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Conserved domains on  [gi|198278531|ref|NP_001107221|]
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hypoxia-inducible factor 1-alpha inhibitor [Rattus norvegicus]

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.
 53-302 3.12e-39

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


:

Pssm-ID: 463936  Cd Length: 251  Bit Score: 139.43  E-value: 3.12e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278531   53 EELIENEEPVVLTDTNLVYPAL-KWD----LEYLQENIGNGDFSVY--SASTHKFLYYDEkkmaNFQNFKPRsnREEIKF 125
Cdd:pfam13621   6 REYVAKNKPVVIRGAVKDWPAVqKWTdsslLDYLKDKYGDVEVTVEvtPDGRADRLFYND----DFTFVNPK--EERMPF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278531  126 HEFVEKLQAIQQRGGEERLYLQQTLNDT----VGRKIVMDFlgfnwnwinkqqGKRGWGQLTSNL-LLIGMEGNVTPAHY 200
Cdd:pfam13621  80 GEFLDRLEAGEDTDTAPYAYLQSDNLRSefpeLLEDNDLPF------------ATEAFGGEPDAVnLWMGNGRSVTSLHY 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278531  201 DEQQNFFAQIKGHKRCILFPPDQFECLYPYPVHHPCDRQ--SQVDFDNPDYERFPNFRNVV-GYETVVGPGDVLYIPMYW 277
Cdd:pfam13621 148 DHYENLYCVVRGRKRFTLFPPSDVPNLYPGPLEPTPEGQvfSLVDPLAPDFERFPRFRDAArPLVVTLNPGDVLYLPALW 227

                         250       260
                  ....*....|....*....|....*
gi 198278531  278 WHHIESLlnGGITITVNFWYKGAPT 302
Cdd:pfam13621 228 WHHVESL--DPFNIAVNYWYDMSFD 250
 
Name Accession Description Interval E-value
Cupin_8 pfam13621
Cupin-like domain; This cupin like domain shares similarity to the JmjC domain.
 53-302 3.12e-39

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


Pssm-ID: 463936  Cd Length: 251  Bit Score: 139.43  E-value: 3.12e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278531   53 EELIENEEPVVLTDTNLVYPAL-KWD----LEYLQENIGNGDFSVY--SASTHKFLYYDEkkmaNFQNFKPRsnREEIKF 125
Cdd:pfam13621   6 REYVAKNKPVVIRGAVKDWPAVqKWTdsslLDYLKDKYGDVEVTVEvtPDGRADRLFYND----DFTFVNPK--EERMPF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278531  126 HEFVEKLQAIQQRGGEERLYLQQTLNDT----VGRKIVMDFlgfnwnwinkqqGKRGWGQLTSNL-LLIGMEGNVTPAHY 200
Cdd:pfam13621  80 GEFLDRLEAGEDTDTAPYAYLQSDNLRSefpeLLEDNDLPF------------ATEAFGGEPDAVnLWMGNGRSVTSLHY 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278531  201 DEQQNFFAQIKGHKRCILFPPDQFECLYPYPVHHPCDRQ--SQVDFDNPDYERFPNFRNVV-GYETVVGPGDVLYIPMYW 277
Cdd:pfam13621 148 DHYENLYCVVRGRKRFTLFPPSDVPNLYPGPLEPTPEGQvfSLVDPLAPDFERFPRFRDAArPLVVTLNPGDVLYLPALW 227

                         250       260
                  ....*....|....*....|....*
gi 198278531  278 WHHIESLlnGGITITVNFWYKGAPT 302
Cdd:pfam13621 228 WHHVESL--DPFNIAVNYWYDMSFD 250
RoxA COG2850
Ribosomal protein L16 Arg81 hydroxylase, contains JmjC domain [Translation, ribosomal ...
 193-302 6.48e-06

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


Pssm-ID: 442098  Cd Length: 274  Bit Score: 47.12  E-value: 6.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278531 193 GNVTPaHYDEQQNFFAQIKGHKRCIlfppdqfeclypypVHHPCDRQSQVDfDNPDYERFPNFRnvVGYETVVGPGDVLY 272
Cdd:COG2850  117 GGVGP-HFDSYDVFLLQGEGRRRWR--------------IGDQPDDDPELV-PDLPLRILADFE--PEIDWVLEPGDMLY 178

                         90       100       110
                 ....*....|....*....|....*....|
gi 198278531 273 IPMYWWHHIESlLNGGITITVNFWykgAPT 302
Cdd:COG2850  179 LPPGFAHDGVA-LEECMTYSIGFR---APS 204
JmjC smart00558
A domain family that is part of the cupin metalloenzyme superfamily; Probable enzymes, but of ...
 160-212 1.87e-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: 41.85  E-value: 1.87e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 198278531   160 MDFLGFNWNWINKQQGKRGWGQLTSNLLlIGMEGNVTPAHYDEQ--QNFFAQIKG 212
Cdd:smart00558   5 LAKLPFKLNLLSDLPEDIPGPDVGPYLY-MGMAGSTTPWHIDDYdlVNYLHQGAG 58
cupin_OxDC-like cd20306
Oxalate decarboxylase (OxDC)-like cupin domain; This subfamily contains bacterial and ...
 264-282 7.95e-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: 7.95e-04
                         10
                 ....*....|....*....
gi 198278531 264 VVGPGDVLYIPMYWWHHIE 282
Cdd:cd20306   81 TVKPGQVVFIPQGWLHWIE 99
 
Name Accession Description Interval E-value
Cupin_8 pfam13621
Cupin-like domain; This cupin like domain shares similarity to the JmjC domain.
 53-302 3.12e-39

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


Pssm-ID: 463936  Cd Length: 251  Bit Score: 139.43  E-value: 3.12e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278531   53 EELIENEEPVVLTDTNLVYPAL-KWD----LEYLQENIGNGDFSVY--SASTHKFLYYDEkkmaNFQNFKPRsnREEIKF 125
Cdd:pfam13621   6 REYVAKNKPVVIRGAVKDWPAVqKWTdsslLDYLKDKYGDVEVTVEvtPDGRADRLFYND----DFTFVNPK--EERMPF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278531  126 HEFVEKLQAIQQRGGEERLYLQQTLNDT----VGRKIVMDFlgfnwnwinkqqGKRGWGQLTSNL-LLIGMEGNVTPAHY 200
Cdd:pfam13621  80 GEFLDRLEAGEDTDTAPYAYLQSDNLRSefpeLLEDNDLPF------------ATEAFGGEPDAVnLWMGNGRSVTSLHY 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278531  201 DEQQNFFAQIKGHKRCILFPPDQFECLYPYPVHHPCDRQ--SQVDFDNPDYERFPNFRNVV-GYETVVGPGDVLYIPMYW 277
Cdd:pfam13621 148 DHYENLYCVVRGRKRFTLFPPSDVPNLYPGPLEPTPEGQvfSLVDPLAPDFERFPRFRDAArPLVVTLNPGDVLYLPALW 227

                         250       260
                  ....*....|....*....|....*
gi 198278531  278 WHHIESLlnGGITITVNFWYKGAPT 302
Cdd:pfam13621 228 WHHVESL--DPFNIAVNYWYDMSFD 250
JmjC_2 pfam08007
JmjC domain; This entry includes proteins with a JmjC domain that belong to the cupin ...
 197-295 2.32e-08

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: 51.48  E-value: 2.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278531  197 PAHYDEQQNFFAQIKGHKRcilfppdqfeclypYPVHHPCDRQSQVDfDNPDYERFPNFRNVvgYETVVGPGDVLYIPMY 276
Cdd:pfam08007  29 GPHYDDYDVFLLQGEGRKR--------------WRVGAPKVPDLEFY-SDPPLRILDDFEPV--HDFVLEPGDMLYLPRG 91

                          90
                  ....*....|....*....
gi 198278531  277 WWHHIESlLNGGITITVNF 295
Cdd:pfam08007  92 FIHQGVA-LDESLHYSVGF 109
RoxA COG2850
Ribosomal protein L16 Arg81 hydroxylase, contains JmjC domain [Translation, ribosomal ...
 193-302 6.48e-06

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


Pssm-ID: 442098  Cd Length: 274  Bit Score: 47.12  E-value: 6.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278531 193 GNVTPaHYDEQQNFFAQIKGHKRCIlfppdqfeclypypVHHPCDRQSQVDfDNPDYERFPNFRnvVGYETVVGPGDVLY 272
Cdd:COG2850  117 GGVGP-HFDSYDVFLLQGEGRRRWR--------------IGDQPDDDPELV-PDLPLRILADFE--PEIDWVLEPGDMLY 178

                         90       100       110
                 ....*....|....*....|....*....|
gi 198278531 273 IPMYWWHHIESlLNGGITITVNFWykgAPT 302
Cdd:COG2850  179 LPPGFAHDGVA-LEECMTYSIGFR---APS 204
JmjC smart00558
A domain family that is part of the cupin metalloenzyme superfamily; Probable enzymes, but of ...
 160-212 1.87e-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: 41.85  E-value: 1.87e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 198278531   160 MDFLGFNWNWINKQQGKRGWGQLTSNLLlIGMEGNVTPAHYDEQ--QNFFAQIKG 212
Cdd:smart00558   5 LAKLPFKLNLLSDLPEDIPGPDVGPYLY-MGMAGSTTPWHIDDYdlVNYLHQGAG 58
cupin_OxDC-like cd20306
Oxalate decarboxylase (OxDC)-like cupin domain; This subfamily contains bacterial and ...
 264-282 7.95e-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: 7.95e-04
                         10
                 ....*....|....*....
gi 198278531 264 VVGPGDVLYIPMYWWHHIE 282
Cdd:cd20306   81 TVKPGQVVFIPQGWLHWIE 99
JmjC pfam02373
JmjC domain, hydroxylase; The JmjC domain belongs to the Cupin superfamily. JmjC-domain ...
 187-295 8.79e-04

JmjC domain, hydroxylase; The JmjC domain belongs to the Cupin superfamily. JmjC-domain proteins may be protein hydroxylases that catalyze a novel histone modification. This is confirmed to be a hydroxylase: the human JmjC protein named Tyw5p unexpectedly acts in the biosynthesis of a hypermodified nucleoside, hydroxy-wybutosine, in tRNA-Phe by catalysing hydroxylation.


Pssm-ID: 396791  Cd Length: 114  Bit Score: 38.43  E-value: 8.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278531  187 LLIGMEGNVTPAHYDEQQNFFAQI---KGHKRCILFPP---DQFE-CLYPYPVHHPCDRQS-QVDFDNPDYERFPNfrnV 258
Cdd:pfam02373   2 LYLGMPFSTTPWHIEDQGLYSINYlhfGAPKVWYIIPPeyaEKFEkVLSDHFGGEQPDDLLhLNTIISPKQLRENG---I 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 198278531  259 VGYETVVGPGDVLYIPMYWWHhieSLLNGG--ITITVNF 295
Cdd:pfam02373  79 PVYRFVQKPGEFVFTFPGWYH---QVFNLGfnIAEAVNF 114
OxdD COG2140
Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate ...
 265-301 8.25e-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: 8.25e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 198278531 265 VGPGDVLYIPMYWWHHIESLLNGGiTITVNFWYKGAP 301
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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