|
Name |
Accession |
Description |
Interval |
E-value |
| PsaA |
cd01137 |
Metal binding protein PsaA. These proteins have been shown to function as initial receptors ... |
19-313 |
4.02e-120 |
|
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: 346.57 E-value: 4.02e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 19 LGIVAALLTGAAYAA-PLPVVTSFSILGDVAKQIGGDRVAVQSLVGPNQDSHAYHMTSGDIKKIRSAKLVLLNGLGLEAa 97
Cdd:cd01137 1 LAACASLGSSPATAAsKLKVVATFSILADIARNIAGDRVNVTSIVPPGADPHEYEPTPSDIKKLSKADLILYNGLNLEP- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 98 DVQRAVK--QSKVPFAEATKGIQALKAEEGGHHHDHdheghhhdhgefDPHVWTDPVLMGTYAQNVANALIQADPEGKTY 175
Cdd:cd01137 80 WLERLVKnaGKDVPVVAVSEGIDPIPLEEGHYKGKP------------DPHAWMSPKNAIIYVKNIAKALSEADPANAET 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 176 YQQRLGNYQMQLKKLHSDAQAAFNAVPAAKRKVLTGHDAFSYMGKRYNIEFIAPQGVSSEAEPSAKQVASIIRQIKREGI 255
Cdd:cd01137 148 YQKNAAAYKAKLKALDEWAKAKFATIPAEKRKLVTSEGAFSYFAKAYGLKEAYLWPINTEEEGTPKQVATLIEQVKKEKV 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 256 KAVFTENIKDTRMIDRIAKETGVNVSGRLYSDALG--GAPANSYIGMYRYNVKVMTDAMK 313
Cdd:cd01137 228 PAVFVESTVNDRLMKQVAKETGAKIGGQLYTDSLSekGGPADTYLDMMEHNLDTIVEGLG 287
|
|
| ZnuA |
COG0803 |
ABC-type Zn uptake system ZnuABC, Zn-binding component ZnuA [Inorganic ion transport and ... |
14-304 |
5.25e-99 |
|
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: 292.92 E-value: 5.25e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 14 MKHWKLGIVAALL--------TGAAYAAPLPVVTSFSILGDVAKQIGGDRVAVQSLVGPNQDSHAYHMTSGDIKKIRSAK 85
Cdd:COG0803 1 MKRLLLALLLLAAlllagcsaAASSAAGKLKVVATFSPLADLAKQIGGDKVEVTSLVPPGADPHDYEPTPSDIAKLAKAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 86 LVLLNGLGLE--AADVQRAVKQSKVPFAEATKGIQALKAEEGGHHHDhdheghhhdhgeFDPHVWTDPVLMGTYAQNVAN 163
Cdd:COG0803 81 LVVYNGLGLEgwLDKLLEAAGNPGVPVVDASEGIDLLELEEGHDHGE------------PDPHVWLDPKNAKKVAENIAD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 164 ALIQADPEGKTYYQQRLGNYQMQLKKLHSDAQAAFNAVPaaKRKVLTGHDAFSYMGKRYNIEFIAPQGVSSEAEPSAKQV 243
Cdd:COG0803 149 ALAELDPANAAYYEANAAAYLAELDALDAEIKAKLAAIP--GRKLVTSHDAFGYLARAYGLEVVAIQGISPGSEPSPADL 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1080520315 244 ASIIRQIKREGIKAVFTENIKDTRMIDRIAKETGVNVsgrLYSDALGGA--PANSYIGMYRYN 304
Cdd:COG0803 227 AELIDLIKEEGVKAIFVESQVSPKLAETLAEETGVKV---LYLDSLGGPggPGDTYLDMMRHN 286
|
|
| ZnuA |
pfam01297 |
Zinc-uptake complex component A periplasmic; ZnuA includes periplasmic solute binding proteins ... |
37-311 |
1.22e-97 |
|
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: 288.68 E-value: 1.22e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 37 VVTSFSILGDVAKQIGGDRVAVQSLVGPNQDSHAYHMTSGDIKKIRSAKLVLLNGLGLEAAdVQRAVKQS-KVPFAEATK 115
Cdd:pfam01297 1 VVATTYPLADLAKQIGGDRVEVTSLVPPGADPHDYEPTPSDIAALSDADLVVYNGLGLEPW-LDKLLEALpNKKVVDASE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 116 GIQALKAEEGGHHHDHDHEGhhhdhgeFDPHVWTDPVLMGTYAQNVANALIQADPEGKTYYQQRLGNYQMQLKKLHSDAQ 195
Cdd:pfam01297 80 GVELLDEEGEEEDHDGHDHG-------YDPHVWLDPKNAKKMAENIADALSELDPANAATYEANAAAYLAELDALDAEIK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 196 AAFNAVPAAKRKVLTGHDAFSYMGKRYNIEFIAPQGVSSEAEPSAKQVASIIRQIKREGIKAVFTENIKDTRMIDRIAKE 275
Cdd:pfam01297 153 EQLASIPEKTRKLVTSHDAFGYLARAYGLEQVGIQGVSPESEPSAADLAELIDLIKEKKVKAIFVEPQVSPKLAETVAKE 232
|
250 260 270
....*....|....*....|....*....|....*..
gi 1080520315 276 TGVNVSGRLYSDALGGAPAN-SYIGMYRYNVKVMTDA 311
Cdd:pfam01297 233 TGVKVLGPLYTDSLGEPGGGaTYLDLMRHNLDTLAEA 269
|
|
| AztC |
NF040870 |
zinc ABC transporter substrate-binding protein AztC; |
37-312 |
3.62e-78 |
|
zinc ABC transporter substrate-binding protein AztC;
Pssm-ID: 468807 [Multi-domain] Cd Length: 277 Bit Score: 239.48 E-value: 3.62e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 37 VVTSFSILGDVAKQIGGDRVAVQSLVGPNQDSHAYHMTSGDIKKIRSAKLVLLNGLGLEAADVQRAVK--QSKVPFAEAT 114
Cdd:NF040870 1 VVVTTNILGDLARNVVGDRAEVTTLMKPDADPHSFEPSAADAAALERADLVVVNGLGLEEGFLRHLIAasATGAPVVEVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 115 KGIQALKaeegghHHDHDHEGHHHDHGEFDPHVWTDPVLMGTYAQNVANALIQADPEGKTYYQQRLGNYQMQLKKLHSDA 194
Cdd:NF040870 81 DGVDPLP------YPEGGHYHFEAGAGPPDPHFWTDPARARDAVDNIADAFCEADDGDCAAYRANAAAYRAELDELDAEM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 195 QAAFNAVPAAKRKVLTGHDAFSYMGKRYNIEFIA---PQGvSSEAEPSAKQVASIIRQIKREGIKAVFTENIKDTRMIDR 271
Cdd:NF040870 155 REAFAAIPADRRTLVTNHHVFGYLAERYGFRVLGaviPSG-STLASPSAADLASLARAIREAGVPAIFAESSQPPRLAEV 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1080520315 272 IAKETGVNVSG-RLYSDALGGA--PANSYIGMYRYNVKVMTDAM 312
Cdd:NF040870 234 LASEAGLDVGVvELYSESLSEPdgGAATYLDMMRANAEAIVDGL 277
|
|
| anch_rpt_subst |
TIGR03772 |
anchored repeat ABC transporter, substrate-binding protein; Members of this protein family are ... |
144-312 |
1.53e-19 |
|
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: 88.77 E-value: 1.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 144 DPHVWTDPVLMGTYAQNVANALIQADPEGKTYYQQRLGNYQMQLKKLHSDAQAAFNAVPAAKRKVLTGHDAFSYMGKRYN 223
Cdd:TIGR03772 310 DPHLWHNVKNAIAYVEVIRDKLIEVDPRGAQAYRSNASAYIHRLERLDTYVRRTIATIPPSRRHLITTHDAYSYLGQAYG 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 224 IE---FIAPqgvSSEAEPSAKQVASIIRQIKREGIKAVFTEN--IKDTRMIDRIAKETGVNVSgRLYSDALGGAPANsYI 298
Cdd:TIGR03772 390 LNiagFVTP---NPAVEPSLADRRRLTRTIENLKVPAVFLEPnlAARSTTLNEIADELGVRVC-AIYGDTFDDDVTN-YV 464
|
170
....*....|....
gi 1080520315 299 GMYRYNVKVMTDAM 312
Cdd:TIGR03772 465 DLMRFNADSLADCL 478
|
|
| Zn_bnd_ABC_AdcA |
NF033605 |
zinc ABC transporter substrate-binding lipoprotein AdcA; |
35-276 |
2.42e-16 |
|
zinc ABC transporter substrate-binding lipoprotein AdcA;
Pssm-ID: 468109 [Multi-domain] Cd Length: 516 Bit Score: 79.43 E-value: 2.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 35 LPVVTSFSILGDVAKQIGGDRVAVQSLVGPNQDSHAYHMTSGDIKKIRSAKLVLLNGLGLE--AADVQRAVKQS--KVPF 110
Cdd:NF033605 34 IKINTTVFPLKSFAEQIGGKHVEVESIYPAGTDLHSYEPTQKDILNASKADLFVYTGDDLDpvAKKVASTIKKDdkKLSL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 111 AEATKGIQAL-----KAEEGGHHHDHDHEGHHHDHGEFDPHVWTDPVLMGTYAQNVANALIQADPEGKTYYQQR------ 179
Cdd:NF033605 114 EDKLDKSTLLtdqheHGEEHEHEEEGHEHEHHHHHGGYDPHVWLDPKFDQTFAKEIKDELVKKDPKHKDEYEKNykklnk 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 180 -LGNYQMQLKKLHSDAQAafNAvpaakrkVLTGHDAFSYMGKRYNIEFIAPQGVSSEaEPSAKQVASIIRQIKREGIKAV 258
Cdd:NF033605 194 dLKGIDKDMKDITKDKQG--NA-------VFISHESLGYLADRYGFVQKGVQNMNAE-DPSQKELTEIVKEINDSGAKYI 263
|
250
....*....|....*...
gi 1080520315 259 FTENIKDTRMIDRIAKET 276
Cdd:NF033605 264 LYEDNVSNKVTDTIRKET 281
|
|
| znuA |
PRK09545 |
zinc ABC transporter substrate-binding protein ZnuA; |
18-297 |
1.19e-12 |
|
zinc ABC transporter substrate-binding protein ZnuA;
Pssm-ID: 236558 [Multi-domain] Cd Length: 311 Bit Score: 67.34 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 18 KLGIVAALLTGAAYAAPLPVVTSFSILGDVAKQIGGDRVAVQSLVGPNQDSHAYHMTSGDIKKIRSAKLVLLNGLGLEA- 96
Cdd:PRK09545 8 FAALLAALLGGATQAANAAVVTSIKPLGFIASAIADGVTETEVLLPDGASPHDYSLRPSDVKRLQSADLVVWVGPEMEAf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 97 --ADVQRAVKQSKVPFAEaTKGIQAL--KAEEGGHHHDHDHEGHHHDHGE------FDPHVWTDPVLMGTYAQNVANALI 166
Cdd:PRK09545 88 leKPVSKLPENKQVTIAQ-LPDVKPLlmKGAHDDHHDDDHDHAGHEKSDEdhhhgeYNMHIWLSPEIARATAVAIHDKLV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 167 QADPEGKTYYQQRLGNYQMQLKKlhSDAQAAFNAVPAAKRKVLTGHDAFSYMGKRYNiefIAPQG---VSSEAEPSAKQV 243
Cdd:PRK09545 167 ELMPQSKAKLDANLKDFEAQLAQ--TDKQIGNQLAPVKGKGYFVFHDAYGYFEKHYG---LTPLGhftVNPEIQPGAQRL 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1080520315 244 ASIIRQIKREGIKAVFTENIKDTRMIDRIAKETGVNVsGRLysDALGGAPA---NSY 297
Cdd:PRK09545 242 HEIRTQLVEQKATCVFAEPQFRPAVIESVAKGTSVRM-GTL--DPLGTNIKlgkDSY 295
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PsaA |
cd01137 |
Metal binding protein PsaA. These proteins have been shown to function as initial receptors ... |
19-313 |
4.02e-120 |
|
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: 346.57 E-value: 4.02e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 19 LGIVAALLTGAAYAA-PLPVVTSFSILGDVAKQIGGDRVAVQSLVGPNQDSHAYHMTSGDIKKIRSAKLVLLNGLGLEAa 97
Cdd:cd01137 1 LAACASLGSSPATAAsKLKVVATFSILADIARNIAGDRVNVTSIVPPGADPHEYEPTPSDIKKLSKADLILYNGLNLEP- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 98 DVQRAVK--QSKVPFAEATKGIQALKAEEGGHHHDHdheghhhdhgefDPHVWTDPVLMGTYAQNVANALIQADPEGKTY 175
Cdd:cd01137 80 WLERLVKnaGKDVPVVAVSEGIDPIPLEEGHYKGKP------------DPHAWMSPKNAIIYVKNIAKALSEADPANAET 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 176 YQQRLGNYQMQLKKLHSDAQAAFNAVPAAKRKVLTGHDAFSYMGKRYNIEFIAPQGVSSEAEPSAKQVASIIRQIKREGI 255
Cdd:cd01137 148 YQKNAAAYKAKLKALDEWAKAKFATIPAEKRKLVTSEGAFSYFAKAYGLKEAYLWPINTEEEGTPKQVATLIEQVKKEKV 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 256 KAVFTENIKDTRMIDRIAKETGVNVSGRLYSDALG--GAPANSYIGMYRYNVKVMTDAMK 313
Cdd:cd01137 228 PAVFVESTVNDRLMKQVAKETGAKIGGQLYTDSLSekGGPADTYLDMMEHNLDTIVEGLG 287
|
|
| ZnuA |
COG0803 |
ABC-type Zn uptake system ZnuABC, Zn-binding component ZnuA [Inorganic ion transport and ... |
14-304 |
5.25e-99 |
|
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: 292.92 E-value: 5.25e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 14 MKHWKLGIVAALL--------TGAAYAAPLPVVTSFSILGDVAKQIGGDRVAVQSLVGPNQDSHAYHMTSGDIKKIRSAK 85
Cdd:COG0803 1 MKRLLLALLLLAAlllagcsaAASSAAGKLKVVATFSPLADLAKQIGGDKVEVTSLVPPGADPHDYEPTPSDIAKLAKAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 86 LVLLNGLGLE--AADVQRAVKQSKVPFAEATKGIQALKAEEGGHHHDhdheghhhdhgeFDPHVWTDPVLMGTYAQNVAN 163
Cdd:COG0803 81 LVVYNGLGLEgwLDKLLEAAGNPGVPVVDASEGIDLLELEEGHDHGE------------PDPHVWLDPKNAKKVAENIAD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 164 ALIQADPEGKTYYQQRLGNYQMQLKKLHSDAQAAFNAVPaaKRKVLTGHDAFSYMGKRYNIEFIAPQGVSSEAEPSAKQV 243
Cdd:COG0803 149 ALAELDPANAAYYEANAAAYLAELDALDAEIKAKLAAIP--GRKLVTSHDAFGYLARAYGLEVVAIQGISPGSEPSPADL 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1080520315 244 ASIIRQIKREGIKAVFTENIKDTRMIDRIAKETGVNVsgrLYSDALGGA--PANSYIGMYRYN 304
Cdd:COG0803 227 AELIDLIKEEGVKAIFVESQVSPKLAETLAEETGVKV---LYLDSLGGPggPGDTYLDMMRHN 286
|
|
| ZnuA |
pfam01297 |
Zinc-uptake complex component A periplasmic; ZnuA includes periplasmic solute binding proteins ... |
37-311 |
1.22e-97 |
|
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: 288.68 E-value: 1.22e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 37 VVTSFSILGDVAKQIGGDRVAVQSLVGPNQDSHAYHMTSGDIKKIRSAKLVLLNGLGLEAAdVQRAVKQS-KVPFAEATK 115
Cdd:pfam01297 1 VVATTYPLADLAKQIGGDRVEVTSLVPPGADPHDYEPTPSDIAALSDADLVVYNGLGLEPW-LDKLLEALpNKKVVDASE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 116 GIQALKAEEGGHHHDHDHEGhhhdhgeFDPHVWTDPVLMGTYAQNVANALIQADPEGKTYYQQRLGNYQMQLKKLHSDAQ 195
Cdd:pfam01297 80 GVELLDEEGEEEDHDGHDHG-------YDPHVWLDPKNAKKMAENIADALSELDPANAATYEANAAAYLAELDALDAEIK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 196 AAFNAVPAAKRKVLTGHDAFSYMGKRYNIEFIAPQGVSSEAEPSAKQVASIIRQIKREGIKAVFTENIKDTRMIDRIAKE 275
Cdd:pfam01297 153 EQLASIPEKTRKLVTSHDAFGYLARAYGLEQVGIQGVSPESEPSAADLAELIDLIKEKKVKAIFVEPQVSPKLAETVAKE 232
|
250 260 270
....*....|....*....|....*....|....*..
gi 1080520315 276 TGVNVSGRLYSDALGGAPAN-SYIGMYRYNVKVMTDA 311
Cdd:pfam01297 233 TGVKVLGPLYTDSLGEPGGGaTYLDLMRHNLDTLAEA 269
|
|
| AztC |
NF040870 |
zinc ABC transporter substrate-binding protein AztC; |
37-312 |
3.62e-78 |
|
zinc ABC transporter substrate-binding protein AztC;
Pssm-ID: 468807 [Multi-domain] Cd Length: 277 Bit Score: 239.48 E-value: 3.62e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 37 VVTSFSILGDVAKQIGGDRVAVQSLVGPNQDSHAYHMTSGDIKKIRSAKLVLLNGLGLEAADVQRAVK--QSKVPFAEAT 114
Cdd:NF040870 1 VVVTTNILGDLARNVVGDRAEVTTLMKPDADPHSFEPSAADAAALERADLVVVNGLGLEEGFLRHLIAasATGAPVVEVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 115 KGIQALKaeegghHHDHDHEGHHHDHGEFDPHVWTDPVLMGTYAQNVANALIQADPEGKTYYQQRLGNYQMQLKKLHSDA 194
Cdd:NF040870 81 DGVDPLP------YPEGGHYHFEAGAGPPDPHFWTDPARARDAVDNIADAFCEADDGDCAAYRANAAAYRAELDELDAEM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 195 QAAFNAVPAAKRKVLTGHDAFSYMGKRYNIEFIA---PQGvSSEAEPSAKQVASIIRQIKREGIKAVFTENIKDTRMIDR 271
Cdd:NF040870 155 REAFAAIPADRRTLVTNHHVFGYLAERYGFRVLGaviPSG-STLASPSAADLASLARAIREAGVPAIFAESSQPPRLAEV 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1080520315 272 IAKETGVNVSG-RLYSDALGGA--PANSYIGMYRYNVKVMTDAM 312
Cdd:NF040870 234 LASEAGLDVGVvELYSESLSEPdgGAATYLDMMRANAEAIVDGL 277
|
|
| AdcA |
cd01017 |
Metal binding protein AdcA. These proteins have been shown to function in the ABC uptake of ... |
32-313 |
4.62e-69 |
|
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: 216.39 E-value: 4.62e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 32 AAPLPVVTSFSILGDVAKQIGGDRVAVQSLVGPNQDSHAYHMTSGDIKKIRSAKLVLLNGLGLE--AADVQRAVKQSKVP 109
Cdd:cd01017 1 SGKLKVVTTFYPLYEFTKAIGGDKADVKLIIPAGTEPHDFEPSPKDIARIADADVFVYNGLGMEtwAEKVLKSLQNKKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 110 FAEATKGIQALKAEEGGHHHDHDHEGHHHDhgeFDPHVWTDPVLMGTYAQNVANALIQADPEGKTYYQQRLGNYQMQLKK 189
Cdd:cd01017 81 VVEASKGIKLLKAGGAEHDHDHSHSHHHGD---YDPHVWLSPVLAIQQVENIKDALIKLDPDNKEYYEKNAAAYAKKLEA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 190 LHSDAQAAFNAvpAAKRKVLTGHDAFSYMGKRYNIEFIAPQGVSSEAEPSAKQVASIIRQIKREGIKAVFTENIKDTRMI 269
Cdd:cd01017 158 LDQEYRAKLAK--AKGKTFVTQHAAFGYLARRYGLKQIAIVGVSPEVEPSPKQLAELVEFVKKSDVKYIFFEENASSKIA 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1080520315 270 DRIAKETGVNVSgRLYSdaLGGAP------ANSYIGMYRYNVKVMTDAMK 313
Cdd:cd01017 236 ETLAKETGAKLL-VLNP--LETLTkeeiddGKDYFSLMKENLETLKRALK 282
|
|
| TroA |
cd01016 |
Metal binding protein TroA. These proteins have been shown to function as initial receptors in ... |
37-313 |
6.32e-64 |
|
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: 202.98 E-value: 6.32e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 37 VVTSFSILGDVAKQIGGDRVAVQSLVGPNQDSHAYHMTSGDIKKIRSAKLVLLNGLGLEA--ADVQRAVKQSKVPFAeAT 114
Cdd:cd01016 4 VVTTTGMIADAVENIGGDHVEVTGLMGPGVDPHLYKATAGDVEKLQNADVVFYNGLHLEGkmSDVLSKLGSSKSVIA-LE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 115 KGIqalkaeegghhhDHDHEGHHHDHGEFDPHVWTDPVLMGTYAQNVANALIQADPEGKTYYQQRLGNYQMQLKKLHSDA 194
Cdd:cd01016 83 DTL------------DRSQLILDEEEGTYDPHIWFDVKLWKYAVKAVAEVLSEKLPEHKDEFQANSEAYVEELDSLDAYA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 195 QAAFNAVPAAKRKVLTGHDAFSYMGKRYNIEFIAPQGVSSEAEPSAKQVASIIRQIKREGIKAVFTE---NIKDTRMIDR 271
Cdd:cd01016 151 KKKIAEIPEQQRVLVTAHDAFGYFGRAYGFEVKGLQGISTDSEAGLRDINELVDLIVERKIKAIFVEssvNQKSIEALQD 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1080520315 272 IAKETGVNVS--GRLYSDALG--GAPANSYIGMYRYNVKVMTDAMK 313
Cdd:cd01016 231 AVKARGHDVQigGELYSDAMGeeGTSEGTYIGMFKHNVDTIVEALK 276
|
|
| ZnuA |
cd01019 |
Zinc binding protein ZnuA. These proteins have been shown to function as initial receptors in ... |
37-304 |
1.91e-41 |
|
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: 145.21 E-value: 1.91e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 37 VVTSFSILGDVAKQIGGDRVAVQSLVGPNQDSHAYHMTSGDIKKIRSAKLVLLNGLGLEAADVQRAVKQSKVPFAEATKG 116
Cdd:cd01019 6 VLTSIKPLGFIAAAIMGGVGEVEVLVPPGASPHDYELRPSDARKLQEADLVVWIGPDLEAFLDKVLQGRKKGKVLTLAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 117 IQALKAEEGGHHHDHDHEGHHHDHGE-------FDPHVWTDPVLMGTYAQNVANALIQADPEGKTYYQQRLGNYQMQLKK 189
Cdd:cd01019 86 IDLKTLEDGASHGDHEHDHEHAHGEHdgheeggLDPHLWLSPENAAEVAQAVAEKLSALDPDNAATYAANLEAFNARLAE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 190 LhsDAQAAFNAVPAAKRKVLTGHDAFSYMGKRYNIEFIAPQGVSSEAEPSAKQVASIIRQIKREGIKAVFTENIKDTRMI 269
Cdd:cd01019 166 L--DATIKERLAPVKTKPFFVFHDAYGYFEKRYGLTQAGVFTIDPEIDPGAKRLAKIRKEIKEKGATCVFAEPQFHPKIA 243
|
250 260 270
....*....|....*....|....*....|....*...
gi 1080520315 270 DRIAKETGVNVsGRLysDALGG---APANSYIGMYRYN 304
Cdd:cd01019 244 ETLAEGTGAKV-GEL--DPLGGlieLGKNSYVNFLRNL 278
|
|
| ZntC |
cd01018 |
Metal binding protein ZntC. These proteins are predicted to function as initial receptors in ... |
48-280 |
5.16e-33 |
|
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: 122.47 E-value: 5.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 48 AKQIGGDRVAVQSLVGPNQDSHAYHMTSGDIKKIRSAKLVLLNGLGLEAADVQRAVK-QSKVPFAEATKGIQalKAEEGG 126
Cdd:cd01018 16 VEKIAGDTVDVVVLVPPGSNPHTYEPKPQQMKKLSEADLYFRIGLGFEEVWLERFRSnNPKMQVVNMSKGIT--LIPMAD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 127 HHHDHDHEGHHHDHGEFDPHVWTDPVLMGTYAQNVANALIQADPEGKTYYQQRLGNYQMQLKKLHSDAQAAFNAVPAakR 206
Cdd:cd01018 94 HHHHHHGEHEHHHHGNYDPHIWLSPANAKIMAENIYEALAELDPQNATYYQANLDALLAELDALDSEIRTILSKLKQ--R 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1080520315 207 KVLTGHDAFSYMGKRYNIEFIApqgVSSEA-EPSAKQVASIIRQIKREGIKAVFTENIKDTRMIDRIAKETGVNV 280
Cdd:cd01018 172 AFMVYHPAWGYFARDYGLTQIP---IEEEGkEPSPADLKRLIDLAKEKGVRVVFVQPQFSTKSAEAIAREIGAKV 243
|
|
| ZnuA |
COG4531 |
ABC-type Zn2+ transport system, periplasmic component/surface adhesin ZnuA [Inorganic ion ... |
26-302 |
9.18e-28 |
|
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: 109.15 E-value: 9.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 26 LTGAAYAAPLPVVTSFSILGDVAKQIGGDRVAVQSLVGPNQDSHAYHMTSGDIKKIRSAKLVLLNGLGLEA--ADV--QR 101
Cdd:COG4531 1 LASAAAAAAPRVVTSIKPLHSLVAAVMDGVGEPELLLPPGASPHDYALRPSDARALQDADLVFWVGPDLEPflEKPleTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 102 AVKQSKVPFAEATkGIQALKAEEGGHHHDHDHEGHHHDHGE------------FDPHVWTDPVLMGTYAQNVANALIQAD 169
Cdd:COG4531 81 APDAKVVELLELP-GLTLLPFREGGDFEHHDHHDEHHHHHHhhddhhdhhhggYDPHLWLSPENAKAWAAAIADALSELD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 170 PEGKTYYQQRLGNYQMQLKKLHSDAQAAFNavPAAKRKVLTGHDAFSYMGKRYNIEfiaPQG---VSSEAEPSAKQVASI 246
Cdd:COG4531 160 PENAATYQANAAAFEARLDALDAEIAAQLA--PVKGKPFFVFHDAYQYFEKRFGLN---ALGaitLNPEIQPGAKRLAEI 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1080520315 247 IRQIKREGIKAVFTENIKDTRMIDRIAKETGVNVsGRLysDALGG---APANSYIGMYR 302
Cdd:COG4531 235 REKLKELGAVCVFAEPQFNPALVETVAEGTGVRT-GVL--DPLGAdlePGPDLYFQLLR 290
|
|
| TroA_b |
cd01020 |
Metal binding protein TroA_b. These proteins are predicted to function as initial receptors ... |
33-280 |
2.95e-26 |
|
Metal binding protein TroA_b. These proteins are predicted to function as initial receptors in ABC transport of metal ions. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains. In addition, these proteins sometimes have a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence).
Pssm-ID: 238502 [Multi-domain] Cd Length: 264 Bit Score: 104.44 E-value: 2.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 33 APLPVVTSFSILGDVAKQIGGDRVAVQSLVG-PNQDSHAYHMTSGDIKKIRSAKLVLLNGLGLEAAdvqravkqskvpfa 111
Cdd:cd01020 1 GKINVVASTNFWGSVAEAVGGDHVEVTSIITnPDVDPHDFEPTPTDAAKVSTADIVVYNGGGYDPW-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 112 eATKGIQALKAEEGGHHHDHDHEGHHHDhgefDPHVWTDPVLMGTYAQNVANALIQADPEGKTYYQQRLGNYQMQLKKLH 191
Cdd:cd01020 67 -MTKLLADTKDVIVIAADLDGHDDKEGD----NPHLWYDPETMSKVANALADALVKADPDNKKYYQANAKKFVASLKPLA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 192 SdAQAAFNAVPAAKRkVLTGHDAFSYMGKRYNIEFIAPQG----VSSEAEPSAKQVASIIRQIKREGIKAVF---TENIK 264
Cdd:cd01020 142 A-KIAELSAKYKGAP-VAATEPVFDYLLDALGMKERTPKGytatTESETEPSPADIAAFQNAIKNRQIDALIvnpQQASS 219
|
250
....*....|....*.
gi 1080520315 265 DTRMIDRIAKETGVNV 280
Cdd:cd01020 220 ATTNITGLAKRSGVPV 235
|
|
| TroA_c |
cd01145 |
Periplasmic binding protein TroA_c. These proteins are predicted to function as initial ... |
33-228 |
1.03e-23 |
|
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: 96.03 E-value: 1.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 33 APLPVVTSFSILGDVAKQIGGDRVAVQSLVGPNQDSHAYHMTSGDIKKIRSAKLVLLNGLGLEAADvQRAVKQSKVPFAE 112
Cdd:cd01145 1 AALNVVVTFPDLKDLVREVAGDAVIVSALTPPGVDPHQYQLKPSDIAKMRKADLVVTSGHELEGFE-PKLAELSSNSKVQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 113 atKGIQALKAEEGGHHHDHDHEGHHHDHGefDPHVWTDPVLMGTYAQNVANALIQADPEGKTYYQQRLGNYQMQLKKLHS 192
Cdd:cd01145 80 --PGIKILIEDSDTVGMVDRAMGDYHGKG--NPHVWLDPNNAPALAKALADALIELDPSEQEEYKENLRVFLAKLNKLLR 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 1080520315 193 DAQAAFNavPAAKRKVLTGHDAFSYMGKRYNIEFIA 228
Cdd:cd01145 156 EWERQFE--GLKGIQVVAYHPSYQYLADWLGIEVVA 189
|
|
| anch_rpt_subst |
TIGR03772 |
anchored repeat ABC transporter, substrate-binding protein; Members of this protein family are ... |
144-312 |
1.53e-19 |
|
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: 88.77 E-value: 1.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 144 DPHVWTDPVLMGTYAQNVANALIQADPEGKTYYQQRLGNYQMQLKKLHSDAQAAFNAVPAAKRKVLTGHDAFSYMGKRYN 223
Cdd:TIGR03772 310 DPHLWHNVKNAIAYVEVIRDKLIEVDPRGAQAYRSNASAYIHRLERLDTYVRRTIATIPPSRRHLITTHDAYSYLGQAYG 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 224 IE---FIAPqgvSSEAEPSAKQVASIIRQIKREGIKAVFTEN--IKDTRMIDRIAKETGVNVSgRLYSDALGGAPANsYI 298
Cdd:TIGR03772 390 LNiagFVTP---NPAVEPSLADRRRLTRTIENLKVPAVFLEPnlAARSTTLNEIADELGVRVC-AIYGDTFDDDVTN-YV 464
|
170
....*....|....
gi 1080520315 299 GMYRYNVKVMTDAM 312
Cdd:TIGR03772 465 DLMRFNADSLADCL 478
|
|
| Zn_bnd_ABC_AdcA |
NF033605 |
zinc ABC transporter substrate-binding lipoprotein AdcA; |
35-276 |
2.42e-16 |
|
zinc ABC transporter substrate-binding lipoprotein AdcA;
Pssm-ID: 468109 [Multi-domain] Cd Length: 516 Bit Score: 79.43 E-value: 2.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 35 LPVVTSFSILGDVAKQIGGDRVAVQSLVGPNQDSHAYHMTSGDIKKIRSAKLVLLNGLGLE--AADVQRAVKQS--KVPF 110
Cdd:NF033605 34 IKINTTVFPLKSFAEQIGGKHVEVESIYPAGTDLHSYEPTQKDILNASKADLFVYTGDDLDpvAKKVASTIKKDdkKLSL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 111 AEATKGIQAL-----KAEEGGHHHDHDHEGHHHDHGEFDPHVWTDPVLMGTYAQNVANALIQADPEGKTYYQQR------ 179
Cdd:NF033605 114 EDKLDKSTLLtdqheHGEEHEHEEEGHEHEHHHHHGGYDPHVWLDPKFDQTFAKEIKDELVKKDPKHKDEYEKNykklnk 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 180 -LGNYQMQLKKLHSDAQAafNAvpaakrkVLTGHDAFSYMGKRYNIEFIAPQGVSSEaEPSAKQVASIIRQIKREGIKAV 258
Cdd:NF033605 194 dLKGIDKDMKDITKDKQG--NA-------VFISHESLGYLADRYGFVQKGVQNMNAE-DPSQKELTEIVKEINDSGAKYI 263
|
250
....*....|....*...
gi 1080520315 259 FTENIKDTRMIDRIAKET 276
Cdd:NF033605 264 LYEDNVSNKVTDTIRKET 281
|
|
| znuA |
PRK09545 |
zinc ABC transporter substrate-binding protein ZnuA; |
18-297 |
1.19e-12 |
|
zinc ABC transporter substrate-binding protein ZnuA;
Pssm-ID: 236558 [Multi-domain] Cd Length: 311 Bit Score: 67.34 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 18 KLGIVAALLTGAAYAAPLPVVTSFSILGDVAKQIGGDRVAVQSLVGPNQDSHAYHMTSGDIKKIRSAKLVLLNGLGLEA- 96
Cdd:PRK09545 8 FAALLAALLGGATQAANAAVVTSIKPLGFIASAIADGVTETEVLLPDGASPHDYSLRPSDVKRLQSADLVVWVGPEMEAf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 97 --ADVQRAVKQSKVPFAEaTKGIQAL--KAEEGGHHHDHDHEGHHHDHGE------FDPHVWTDPVLMGTYAQNVANALI 166
Cdd:PRK09545 88 leKPVSKLPENKQVTIAQ-LPDVKPLlmKGAHDDHHDDDHDHAGHEKSDEdhhhgeYNMHIWLSPEIARATAVAIHDKLV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520315 167 QADPEGKTYYQQRLGNYQMQLKKlhSDAQAAFNAVPAAKRKVLTGHDAFSYMGKRYNiefIAPQG---VSSEAEPSAKQV 243
Cdd:PRK09545 167 ELMPQSKAKLDANLKDFEAQLAQ--TDKQIGNQLAPVKGKGYFVFHDAYGYFEKHYG---LTPLGhftVNPEIQPGAQRL 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1080520315 244 ASIIRQIKREGIKAVFTENIKDTRMIDRIAKETGVNVsGRLysDALGGAPA---NSY 297
Cdd:PRK09545 242 HEIRTQLVEQKATCVFAEPQFRPAVIESVAKGTSVRM-GTL--DPLGTNIKlgkDSY 295
|
|
| |
