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Conserved domains on  [gi|15240508|ref|NP_199768|]
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peptide-N-glycanase 1 [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
 199-296 1.75e-15

Transglutaminase-like superfamily; This family includes animal transglutaminases and other bacterial proteins of unknown function. Sequence conservation in this superfamily primarily involves three motifs that centre around conserved cysteine, histidine, and aspartate residues that form the catalytic triad in the structurally characterized transglutaminase, the human blood clotting factor XIIIa'. On the basis of the experimentally demonstrated activity of the Methanobacterium phage pseudomurein endoisopeptidase, it is proposed that many, if not all, microbial homologs of the transglutaminases are proteases and that the eukaryotic transglutaminases have evolved from an ancestral protease.


:

Pssm-ID: 376628 [Multi-domain]  Cd Length: 108  Bit Score: 72.82  E-value: 1.75e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240508   199 KTIGQGMGNPLTSELaYGANRVEIYRCTMCP--TTTRFPRYNDPLKLVETKKGRCGEWANCFTLYCRTFGYDSRLIMDFT 276
Cdd:pfam01841   1 KALADRITGGATDPL-EKARAIYDYVRKNITydLPGRSPGDGDAEEFLFTGKGDCEDFASLFVALLRALGIPARYVTGYL 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 15240508   277 D----------HVWTECYSHSLkRWIHLDP 296
Cdd:pfam01841  80 RgpdtvrggdaHAWVEVYLPGY-GWVPVDP 108
Rad4 super family cl44506
Rad4 transglutaminase-like domain;
280-347 2.06e-10

Rad4 transglutaminase-like domain;


The actual alignment was detected with superfamily member pfam03835:

Pssm-ID: 427539 [Multi-domain]  Cd Length: 146  Bit Score: 59.34  E-value: 2.06e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15240508   280 WTECYSHSLKRWIHLDP--CEGVYDKPMLYEKGWNKKLN---YVIAISKDGVC-DVTKRYTKKWHEVLSRRTLT 347
Cdd:pfam03835  39 WVEVFNPETKKWISVDPlvLKTIELKSKFEPRIAEKALNvmtYVVAFDSDGGAkDVTRRYCSTYNAKTRKRRIE 112
Ubl1_cv_Nsp3_N-like super family cl28922
first ubiquitin-like (Ubl) domain located at the N-terminus of coronavirus SARS-CoV ...
 16-63 1.99e-03

first ubiquitin-like (Ubl) domain located at the N-terminus of coronavirus SARS-CoV non-structural protein 3 (Nsp3) and related proteins; This ubiquitin-like (Ubl) domain (Ubl1) is found at the N-terminus of coronavirus Nsp3, a large multi-functional multi-domain protein which is an essential component of the replication/transcription complex (RTC). The functions of Ubl1 in CoVs are related to single-stranded RNA (ssRNA) binding and to interacting with the nucleocapsid (N) protein. SARS-CoV Ubl1 has been shown to bind ssRNA having AUA patterns, and since the 5'-UTR of the SARS-CoV genome has a number of AUA repeats, it may bind there. In mouse hepatitis virus (MHV), this Ubl1 domain binds the cognate N protein. Adjacent to Ubl1 is a Glu-rich acidic region (also referred to as hypervariable region, HVR); Ubl1 together with HVR has been called Nsp3a. Currently, the function of HVR in CoVs is unknown. This model corresponds to one of two Ubl domains in Nsp3; the other is located N-terminal to the papain-like protease (PLpro) and is not represented by this model.


The actual alignment was detected with superfamily member cd16104:

Pssm-ID: 475130  Cd Length: 75  Bit Score: 37.60  E-value: 1.99e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 15240508  16 DVDYNTEDGLEVLRFLIFSLTLVPPEEQKIVAEddNRLVSDESDLASL 63
Cdd:cd16104  15 DVELDTDEPPLVFKAQLFALTGVPPERQKIMVK--GGVLKDDDDLSKL 60
 
Name Accession Description Interval E-value
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
 199-296 1.75e-15

Transglutaminase-like superfamily; This family includes animal transglutaminases and other bacterial proteins of unknown function. Sequence conservation in this superfamily primarily involves three motifs that centre around conserved cysteine, histidine, and aspartate residues that form the catalytic triad in the structurally characterized transglutaminase, the human blood clotting factor XIIIa'. On the basis of the experimentally demonstrated activity of the Methanobacterium phage pseudomurein endoisopeptidase, it is proposed that many, if not all, microbial homologs of the transglutaminases are proteases and that the eukaryotic transglutaminases have evolved from an ancestral protease.


Pssm-ID: 376628 [Multi-domain]  Cd Length: 108  Bit Score: 72.82  E-value: 1.75e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240508   199 KTIGQGMGNPLTSELaYGANRVEIYRCTMCP--TTTRFPRYNDPLKLVETKKGRCGEWANCFTLYCRTFGYDSRLIMDFT 276
Cdd:pfam01841   1 KALADRITGGATDPL-EKARAIYDYVRKNITydLPGRSPGDGDAEEFLFTGKGDCEDFASLFVALLRALGIPARYVTGYL 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 15240508   277 D----------HVWTECYSHSLkRWIHLDP 296
Cdd:pfam01841  80 RgpdtvrggdaHAWVEVYLPGY-GWVPVDP 108
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
 243-297 1.06e-10

Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish covalent links between proteins. A subset of transglutaminase homologues appear to catalyse the reverse reaction, the hydrolysis of peptide bonds. Proteins with this domain are both extracellular and intracellular, and it is likely that the eukaryotic intracellular proteins are involved in signalling events.


Pssm-ID: 214673  Cd Length: 68  Bit Score: 57.78  E-value: 1.06e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15240508    243 LVETKKGRCGEWANCFTLYCRTFGYDSRLIMDF--------------TDHVWTECYSHslKRWIHLDPC 297
Cdd:smart00460   1 LLKTKYGTCGEFAALFVALLRSLGIPARVVSGYlkapdtigglrsiwEAHAWAEVYLE--GGWVPVDPT 67
Rad4 pfam03835
Rad4 transglutaminase-like domain;
280-347 2.06e-10

Rad4 transglutaminase-like domain;


Pssm-ID: 427539 [Multi-domain]  Cd Length: 146  Bit Score: 59.34  E-value: 2.06e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15240508   280 WTECYSHSLKRWIHLDP--CEGVYDKPMLYEKGWNKKLN---YVIAISKDGVC-DVTKRYTKKWHEVLSRRTLT 347
Cdd:pfam03835  39 WVEVFNPETKKWISVDPlvLKTIELKSKFEPRIAEKALNvmtYVVAFDSDGGAkDVTRRYCSTYNAKTRKRRIE 112
rad4 TIGR00605
DNA repair protein rad4; All proteins in this family for which functions are known are ...
 280-349 3.51e-06

DNA repair protein rad4; All proteins in this family for which functions are known are involved in targeting nucleotide excision repair to specific regions of the genome.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273170 [Multi-domain]  Cd Length: 713  Bit Score: 50.26  E-value: 3.51e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15240508   280 WTECYSHSLKRWIHLDPC-EGVYDKPMLYEKGWNKKLNYVIAISKDGVC-DVTKRYTKKWHEVLSRRTLTTE 349
Cdd:TIGR00605 373 WVEVFIEQEEKWVCVDAVhSGVVPKGVTCFEPATLMMTYVFAYDRDGYVkDVTRRYCDQWSTKVRKRRVEKA 444
Ubl_USP14_like cd16104
ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 14 (USP14) and ...
 16-63 1.99e-03

ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 14 (USP14) and similar proteins; USP14 (EC 3.4.19.12), also termed deubiquitinating enzyme 14, or ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, or ubiquitin carboxyl-terminal hydrolase 14, is a component of proteasome regulatory subunit 19S that regulates deubiquitinated proteins entering inside the proteasome core 20S, which plays an inhibitory role in protein degradation. USP14 is also associated with various signal transduction pathways and tumorigenesis, and thus plays an essential role in the development of various types of cancer. Moreover, USP14 mediates the development of cardiac hypertrophy by promoting GSK-3beta phosphorylation, suggesting a role in cardiac hypertrophy treatment. USP14 contains an N-terminal ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, and a C-terminal ubiquitin-specific protease (USP) domain.


Pssm-ID: 340521  Cd Length: 75  Bit Score: 37.60  E-value: 1.99e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 15240508  16 DVDYNTEDGLEVLRFLIFSLTLVPPEEQKIVAEddNRLVSDESDLASL 63
Cdd:cd16104  15 DVELDTDEPPLVFKAQLFALTGVPPERQKIMVK--GGVLKDDDDLSKL 60
 
Name Accession Description Interval E-value
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
 199-296 1.75e-15

Transglutaminase-like superfamily; This family includes animal transglutaminases and other bacterial proteins of unknown function. Sequence conservation in this superfamily primarily involves three motifs that centre around conserved cysteine, histidine, and aspartate residues that form the catalytic triad in the structurally characterized transglutaminase, the human blood clotting factor XIIIa'. On the basis of the experimentally demonstrated activity of the Methanobacterium phage pseudomurein endoisopeptidase, it is proposed that many, if not all, microbial homologs of the transglutaminases are proteases and that the eukaryotic transglutaminases have evolved from an ancestral protease.


Pssm-ID: 376628 [Multi-domain]  Cd Length: 108  Bit Score: 72.82  E-value: 1.75e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240508   199 KTIGQGMGNPLTSELaYGANRVEIYRCTMCP--TTTRFPRYNDPLKLVETKKGRCGEWANCFTLYCRTFGYDSRLIMDFT 276
Cdd:pfam01841   1 KALADRITGGATDPL-EKARAIYDYVRKNITydLPGRSPGDGDAEEFLFTGKGDCEDFASLFVALLRALGIPARYVTGYL 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 15240508   277 D----------HVWTECYSHSLkRWIHLDP 296
Cdd:pfam01841  80 RgpdtvrggdaHAWVEVYLPGY-GWVPVDP 108
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
 243-297 1.06e-10

Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish covalent links between proteins. A subset of transglutaminase homologues appear to catalyse the reverse reaction, the hydrolysis of peptide bonds. Proteins with this domain are both extracellular and intracellular, and it is likely that the eukaryotic intracellular proteins are involved in signalling events.


Pssm-ID: 214673  Cd Length: 68  Bit Score: 57.78  E-value: 1.06e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15240508    243 LVETKKGRCGEWANCFTLYCRTFGYDSRLIMDF--------------TDHVWTECYSHslKRWIHLDPC 297
Cdd:smart00460   1 LLKTKYGTCGEFAALFVALLRSLGIPARVVSGYlkapdtigglrsiwEAHAWAEVYLE--GGWVPVDPT 67
Rad4 pfam03835
Rad4 transglutaminase-like domain;
280-347 2.06e-10

Rad4 transglutaminase-like domain;


Pssm-ID: 427539 [Multi-domain]  Cd Length: 146  Bit Score: 59.34  E-value: 2.06e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15240508   280 WTECYSHSLKRWIHLDP--CEGVYDKPMLYEKGWNKKLN---YVIAISKDGVC-DVTKRYTKKWHEVLSRRTLT 347
Cdd:pfam03835  39 WVEVFNPETKKWISVDPlvLKTIELKSKFEPRIAEKALNvmtYVVAFDSDGGAkDVTRRYCSTYNAKTRKRRIE 112
rad4 TIGR00605
DNA repair protein rad4; All proteins in this family for which functions are known are ...
 280-349 3.51e-06

DNA repair protein rad4; All proteins in this family for which functions are known are involved in targeting nucleotide excision repair to specific regions of the genome.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273170 [Multi-domain]  Cd Length: 713  Bit Score: 50.26  E-value: 3.51e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15240508   280 WTECYSHSLKRWIHLDPC-EGVYDKPMLYEKGWNKKLNYVIAISKDGVC-DVTKRYTKKWHEVLSRRTLTTE 349
Cdd:TIGR00605 373 WVEVFIEQEEKWVCVDAVhSGVVPKGVTCFEPATLMMTYVFAYDRDGYVkDVTRRYCDQWSTKVRKRRVEKA 444
Ubl_USP14_like cd16104
ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 14 (USP14) and ...
 16-63 1.99e-03

ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 14 (USP14) and similar proteins; USP14 (EC 3.4.19.12), also termed deubiquitinating enzyme 14, or ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, or ubiquitin carboxyl-terminal hydrolase 14, is a component of proteasome regulatory subunit 19S that regulates deubiquitinated proteins entering inside the proteasome core 20S, which plays an inhibitory role in protein degradation. USP14 is also associated with various signal transduction pathways and tumorigenesis, and thus plays an essential role in the development of various types of cancer. Moreover, USP14 mediates the development of cardiac hypertrophy by promoting GSK-3beta phosphorylation, suggesting a role in cardiac hypertrophy treatment. USP14 contains an N-terminal ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, and a C-terminal ubiquitin-specific protease (USP) domain.


Pssm-ID: 340521  Cd Length: 75  Bit Score: 37.60  E-value: 1.99e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 15240508  16 DVDYNTEDGLEVLRFLIFSLTLVPPEEQKIVAEddNRLVSDESDLASL 63
Cdd:cd16104  15 DVELDTDEPPLVFKAQLFALTGVPPERQKIMVK--GGVLKDDDDLSKL 60
 
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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