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Conserved domains on  [gi|7019335|ref|NP_037411|]
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myelin regulatory factor isoform 1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MRF_C2 pfam13888
Myelin gene regulatory factor C-terminal domain 2; This domain is found further downstream of ...
 976-1110 4.41e-50

Myelin gene regulatory factor C-terminal domain 2; This domain is found further downstream of Peptidase_S74, pfam13884, and MRF_C1, pfam13887. The function is not known.


:

Pssm-ID: 464020  Cd Length: 139  Bit Score: 173.30  E-value: 4.41e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019335     976 LTSIQVLENSMSITSQYCAPGDACRPGNFTYHIPVSSGTPLHLSLTLQMNSSSPVSVVLCSLrSKEEPCEEGSLPQSLHT 1055
Cdd:pfam13888    1 LSSIQILETNQEIDSRYCSERLSCRSGNYSYFIPVSKYTPVNVKLTLEINSTESLVVFLCGS-TSGNLCPDSKSSEDSLS 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019335    1056 HQ-DTQG--TSHRWPITILSFREFTYHFRVALLGQANCSSEALAQPA--TDYHFHFYRLC 1110
Cdd:pfam13888   80 DQtDTQGkgTQHLWSLPVASFQDSTYHFRVAVPGEADCSTDPNQAGGffTDYYFYFYRLC 139
NDT80_PhoG pfam05224
NDT80 / PhoG like DNA-binding family; This family includes the DNA-binding region of NDT80 as ...
 384-531 1.03e-38

NDT80 / PhoG like DNA-binding family; This family includes the DNA-binding region of NDT80 as well as PhoG and its homologs. The family contains VIB-1. VIB-1 is thought to be a regulator of conidiation in Neurospora crassa and shares a region of similarity to PHOG, a possible phosphate nonrepressible acid phosphatase in Aspergillus nidulans. It has been found that vib-1 is not the structural gene for nonrepressible acid phosphatase, but rather may regulate nonrepressible acid phosphatase activity.


:

Pssm-ID: 398753  Cd Length: 180  Bit Score: 142.57  E-value: 1.03e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019335     384 AFVCQKKNHFQVTVYIGMLGE--PKYVK--------TPEGLKPLDCFYLKLHGVKLEALNQSINIEQ-SQSDRSKRPFNP 452
Cdd:pfam05224    1 EWTCYRRNYFQVTASFTLPGFspPTFVKhvfttlqsGSGERVPIKYFALKISATKNSADNSPIELVQhTAKRDKGPQFAP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019335     453 VTVNLPP----------------------EQVTKVTVGRLHFSETTANNMRKKGKpnpdQRYFMLVVALQAHAQNQNYT- 509
Cdd:pfam05224   81 VIVPLVPgplpphqlireasnvrnnskmdEIKTVVTVERLQFKSATANNGRRKGL----QQYFVLVVKLGAIHTLSDGTk 156

                          170       180
                   ....*....|....*....|....
gi 7019335     510 --LAAQISERIIVRASNPGQFESD 531
Cdd:pfam05224  157 icLAELVSPPIIVRGRSPGNYESR 180
Peptidase_S74_CIMCD cd10144
Peptidase S74 family, C-terminal intramolecular chaperone domain of Escherichia coli phage K1F ...
 578-696 1.62e-30

Peptidase S74 family, C-terminal intramolecular chaperone domain of Escherichia coli phage K1F endosialidase and related proteins; This peptidase S74 family includes C-terminal intramolecular chaperone domain (CIMCD) of Escherichia coli phage K1F endosialidase, Bacillus phage GA-1 neck appendage protein, and Bacteriophage T5 L-shaped tail fibre. This domain acts as a molecular chaperone; during virus particle assembly, the CIMCD of phage tailspike proteins induces the homo-trimerization of phage tailspike proteins by chaperoning the formation of a triple beta-helix. Homo-trimeric phage tailspike proteins are then auto-cleaved by the CIMCD domain. This family also includes the peptidase S74 Intramolecular Chaperone Auto-processing (ICA) domain of mammalian Myrf. The ICA domain drives the homo-oligomerization of Myrf in the endoplasmic reticulum (ER) membrane. The homo-oligomeric Myrf is proteolyzed by the ICA domain, releasing its N-terminal fragments from the ER membrane.


:

Pssm-ID: 381748 [Multi-domain]  Cd Length: 113  Bit Score: 116.27  E-value: 1.62e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019335   578 SDLRAKEHVQEVDTtEQLKRISRMRLVHYRYKpEFAASAGIEATaPETGVIAQEVKEILPEAVKDTGDMVFangKTIENF 657
Cdd:cd10144    1 SDARLKTEIREIDD-AELDAWKKVRFVQYKWK-EAVAEKGDDAR-LHFGVIAQEVIAAFEDAGLDAGKYGI---LCYDEW 74

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 7019335   658 LVVNKERIFMENVGAVKELCKLTDNLETRIDELERWSHK 696
Cdd:cd10144   75 DAVTDEVITMENVGIEAGERYGTRYDELLIFEAAAQRRR 113
 
Name Accession Description Interval E-value
MRF_C2 pfam13888
Myelin gene regulatory factor C-terminal domain 2; This domain is found further downstream of ...
 976-1110 4.41e-50

Myelin gene regulatory factor C-terminal domain 2; This domain is found further downstream of Peptidase_S74, pfam13884, and MRF_C1, pfam13887. The function is not known.


Pssm-ID: 464020  Cd Length: 139  Bit Score: 173.30  E-value: 4.41e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019335     976 LTSIQVLENSMSITSQYCAPGDACRPGNFTYHIPVSSGTPLHLSLTLQMNSSSPVSVVLCSLrSKEEPCEEGSLPQSLHT 1055
Cdd:pfam13888    1 LSSIQILETNQEIDSRYCSERLSCRSGNYSYFIPVSKYTPVNVKLTLEINSTESLVVFLCGS-TSGNLCPDSKSSEDSLS 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019335    1056 HQ-DTQG--TSHRWPITILSFREFTYHFRVALLGQANCSSEALAQPA--TDYHFHFYRLC 1110
Cdd:pfam13888   80 DQtDTQGkgTQHLWSLPVASFQDSTYHFRVAVPGEADCSTDPNQAGGffTDYYFYFYRLC 139
NDT80_PhoG pfam05224
NDT80 / PhoG like DNA-binding family; This family includes the DNA-binding region of NDT80 as ...
 384-531 1.03e-38

NDT80 / PhoG like DNA-binding family; This family includes the DNA-binding region of NDT80 as well as PhoG and its homologs. The family contains VIB-1. VIB-1 is thought to be a regulator of conidiation in Neurospora crassa and shares a region of similarity to PHOG, a possible phosphate nonrepressible acid phosphatase in Aspergillus nidulans. It has been found that vib-1 is not the structural gene for nonrepressible acid phosphatase, but rather may regulate nonrepressible acid phosphatase activity.


Pssm-ID: 398753  Cd Length: 180  Bit Score: 142.57  E-value: 1.03e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019335     384 AFVCQKKNHFQVTVYIGMLGE--PKYVK--------TPEGLKPLDCFYLKLHGVKLEALNQSINIEQ-SQSDRSKRPFNP 452
Cdd:pfam05224    1 EWTCYRRNYFQVTASFTLPGFspPTFVKhvfttlqsGSGERVPIKYFALKISATKNSADNSPIELVQhTAKRDKGPQFAP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019335     453 VTVNLPP----------------------EQVTKVTVGRLHFSETTANNMRKKGKpnpdQRYFMLVVALQAHAQNQNYT- 509
Cdd:pfam05224   81 VIVPLVPgplpphqlireasnvrnnskmdEIKTVVTVERLQFKSATANNGRRKGL----QQYFVLVVKLGAIHTLSDGTk 156

                          170       180
                   ....*....|....*....|....
gi 7019335     510 --LAAQISERIIVRASNPGQFESD 531
Cdd:pfam05224  157 icLAELVSPPIIVRGRSPGNYESR 180
Peptidase_S74_CIMCD cd10144
Peptidase S74 family, C-terminal intramolecular chaperone domain of Escherichia coli phage K1F ...
 578-696 1.62e-30

Peptidase S74 family, C-terminal intramolecular chaperone domain of Escherichia coli phage K1F endosialidase and related proteins; This peptidase S74 family includes C-terminal intramolecular chaperone domain (CIMCD) of Escherichia coli phage K1F endosialidase, Bacillus phage GA-1 neck appendage protein, and Bacteriophage T5 L-shaped tail fibre. This domain acts as a molecular chaperone; during virus particle assembly, the CIMCD of phage tailspike proteins induces the homo-trimerization of phage tailspike proteins by chaperoning the formation of a triple beta-helix. Homo-trimeric phage tailspike proteins are then auto-cleaved by the CIMCD domain. This family also includes the peptidase S74 Intramolecular Chaperone Auto-processing (ICA) domain of mammalian Myrf. The ICA domain drives the homo-oligomerization of Myrf in the endoplasmic reticulum (ER) membrane. The homo-oligomeric Myrf is proteolyzed by the ICA domain, releasing its N-terminal fragments from the ER membrane.


Pssm-ID: 381748 [Multi-domain]  Cd Length: 113  Bit Score: 116.27  E-value: 1.62e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019335   578 SDLRAKEHVQEVDTtEQLKRISRMRLVHYRYKpEFAASAGIEATaPETGVIAQEVKEILPEAVKDTGDMVFangKTIENF 657
Cdd:cd10144    1 SDARLKTEIREIDD-AELDAWKKVRFVQYKWK-EAVAEKGDDAR-LHFGVIAQEVIAAFEDAGLDAGKYGI---LCYDEW 74

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 7019335   658 LVVNKERIFMENVGAVKELCKLTDNLETRIDELERWSHK 696
Cdd:cd10144   75 DAVTDEVITMENVGIEAGERYGTRYDELLIFEAAAQRRR 113
MYRF_ICA pfam13887
Myelin regulatory factor ICA domain; This domain corresponds to the Intramolecular Chaperone ...
 658-693 3.07e-19

Myelin regulatory factor ICA domain; This domain corresponds to the Intramolecular Chaperone Auto-processing (ICA) domain of myelin regulatory factor (Myrf) located at its C-terminal and belongs to the Peptidase S74 family. It forms a homo-trimer and carries out the auto-cleavage of Myrf releasing the Myrf N-terminal homo-trimer from the ER membrane. This allows its entry to the nucleus to function as a homo-trimer transcription factor.


Pssm-ID: 464019  Cd Length: 36  Bit Score: 81.62  E-value: 3.07e-19
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 7019335     658 LVVNKERIFMENVGAVKELCKLTDNLETRIDELERW 693
Cdd:pfam13887    1 LVVNKDRIFMENVGAVQELCKLTDNLETRIDELEAW 36
 
Name Accession Description Interval E-value
MRF_C2 pfam13888
Myelin gene regulatory factor C-terminal domain 2; This domain is found further downstream of ...
 976-1110 4.41e-50

Myelin gene regulatory factor C-terminal domain 2; This domain is found further downstream of Peptidase_S74, pfam13884, and MRF_C1, pfam13887. The function is not known.


Pssm-ID: 464020  Cd Length: 139  Bit Score: 173.30  E-value: 4.41e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019335     976 LTSIQVLENSMSITSQYCAPGDACRPGNFTYHIPVSSGTPLHLSLTLQMNSSSPVSVVLCSLrSKEEPCEEGSLPQSLHT 1055
Cdd:pfam13888    1 LSSIQILETNQEIDSRYCSERLSCRSGNYSYFIPVSKYTPVNVKLTLEINSTESLVVFLCGS-TSGNLCPDSKSSEDSLS 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019335    1056 HQ-DTQG--TSHRWPITILSFREFTYHFRVALLGQANCSSEALAQPA--TDYHFHFYRLC 1110
Cdd:pfam13888   80 DQtDTQGkgTQHLWSLPVASFQDSTYHFRVAVPGEADCSTDPNQAGGffTDYYFYFYRLC 139
NDT80_PhoG pfam05224
NDT80 / PhoG like DNA-binding family; This family includes the DNA-binding region of NDT80 as ...
 384-531 1.03e-38

NDT80 / PhoG like DNA-binding family; This family includes the DNA-binding region of NDT80 as well as PhoG and its homologs. The family contains VIB-1. VIB-1 is thought to be a regulator of conidiation in Neurospora crassa and shares a region of similarity to PHOG, a possible phosphate nonrepressible acid phosphatase in Aspergillus nidulans. It has been found that vib-1 is not the structural gene for nonrepressible acid phosphatase, but rather may regulate nonrepressible acid phosphatase activity.


Pssm-ID: 398753  Cd Length: 180  Bit Score: 142.57  E-value: 1.03e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019335     384 AFVCQKKNHFQVTVYIGMLGE--PKYVK--------TPEGLKPLDCFYLKLHGVKLEALNQSINIEQ-SQSDRSKRPFNP 452
Cdd:pfam05224    1 EWTCYRRNYFQVTASFTLPGFspPTFVKhvfttlqsGSGERVPIKYFALKISATKNSADNSPIELVQhTAKRDKGPQFAP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019335     453 VTVNLPP----------------------EQVTKVTVGRLHFSETTANNMRKKGKpnpdQRYFMLVVALQAHAQNQNYT- 509
Cdd:pfam05224   81 VIVPLVPgplpphqlireasnvrnnskmdEIKTVVTVERLQFKSATANNGRRKGL----QQYFVLVVKLGAIHTLSDGTk 156

                          170       180
                   ....*....|....*....|....
gi 7019335     510 --LAAQISERIIVRASNPGQFESD 531
Cdd:pfam05224  157 icLAELVSPPIIVRGRSPGNYESR 180
Peptidase_S74_CIMCD cd10144
Peptidase S74 family, C-terminal intramolecular chaperone domain of Escherichia coli phage K1F ...
 578-696 1.62e-30

Peptidase S74 family, C-terminal intramolecular chaperone domain of Escherichia coli phage K1F endosialidase and related proteins; This peptidase S74 family includes C-terminal intramolecular chaperone domain (CIMCD) of Escherichia coli phage K1F endosialidase, Bacillus phage GA-1 neck appendage protein, and Bacteriophage T5 L-shaped tail fibre. This domain acts as a molecular chaperone; during virus particle assembly, the CIMCD of phage tailspike proteins induces the homo-trimerization of phage tailspike proteins by chaperoning the formation of a triple beta-helix. Homo-trimeric phage tailspike proteins are then auto-cleaved by the CIMCD domain. This family also includes the peptidase S74 Intramolecular Chaperone Auto-processing (ICA) domain of mammalian Myrf. The ICA domain drives the homo-oligomerization of Myrf in the endoplasmic reticulum (ER) membrane. The homo-oligomeric Myrf is proteolyzed by the ICA domain, releasing its N-terminal fragments from the ER membrane.


Pssm-ID: 381748 [Multi-domain]  Cd Length: 113  Bit Score: 116.27  E-value: 1.62e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7019335   578 SDLRAKEHVQEVDTtEQLKRISRMRLVHYRYKpEFAASAGIEATaPETGVIAQEVKEILPEAVKDTGDMVFangKTIENF 657
Cdd:cd10144    1 SDARLKTEIREIDD-AELDAWKKVRFVQYKWK-EAVAEKGDDAR-LHFGVIAQEVIAAFEDAGLDAGKYGI---LCYDEW 74

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 7019335   658 LVVNKERIFMENVGAVKELCKLTDNLETRIDELERWSHK 696
Cdd:cd10144   75 DAVTDEVITMENVGIEAGERYGTRYDELLIFEAAAQRRR 113
MYRF_ICA pfam13887
Myelin regulatory factor ICA domain; This domain corresponds to the Intramolecular Chaperone ...
 658-693 3.07e-19

Myelin regulatory factor ICA domain; This domain corresponds to the Intramolecular Chaperone Auto-processing (ICA) domain of myelin regulatory factor (Myrf) located at its C-terminal and belongs to the Peptidase S74 family. It forms a homo-trimer and carries out the auto-cleavage of Myrf releasing the Myrf N-terminal homo-trimer from the ER membrane. This allows its entry to the nucleus to function as a homo-trimer transcription factor.


Pssm-ID: 464019  Cd Length: 36  Bit Score: 81.62  E-value: 3.07e-19
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 7019335     658 LVVNKERIFMENVGAVKELCKLTDNLETRIDELERW 693
Cdd:pfam13887    1 LVVNKDRIFMENVGAVQELCKLTDNLETRIDELEAW 36
Peptidase_S74 pfam13884
Chaperone of endosialidase; This is the very C-terminal, chaperone, domain of the ...
 578-638 1.12e-13

Chaperone of endosialidase; This is the very C-terminal, chaperone, domain of the bacteriophage protein endosialidase. It releases itself, via the serine-lysine dyad at the N-terminus, from the remainder of the end-tail-spike. Cleavage occurs after the threonine which is the final residue of the End-tail-spike family, pfam12219. The endosialidase protein forms homotrimeric molecules in bacteriophages. The catalytic dyad allows this portion of the molecule to be cleaved from the more N-terminal region such that the latter can fold and bind to polysialic acid in the bacterial outer envelope.


Pssm-ID: 404724  Cd Length: 56  Bit Score: 66.50  E-value: 1.12e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7019335     578 SDLRAKEHVQEVDTTEqLKRISRMRLVHYRYKPEfaasAGIEATAPETGVIAQEVKEILPE 638
Cdd:pfam13884    1 SDRRLKTNIKPIDENA-LDKIEQLEPVSYDYKDE----KGEDGARRHIGVIAQEVEEVFPE 56
 
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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