|
Name |
Accession |
Description |
Interval |
E-value |
| ZnuA |
COG4531 |
ABC-type Zn2+ transport system, periplasmic component/surface adhesin ZnuA [Inorganic ion ... |
12-291 |
2.80e-137 |
|
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: 389.57 E-value: 2.80e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330282354 12 LLAPSVASANTILTSFKPIQMIVTELTQGVSEPDVLMNSNASPHDYALKPSDVKKVHSADMVIWFGPDLEAFLTKVI--- 88
Cdd:COG4531 1 LASAAAAAAPRVVTSIKPLHSLVAAVMDGVGEPELLLPPGASPHDYALRPSDARALQDADLVFWVGPDLEPFLEKPLetl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330282354 89 GSKENVIKISEIPGINLREF-----------------GHDDHDAHEGHNHGSHDPHFWLGIDQVEVAAKYISAKLIESDP 151
Cdd:COG4531 81 APDAKVVELLELPGLTLLPFreggdfehhdhhdehhhHHHHHDDHHDHHHGGYDPHLWLSPENAKAWAAAIADALSELDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330282354 152 DNAMAYQENLDSFLIALKEKQQSIHEQLAPVKDKGYYVFHDAYGYFEQEFELNNLGHFTVSPERKPGAKSLIAIKKTLVR 231
Cdd:COG4531 161 ENAATYQANAAAFEARLDALDAEIAAQLAPVKGKPFFVFHDAYQYFEKRFGLNALGAITLNPEIQPGAKRLAEIREKLKE 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330282354 232 DNVQCVFAEPQFTPAVIESVTRGSNAKQGQLDPIGSTVEVKSGSYFDFLQQLTDSYTSCL 291
Cdd:COG4531 241 LGAVCVFAEPQFNPALVETVAEGTGVRTGVLDPLGADLEPGPDLYFQLLRQLADSLASCL 300
|
|
| znuA |
PRK09545 |
zinc ABC transporter substrate-binding protein ZnuA; |
4-291 |
7.10e-116 |
|
zinc ABC transporter substrate-binding protein ZnuA;
Pssm-ID: 236558 [Multi-domain] Cd Length: 311 Bit Score: 335.82 E-value: 7.10e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330282354 4 SSFILATLLLAPSVASANtILTSFKPIQMIVTELTQGVSEPDVLMNSNASPHDYALKPSDVKKVHSADMVIWFGPDLEAF 83
Cdd:PRK09545 9 AALLAALLGGATQAANAA-VVTSIKPLGFIASAIADGVTETEVLLPDGASPHDYSLRPSDVKRLQSADLVVWVGPEMEAF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330282354 84 LTKVIGS--KENVIKISEIPGIN---LREFGHDDHD----------AHEGHNHGSHDPHFWLGIDQVEVAAKYISAKLIE 148
Cdd:PRK09545 88 LEKPVSKlpENKQVTIAQLPDVKpllMKGAHDDHHDddhdhaghekSDEDHHHGEYNMHIWLSPEIARATAVAIHDKLVE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330282354 149 SDPDNAMAYQENLDSFLIALKEKQQSIHEQLAPVKDKGYYVFHDAYGYFEQEFELNNLGHFTVSPERKPGAKSLIAIKKT 228
Cdd:PRK09545 168 LMPQSKAKLDANLKDFEAQLAQTDKQIGNQLAPVKGKGYFVFHDAYGYFEKHYGLTPLGHFTVNPEIQPGAQRLHEIRTQ 247
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1330282354 229 LVRDNVQCVFAEPQFTPAVIESVTRGSNAKQGQLDPIGSTVEVKSGSYFDFLQQLTDSYTSCL 291
Cdd:PRK09545 248 LVEQKATCVFAEPQFRPAVIESVAKGTSVRMGTLDPLGTNIKLGKDSYSEFLSQLANQYASCL 310
|
|
| ZnuA |
cd01019 |
Zinc binding protein ZnuA. These proteins have been shown to function as initial receptors in ... |
18-291 |
1.14e-110 |
|
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: 321.63 E-value: 1.14e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330282354 18 ASANTILTSFKPIQMIVTELTQGVSEPDVLMNSNASPHDYALKPSDVKKVHSADMVIWFGPDLEAFLTKVI--GSKENVI 95
Cdd:cd01019 1 AAEASVLTSIKPLGFIAAAIMGGVGEVEVLVPPGASPHDYELRPSDARKLQEADLVVWIGPDLEAFLDKVLqgRKKGKVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330282354 96 KISEIPGINLREFGHDDHDA----------HEGHNHGSHDPHFWLGIDQVEVAAKYISAKLIESDPDNAMAYQENLDSFL 165
Cdd:cd01019 81 TLAKLIDLKTLEDGASHGDHehdhehahgeHDGHEEGGLDPHLWLSPENAAEVAQAVAEKLSALDPDNAATYAANLEAFN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330282354 166 IALKEKQQSIHEQLAPVKDKGYYVFHDAYGYFEQEFELNNLGHFTVSPERKPGAKSLIAIKKTLVRDNVQCVFAEPQFTP 245
Cdd:cd01019 161 ARLAELDATIKERLAPVKTKPFFVFHDAYGYFEKRYGLTQAGVFTIDPEIDPGAKRLAKIRKEIKEKGATCVFAEPQFHP 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1330282354 246 AVIESVTRGSNAKQGQLDPIGSTVEVKSGSYFDFLQQLTDSYTSCL 291
Cdd:cd01019 241 KIAETLAEGTGAKVGELDPLGGLIELGKNSYVNFLRNLADSLASCL 286
|
|
| ZnuA |
pfam01297 |
Zinc-uptake complex component A periplasmic; ZnuA includes periplasmic solute binding proteins ... |
23-290 |
5.88e-76 |
|
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: 232.83 E-value: 5.88e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330282354 23 ILTSFKPIQMIVTELTQGVSEPDVLMNSNASPHDYALKPSDVKKVHSADMVIWFGPDLEAFLTKVIGS--KENVIKISEi 100
Cdd:pfam01297 1 VVATTYPLADLAKQIGGDRVEVTSLVPPGADPHDYEPTPSDIAALSDADLVVYNGLGLEPWLDKLLEAlpNKKVVDASE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330282354 101 pGINLREFGHDDHDaHEGHNHGsHDPHFWLGIDQVEVAAKYISAKLIESDPDNAMAYQENLDSFLIALKEKQQSIHEQLA 180
Cdd:pfam01297 80 -GVELLDEEGEEED-HDGHDHG-YDPHVWLDPKNAKKMAENIADALSELDPANAATYEANAAAYLAELDALDAEIKEQLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330282354 181 PVKDKG--YYVFHDAYGYFEQEFELNNLGHFTVSPERKPGAKSLIAIKKTLVRDNVQCVFAEPQFTPAVIESVTRGSNAK 258
Cdd:pfam01297 157 SIPEKTrkLVTSHDAFGYLARAYGLEQVGIQGVSPESEPSAADLAELIDLIKEKKVKAIFVEPQVSPKLAETVAKETGVK 236
|
250 260 270
....*....|....*....|....*....|...
gi 1330282354 259 -QGQLDPIGSTVEVKSGSYFDFLQQLTDSYTSC 290
Cdd:pfam01297 237 vLGPLYTDSLGEPGGGATYLDLMRHNLDTLAEA 269
|
|
| AztC |
NF040870 |
zinc ABC transporter substrate-binding protein AztC; |
23-291 |
1.24e-40 |
|
zinc ABC transporter substrate-binding protein AztC;
Pssm-ID: 468807 [Multi-domain] Cd Length: 277 Bit Score: 142.41 E-value: 1.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330282354 23 ILTSFKPIQMIVTELTQGVSEPDVLMNSNASPHDYALKPSDVKKVHSADMVIWFGPDL-EAFLTKVIGSKENVIKISEI- 100
Cdd:NF040870 1 VVVTTNILGDLARNVVGDRAEVTTLMKPDADPHSFEPSAADAAALERADLVVVNGLGLeEGFLRHLIAASATGAPVVEVg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330282354 101 PGINLREFGHDDHDAHEGHnHGSHDPHFWLGIDQVEVAAKYISAKLIESDPDNAMAYQENLDSFLIALKEKQQSIHEQLA 180
Cdd:NF040870 81 DGVDPLPYPEGGHYHFEAG-AGPPDPHFWTDPARARDAVDNIADAFCEADDGDCAAYRANAAAYRAELDELDAEMREAFA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330282354 181 --PVKDKGYYVFHDAYGYFEQEFELNNLGHFTV--SPERKPGAKSLIAIKKTLVRDNVQCVFAEPQFTPAVIESVTRGSN 256
Cdd:NF040870 160 aiPADRRTLVTNHHVFGYLAERYGFRVLGAVIPsgSTLASPSAADLASLARAIREAGVPAIFAESSQPPRLAEVLASEAG 239
|
250 260 270
....*....|....*....|....*....|....*...
gi 1330282354 257 AKQGQLDPIGSTVEVKSG---SYFDFLQQLTDSYTSCL 291
Cdd:NF040870 240 LDVGVVELYSESLSEPDGgaaTYLDMMRANAEAIVDGL 277
|
|
| anch_rpt_subst |
TIGR03772 |
anchored repeat ABC transporter, substrate-binding protein; Members of this protein family are ... |
97-292 |
4.23e-20 |
|
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: 89.92 E-value: 4.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330282354 97 ISEIPG-INLREFGHDDHDAHE-------GHNHGSHDPHFWLGIDQVEVAAKYISAKLIESDPDNAMAYQENLDSFLIAL 168
Cdd:TIGR03772 274 LQEIPGdPRFRFLGRPGSEVYQlpqavlgKHVHGEIDPHLWHNVKNAIAYVEVIRDKLIEVDPRGAQAYRSNASAYIHRL 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330282354 169 KEKQQSIHEQLA--PVKDKGYYVFHDAYGYFEQEFELNNLGHFTVSPERKPGAKSLIAIKKTLVRDNVQCVFAEPQFtpA 246
Cdd:TIGR03772 354 ERLDTYVRRTIAtiPPSRRHLITTHDAYSYLGQAYGLNIAGFVTPNPAVEPSLADRRRLTRTIENLKVPAVFLEPNL--A 431
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1330282354 247 VIESVTRGSNAKQG-QLDPI-GSTVEVKSGSYFDFLQQLTDSYTSCLS 292
Cdd:TIGR03772 432 ARSTTLNEIADELGvRVCAIyGDTFDDDVTNYVDLMRFNADSLADCLG 479
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ZnuA |
COG4531 |
ABC-type Zn2+ transport system, periplasmic component/surface adhesin ZnuA [Inorganic ion ... |
12-291 |
2.80e-137 |
|
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: 389.57 E-value: 2.80e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330282354 12 LLAPSVASANTILTSFKPIQMIVTELTQGVSEPDVLMNSNASPHDYALKPSDVKKVHSADMVIWFGPDLEAFLTKVI--- 88
Cdd:COG4531 1 LASAAAAAAPRVVTSIKPLHSLVAAVMDGVGEPELLLPPGASPHDYALRPSDARALQDADLVFWVGPDLEPFLEKPLetl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330282354 89 GSKENVIKISEIPGINLREF-----------------GHDDHDAHEGHNHGSHDPHFWLGIDQVEVAAKYISAKLIESDP 151
Cdd:COG4531 81 APDAKVVELLELPGLTLLPFreggdfehhdhhdehhhHHHHHDDHHDHHHGGYDPHLWLSPENAKAWAAAIADALSELDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330282354 152 DNAMAYQENLDSFLIALKEKQQSIHEQLAPVKDKGYYVFHDAYGYFEQEFELNNLGHFTVSPERKPGAKSLIAIKKTLVR 231
Cdd:COG4531 161 ENAATYQANAAAFEARLDALDAEIAAQLAPVKGKPFFVFHDAYQYFEKRFGLNALGAITLNPEIQPGAKRLAEIREKLKE 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330282354 232 DNVQCVFAEPQFTPAVIESVTRGSNAKQGQLDPIGSTVEVKSGSYFDFLQQLTDSYTSCL 291
Cdd:COG4531 241 LGAVCVFAEPQFNPALVETVAEGTGVRTGVLDPLGADLEPGPDLYFQLLRQLADSLASCL 300
|
|
| znuA |
PRK09545 |
zinc ABC transporter substrate-binding protein ZnuA; |
4-291 |
7.10e-116 |
|
zinc ABC transporter substrate-binding protein ZnuA;
Pssm-ID: 236558 [Multi-domain] Cd Length: 311 Bit Score: 335.82 E-value: 7.10e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330282354 4 SSFILATLLLAPSVASANtILTSFKPIQMIVTELTQGVSEPDVLMNSNASPHDYALKPSDVKKVHSADMVIWFGPDLEAF 83
Cdd:PRK09545 9 AALLAALLGGATQAANAA-VVTSIKPLGFIASAIADGVTETEVLLPDGASPHDYSLRPSDVKRLQSADLVVWVGPEMEAF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330282354 84 LTKVIGS--KENVIKISEIPGIN---LREFGHDDHD----------AHEGHNHGSHDPHFWLGIDQVEVAAKYISAKLIE 148
Cdd:PRK09545 88 LEKPVSKlpENKQVTIAQLPDVKpllMKGAHDDHHDddhdhaghekSDEDHHHGEYNMHIWLSPEIARATAVAIHDKLVE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330282354 149 SDPDNAMAYQENLDSFLIALKEKQQSIHEQLAPVKDKGYYVFHDAYGYFEQEFELNNLGHFTVSPERKPGAKSLIAIKKT 228
Cdd:PRK09545 168 LMPQSKAKLDANLKDFEAQLAQTDKQIGNQLAPVKGKGYFVFHDAYGYFEKHYGLTPLGHFTVNPEIQPGAQRLHEIRTQ 247
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1330282354 229 LVRDNVQCVFAEPQFTPAVIESVTRGSNAKQGQLDPIGSTVEVKSGSYFDFLQQLTDSYTSCL 291
Cdd:PRK09545 248 LVEQKATCVFAEPQFRPAVIESVAKGTSVRMGTLDPLGTNIKLGKDSYSEFLSQLANQYASCL 310
|
|
| ZnuA |
cd01019 |
Zinc binding protein ZnuA. These proteins have been shown to function as initial receptors in ... |
18-291 |
1.14e-110 |
|
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: 321.63 E-value: 1.14e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330282354 18 ASANTILTSFKPIQMIVTELTQGVSEPDVLMNSNASPHDYALKPSDVKKVHSADMVIWFGPDLEAFLTKVI--GSKENVI 95
Cdd:cd01019 1 AAEASVLTSIKPLGFIAAAIMGGVGEVEVLVPPGASPHDYELRPSDARKLQEADLVVWIGPDLEAFLDKVLqgRKKGKVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330282354 96 KISEIPGINLREFGHDDHDA----------HEGHNHGSHDPHFWLGIDQVEVAAKYISAKLIESDPDNAMAYQENLDSFL 165
Cdd:cd01019 81 TLAKLIDLKTLEDGASHGDHehdhehahgeHDGHEEGGLDPHLWLSPENAAEVAQAVAEKLSALDPDNAATYAANLEAFN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330282354 166 IALKEKQQSIHEQLAPVKDKGYYVFHDAYGYFEQEFELNNLGHFTVSPERKPGAKSLIAIKKTLVRDNVQCVFAEPQFTP 245
Cdd:cd01019 161 ARLAELDATIKERLAPVKTKPFFVFHDAYGYFEKRYGLTQAGVFTIDPEIDPGAKRLAKIRKEIKEKGATCVFAEPQFHP 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1330282354 246 AVIESVTRGSNAKQGQLDPIGSTVEVKSGSYFDFLQQLTDSYTSCL 291
Cdd:cd01019 241 KIAETLAEGTGAKVGELDPLGGLIELGKNSYVNFLRNLADSLASCL 286
|
|
| ZnuA |
pfam01297 |
Zinc-uptake complex component A periplasmic; ZnuA includes periplasmic solute binding proteins ... |
23-290 |
5.88e-76 |
|
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: 232.83 E-value: 5.88e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330282354 23 ILTSFKPIQMIVTELTQGVSEPDVLMNSNASPHDYALKPSDVKKVHSADMVIWFGPDLEAFLTKVIGS--KENVIKISEi 100
Cdd:pfam01297 1 VVATTYPLADLAKQIGGDRVEVTSLVPPGADPHDYEPTPSDIAALSDADLVVYNGLGLEPWLDKLLEAlpNKKVVDASE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330282354 101 pGINLREFGHDDHDaHEGHNHGsHDPHFWLGIDQVEVAAKYISAKLIESDPDNAMAYQENLDSFLIALKEKQQSIHEQLA 180
Cdd:pfam01297 80 -GVELLDEEGEEED-HDGHDHG-YDPHVWLDPKNAKKMAENIADALSELDPANAATYEANAAAYLAELDALDAEIKEQLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330282354 181 PVKDKG--YYVFHDAYGYFEQEFELNNLGHFTVSPERKPGAKSLIAIKKTLVRDNVQCVFAEPQFTPAVIESVTRGSNAK 258
Cdd:pfam01297 157 SIPEKTrkLVTSHDAFGYLARAYGLEQVGIQGVSPESEPSAADLAELIDLIKEKKVKAIFVEPQVSPKLAETVAKETGVK 236
|
250 260 270
....*....|....*....|....*....|...
gi 1330282354 259 -QGQLDPIGSTVEVKSGSYFDFLQQLTDSYTSC 290
Cdd:pfam01297 237 vLGPLYTDSLGEPGGGATYLDLMRHNLDTLAEA 269
|
|
| ZnuA |
COG0803 |
ABC-type Zn uptake system ZnuABC, Zn-binding component ZnuA [Inorganic ion transport and ... |
1-282 |
1.02e-60 |
|
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: 194.31 E-value: 1.02e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330282354 1 MSRSSFILATLLLAPSVASAN---------TILTSFKPIQMIVTELTQGVSEPDVLMNSNASPHDYALKPSDVKKVHSAD 71
Cdd:COG0803 1 MKRLLLALLLLAALLLAGCSAaassaagklKVVATFSPLADLAKQIGGDKVEVTSLVPPGADPHDYEPTPSDIAKLAKAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330282354 72 MVIWFGPDLEAFLTKVIGSKEN----VIKISEipGINLREFghddhdaHEGHNHGSHDPHFWLGIDQVEVAAKYISAKLI 147
Cdd:COG0803 81 LVVYNGLGLEGWLDKLLEAAGNpgvpVVDASE--GIDLLEL-------EEGHDHGEPDPHVWLDPKNAKKVAENIADALA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330282354 148 ESDPDNAMAYQENLDSFLIALKEKQQSIHEQLAPVKDKGYYVFHDAYGYFEQEFELNNLGHFTVSPERKPGAKSLIAIKK 227
Cdd:COG0803 152 ELDPANAAYYEANAAAYLAELDALDAEIKAKLAAIPGRKLVTSHDAFGYLARAYGLEVVAIQGISPGSEPSPADLAELID 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1330282354 228 TLVRDNVQCVFAEPQFTPAVIESVTRGSNAKQGQLDPIGSTVEvKSGSYFDFLQQ 282
Cdd:COG0803 232 LIKEEGVKAIFVESQVSPKLAETLAEETGVKVLYLDSLGGPGG-PGDTYLDMMRH 285
|
|
| AdcA |
cd01017 |
Metal binding protein AdcA. These proteins have been shown to function in the ABC uptake of ... |
22-282 |
9.75e-44 |
|
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: 150.52 E-value: 9.75e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330282354 22 TILTSFKPIQmivtELTQGVS----EPDVLMNSNASPHDYALKPSDVKKVHSADMVIWFGPDLEAFLTKVIGSKEN---- 93
Cdd:cd01017 5 KVVTTFYPLY----EFTKAIGgdkaDVKLIIPAGTEPHDFEPSPKDIARIADADVFVYNGLGMETWAEKVLKSLQNkklk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330282354 94 VIKISEipGINLREFGHDDHDAHEGHNHGSH--DPHFWLGIDQVEVAAKYISAKLIESDPDNAMAYQENLDSFLIALKEK 171
Cdd:cd01017 81 VVEASK--GIKLLKAGGAEHDHDHSHSHHHGdyDPHVWLSPVLAIQQVENIKDALIKLDPDNKEYYEKNAAAYAKKLEAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330282354 172 QQSIHEQLAPVKDKGYYVFHDAYGYFEQEFELNNLGHFTVSPERKPGAKSLIAIKKTLVRDNVQCVFAEPQFTPAVIESV 251
Cdd:cd01017 159 DQEYRAKLAKAKGKTFVTQHAAFGYLARRYGLKQIAIVGVSPEVEPSPKQLAELVEFVKKSDVKYIFFEENASSKIAETL 238
|
250 260 270
....*....|....*....|....*....|....
gi 1330282354 252 TRGSNAKQGQLDPI--GSTVEVKSG-SYFDFLQQ 282
Cdd:cd01017 239 AKETGAKLLVLNPLetLTKEEIDDGkDYFSLMKE 272
|
|
| AztC |
NF040870 |
zinc ABC transporter substrate-binding protein AztC; |
23-291 |
1.24e-40 |
|
zinc ABC transporter substrate-binding protein AztC;
Pssm-ID: 468807 [Multi-domain] Cd Length: 277 Bit Score: 142.41 E-value: 1.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330282354 23 ILTSFKPIQMIVTELTQGVSEPDVLMNSNASPHDYALKPSDVKKVHSADMVIWFGPDL-EAFLTKVIGSKENVIKISEI- 100
Cdd:NF040870 1 VVVTTNILGDLARNVVGDRAEVTTLMKPDADPHSFEPSAADAAALERADLVVVNGLGLeEGFLRHLIAASATGAPVVEVg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330282354 101 PGINLREFGHDDHDAHEGHnHGSHDPHFWLGIDQVEVAAKYISAKLIESDPDNAMAYQENLDSFLIALKEKQQSIHEQLA 180
Cdd:NF040870 81 DGVDPLPYPEGGHYHFEAG-AGPPDPHFWTDPARARDAVDNIADAFCEADDGDCAAYRANAAAYRAELDELDAEMREAFA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330282354 181 --PVKDKGYYVFHDAYGYFEQEFELNNLGHFTV--SPERKPGAKSLIAIKKTLVRDNVQCVFAEPQFTPAVIESVTRGSN 256
Cdd:NF040870 160 aiPADRRTLVTNHHVFGYLAERYGFRVLGAVIPsgSTLASPSAADLASLARAIREAGVPAIFAESSQPPRLAEVLASEAG 239
|
250 260 270
....*....|....*....|....*....|....*...
gi 1330282354 257 AKQGQLDPIGSTVEVKSG---SYFDFLQQLTDSYTSCL 291
Cdd:NF040870 240 LDVGVVELYSESLSEPDGgaaTYLDMMRANAEAIVDGL 277
|
|
| ZntC |
cd01018 |
Metal binding protein ZntC. These proteins are predicted to function as initial receptors in ... |
46-271 |
9.52e-35 |
|
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: 126.71 E-value: 9.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330282354 46 VLMNSNASPHDYALKPSDVKKVHSADMVIWFGPDLE-AFLTKV--IGSKENVIKISEipGINLREF-GHDDHDA--HEGH 119
Cdd:cd01018 28 VLVPPGSNPHTYEPKPQQMKKLSEADLYFRIGLGFEeVWLERFrsNNPKMQVVNMSK--GITLIPMaDHHHHHHgeHEHH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330282354 120 NHGSHDPHFWLGIDQVEVAAKYISAKLIESDPDNAMAYQENLDSFLIALKEKQQSIHEQLAPVKDKGYYVFHDAYGYFEQ 199
Cdd:cd01018 106 HHGNYDPHIWLSPANAKIMAENIYEALAELDPQNATYYQANLDALLAELDALDSEIRTILSKLKQRAFMVYHPAWGYFAR 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1330282354 200 EFelnNLGHFTVSPERK-PGAKSLIAIKKTLVRDNVQCVFAEPQFTPAVIESVTRGSNAKQGQLDPIGSTVEV 271
Cdd:cd01018 186 DY---GLTQIPIEEEGKePSPADLKRLIDLAKEKGVRVVFVQPQFSTKSAEAIAREIGAKVVTIDPLAADWEE 255
|
|
| PsaA |
cd01137 |
Metal binding protein PsaA. These proteins have been shown to function as initial receptors ... |
6-292 |
1.34e-34 |
|
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: 126.62 E-value: 1.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330282354 6 FILATLLLAPSVASAN-TILTSFKpiqmIVTELTQGVSEPDVLMNS----NASPHDYALKPSDVKKVHSADMVIWFGPDL 80
Cdd:cd01137 2 AACASLGSSPATAASKlKVVATFS----ILADIARNIAGDRVNVTSivppGADPHEYEPTPSDIKKLSKADLILYNGLNL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330282354 81 EAFLTKVIG-SKENVIKISEIPGInlrefghDDHDAHEGHNHGSHDPHFWLGIDQVEVAAKYISAKLIESDPDNAMAYQE 159
Cdd:cd01137 78 EPWLERLVKnAGKDVPVVAVSEGI-------DPIPLEEGHYKGKPDPHAWMSPKNAIIYVKNIAKALSEADPANAETYQK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330282354 160 NLDSFLIALKEKQQSIHEQLAPV-KDKGYYVF-HDAYGYFEQEFELNNLGHFTVSPERKPGAKSLIAIKKTLVRDNVQCV 237
Cdd:cd01137 151 NAAAYKAKLKALDEWAKAKFATIpAEKRKLVTsEGAFSYFAKAYGLKEAYLWPINTEEEGTPKQVATLIEQVKKEKVPAV 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1330282354 238 FAEPQFTPAVIESVTRGSNAK-QGQL--DPIGStvevKSG---SYFDFLQQLTDSYTSCLS 292
Cdd:cd01137 231 FVESTVNDRLMKQVAKETGAKiGGQLytDSLSE----KGGpadTYLDMMEHNLDTIVEGLG 287
|
|
| TroA |
cd01016 |
Metal binding protein TroA. These proteins have been shown to function as initial receptors in ... |
23-277 |
2.64e-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: 96.28 E-value: 2.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330282354 23 ILTSFKPIQMIVTELTQGVSEPDVLMNSNASPHDYALKPSDVKKVHSADMVIWFGPDLEAFLTKV---IGSKENVIKISE 99
Cdd:cd01016 4 VVTTTGMIADAVENIGGDHVEVTGLMGPGVDPHLYKATAGDVEKLQNADVVFYNGLHLEGKMSDVlskLGSSKSVIALED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330282354 100 ipGINLREFGHDDHDAHeghnhgsHDPHFWLGIDQVEVAAKYISAKLIESDPDNAMAYQENLDSFLIALKEKQQSIHEQL 179
Cdd:cd01016 84 --TLDRSQLILDEEEGT-------YDPHIWFDVKLWKYAVKAVAEVLSEKLPEHKDEFQANSEAYVEELDSLDAYAKKKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330282354 180 APVKDKGYYVF--HDAYGYFEQEFELNNLGHFTVSPERKPGAKSLIAIKKTLVRDNVQCVFAEPQFTPAVIESVTRGSNA 257
Cdd:cd01016 155 AEIPEQQRVLVtaHDAFGYFGRAYGFEVKGLQGISTDSEAGLRDINELVDLIVERKIKAIFVESSVNQKSIEALQDAVKA 234
|
250 260
....*....|....*....|....*...
gi 1330282354 258 K------QGQL--DPIGSTvEVKSGSYF 277
Cdd:cd01016 235 RghdvqiGGELysDAMGEE-GTSEGTYI 261
|
|
| TroA_c |
cd01145 |
Periplasmic binding protein TroA_c. These proteins are predicted to function as initial ... |
33-207 |
6.26e-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: 93.72 E-value: 6.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330282354 33 IVTELTQGVSEPdvlmnsnaspHDYALKPSDVKKVHSADMVIWFGPDLEAFLTKVIGSKENVikiSEIPGINLREFGHDD 112
Cdd:cd01145 25 IVSALTPPGVDP----------HQYQLKPSDIAKMRKADLVVTSGHELEGFEPKLAELSSNS---KVQPGIKILIEDSDT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330282354 113 H---DAHEGHNHGSHDPHFWLGIDQVEVAAKYISAKLIESDPDNAMAYQENLDSFLIALKEKQQSIHEQLAPVKDKGYYV 189
Cdd:cd01145 92 VgmvDRAMGDYHGKGNPHVWLDPNNAPALAKALADALIELDPSEQEEYKENLRVFLAKLNKLLREWERQFEGLKGIQVVA 171
|
170
....*....|....*...
gi 1330282354 190 FHDAYGYFeqefeLNNLG 207
Cdd:cd01145 172 YHPSYQYL-----ADWLG 184
|
|
| TroA_b |
cd01020 |
Metal binding protein TroA_b. These proteins are predicted to function as initial receptors ... |
41-252 |
8.25e-21 |
|
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: 89.42 E-value: 8.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330282354 41 VSEPDVLMNSNASPHDYALKPSDVKKVHSADMVIWFGPDLEAFLTKVIGSKENVIKISeipginlreFGHDDHDAHEGHN 120
Cdd:cd01020 24 VEVTSIITNPDVDPHDFEPTPTDAAKVSTADIVVYNGGGYDPWMTKLLADTKDVIVIA---------ADLDGHDDKEGDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330282354 121 hgshdPHFWLGIDQVEVAAKYISAKLIESDPDNAMAYQENLDSFLIALKEKQQSIHEQLAPVKDKGYY----VFH---DA 193
Cdd:cd01020 95 -----PHLWYDPETMSKVANALADALVKADPDNKKYYQANAKKFVASLKPLAAKIAELSAKYKGAPVAatepVFDyllDA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1330282354 194 YGYFEQ--EFELNnlghfTVSPERKPGAKSLIAIKKTLVRDNVQCVFAEPQFTPAVIESVT 252
Cdd:cd01020 170 LGMKERtpKGYTA-----TTESETEPSPADIAAFQNAIKNRQIDALIVNPQQASSATTNIT 225
|
|
| anch_rpt_subst |
TIGR03772 |
anchored repeat ABC transporter, substrate-binding protein; Members of this protein family are ... |
97-292 |
4.23e-20 |
|
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: 89.92 E-value: 4.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330282354 97 ISEIPG-INLREFGHDDHDAHE-------GHNHGSHDPHFWLGIDQVEVAAKYISAKLIESDPDNAMAYQENLDSFLIAL 168
Cdd:TIGR03772 274 LQEIPGdPRFRFLGRPGSEVYQlpqavlgKHVHGEIDPHLWHNVKNAIAYVEVIRDKLIEVDPRGAQAYRSNASAYIHRL 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330282354 169 KEKQQSIHEQLA--PVKDKGYYVFHDAYGYFEQEFELNNLGHFTVSPERKPGAKSLIAIKKTLVRDNVQCVFAEPQFtpA 246
Cdd:TIGR03772 354 ERLDTYVRRTIAtiPPSRRHLITTHDAYSYLGQAYGLNIAGFVTPNPAVEPSLADRRRLTRTIENLKVPAVFLEPNL--A 431
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1330282354 247 VIESVTRGSNAKQG-QLDPI-GSTVEVKSGSYFDFLQQLTDSYTSCLS 292
Cdd:TIGR03772 432 ARSTTLNEIADELGvRVCAIyGDTFDDDVTNYVDLMRFNADSLADCLG 479
|
|
| |
