NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1207109956|ref|XP_021335268|]
View 

egl nine homolog 1b isoform X1 [Danio rerio]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
EGL9 COG3751
Proline 4-hydroxylase (includes Rps23 Pro-64 3,4-dihydroxylase Tpa1), contains SM-20 domain ...
133-288 3.78e-22

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: 91.93  E-value: 3.78e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207109956 133 IVPCMNKHGICVVDNFLGNEVGRSILEDVRALYLTGGFTDGQLVSQRSDS-SKDIRGDKITWVEGKEPGCERIAFLmSRM 211
Cdd:COG3751     3 LADALAAQGYVVIDDFLPPELAEALLAELPALDEAGAFKPAGIGRGLDHQvNEWIRRDSILWLDEKLASAAQARYL-AAL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207109956 212 DDLIRHCNGKL----------------GN-YRI--------NGRT------------KEHGGLLRIFPE-GTAQFADIEP 253
Cdd:COG3751    82 EELREALNSPLflglfeyeghfaryppGGfYKRhldafrgdLNRRlslvlylnpdwqPEWGGELELYDDdGSEEEVTVAP 161
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1207109956 254 KFDRLLLFWSDRRnPHEVQPAYATRYAITVWYFDA 288
Cdd:COG3751   162 RFNRLVLFLSEEF-PHEVLPVGRERLSIAGWFRTR 195
zf-MYND pfam01753
MYND finger;
18-55 3.79e-13

MYND finger;


:

Pssm-ID: 460312  Cd Length: 39  Bit Score: 62.82  E-value: 3.79e-13
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1207109956  18 CELCGKM-ENLMKCGRCRSSFYCSKEHQRQDWKKHKRVC 55
Cdd:pfam01753   1 CAVCGKEaLKLLRCSRCKSVYYCSKECQKADWPYHKKEC 39
 
Name Accession Description Interval E-value
EGL9 COG3751
Proline 4-hydroxylase (includes Rps23 Pro-64 3,4-dihydroxylase Tpa1), contains SM-20 domain ...
133-288 3.78e-22

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: 91.93  E-value: 3.78e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207109956 133 IVPCMNKHGICVVDNFLGNEVGRSILEDVRALYLTGGFTDGQLVSQRSDS-SKDIRGDKITWVEGKEPGCERIAFLmSRM 211
Cdd:COG3751     3 LADALAAQGYVVIDDFLPPELAEALLAELPALDEAGAFKPAGIGRGLDHQvNEWIRRDSILWLDEKLASAAQARYL-AAL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207109956 212 DDLIRHCNGKL----------------GN-YRI--------NGRT------------KEHGGLLRIFPE-GTAQFADIEP 253
Cdd:COG3751    82 EELREALNSPLflglfeyeghfaryppGGfYKRhldafrgdLNRRlslvlylnpdwqPEWGGELELYDDdGSEEEVTVAP 161
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1207109956 254 KFDRLLLFWSDRRnPHEVQPAYATRYAITVWYFDA 288
Cdd:COG3751   162 RFNRLVLFLSEEF-PHEVLPVGRERLSIAGWFRTR 195
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
152-286 1.93e-18

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: 80.89  E-value: 1.93e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207109956  152 EVGRSILEDVRALYLTGGFTDGQLVSQRSDsskDIRGDKITWVEGkEPGCERIAFLMSRMDDLIRHCNGKLG-------- 223
Cdd:smart00702   3 AECQKLLEEAEPLGWRGEVTRGIGNPNETS---QYRQSNGTWLEL-LERDLVIERIRQRLADFLGLLAGLPLsaedaqva 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207109956  224 NYRING-------------RT---------KEHGGLLRIFPEGTAQFADIEPKFDRLLLFWS-DRRNPHEVQPAY-ATRY 279
Cdd:smart00702  79 RYGPGGhygphvdnflygdRIatfilylndVEEGGELVFPGLRLMVVATVKPKKGDLLFFPSgHGRSLHGVCPVTrGSRW 158

                   ....*..
gi 1207109956  280 AITVWYF 286
Cdd:smart00702 159 AITGWIR 165
2OG-FeII_Oxy_3 pfam13640
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
228-286 4.68e-14

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: 66.63  E-value: 4.68e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207109956 228 NGRTKEHGGLLRIFPEGTAQfaDIEPKFDRLLLFWSDRRNPHEVQPAYA-TRYAITVWYF 286
Cdd:pfam13640  37 NDWEEEEGGELVLYDGDGVE--DIKPKKGRLVLFPSSELSLHEVLPVTGgERWSITGWFR 94
zf-MYND pfam01753
MYND finger;
18-55 3.79e-13

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 62.82  E-value: 3.79e-13
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1207109956  18 CELCGKM-ENLMKCGRCRSSFYCSKEHQRQDWKKHKRVC 55
Cdd:pfam01753   1 CAVCGKEaLKLLRCSRCKSVYYCSKECQKADWPYHKKEC 39
 
Name Accession Description Interval E-value
EGL9 COG3751
Proline 4-hydroxylase (includes Rps23 Pro-64 3,4-dihydroxylase Tpa1), contains SM-20 domain ...
133-288 3.78e-22

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: 91.93  E-value: 3.78e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207109956 133 IVPCMNKHGICVVDNFLGNEVGRSILEDVRALYLTGGFTDGQLVSQRSDS-SKDIRGDKITWVEGKEPGCERIAFLmSRM 211
Cdd:COG3751     3 LADALAAQGYVVIDDFLPPELAEALLAELPALDEAGAFKPAGIGRGLDHQvNEWIRRDSILWLDEKLASAAQARYL-AAL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207109956 212 DDLIRHCNGKL----------------GN-YRI--------NGRT------------KEHGGLLRIFPE-GTAQFADIEP 253
Cdd:COG3751    82 EELREALNSPLflglfeyeghfaryppGGfYKRhldafrgdLNRRlslvlylnpdwqPEWGGELELYDDdGSEEEVTVAP 161
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1207109956 254 KFDRLLLFWSDRRnPHEVQPAYATRYAITVWYFDA 288
Cdd:COG3751   162 RFNRLVLFLSEEF-PHEVLPVGRERLSIAGWFRTR 195
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
152-286 1.93e-18

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: 80.89  E-value: 1.93e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207109956  152 EVGRSILEDVRALYLTGGFTDGQLVSQRSDsskDIRGDKITWVEGkEPGCERIAFLMSRMDDLIRHCNGKLG-------- 223
Cdd:smart00702   3 AECQKLLEEAEPLGWRGEVTRGIGNPNETS---QYRQSNGTWLEL-LERDLVIERIRQRLADFLGLLAGLPLsaedaqva 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207109956  224 NYRING-------------RT---------KEHGGLLRIFPEGTAQFADIEPKFDRLLLFWS-DRRNPHEVQPAY-ATRY 279
Cdd:smart00702  79 RYGPGGhygphvdnflygdRIatfilylndVEEGGELVFPGLRLMVVATVKPKKGDLLFFPSgHGRSLHGVCPVTrGSRW 158

                   ....*..
gi 1207109956  280 AITVWYF 286
Cdd:smart00702 159 AITGWIR 165
2OG-FeII_Oxy_3 pfam13640
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
228-286 4.68e-14

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: 66.63  E-value: 4.68e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207109956 228 NGRTKEHGGLLRIFPEGTAQfaDIEPKFDRLLLFWSDRRNPHEVQPAYA-TRYAITVWYF 286
Cdd:pfam13640  37 NDWEEEEGGELVLYDGDGVE--DIKPKKGRLVLFPSSELSLHEVLPVTGgERWSITGWFR 94
zf-MYND pfam01753
MYND finger;
18-55 3.79e-13

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 62.82  E-value: 3.79e-13
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1207109956  18 CELCGKM-ENLMKCGRCRSSFYCSKEHQRQDWKKHKRVC 55
Cdd:pfam01753   1 CAVCGKEaLKLLRCSRCKSVYYCSKECQKADWPYHKKEC 39
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH