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Conserved domains on  [gi|118092763|ref|XP_426507|]
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hypoxia-inducible factor 1-alpha inhibitor [Gallus gallus]

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

 Zoom to residue level

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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.
 49-298 4.43e-41

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


:

Pssm-ID: 463936  Cd Length: 251  Bit Score: 144.05  E-value: 4.43e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118092763   49 EELIENEEPVVLTDTNLVYPAL-KWD----LDYLQENIGNGDFSVY---SASTHKFLYYDEKKMANFKnfkpkssREEMK 120
Cdd:pfam13621   6 REYVAKNKPVVIRGAVKDWPAVqKWTdsslLDYLKDKYGDVEVTVEvtpDGRADRLFYNDDFTFVNPK-------EERMP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118092763  121 FAEFVDRLQEIQQKGSAERLYLQQTLNDTVGRKIVVDF-LGFNWNWINKQQgkrgwgQLTSnlLLIGMEGNVTPAHYDEQ 199
Cdd:pfam13621  79 FGEFLDRLEAGEDTDTAPYAYLQSDNLRSEFPELLEDNdLPFATEAFGGEP------DAVN--LWMGNGRSVTSLHYDHY 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118092763  200 QNFFAQIKGYKRCILFPPDQFECLYPYPVHHPCDRQ--SQVDFDNPDYEKFPNFRSVV-GYETVVGPGDVLYIPMYWWHH 276
Cdd:pfam13621 151 ENLYCVVRGRKRFTLFPPSDVPNLYPGPLEPTPEGQvfSLVDPLAPDFERFPRFRDAArPLVVTLNPGDVLYLPALWWHH 230

                         250       260
                  ....*....|....*....|..
gi 118092763  277 IESLlnGGITITVNFWYKGAPT 298
Cdd:pfam13621 231 VESL--DPFNIAVNYWYDMSFD 250
 
Name Accession Description Interval E-value
Cupin_8 pfam13621
Cupin-like domain; This cupin like domain shares similarity to the JmjC domain.
 49-298 4.43e-41

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


Pssm-ID: 463936  Cd Length: 251  Bit Score: 144.05  E-value: 4.43e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118092763   49 EELIENEEPVVLTDTNLVYPAL-KWD----LDYLQENIGNGDFSVY---SASTHKFLYYDEKKMANFKnfkpkssREEMK 120
Cdd:pfam13621   6 REYVAKNKPVVIRGAVKDWPAVqKWTdsslLDYLKDKYGDVEVTVEvtpDGRADRLFYNDDFTFVNPK-------EERMP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118092763  121 FAEFVDRLQEIQQKGSAERLYLQQTLNDTVGRKIVVDF-LGFNWNWINKQQgkrgwgQLTSnlLLIGMEGNVTPAHYDEQ 199
Cdd:pfam13621  79 FGEFLDRLEAGEDTDTAPYAYLQSDNLRSEFPELLEDNdLPFATEAFGGEP------DAVN--LWMGNGRSVTSLHYDHY 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118092763  200 QNFFAQIKGYKRCILFPPDQFECLYPYPVHHPCDRQ--SQVDFDNPDYEKFPNFRSVV-GYETVVGPGDVLYIPMYWWHH 276
Cdd:pfam13621 151 ENLYCVVRGRKRFTLFPPSDVPNLYPGPLEPTPEGQvfSLVDPLAPDFERFPRFRDAArPLVVTLNPGDVLYLPALWWHH 230

                         250       260
                  ....*....|....*....|..
gi 118092763  277 IESLlnGGITITVNFWYKGAPT 298
Cdd:pfam13621 231 VESL--DPFNIAVNYWYDMSFD 250
RoxA COG2850
Ribosomal protein L16 Arg81 hydroxylase, contains JmjC domain [Translation, ribosomal ...
 189-298 3.43e-05

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


Pssm-ID: 442098  Cd Length: 274  Bit Score: 44.81  E-value: 3.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118092763 189 GNVTPaHYDEQQNFFAQIKGYKRCIlfppdqfeclypypVHHPCDRQSQVDfDNPDYEKFPNFRSVvgYETVVGPGDVLY 268
Cdd:COG2850  117 GGVGP-HFDSYDVFLLQGEGRRRWR--------------IGDQPDDDPELV-PDLPLRILADFEPE--IDWVLEPGDMLY 178

                         90       100       110
                 ....*....|....*....|....*....|
gi 118092763 269 IPMYWWHHIESlLNGGITITVNFWykgAPT 298
Cdd:COG2850  179 LPPGFAHDGVA-LEECMTYSIGFR---APS 204
JmjC smart00558
A domain family that is part of the cupin metalloenzyme superfamily; Probable enzymes, but of ...
 158-208 6.38e-05

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: 40.31  E-value: 6.38e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 118092763   158 FLGFNWNWINKQQGKRGWGQLTSNLLlIGMEGNVTPAHYDEQ--QNFFAQIKG 208
Cdd:smart00558   7 KLPFKLNLLSDLPEDIPGPDVGPYLY-MGMAGSTTPWHIDDYdlVNYLHQGAG 58
cupin_OxDC-like cd20306
Oxalate decarboxylase (OxDC)-like cupin domain; This subfamily contains bacterial and ...
 260-304 6.99e-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: 39.50  E-value: 6.99e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 118092763 260 VVGPGDVLYIPMYWWHHIESLLNGGITITVNFwykGAPTPKRIEY 304
Cdd:cd20306   81 TVKPGQVVFIPQGWLHWIENVGDEEAHLLIFF---NHETPEDIGL 122
 
Name Accession Description Interval E-value
Cupin_8 pfam13621
Cupin-like domain; This cupin like domain shares similarity to the JmjC domain.
 49-298 4.43e-41

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


Pssm-ID: 463936  Cd Length: 251  Bit Score: 144.05  E-value: 4.43e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118092763   49 EELIENEEPVVLTDTNLVYPAL-KWD----LDYLQENIGNGDFSVY---SASTHKFLYYDEKKMANFKnfkpkssREEMK 120
Cdd:pfam13621   6 REYVAKNKPVVIRGAVKDWPAVqKWTdsslLDYLKDKYGDVEVTVEvtpDGRADRLFYNDDFTFVNPK-------EERMP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118092763  121 FAEFVDRLQEIQQKGSAERLYLQQTLNDTVGRKIVVDF-LGFNWNWINKQQgkrgwgQLTSnlLLIGMEGNVTPAHYDEQ 199
Cdd:pfam13621  79 FGEFLDRLEAGEDTDTAPYAYLQSDNLRSEFPELLEDNdLPFATEAFGGEP------DAVN--LWMGNGRSVTSLHYDHY 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118092763  200 QNFFAQIKGYKRCILFPPDQFECLYPYPVHHPCDRQ--SQVDFDNPDYEKFPNFRSVV-GYETVVGPGDVLYIPMYWWHH 276
Cdd:pfam13621 151 ENLYCVVRGRKRFTLFPPSDVPNLYPGPLEPTPEGQvfSLVDPLAPDFERFPRFRDAArPLVVTLNPGDVLYLPALWWHH 230

                         250       260
                  ....*....|....*....|..
gi 118092763  277 IESLlnGGITITVNFWYKGAPT 298
Cdd:pfam13621 231 VESL--DPFNIAVNYWYDMSFD 250
JmjC_2 pfam08007
JmjC domain; This entry includes proteins with a JmjC domain that belong to the cupin ...
 193-291 7.79e-07

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: 47.25  E-value: 7.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118092763  193 PAHYDEQQNFFAQIKGYKRcilfppdqfeclypYPVHHPCDRQSQVDfDNPDYEKFPNFRSVvgYETVVGPGDVLYIPMY 272
Cdd:pfam08007  29 GPHYDDYDVFLLQGEGRKR--------------WRVGAPKVPDLEFY-SDPPLRILDDFEPV--HDFVLEPGDMLYLPRG 91

                          90
                  ....*....|....*....
gi 118092763  273 WWHHIESlLNGGITITVNF 291
Cdd:pfam08007  92 FIHQGVA-LDESLHYSVGF 109
RoxA COG2850
Ribosomal protein L16 Arg81 hydroxylase, contains JmjC domain [Translation, ribosomal ...
 189-298 3.43e-05

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


Pssm-ID: 442098  Cd Length: 274  Bit Score: 44.81  E-value: 3.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118092763 189 GNVTPaHYDEQQNFFAQIKGYKRCIlfppdqfeclypypVHHPCDRQSQVDfDNPDYEKFPNFRSVvgYETVVGPGDVLY 268
Cdd:COG2850  117 GGVGP-HFDSYDVFLLQGEGRRRWR--------------IGDQPDDDPELV-PDLPLRILADFEPE--IDWVLEPGDMLY 178

                         90       100       110
                 ....*....|....*....|....*....|
gi 118092763 269 IPMYWWHHIESlLNGGITITVNFWykgAPT 298
Cdd:COG2850  179 LPPGFAHDGVA-LEECMTYSIGFR---APS 204
JmjC smart00558
A domain family that is part of the cupin metalloenzyme superfamily; Probable enzymes, but of ...
 158-208 6.38e-05

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: 40.31  E-value: 6.38e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 118092763   158 FLGFNWNWINKQQGKRGWGQLTSNLLlIGMEGNVTPAHYDEQ--QNFFAQIKG 208
Cdd:smart00558   7 KLPFKLNLLSDLPEDIPGPDVGPYLY-MGMAGSTTPWHIDDYdlVNYLHQGAG 58
cupin_OxDC-like cd20306
Oxalate decarboxylase (OxDC)-like cupin domain; This subfamily contains bacterial and ...
 260-304 6.99e-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: 39.50  E-value: 6.99e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 118092763 260 VVGPGDVLYIPMYWWHHIESLLNGGITITVNFwykGAPTPKRIEY 304
Cdd:cd20306   81 TVKPGQVVFIPQGWLHWIENVGDEEAHLLIFF---NHETPEDIGL 122
OxdD COG2140
Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate ...
 261-297 7.83e-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: 35.71  E-value: 7.83e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 118092763 261 VGPGDVLYIPMYWWHHIESLLNGGiTITVNFWYKGAP 297
Cdd:COG2140   51 VGPGDVVYVPPGYGHYIINTGDEP-LVFLAVFDDDAG 86
 
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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