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Conserved domains on  [gi|1786332056|ref|NP_001364189|]
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egl nine homolog 1 isoform 2 [Homo sapiens]

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 ...
220-380 3.77e-33

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: 121.73  E-value: 3.77e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786332056  220 QQIGDEVRALHDTGKFTDGQlvsQKSDSSKDIRGDKITWIEGkEPGCETIGLLMSSMDDLIRHCNGKLGSykingRTKAM 299
Cdd:smart00702   6 QKLLEEAEPLGWRGEVTRGI---GNPNETSQYRQSNGTWLEL-LERDLVIERIRQRLADFLGLLAGLPLS-----AEDAQ 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786332056  300 VACYPGnGTGYVRHVDNPNGDGRCVTCIYYLNKDwdakVSGGILRIFPEGKAQFADIEPKFDRLLFFWS-DRRNPHEVQP 378
Cdd:smart00702  77 VARYGP-GGHYGPHVDNFLYGDRIATFILYLNDV----EEGGELVFPGLRLMVVATVKPKKGDLLFFPSgHGRSLHGVCP 151

                   ..
gi 1786332056  379 AY 380
Cdd:smart00702 152 VT 153
zf-MYND pfam01753
MYND finger;
21-58 3.33e-12

MYND finger;


:

Pssm-ID: 460312  Cd Length: 39  Bit Score: 60.51  E-value: 3.33e-12
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1786332056  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 ...
220-380 3.77e-33

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: 121.73  E-value: 3.77e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786332056  220 QQIGDEVRALHDTGKFTDGQlvsQKSDSSKDIRGDKITWIEGkEPGCETIGLLMSSMDDLIRHCNGKLGSykingRTKAM 299
Cdd:smart00702   6 QKLLEEAEPLGWRGEVTRGI---GNPNETSQYRQSNGTWLEL-LERDLVIERIRQRLADFLGLLAGLPLS-----AEDAQ 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786332056  300 VACYPGnGTGYVRHVDNPNGDGRCVTCIYYLNKDwdakVSGGILRIFPEGKAQFADIEPKFDRLLFFWS-DRRNPHEVQP 378
Cdd:smart00702  77 VARYGP-GGHYGPHVDNFLYGDRIATFILYLNDV----EEGGELVFPGLRLMVVATVKPKKGDLLFFPSgHGRSLHGVCP 151

                   ..
gi 1786332056  379 AY 380
Cdd:smart00702 152 VT 153
EGL9 COG3751
Proline 4-hydroxylase (includes Rps23 Pro-64 3,4-dihydroxylase Tpa1), contains SM-20 domain ...
198-383 1.07e-31

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: 118.51  E-value: 1.07e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786332056 198 IVPCMNKHGICVVDDFLGKETGQQIGDEVRALHDTGKFTDGQlVSQKSDSS--KDIRGDKITWIEGKEPGcETIGLLMSS 275
Cdd:COG3751     3 LADALAAQGYVVIDDFLPPELAEALLAELPALDEAGAFKPAG-IGRGLDHQvnEWIRRDSILWLDEKLAS-AAQARYLAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786332056 276 MDDLIRHCNGK--LGSYKINGrtkaMVACYPgNGTGYVRHVD-NPNGDGRCVTCIYYLNKDWDAKvSGGILRIFPE-GKA 351
Cdd:COG3751    81 LEELREALNSPlfLGLFEYEG----HFARYP-PGGFYKRHLDaFRGDLNRRLSLVLYLNPDWQPE-WGGELELYDDdGSE 154
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1786332056 352 QFADIEPKFDRLLFFWSDRRnPHEVQPAYATR 383
Cdd:COG3751   155 EEVTVAPRFNRLVLFLSEEF-PHEVLPVGRER 185
2OG-FeII_Oxy_3 pfam13640
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
298-381 3.83e-20

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: 84.35  E-value: 3.83e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786332056 298 AMVACYpGNGTGYVRHVDN----PNGDGRCVTCIYYLNkDWDAKvSGGILRIFPEGKAQfaDIEPKFDRLLFFWSDRRNP 373
Cdd:pfam13640   1 LQLARY-GDGGFYKPHLDFfegaEGGGQRRLTVVLYLN-DWEEE-EGGELVLYDGDGVE--DIKPKKGRLVLFPSSELSL 75

                  ....*...
gi 1786332056 374 HEVQPAYA 381
Cdd:pfam13640  76 HEVLPVTG 83
zf-MYND pfam01753
MYND finger;
21-58 3.33e-12

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 60.51  E-value: 3.33e-12
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1786332056  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 ...
220-380 3.77e-33

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: 121.73  E-value: 3.77e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786332056  220 QQIGDEVRALHDTGKFTDGQlvsQKSDSSKDIRGDKITWIEGkEPGCETIGLLMSSMDDLIRHCNGKLGSykingRTKAM 299
Cdd:smart00702   6 QKLLEEAEPLGWRGEVTRGI---GNPNETSQYRQSNGTWLEL-LERDLVIERIRQRLADFLGLLAGLPLS-----AEDAQ 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786332056  300 VACYPGnGTGYVRHVDNPNGDGRCVTCIYYLNKDwdakVSGGILRIFPEGKAQFADIEPKFDRLLFFWS-DRRNPHEVQP 378
Cdd:smart00702  77 VARYGP-GGHYGPHVDNFLYGDRIATFILYLNDV----EEGGELVFPGLRLMVVATVKPKKGDLLFFPSgHGRSLHGVCP 151

                   ..
gi 1786332056  379 AY 380
Cdd:smart00702 152 VT 153
EGL9 COG3751
Proline 4-hydroxylase (includes Rps23 Pro-64 3,4-dihydroxylase Tpa1), contains SM-20 domain ...
198-383 1.07e-31

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: 118.51  E-value: 1.07e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786332056 198 IVPCMNKHGICVVDDFLGKETGQQIGDEVRALHDTGKFTDGQlVSQKSDSS--KDIRGDKITWIEGKEPGcETIGLLMSS 275
Cdd:COG3751     3 LADALAAQGYVVIDDFLPPELAEALLAELPALDEAGAFKPAG-IGRGLDHQvnEWIRRDSILWLDEKLAS-AAQARYLAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786332056 276 MDDLIRHCNGK--LGSYKINGrtkaMVACYPgNGTGYVRHVD-NPNGDGRCVTCIYYLNKDWDAKvSGGILRIFPE-GKA 351
Cdd:COG3751    81 LEELREALNSPlfLGLFEYEG----HFARYP-PGGFYKRHLDaFRGDLNRRLSLVLYLNPDWQPE-WGGELELYDDdGSE 154
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1786332056 352 QFADIEPKFDRLLFFWSDRRnPHEVQPAYATR 383
Cdd:COG3751   155 EEVTVAPRFNRLVLFLSEEF-PHEVLPVGRER 185
2OG-FeII_Oxy_3 pfam13640
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
298-381 3.83e-20

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: 84.35  E-value: 3.83e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786332056 298 AMVACYpGNGTGYVRHVDN----PNGDGRCVTCIYYLNkDWDAKvSGGILRIFPEGKAQfaDIEPKFDRLLFFWSDRRNP 373
Cdd:pfam13640   1 LQLARY-GDGGFYKPHLDFfegaEGGGQRRLTVVLYLN-DWEEE-EGGELVLYDGDGVE--DIKPKKGRLVLFPSSELSL 75

                  ....*...
gi 1786332056 374 HEVQPAYA 381
Cdd:pfam13640  76 HEVLPVTG 83
zf-MYND pfam01753
MYND finger;
21-58 3.33e-12

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 60.51  E-value: 3.33e-12
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1786332056  21 CELCGKM-ENLLRCSRCRSSFYCCKEHQRQDWKKHKLVC 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 ...
300-383 7.73e-07

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: 46.96  E-value: 7.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786332056 300 VACYPgNGTGYVRHVDNpnGDGRCVTCIYYLNKDWDAKvSGGILRIFP-EGKAQFAD----IEPKFDRLLFFwsdRRNP- 373
Cdd:pfam13661   3 CSRYE-KGDFLLCHDDV--IEGRRIAFILYLVENWKPD-DGGALDLYDtDGHGQPADitksIVPTWNKLVFF---EVSPg 75
                          90
                  ....*....|...
gi 1786332056 374 ---HEVQPAYATR 383
Cdd:pfam13661  76 hsfHQVAEVVAEK 88
 
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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