NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|515953403|ref|WP_017383986|]
View 

MULTISPECIES: metal-binding protein ZinT [Enterobacter]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PRK10306 PRK10306
zinc/cadmium-binding protein; Provisional
1-212 3.16e-144

zinc/cadmium-binding protein; Provisional


:

Pssm-ID: 182368 [Multi-domain]  Cd Length: 216  Bit Score: 400.69  E-value: 3.16e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953403   1 MAAQLAKIALTLGTLLVSGSLFA---HSHGHQMTEAEQKAANGVFEDKDVRDRTLSDWDGTWQSVYPFLLDGSLDPVFEK 77
Cdd:PRK10306   1 MAIRLHKLAVALGVLLVSAPAFAhghHSHGKPLTEVEQKAANGVFDDANVQDRTLSDWDGVWQSVYPYLQSGKLDPVFQK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953403  78 KAQK-GEKSAAEVKAYYRKGYATDVDAIGIENNVMEFHRGKTVSSCRYDYSGYKILTYASGKKGVRYLFECKDNASQAPK 156
Cdd:PRK10306  81 KAKKdKTKTFEEIKAYYRKGYATDVEMIGIENGIVEFHRGNEVTSCKYDYDGYKILTYASGKKGVRYLFECKDAESKAPK 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 515953403 157 FVQFSDHIIGPKASSHFHIFMGNTSHEALLKEMDNWPTYYPNEMYKEQVVEEMLHH 212
Cdd:PRK10306 161 YVQFSDHIIAPRKSSHFHIFMGNDSQQALLNEMENWPTYYPYQLSSEEVVDEMLHH 216
 
Name Accession Description Interval E-value
PRK10306 PRK10306
zinc/cadmium-binding protein; Provisional
1-212 3.16e-144

zinc/cadmium-binding protein; Provisional


Pssm-ID: 182368 [Multi-domain]  Cd Length: 216  Bit Score: 400.69  E-value: 3.16e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953403   1 MAAQLAKIALTLGTLLVSGSLFA---HSHGHQMTEAEQKAANGVFEDKDVRDRTLSDWDGTWQSVYPFLLDGSLDPVFEK 77
Cdd:PRK10306   1 MAIRLHKLAVALGVLLVSAPAFAhghHSHGKPLTEVEQKAANGVFDDANVQDRTLSDWDGVWQSVYPYLQSGKLDPVFQK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953403  78 KAQK-GEKSAAEVKAYYRKGYATDVDAIGIENNVMEFHRGKTVSSCRYDYSGYKILTYASGKKGVRYLFECKDNASQAPK 156
Cdd:PRK10306  81 KAKKdKTKTFEEIKAYYRKGYATDVEMIGIENGIVEFHRGNEVTSCKYDYDGYKILTYASGKKGVRYLFECKDAESKAPK 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 515953403 157 FVQFSDHIIGPKASSHFHIFMGNTSHEALLKEMDNWPTYYPNEMYKEQVVEEMLHH 212
Cdd:PRK10306 161 YVQFSDHIIAPRKSSHFHIFMGNDSQQALLNEMENWPTYYPYQLSSEEVVDEMLHH 216
ZinT COG3443
Periplasmic Zn/Cd-binding protein ZinT [Inorganic ion transport and metabolism];
24-212 1.14e-125

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


Pssm-ID: 442667  Cd Length: 191  Bit Score: 352.67  E-value: 1.14e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953403  24 HSHGHQMTEAEQKAANGVFEDKDVRDRTLSDWDGTWQSVYPFLLDGSLDPVFEKKAQK-GEKSAAEVKAYYRKGYATDVD 102
Cdd:COG3443    3 HSHGHPHTEAEKKAYEGYFDDKDVKDRSLSDWEGDWQSVYPYLQDGTLDPVFEHKAKKdGDKTAEEYKAYYTKGYATDVD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953403 103 AIGIENNVMEFHRGKTVSSCRYDYSGYKILTYASGKKGVRYLFECKDNASQAPKFVQFSDHIIGPKASSHFHIFMGNtSH 182
Cdd:COG3443   83 RIVIEGNTVTFHKNGKVKSCEYKYDGYKILTYKSGNRGVRYLFECKDADAGAPKYIQFSDHIIAPEKSAHFHIYWGN-DQ 161
                        170       180       190
                 ....*....|....*....|....*....|
gi 515953403 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 9.38e-115

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: 324.58  E-value: 9.38e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953403   33 AEQKAANGVFEDKDVRDRTLSDWDGTWQSVYPFLLDGSLDPVFEKKA-QKGEKSAAEVKAYYRKGYATDVDAIGIENNVM 111
Cdd:pfam09223   1 EEKTVYNGYFEDSQVKDRTLSDWAGDWQSVYPYLLDGTLDPVFEHKAkEKGDKTAEEYKAYYTKGYKTDVDRIVIDGDTI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953403  112 EFHRGKTVSSCRYDYSGYKILTYASGKKGVRYLFECKDNASQAPKFVQFSDHIIGPKASSHFHIFMGNTSHEALLKEMDN 191
Cdd:pfam09223  81 TFTKNGKKKSGTYKYDGYKILTYEKGNRGVRYLFEAKDKDAGAPKYIQFSDHIIAPTKAEHFHIYWGNDSQEALLEEMDN 160
                         170       180
                  ....*....|....*....|.
gi 515953403  192 WPTYYPNEMYKEQVVEEMLHH 212
Cdd:pfam09223 161 WPTYYPSSLSGEEIVQEMLAH 181
Zn_bnd_ABC_AdcA NF033605
zinc ABC transporter substrate-binding lipoprotein AdcA;
38-212 1.22e-69

zinc ABC transporter substrate-binding lipoprotein AdcA;


Pssm-ID: 468109 [Multi-domain]  Cd Length: 516  Bit Score: 220.80  E-value: 1.22e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953403  38 ANGVFEDKDVRDRTLSDWDGTWQSVYPFLLDGSLDPVFEKKAQ-KGEKSAAEVKAYYRKGYATDVDAIGIENNVMEFHR- 115
Cdd:NF033605 341 SDGYFKDSQVKDRELSDYEGDWQSVYPYLKDGTLDEVMKHKAEdDGDMSAKEYKAYYDKGYKTDISNIKITGDTITFTKn 420
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953403 116 GKTVSScRYDYSGYKILTYASGKKGVRYLFECKDNASQA-PKFVQFSDHIIGPKASSHFHIFMGNtSHEALLKEMDNWPT 194
Cdd:NF033605 421 GKKVTG-KYEYDGKDILKYEKGNRGVRYTFKLVGDANKDlPKYVQFSDHNIAPKKAEHFHIFMGN-DKDKVLKELDNWPT 498
                        170
                 ....*....|....*...
gi 515953403 195 YYPNEMYKEQVVEEMLHH 212
Cdd:NF033605 499 YYPAKLSKDEIKEEMLAH 516
 
Name Accession Description Interval E-value
PRK10306 PRK10306
zinc/cadmium-binding protein; Provisional
1-212 3.16e-144

zinc/cadmium-binding protein; Provisional


Pssm-ID: 182368 [Multi-domain]  Cd Length: 216  Bit Score: 400.69  E-value: 3.16e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953403   1 MAAQLAKIALTLGTLLVSGSLFA---HSHGHQMTEAEQKAANGVFEDKDVRDRTLSDWDGTWQSVYPFLLDGSLDPVFEK 77
Cdd:PRK10306   1 MAIRLHKLAVALGVLLVSAPAFAhghHSHGKPLTEVEQKAANGVFDDANVQDRTLSDWDGVWQSVYPYLQSGKLDPVFQK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953403  78 KAQK-GEKSAAEVKAYYRKGYATDVDAIGIENNVMEFHRGKTVSSCRYDYSGYKILTYASGKKGVRYLFECKDNASQAPK 156
Cdd:PRK10306  81 KAKKdKTKTFEEIKAYYRKGYATDVEMIGIENGIVEFHRGNEVTSCKYDYDGYKILTYASGKKGVRYLFECKDAESKAPK 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 515953403 157 FVQFSDHIIGPKASSHFHIFMGNTSHEALLKEMDNWPTYYPNEMYKEQVVEEMLHH 212
Cdd:PRK10306 161 YVQFSDHIIAPRKSSHFHIFMGNDSQQALLNEMENWPTYYPYQLSSEEVVDEMLHH 216
ZinT COG3443
Periplasmic Zn/Cd-binding protein ZinT [Inorganic ion transport and metabolism];
24-212 1.14e-125

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


Pssm-ID: 442667  Cd Length: 191  Bit Score: 352.67  E-value: 1.14e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953403  24 HSHGHQMTEAEQKAANGVFEDKDVRDRTLSDWDGTWQSVYPFLLDGSLDPVFEKKAQK-GEKSAAEVKAYYRKGYATDVD 102
Cdd:COG3443    3 HSHGHPHTEAEKKAYEGYFDDKDVKDRSLSDWEGDWQSVYPYLQDGTLDPVFEHKAKKdGDKTAEEYKAYYTKGYATDVD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953403 103 AIGIENNVMEFHRGKTVSSCRYDYSGYKILTYASGKKGVRYLFECKDNASQAPKFVQFSDHIIGPKASSHFHIFMGNtSH 182
Cdd:COG3443   83 RIVIEGNTVTFHKNGKVKSCEYKYDGYKILTYKSGNRGVRYLFECKDADAGAPKYIQFSDHIIAPEKSAHFHIYWGN-DQ 161
                        170       180       190
                 ....*....|....*....|....*....|
gi 515953403 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 9.38e-115

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: 324.58  E-value: 9.38e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953403   33 AEQKAANGVFEDKDVRDRTLSDWDGTWQSVYPFLLDGSLDPVFEKKA-QKGEKSAAEVKAYYRKGYATDVDAIGIENNVM 111
Cdd:pfam09223   1 EEKTVYNGYFEDSQVKDRTLSDWAGDWQSVYPYLLDGTLDPVFEHKAkEKGDKTAEEYKAYYTKGYKTDVDRIVIDGDTI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953403  112 EFHRGKTVSSCRYDYSGYKILTYASGKKGVRYLFECKDNASQAPKFVQFSDHIIGPKASSHFHIFMGNTSHEALLKEMDN 191
Cdd:pfam09223  81 TFTKNGKKKSGTYKYDGYKILTYEKGNRGVRYLFEAKDKDAGAPKYIQFSDHIIAPTKAEHFHIYWGNDSQEALLEEMDN 160
                         170       180
                  ....*....|....*....|.
gi 515953403  192 WPTYYPNEMYKEQVVEEMLHH 212
Cdd:pfam09223 161 WPTYYPSSLSGEEIVQEMLAH 181
Zn_bnd_ABC_AdcA NF033605
zinc ABC transporter substrate-binding lipoprotein AdcA;
38-212 1.22e-69

zinc ABC transporter substrate-binding lipoprotein AdcA;


Pssm-ID: 468109 [Multi-domain]  Cd Length: 516  Bit Score: 220.80  E-value: 1.22e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953403  38 ANGVFEDKDVRDRTLSDWDGTWQSVYPFLLDGSLDPVFEKKAQ-KGEKSAAEVKAYYRKGYATDVDAIGIENNVMEFHR- 115
Cdd:NF033605 341 SDGYFKDSQVKDRELSDYEGDWQSVYPYLKDGTLDEVMKHKAEdDGDMSAKEYKAYYDKGYKTDISNIKITGDTITFTKn 420
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953403 116 GKTVSScRYDYSGYKILTYASGKKGVRYLFECKDNASQA-PKFVQFSDHIIGPKASSHFHIFMGNtSHEALLKEMDNWPT 194
Cdd:NF033605 421 GKKVTG-KYEYDGKDILKYEKGNRGVRYTFKLVGDANKDlPKYVQFSDHNIAPKKAEHFHIFMGN-DKDKVLKELDNWPT 498
                        170
                 ....*....|....*...
gi 515953403 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH