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Conserved domains on  [gi|120587017|ref|NP_780320|]
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HSPB1-associated protein 1 [Mus musculus]

Protein Classification

cupin-like domain-containing protein( domain architecture ID 10613792)

cupin-like domain-containing protein adopts a beta-barrel fold, similar to Homo sapiens lysine-specific demethylase 8, tRNA wybutosine-synthesizing protein 5, HSPB1-associated protein 1, and hypoxia-inducible factor 1-alpha inhibitor

CATH:  2.60.120.10
Gene Ontology:  GO:0046872
PubMed:  14697267|19478949

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Cupin_8 pfam13621
Cupin-like domain; This cupin like domain shares similarity to the JmjC domain.
 37-272 2.60e-36

Cupin-like domain; This cupin like domain shares similarity to the JmjC domain.


:

Pssm-ID: 463936  Cd Length: 251  Bit Score: 134.80  E-value: 2.60e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120587017   37 IMSLQQPAIFCNMVFDWPS-RHWTAKHLSKVLEGKQIRFRmglrgtgtVPQYETECSYVDATLEEFLTWNCDQSSISGPF 115
Cdd:pfam13621   8 YVAKNKPVVIRGAVKDWPAvQKWTDSSLLDYLKDKYGDVE--------VTVEVTPDGRADRLFYNDDFTFVNPKEERMPF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120587017  116 KDY-EHSKfwAYADYKYFVTLFEDKTDVFQEV--VWSDFGFP------GRNGQESTLWIGSFGAHTPCHLDSYGcNLVFQ 186
Cdd:pfam13621  80 GEFlDRLE--AGEDTDTAPYAYLQSDNLRSEFpeLLEDNDLPfateafGGEPDAVNLWMGNGRSVTSLHYDHYE-NLYCV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120587017  187 VQGRKRWHLFPPEDTPFLYPTRI-PYEESSVFSKINVVNPDLKCFPQFQKARR-HMVTLSPGQVLFVPRHWWHYVESLDP 264
Cdd:pfam13621 157 VRGRKRFTLFPPSDVPNLYPGPLePTPEGQVFSLVDPLAPDFERFPRFRDAARpLVVTLNPGDVLYLPALWWHHVESLDP 236


                  ....*...
gi 120587017  265 VTVSINSW 272
Cdd:pfam13621 237 FNIAVNYW 244
 
Name Accession Description Interval E-value
Cupin_8 pfam13621
Cupin-like domain; This cupin like domain shares similarity to the JmjC domain.
 37-272 2.60e-36

Cupin-like domain; This cupin like domain shares similarity to the JmjC domain.


Pssm-ID: 463936  Cd Length: 251  Bit Score: 134.80  E-value: 2.60e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120587017   37 IMSLQQPAIFCNMVFDWPS-RHWTAKHLSKVLEGKQIRFRmglrgtgtVPQYETECSYVDATLEEFLTWNCDQSSISGPF 115
Cdd:pfam13621   8 YVAKNKPVVIRGAVKDWPAvQKWTDSSLLDYLKDKYGDVE--------VTVEVTPDGRADRLFYNDDFTFVNPKEERMPF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120587017  116 KDY-EHSKfwAYADYKYFVTLFEDKTDVFQEV--VWSDFGFP------GRNGQESTLWIGSFGAHTPCHLDSYGcNLVFQ 186
Cdd:pfam13621  80 GEFlDRLE--AGEDTDTAPYAYLQSDNLRSEFpeLLEDNDLPfateafGGEPDAVNLWMGNGRSVTSLHYDHYE-NLYCV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120587017  187 VQGRKRWHLFPPEDTPFLYPTRI-PYEESSVFSKINVVNPDLKCFPQFQKARR-HMVTLSPGQVLFVPRHWWHYVESLDP 264
Cdd:pfam13621 157 VRGRKRFTLFPPSDVPNLYPGPLePTPEGQVFSLVDPLAPDFERFPRFRDAARpLVVTLNPGDVLYLPALWWHHVESLDP 236


                  ....*...
gi 120587017  265 VTVSINSW 272
Cdd:pfam13621 237 FNIAVNYW 244
RoxA COG2850
Ribosomal protein L16 Arg81 hydroxylase, contains JmjC domain [Translation, ribosomal ...
 166-285 6.20e-12

Ribosomal protein L16 Arg81 hydroxylase, contains JmjC domain [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442098  Cd Length: 274  Bit Score: 65.99  E-value: 6.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120587017 166 GSFGAHtpchLDSYGcnlVF--QVQGRKRWHLFPPEDTPflyPTRIPyeessvfskinvvNPDLKCFPQFQKARRhmVTL 243
Cdd:COG2850  117 GGVGPH----FDSYD---VFllQGEGRRRWRIGDQPDDD---PELVP-------------DLPLRILADFEPEID--WVL 171

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 120587017 244 SPGQVLFVPRHWWHYVESLDP-VTVSI----NSWIELEEDHLARVEE 285
Cdd:COG2850  172 EPGDMLYLPPGFAHDGVALEEcMTYSIgfraPSWAELLSELADYLAD 218
cupin_OxDC-like cd20306
Oxalate decarboxylase (OxDC)-like cupin domain; This subfamily contains bacterial and ...
 219-260 2.45e-03

Oxalate decarboxylase (OxDC)-like cupin domain; This subfamily contains bacterial and eukaryotic cupin domains of proteins homologous to oxalate decarboxylase (OxDC; EC 4.1.1.2) such as MSMEG_2254, a putative OxDC from Mycobacterium smegmatis. OxDC is a manganese-dependent bicupin that catalyzes the conversion of oxalate to formate and carbon dioxide, utilizing dioxygen as a cofactor. It is evolutionarily related to oxalate oxidase (OxOx or germin; EC 1.2.3.4) which, in contrast, converts oxalate and dioxygen to carbon dioxide and hydrogen peroxide. OxDC is classified as a bicupin because it contains two cupin folds with each domain containing one manganese binding site, with four manganese binding residues (three histidines and one glutamate) conserved as well as a number of hydrophobic residues.


Pssm-ID: 380440 [Multi-domain]  Cd Length: 151  Bit Score: 38.34  E-value: 2.45e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 120587017 219 KINVVNPDlkcfpqfqkARRHMVTLSPGQVLFVPRHWWHYVE 260
Cdd:cd20306   67 RVSILDPT---------GSLDTFTVKPGQVVFIPQGWLHWIE 99
JmjC smart00558
A domain family that is part of the cupin metalloenzyme superfamily; Probable enzymes, but of ...
 150-189 2.54e-03

A domain family that is part of the cupin metalloenzyme superfamily; Probable enzymes, but of unknown functions, that regulate chromatin reorganisation processes (Clissold and Ponting, in press).


Pssm-ID: 214721  Cd Length: 58  Bit Score: 36.08  E-value: 2.54e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 120587017   150 DFGFPGRNGQeSTLWIGSFGAHTPCHLDSYG-CNLVFQVQG 189
Cdd:smart00558  19 PEDIPGPDVG-PYLYMGMAGSTTPWHIDDYDlVNYLHQGAG 58
 
Name Accession Description Interval E-value
Cupin_8 pfam13621
Cupin-like domain; This cupin like domain shares similarity to the JmjC domain.
 37-272 2.60e-36

Cupin-like domain; This cupin like domain shares similarity to the JmjC domain.


Pssm-ID: 463936  Cd Length: 251  Bit Score: 134.80  E-value: 2.60e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120587017   37 IMSLQQPAIFCNMVFDWPS-RHWTAKHLSKVLEGKQIRFRmglrgtgtVPQYETECSYVDATLEEFLTWNCDQSSISGPF 115
Cdd:pfam13621   8 YVAKNKPVVIRGAVKDWPAvQKWTDSSLLDYLKDKYGDVE--------VTVEVTPDGRADRLFYNDDFTFVNPKEERMPF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120587017  116 KDY-EHSKfwAYADYKYFVTLFEDKTDVFQEV--VWSDFGFP------GRNGQESTLWIGSFGAHTPCHLDSYGcNLVFQ 186
Cdd:pfam13621  80 GEFlDRLE--AGEDTDTAPYAYLQSDNLRSEFpeLLEDNDLPfateafGGEPDAVNLWMGNGRSVTSLHYDHYE-NLYCV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120587017  187 VQGRKRWHLFPPEDTPFLYPTRI-PYEESSVFSKINVVNPDLKCFPQFQKARR-HMVTLSPGQVLFVPRHWWHYVESLDP 264
Cdd:pfam13621 157 VRGRKRFTLFPPSDVPNLYPGPLePTPEGQVFSLVDPLAPDFERFPRFRDAARpLVVTLNPGDVLYLPALWWHHVESLDP 236


                  ....*...
gi 120587017  265 VTVSINSW 272
Cdd:pfam13621 237 FNIAVNYW 244
RoxA COG2850
Ribosomal protein L16 Arg81 hydroxylase, contains JmjC domain [Translation, ribosomal ...
 166-285 6.20e-12

Ribosomal protein L16 Arg81 hydroxylase, contains JmjC domain [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442098  Cd Length: 274  Bit Score: 65.99  E-value: 6.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120587017 166 GSFGAHtpchLDSYGcnlVF--QVQGRKRWHLFPPEDTPflyPTRIPyeessvfskinvvNPDLKCFPQFQKARRhmVTL 243
Cdd:COG2850  117 GGVGPH----FDSYD---VFllQGEGRRRWRIGDQPDDD---PELVP-------------DLPLRILADFEPEID--WVL 171

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 120587017 244 SPGQVLFVPRHWWHYVESLDP-VTVSI----NSWIELEEDHLARVEE 285
Cdd:COG2850  172 EPGDMLYLPPGFAHDGVALEEcMTYSIgfraPSWAELLSELADYLAD 218
JmjC_2 pfam08007
JmjC domain; This entry includes proteins with a JmjC domain that belong to the cupin ...
 166-269 2.15e-09

JmjC domain; This entry includes proteins with a JmjC domain that belong to the cupin superfamily, including Bifunctional lysine-specific demethylase and histidyl-hydroxylase NO66, Ribosomal oxygenase 1/2, and 50S ribosomal protein L16 3-hydroxylase from Escherichia coli. Proteins are bifunctional, acting as histone lysine demethylases and ribosomal histidine hydroxylases.


Pssm-ID: 462340  Cd Length: 116  Bit Score: 54.95  E-value: 2.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120587017  166 GSFGAHtpchLDSYGcnlVF--QVQGRKRWHLFPPedtpflyptriPYEESSVFSkinvvNPDLKCFPQFQKArrHMVTL 243
Cdd:pfam08007  26 GGVGPH----YDDYD---VFllQGEGRKRWRVGAP-----------KVPDLEFYS-----DPPLRILDDFEPV--HDFVL 80

                          90       100
                  ....*....|....*....|....*..
gi 120587017  244 SPGQVLFVPRHWWHYVESLDP-VTVSI 269
Cdd:pfam08007  81 EPGDMLYLPRGFIHQGVALDEsLHYSV 107
cupin_OxDC-like cd20306
Oxalate decarboxylase (OxDC)-like cupin domain; This subfamily contains bacterial and ...
 219-260 2.45e-03

Oxalate decarboxylase (OxDC)-like cupin domain; This subfamily contains bacterial and eukaryotic cupin domains of proteins homologous to oxalate decarboxylase (OxDC; EC 4.1.1.2) such as MSMEG_2254, a putative OxDC from Mycobacterium smegmatis. OxDC is a manganese-dependent bicupin that catalyzes the conversion of oxalate to formate and carbon dioxide, utilizing dioxygen as a cofactor. It is evolutionarily related to oxalate oxidase (OxOx or germin; EC 1.2.3.4) which, in contrast, converts oxalate and dioxygen to carbon dioxide and hydrogen peroxide. OxDC is classified as a bicupin because it contains two cupin folds with each domain containing one manganese binding site, with four manganese binding residues (three histidines and one glutamate) conserved as well as a number of hydrophobic residues.


Pssm-ID: 380440 [Multi-domain]  Cd Length: 151  Bit Score: 38.34  E-value: 2.45e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 120587017 219 KINVVNPDlkcfpqfqkARRHMVTLSPGQVLFVPRHWWHYVE 260
Cdd:cd20306   67 RVSILDPT---------GSLDTFTVKPGQVVFIPQGWLHWIE 99
JmjC smart00558
A domain family that is part of the cupin metalloenzyme superfamily; Probable enzymes, but of ...
 150-189 2.54e-03

A domain family that is part of the cupin metalloenzyme superfamily; Probable enzymes, but of unknown functions, that regulate chromatin reorganisation processes (Clissold and Ponting, in press).


Pssm-ID: 214721  Cd Length: 58  Bit Score: 36.08  E-value: 2.54e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 120587017   150 DFGFPGRNGQeSTLWIGSFGAHTPCHLDSYG-CNLVFQVQG 189
Cdd:smart00558  19 PEDIPGPDVG-PYLYMGMAGSTTPWHIDDYDlVNYLHQGAG 58
 
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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