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Conserved domains on  [gi|1737198857|emb|VAF30008|]
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metal-binding protein YodA [Enterobacter hormaechei]

Protein Classification

metal-binding protein ZinT( domain architecture ID 11484649)

metal-binding protein ZinT operates as an accessory component of ZnuABC transporter to recruit zinc in gram-negative bacteria

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK10306 PRK10306
zinc/cadmium-binding protein; Provisional
1-212 6.66e-144

zinc/cadmium-binding protein; Provisional


:

Pssm-ID: 182368 [Multi-domain]  Cd Length: 216  Bit Score: 399.53  E-value: 6.66e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198857   1 MAAQLAKIALTLGTLLVSGSLFA---HSHGHQMTEAEQKAANGVFEDKDVRDRKLSDWDGTWQSVYPFLLDGSLDPVFEK 77
Cdd:PRK10306    1 MAIRLHKLAVALGVLLVSAPAFAhghHSHGKPLTEVEQKAANGVFDDANVQDRTLSDWDGVWQSVYPYLQSGKLDPVFQK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198857  78 KAQK-GEKSAAEVKAYYRKGYATDVDAIGIENNVMEFHRGKTVSSCRYDYSGYKILTYASGKKGVRYLFECKDNASQAPK 156
Cdd:PRK10306   81 KAKKdKTKTFEEIKAYYRKGYATDVEMIGIENGIVEFHRGNEVTSCKYDYDGYKILTYASGKKGVRYLFECKDAESKAPK 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1737198857 157 FVQFSDHIIGPKASSHFHIFMGNTSHEALLKEMDNWPTYYPNEMYKEQVVEEMLHH 212
Cdd:PRK10306  161 YVQFSDHIIAPRKSSHFHIFMGNDSQQALLNEMENWPTYYPYQLSSEEVVDEMLHH 216
 
Name Accession Description Interval E-value
PRK10306 PRK10306
zinc/cadmium-binding protein; Provisional
1-212 6.66e-144

zinc/cadmium-binding protein; Provisional


Pssm-ID: 182368 [Multi-domain]  Cd Length: 216  Bit Score: 399.53  E-value: 6.66e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198857   1 MAAQLAKIALTLGTLLVSGSLFA---HSHGHQMTEAEQKAANGVFEDKDVRDRKLSDWDGTWQSVYPFLLDGSLDPVFEK 77
Cdd:PRK10306    1 MAIRLHKLAVALGVLLVSAPAFAhghHSHGKPLTEVEQKAANGVFDDANVQDRTLSDWDGVWQSVYPYLQSGKLDPVFQK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198857  78 KAQK-GEKSAAEVKAYYRKGYATDVDAIGIENNVMEFHRGKTVSSCRYDYSGYKILTYASGKKGVRYLFECKDNASQAPK 156
Cdd:PRK10306   81 KAKKdKTKTFEEIKAYYRKGYATDVEMIGIENGIVEFHRGNEVTSCKYDYDGYKILTYASGKKGVRYLFECKDAESKAPK 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1737198857 157 FVQFSDHIIGPKASSHFHIFMGNTSHEALLKEMDNWPTYYPNEMYKEQVVEEMLHH 212
Cdd:PRK10306  161 YVQFSDHIIAPRKSSHFHIFMGNDSQQALLNEMENWPTYYPYQLSSEEVVDEMLHH 216
ZinT COG3443
Periplasmic Zn/Cd-binding protein ZinT [Inorganic ion transport and metabolism];
24-212 3.13e-125

Periplasmic Zn/Cd-binding protein ZinT [Inorganic ion transport and metabolism];


Pssm-ID: 442667  Cd Length: 191  Bit Score: 351.52  E-value: 3.13e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198857  24 HSHGHQMTEAEQKAANGVFEDKDVRDRKLSDWDGTWQSVYPFLLDGSLDPVFEKKAQK-GEKSAAEVKAYYRKGYATDVD 102
Cdd:COG3443     3 HSHGHPHTEAEKKAYEGYFDDKDVKDRSLSDWEGDWQSVYPYLQDGTLDPVFEHKAKKdGDKTAEEYKAYYTKGYATDVD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198857 103 AIGIENNVMEFHRGKTVSSCRYDYSGYKILTYASGKKGVRYLFECKDNASQAPKFVQFSDHIIGPKASSHFHIFMGNtSH 182
Cdd:COG3443    83 RIVIEGNTVTFHKNGKVKSCEYKYDGYKILTYKSGNRGVRYLFECKDADAGAPKYIQFSDHIIAPEKSAHFHIYWGN-DQ 161
                         170       180       190
                  ....*....|....*....|....*....|
gi 1737198857 183 EALLKEMDNWPTYYPNEMYKEQVVEEMLHH 212
Cdd:COG3443   162 EALLEEMDNWPTYYPYQLSGDQIVDEMLAH 191
ZinT pfam09223
ZinT (YodA) periplasmic lipocalin-like zinc-recruitment; ZinT plays a critical role in ...
33-212 2.84e-114

ZinT (YodA) periplasmic lipocalin-like zinc-recruitment; ZinT plays a critical role in recruiting periplasmic zinc to the bacterial zinc-uptake complex ZnuABC, consisting of families pfam01297,pfam00950, pfam00005, regulated by the transcription-regulator FUR, pfam01475. ZinT acts as a Zn2+-buffering protein that delivers Zn2+ to ZnuA (TroA), pfam01297. Members of this family of prokaryotic domains were first identified as part of the response of bacteria to a challenge with the toxic heavy metal cadmium. They are able to bind to cadmium, and ensure its subsequent elimination.


Pssm-ID: 430470  Cd Length: 181  Bit Score: 323.43  E-value: 2.84e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198857  33 AEQKAANGVFEDKDVRDRKLSDWDGTWQSVYPFLLDGSLDPVFEKKA-QKGEKSAAEVKAYYRKGYATDVDAIGIENNVM 111
Cdd:pfam09223   1 EEKTVYNGYFEDSQVKDRTLSDWAGDWQSVYPYLLDGTLDPVFEHKAkEKGDKTAEEYKAYYTKGYKTDVDRIVIDGDTI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198857 112 EFHRGKTVSSCRYDYSGYKILTYASGKKGVRYLFECKDNASQAPKFVQFSDHIIGPKASSHFHIFMGNTSHEALLKEMDN 191
Cdd:pfam09223  81 TFTKNGKKKSGTYKYDGYKILTYEKGNRGVRYLFEAKDKDAGAPKYIQFSDHIIAPTKAEHFHIYWGNDSQEALLEEMDN 160
                         170       180
                  ....*....|....*....|.
gi 1737198857 192 WPTYYPNEMYKEQVVEEMLHH 212
Cdd:pfam09223 161 WPTYYPSSLSGEEIVQEMLAH 181
Zn_bnd_ABC_AdcA NF033605
zinc ABC transporter substrate-binding lipoprotein AdcA;
38-212 1.98e-69

zinc ABC transporter substrate-binding lipoprotein AdcA;


Pssm-ID: 468109 [Multi-domain]  Cd Length: 516  Bit Score: 220.41  E-value: 1.98e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198857  38 ANGVFEDKDVRDRKLSDWDGTWQSVYPFLLDGSLDPVFEKKAQ-KGEKSAAEVKAYYRKGYATDVDAIGIENNVMEFHR- 115
Cdd:NF033605  341 SDGYFKDSQVKDRELSDYEGDWQSVYPYLKDGTLDEVMKHKAEdDGDMSAKEYKAYYDKGYKTDISNIKITGDTITFTKn 420
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198857 116 GKTVSScRYDYSGYKILTYASGKKGVRYLFECKDNASQA-PKFVQFSDHIIGPKASSHFHIFMGNtSHEALLKEMDNWPT 194
Cdd:NF033605  421 GKKVTG-KYEYDGKDILKYEKGNRGVRYTFKLVGDANKDlPKYVQFSDHNIAPKKAEHFHIFMGN-DKDKVLKELDNWPT 498
                         170
                  ....*....|....*...
gi 1737198857 195 YYPNEMYKEQVVEEMLHH 212
Cdd:NF033605  499 YYPAKLSKDEIKEEMLAH 516
 
Name Accession Description Interval E-value
PRK10306 PRK10306
zinc/cadmium-binding protein; Provisional
1-212 6.66e-144

zinc/cadmium-binding protein; Provisional


Pssm-ID: 182368 [Multi-domain]  Cd Length: 216  Bit Score: 399.53  E-value: 6.66e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198857   1 MAAQLAKIALTLGTLLVSGSLFA---HSHGHQMTEAEQKAANGVFEDKDVRDRKLSDWDGTWQSVYPFLLDGSLDPVFEK 77
Cdd:PRK10306    1 MAIRLHKLAVALGVLLVSAPAFAhghHSHGKPLTEVEQKAANGVFDDANVQDRTLSDWDGVWQSVYPYLQSGKLDPVFQK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198857  78 KAQK-GEKSAAEVKAYYRKGYATDVDAIGIENNVMEFHRGKTVSSCRYDYSGYKILTYASGKKGVRYLFECKDNASQAPK 156
Cdd:PRK10306   81 KAKKdKTKTFEEIKAYYRKGYATDVEMIGIENGIVEFHRGNEVTSCKYDYDGYKILTYASGKKGVRYLFECKDAESKAPK 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1737198857 157 FVQFSDHIIGPKASSHFHIFMGNTSHEALLKEMDNWPTYYPNEMYKEQVVEEMLHH 212
Cdd:PRK10306  161 YVQFSDHIIAPRKSSHFHIFMGNDSQQALLNEMENWPTYYPYQLSSEEVVDEMLHH 216
ZinT COG3443
Periplasmic Zn/Cd-binding protein ZinT [Inorganic ion transport and metabolism];
24-212 3.13e-125

Periplasmic Zn/Cd-binding protein ZinT [Inorganic ion transport and metabolism];


Pssm-ID: 442667  Cd Length: 191  Bit Score: 351.52  E-value: 3.13e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198857  24 HSHGHQMTEAEQKAANGVFEDKDVRDRKLSDWDGTWQSVYPFLLDGSLDPVFEKKAQK-GEKSAAEVKAYYRKGYATDVD 102
Cdd:COG3443     3 HSHGHPHTEAEKKAYEGYFDDKDVKDRSLSDWEGDWQSVYPYLQDGTLDPVFEHKAKKdGDKTAEEYKAYYTKGYATDVD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198857 103 AIGIENNVMEFHRGKTVSSCRYDYSGYKILTYASGKKGVRYLFECKDNASQAPKFVQFSDHIIGPKASSHFHIFMGNtSH 182
Cdd:COG3443    83 RIVIEGNTVTFHKNGKVKSCEYKYDGYKILTYKSGNRGVRYLFECKDADAGAPKYIQFSDHIIAPEKSAHFHIYWGN-DQ 161
                         170       180       190
                  ....*....|....*....|....*....|
gi 1737198857 183 EALLKEMDNWPTYYPNEMYKEQVVEEMLHH 212
Cdd:COG3443   162 EALLEEMDNWPTYYPYQLSGDQIVDEMLAH 191
ZinT pfam09223
ZinT (YodA) periplasmic lipocalin-like zinc-recruitment; ZinT plays a critical role in ...
33-212 2.84e-114

ZinT (YodA) periplasmic lipocalin-like zinc-recruitment; ZinT plays a critical role in recruiting periplasmic zinc to the bacterial zinc-uptake complex ZnuABC, consisting of families pfam01297,pfam00950, pfam00005, regulated by the transcription-regulator FUR, pfam01475. ZinT acts as a Zn2+-buffering protein that delivers Zn2+ to ZnuA (TroA), pfam01297. Members of this family of prokaryotic domains were first identified as part of the response of bacteria to a challenge with the toxic heavy metal cadmium. They are able to bind to cadmium, and ensure its subsequent elimination.


Pssm-ID: 430470  Cd Length: 181  Bit Score: 323.43  E-value: 2.84e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198857  33 AEQKAANGVFEDKDVRDRKLSDWDGTWQSVYPFLLDGSLDPVFEKKA-QKGEKSAAEVKAYYRKGYATDVDAIGIENNVM 111
Cdd:pfam09223   1 EEKTVYNGYFEDSQVKDRTLSDWAGDWQSVYPYLLDGTLDPVFEHKAkEKGDKTAEEYKAYYTKGYKTDVDRIVIDGDTI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198857 112 EFHRGKTVSSCRYDYSGYKILTYASGKKGVRYLFECKDNASQAPKFVQFSDHIIGPKASSHFHIFMGNTSHEALLKEMDN 191
Cdd:pfam09223  81 TFTKNGKKKSGTYKYDGYKILTYEKGNRGVRYLFEAKDKDAGAPKYIQFSDHIIAPTKAEHFHIYWGNDSQEALLEEMDN 160
                         170       180
                  ....*....|....*....|.
gi 1737198857 192 WPTYYPNEMYKEQVVEEMLHH 212
Cdd:pfam09223 161 WPTYYPSSLSGEEIVQEMLAH 181
Zn_bnd_ABC_AdcA NF033605
zinc ABC transporter substrate-binding lipoprotein AdcA;
38-212 1.98e-69

zinc ABC transporter substrate-binding lipoprotein AdcA;


Pssm-ID: 468109 [Multi-domain]  Cd Length: 516  Bit Score: 220.41  E-value: 1.98e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198857  38 ANGVFEDKDVRDRKLSDWDGTWQSVYPFLLDGSLDPVFEKKAQ-KGEKSAAEVKAYYRKGYATDVDAIGIENNVMEFHR- 115
Cdd:NF033605  341 SDGYFKDSQVKDRELSDYEGDWQSVYPYLKDGTLDEVMKHKAEdDGDMSAKEYKAYYDKGYKTDISNIKITGDTITFTKn 420
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198857 116 GKTVSScRYDYSGYKILTYASGKKGVRYLFECKDNASQA-PKFVQFSDHIIGPKASSHFHIFMGNtSHEALLKEMDNWPT 194
Cdd:NF033605  421 GKKVTG-KYEYDGKDILKYEKGNRGVRYTFKLVGDANKDlPKYVQFSDHNIAPKKAEHFHIFMGN-DKDKVLKELDNWPT 498
                         170
                  ....*....|....*...
gi 1737198857 195 YYPNEMYKEQVVEEMLHH 212
Cdd:NF033605  499 YYPAKLSKDEIKEEMLAH 516
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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