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Conserved domains on  [gi|1394533396|ref|NP_001350785|]
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iron-sulfur cluster co-chaperone protein HscB isoform 3 precursor [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
hscB super family cl32072
co-chaperone HscB; Provisional
 72-143 9.76e-18

co-chaperone HscB; Provisional


The actual alignment was detected with superfamily member PRK05014:

Pssm-ID: 179914 [Multi-domain]  Cd Length: 171  Bit Score: 74.94  E-value: 9.76e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1394533396  72 DYFSLMDCNRSFRVDTAKLQHRYQQLQRLVHPDFFSQRSQTEKDFSEKHSTLVNDAYKTLLAPLSRGLYLVS 143
Cdd:PRK05014    2 DYFTLFGLPARYDIDTQLLASRYQELQRQFHPDKFANASERERLLAVQQAATINDAYQTLKHPLKRAEYLLS 73
HscB_4_cys pfam18256
Co-chaperone HscB tetracysteine metal binding motif; This is the N-terminal domain of human ...
 39-65 3.71e-12

Co-chaperone HscB tetracysteine metal binding motif; This is the N-terminal domain of human co-chaperone protein HscB (hHscB). This domain is capable of binding a metal ion through its tetracysteine metal binding motif. The metal atom is coordinated by a set of four cysteine residues (Cys41, Cys44, Cys58 and Cys61) on opposed beta-hairpins. Although the N-domain lacks any recognizable secondary structure elements, it has several distant structural homologs including C-4 zinc finger domains and rubredoxin.


:

Pssm-ID: 375683  Cd Length: 27  Bit Score: 56.65  E-value: 3.71e-12
                          10        20
                  ....*....|....*....|....*..
gi 1394533396  39 PRCWNCGGPWGPGREDRFFCPQCRALQ 65
Cdd:pfam18256   1 PRCWNCGGPGAPGRGDGFFCPQCRALQ 27
 
Name Accession Description Interval E-value
hscB PRK05014
co-chaperone HscB; Provisional
 72-143 9.76e-18

co-chaperone HscB; Provisional


Pssm-ID: 179914 [Multi-domain]  Cd Length: 171  Bit Score: 74.94  E-value: 9.76e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1394533396  72 DYFSLMDCNRSFRVDTAKLQHRYQQLQRLVHPDFFSQRSQTEKDFSEKHSTLVNDAYKTLLAPLSRGLYLVS 143
Cdd:PRK05014    2 DYFTLFGLPARYDIDTQLLASRYQELQRQFHPDKFANASERERLLAVQQAATINDAYQTLKHPLKRAEYLLS 73
HscB_4_cys pfam18256
Co-chaperone HscB tetracysteine metal binding motif; This is the N-terminal domain of human ...
 39-65 3.71e-12

Co-chaperone HscB tetracysteine metal binding motif; This is the N-terminal domain of human co-chaperone protein HscB (hHscB). This domain is capable of binding a metal ion through its tetracysteine metal binding motif. The metal atom is coordinated by a set of four cysteine residues (Cys41, Cys44, Cys58 and Cys61) on opposed beta-hairpins. Although the N-domain lacks any recognizable secondary structure elements, it has several distant structural homologs including C-4 zinc finger domains and rubredoxin.


Pssm-ID: 375683  Cd Length: 27  Bit Score: 56.65  E-value: 3.71e-12
                          10        20
                  ....*....|....*....|....*..
gi 1394533396  39 PRCWNCGGPWGPGREDRFFCPQCRALQ 65
Cdd:pfam18256   1 PRCWNCGGPGAPGRGDGFFCPQCRALQ 27
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
71-141 3.94e-12

DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 57.88  E-value: 3.94e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1394533396  71 RDYFSLMDCNRSfrVDTAKLQHRYQQLQRLVHPDFF-SQRSQTEKDFSEKHSTLVNDAYKTLLAPlsRGLYL 141
Cdd:COG1076     4 DDAFELLGLPPD--ADDAELKRAYRKLQREHHPDRLaAGLPEEEQRLALQKAAAINEAYETLKDP--RGIDL 71
hscB TIGR00714
Fe-S protein assembly co-chaperone HscB; This model describes the small subunit, Hsc20 (20K ...
 83-143 6.19e-11

Fe-S protein assembly co-chaperone HscB; This model describes the small subunit, Hsc20 (20K heat shock cognate protein) of a pair of proteins Hsc66-Hsc20, related to the DnaK-DnaJ heat shock proteins, which also serve as molecular chaperones. Hsc20, unlike DnaJ, appears not to have chaperone activity on its own, but to act solely as a regulatory subunit for Hsc66 (i.e., to be a co-chaperone). The gene for Hsc20 in E. coli, hscB, is not induced by heat shock. [Protein fate, Protein folding and stabilization]


Pssm-ID: 211601 [Multi-domain]  Cd Length: 155  Bit Score: 56.82  E-value: 6.19e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1394533396  83 FRVDTAKLQHRYQQLQRLVHPDffSQRSQTEKDFSEKHSTLVNDAYKTLLAPLSRGLYLVS 143
Cdd:TIGR00714   1 WQLDQSRLRKRYRQLQAQYHPD--ASGMAQEQLAASQQSTTLNQAYHTLKDPLRRAEYMLK 59
 
Name Accession Description Interval E-value
hscB PRK05014
co-chaperone HscB; Provisional
 72-143 9.76e-18

co-chaperone HscB; Provisional


Pssm-ID: 179914 [Multi-domain]  Cd Length: 171  Bit Score: 74.94  E-value: 9.76e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1394533396  72 DYFSLMDCNRSFRVDTAKLQHRYQQLQRLVHPDFFSQRSQTEKDFSEKHSTLVNDAYKTLLAPLSRGLYLVS 143
Cdd:PRK05014    2 DYFTLFGLPARYDIDTQLLASRYQELQRQFHPDKFANASERERLLAVQQAATINDAYQTLKHPLKRAEYLLS 73
hscB PRK03578
Fe-S protein assembly co-chaperone HscB;
68-143 4.00e-16

Fe-S protein assembly co-chaperone HscB;


Pssm-ID: 235133 [Multi-domain]  Cd Length: 176  Bit Score: 70.82  E-value: 4.00e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1394533396  68 DPTRDYFSLMDCNRSFRVDTAKLQHRYQQLQRLVHPDFFSQRSQTEKDFSEKHSTLVNDAYKTLLAPLSRGLYLVS 143
Cdd:PRK03578    3 SLKDDHFSLFGLPARFALDEAALDAAYRTVQAQVHPDRFAAAGDAEKRVAMQWATRANEAYQTLRDPLKRARYLLH 78
hscB PRK00294
co-chaperone HscB; Provisional
 73-143 6.35e-13

co-chaperone HscB; Provisional


Pssm-ID: 166894 [Multi-domain]  Cd Length: 173  Bit Score: 62.18  E-value: 6.35e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1394533396  73 YFSLMDCNRSFRVDTAKLQHRYQQLQRLVHPDFFSQRSQTEKDFSEKHSTLVNDAYKTLLAPLSRGLYLVS 143
Cdd:PRK00294    6 HFALFDLQPSFRLDLDQLATRYRELAREVHPDRFADAPEREQRLALERSASLNEAYQTLKSPPRRARYLLA 76
hscB PRK01773
Fe-S protein assembly co-chaperone HscB;
74-137 2.36e-12

Fe-S protein assembly co-chaperone HscB;


Pssm-ID: 179335 [Multi-domain]  Cd Length: 173  Bit Score: 60.91  E-value: 2.36e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1394533396  74 FSLMDCNRSFRVDTAKLQHRYQQLQRLVHPDFFSQRSQTEKDFSEKHSTLVNDAYKTLLAPLSR 137
Cdd:PRK01773    5 FALFDLPVDFQLDNALLSERYLALQKSLHPDNFANSSAQEQRLAMQKSAEVNDALQILKDPILR 68
HscB_4_cys pfam18256
Co-chaperone HscB tetracysteine metal binding motif; This is the N-terminal domain of human ...
 39-65 3.71e-12

Co-chaperone HscB tetracysteine metal binding motif; This is the N-terminal domain of human co-chaperone protein HscB (hHscB). This domain is capable of binding a metal ion through its tetracysteine metal binding motif. The metal atom is coordinated by a set of four cysteine residues (Cys41, Cys44, Cys58 and Cys61) on opposed beta-hairpins. Although the N-domain lacks any recognizable secondary structure elements, it has several distant structural homologs including C-4 zinc finger domains and rubredoxin.


Pssm-ID: 375683  Cd Length: 27  Bit Score: 56.65  E-value: 3.71e-12
                          10        20
                  ....*....|....*....|....*..
gi 1394533396  39 PRCWNCGGPWGPGREDRFFCPQCRALQ 65
Cdd:pfam18256   1 PRCWNCGGPGAPGRGDGFFCPQCRALQ 27
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
71-141 3.94e-12

DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 57.88  E-value: 3.94e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1394533396  71 RDYFSLMDCNRSfrVDTAKLQHRYQQLQRLVHPDFF-SQRSQTEKDFSEKHSTLVNDAYKTLLAPlsRGLYL 141
Cdd:COG1076     4 DDAFELLGLPPD--ADDAELKRAYRKLQREHHPDRLaAGLPEEEQRLALQKAAAINEAYETLKDP--RGIDL 71
hscB TIGR00714
Fe-S protein assembly co-chaperone HscB; This model describes the small subunit, Hsc20 (20K ...
 83-143 6.19e-11

Fe-S protein assembly co-chaperone HscB; This model describes the small subunit, Hsc20 (20K heat shock cognate protein) of a pair of proteins Hsc66-Hsc20, related to the DnaK-DnaJ heat shock proteins, which also serve as molecular chaperones. Hsc20, unlike DnaJ, appears not to have chaperone activity on its own, but to act solely as a regulatory subunit for Hsc66 (i.e., to be a co-chaperone). The gene for Hsc20 in E. coli, hscB, is not induced by heat shock. [Protein fate, Protein folding and stabilization]


Pssm-ID: 211601 [Multi-domain]  Cd Length: 155  Bit Score: 56.82  E-value: 6.19e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1394533396  83 FRVDTAKLQHRYQQLQRLVHPDffSQRSQTEKDFSEKHSTLVNDAYKTLLAPLSRGLYLVS 143
Cdd:TIGR00714   1 WQLDQSRLRKRYRQLQAQYHPD--ASGMAQEQLAASQQSTTLNQAYHTLKDPLRRAEYMLK 59
hscB PRK01356
co-chaperone HscB; Provisional
 72-142 7.37e-06

co-chaperone HscB; Provisional


Pssm-ID: 167217 [Multi-domain]  Cd Length: 166  Bit Score: 43.33  E-value: 7.37e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1394533396  72 DYFSLMDCNRSFRVDTAKLQHRYQQLQRLVHPDffsqrsqTEKDFSEKHSTLV-----NDAYKTLLAPLSRGLYLV 142
Cdd:PRK01356    3 NYFQLLGLPQEYNIDLKILEKQYFAMQVKYHPD-------KAKTLQEKEQNLIiaselNNAYSTLKDALKRAEYML 71
 
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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