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Conserved domains on  [gi|807045893|ref|NP_872336|]
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myelin regulatory factor-like protein [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 ...
 781-896 6.31e-53

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: 181.00  E-value: 6.31e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045893  781 DHQYCIQSLQCGSGNYNYNIPVNKHTPTNVKFSLEINTTEPLIVFQCKFTLGNICFHSKRGTKGLEshreiSQEMTQG-- 858
Cdd:pfam13888  14 DSRYCSERLSCRSGNYSYFIPVSKYTPVNVKLTLEINSTESLVVFLCGSTSGNLCPDSKSSEDSLS-----DQTDTQGkg 88

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 807045893  859 YQHIWSLPVAPFSDSMFHFRVAAPDLADCSTDPYFAGI 896
Cdd:pfam13888  89 TQHLWSLPVASFQDSTYHFRVAVPGEADCSTDPNQAGG 126
NDT80_PhoG super family cl04998
NDT80 / PhoG like DNA-binding family; This family includes the DNA-binding region of NDT80 as ...
 257-404 1.41e-34

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.


The actual alignment was detected with superfamily member pfam05224:

Pssm-ID: 398753  Cd Length: 180  Bit Score: 130.24  E-value: 1.41e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045893  257 AFVCQKKNHFQIT--IHIQVWGSPKFVETEM--------GLKPIEMFYLKVFGTKVEATNQIIAIEQSQADRSKKI-FNP 325
Cdd:pfam05224   1 EWTCYRRNYFQVTasFTLPGFSPPTFVKHVFttlqsgsgERVPIKYFALKISATKNSADNSPIELVQHTAKRDKGPqFAP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045893  326 VKIDLLAD----------------------QVTKVTLGRLHFSETTANNMRKKGKpnpdQRYFMLVVGLYAANQD---QF 380
Cdd:pfam05224  81 VIVPLVPGplpphqlireasnvrnnskmdeIKTVVTVERLQFKSATANNGRRKGL----QQYFVLVVKLGAIHTLsdgTK 156

                         170       180
                  ....*....|....*....|....
gi 807045893  381 YLLSAHISERIIVRASNPGQFEND 404
Cdd:pfam05224 157 ICLAELVSPPIIVRGRSPGNYESR 180
Peptidase_S74_CIMCD super family cl16452
Peptidase S74 family, C-terminal intramolecular chaperone domain of Escherichia coli phage K1F ...
 451-552 2.86e-17

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.


The actual alignment was detected with superfamily member cd10144:

Pssm-ID: 418048 [Multi-domain]  Cd Length: 113  Bit Score: 78.52  E-value: 2.86e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045893 451 SDSRAKQNIQEVDTNEqLKRIAQMRIVEYDYKpEFASAMGINTAHQTGMIAQEVQEILPRAVREVGDVTCgngETLENFL 530
Cdd:cd10144    1 SDARLKTEIREIDDAE-LDAWKKVRFVQYKWK-EAVAEKGDDARLHFGVIAQEVIAAFEDAGLDAGKYGI---LCYDEWD 75

                         90       100
                 ....*....|....*....|..
gi 807045893 531 MVDKDQIFMENVGAVKQLCKLT 552
Cdd:cd10144   76 AVTDEVITMENVGIEAGERYGT 97
 
Name Accession Description Interval E-value
MRF_C2 pfam13888
Myelin gene regulatory factor C-terminal domain 2; This domain is found further downstream of ...
 781-896 6.31e-53

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: 181.00  E-value: 6.31e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045893  781 DHQYCIQSLQCGSGNYNYNIPVNKHTPTNVKFSLEINTTEPLIVFQCKFTLGNICFHSKRGTKGLEshreiSQEMTQG-- 858
Cdd:pfam13888  14 DSRYCSERLSCRSGNYSYFIPVSKYTPVNVKLTLEINSTESLVVFLCGSTSGNLCPDSKSSEDSLS-----DQTDTQGkg 88

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 807045893  859 YQHIWSLPVAPFSDSMFHFRVAAPDLADCSTDPYFAGI 896
Cdd:pfam13888  89 TQHLWSLPVASFQDSTYHFRVAVPGEADCSTDPNQAGG 126
NDT80_PhoG pfam05224
NDT80 / PhoG like DNA-binding family; This family includes the DNA-binding region of NDT80 as ...
 257-404 1.41e-34

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: 130.24  E-value: 1.41e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045893  257 AFVCQKKNHFQIT--IHIQVWGSPKFVETEM--------GLKPIEMFYLKVFGTKVEATNQIIAIEQSQADRSKKI-FNP 325
Cdd:pfam05224   1 EWTCYRRNYFQVTasFTLPGFSPPTFVKHVFttlqsgsgERVPIKYFALKISATKNSADNSPIELVQHTAKRDKGPqFAP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045893  326 VKIDLLAD----------------------QVTKVTLGRLHFSETTANNMRKKGKpnpdQRYFMLVVGLYAANQD---QF 380
Cdd:pfam05224  81 VIVPLVPGplpphqlireasnvrnnskmdeIKTVVTVERLQFKSATANNGRRKGL----QQYFVLVVKLGAIHTLsdgTK 156

                         170       180
                  ....*....|....*....|....
gi 807045893  381 YLLSAHISERIIVRASNPGQFEND 404
Cdd:pfam05224 157 ICLAELVSPPIIVRGRSPGNYESR 180
Peptidase_S74_CIMCD cd10144
Peptidase S74 family, C-terminal intramolecular chaperone domain of Escherichia coli phage K1F ...
 451-552 2.86e-17

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: 78.52  E-value: 2.86e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045893 451 SDSRAKQNIQEVDTNEqLKRIAQMRIVEYDYKpEFASAMGINTAHQTGMIAQEVQEILPRAVREVGDVTCgngETLENFL 530
Cdd:cd10144    1 SDARLKTEIREIDDAE-LDAWKKVRFVQYKWK-EAVAEKGDDARLHFGVIAQEVIAAFEDAGLDAGKYGI---LCYDEWD 75

                         90       100
                 ....*....|....*....|..
gi 807045893 531 MVDKDQIFMENVGAVKQLCKLT 552
Cdd:cd10144   76 AVTDEVITMENVGIEAGERYGT 97
Peptidase_S74 pfam13884
Chaperone of endosialidase; This is the very C-terminal, chaperone, domain of the ...
 451-509 1.23e-15

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: 71.89  E-value: 1.23e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 807045893  451 SDSRAKQNIQEVDTNEqLKRIAQMRIVEYDYKPEFAsamGINTAHQTGMIAQEVQEILP 509
Cdd:pfam13884   1 SDRRLKTNIKPIDENA-LDKIEQLEPVSYDYKDEKG---EDGARRHIGVIAQEVEEVFP 55
 
Name Accession Description Interval E-value
MRF_C2 pfam13888
Myelin gene regulatory factor C-terminal domain 2; This domain is found further downstream of ...
 781-896 6.31e-53

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: 181.00  E-value: 6.31e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045893  781 DHQYCIQSLQCGSGNYNYNIPVNKHTPTNVKFSLEINTTEPLIVFQCKFTLGNICFHSKRGTKGLEshreiSQEMTQG-- 858
Cdd:pfam13888  14 DSRYCSERLSCRSGNYSYFIPVSKYTPVNVKLTLEINSTESLVVFLCGSTSGNLCPDSKSSEDSLS-----DQTDTQGkg 88

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 807045893  859 YQHIWSLPVAPFSDSMFHFRVAAPDLADCSTDPYFAGI 896
Cdd:pfam13888  89 TQHLWSLPVASFQDSTYHFRVAVPGEADCSTDPNQAGG 126
NDT80_PhoG pfam05224
NDT80 / PhoG like DNA-binding family; This family includes the DNA-binding region of NDT80 as ...
 257-404 1.41e-34

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: 130.24  E-value: 1.41e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045893  257 AFVCQKKNHFQIT--IHIQVWGSPKFVETEM--------GLKPIEMFYLKVFGTKVEATNQIIAIEQSQADRSKKI-FNP 325
Cdd:pfam05224   1 EWTCYRRNYFQVTasFTLPGFSPPTFVKHVFttlqsgsgERVPIKYFALKISATKNSADNSPIELVQHTAKRDKGPqFAP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045893  326 VKIDLLAD----------------------QVTKVTLGRLHFSETTANNMRKKGKpnpdQRYFMLVVGLYAANQD---QF 380
Cdd:pfam05224  81 VIVPLVPGplpphqlireasnvrnnskmdeIKTVVTVERLQFKSATANNGRRKGL----QQYFVLVVKLGAIHTLsdgTK 156

                         170       180
                  ....*....|....*....|....
gi 807045893  381 YLLSAHISERIIVRASNPGQFEND 404
Cdd:pfam05224 157 ICLAELVSPPIIVRGRSPGNYESR 180
Peptidase_S74_CIMCD cd10144
Peptidase S74 family, C-terminal intramolecular chaperone domain of Escherichia coli phage K1F ...
 451-552 2.86e-17

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: 78.52  E-value: 2.86e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807045893 451 SDSRAKQNIQEVDTNEqLKRIAQMRIVEYDYKpEFASAMGINTAHQTGMIAQEVQEILPRAVREVGDVTCgngETLENFL 530
Cdd:cd10144    1 SDARLKTEIREIDDAE-LDAWKKVRFVQYKWK-EAVAEKGDDARLHFGVIAQEVIAAFEDAGLDAGKYGI---LCYDEWD 75

                         90       100
                 ....*....|....*....|..
gi 807045893 531 MVDKDQIFMENVGAVKQLCKLT 552
Cdd:cd10144   76 AVTDEVITMENVGIEAGERYGT 97
Peptidase_S74 pfam13884
Chaperone of endosialidase; This is the very C-terminal, chaperone, domain of the ...
 451-509 1.23e-15

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: 71.89  E-value: 1.23e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 807045893  451 SDSRAKQNIQEVDTNEqLKRIAQMRIVEYDYKPEFAsamGINTAHQTGMIAQEVQEILP 509
Cdd:pfam13884   1 SDRRLKTNIKPIDENA-LDKIEQLEPVSYDYKDEKG---EDGARRHIGVIAQEVEEVFP 55
MYRF_ICA pfam13887
Myelin regulatory factor ICA domain; This domain corresponds to the Intramolecular Chaperone ...
 530-554 2.37e-10

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: 56.20  E-value: 2.37e-10
                          10        20
                  ....*....|....*....|....*
gi 807045893  530 LMVDKDQIFMENVGAVKQLCKLTNN 554
Cdd:pfam13887   1 LVVNKDRIFMENVGAVQELCKLTDN 25
 
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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