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Conserved domains on  [gi|158303306|ref|NP_444437|]
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egl nine homolog 1 isoform 1 [Mus musculus]

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

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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 ...
192-368 1.76e-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: 1.76e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303306   192 GRETGQQIGDEVRALHDTGKFTDGQlvsQKSDSSKDIRGDQITWIEGkEPGCETIGLLMSSMDDLIRHCSGKLGNyring 271
Cdd:smart00702   1 SPAECQKLLEEAEPLGWRGEVTRGI---GNPNETSQYRQSNGTWLEL-LERDLVIERIRQRLADFLGLLAGLPLS----- 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303306   272 RTKAMVACYPGnGTGYVRHVDNPNGDGRCVTCIYYLNKDwdakVSGGILRIFPEGKAQFADIEPKFDRLLFFWS-DRRNP 350
Cdd:smart00702  72 AEDAQVARYGP-GGHYGPHVDNFLYGDRIATFILYLNDV----EEGGELVFPGLRLMVVATVKPKKGDLLFFPSgHGRSL 146
                          170
                   ....*....|....*....
gi 158303306   351 HEVQPAY-ATRYAITVWYF 368
Cdd:smart00702 147 HGVCPVTrGSRWAITGWIR 165
zf-MYND pfam01753
MYND finger;
21-58 2.17e-12

MYND finger;


:

Pssm-ID: 460312  Cd Length: 39  Bit Score: 60.90  E-value: 2.17e-12
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 158303306   21 CELCGKM-ENLLRCGRCRSSFYCCKEHQRQDWKKHKLVC 58
Cdd:pfam01753   1 CAVCGKEaLKLLRCSRCKSVYYCSKECQKADWPYHKKEC 39
PHA03247 super family cl33720
large tegument protein UL36; Provisional
63-167 1.96e-04

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 1.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303306   63 APRAQPAPAQPRVAPPPGGAPGAARAGGAARRGDSAAASRVPGP---EDAAQARSGPGPAEPGSEDPPLSRSPGPERASL 139
Cdd:PHA03247 2771 PPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPaaaLPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSL 2850
                          90       100
                  ....*....|....*....|....*...
gi 158303306  140 CPAGGgpgeaLSPGGGLRPNGQTKPLPA 167
Cdd:PHA03247 2851 PLGGS-----VAPGGDVRRRPPSRSPAA 2873
 
Name Accession Description Interval E-value
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
192-368 1.76e-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: 1.76e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303306   192 GRETGQQIGDEVRALHDTGKFTDGQlvsQKSDSSKDIRGDQITWIEGkEPGCETIGLLMSSMDDLIRHCSGKLGNyring 271
Cdd:smart00702   1 SPAECQKLLEEAEPLGWRGEVTRGI---GNPNETSQYRQSNGTWLEL-LERDLVIERIRQRLADFLGLLAGLPLS----- 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303306   272 RTKAMVACYPGnGTGYVRHVDNPNGDGRCVTCIYYLNKDwdakVSGGILRIFPEGKAQFADIEPKFDRLLFFWS-DRRNP 350
Cdd:smart00702  72 AEDAQVARYGP-GGHYGPHVDNFLYGDRIATFILYLNDV----EEGGELVFPGLRLMVVATVKPKKGDLLFFPSgHGRSL 146
                          170
                   ....*....|....*....
gi 158303306   351 HEVQPAY-ATRYAITVWYF 368
Cdd:smart00702 147 HGVCPVTrGSRWAITGWIR 165
EGL9 COG3751
Proline 4-hydroxylase (includes Rps23 Pro-64 3,4-dihydroxylase Tpa1), contains SM-20 domain ...
175-370 2.22e-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: 131.22  E-value: 2.22e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303306 175 IVPCMNKHGICVVDDFLGRETGQQIGDEVRALHDTGKFTDGQlVSQKSDSS--KDIRGDQITWIEGKEPGcETIGLLMSS 252
Cdd:COG3751    3 LADALAAQGYVVIDDFLPPELAEALLAELPALDEAGAFKPAG-IGRGLDHQvnEWIRRDSILWLDEKLAS-AAQARYLAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303306 253 MDDLIRHcsgklgnyrINGRT-------KAMVACYPgNGTGYVRHVD-NPNGDGRCVTCIYYLNKDWDAKvSGGILRIFP 324
Cdd:COG3751   81 LEELREA---------LNSPLflglfeyEGHFARYP-PGGFYKRHLDaFRGDLNRRLSLVLYLNPDWQPE-WGGELELYD 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 158303306 325 E-GKAQFADIEPKFDRLLFFWSDRRnPHEVQPAYATRYAITVWYFDA 370
Cdd:COG3751  150 DdGSEEEVTVAPRFNRLVLFLSEEF-PHEVLPVGRERLSIAGWFRTR 195
2OG-FeII_Oxy_3 pfam13640
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
275-368 6.73e-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: 6.73e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303306  275 AMVACYpGNGTGYVRHVDN----PNGDGRCVTCIYYLNkDWDAKvSGGILRIFPEGKAQfaDIEPKFDRLLFFWSDRRNP 350
Cdd:pfam13640   1 LQLARY-GDGGFYKPHLDFfegaEGGGQRRLTVVLYLN-DWEEE-EGGELVLYDGDGVE--DIKPKKGRLVLFPSSELSL 75
                          90
                  ....*....|....*....
gi 158303306  351 HEVQPAYA-TRYAITVWYF 368
Cdd:pfam13640  76 HEVLPVTGgERWSITGWFR 94
zf-MYND pfam01753
MYND finger;
21-58 2.17e-12

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 60.90  E-value: 2.17e-12
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 158303306   21 CELCGKM-ENLLRCGRCRSSFYCCKEHQRQDWKKHKLVC 58
Cdd:pfam01753   1 CAVCGKEaLKLLRCSRCKSVYYCSKECQKADWPYHKKEC 39
PHA03247 PHA03247
large tegument protein UL36; Provisional
63-167 1.96e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 1.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303306   63 APRAQPAPAQPRVAPPPGGAPGAARAGGAARRGDSAAASRVPGP---EDAAQARSGPGPAEPGSEDPPLSRSPGPERASL 139
Cdd:PHA03247 2771 PPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPaaaLPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSL 2850
                          90       100
                  ....*....|....*....|....*...
gi 158303306  140 CPAGGgpgeaLSPGGGLRPNGQTKPLPA 167
Cdd:PHA03247 2851 PLGGS-----VAPGGDVRRRPPSRSPAA 2873
 
Name Accession Description Interval E-value
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
192-368 1.76e-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: 1.76e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303306   192 GRETGQQIGDEVRALHDTGKFTDGQlvsQKSDSSKDIRGDQITWIEGkEPGCETIGLLMSSMDDLIRHCSGKLGNyring 271
Cdd:smart00702   1 SPAECQKLLEEAEPLGWRGEVTRGI---GNPNETSQYRQSNGTWLEL-LERDLVIERIRQRLADFLGLLAGLPLS----- 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303306   272 RTKAMVACYPGnGTGYVRHVDNPNGDGRCVTCIYYLNKDwdakVSGGILRIFPEGKAQFADIEPKFDRLLFFWS-DRRNP 350
Cdd:smart00702  72 AEDAQVARYGP-GGHYGPHVDNFLYGDRIATFILYLNDV----EEGGELVFPGLRLMVVATVKPKKGDLLFFPSgHGRSL 146
                          170
                   ....*....|....*....
gi 158303306   351 HEVQPAY-ATRYAITVWYF 368
Cdd:smart00702 147 HGVCPVTrGSRWAITGWIR 165
EGL9 COG3751
Proline 4-hydroxylase (includes Rps23 Pro-64 3,4-dihydroxylase Tpa1), contains SM-20 domain ...
175-370 2.22e-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: 131.22  E-value: 2.22e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303306 175 IVPCMNKHGICVVDDFLGRETGQQIGDEVRALHDTGKFTDGQlVSQKSDSS--KDIRGDQITWIEGKEPGcETIGLLMSS 252
Cdd:COG3751    3 LADALAAQGYVVIDDFLPPELAEALLAELPALDEAGAFKPAG-IGRGLDHQvnEWIRRDSILWLDEKLAS-AAQARYLAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303306 253 MDDLIRHcsgklgnyrINGRT-------KAMVACYPgNGTGYVRHVD-NPNGDGRCVTCIYYLNKDWDAKvSGGILRIFP 324
Cdd:COG3751   81 LEELREA---------LNSPLflglfeyEGHFARYP-PGGFYKRHLDaFRGDLNRRLSLVLYLNPDWQPE-WGGELELYD 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 158303306 325 E-GKAQFADIEPKFDRLLFFWSDRRnPHEVQPAYATRYAITVWYFDA 370
Cdd:COG3751  150 DdGSEEEVTVAPRFNRLVLFLSEEF-PHEVLPVGRERLSIAGWFRTR 195
2OG-FeII_Oxy_3 pfam13640
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
275-368 6.73e-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: 6.73e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303306  275 AMVACYpGNGTGYVRHVDN----PNGDGRCVTCIYYLNkDWDAKvSGGILRIFPEGKAQfaDIEPKFDRLLFFWSDRRNP 350
Cdd:pfam13640   1 LQLARY-GDGGFYKPHLDFfegaEGGGQRRLTVVLYLN-DWEEE-EGGELVLYDGDGVE--DIKPKKGRLVLFPSSELSL 75
                          90
                  ....*....|....*....
gi 158303306  351 HEVQPAYA-TRYAITVWYF 368
Cdd:pfam13640  76 HEVLPVTGgERWSITGWFR 94
zf-MYND pfam01753
MYND finger;
21-58 2.17e-12

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 60.90  E-value: 2.17e-12
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 158303306   21 CELCGKM-ENLLRCGRCRSSFYCCKEHQRQDWKKHKLVC 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 ...
277-367 1.42e-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: 1.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303306  277 VACYPgNGTGYVRHVDNpnGDGRCVTCIYYLNKDWDAKvSGGILRIFP-EGKAQFAD----IEPKFDRLLFFwsdRRNP- 350
Cdd:pfam13661   3 CSRYE-KGDFLLCHDDV--IEGRRIAFILYLVENWKPD-DGGALDLYDtDGHGQPADitksIVPTWNKLVFF---EVSPg 75
                          90       100
                  ....*....|....*....|..
gi 158303306  351 ---HEVQPAYA--TRYAITVWY 367
Cdd:pfam13661  76 hsfHQVAEVVAekPRLSISGWF 97
PHA03247 PHA03247
large tegument protein UL36; Provisional
63-167 1.96e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 1.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303306   63 APRAQPAPAQPRVAPPPGGAPGAARAGGAARRGDSAAASRVPGP---EDAAQARSGPGPAEPGSEDPPLSRSPGPERASL 139
Cdd:PHA03247 2771 PPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPaaaLPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSL 2850
                          90       100
                  ....*....|....*....|....*...
gi 158303306  140 CPAGGgpgeaLSPGGGLRPNGQTKPLPA 167
Cdd:PHA03247 2851 PLGGS-----VAPGGDVRRRPPSRSPAA 2873
PHA03247 PHA03247
large tegument protein UL36; Provisional
63-160 3.90e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 3.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303306   63 APRAQPAPAQPRVAPPPGGAPGAARAGGAARRGDSAAASrVPGPEDAAQARSGPGPAEPGSEDP--PLSRSPGPERASLC 140
Cdd:PHA03247 2762 TTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPS-PWDPADPPAAVLAPAAALPPAASPagPLPPPTSAQPTAPP 2840
                          90       100
                  ....*....|....*....|
gi 158303306  141 PAGGGPGEALSPGGGLRPNG 160
Cdd:PHA03247 2841 PPPGPPPPSLPLGGSVAPGG 2860
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
62-150 1.78e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.74  E-value: 1.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303306  62 EAPRAQPAPAQPRVAPPPGGAPGAARAGGAARRGDSAAASRVPGPEDAAQARSGPGPAEPGSEDPPLSRSPGPERASLCP 141
Cdd:PRK07764 424 APAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAP 503

                 ....*....
gi 158303306 142 AGGGPGEAL 150
Cdd:PRK07764 504 AGADDAATL 512
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
60-171 8.05e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 38.29  E-value: 8.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158303306  60 GGEAPRAQPAPAQPRV--APPPGGAPGAARAGGAARRGDSAAASRVPGPEDAAQARSGPGPAEPGSEDPPLSR------- 130
Cdd:PRK07003 364 GGGAPGGGVPARVAGAvpAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATAdrgddaa 443
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 158303306 131 ---------SPGPERASLCPAGGGPGEALSPGGGLRPNGQTKPLPALKLA 171
Cdd:PRK07003 444 dgdapvpakANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPA 493
 
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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