PNGase/UBA or UBX (PUB) domain of p97 adaptor proteins; The PUB domain is found in p97 adaptor proteins such as PNGase, UBXD1 (UBX domain-containing protein 1), and RNF31 (RING finger protein 31). It functions as a p97 (also known as valosin-containing protein or VCP) adaptor by interacting with the D1 and/or D2 ATPase domains. The p97, a type II AAA+ ATPase, is involved in a variety of cellular processes such as the deglycosylation of ERAD substrates, membrane fusion, transcription factor activation and cell cycle regulation through differential binding to specific adaptor proteins. The PUB domain in UBX-domain protein 1 (UBXD1), which is widely expressed in higher eukaryotes (except for fungi) and which is involved in substrate recruitment to p97, interacts strongly with the C-terminus of p97. Peptide:N-glycanase (PNGase), a deglycosylating enzyme that functions in proteasome-dependent degradation of misfolded glycoproteins which are translocated from the endoplasmic reticulum (ER) to the cytosol during ERAD, associates with the ubiquitin-proteasome system proteins mediated by the N-terminal PUB domain. PNGase is present in all eukaryotic organisms; however, the yeast PNGase ortholog does not contain the PUB domain. The RNF31 protein, also known as HOIP or Zibra, contains an N-terminal PUB domain similar to those in PNGase and UBXD1, suggesting its association with p97.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 223941803   1 MRNPNDEKYRSIRIGNTAFSTRLLPVRGAVECLFEMGFEEGETHLIFPKKASVEQLQKIRDLIAIER 67
Cdd:cd10459   27 LRNPNDPKYRSIRLDNPVFSTKLLPARGAIECLFEMGFVEDEDRLFLPRNASLEKLQDLRDLLAAER 93

Rad4 transglutaminase-like domain;

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 223941803  296 WTEVYSPSQQRWLHCDACEDV------CDKPLLYEigwgKK---LSYVIAFSKDEVV-DVTWRYS 350
Cdd:pfam03835  39 WVEVFNPETKKWISVDPLVLKtielksKFEPRIAE----KAlnvMTYVVAFDSDGGAkDVTRRYC 99

PNGase/UBA or UBX (PUB) domain of the P97 adaptor protein Peptide:N-glycanase (PNGase); This PUB (PNGase/UBA or UBX) domain is found in the p97 adaptor protein PNGase (Peptide:N-glycanase). The PUB domain functions as a p97 (also known as valosin-containing protein or VCP) adaptor by interacting with the D1 and/or D2 ATPase domains. The type II AAA+ ATPase p97 is involved in a variety of cellular processes such as the deglycosylation of ERAD substrates, membrane fusion, transcription factor activation and cell cycle regulation through differential binding to specific adaptor proteins. Peptide:N-glycanase (PNGase), a deglycosylating enzyme that functions in proteasome-dependent degradation of misfolded glycoproteins which are translocated from the endoplasmic reticulum (ER) to the cytosol during ERAD, associates with the ubiquitin-proteasome system proteins mediated by the N-terminal PUB domain. PNGase is present in all eukaryotic organisms; however, the yeast PNGase ortholog does not contain the PUB domain. The mammalian PNGase binds a considerable number of proteins via its PUB domain; these include ERAD E3 enzyme, the autocrine motility factor receptor (AMFR or gp78), SAKS and Derlin-1.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 223941803   1 MRNPNDEKYRSIRIGNTAFSTRLLPVRGAVECLFEMGFEEGETHLIFPKKASVEQLQKIRDLIAIER 67
Cdd:cd10459   27 LRNPNDPKYRSIRLDNPVFSTKLLPARGAIECLFEMGFVEDEDRLFLPRNASLEKLQDLRDLLAAER 93

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223941803  233 AKEVEDHYCD--ACQFSNRFPRYNNPEKLLETRCGRCGEWANCFTLCCRAVGFEARYVWDYTD----------HVWTEVY 300
Cdd:pfam01841  18 ARAIYDYVRKniTYDLPGRSPGDGDAEEFLFTGKGDCEDFASLFVALLRALGIPARYVTGYLRgpdtvrggdaHAWVEVY 97

                          90
                  ....*....|..
gi 223941803  301 SPsQQRWLHCDA 312
Cdd:pfam01841  98 LP-GYGWVPVDP 108

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.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 223941803   259 LLETRCGRCGEWANCFTLCCRAVGFEARYVWDY--------------TDHVWTEVYSPsqQRWLHCDAC 313
Cdd:smart00460   1 LLKTKYGTCGEFAALFVALLRSLGIPARVVSGYlkapdtigglrsiwEAHAWAEVYLE--GGWVPVDPT 67

domain in protein kinases, N-glycanases and other nuclear proteins;

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 223941803     2 RNPNDEKyrsiriGNTAFSTRLLPVRGAVECLFEMGFE--EGETHLIFPK 49
Cdd:smart00580  14 HHPREEK------GNPAIKERLGPVPGGFELYFTVGFPrlLISEVYTLPK 57

PNGase/UBA or UBX (PUB) domain of the P97 adaptor protein Peptide:N-glycanase (PNGase); This PUB (PNGase/UBA or UBX) domain is found in the p97 adaptor protein PNGase (Peptide:N-glycanase). The PUB domain functions as a p97 (also known as valosin-containing protein or VCP) adaptor by interacting with the D1 and/or D2 ATPase domains. The type II AAA+ ATPase p97 is involved in a variety of cellular processes such as the deglycosylation of ERAD substrates, membrane fusion, transcription factor activation and cell cycle regulation through differential binding to specific adaptor proteins. Peptide:N-glycanase (PNGase), a deglycosylating enzyme that functions in proteasome-dependent degradation of misfolded glycoproteins which are translocated from the endoplasmic reticulum (ER) to the cytosol during ERAD, associates with the ubiquitin-proteasome system proteins mediated by the N-terminal PUB domain. PNGase is present in all eukaryotic organisms; however, the yeast PNGase ortholog does not contain the PUB domain. The mammalian PNGase binds a considerable number of proteins via its PUB domain; these include ERAD E3 enzyme, the autocrine motility factor receptor (AMFR or gp78), SAKS and Derlin-1.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 223941803   1 MRNPNDEKYRSIRIGNTAFSTRLLPVRGAVECLFEMGFEEGETHLIFPKKASVEQLQKIRDLIAIER 67
Cdd:cd10459   27 LRNPNDPKYRSIRLDNPVFSTKLLPARGAIECLFEMGFVEDEDRLFLPRNASLEKLQDLRDLLAAER 93

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223941803  233 AKEVEDHYCD--ACQFSNRFPRYNNPEKLLETRCGRCGEWANCFTLCCRAVGFEARYVWDYTD----------HVWTEVY 300
Cdd:pfam01841  18 ARAIYDYVRKniTYDLPGRSPGDGDAEEFLFTGKGDCEDFASLFVALLRALGIPARYVTGYLRgpdtvrggdaHAWVEVY 97

                          90
                  ....*....|..
gi 223941803  301 SPsQQRWLHCDA 312
Cdd:pfam01841  98 LP-GYGWVPVDP 108

PNGase/UBA or UBX (PUB) domain of p97 adaptor proteins; The PUB domain is found in p97 adaptor proteins such as PNGase, UBXD1 (UBX domain-containing protein 1), and RNF31 (RING finger protein 31). It functions as a p97 (also known as valosin-containing protein or VCP) adaptor by interacting with the D1 and/or D2 ATPase domains. The p97, a type II AAA+ ATPase, is involved in a variety of cellular processes such as the deglycosylation of ERAD substrates, membrane fusion, transcription factor activation and cell cycle regulation through differential binding to specific adaptor proteins. The PUB domain in UBX-domain protein 1 (UBXD1), which is widely expressed in higher eukaryotes (except for fungi) and which is involved in substrate recruitment to p97, interacts strongly with the C-terminus of p97. Peptide:N-glycanase (PNGase), a deglycosylating enzyme that functions in proteasome-dependent degradation of misfolded glycoproteins which are translocated from the endoplasmic reticulum (ER) to the cytosol during ERAD, associates with the ubiquitin-proteasome system proteins mediated by the N-terminal PUB domain. PNGase is present in all eukaryotic organisms; however, the yeast PNGase ortholog does not contain the PUB domain. The RNF31 protein, also known as HOIP or Zibra, contains an N-terminal PUB domain similar to those in PNGase and UBXD1, suggesting its association with p97.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 223941803   2 RNPNDEKYRSIRIGNTAFSTRLLPVRGAVECLFEMGFEE----GETHLIFPKKASVEQLQKIRDLI 63
Cdd:cd09212   29 SNPTEEKYRRIRLSNKAFQEKVLPVPGGLELLLALGFVEetesGESFLVLPDDADVDLLKDAKAAL 94

PNGase/UBA or UBX (PUB) domain of UBXD1; This PUB domain is found in p97 adaptor protein UBXD1 (UBX domain-containing protein 1, also called UBXD6). It functions as a p97 (also known as valosin-containing protein or VCP) adaptor by interacting with the D1 and/or D2 ATPase domains. The type II AAA+ ATPase p97 is involved in a variety of cellular processes such as the deglycosylation of ERAD substrates, membrane fusion, transcription factor activation and cell cycle regulation through differential binding to specific adaptor proteins. The PUB domain in UBX-domain protein 1 (UBXD1), which is widely expressed in higher eukaryotes, except for fungi, and which is involved in substrate recruitment to p97, interacts strongly with the C-terminus of p97. UBXD1 also interacts with HRD1 and HERP, both components of the ERAD pathway, via p97. It is possibly involved in aggresome formation; aggresomes are perinuclear compartments that contain misfolded proteins colocalized with centrosome markers.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 223941803   3 NPNDEKYRSIRIGNTAFSTRLLPVRGAVECLFEMGFEE--------GETHLIFPKKASVEQLQKIRDLI 63
Cdd:cd10460   31 HPDEEKYRKIRLSNKVFQEKVLPVEGALEFLEAAGFEEktlpeqedEEDFLVLSEECDIDSLELAKDLL 99

PNGase/UBA or UBX (PUB) domain of plant Ubiquitin-associated (UBA) domain containing proteins; The PUB domain functions as a p97 (also known as valosin-containing protein or VCP) adaptor by interacting with the D1 and/or D2 ATPase domains. The type II AAA+ ATPase p97 is involved in a variety of cellular processes such as the deglycosylation of ERAD substrates, membrane fusion, transcription factor activation and cell cycle regulation through differential binding to specific adaptor proteins. The UBA domain, along with UBL (ubiquitin-like) domain, has been implicated in proteasomal degradation by associating with substrates destined for degradation as well as with subunits of the proteasome, thus regulating protein turnover. This family contains only plant UBA domain-containing proteins.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 223941803   2 RNPNDEKYRSIRIGNTAFSTRLLPVRGAVECLFEMGFE--EGETHLIFPK 49
Cdd:cd10461   31 KNPDEEKFRRIRLTNAAFQERVGALRGGIEFLELCGFErdEGDEALVLPR 80

domain in protein kinases, N-glycanases and other nuclear proteins;

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 223941803     2 RNPNDEKyrsiriGNTAFSTRLLPVRGAVECLFEMGFE--EGETHLIFPK 49
Cdd:smart00580  14 HHPREEK------GNPAIKERLGPVPGGFELYFTVGFPrlLISEVYTLPK 57

PNGase/UBA or UBX (PUB) domain of Ubiquitin-associated (UBA) domain containing proteins; The PUB domain functions as a p97 (also known as valosin-containing protein or VCP) adaptor by interacting with the D1 and/or D2 ATPase domains. The type II AAA+ ATPase p97 is involved in a variety of cellular processes such as the deglycosylation of ERAD substrates, membrane fusion, transcription factor activation and cell cycle regulation through differential binding to specific adaptor proteins. The UBA domain, along with UBL (ubiquitin-like) domain, has been implicated in proteasomal degradation by associating with substrates destined for degradation as well as with subunits of the proteasome, thus regulating protein turnover.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 223941803   3 NPNDEKYRSIRIGNTAFSTRLLPVRGAVECLFEMGFEEGETHLIFPKK 50
Cdd:cd10462   33 HPLEEKYKKIRKENKAFVSKVLIFEGAIEILLACGFEDTGDFLFIINK 80