNPHAWMSADNALIYVDNIRDALVKYDPPHADTYRRNAEAYKEKirqtMAPLQARLAQLPAD 187
Cdd:cd01020 79 VIA----ADLDGHDDKEGDNPHLWYDPETMSKVANALADALVKADPDNKKYYQANAKKFVAS----LKPLAAKIAELSAK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004419 188 ---KRWLVTsEGAFSYLARDYGLRE----LYLWPINADQQGTPQQVRKVIDTMKKERIPTIFSESTISDKPARQVAREAG 260
Cdd:cd01020 151 ykgAPVAAT-EPVFDYLLDALGMKErtpkGYTATTESETEPSPADIAAFQNAIKNRQIDALIVNPQQASSATTNITGLAK 229
|
..
gi 489004419 261 AH 262
Cdd:cd01020 230 RS 231
|
|
| TroA_c |
cd01145 |
Periplasmic binding protein TroA_c. These proteins are predicted to function as initial ... |
32-210 |
1.72e-21 |
|
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: 89.87 E-value: 1.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004419 32 VITTFTVIADMAQNVAGDAAVVSSITKPGAEIHDYQPTPGDIKRAQGAQLILSNGLNLERWFARFyQHLQGVPEV----- 106
Cdd:cd01145 5 VVVTFPDLKDLVREVAGDAVIVSALTPPGVDPHQYQLKPSDIAKMRKADLVVTSGHELEGFEPKL-AELSSNSKVqpgik 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004419 107 ---VVSEGIQPMGISAGPYSGKPNPHAWMSADNALIYVDNIRDALVKYDPPHADTYRRNAEAYKEKIrQTMAPLQARLAQ 183
Cdd:cd01145 84 iliEDSDTVGMVDRAMGDYHGKGNPHVWLDPNNAPALAKALADALIELDPSEQEEYKENLRVFLAKL-NKLLREWERQFE 162
|
170 180
....*....|....*....|....*..
gi 489004419 184 LPADKRwLVTSEGAFSYLARDYGLREL 210
Cdd:cd01145 163 GLKGIQ-VVAYHPSYQYLADWLGIEVV 188
|
|
| znuA |
PRK09545 |
zinc ABC transporter substrate-binding protein ZnuA; |
32-216 |
3.54e-05 |
|
zinc ABC transporter substrate-binding protein ZnuA;
Pssm-ID: 236558 [Multi-domain] Cd Length: 311 Bit Score: 44.61 E-value: 3.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004419 32 VITTFTVIADMAQNVAGDAAVVSSItKP---------------------GAEIHDYQPTPGDIKRAQGAQLILSNGLNLE 90
Cdd:PRK09545 7 LFAALLAALLGGATQAANAAVVTSI-KPlgfiasaiadgvtetevllpdGASPHDYSLRPSDVKRLQSADLVVWVGPEME 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004419 91 RWFARFYQHLQGVPEVVVSE--GIQPMGISA--------------------GPYSGKPNPHAWMSADNALIYVDNIRDAL 148
Cdd:PRK09545 86 AFLEKPVSKLPENKQVTIAQlpDVKPLLMKGahddhhdddhdhagheksdeDHHHGEYNMHIWLSPEIARATAVAIHDKL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489004419 149 VKYDPPHAD-------TYRRNAEAYKEKIRQTMAPLQarlaqlpaDKRWLVTSEgAFSYLARDYGLRELYLWPIN 216
Cdd:PRK09545 166 VELMPQSKAkldanlkDFEAQLAQTDKQIGNQLAPVK--------GKGYFVFHD-AYGYFEKHYGLTPLGHFTVN 231
|
|
| PLN00061 |
PLN00061 |
photosystem II protein Psb27; Provisional |
123-172 |
6.76e-03 |
|
photosystem II protein Psb27; Provisional
Pssm-ID: 215043 Cd Length: 150 Bit Score: 36.35 E-value: 6.76e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 489004419 123 SGKPNPHAWMSAdnALIYVDNIRDALvKYDPPHADTYRRNAEAYKEKIRQ 172
Cdd:PLN00061 48 SGKKLPKAYLKS--AREVVKTLRESL-KEDPKDEAKFRRTADAAKESIRE 94
|
|
| |
