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Conserved domains on  [gi|672073361|ref|XP_008767562|]
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iron-sulfur cluster co-chaperone protein HscB isoform X1 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
hscB super family cl35209
Fe-S protein assembly co-chaperone HscB;
67-189 3.17e-21

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: 87.00  E-value: 3.17e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073361  67 DPTRDYFSLMNCNQSFRVDIRKLQQRYQQLQRLVHPDFFSQKSQTEKRFSEKHSTLVNDAYKTLQAPVSRGLYLLKLQGI 146
Cdd:PRK03578   3 SLKDDHFSLFGLPARFALDEAALDAAYRTVQAQVHPDRFAAAGDAEKRVAMQWATRANEAYQTLRDPLKRARYLLHLRGV 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 672073361 147 EIPEGTDYRTDSQFLVEIMEINEKLADAKSEAAMEEVEATVRE 189
Cdd:PRK03578  83 DVQAENNTAMPPAFLMQQMEWREAIEDARAARDVDALDALLAE 125
HscB_4_cys pfam18256
Co-chaperone HscB tetracysteine metal binding motif; This is the N-terminal domain of human ...
38-64 3.53e-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: 58.96  E-value: 3.53e-12
                          10        20
                  ....*....|....*....|....*..
gi 672073361   38 PQCWNCGRAMGAGRGDEFFCAHCRALQ 64
Cdd:pfam18256   1 PRCWNCGGPGAPGRGDGFFCPQCRALQ 27
 
Name Accession Description Interval E-value
hscB PRK03578
Fe-S protein assembly co-chaperone HscB;
67-189 3.17e-21

Fe-S protein assembly co-chaperone HscB;


Pssm-ID: 235133 [Multi-domain]  Cd Length: 176  Bit Score: 87.00  E-value: 3.17e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073361  67 DPTRDYFSLMNCNQSFRVDIRKLQQRYQQLQRLVHPDFFSQKSQTEKRFSEKHSTLVNDAYKTLQAPVSRGLYLLKLQGI 146
Cdd:PRK03578   3 SLKDDHFSLFGLPARFALDEAALDAAYRTVQAQVHPDRFAAAGDAEKRVAMQWATRANEAYQTLRDPLKRARYLLHLRGV 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 672073361 147 EIPEGTDYRTDSQFLVEIMEINEKLADAKSEAAMEEVEATVRE 189
Cdd:PRK03578  83 DVQAENNTAMPPAFLMQQMEWREAIEDARAARDVDALDALLAE 125
HscB_4_cys pfam18256
Co-chaperone HscB tetracysteine metal binding motif; This is the N-terminal domain of human ...
38-64 3.53e-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: 58.96  E-value: 3.53e-12
                          10        20
                  ....*....|....*....|....*..
gi 672073361   38 PQCWNCGRAMGAGRGDEFFCAHCRALQ 64
Cdd:pfam18256   1 PRCWNCGGPGAPGRGDGFFCPQCRALQ 27
hscB TIGR00714
Fe-S protein assembly co-chaperone HscB; This model describes the small subunit, Hsc20 (20K ...
101-189 1.29e-10

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: 57.97  E-value: 1.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073361  101 HPDffSQKSQTEKRFSEKHSTLVNDAYKTLQAPVSRGLYLLKLQGIEIP-EGTDYRT--DSQFLVEIMEINEKLADAKSE 177
Cdd:TIGR00714  20 HPD--ASGMAQEQLAASQQSTTLNQAYHTLKDPLRRAEYMLKLLNIDLTqEQTSERDtaFPMELLKVRDELDEIEQMDDE 97
                          90
                  ....*....|..
gi 672073361  178 AAMEEVEATVRE 189
Cdd:TIGR00714  98 AGLELLEKQNKE 109
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
99-140 1.04e-04

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 39.78  E-value: 1.04e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 672073361  99 LVHPDFF-SQKSQTEKRFSEKHSTLVNDAYKTLQAPvsRGLYL 140
Cdd:COG1076   31 EHHPDRLaAGLPEEEQRLALQKAAAINEAYETLKDP--RGIDL 71
HSCB_C pfam07743
HSCB C-terminal oligomerization domain; This domain is the HSCB C-terminal oligomerization ...
157-189 2.05e-04

HSCB C-terminal oligomerization domain; This domain is the HSCB C-terminal oligomerization domain and is found on co-chaperone proteins.


Pssm-ID: 462252  Cd Length: 75  Bit Score: 38.66  E-value: 2.05e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 672073361  157 DSQFLVEIMEINEKLADAKS--EAAMEEVEATVRE 189
Cdd:pfam07743   2 DPEFLMEQMEWREELEEAEArdEEELEELKAENKE 36
 
Name Accession Description Interval E-value
hscB PRK03578
Fe-S protein assembly co-chaperone HscB;
67-189 3.17e-21

Fe-S protein assembly co-chaperone HscB;


Pssm-ID: 235133 [Multi-domain]  Cd Length: 176  Bit Score: 87.00  E-value: 3.17e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073361  67 DPTRDYFSLMNCNQSFRVDIRKLQQRYQQLQRLVHPDFFSQKSQTEKRFSEKHSTLVNDAYKTLQAPVSRGLYLLKLQGI 146
Cdd:PRK03578   3 SLKDDHFSLFGLPARFALDEAALDAAYRTVQAQVHPDRFAAAGDAEKRVAMQWATRANEAYQTLRDPLKRARYLLHLRGV 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 672073361 147 EIPEGTDYRTDSQFLVEIMEINEKLADAKSEAAMEEVEATVRE 189
Cdd:PRK03578  83 DVQAENNTAMPPAFLMQQMEWREAIEDARAARDVDALDALLAE 125
hscB PRK05014
co-chaperone HscB; Provisional
71-187 1.91e-16

co-chaperone HscB; Provisional


Pssm-ID: 179914 [Multi-domain]  Cd Length: 171  Bit Score: 74.17  E-value: 1.91e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073361  71 DYFSLMNCNQSFRVDIRKLQQRYQQLQRLVHPDFFSQKSQTEKRFSEKHSTLVNDAYKTLQAPVSRGLYLLKLQGIEIPE 150
Cdd:PRK05014   2 DYFTLFGLPARYDIDTQLLASRYQELQRQFHPDKFANASERERLLAVQQAATINDAYQTLKHPLKRAEYLLSLHGFDLAH 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 672073361 151 GTDYRTDSQFLVEIMEINEKLADAKS----EAAMEEVEATV 187
Cdd:PRK05014  82 EQHTVRDTAFLMEQMELREELEDIEQskdpEAALESFIKRV 122
hscB PRK00294
co-chaperone HscB; Provisional
72-196 2.47e-16

co-chaperone HscB; Provisional


Pssm-ID: 166894 [Multi-domain]  Cd Length: 173  Bit Score: 74.12  E-value: 2.47e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073361  72 YFSLMNCNQSFRVDIRKLQQRYQQLQRLVHPDFFSQKSQTEKRFSEKHSTLVNDAYKTLQAPVSRGLYLLKLQGIEIPEG 151
Cdd:PRK00294   6 HFALFDLQPSFRLDLDQLATRYRELAREVHPDRFADAPEREQRLALERSASLNEAYQTLKSPPRRARYLLALSGHEVPLE 85
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 672073361 152 TDYRtDSQFLVEIMEINEKLADAKSEAAMEEVEATVREPSFCNEQ 196
Cdd:PRK00294  86 VTVH-DPEFLLQQMQLREELEELQDEADLAGVATFKRRLKAAQDE 129
HscB_4_cys pfam18256
Co-chaperone HscB tetracysteine metal binding motif; This is the N-terminal domain of human ...
38-64 3.53e-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: 58.96  E-value: 3.53e-12
                          10        20
                  ....*....|....*....|....*..
gi 672073361   38 PQCWNCGRAMGAGRGDEFFCAHCRALQ 64
Cdd:pfam18256   1 PRCWNCGGPGAPGRGDGFFCPQCRALQ 27
hscB TIGR00714
Fe-S protein assembly co-chaperone HscB; This model describes the small subunit, Hsc20 (20K ...
101-189 1.29e-10

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: 57.97  E-value: 1.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073361  101 HPDffSQKSQTEKRFSEKHSTLVNDAYKTLQAPVSRGLYLLKLQGIEIP-EGTDYRT--DSQFLVEIMEINEKLADAKSE 177
Cdd:TIGR00714  20 HPD--ASGMAQEQLAASQQSTTLNQAYHTLKDPLRRAEYMLKLLNIDLTqEQTSERDtaFPMELLKVRDELDEIEQMDDE 97
                          90
                  ....*....|..
gi 672073361  178 AAMEEVEATVRE 189
Cdd:TIGR00714  98 AGLELLEKQNKE 109
hscB PRK01773
Fe-S protein assembly co-chaperone HscB;
73-198 2.99e-08

Fe-S protein assembly co-chaperone HscB;


Pssm-ID: 179335 [Multi-domain]  Cd Length: 173  Bit Score: 52.05  E-value: 2.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672073361  73 FSLMNCNQSFRVDIRKLQQRYQQLQRLVHPDFFSQKSQTEKRFSEKHSTLVNDAYKTLQAPVSRG-----LYLLKLQGIE 147
Cdd:PRK01773   5 FALFDLPVDFQLDNALLSERYLALQKSLHPDNFANSSAQEQRLAMQKSAEVNDALQILKDPILRAeaiiaLNTGEQQNLE 84
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 672073361 148 ipegTDYRTDSQFLVEIMEINEKLAD---AKSEAA----MEEVEATVRE-----PSFCNEQPW 198
Cdd:PRK01773  85 ----EKSTQDMAFLMQQMEWREQLEEieqQQDEDAltafSKEIKQEQQAiltelSTALNSQQW 143
hscB PRK01356
co-chaperone HscB; Provisional
71-148 1.67e-06

co-chaperone HscB; Provisional


Pssm-ID: 167217 [Multi-domain]  Cd Length: 166  Bit Score: 46.79  E-value: 1.67e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672073361  71 DYFSLMNCNQSFRVDIRKLQQRYQQLQRLVHPDffSQKSQTEKRFSEKHSTLVNDAYKTLQAPVSRGLYLLKLQGIEI 148
Cdd:PRK01356   3 NYFQLLGLPQEYNIDLKILEKQYFAMQVKYHPD--KAKTLQEKEQNLIIASELNNAYSTLKDALKRAEYMLLLQNINL 78
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
99-140 1.04e-04

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 39.78  E-value: 1.04e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 672073361  99 LVHPDFF-SQKSQTEKRFSEKHSTLVNDAYKTLQAPvsRGLYL 140
Cdd:COG1076   31 EHHPDRLaAGLPEEEQRLALQKAAAINEAYETLKDP--RGIDL 71
HSCB_C pfam07743
HSCB C-terminal oligomerization domain; This domain is the HSCB C-terminal oligomerization ...
157-189 2.05e-04

HSCB C-terminal oligomerization domain; This domain is the HSCB C-terminal oligomerization domain and is found on co-chaperone proteins.


Pssm-ID: 462252  Cd Length: 75  Bit Score: 38.66  E-value: 2.05e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 672073361  157 DSQFLVEIMEINEKLADAKS--EAAMEEVEATVRE 189
Cdd:pfam07743   2 DPEFLMEQMEWREELEEAEArdEEELEELKAENKE 36
PknG_rubred pfam16919
Protein kinase G rubredoxin domain; This rubredoxin domain is found at the N-terminus of ...
40-60 7.80e-04

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: 38.57  E-value: 7.80e-04
                          10        20
                  ....*....|....*....|....*.
gi 672073361   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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