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Conserved domains on  [gi|501419141|gb|AGL94931|]
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hypoxia-inducible factor prolyl hydroxylase 2 [Homo sapiens]

Protein Classification

hypoxia-inducible factor-proline dioxygenase family protein( domain architecture ID 10484654)

hypoxia-inducible factor-proline dioxygenase family protein, similar to Egl nine homolog 1, an alpha-ketoglutarate/2-oxoglutarate-dependent hydroxylase, catalyzes the hydroxylation of two sites on HIF-a, the N-terminal oxygen dependent degradation domain and the C-terminal oxygen dependent degradation domain

CATH:  2.60.120.620
EC:  1.14.11.29
Gene Ontology:  GO:0008198|GO:0160082|GO:0031545

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
220-391 9.64e-38

Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of collagen, for example. Prokaryotic enzymes might catalyse hydroxylation of antibiotic peptides. These are 2-oxoglutarate-dependent dioxygenases, requiring 2-oxoglutarate and dioxygen as cosubstrates and ferrous iron as a cofactor.


:

Pssm-ID: 214780  Cd Length: 165  Bit Score: 134.44  E-value: 9.64e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501419141   220 QQIGDEVRALHDTGKFTDGQlvsQKSDSSKDIRGDKITWIEGkEPGCETIGLLMSSMDDLIRHCNGKLGSykingRTKAM 299
Cdd:smart00702   6 QKLLEEAEPLGWRGEVTRGI---GNPNETSQYRQSNGTWLEL-LERDLVIERIRQRLADFLGLLAGLPLS-----AEDAQ 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501419141   300 VACYPGnGTGYVRHVDNPNGDGRCVTCIYYLNKDwdakVSGGILRIFPEGKAQFADIEPKFDRLLFFWS-DRRNPHEVQP 378
Cdd:smart00702  77 VARYGP-GGHYGPHVDNFLYGDRIATFILYLNDV----EEGGELVFPGLRLMVVATVKPKKGDLLFFPSgHGRSLHGVCP 151
                          170
                   ....*....|....
gi 501419141   379 AY-ATRYAITVWYF 391
Cdd:smart00702 152 VTrGSRWAITGWIR 165
zf-MYND pfam01753
MYND finger;
21-58 1.43e-12

MYND finger;


:

Pssm-ID: 460312  Cd Length: 39  Bit Score: 61.67  E-value: 1.43e-12
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 501419141   21 CELCGKM-ENLLRCSRCRSSFYCCKEHQRQDWKKHKLVC 58
Cdd:pfam01753   1 CAVCGKEaLKLLRCSRCKSVYYCSKECQKADWPYHKKEC 39
 
Name Accession Description Interval E-value
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
220-391 9.64e-38

Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of collagen, for example. Prokaryotic enzymes might catalyse hydroxylation of antibiotic peptides. These are 2-oxoglutarate-dependent dioxygenases, requiring 2-oxoglutarate and dioxygen as cosubstrates and ferrous iron as a cofactor.


Pssm-ID: 214780  Cd Length: 165  Bit Score: 134.44  E-value: 9.64e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501419141   220 QQIGDEVRALHDTGKFTDGQlvsQKSDSSKDIRGDKITWIEGkEPGCETIGLLMSSMDDLIRHCNGKLGSykingRTKAM 299
Cdd:smart00702   6 QKLLEEAEPLGWRGEVTRGI---GNPNETSQYRQSNGTWLEL-LERDLVIERIRQRLADFLGLLAGLPLS-----AEDAQ 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501419141   300 VACYPGnGTGYVRHVDNPNGDGRCVTCIYYLNKDwdakVSGGILRIFPEGKAQFADIEPKFDRLLFFWS-DRRNPHEVQP 378
Cdd:smart00702  77 VARYGP-GGHYGPHVDNFLYGDRIATFILYLNDV----EEGGELVFPGLRLMVVATVKPKKGDLLFFPSgHGRSLHGVCP 151
                          170
                   ....*....|....
gi 501419141   379 AY-ATRYAITVWYF 391
Cdd:smart00702 152 VTrGSRWAITGWIR 165
EGL9 COG3751
Proline 4-hydroxylase (includes Rps23 Pro-64 3,4-dihydroxylase Tpa1), contains SM-20 domain ...
198-393 1.70e-36

Proline 4-hydroxylase (includes Rps23 Pro-64 3,4-dihydroxylase Tpa1), contains SM-20 domain [Translation, ribosomal structure and biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442965 [Multi-domain]  Cd Length: 195  Bit Score: 132.38  E-value: 1.70e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501419141 198 IVPCMNKHGICVVDDFLGKETGQQIGDEVRALHDTGKFTDGQlVSQKSDSS--KDIRGDKITWIEGKEPGcETIGLLMSS 275
Cdd:COG3751    3 LADALAAQGYVVIDDFLPPELAEALLAELPALDEAGAFKPAG-IGRGLDHQvnEWIRRDSILWLDEKLAS-AAQARYLAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501419141 276 MDDLIRHCNGK--LGSYKINGrtkaMVACYPgNGTGYVRHVD-NPNGDGRCVTCIYYLNKDWDAKvSGGILRIFPE-GKA 351
Cdd:COG3751   81 LEELREALNSPlfLGLFEYEG----HFARYP-PGGFYKRHLDaFRGDLNRRLSLVLYLNPDWQPE-WGGELELYDDdGSE 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 501419141 352 QFADIEPKFDRLLFFWSDRRnPHEVQPAYATRYAITVWYFDA 393
Cdd:COG3751  155 EEVTVAPRFNRLVLFLSEEF-PHEVLPVGRERLSIAGWFRTR 195
2OG-FeII_Oxy_3 pfam13640
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
298-391 9.38e-25

2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and Fe(II)-dependent oxygenase superfamily.


Pssm-ID: 463943  Cd Length: 94  Bit Score: 97.45  E-value: 9.38e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501419141  298 AMVACYpGNGTGYVRHVDN----PNGDGRCVTCIYYLNkDWDAKvSGGILRIFPEGKAQfaDIEPKFDRLLFFWSDRRNP 373
Cdd:pfam13640   1 LQLARY-GDGGFYKPHLDFfegaEGGGQRRLTVVLYLN-DWEEE-EGGELVLYDGDGVE--DIKPKKGRLVLFPSSELSL 75
                          90
                  ....*....|....*....
gi 501419141  374 HEVQPAYA-TRYAITVWYF 391
Cdd:pfam13640  76 HEVLPVTGgERWSITGWFR 94
zf-MYND pfam01753
MYND finger;
21-58 1.43e-12

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 61.67  E-value: 1.43e-12
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 501419141   21 CELCGKM-ENLLRCSRCRSSFYCCKEHQRQDWKKHKLVC 58
Cdd:pfam01753   1 CAVCGKEaLKLLRCSRCKSVYYCSKECQKADWPYHKKEC 39
 
Name Accession Description Interval E-value
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
220-391 9.64e-38

Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of collagen, for example. Prokaryotic enzymes might catalyse hydroxylation of antibiotic peptides. These are 2-oxoglutarate-dependent dioxygenases, requiring 2-oxoglutarate and dioxygen as cosubstrates and ferrous iron as a cofactor.


Pssm-ID: 214780  Cd Length: 165  Bit Score: 134.44  E-value: 9.64e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501419141   220 QQIGDEVRALHDTGKFTDGQlvsQKSDSSKDIRGDKITWIEGkEPGCETIGLLMSSMDDLIRHCNGKLGSykingRTKAM 299
Cdd:smart00702   6 QKLLEEAEPLGWRGEVTRGI---GNPNETSQYRQSNGTWLEL-LERDLVIERIRQRLADFLGLLAGLPLS-----AEDAQ 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501419141   300 VACYPGnGTGYVRHVDNPNGDGRCVTCIYYLNKDwdakVSGGILRIFPEGKAQFADIEPKFDRLLFFWS-DRRNPHEVQP 378
Cdd:smart00702  77 VARYGP-GGHYGPHVDNFLYGDRIATFILYLNDV----EEGGELVFPGLRLMVVATVKPKKGDLLFFPSgHGRSLHGVCP 151
                          170
                   ....*....|....
gi 501419141   379 AY-ATRYAITVWYF 391
Cdd:smart00702 152 VTrGSRWAITGWIR 165
EGL9 COG3751
Proline 4-hydroxylase (includes Rps23 Pro-64 3,4-dihydroxylase Tpa1), contains SM-20 domain ...
198-393 1.70e-36

Proline 4-hydroxylase (includes Rps23 Pro-64 3,4-dihydroxylase Tpa1), contains SM-20 domain [Translation, ribosomal structure and biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442965 [Multi-domain]  Cd Length: 195  Bit Score: 132.38  E-value: 1.70e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501419141 198 IVPCMNKHGICVVDDFLGKETGQQIGDEVRALHDTGKFTDGQlVSQKSDSS--KDIRGDKITWIEGKEPGcETIGLLMSS 275
Cdd:COG3751    3 LADALAAQGYVVIDDFLPPELAEALLAELPALDEAGAFKPAG-IGRGLDHQvnEWIRRDSILWLDEKLAS-AAQARYLAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501419141 276 MDDLIRHCNGK--LGSYKINGrtkaMVACYPgNGTGYVRHVD-NPNGDGRCVTCIYYLNKDWDAKvSGGILRIFPE-GKA 351
Cdd:COG3751   81 LEELREALNSPlfLGLFEYEG----HFARYP-PGGFYKRHLDaFRGDLNRRLSLVLYLNPDWQPE-WGGELELYDDdGSE 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 501419141 352 QFADIEPKFDRLLFFWSDRRnPHEVQPAYATRYAITVWYFDA 393
Cdd:COG3751  155 EEVTVAPRFNRLVLFLSEEF-PHEVLPVGRERLSIAGWFRTR 195
2OG-FeII_Oxy_3 pfam13640
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
298-391 9.38e-25

2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and Fe(II)-dependent oxygenase superfamily.


Pssm-ID: 463943  Cd Length: 94  Bit Score: 97.45  E-value: 9.38e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501419141  298 AMVACYpGNGTGYVRHVDN----PNGDGRCVTCIYYLNkDWDAKvSGGILRIFPEGKAQfaDIEPKFDRLLFFWSDRRNP 373
Cdd:pfam13640   1 LQLARY-GDGGFYKPHLDFfegaEGGGQRRLTVVLYLN-DWEEE-EGGELVLYDGDGVE--DIKPKKGRLVLFPSSELSL 75
                          90
                  ....*....|....*....
gi 501419141  374 HEVQPAYA-TRYAITVWYF 391
Cdd:pfam13640  76 HEVLPVTGgERWSITGWFR 94
zf-MYND pfam01753
MYND finger;
21-58 1.43e-12

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 61.67  E-value: 1.43e-12
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 501419141   21 CELCGKM-ENLLRCSRCRSSFYCCKEHQRQDWKKHKLVC 58
Cdd:pfam01753   1 CAVCGKEaLKLLRCSRCKSVYYCSKECQKADWPYHKKEC 39
2OG-FeII_Oxy_4 pfam13661
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
300-390 1.53e-08

2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and Fe(II)-dependent oxygenase superfamily.


Pssm-ID: 433386  Cd Length: 98  Bit Score: 51.96  E-value: 1.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501419141  300 VACYPgNGTGYVRHVDNpnGDGRCVTCIYYLNKDWDAKvSGGILRIFP-EGKAQFAD----IEPKFDRLLFFwsdRRNP- 373
Cdd:pfam13661   3 CSRYE-KGDFLLCHDDV--IEGRRIAFILYLVENWKPD-DGGALDLYDtDGHGQPADitksIVPTWNKLVFF---EVSPg 75
                          90       100
                  ....*....|....*....|..
gi 501419141  374 ---HEVQPAYA--TRYAITVWY 390
Cdd:pfam13661  76 hsfHQVAEVVAekPRLSISGWF 97
 
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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