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Conserved domains on  [gi|2280650036|ref|XP_049553507|]
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egl nine homolog 1 [Orcinus orca]

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 ...
233-404 3.26e-37

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: 133.28  E-value: 3.26e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280650036  233 QQIGDEVRALHDTGKFTDGQlvsQKSDSSKDIRGDKITWIEGkEPGCETIGLLMSSMDDLIRHCNGKLGNykingRTKAM 312
Cdd:smart00702   6 QKLLEEAEPLGWRGEVTRGI---GNPNETSQYRQSNGTWLEL-LERDLVIERIRQRLADFLGLLAGLPLS-----AEDAQ 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280650036  313 VACYPGnGTGYVRHVDNPNGDGRCVTCIYYLNKDwdakVSGGILRIFPEGKAQFADIEPRFDRLLFFWS-DRRNPHEVQP 391
Cdd:smart00702  77 VARYGP-GGHYGPHVDNFLYGDRIATFILYLNDV----EEGGELVFPGLRLMVVATVKPKKGDLLFFPSgHGRSLHGVCP 151
                          170
                   ....*....|....
gi 2280650036  392 AY-ATRYAITVWYF 404
Cdd:smart00702 152 VTrGSRWAITGWIR 165
zf-MYND pfam01753
MYND finger;
21-58 4.10e-13

MYND finger;


:

Pssm-ID: 460312  Cd Length: 39  Bit Score: 63.21  E-value: 4.10e-13
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2280650036  21 CELCGKM-ENLLRCSRCRSSFYCSKEHQRQDWKKHKLVC 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 ...
233-404 3.26e-37

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: 133.28  E-value: 3.26e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280650036  233 QQIGDEVRALHDTGKFTDGQlvsQKSDSSKDIRGDKITWIEGkEPGCETIGLLMSSMDDLIRHCNGKLGNykingRTKAM 312
Cdd:smart00702   6 QKLLEEAEPLGWRGEVTRGI---GNPNETSQYRQSNGTWLEL-LERDLVIERIRQRLADFLGLLAGLPLS-----AEDAQ 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280650036  313 VACYPGnGTGYVRHVDNPNGDGRCVTCIYYLNKDwdakVSGGILRIFPEGKAQFADIEPRFDRLLFFWS-DRRNPHEVQP 391
Cdd:smart00702  77 VARYGP-GGHYGPHVDNFLYGDRIATFILYLNDV----EEGGELVFPGLRLMVVATVKPKKGDLLFFPSgHGRSLHGVCP 151
                          170
                   ....*....|....
gi 2280650036  392 AY-ATRYAITVWYF 404
Cdd:smart00702 152 VTrGSRWAITGWIR 165
EGL9 COG3751
Proline 4-hydroxylase (includes Rps23 Pro-64 3,4-dihydroxylase Tpa1), contains SM-20 domain ...
211-406 1.15e-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: 133.15  E-value: 1.15e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280650036 211 IVPCMNKHGICVVDDFLGKETGQQIGDEVRALHDTGKFTDGQlVSQKSDSS--KDIRGDKITWIEGKEPGcETIGLLMSS 288
Cdd:COG3751     3 LADALAAQGYVVIDDFLPPELAEALLAELPALDEAGAFKPAG-IGRGLDHQvnEWIRRDSILWLDEKLAS-AAQARYLAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280650036 289 MDDLIRHCNGK--LGNYKINGrtkaMVACYPgNGTGYVRHVD-NPNGDGRCVTCIYYLNKDWDAKvSGGILRIFPE-GKA 364
Cdd:COG3751    81 LEELREALNSPlfLGLFEYEG----HFARYP-PGGFYKRHLDaFRGDLNRRLSLVLYLNPDWQPE-WGGELELYDDdGSE 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2280650036 365 QFADIEPRFDRLLFFWSDRRnPHEVQPAYATRYAITVWYFDA 406
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 ...
311-404 1.41e-24

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: 97.06  E-value: 1.41e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280650036 311 AMVACYpGNGTGYVRHVDN----PNGDGRCVTCIYYLNkDWDAKvSGGILRIFPEGKAQfaDIEPRFDRLLFFWSDRRNP 386
Cdd:pfam13640   1 LQLARY-GDGGFYKPHLDFfegaEGGGQRRLTVVLYLN-DWEEE-EGGELVLYDGDGVE--DIKPKKGRLVLFPSSELSL 75
                          90
                  ....*....|....*....
gi 2280650036 387 HEVQPAYA-TRYAITVWYF 404
Cdd:pfam13640  76 HEVLPVTGgERWSITGWFR 94
zf-MYND pfam01753
MYND finger;
21-58 4.10e-13

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 63.21  E-value: 4.10e-13
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2280650036  21 CELCGKM-ENLLRCSRCRSSFYCSKEHQRQDWKKHKLVC 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 ...
233-404 3.26e-37

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: 133.28  E-value: 3.26e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280650036  233 QQIGDEVRALHDTGKFTDGQlvsQKSDSSKDIRGDKITWIEGkEPGCETIGLLMSSMDDLIRHCNGKLGNykingRTKAM 312
Cdd:smart00702   6 QKLLEEAEPLGWRGEVTRGI---GNPNETSQYRQSNGTWLEL-LERDLVIERIRQRLADFLGLLAGLPLS-----AEDAQ 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280650036  313 VACYPGnGTGYVRHVDNPNGDGRCVTCIYYLNKDwdakVSGGILRIFPEGKAQFADIEPRFDRLLFFWS-DRRNPHEVQP 391
Cdd:smart00702  77 VARYGP-GGHYGPHVDNFLYGDRIATFILYLNDV----EEGGELVFPGLRLMVVATVKPKKGDLLFFPSgHGRSLHGVCP 151
                          170
                   ....*....|....
gi 2280650036  392 AY-ATRYAITVWYF 404
Cdd:smart00702 152 VTrGSRWAITGWIR 165
EGL9 COG3751
Proline 4-hydroxylase (includes Rps23 Pro-64 3,4-dihydroxylase Tpa1), contains SM-20 domain ...
211-406 1.15e-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: 133.15  E-value: 1.15e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280650036 211 IVPCMNKHGICVVDDFLGKETGQQIGDEVRALHDTGKFTDGQlVSQKSDSS--KDIRGDKITWIEGKEPGcETIGLLMSS 288
Cdd:COG3751     3 LADALAAQGYVVIDDFLPPELAEALLAELPALDEAGAFKPAG-IGRGLDHQvnEWIRRDSILWLDEKLAS-AAQARYLAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280650036 289 MDDLIRHCNGK--LGNYKINGrtkaMVACYPgNGTGYVRHVD-NPNGDGRCVTCIYYLNKDWDAKvSGGILRIFPE-GKA 364
Cdd:COG3751    81 LEELREALNSPlfLGLFEYEG----HFARYP-PGGFYKRHLDaFRGDLNRRLSLVLYLNPDWQPE-WGGELELYDDdGSE 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2280650036 365 QFADIEPRFDRLLFFWSDRRnPHEVQPAYATRYAITVWYFDA 406
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 ...
311-404 1.41e-24

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: 97.06  E-value: 1.41e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280650036 311 AMVACYpGNGTGYVRHVDN----PNGDGRCVTCIYYLNkDWDAKvSGGILRIFPEGKAQfaDIEPRFDRLLFFWSDRRNP 386
Cdd:pfam13640   1 LQLARY-GDGGFYKPHLDFfegaEGGGQRRLTVVLYLN-DWEEE-EGGELVLYDGDGVE--DIKPKKGRLVLFPSSELSL 75
                          90
                  ....*....|....*....
gi 2280650036 387 HEVQPAYA-TRYAITVWYF 404
Cdd:pfam13640  76 HEVLPVTGgERWSITGWFR 94
zf-MYND pfam01753
MYND finger;
21-58 4.10e-13

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 63.21  E-value: 4.10e-13
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2280650036  21 CELCGKM-ENLLRCSRCRSSFYCSKEHQRQDWKKHKLVC 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 ...
313-403 1.35e-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: 52.35  E-value: 1.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2280650036 313 VACYPgNGTGYVRHVDNpnGDGRCVTCIYYLNKDWDAKvSGGILRIFP-EGKAQFAD----IEPRFDRLLFFwsdRRNP- 386
Cdd:pfam13661   3 CSRYE-KGDFLLCHDDV--IEGRRIAFILYLVENWKPD-DGGALDLYDtDGHGQPADitksIVPTWNKLVFF---EVSPg 75
                          90       100
                  ....*....|....*....|..
gi 2280650036 387 ---HEVQPAYA--TRYAITVWY 403
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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