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Conserved domains on  [gi|488972060|ref|WP_002882986|]
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MULTISPECIES: metal-binding protein ZinT [Klebsiella]

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
1-216 1.26e-150

zinc/cadmium-binding protein; Provisional


:

Pssm-ID: 182368 [Multi-domain]  Cd Length: 216  Bit Score: 416.87  E-value: 1.26e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972060   1 MTRKIPLLALGFGMALASAQAFAHGNHSHGPALTEVERQASEGIFADKDVQDRALSDWEGVWQSVNPYLLNGDLDPVLEQ 80
Cdd:PRK10306   1 MAIRLHKLAVALGVLLVSAPAFAHGHHSHGKPLTEVEQKAANGVFDDANVQDRTLSDWDGVWQSVYPYLQSGKLDPVFQK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972060  81 KAKKPGGKSVEEYRAYYKKGYATDVEQIGIEDDVIEFHVGQTVNSCKYRYSGYKILHYASGKKGVRYLFECQQGDANAPK 160
Cdd:PRK10306  81 KAKKDKTKTFEEIKAYYRKGYATDVEMIGIENGIVEFHRGNEVTSCKYDYDGYKILTYASGKKGVRYLFECKDAESKAPK 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488972060 161 FVQFSDHIIDPRKSQHFHIFMGNESQEALLKEMDNWPTYYPYALHKEQIVDEMLHH 216
Cdd:PRK10306 161 YVQFSDHIIAPRKSSHFHIFMGNDSQQALLNEMENWPTYYPYQLSSEEVVDEMLHH 216
 
Name Accession Description Interval E-value
PRK10306 PRK10306
zinc/cadmium-binding protein; Provisional
1-216 1.26e-150

zinc/cadmium-binding protein; Provisional


Pssm-ID: 182368 [Multi-domain]  Cd Length: 216  Bit Score: 416.87  E-value: 1.26e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972060   1 MTRKIPLLALGFGMALASAQAFAHGNHSHGPALTEVERQASEGIFADKDVQDRALSDWEGVWQSVNPYLLNGDLDPVLEQ 80
Cdd:PRK10306   1 MAIRLHKLAVALGVLLVSAPAFAHGHHSHGKPLTEVEQKAANGVFDDANVQDRTLSDWDGVWQSVYPYLQSGKLDPVFQK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972060  81 KAKKPGGKSVEEYRAYYKKGYATDVEQIGIEDDVIEFHVGQTVNSCKYRYSGYKILHYASGKKGVRYLFECQQGDANAPK 160
Cdd:PRK10306  81 KAKKDKTKTFEEIKAYYRKGYATDVEMIGIENGIVEFHRGNEVTSCKYDYDGYKILTYASGKKGVRYLFECKDAESKAPK 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488972060 161 FVQFSDHIIDPRKSQHFHIFMGNESQEALLKEMDNWPTYYPYALHKEQIVDEMLHH 216
Cdd:PRK10306 161 YVQFSDHIIAPRKSSHFHIFMGNDSQQALLNEMENWPTYYPYQLSSEEVVDEMLHH 216
ZinT COG3443
Periplasmic Zn/Cd-binding protein ZinT [Inorganic ion transport and metabolism];
24-216 4.72e-127

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


Pssm-ID: 442667  Cd Length: 191  Bit Score: 356.14  E-value: 4.72e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972060  24 HGnHSHGPALTEVERQASEGIFADKDVQDRALSDWEGVWQSVNPYLLNGDLDPVLEQKAKKPGGKSVEEYRAYYKKGYAT 103
Cdd:COG3443    1 HG-HSHGHPHTEAEKKAYEGYFDDKDVKDRSLSDWEGDWQSVYPYLQDGTLDPVFEHKAKKDGDKTAEEYKAYYTKGYAT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972060 104 DVEQIGIEDDVIEFHVGQTVNSCKYRYSGYKILHYASGKKGVRYLFECQQGDANAPKFVQFSDHIIDPRKSQHFHIFMGN 183
Cdd:COG3443   80 DVDRIVIEGNTVTFHKNGKVKSCEYKYDGYKILTYKSGNRGVRYLFECKDADAGAPKYIQFSDHIIAPEKSAHFHIYWGN 159
                        170       180       190
                 ....*....|....*....|....*....|...
gi 488972060 184 eSQEALLKEMDNWPTYYPYALHKEQIVDEMLHH 216
Cdd:COG3443  160 -DQEALLEEMDNWPTYYPYQLSGDQIVDEMLAH 191
ZinT pfam09223
ZinT (YodA) periplasmic lipocalin-like zinc-recruitment; ZinT plays a critical role in ...
37-216 2.61e-117

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: 331.13  E-value: 2.61e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972060   37 ERQASEGIFADKDVQDRALSDWEGVWQSVNPYLLNGDLDPVLEQKAKKPGGKSVEEYRAYYKKGYATDVEQIGIEDDVIE 116
Cdd:pfam09223   2 EKTVYNGYFEDSQVKDRTLSDWAGDWQSVYPYLLDGTLDPVFEHKAKEKGDKTAEEYKAYYTKGYKTDVDRIVIDGDTIT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972060  117 FHVGQTVNSCKYRYSGYKILHYASGKKGVRYLFECQQGDANAPKFVQFSDHIIDPRKSQHFHIFMGNESQEALLKEMDNW 196
Cdd:pfam09223  82 FTKNGKKKSGTYKYDGYKILTYEKGNRGVRYLFEAKDKDAGAPKYIQFSDHIIAPTKAEHFHIYWGNDSQEALLEEMDNW 161
                         170       180
                  ....*....|....*....|
gi 488972060  197 PTYYPYALHKEQIVDEMLHH 216
Cdd:pfam09223 162 PTYYPSSLSGEEIVQEMLAH 181
Zn_bnd_ABC_AdcA NF033605
zinc ABC transporter substrate-binding lipoprotein AdcA;
37-216 3.67e-69

zinc ABC transporter substrate-binding lipoprotein AdcA;


Pssm-ID: 468109 [Multi-domain]  Cd Length: 516  Bit Score: 220.03  E-value: 3.67e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972060  37 ERQASEGIFADKDVQDRALSDWEGVWQSVNPYLLNGDLDPVLEQKAKKPGGKSVEEYRAYYKKGYATDVEQIGIEDDVIE 116
Cdd:NF033605 337 DKAISDGYFKDSQVKDRELSDYEGDWQSVYPYLKDGTLDEVMKHKAEDDGDMSAKEYKAYYDKGYKTDISNIKITGDTIT 416
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972060 117 FHVGQTVNSCKYRYSGYKILHYASGKKGVRYLFECQ-QGDANAPKFVQFSDHIIDPRKSQHFHIFMGNEsQEALLKEMDN 195
Cdd:NF033605 417 FTKNGKKVTGKYEYDGKDILKYEKGNRGVRYTFKLVgDANKDLPKYVQFSDHNIAPKKAEHFHIFMGND-KDKVLKELDN 495
                        170       180
                 ....*....|....*....|.
gi 488972060 196 WPTYYPYALHKEQIVDEMLHH 216
Cdd:NF033605 496 WPTYYPAKLSKDEIKEEMLAH 516
 
Name Accession Description Interval E-value
PRK10306 PRK10306
zinc/cadmium-binding protein; Provisional
1-216 1.26e-150

zinc/cadmium-binding protein; Provisional


Pssm-ID: 182368 [Multi-domain]  Cd Length: 216  Bit Score: 416.87  E-value: 1.26e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972060   1 MTRKIPLLALGFGMALASAQAFAHGNHSHGPALTEVERQASEGIFADKDVQDRALSDWEGVWQSVNPYLLNGDLDPVLEQ 80
Cdd:PRK10306   1 MAIRLHKLAVALGVLLVSAPAFAHGHHSHGKPLTEVEQKAANGVFDDANVQDRTLSDWDGVWQSVYPYLQSGKLDPVFQK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972060  81 KAKKPGGKSVEEYRAYYKKGYATDVEQIGIEDDVIEFHVGQTVNSCKYRYSGYKILHYASGKKGVRYLFECQQGDANAPK 160
Cdd:PRK10306  81 KAKKDKTKTFEEIKAYYRKGYATDVEMIGIENGIVEFHRGNEVTSCKYDYDGYKILTYASGKKGVRYLFECKDAESKAPK 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488972060 161 FVQFSDHIIDPRKSQHFHIFMGNESQEALLKEMDNWPTYYPYALHKEQIVDEMLHH 216
Cdd:PRK10306 161 YVQFSDHIIAPRKSSHFHIFMGNDSQQALLNEMENWPTYYPYQLSSEEVVDEMLHH 216
ZinT COG3443
Periplasmic Zn/Cd-binding protein ZinT [Inorganic ion transport and metabolism];
24-216 4.72e-127

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


Pssm-ID: 442667  Cd Length: 191  Bit Score: 356.14  E-value: 4.72e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972060  24 HGnHSHGPALTEVERQASEGIFADKDVQDRALSDWEGVWQSVNPYLLNGDLDPVLEQKAKKPGGKSVEEYRAYYKKGYAT 103
Cdd:COG3443    1 HG-HSHGHPHTEAEKKAYEGYFDDKDVKDRSLSDWEGDWQSVYPYLQDGTLDPVFEHKAKKDGDKTAEEYKAYYTKGYAT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972060 104 DVEQIGIEDDVIEFHVGQTVNSCKYRYSGYKILHYASGKKGVRYLFECQQGDANAPKFVQFSDHIIDPRKSQHFHIFMGN 183
Cdd:COG3443   80 DVDRIVIEGNTVTFHKNGKVKSCEYKYDGYKILTYKSGNRGVRYLFECKDADAGAPKYIQFSDHIIAPEKSAHFHIYWGN 159
                        170       180       190
                 ....*....|....*....|....*....|...
gi 488972060 184 eSQEALLKEMDNWPTYYPYALHKEQIVDEMLHH 216
Cdd:COG3443  160 -DQEALLEEMDNWPTYYPYQLSGDQIVDEMLAH 191
ZinT pfam09223
ZinT (YodA) periplasmic lipocalin-like zinc-recruitment; ZinT plays a critical role in ...
37-216 2.61e-117

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: 331.13  E-value: 2.61e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972060   37 ERQASEGIFADKDVQDRALSDWEGVWQSVNPYLLNGDLDPVLEQKAKKPGGKSVEEYRAYYKKGYATDVEQIGIEDDVIE 116
Cdd:pfam09223   2 EKTVYNGYFEDSQVKDRTLSDWAGDWQSVYPYLLDGTLDPVFEHKAKEKGDKTAEEYKAYYTKGYKTDVDRIVIDGDTIT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972060  117 FHVGQTVNSCKYRYSGYKILHYASGKKGVRYLFECQQGDANAPKFVQFSDHIIDPRKSQHFHIFMGNESQEALLKEMDNW 196
Cdd:pfam09223  82 FTKNGKKKSGTYKYDGYKILTYEKGNRGVRYLFEAKDKDAGAPKYIQFSDHIIAPTKAEHFHIYWGNDSQEALLEEMDNW 161
                         170       180
                  ....*....|....*....|
gi 488972060  197 PTYYPYALHKEQIVDEMLHH 216
Cdd:pfam09223 162 PTYYPSSLSGEEIVQEMLAH 181
Zn_bnd_ABC_AdcA NF033605
zinc ABC transporter substrate-binding lipoprotein AdcA;
37-216 3.67e-69

zinc ABC transporter substrate-binding lipoprotein AdcA;


Pssm-ID: 468109 [Multi-domain]  Cd Length: 516  Bit Score: 220.03  E-value: 3.67e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972060  37 ERQASEGIFADKDVQDRALSDWEGVWQSVNPYLLNGDLDPVLEQKAKKPGGKSVEEYRAYYKKGYATDVEQIGIEDDVIE 116
Cdd:NF033605 337 DKAISDGYFKDSQVKDRELSDYEGDWQSVYPYLKDGTLDEVMKHKAEDDGDMSAKEYKAYYDKGYKTDISNIKITGDTIT 416
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972060 117 FHVGQTVNSCKYRYSGYKILHYASGKKGVRYLFECQ-QGDANAPKFVQFSDHIIDPRKSQHFHIFMGNEsQEALLKEMDN 195
Cdd:NF033605 417 FTKNGKKVTGKYEYDGKDILKYEKGNRGVRYTFKLVgDANKDLPKYVQFSDHNIAPKKAEHFHIFMGND-KDKVLKELDN 495
                        170       180
                 ....*....|....*....|.
gi 488972060 196 WPTYYPYALHKEQIVDEMLHH 216
Cdd:NF033605 496 WPTYYPAKLSKDEIKEEMLAH 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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