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Conserved domains on  [gi|1907132210|ref|XP_036017438|]
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myelin regulatory factor isoform X11 [Mus musculus]

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 ...
 889-1023 1.24e-47

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: 166.36  E-value: 1.24e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132210  889 LTSIQLLENSMPITSQYCVPEGACRLGNFTYHIPVSSSTPLHLSLTLQMNSSTPVSVVLCSLTSeEEPCEEGGFLQRFHP 968
Cdd:pfam13888    1 LSSIQILETNQEIDSRYCSERLSCRSGNYSYFIPVSKYTPVNVKLTLEINSTESLVVFLCGSTS-GNLCPDSKSSEDSLS 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132210  969 HQ-DTQG--TSHQWPVTILSFREFTYHFRVTLLGQANCSSEAIVQPA--TDYYFHFYRLC 1023
Cdd:pfam13888   80 DQtDTQGkgTQHLWSLPVASFQDSTYHFRVAVPGEADCSTDPNQAGGffTDYYFYFYRLC 139
NDT80_PhoG pfam05224
NDT80 / PhoG like DNA-binding family; This family includes the DNA-binding region of NDT80 as ...
 305-452 2.12e-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: 141.41  E-value: 2.12e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132210  305 AFVCQKKNHFQVTVYIGMLGE--PKYVK--------TPEGLKPLDCFYLKLHGVKLEALNQSINIEQ-SQSDRSKRPFNP 373
Cdd:pfam05224    1 EWTCYRRNYFQVTASFTLPGFspPTFVKhvfttlqsGSGERVPIKYFALKISATKNSADNSPIELVQhTAKRDKGPQFAP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132210  374 VTVNLPP----------------------EQVTKVTVGRLHFSETTANNMRKKGKpnpdQRYFMLVVALQAHAQNQNYT- 430
Cdd:pfam05224   81 VIVPLVPgplpphqlireasnvrnnskmdEIKTVVTVERLQFKSATANNGRRKGL----QQYFVLVVKLGAIHTLSDGTk 156

                          170       180
                   ....*....|....*....|....
gi 1907132210  431 --LAAQISERIIVRASNPGQFESD 452
Cdd:pfam05224  157 icLAELVSPPIIVRGRSPGNYESR 180
Peptidase_S74_CIMCD cd10144
Peptidase S74 family, C-terminal intramolecular chaperone domain of Escherichia coli phage K1F ...
 499-617 1.70e-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: 1.70e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132210  499 SDLRAKEHVQEVDTtEQLKRISRMRLVHYRYKpEFAASAGIEATaPETGVIAQEVKEILPEAVKDTGDVVFangKTIENF 578
Cdd:cd10144      1 SDARLKTEIREIDD-AELDAWKKVRFVQYKWK-EAVAEKGDDAR-LHFGVIAQEVIAAFEDAGLDAGKYGI---LCYDEW 74

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1907132210  579 LVVNKERIFMENVGAVKELCKLTDNLETRIDELERWSHK 617
Cdd:cd10144     75 DAVTDEVITMENVGIEAGERYGTRYDELLIFEAAAQRRR 113
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 770-976 2.06e-05

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.78  E-value: 2.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132210  770 SPPVSSPATDPALGPTLTPTPSPSSNP------------KHSGPGQMAPLPVTNIRAKSWGISANGISYSKHSKSLEPLA 837
Cdd:PHA03247  2825 AGPLPPPTSAQPTAPPPPPGPPPPSLPlggsvapggdvrRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQ 2904

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132210  838 SPVVPFPGGQSKTKNSPSFNLQSR---ARRGAPQPSPSPAQFTQTQGQLDPAPSLTSIQLlenSMPITSQYCVPEGACRL 914
Cdd:PHA03247  2905 PERPPQPQAPPPPQPQPQPPPPPQpqpPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWL---GALVPGRVAVPRFRVPQ 2981

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907132210  915 GNFTYHIPVSSSTPLHlsltlqmNSSTP-VSVVLCSLTSEEEPCE-EGGFLQRFHPHQDTQGTS 976
Cdd:PHA03247  2982 PAPSREAPASSTPPLT-------GHSLSrVSSWASSLALHEETDPpPVSLKQTLWPPDDTEDSD 3038
 
Name Accession Description Interval E-value
MRF_C2 pfam13888
Myelin gene regulatory factor C-terminal domain 2; This domain is found further downstream of ...
 889-1023 1.24e-47

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: 166.36  E-value: 1.24e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132210  889 LTSIQLLENSMPITSQYCVPEGACRLGNFTYHIPVSSSTPLHLSLTLQMNSSTPVSVVLCSLTSeEEPCEEGGFLQRFHP 968
Cdd:pfam13888    1 LSSIQILETNQEIDSRYCSERLSCRSGNYSYFIPVSKYTPVNVKLTLEINSTESLVVFLCGSTS-GNLCPDSKSSEDSLS 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132210  969 HQ-DTQG--TSHQWPVTILSFREFTYHFRVTLLGQANCSSEAIVQPA--TDYYFHFYRLC 1023
Cdd:pfam13888   80 DQtDTQGkgTQHLWSLPVASFQDSTYHFRVAVPGEADCSTDPNQAGGffTDYYFYFYRLC 139
NDT80_PhoG pfam05224
NDT80 / PhoG like DNA-binding family; This family includes the DNA-binding region of NDT80 as ...
 305-452 2.12e-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: 141.41  E-value: 2.12e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132210  305 AFVCQKKNHFQVTVYIGMLGE--PKYVK--------TPEGLKPLDCFYLKLHGVKLEALNQSINIEQ-SQSDRSKRPFNP 373
Cdd:pfam05224    1 EWTCYRRNYFQVTASFTLPGFspPTFVKhvfttlqsGSGERVPIKYFALKISATKNSADNSPIELVQhTAKRDKGPQFAP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132210  374 VTVNLPP----------------------EQVTKVTVGRLHFSETTANNMRKKGKpnpdQRYFMLVVALQAHAQNQNYT- 430
Cdd:pfam05224   81 VIVPLVPgplpphqlireasnvrnnskmdEIKTVVTVERLQFKSATANNGRRKGL----QQYFVLVVKLGAIHTLSDGTk 156

                          170       180
                   ....*....|....*....|....
gi 1907132210  431 --LAAQISERIIVRASNPGQFESD 452
Cdd:pfam05224  157 icLAELVSPPIIVRGRSPGNYESR 180
Peptidase_S74_CIMCD cd10144
Peptidase S74 family, C-terminal intramolecular chaperone domain of Escherichia coli phage K1F ...
 499-617 1.70e-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: 1.70e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132210  499 SDLRAKEHVQEVDTtEQLKRISRMRLVHYRYKpEFAASAGIEATaPETGVIAQEVKEILPEAVKDTGDVVFangKTIENF 578
Cdd:cd10144      1 SDARLKTEIREIDD-AELDAWKKVRFVQYKWK-EAVAEKGDDAR-LHFGVIAQEVIAAFEDAGLDAGKYGI---LCYDEW 74

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1907132210  579 LVVNKERIFMENVGAVKELCKLTDNLETRIDELERWSHK 617
Cdd:cd10144     75 DAVTDEVITMENVGIEAGERYGTRYDELLIFEAAAQRRR 113
MYRF_ICA pfam13887
Myelin regulatory factor ICA domain; This domain corresponds to the Intramolecular Chaperone ...
 579-614 2.83e-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: 2.83e-19
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1907132210  579 LVVNKERIFMENVGAVKELCKLTDNLETRIDELERW 614
Cdd:pfam13887    1 LVVNKDRIFMENVGAVQELCKLTDNLETRIDELEAW 36
PHA03247 PHA03247
large tegument protein UL36; Provisional
 770-976 2.06e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.78  E-value: 2.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132210  770 SPPVSSPATDPALGPTLTPTPSPSSNP------------KHSGPGQMAPLPVTNIRAKSWGISANGISYSKHSKSLEPLA 837
Cdd:PHA03247  2825 AGPLPPPTSAQPTAPPPPPGPPPPSLPlggsvapggdvrRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQ 2904

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132210  838 SPVVPFPGGQSKTKNSPSFNLQSR---ARRGAPQPSPSPAQFTQTQGQLDPAPSLTSIQLlenSMPITSQYCVPEGACRL 914
Cdd:PHA03247  2905 PERPPQPQAPPPPQPQPQPPPPPQpqpPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWL---GALVPGRVAVPRFRVPQ 2981

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907132210  915 GNFTYHIPVSSSTPLHlsltlqmNSSTP-VSVVLCSLTSEEEPCE-EGGFLQRFHPHQDTQGTS 976
Cdd:PHA03247  2982 PAPSREAPASSTPPLT-------GHSLSrVSSWASSLALHEETDPpPVSLKQTLWPPDDTEDSD 3038
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 716-952 3.74e-04

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 44.52  E-value: 3.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132210  716 SSQSFGTTQLRQSSMTTGLPG-TQPSLLLVTKSASGPALRALDLCSSQPCPIVCCSPPVsspatdpalgptlTPTPSPSS 794
Cdd:pfam05109  430 TSPTLNTTGFAAPNTTTGLPSsTHVPTNLTAPASTGPTVSTADVTSPTPAGTTSGASPV-------------TPSPSPRD 496

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132210  795 N------PKHSGPGQMAPLPVTNIRAKSWGISA---NGIS-----YSKHSKSLEPLASPVVPFPGGQSKTKNSPSFNLQS 860
Cdd:pfam05109  497 NgteskaPDMTSPTSAVTTPTPNATSPTPAVTTptpNATSptlgkTSPTSAVTTPTPNATSPTPAVTTPTPNATIPTLGK 576

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132210  861 RARRGAPQpSPSPAQFTQTQGQLDPAPSLTSIQL-LENSMPITSQycVPEGACRLGNFTYHIPVSSST------PLHLSL 933
Cdd:pfam05109  577 TSPTSAVT-TPTPNATSPTVGETSPQANTTNHTLgGTSSTPVVTS--PPKNATSAVTTGQHNITSSSTssmslrPSSISE 653

                          250
                   ....*....|....*....
gi 1907132210  934 TLQMNSSTPVSVVLCSLTS 952
Cdd:pfam05109  654 TLSPSTSDNSTSHMPLLTS 672
 
Name Accession Description Interval E-value
MRF_C2 pfam13888
Myelin gene regulatory factor C-terminal domain 2; This domain is found further downstream of ...
 889-1023 1.24e-47

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: 166.36  E-value: 1.24e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132210  889 LTSIQLLENSMPITSQYCVPEGACRLGNFTYHIPVSSSTPLHLSLTLQMNSSTPVSVVLCSLTSeEEPCEEGGFLQRFHP 968
Cdd:pfam13888    1 LSSIQILETNQEIDSRYCSERLSCRSGNYSYFIPVSKYTPVNVKLTLEINSTESLVVFLCGSTS-GNLCPDSKSSEDSLS 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132210  969 HQ-DTQG--TSHQWPVTILSFREFTYHFRVTLLGQANCSSEAIVQPA--TDYYFHFYRLC 1023
Cdd:pfam13888   80 DQtDTQGkgTQHLWSLPVASFQDSTYHFRVAVPGEADCSTDPNQAGGffTDYYFYFYRLC 139
NDT80_PhoG pfam05224
NDT80 / PhoG like DNA-binding family; This family includes the DNA-binding region of NDT80 as ...
 305-452 2.12e-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: 141.41  E-value: 2.12e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132210  305 AFVCQKKNHFQVTVYIGMLGE--PKYVK--------TPEGLKPLDCFYLKLHGVKLEALNQSINIEQ-SQSDRSKRPFNP 373
Cdd:pfam05224    1 EWTCYRRNYFQVTASFTLPGFspPTFVKhvfttlqsGSGERVPIKYFALKISATKNSADNSPIELVQhTAKRDKGPQFAP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132210  374 VTVNLPP----------------------EQVTKVTVGRLHFSETTANNMRKKGKpnpdQRYFMLVVALQAHAQNQNYT- 430
Cdd:pfam05224   81 VIVPLVPgplpphqlireasnvrnnskmdEIKTVVTVERLQFKSATANNGRRKGL----QQYFVLVVKLGAIHTLSDGTk 156

                          170       180
                   ....*....|....*....|....
gi 1907132210  431 --LAAQISERIIVRASNPGQFESD 452
Cdd:pfam05224  157 icLAELVSPPIIVRGRSPGNYESR 180
Peptidase_S74_CIMCD cd10144
Peptidase S74 family, C-terminal intramolecular chaperone domain of Escherichia coli phage K1F ...
 499-617 1.70e-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: 1.70e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132210  499 SDLRAKEHVQEVDTtEQLKRISRMRLVHYRYKpEFAASAGIEATaPETGVIAQEVKEILPEAVKDTGDVVFangKTIENF 578
Cdd:cd10144      1 SDARLKTEIREIDD-AELDAWKKVRFVQYKWK-EAVAEKGDDAR-LHFGVIAQEVIAAFEDAGLDAGKYGI---LCYDEW 74

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1907132210  579 LVVNKERIFMENVGAVKELCKLTDNLETRIDELERWSHK 617
Cdd:cd10144     75 DAVTDEVITMENVGIEAGERYGTRYDELLIFEAAAQRRR 113
MYRF_ICA pfam13887
Myelin regulatory factor ICA domain; This domain corresponds to the Intramolecular Chaperone ...
 579-614 2.83e-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: 2.83e-19
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1907132210  579 LVVNKERIFMENVGAVKELCKLTDNLETRIDELERW 614
Cdd:pfam13887    1 LVVNKDRIFMENVGAVQELCKLTDNLETRIDELEAW 36
Peptidase_S74 pfam13884
Chaperone of endosialidase; This is the very C-terminal, chaperone, domain of the ...
 499-559 1.04e-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: 1.04e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907132210  499 SDLRAKEHVQEVDTTEqLKRISRMRLVHYRYKPEfaasAGIEATAPETGVIAQEVKEILPE 559
Cdd:pfam13884    1 SDRRLKTNIKPIDENA-LDKIEQLEPVSYDYKDE----KGEDGARRHIGVIAQEVEEVFPE 56
PHA03247 PHA03247
large tegument protein UL36; Provisional
 770-976 2.06e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.78  E-value: 2.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132210  770 SPPVSSPATDPALGPTLTPTPSPSSNP------------KHSGPGQMAPLPVTNIRAKSWGISANGISYSKHSKSLEPLA 837
Cdd:PHA03247  2825 AGPLPPPTSAQPTAPPPPPGPPPPSLPlggsvapggdvrRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQ 2904

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132210  838 SPVVPFPGGQSKTKNSPSFNLQSR---ARRGAPQPSPSPAQFTQTQGQLDPAPSLTSIQLlenSMPITSQYCVPEGACRL 914
Cdd:PHA03247  2905 PERPPQPQAPPPPQPQPQPPPPPQpqpPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWL---GALVPGRVAVPRFRVPQ 2981

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907132210  915 GNFTYHIPVSSSTPLHlsltlqmNSSTP-VSVVLCSLTSEEEPCE-EGGFLQRFHPHQDTQGTS 976
Cdd:PHA03247  2982 PAPSREAPASSTPPLT-------GHSLSrVSSWASSLALHEETDPpPVSLKQTLWPPDDTEDSD 3038
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 716-952 3.74e-04

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 44.52  E-value: 3.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132210  716 SSQSFGTTQLRQSSMTTGLPG-TQPSLLLVTKSASGPALRALDLCSSQPCPIVCCSPPVsspatdpalgptlTPTPSPSS 794
Cdd:pfam05109  430 TSPTLNTTGFAAPNTTTGLPSsTHVPTNLTAPASTGPTVSTADVTSPTPAGTTSGASPV-------------TPSPSPRD 496

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132210  795 N------PKHSGPGQMAPLPVTNIRAKSWGISA---NGIS-----YSKHSKSLEPLASPVVPFPGGQSKTKNSPSFNLQS 860
Cdd:pfam05109  497 NgteskaPDMTSPTSAVTTPTPNATSPTPAVTTptpNATSptlgkTSPTSAVTTPTPNATSPTPAVTTPTPNATIPTLGK 576

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132210  861 RARRGAPQpSPSPAQFTQTQGQLDPAPSLTSIQL-LENSMPITSQycVPEGACRLGNFTYHIPVSSST------PLHLSL 933
Cdd:pfam05109  577 TSPTSAVT-TPTPNATSPTVGETSPQANTTNHTLgGTSSTPVVTS--PPKNATSAVTTGQHNITSSSTssmslrPSSISE 653

                          250
                   ....*....|....*....
gi 1907132210  934 TLQMNSSTPVSVVLCSLTS 952
Cdd:pfam05109  654 TLSPSTSDNSTSHMPLLTS 672
 
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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