|
Name |
Accession |
Description |
Interval |
E-value |
| ZnuA |
COG4531 |
ABC-type Zn2+ transport system, periplasmic component/surface adhesin ZnuA [Inorganic ion ... |
17-345 |
2.99e-150 |
|
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: 424.63 E-value: 2.99e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391183334 17 LGSTAFAADRDgVVVSIKPLHSLVSAVMQGVGEPKLIVQGAGSEHVYSLKPSDAEAIEHAKVIFWAGPSMETFLDKPIDT 96
Cdd:COG4531 1 LASAAAAAAPR-VVTSIKPLHSLVAAVMDGVGEPELLLPPGASPHDYALRPSDARALQDADLVFWVGPDLEPFLEKPLET 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391183334 97 LGEGAKVVALGESEGLTRLKFREGGPFEahdhghegegheghdhahghdhddgdkkEAEAGHDHAAEAGEGAHEHHHGHG 176
Cdd:COG4531 80 LAPDAKVVELLELPGLTLLPFREGGDFE----------------------------HHDHHDEHHHHHHHHDDHHDHHHG 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391183334 177 EYDLHFWLDPQNGKVLVTNIAKVLSESDPAHAAQYEQNAKAYAEKLDALTKDIATELQPVKDKPFVVFHDAYQYFENRFD 256
Cdd:COG4531 132 GYDPHLWLSPENAKAWAAAIADALSELDPENAATYQANAAAFEARLDALDAEIAAQLAPVKGKPFFVFHDAYQYFEKRFG 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391183334 257 VKAAGSITVSPEKAPGAARIQQIHDKIKSLKVACVFSEPQFEPKLVNTVIDGTDAKTGVLDPLGAELKDGPDLYPQLIRN 336
Cdd:COG4531 212 LNALGAITLNPEIQPGAKRLAEIREKLKELGAVCVFAEPQFNPALVETVAEGTGVRTGVLDPLGADLEPGPDLYFQLLRQ 291
|
....*....
gi 1391183334 337 LADSLKACL 345
Cdd:COG4531 292 LADSLASCL 300
|
|
| ZnuA |
cd01019 |
Zinc binding protein ZnuA. These proteins have been shown to function as initial receptors in ... |
24-345 |
2.08e-97 |
|
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: 290.04 E-value: 2.08e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391183334 24 ADRDGVVVSIKPLHSLVSAVMQGVGEPKLIVQGAGSEHVYSLKPSDAEAIEHAKVIFWAGPSMETFLDKPIDTLgEGAKV 103
Cdd:cd01019 1 AAEASVLTSIKPLGFIAAAIMGGVGEVEVLVPPGASPHDYELRPSDARKLQEADLVVWIGPDLEAFLDKVLQGR-KKGKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391183334 104 VALgesEGLTRLKFREGGpfeahdhghegegheghdhahghdhddgdkkeAEAGHDHAAEAGEGAHEHHHGHGEYDLHFW 183
Cdd:cd01019 80 LTL---AKLIDLKTLEDG--------------------------------ASHGDHEHDHEHAHGEHDGHEEGGLDPHLW 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391183334 184 LDPQNGKVLVTNIAKVLSESDPAHAAQYEQNAKAYAEKLDALTKDIATELQPVKDKPFVVFHDAYQYFENRFDVKAAGSI 263
Cdd:cd01019 125 LSPENAAEVAQAVAEKLSALDPDNAATYAANLEAFNARLAELDATIKERLAPVKTKPFFVFHDAYGYFEKRYGLTQAGVF 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391183334 264 TVSPEKAPGAARIQQIHDKIKSLKVACVFSEPQFEPKLVNTVIDGTDAKTGVLDPLGAELKDGPDLYPQLIRNLADSLKA 343
Cdd:cd01019 205 TIDPEIDPGAKRLAKIRKEIKEKGATCVFAEPQFHPKIAETLAEGTGAKVGELDPLGGLIELGKNSYVNFLRNLADSLAS 284
|
..
gi 1391183334 344 CL 345
Cdd:cd01019 285 CL 286
|
|
| ZnuA |
pfam01297 |
Zinc-uptake complex component A periplasmic; ZnuA includes periplasmic solute binding proteins ... |
29-344 |
1.20e-80 |
|
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: 246.70 E-value: 1.20e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391183334 29 VVVSIKPLHSLVSAVMQGVGEPKLIVQGAGSEHVYSLKPSDAEAIEHAKVIFWAGPSMETFLDKPIDTLGeGAKVVALge 108
Cdd:pfam01297 1 VVATTYPLADLAKQIGGDRVEVTSLVPPGADPHDYEPTPSDIAALSDADLVVYNGLGLEPWLDKLLEALP-NKKVVDA-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391183334 109 SEGLTRLKFREGGpfeahdhghegegheghdhahghdhddgdkkEAEAGHDHAaeagegahehhhghgeYDLHFWLDPQN 188
Cdd:pfam01297 78 SEGVELLDEEGEE-------------------------------EDHDGHDHG----------------YDPHVWLDPKN 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391183334 189 GKVLVTNIAKVLSESDPAHAAQYEQNAKAYAEKLDALTKDIATELQPVKDK--PFVVFHDAYQYFENRFDVKAAGSITVS 266
Cdd:pfam01297 111 AKKMAENIADALSELDPANAATYEANAAAYLAELDALDAEIKEQLASIPEKtrKLVTSHDAFGYLARAYGLEQVGIQGVS 190
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1391183334 267 PEKAPGAARIQQIHDKIKSLKVACVFSEPQFEPKLVNTVIDGTDAKT-GVLDPLGAELKDGPDLYPQLIRNLADSLKAC 344
Cdd:pfam01297 191 PESEPSAADLAELIDLIKEKKVKAIFVEPQVSPKLAETVAKETGVKVlGPLYTDSLGEPGGGATYLDLMRHNLDTLAEA 269
|
|
| znuA |
PRK09545 |
zinc ABC transporter substrate-binding protein ZnuA; |
3-345 |
9.59e-75 |
|
zinc ABC transporter substrate-binding protein ZnuA;
Pssm-ID: 236558 [Multi-domain] Cd Length: 311 Bit Score: 232.98 E-value: 9.59e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391183334 3 HLRSLLLASAFLAGLGSTAFAADRDgVVVSIKPLHSLVSAVMQGVGEPKLIVQGAGSEHVYSLKPSDAEAIEHAKVIFWA 82
Cdd:PRK09545 2 HKKTLLFAALLAALLGGATQAANAA-VVTSIKPLGFIASAIADGVTETEVLLPDGASPHDYSLRPSDVKRLQSADLVVWV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391183334 83 GPSMETFLDKPIDTLgEGAKVVALGESEGLTRLKFREGgpfeahdhghegegheghdhahghdhddgdkkEAEAGHDHAA 162
Cdd:PRK09545 81 GPEMEAFLEKPVSKL-PENKQVTIAQLPDVKPLLMKGA--------------------------------HDDHHDDDHD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391183334 163 EAGEGAHEHHHGHGEYDLHFWLDPQNGKVLVTNIAKVLSESDPAHAAQYEQNAKAYAEKLDALTKDIATELQPVKDKPFV 242
Cdd:PRK09545 128 HAGHEKSDEDHHHGEYNMHIWLSPEIARATAVAIHDKLVELMPQSKAKLDANLKDFEAQLAQTDKQIGNQLAPVKGKGYF 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391183334 243 VFHDAYQYFENRFDVKAAGSITVSPEKAPGAARIQQIHDKIKSLKVACVFSEPQFEPKLVNTVIDGTDAKTGVLDPLGAE 322
Cdd:PRK09545 208 VFHDAYGYFEKHYGLTPLGHFTVNPEIQPGAQRLHEIRTQLVEQKATCVFAEPQFRPAVIESVAKGTSVRMGTLDPLGTN 287
|
330 340
....*....|....*....|...
gi 1391183334 323 LKDGPDLYPQLIRNLADSLKACL 345
Cdd:PRK09545 288 IKLGKDSYSEFLSQLANQYASCL 310
|
|
| anch_rpt_subst |
TIGR03772 |
anchored repeat ABC transporter, substrate-binding protein; Members of this protein family are ... |
179-346 |
7.85e-21 |
|
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: 93.00 E-value: 7.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391183334 179 DLHFWLDPQNGKVLVTNIAKVLSESDPAHAAQYEQNAKAYAEKLDALTKDIATELQ--PVKDKPFVVFHDAYQYFENRFD 256
Cdd:TIGR03772 310 DPHLWHNVKNAIAYVEVIRDKLIEVDPRGAQAYRSNASAYIHRLERLDTYVRRTIAtiPPSRRHLITTHDAYSYLGQAYG 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391183334 257 VKAAGSITVSPEKAPGAARIQQIHDKIKSLKVACVFSEPQFEPKlvNTVIDGTDAKTG--VLDPLGAELKDGPDLYPQLI 334
Cdd:TIGR03772 390 LNIAGFVTPNPAVEPSLADRRRLTRTIENLKVPAVFLEPNLAAR--STTLNEIADELGvrVCAIYGDTFDDDVTNYVDLM 467
|
170
....*....|..
gi 1391183334 335 RNLADSLKACLS 346
Cdd:TIGR03772 468 RFNADSLADCLG 479
|
|
| Zn_bnd_ABC_AdcA |
NF033605 |
zinc ABC transporter substrate-binding lipoprotein AdcA; |
175-313 |
7.44e-09 |
|
zinc ABC transporter substrate-binding lipoprotein AdcA;
Pssm-ID: 468109 [Multi-domain] Cd Length: 516 Bit Score: 57.09 E-value: 7.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391183334 175 HGEYDLHFWLDPQNGKVLVTNIAKVLSESDPAHAAQYEQNAKayaeKLDALTKDIATELQPV-KDKP-FVVF--HDAYQY 250
Cdd:NF033605 148 HGGYDPHVWLDPKFDQTFAKEIKDELVKKDPKHKDEYEKNYK----KLNKDLKGIDKDMKDItKDKQgNAVFisHESLGY 223
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1391183334 251 FENRFDVKAAGSITVSPEKaPGAARIQQIHDKIKSLKVACVFSEPQFEPKLVNTVIDGTDAKT 313
Cdd:NF033605 224 LADRYGFVQKGVQNMNAED-PSQKELTEIVKEINDSGAKYILYEDNVSNKVTDTIRKETDAKP 285
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ZnuA |
COG4531 |
ABC-type Zn2+ transport system, periplasmic component/surface adhesin ZnuA [Inorganic ion ... |
17-345 |
2.99e-150 |
|
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: 424.63 E-value: 2.99e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391183334 17 LGSTAFAADRDgVVVSIKPLHSLVSAVMQGVGEPKLIVQGAGSEHVYSLKPSDAEAIEHAKVIFWAGPSMETFLDKPIDT 96
Cdd:COG4531 1 LASAAAAAAPR-VVTSIKPLHSLVAAVMDGVGEPELLLPPGASPHDYALRPSDARALQDADLVFWVGPDLEPFLEKPLET 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391183334 97 LGEGAKVVALGESEGLTRLKFREGGPFEahdhghegegheghdhahghdhddgdkkEAEAGHDHAAEAGEGAHEHHHGHG 176
Cdd:COG4531 80 LAPDAKVVELLELPGLTLLPFREGGDFE----------------------------HHDHHDEHHHHHHHHDDHHDHHHG 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391183334 177 EYDLHFWLDPQNGKVLVTNIAKVLSESDPAHAAQYEQNAKAYAEKLDALTKDIATELQPVKDKPFVVFHDAYQYFENRFD 256
Cdd:COG4531 132 GYDPHLWLSPENAKAWAAAIADALSELDPENAATYQANAAAFEARLDALDAEIAAQLAPVKGKPFFVFHDAYQYFEKRFG 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391183334 257 VKAAGSITVSPEKAPGAARIQQIHDKIKSLKVACVFSEPQFEPKLVNTVIDGTDAKTGVLDPLGAELKDGPDLYPQLIRN 336
Cdd:COG4531 212 LNALGAITLNPEIQPGAKRLAEIREKLKELGAVCVFAEPQFNPALVETVAEGTGVRTGVLDPLGADLEPGPDLYFQLLRQ 291
|
....*....
gi 1391183334 337 LADSLKACL 345
Cdd:COG4531 292 LADSLASCL 300
|
|
| ZnuA |
cd01019 |
Zinc binding protein ZnuA. These proteins have been shown to function as initial receptors in ... |
24-345 |
2.08e-97 |
|
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: 290.04 E-value: 2.08e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391183334 24 ADRDGVVVSIKPLHSLVSAVMQGVGEPKLIVQGAGSEHVYSLKPSDAEAIEHAKVIFWAGPSMETFLDKPIDTLgEGAKV 103
Cdd:cd01019 1 AAEASVLTSIKPLGFIAAAIMGGVGEVEVLVPPGASPHDYELRPSDARKLQEADLVVWIGPDLEAFLDKVLQGR-KKGKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391183334 104 VALgesEGLTRLKFREGGpfeahdhghegegheghdhahghdhddgdkkeAEAGHDHAAEAGEGAHEHHHGHGEYDLHFW 183
Cdd:cd01019 80 LTL---AKLIDLKTLEDG--------------------------------ASHGDHEHDHEHAHGEHDGHEEGGLDPHLW 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391183334 184 LDPQNGKVLVTNIAKVLSESDPAHAAQYEQNAKAYAEKLDALTKDIATELQPVKDKPFVVFHDAYQYFENRFDVKAAGSI 263
Cdd:cd01019 125 LSPENAAEVAQAVAEKLSALDPDNAATYAANLEAFNARLAELDATIKERLAPVKTKPFFVFHDAYGYFEKRYGLTQAGVF 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391183334 264 TVSPEKAPGAARIQQIHDKIKSLKVACVFSEPQFEPKLVNTVIDGTDAKTGVLDPLGAELKDGPDLYPQLIRNLADSLKA 343
Cdd:cd01019 205 TIDPEIDPGAKRLAKIRKEIKEKGATCVFAEPQFHPKIAETLAEGTGAKVGELDPLGGLIELGKNSYVNFLRNLADSLAS 284
|
..
gi 1391183334 344 CL 345
Cdd:cd01019 285 CL 286
|
|
| ZnuA |
pfam01297 |
Zinc-uptake complex component A periplasmic; ZnuA includes periplasmic solute binding proteins ... |
29-344 |
1.20e-80 |
|
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: 246.70 E-value: 1.20e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391183334 29 VVVSIKPLHSLVSAVMQGVGEPKLIVQGAGSEHVYSLKPSDAEAIEHAKVIFWAGPSMETFLDKPIDTLGeGAKVVALge 108
Cdd:pfam01297 1 VVATTYPLADLAKQIGGDRVEVTSLVPPGADPHDYEPTPSDIAALSDADLVVYNGLGLEPWLDKLLEALP-NKKVVDA-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391183334 109 SEGLTRLKFREGGpfeahdhghegegheghdhahghdhddgdkkEAEAGHDHAaeagegahehhhghgeYDLHFWLDPQN 188
Cdd:pfam01297 78 SEGVELLDEEGEE-------------------------------EDHDGHDHG----------------YDPHVWLDPKN 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391183334 189 GKVLVTNIAKVLSESDPAHAAQYEQNAKAYAEKLDALTKDIATELQPVKDK--PFVVFHDAYQYFENRFDVKAAGSITVS 266
Cdd:pfam01297 111 AKKMAENIADALSELDPANAATYEANAAAYLAELDALDAEIKEQLASIPEKtrKLVTSHDAFGYLARAYGLEQVGIQGVS 190
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1391183334 267 PEKAPGAARIQQIHDKIKSLKVACVFSEPQFEPKLVNTVIDGTDAKT-GVLDPLGAELKDGPDLYPQLIRNLADSLKAC 344
Cdd:pfam01297 191 PESEPSAADLAELIDLIKEKKVKAIFVEPQVSPKLAETVAKETGVKVlGPLYTDSLGEPGGGATYLDLMRHNLDTLAEA 269
|
|
| znuA |
PRK09545 |
zinc ABC transporter substrate-binding protein ZnuA; |
3-345 |
9.59e-75 |
|
zinc ABC transporter substrate-binding protein ZnuA;
Pssm-ID: 236558 [Multi-domain] Cd Length: 311 Bit Score: 232.98 E-value: 9.59e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391183334 3 HLRSLLLASAFLAGLGSTAFAADRDgVVVSIKPLHSLVSAVMQGVGEPKLIVQGAGSEHVYSLKPSDAEAIEHAKVIFWA 82
Cdd:PRK09545 2 HKKTLLFAALLAALLGGATQAANAA-VVTSIKPLGFIASAIADGVTETEVLLPDGASPHDYSLRPSDVKRLQSADLVVWV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391183334 83 GPSMETFLDKPIDTLgEGAKVVALGESEGLTRLKFREGgpfeahdhghegegheghdhahghdhddgdkkEAEAGHDHAA 162
Cdd:PRK09545 81 GPEMEAFLEKPVSKL-PENKQVTIAQLPDVKPLLMKGA--------------------------------HDDHHDDDHD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391183334 163 EAGEGAHEHHHGHGEYDLHFWLDPQNGKVLVTNIAKVLSESDPAHAAQYEQNAKAYAEKLDALTKDIATELQPVKDKPFV 242
Cdd:PRK09545 128 HAGHEKSDEDHHHGEYNMHIWLSPEIARATAVAIHDKLVELMPQSKAKLDANLKDFEAQLAQTDKQIGNQLAPVKGKGYF 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391183334 243 VFHDAYQYFENRFDVKAAGSITVSPEKAPGAARIQQIHDKIKSLKVACVFSEPQFEPKLVNTVIDGTDAKTGVLDPLGAE 322
Cdd:PRK09545 208 VFHDAYGYFEKHYGLTPLGHFTVNPEIQPGAQRLHEIRTQLVEQKATCVFAEPQFRPAVIESVAKGTSVRMGTLDPLGTN 287
|
330 340
....*....|....*....|...
gi 1391183334 323 LKDGPDLYPQLIRNLADSLKACL 345
Cdd:PRK09545 288 IKLGKDSYSEFLSQLANQYASCL 310
|
|
| ZnuA |
COG0803 |
ABC-type Zn uptake system ZnuABC, Zn-binding component ZnuA [Inorganic ion transport and ... |
1-335 |
1.08e-67 |
|
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: 214.34 E-value: 1.08e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391183334 1 MKH--LRSLLLASAFLAGLGSTA-FAADRDGVVVSIKPLHSLVSAVMQGVGEPKLIVQGAGSEHVYSLKPSDAEAIEHAK 77
Cdd:COG0803 1 MKRllLALLLLAALLLAGCSAAAsSAAGKLKVVATFSPLADLAKQIGGDKVEVTSLVPPGADPHDYEPTPSDIAKLAKAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391183334 78 VIFWAGPSMETFLDKPIDTLG-EGAKVVALgeSEGLTRLKFREGgpfeahdhghegegheghdhahghdhddgdkkeaea 156
Cdd:COG0803 81 LVVYNGLGLEGWLDKLLEAAGnPGVPVVDA--SEGIDLLELEEG------------------------------------ 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391183334 157 ghdhaaeagegahehhHGHGEYDLHFWLDPQNGKVLVTNIAKVLSESDPAHAAQYEQNAKAYAEKLDALTKDIATELQPV 236
Cdd:COG0803 123 ----------------HDHGEPDPHVWLDPKNAKKVAENIADALAELDPANAAYYEANAAAYLAELDALDAEIKAKLAAI 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391183334 237 KDKPFVVFHDAYQYFENRFDVKAAGSITVSPEKAPGAARIQQIHDKIKSLKVACVFSEPQFEPKLVNTVIDGTDAKTGVL 316
Cdd:COG0803 187 PGRKLVTSHDAFGYLARAYGLEVVAIQGISPGSEPSPADLAELIDLIKEEGVKAIFVESQVSPKLAETLAEETGVKVLYL 266
|
330
....*....|....*....
gi 1391183334 317 DPLGAELKDGPDlYPQLIR 335
Cdd:COG0803 267 DSLGGPGGPGDT-YLDMMR 284
|
|
| AdcA |
cd01017 |
Metal binding protein AdcA. These proteins have been shown to function in the ABC uptake of ... |
29-342 |
1.86e-45 |
|
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: 156.68 E-value: 1.86e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391183334 29 VVVSIKPLHSLVSAVMQGVGEPKLIVqGAGSE-HVYSLKPSDAEAIEHAKVIFWAGPSMETFLDKPIDTLgEGAKVVALG 107
Cdd:cd01017 6 VVTTFYPLYEFTKAIGGDKADVKLII-PAGTEpHDFEPSPKDIARIADADVFVYNGLGMETWAEKVLKSL-QNKKLKVVE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391183334 108 ESEGLTRLKfrEGGPFEahdhghegegheghDHAHghdhddgdkKEAEAGHDhaaeagegahehhhghgeYDLHFWLDPQ 187
Cdd:cd01017 84 ASKGIKLLK--AGGAEH--------------DHDH---------SHSHHHGD------------------YDPHVWLSPV 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391183334 188 NGKVLVTNIAKVLSESDPAHAAQYEQNAKAYAEKLDALTKDIATELQPVKDKPFVVFHDAYQYFENRFDVKAAGSITVSP 267
Cdd:cd01017 121 LAIQQVENIKDALIKLDPDNKEYYEKNAAAYAKKLEALDQEYRAKLAKAKGKTFVTQHAAFGYLARRYGLKQIAIVGVSP 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391183334 268 EKAPGAARIQQIHDKIKSLKVACVFSEPQFEPKLVNTVIDGTDAKTGVLDPLGA---ELKDGPDLYPQLIR----NLADS 340
Cdd:cd01017 201 EVEPSPKQLAELVEFVKKSDVKYIFFEENASSKIAETLAKETGAKLLVLNPLETltkEEIDDGKDYFSLMKenleTLKRA 280
|
..
gi 1391183334 341 LK 342
Cdd:cd01017 281 LK 282
|
|
| PsaA |
cd01137 |
Metal binding protein PsaA. These proteins have been shown to function as initial receptors ... |
11-346 |
1.18e-41 |
|
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: 146.65 E-value: 1.18e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391183334 11 SAFLAGLGSTAFAADRDGVVVSIkplhSLVSAVMQGVGEPKL----IVQGAGSEHVYSLKPSDAEAIEHAKVIFWAGPSM 86
Cdd:cd01137 2 AACASLGSSPATAASKLKVVATF----SILADIARNIAGDRVnvtsIVPPGADPHEYEPTPSDIKKLSKADLILYNGLNL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391183334 87 ETFLDKPIDTLGEGAKVVALgeSEGLTRLKFREGGpfeahdhghegegheghdhahghdhddgdkkeaEAGHdhaaeage 166
Cdd:cd01137 78 EPWLERLVKNAGKDVPVVAV--SEGIDPIPLEEGH---------------------------------YKGK-------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391183334 167 gahehhhghgeYDLHFWLDPQNGKVLVTNIAKVLSESDPAHAAQYEQNAKAYAEKLDALTKDIATELQPV-KDKPFVVF- 244
Cdd:cd01137 115 -----------PDPHAWMSPKNAIIYVKNIAKALSEADPANAETYQKNAAAYKAKLKALDEWAKAKFATIpAEKRKLVTs 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391183334 245 HDAYQYFENRFDVKAAGSITVSPEKAPGAARIQQIHDKIKSLKVACVFSEPQFEPKLVNTVIDGTDAKT-GVL--DPLGA 321
Cdd:cd01137 184 EGAFSYFAKAYGLKEAYLWPINTEEEGTPKQVATLIEQVKKEKVPAVFVESTVNDRLMKQVAKETGAKIgGQLytDSLSE 263
|
330 340
....*....|....*....|....*
gi 1391183334 322 ELKDGPDlYPQLIRNLADSLKACLS 346
Cdd:cd01137 264 KGGPADT-YLDMMEHNLDTIVEGLG 287
|
|
| ZntC |
cd01018 |
Metal binding protein ZntC. These proteins are predicted to function as initial receptors in ... |
29-321 |
1.39e-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: 127.48 E-value: 1.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391183334 29 VVVSIKPLHSLVSAVMQGVGEPKLIVQGAGSEHVYSLKPSDAEAIEHAKVIFWAGPSME-TFLDKpIDTLGEGAKVVALg 107
Cdd:cd01018 5 VAVSIEPQKYFVEKIAGDTVDVVVLVPPGSNPHTYEPKPQQMKKLSEADLYFRIGLGFEeVWLER-FRSNNPKMQVVNM- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391183334 108 eSEGLTRLKFREggpfeahdhghegegheghdhahghdhddgdKKEAEAGHDhaaeagegaheHHHGHGEYDLHFWLDPQ 187
Cdd:cd01018 83 -SKGITLIPMAD-------------------------------HHHHHHGEH-----------EHHHHGNYDPHIWLSPA 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391183334 188 NGKVLVTNIAKVLSESDPAHAAQYEQNAKAYAEKLDALTKDIATELQPVKDKPFVVFHDAYQYFENRFDVKaagSITVSP 267
Cdd:cd01018 120 NAKIMAENIYEALAELDPQNATYYQANLDALLAELDALDSEIRTILSKLKQRAFMVYHPAWGYFARDYGLT---QIPIEE 196
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1391183334 268 E-KAPGAARIQQIHDKIKSLKVACVFSEPQFEPKLVNTVIDGTDAKTGVLDPLGA 321
Cdd:cd01018 197 EgKEPSPADLKRLIDLAKEKGVRVVFVQPQFSTKSAEAIAREIGAKVVTIDPLAA 251
|
|
| TroA |
cd01016 |
Metal binding protein TroA. These proteins have been shown to function as initial receptors in ... |
29-323 |
2.87e-23 |
|
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: 97.43 E-value: 2.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391183334 29 VVVSIKPLHSLVSAVMQGVGEPKLIVQGAGSEHVYSLKPSDAEAIEHAKVIFWAGPSMETFLDKPIDTLGEGAKVVALGE 108
Cdd:cd01016 4 VVTTTGMIADAVENIGGDHVEVTGLMGPGVDPHLYKATAGDVEKLQNADVVFYNGLHLEGKMSDVLSKLGSSKSVIALED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391183334 109 SegLTRLKFREggpfeahdhghegegheghdhahghdhddgdkkEAEAGHdhaaeagegahehhhghgeYDLHFWLDPQN 188
Cdd:cd01016 84 T--LDRSQLIL---------------------------------DEEEGT-------------------YDPHIWFDVKL 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391183334 189 GKVLVTNIAKVLSESDPAHAAQYEQNAKAYAEKLDALTKDIATELQ--PVKDKPFVVFHDAYQYFENRFDVKAAGSITVS 266
Cdd:cd01016 110 WKYAVKAVAEVLSEKLPEHKDEFQANSEAYVEELDSLDAYAKKKIAeiPEQQRVLVTAHDAFGYFGRAYGFEVKGLQGIS 189
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1391183334 267 PEKAPGAARIQQIHDKIKSLKVACVFSEPQFEPKLVNTVIDGTDAKTGVLDpLGAEL 323
Cdd:cd01016 190 TDSEAGLRDINELVDLIVERKIKAIFVESSVNQKSIEALQDAVKARGHDVQ-IGGEL 245
|
|
| anch_rpt_subst |
TIGR03772 |
anchored repeat ABC transporter, substrate-binding protein; Members of this protein family are ... |
179-346 |
7.85e-21 |
|
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: 93.00 E-value: 7.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391183334 179 DLHFWLDPQNGKVLVTNIAKVLSESDPAHAAQYEQNAKAYAEKLDALTKDIATELQ--PVKDKPFVVFHDAYQYFENRFD 256
Cdd:TIGR03772 310 DPHLWHNVKNAIAYVEVIRDKLIEVDPRGAQAYRSNASAYIHRLERLDTYVRRTIAtiPPSRRHLITTHDAYSYLGQAYG 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391183334 257 VKAAGSITVSPEKAPGAARIQQIHDKIKSLKVACVFSEPQFEPKlvNTVIDGTDAKTG--VLDPLGAELKDGPDLYPQLI 334
Cdd:TIGR03772 390 LNIAGFVTPNPAVEPSLADRRRLTRTIENLKVPAVFLEPNLAAR--STTLNEIADELGvrVCAIYGDTFDDDVTNYVDLM 467
|
170
....*....|..
gi 1391183334 335 RNLADSLKACLS 346
Cdd:TIGR03772 468 RFNADSLADCLG 479
|
|
| TroA_c |
cd01145 |
Periplasmic binding protein TroA_c. These proteins are predicted to function as initial ... |
179-275 |
2.00e-10 |
|
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: 59.44 E-value: 2.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391183334 179 DLHFWLDPQNGKVLVTNIAKVLSESDPAHAAQYEQNAKAYAEKLDALTKDIATELQPVKDKPFVVFHDAYQYFENRFDVK 258
Cdd:cd01145 107 NPHVWLDPNNAPALAKALADALIELDPSEQEEYKENLRVFLAKLNKLLREWERQFEGLKGIQVVAYHPSYQYLADWLGIE 186
|
90
....*....|....*..
gi 1391183334 259 AAGSITVSPEKAPGAAR 275
Cdd:cd01145 187 VVASLEPLPELPPTSSH 203
|
|
| Zn_bnd_ABC_AdcA |
NF033605 |
zinc ABC transporter substrate-binding lipoprotein AdcA; |
175-313 |
7.44e-09 |
|
zinc ABC transporter substrate-binding lipoprotein AdcA;
Pssm-ID: 468109 [Multi-domain] Cd Length: 516 Bit Score: 57.09 E-value: 7.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391183334 175 HGEYDLHFWLDPQNGKVLVTNIAKVLSESDPAHAAQYEQNAKayaeKLDALTKDIATELQPV-KDKP-FVVF--HDAYQY 250
Cdd:NF033605 148 HGGYDPHVWLDPKFDQTFAKEIKDELVKKDPKHKDEYEKNYK----KLNKDLKGIDKDMKDItKDKQgNAVFisHESLGY 223
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1391183334 251 FENRFDVKAAGSITVSPEKaPGAARIQQIHDKIKSLKVACVFSEPQFEPKLVNTVIDGTDAKT 313
Cdd:NF033605 224 LADRYGFVQKGVQNMNAED-PSQKELTEIVKEINDSGAKYILYEDNVSNKVTDTIRKETDAKP 285
|
|
| TroA_b |
cd01020 |
Metal binding protein TroA_b. These proteins are predicted to function as initial receptors ... |
181-307 |
2.09e-06 |
|
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: 48.59 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391183334 181 HFWLDPQNGKVLVTNIAKVLSESDPAHAAQYEQNAKAYAEKLDALTKDIA-----TELQPVKDKPFVVFH--DAYQYFEN 253
Cdd:cd01020 96 HLWYDPETMSKVANALADALVKADPDNKKYYQANAKKFVASLKPLAAKIAelsakYKGAPVAATEPVFDYllDALGMKER 175
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1391183334 254 rfDVKAAGSITVSpEKAPGAARIQQIHDKIKSLKVACVFSEPQFEPKLVNTVID 307
Cdd:cd01020 176 --TPKGYTATTES-ETEPSPADIAAFQNAIKNRQIDALIVNPQQASSATTNITG 226
|
|
| |
