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Conserved domains on  [gi|32129514|sp|Q9GZT9|]
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RecName: Full=Egl nine homolog 1; AltName: Full=Hypoxia-inducible factor prolyl hydroxylase 2; Short=HIF-PH2; Short=HIF-prolyl hydroxylase 2; Short=HPH-2; AltName: Full=Prolyl hydroxylase domain-containing protein 2; Short=PHD2; AltName: Full=SM-20

Protein Classification

zf-MYND and P4Hc domain-containing protein( domain architecture ID 10484654)

zf-MYND and P4Hc domain-containing protein

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 9.24e-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: 9.24e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32129514    220 QQIGDEVRALHDTGKFTDGQlvsQKSDSSKDIRGDKITWIEGkEPGCETIGLLMSSMDDLIRHCNGKLGSykingRTKAM 299
Cdd:smart00702   6 QKLLEEAEPLGWRGEVTRGI---GNPNETSQYRQSNGTWLEL-LERDLVIERIRQRLADFLGLLAGLPLS-----AEDAQ 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32129514    300 VACYPGnGTGYVRHVDNPNGDGRCVTCIYYLNKDwdakVSGGILRIFPEGKAQFADIEPKFDRLLFFWS-DRRNPHEVQP 378
Cdd:smart00702  77 VARYGP-GGHYGPHVDNFLYGDRIATFILYLNDV----EEGGELVFPGLRLMVVATVKPKKGDLLFFPSgHGRSLHGVCP 151
                          170
                   ....*....|....
gi 32129514    379 AY-ATRYAITVWYF 391
Cdd:smart00702 152 VTrGSRWAITGWIR 165
zf-MYND pfam01753
MYND finger;
21-58 2.74e-12

MYND finger;


:

Pssm-ID: 426410  Cd Length: 39  Bit Score: 60.89  E-value: 2.74e-12
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 32129514    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 9.24e-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: 9.24e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32129514    220 QQIGDEVRALHDTGKFTDGQlvsQKSDSSKDIRGDKITWIEGkEPGCETIGLLMSSMDDLIRHCNGKLGSykingRTKAM 299
Cdd:smart00702   6 QKLLEEAEPLGWRGEVTRGI---GNPNETSQYRQSNGTWLEL-LERDLVIERIRQRLADFLGLLAGLPLS-----AEDAQ 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32129514    300 VACYPGnGTGYVRHVDNPNGDGRCVTCIYYLNKDwdakVSGGILRIFPEGKAQFADIEPKFDRLLFFWS-DRRNPHEVQP 378
Cdd:smart00702  77 VARYGP-GGHYGPHVDNFLYGDRIATFILYLNDV----EEGGELVFPGLRLMVVATVKPKKGDLLFFPSgHGRSLHGVCP 151
                          170
                   ....*....|....
gi 32129514    379 AY-ATRYAITVWYF 391
Cdd:smart00702 152 VTrGSRWAITGWIR 165
2OG-FeII_Oxy_3 pfam13640
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
298-391 1.59e-24

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


Pssm-ID: 433371  Cd Length: 94  Bit Score: 96.68  E-value: 1.59e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32129514   298 AMVACYpGNGTGYVRHVDN----PNGDGRCVTCIYYLNkDWDAKvSGGILRIFPEGKAQfaDIEPKFDRLLFFWSDRRNP 373
Cdd:pfam13640   1 LQLARY-GDGGFYKPHLDFfegaEGGGQRRLTVVLYLN-DWEEE-EGGELVLYDGDGVE--DIKPKKGRLVLFPSSELSL 75
                          90
                  ....*....|....*....
gi 32129514   374 HEVQPAYA-TRYAITVWYF 391
Cdd:pfam13640  76 HEVLPVTGgERWSITGWFR 94
zf-MYND pfam01753
MYND finger;
21-58 2.74e-12

MYND finger;


Pssm-ID: 426410  Cd Length: 39  Bit Score: 60.89  E-value: 2.74e-12
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 32129514    21 CELCGKM-ENLLRCSRCRSSFYCCKEHQRQDWKKHKLVC 58
Cdd:pfam01753   1 CAVCGKEaLKLLRCSRCKSVYYCSKECQKADWPYHKKEC 39
EGL9 COG3751
Proline 4-hydroxylase (includes Rps23 Pro-64 3,4-dihydroxylase Tpa1), contains SM-20 domain ...
283-391 7.49e-10

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: 226274  Cd Length: 252  Bit Score: 58.98  E-value: 7.49e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32129514 283 CNGKLGSYKIngrtKAMVACYPgNGTGYVRHVDNPNG-DGRCVTCIYYLNKDWDAKvSGGILRIFPEGKAQ------FAD 355
Cdd:COG3751 127 LLGILDVSEV----EGQITVYN-PGCFLLKHDDNGRDkDIRLATYVYYLTREWKPE-YGGELRLFHSLQKNntaadsFKT 200
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 32129514 356 IEPKFDRLLFFWSDRRN-PHEVQPAYA--TRYAITVWYF 391
Cdd:COG3751 201 IAPVFNSLVFFKSRPSHsVHSVEEPYAaaDRLSVTGWFR 239
 
Name Accession Description Interval E-value
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
220-391 9.24e-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: 9.24e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32129514    220 QQIGDEVRALHDTGKFTDGQlvsQKSDSSKDIRGDKITWIEGkEPGCETIGLLMSSMDDLIRHCNGKLGSykingRTKAM 299
Cdd:smart00702   6 QKLLEEAEPLGWRGEVTRGI---GNPNETSQYRQSNGTWLEL-LERDLVIERIRQRLADFLGLLAGLPLS-----AEDAQ 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32129514    300 VACYPGnGTGYVRHVDNPNGDGRCVTCIYYLNKDwdakVSGGILRIFPEGKAQFADIEPKFDRLLFFWS-DRRNPHEVQP 378
Cdd:smart00702  77 VARYGP-GGHYGPHVDNFLYGDRIATFILYLNDV----EEGGELVFPGLRLMVVATVKPKKGDLLFFPSgHGRSLHGVCP 151
                          170
                   ....*....|....
gi 32129514    379 AY-ATRYAITVWYF 391
Cdd:smart00702 152 VTrGSRWAITGWIR 165
2OG-FeII_Oxy_3 pfam13640
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
298-391 1.59e-24

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


Pssm-ID: 433371  Cd Length: 94  Bit Score: 96.68  E-value: 1.59e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32129514   298 AMVACYpGNGTGYVRHVDN----PNGDGRCVTCIYYLNkDWDAKvSGGILRIFPEGKAQfaDIEPKFDRLLFFWSDRRNP 373
Cdd:pfam13640   1 LQLARY-GDGGFYKPHLDFfegaEGGGQRRLTVVLYLN-DWEEE-EGGELVLYDGDGVE--DIKPKKGRLVLFPSSELSL 75
                          90
                  ....*....|....*....
gi 32129514   374 HEVQPAYA-TRYAITVWYF 391
Cdd:pfam13640  76 HEVLPVTGgERWSITGWFR 94
zf-MYND pfam01753
MYND finger;
21-58 2.74e-12

MYND finger;


Pssm-ID: 426410  Cd Length: 39  Bit Score: 60.89  E-value: 2.74e-12
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 32129514    21 CELCGKM-ENLLRCSRCRSSFYCCKEHQRQDWKKHKLVC 58
Cdd:pfam01753   1 CAVCGKEaLKLLRCSRCKSVYYCSKECQKADWPYHKKEC 39
EGL9 COG3751
Proline 4-hydroxylase (includes Rps23 Pro-64 3,4-dihydroxylase Tpa1), contains SM-20 domain ...
283-391 7.49e-10

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: 226274  Cd Length: 252  Bit Score: 58.98  E-value: 7.49e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32129514 283 CNGKLGSYKIngrtKAMVACYPgNGTGYVRHVDNPNG-DGRCVTCIYYLNKDWDAKvSGGILRIFPEGKAQ------FAD 355
Cdd:COG3751 127 LLGILDVSEV----EGQITVYN-PGCFLLKHDDNGRDkDIRLATYVYYLTREWKPE-YGGELRLFHSLQKNntaadsFKT 200
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 32129514 356 IEPKFDRLLFFWSDRRN-PHEVQPAYA--TRYAITVWYF 391
Cdd:COG3751 201 IAPVFNSLVFFKSRPSHsVHSVEEPYAaaDRLSVTGWFR 239
2OG-FeII_Oxy_4 pfam13661
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
300-390 1.46e-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: 1.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32129514   300 VACYPgNGTGYVRHVDNpnGDGRCVTCIYYLNKDWDAKvSGGILRIFP-EGKAQFAD----IEPKFDRLLFFwsdRRNP- 373
Cdd:pfam13661   3 CSRYE-KGDFLLCHDDV--IEGRRIAFILYLVENWKPD-DGGALDLYDtDGHGQPADitksIVPTWNKLVFF---EVSPg 75
                          90       100
                  ....*....|....*....|..
gi 32129514   374 ---HEVQPAYA--TRYAITVWY 390
Cdd:pfam13661  76 hsfHQVAEVVAekPRLSISGWF 97
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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