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Conserved domains on  [gi|1958669194|ref|XP_038945544|]
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iron-sulfur cluster co-chaperone protein HscB isoform X3 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HscB_4_cys pfam18256
Co-chaperone HscB tetracysteine metal binding motif; This is the N-terminal domain of human ...
38-64 4.09e-11

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: 54.72  E-value: 4.09e-11
                          10        20
                  ....*....|....*....|....*..
gi 1958669194  38 PQCWNCGRAMGAGRGDEFFCAHCRALQ 64
Cdd:pfam18256   1 PRCWNCGGPGAPGRGDGFFCPQCRALQ 27
hscB super family cl35209
Fe-S protein assembly co-chaperone HscB;
67-142 1.40e-10

Fe-S protein assembly co-chaperone HscB;


The actual alignment was detected with superfamily member PRK03578:

Pssm-ID: 235133 [Multi-domain]  Cd Length: 176  Bit Score: 56.95  E-value: 1.40e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958669194  67 DPTRDYFSLMNCNQSFRVDIRKLQQRYQQLQRLVHPDFFSQKSQTEKRFSEKHSTLVNDAYKTLQAPVSRGLYLVR 142
Cdd:PRK03578    3 SLKDDHFSLFGLPARFALDEAALDAAYRTVQAQVHPDRFAAAGDAEKRVAMQWATRANEAYQTLRDPLKRARYLLH 78
 
Name Accession Description Interval E-value
HscB_4_cys pfam18256
Co-chaperone HscB tetracysteine metal binding motif; This is the N-terminal domain of human ...
38-64 4.09e-11

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: 54.72  E-value: 4.09e-11
                          10        20
                  ....*....|....*....|....*..
gi 1958669194  38 PQCWNCGRAMGAGRGDEFFCAHCRALQ 64
Cdd:pfam18256   1 PRCWNCGGPGAPGRGDGFFCPQCRALQ 27
hscB PRK03578
Fe-S protein assembly co-chaperone HscB;
67-142 1.40e-10

Fe-S protein assembly co-chaperone HscB;


Pssm-ID: 235133 [Multi-domain]  Cd Length: 176  Bit Score: 56.95  E-value: 1.40e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958669194  67 DPTRDYFSLMNCNQSFRVDIRKLQQRYQQLQRLVHPDFFSQKSQTEKRFSEKHSTLVNDAYKTLQAPVSRGLYLVR 142
Cdd:PRK03578    3 SLKDDHFSLFGLPARFALDEAALDAAYRTVQAQVHPDRFAAAGDAEKRVAMQWATRANEAYQTLRDPLKRARYLLH 78
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
99-140 7.24e-05

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 39.39  E-value: 7.24e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1958669194  99 LVHPDFF-SQKSQTEKRFSEKHSTLVNDAYKTLQAPvsRGLYL 140
Cdd:COG1076    31 EHHPDRLaAGLPEEEQRLALQKAAAINEAYETLKDP--RGIDL 71
hscB TIGR00714
Fe-S protein assembly co-chaperone HscB; This model describes the small subunit, Hsc20 (20K ...
101-141 2.02e-04

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: 39.48  E-value: 2.02e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1958669194 101 HPDffSQKSQTEKRFSEKHSTLVNDAYKTLQAPVSRGLYLV 141
Cdd:TIGR00714  20 HPD--ASGMAQEQLAASQQSTTLNQAYHTLKDPLRRAEYML 58
 
Name Accession Description Interval E-value
HscB_4_cys pfam18256
Co-chaperone HscB tetracysteine metal binding motif; This is the N-terminal domain of human ...
38-64 4.09e-11

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: 54.72  E-value: 4.09e-11
                          10        20
                  ....*....|....*....|....*..
gi 1958669194  38 PQCWNCGRAMGAGRGDEFFCAHCRALQ 64
Cdd:pfam18256   1 PRCWNCGGPGAPGRGDGFFCPQCRALQ 27
hscB PRK03578
Fe-S protein assembly co-chaperone HscB;
67-142 1.40e-10

Fe-S protein assembly co-chaperone HscB;


Pssm-ID: 235133 [Multi-domain]  Cd Length: 176  Bit Score: 56.95  E-value: 1.40e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958669194  67 DPTRDYFSLMNCNQSFRVDIRKLQQRYQQLQRLVHPDFFSQKSQTEKRFSEKHSTLVNDAYKTLQAPVSRGLYLVR 142
Cdd:PRK03578    3 SLKDDHFSLFGLPARFALDEAALDAAYRTVQAQVHPDRFAAAGDAEKRVAMQWATRANEAYQTLRDPLKRARYLLH 78
hscB PRK00294
co-chaperone HscB; Provisional
72-141 1.11e-08

co-chaperone HscB; Provisional


Pssm-ID: 166894 [Multi-domain]  Cd Length: 173  Bit Score: 51.78  E-value: 1.11e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669194  72 YFSLMNCNQSFRVDIRKLQQRYQQLQRLVHPDFFSQKSQTEKRFSEKHSTLVNDAYKTLQAPVSRGLYLV 141
Cdd:PRK00294    6 HFALFDLQPSFRLDLDQLATRYRELAREVHPDRFADAPEREQRLALERSASLNEAYQTLKSPPRRARYLL 75
hscB PRK05014
co-chaperone HscB; Provisional
71-140 3.64e-08

co-chaperone HscB; Provisional


Pssm-ID: 179914 [Multi-domain]  Cd Length: 171  Bit Score: 50.29  E-value: 3.64e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669194  71 DYFSLMNCNQSFRVDIRKLQQRYQQLQRLVHPDFFSQKSQTEKRFSEKHSTLVNDAYKTLQAPVSRGLYL 140
Cdd:PRK05014    2 DYFTLFGLPARYDIDTQLLASRYQELQRQFHPDKFANASERERLLAVQQAATINDAYQTLKHPLKRAEYL 71
hscB PRK01773
Fe-S protein assembly co-chaperone HscB;
73-136 6.80e-06

Fe-S protein assembly co-chaperone HscB;


Pssm-ID: 179335 [Multi-domain]  Cd Length: 173  Bit Score: 43.96  E-value: 6.80e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958669194  73 FSLMNCNQSFRVDIRKLQQRYQQLQRLVHPDFFSQKSQTEKRFSEKHSTLVNDAYKTLQAPVSR 136
Cdd:PRK01773    5 FALFDLPVDFQLDNALLSERYLALQKSLHPDNFANSSAQEQRLAMQKSAEVNDALQILKDPILR 68
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
99-140 7.24e-05

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 39.39  E-value: 7.24e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1958669194  99 LVHPDFF-SQKSQTEKRFSEKHSTLVNDAYKTLQAPvsRGLYL 140
Cdd:COG1076    31 EHHPDRLaAGLPEEEQRLALQKAAAINEAYETLKDP--RGIDL 71
hscB TIGR00714
Fe-S protein assembly co-chaperone HscB; This model describes the small subunit, Hsc20 (20K ...
101-141 2.02e-04

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: 39.48  E-value: 2.02e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1958669194 101 HPDffSQKSQTEKRFSEKHSTLVNDAYKTLQAPVSRGLYLV 141
Cdd:TIGR00714  20 HPD--ASGMAQEQLAASQQSTTLNQAYHTLKDPLRRAEYML 58
hscB PRK01356
co-chaperone HscB; Provisional
71-141 1.89e-03

co-chaperone HscB; Provisional


Pssm-ID: 167217 [Multi-domain]  Cd Length: 166  Bit Score: 37.16  E-value: 1.89e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958669194  71 DYFSLMNCNQSFRVDIRKLQQRYQQLQRLVHPDffSQKSQTEKRFSEKHSTLVNDAYKTLQAPVSRGLYLV 141
Cdd:PRK01356    3 NYFQLLGLPQEYNIDLKILEKQYFAMQVKYHPD--KAKTLQEKEQNLIIASELNNAYSTLKDALKRAEYML 71
PknG_rubred pfam16919
Protein kinase G rubredoxin domain; This rubredoxin domain is found at the N-terminus of ...
40-60 2.16e-03

Protein kinase G rubredoxin domain; This rubredoxin domain is found at the N-terminus of protein kinase G, and is essential for kinase activity.


Pssm-ID: 435653  Cd Length: 139  Bit Score: 36.64  E-value: 2.16e-03
                          10        20
                  ....*....|....*....|....*.
gi 1958669194  40 CWNCGRAMGAGRGD-----EFFCAHC 60
Cdd:pfam16919  95 CWNCGRPVGRSTGEgpgrsEGWCPHC 120
 
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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