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Conserved domains on  [gi|1034635519|ref|XP_016862668|]
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HSPB1-associated protein 1 isoform X2 [Homo sapiens]

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:  19478949|14697267
SCOP:  3001825

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.
 28-210 3.24e-37

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


:

Pssm-ID: 463936  Cd Length: 251  Bit Score: 135.96  E-value: 3.24e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635519  28 TCNYVEATLEEFLtwncdqSSISGPFRDYDHSkfWAYADY----KYFVSLFEDktdlfQDVKWSDFGFpGRNGQESTLWI 103
Cdd:pfam13621  71 NPKEERMPFGEFL------DRLEAGEDTDTAP--YAYLQSdnlrSEFPELLED-----NDLPFATEAF-GGEPDAVNLWM 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635519 104 GSLGAHTPCHLDSYGcNLVFQVQGRKRWHLFPPEDTPFLYPTRI-PYEESSVFSKINVVNPDLKRFPQFRKAQR-HAVTL 181
Cdd:pfam13621 137 GNGRSVTSLHYDHYE-NLYCVVRGRKRFTLFPPSDVPNLYPGPLePTPEGQVFSLVDPLAPDFERFPRFRDAARpLVVTL 215

                         170       180
                  ....*....|....*....|....*....
gi 1034635519 182 SPGQVLFVPRHWWHYVESIDPVTVSINSW 210
Cdd:pfam13621 216 NPGDVLYLPALWWHHVESLDPFNIAVNYW 244
 
Name Accession Description Interval E-value
Cupin_8 pfam13621
Cupin-like domain; This cupin like domain shares similarity to the JmjC domain.
 28-210 3.24e-37

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


Pssm-ID: 463936  Cd Length: 251  Bit Score: 135.96  E-value: 3.24e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635519  28 TCNYVEATLEEFLtwncdqSSISGPFRDYDHSkfWAYADY----KYFVSLFEDktdlfQDVKWSDFGFpGRNGQESTLWI 103
Cdd:pfam13621  71 NPKEERMPFGEFL------DRLEAGEDTDTAP--YAYLQSdnlrSEFPELLED-----NDLPFATEAF-GGEPDAVNLWM 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635519 104 GSLGAHTPCHLDSYGcNLVFQVQGRKRWHLFPPEDTPFLYPTRI-PYEESSVFSKINVVNPDLKRFPQFRKAQR-HAVTL 181
Cdd:pfam13621 137 GNGRSVTSLHYDHYE-NLYCVVRGRKRFTLFPPSDVPNLYPGPLePTPEGQVFSLVDPLAPDFERFPRFRDAARpLVVTL 215

                         170       180
                  ....*....|....*....|....*....
gi 1034635519 182 SPGQVLFVPRHWWHYVESIDPVTVSINSW 210
Cdd:pfam13621 216 NPGDVLYLPALWWHHVESLDPFNIAVNYW 244
RoxA COG2850
Ribosomal protein L16 Arg81 hydroxylase, contains JmjC domain [Translation, ribosomal ...
 104-223 1.14e-11

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


Pssm-ID: 442098  Cd Length: 274  Bit Score: 64.84  E-value: 1.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635519 104 GSLGAHtpchLDSYGcnlVF--QVQGRKRWHLFPPEDTPflyPTRIPyeessvfskinvvNPDLKRFPQFRKAQRhaVTL 181
Cdd:COG2850   117 GGVGPH----FDSYD---VFllQGEGRRRWRIGDQPDDD---PELVP-------------DLPLRILADFEPEID--WVL 171

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1034635519 182 SPGQVLFVPRHWWHYVESIDP-VTVSI----NSWIELEEDHLARVEE 223
Cdd:COG2850   172 EPGDMLYLPPGFAHDGVALEEcMTYSIgfraPSWAELLSELADYLAD 218
JmjC smart00558
A domain family that is part of the cupin metalloenzyme superfamily; Probable enzymes, but of ...
 76-127 1.60e-04

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: 39.54  E-value: 1.60e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1034635519   76 DKTDLFQDVkwsDFGFPGRNGQeSTLWIGSLGAHTPCHLDSYG-CNLVFQVQG 127
Cdd:smart00558  10 FKLNLLSDL---PEDIPGPDVG-PYLYMGMAGSTTPWHIDDYDlVNYLHQGAG 58
cupin_OxDC-like cd20306
Oxalate decarboxylase (OxDC)-like cupin domain; This subfamily contains bacterial and ...
 157-200 1.88e-04

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: 41.42  E-value: 1.88e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1034635519 157 KINVVNPDlkrfpqfrkAQRHAVTLSPGQVLFVPRHWWHYVESI 200
Cdd:cd20306    67 RVSILDPT---------GSLDTFTVKPGQVVFIPQGWLHWIENV 101
 
Name Accession Description Interval E-value
Cupin_8 pfam13621
Cupin-like domain; This cupin like domain shares similarity to the JmjC domain.
 28-210 3.24e-37

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


Pssm-ID: 463936  Cd Length: 251  Bit Score: 135.96  E-value: 3.24e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635519  28 TCNYVEATLEEFLtwncdqSSISGPFRDYDHSkfWAYADY----KYFVSLFEDktdlfQDVKWSDFGFpGRNGQESTLWI 103
Cdd:pfam13621  71 NPKEERMPFGEFL------DRLEAGEDTDTAP--YAYLQSdnlrSEFPELLED-----NDLPFATEAF-GGEPDAVNLWM 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635519 104 GSLGAHTPCHLDSYGcNLVFQVQGRKRWHLFPPEDTPFLYPTRI-PYEESSVFSKINVVNPDLKRFPQFRKAQR-HAVTL 181
Cdd:pfam13621 137 GNGRSVTSLHYDHYE-NLYCVVRGRKRFTLFPPSDVPNLYPGPLePTPEGQVFSLVDPLAPDFERFPRFRDAARpLVVTL 215

                         170       180
                  ....*....|....*....|....*....
gi 1034635519 182 SPGQVLFVPRHWWHYVESIDPVTVSINSW 210
Cdd:pfam13621 216 NPGDVLYLPALWWHHVESLDPFNIAVNYW 244
RoxA COG2850
Ribosomal protein L16 Arg81 hydroxylase, contains JmjC domain [Translation, ribosomal ...
 104-223 1.14e-11

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


Pssm-ID: 442098  Cd Length: 274  Bit Score: 64.84  E-value: 1.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635519 104 GSLGAHtpchLDSYGcnlVF--QVQGRKRWHLFPPEDTPflyPTRIPyeessvfskinvvNPDLKRFPQFRKAQRhaVTL 181
Cdd:COG2850   117 GGVGPH----FDSYD---VFllQGEGRRRWRIGDQPDDD---PELVP-------------DLPLRILADFEPEID--WVL 171

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1034635519 182 SPGQVLFVPRHWWHYVESIDP-VTVSI----NSWIELEEDHLARVEE 223
Cdd:COG2850   172 EPGDMLYLPPGFAHDGVALEEcMTYSIgfraPSWAELLSELADYLAD 218
JmjC_2 pfam08007
JmjC domain; This entry includes proteins with a JmjC domain that belong to the cupin ...
 104-207 2.54e-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: 54.57  E-value: 2.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635519 104 GSLGAHtpchLDSYGcnlVF--QVQGRKRWHLFPPedtpflyptriPYEESSVFSkinvvNPDLKRFPQFRKAqrHAVTL 181
Cdd:pfam08007  26 GGVGPH----YDDYD---VFllQGEGRKRWRVGAP-----------KVPDLEFYS-----DPPLRILDDFEPV--HDFVL 80

                          90       100
                  ....*....|....*....|....*..
gi 1034635519 182 SPGQVLFVPRHWWHYVESIDP-VTVSI 207
Cdd:pfam08007  81 EPGDMLYLPRGFIHQGVALDEsLHYSV 107
JmjC smart00558
A domain family that is part of the cupin metalloenzyme superfamily; Probable enzymes, but of ...
 76-127 1.60e-04

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: 39.54  E-value: 1.60e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1034635519   76 DKTDLFQDVkwsDFGFPGRNGQeSTLWIGSLGAHTPCHLDSYG-CNLVFQVQG 127
Cdd:smart00558  10 FKLNLLSDL---PEDIPGPDVG-PYLYMGMAGSTTPWHIDDYDlVNYLHQGAG 58
cupin_OxDC-like cd20306
Oxalate decarboxylase (OxDC)-like cupin domain; This subfamily contains bacterial and ...
 157-200 1.88e-04

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: 41.42  E-value: 1.88e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1034635519 157 KINVVNPDlkrfpqfrkAQRHAVTLSPGQVLFVPRHWWHYVESI 200
Cdd:cd20306    67 RVSILDPT---------GSLDTFTVKPGQVVFIPQGWLHWIENV 101
OxdD COG2140
Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate ...
 178-202 9.10e-03

Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate transport and metabolism]; Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 441743 [Multi-domain]  Cd Length: 115  Bit Score: 36.10  E-value: 9.10e-03
                          10        20
                  ....*....|....*....|....*
gi 1034635519 178 AVTLSPGQVLFVPRHWWHYVESIDP 202
Cdd:COG2140    48 TVDVGPGDVVYVPPGYGHYIINTGD 72
 
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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