NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1370453535|ref|XP_024303502|]
View 

egl nine homolog 1 isoform X1 [Homo sapiens]

Protein Classification

SET and MYND domain-containing protein( domain architecture ID 10484561)

SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) and zinc finger MYND domain-containing protein similar to human N-lysine methyltransferase SMYD2 and histone-lysine N-methyltransferase SMYD3

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 ...
 198-336 6.40e-18

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: 80.76  E-value: 6.40e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453535 198 IVPCMNKHGICVVDDFLGKETGQQIGDEVRALHDTGKFTDGQlVSQKSDSS--KDIRGDKITWIEGKEPGcETIGLLMSS 275
Cdd:COG3751     3 LADALAAQGYVVIDDFLPPELAEALLAELPALDEAGAFKPAG-IGRGLDHQvnEWIRRDSILWLDEKLAS-AAQARYLAA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370453535 276 MDDLIRHCNGK--LGSYKINGrtkaMVACYPgNGTGYVRHVD-NPNGDGRCVTCIYYLNKDWDA 336
Cdd:COG3751    81 LEELREALNSPlfLGLFEYEG----HFARYP-PGGFYKRHLDaFRGDLNRRLSLVLYLNPDWQP 139
zf-MYND pfam01753
MYND finger;
21-58 1.72e-11

MYND finger;


:

Pssm-ID: 460312  Cd Length: 39  Bit Score: 58.20  E-value: 1.72e-11
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1370453535  21 CELCGKM-ENLLRCSRCRSSFYCCKEHQRQDWKKHKLVC 58
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 ...
 198-336 6.40e-18

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: 80.76  E-value: 6.40e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453535 198 IVPCMNKHGICVVDDFLGKETGQQIGDEVRALHDTGKFTDGQlVSQKSDSS--KDIRGDKITWIEGKEPGcETIGLLMSS 275
Cdd:COG3751     3 LADALAAQGYVVIDDFLPPELAEALLAELPALDEAGAFKPAG-IGRGLDHQvnEWIRRDSILWLDEKLAS-AAQARYLAA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370453535 276 MDDLIRHCNGK--LGSYKINGrtkaMVACYPgNGTGYVRHVD-NPNGDGRCVTCIYYLNKDWDA 336
Cdd:COG3751    81 LEELREALNSPlfLGLFEYEG----HFARYP-PGGFYKRHLDaFRGDLNRRLSLVLYLNPDWQP 139
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
 220-333 1.81e-17

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: 78.58  E-value: 1.81e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453535  220 QQIGDEVRALHDTGKFTDGQlvsQKSDSSKDIRGDKITWIEGkEPGCETIGLLMSSMDDLIRHCNGKLGSykingRTKAM 299
Cdd:smart00702   6 QKLLEEAEPLGWRGEVTRGI---GNPNETSQYRQSNGTWLEL-LERDLVIERIRQRLADFLGLLAGLPLS-----AEDAQ 76

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1370453535  300 VACYPGnGTGYVRHVDNPNGDGRCVTCIYYLNKD 333
Cdd:smart00702  77 VARYGP-GGHYGPHVDNFLYGDRIATFILYLNDV 109
zf-MYND pfam01753
MYND finger;
21-58 1.72e-11

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 58.20  E-value: 1.72e-11
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1370453535  21 CELCGKM-ENLLRCSRCRSSFYCCKEHQRQDWKKHKLVC 58
Cdd:pfam01753   1 CAVCGKEaLKLLRCSRCKSVYYCSKECQKADWPYHKKEC 39
2OG-FeII_Oxy_3 pfam13640
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
 298-335 1.39e-05

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: 43.13  E-value: 1.39e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1370453535 298 AMVACYpGNGTGYVRHVDN----PNGDGRCVTCIYYLNkDWD 335
Cdd:pfam13640   1 LQLARY-GDGGFYKPHLDFfegaEGGGQRRLTVVLYLN-DWE 40
 
Name Accession Description Interval E-value
EGL9 COG3751
Proline 4-hydroxylase (includes Rps23 Pro-64 3,4-dihydroxylase Tpa1), contains SM-20 domain ...
 198-336 6.40e-18

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: 80.76  E-value: 6.40e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453535 198 IVPCMNKHGICVVDDFLGKETGQQIGDEVRALHDTGKFTDGQlVSQKSDSS--KDIRGDKITWIEGKEPGcETIGLLMSS 275
Cdd:COG3751     3 LADALAAQGYVVIDDFLPPELAEALLAELPALDEAGAFKPAG-IGRGLDHQvnEWIRRDSILWLDEKLAS-AAQARYLAA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370453535 276 MDDLIRHCNGK--LGSYKINGrtkaMVACYPgNGTGYVRHVD-NPNGDGRCVTCIYYLNKDWDA 336
Cdd:COG3751    81 LEELREALNSPlfLGLFEYEG----HFARYP-PGGFYKRHLDaFRGDLNRRLSLVLYLNPDWQP 139
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
 220-333 1.81e-17

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: 78.58  E-value: 1.81e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453535  220 QQIGDEVRALHDTGKFTDGQlvsQKSDSSKDIRGDKITWIEGkEPGCETIGLLMSSMDDLIRHCNGKLGSykingRTKAM 299
Cdd:smart00702   6 QKLLEEAEPLGWRGEVTRGI---GNPNETSQYRQSNGTWLEL-LERDLVIERIRQRLADFLGLLAGLPLS-----AEDAQ 76

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1370453535  300 VACYPGnGTGYVRHVDNPNGDGRCVTCIYYLNKD 333
Cdd:smart00702  77 VARYGP-GGHYGPHVDNFLYGDRIATFILYLNDV 109
zf-MYND pfam01753
MYND finger;
21-58 1.72e-11

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 58.20  E-value: 1.72e-11
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1370453535  21 CELCGKM-ENLLRCSRCRSSFYCCKEHQRQDWKKHKLVC 58
Cdd:pfam01753   1 CAVCGKEaLKLLRCSRCKSVYYCSKECQKADWPYHKKEC 39
2OG-FeII_Oxy_3 pfam13640
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
 298-335 1.39e-05

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: 43.13  E-value: 1.39e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1370453535 298 AMVACYpGNGTGYVRHVDN----PNGDGRCVTCIYYLNkDWD 335
Cdd:pfam13640   1 LQLARY-GDGGFYKPHLDFfegaEGGGQRRLTVVLYLN-DWE 40
 
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