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Conserved domains on  [gi|442622389|ref|NP_724444|]
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PNGase-like, isoform C [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PAW pfam04721
PNGase C-terminal domain, mannose-binding module PAW; The PAW domain is found at the ...
 444-630 1.71e-88

PNGase C-terminal domain, mannose-binding module PAW; The PAW domain is found at the C-terminus of PGNase, or peptide-N-glycanase, enzymes. It was named for 'domain present in PNGases and other worm proteins'. PNGase catalyzes the deglycosylation of several misfolded N-linked glycoproteins by cleaving off the bulky glycan chain before these proteins are degraded by the proteasome. PNGase specifically acts on the unfolded form of high-mannose type N-glycosylated proteins, and this domain appears to be the mannose-binding domain, which contributes to the oligosaccharide-binding specificity of PNGase.


:

Pssm-ID: 461409  Cd Length: 197  Bit Score: 273.39  E-value: 1.71e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622389  444 GRSSGSLSWRQSRGEHTF---TNIFVFNLSATELQKRQLNVRYSCATDTYERYAKEGEhitildSYKTWQKAQFSSKNIF 520
Cdd:pfam04721   1 GRTSGSLAWRLARGETGSatqEKEFVFKPTEKEKKAKLFHLRYSIVKDIYTRVSNNNE------TIKGWESGVFSSENIF 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622389  521 RKVERDWKMAYLARLEDTDCGEIAWTFDFSKTNLKVKSYNLVFETKTFGDGKISVTVDATDGS------------ASVEN 588
Cdd:pfam04721  75 RKVEHDWKMVYLARTEGTSSGSISWKFDLSSSGLKIKSISLKASSQTFESGKVSWRLQSDKTTveipgdktlqslSSLSG 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 442622389  589 ATGFKIVAKLTGGKGDVAWQHTQLFRQSLNS-RDYPFDLQVQL 630
Cdd:pfam04721 155 ATELTLTAELSGGDGDVAWQHAQLFRQSLDDtEEYSLEIIITL 197
PUB pfam09409
PUB domain; The PUB (also known as PUG) domain is found in peptide N-glycanase where it ...
 29-109 6.49e-22

PUB domain; The PUB (also known as PUG) domain is found in peptide N-glycanase where it functions as a AAA ATPase binding domain. This domain is also found on other proteins linked to the ubiquitin-proteasome system.


:

Pssm-ID: 462790  Cd Length: 80  Bit Score: 90.02  E-value: 6.49e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622389   29 KEAYLEAVRILLVLLENILAQPENSMFRTIRQENKAIKEKLLSLPGCERLLEAIGFVRaPSSNAYTLPTEVSLQQVKKYR 108
Cdd:pfam09409   1 KEKVKEALETLLKYLNNILSNPNEEKYRKIRLSNKAFQEKVLPLEGALELLLAIGFEK-EDEEEFLLLEEESLKQLAVLL 79


                  .
gi 442622389  109 D 109
Cdd:pfam09409  80 E 80
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
 278-341 4.42e-14

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: 68.59  E-value: 4.42e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442622389  278 KFYRYNDISQLLVSRKGRCGEYANCFTFLCRALDYDARIVH---------SHFD-HVWTEVYSEAQmRWLHVDP 341
Cdd:pfam01841  36 RSPGDGDAEEFLFTGKGDCEDFASLFVALLRALGIPARYVTgylrgpdtvRGGDaHAWVEVYLPGY-GWVPVDP 108
Rad4 super family cl44506
Rad4 transglutaminase-like domain;
325-383 2.21e-04

Rad4 transglutaminase-like domain;


The actual alignment was detected with superfamily member pfam03835:

Pssm-ID: 427539 [Multi-domain]  Cd Length: 146  Bit Score: 42.01  E-value: 2.21e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442622389  325 WTEVYSEAQMRWLHVDP--SENV----IDSPLMYQHGwKRHIDYILAYSRDD-IQDVTWRYTNDHQ 383
Cdd:pfam03835  39 WVEVFNPETKKWISVDPlvLKTIelksKFEPRIAEKA-LNVMTYVVAFDSDGgAKDVTRRYCSTYN 103
 
Name Accession Description Interval E-value
PAW pfam04721
PNGase C-terminal domain, mannose-binding module PAW; The PAW domain is found at the ...
 444-630 1.71e-88

PNGase C-terminal domain, mannose-binding module PAW; The PAW domain is found at the C-terminus of PGNase, or peptide-N-glycanase, enzymes. It was named for 'domain present in PNGases and other worm proteins'. PNGase catalyzes the deglycosylation of several misfolded N-linked glycoproteins by cleaving off the bulky glycan chain before these proteins are degraded by the proteasome. PNGase specifically acts on the unfolded form of high-mannose type N-glycosylated proteins, and this domain appears to be the mannose-binding domain, which contributes to the oligosaccharide-binding specificity of PNGase.


Pssm-ID: 461409  Cd Length: 197  Bit Score: 273.39  E-value: 1.71e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622389  444 GRSSGSLSWRQSRGEHTF---TNIFVFNLSATELQKRQLNVRYSCATDTYERYAKEGEhitildSYKTWQKAQFSSKNIF 520
Cdd:pfam04721   1 GRTSGSLAWRLARGETGSatqEKEFVFKPTEKEKKAKLFHLRYSIVKDIYTRVSNNNE------TIKGWESGVFSSENIF 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622389  521 RKVERDWKMAYLARLEDTDCGEIAWTFDFSKTNLKVKSYNLVFETKTFGDGKISVTVDATDGS------------ASVEN 588
Cdd:pfam04721  75 RKVEHDWKMVYLARTEGTSSGSISWKFDLSSSGLKIKSISLKASSQTFESGKVSWRLQSDKTTveipgdktlqslSSLSG 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 442622389  589 ATGFKIVAKLTGGKGDVAWQHTQLFRQSLNS-RDYPFDLQVQL 630
Cdd:pfam04721 155 ATELTLTAELSGGDGDVAWQHAQLFRQSLDDtEEYSLEIIITL 197
PUB pfam09409
PUB domain; The PUB (also known as PUG) domain is found in peptide N-glycanase where it ...
 29-109 6.49e-22

PUB domain; The PUB (also known as PUG) domain is found in peptide N-glycanase where it functions as a AAA ATPase binding domain. This domain is also found on other proteins linked to the ubiquitin-proteasome system.


Pssm-ID: 462790  Cd Length: 80  Bit Score: 90.02  E-value: 6.49e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622389   29 KEAYLEAVRILLVLLENILAQPENSMFRTIRQENKAIKEKLLSLPGCERLLEAIGFVRaPSSNAYTLPTEVSLQQVKKYR 108
Cdd:pfam09409   1 KEKVKEALETLLKYLNNILSNPNEEKYRKIRLSNKAFQEKVLPLEGALELLLAIGFEK-EDEEEFLLLEEESLKQLAVLL 79


                  .
gi 442622389  109 D 109
Cdd:pfam09409  80 E 80
PAW smart00613
domain present in PNGases and other hypothetical proteins; present in several copies in ...
 473-571 3.81e-20

domain present in PNGases and other hypothetical proteins; present in several copies in proteins with unknown function in C. elegans


Pssm-ID: 214745  Cd Length: 89  Bit Score: 85.40  E-value: 3.81e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622389   473 ELQKRQLNVRYSCATDTYERYAKEGEHITILDsYKTWQKAQFSsknifrkvERDWKMAYLARLEDTDCGeIAWTFDFSKT 552
Cdd:smart00613   1 ESGENYVKFTYDIINDTYSHTNEDGSPVQPYE-VKNIERVVDK--------ELNEVYLHKKRPEEEGNY-IYWKFDLKST 70

                           90
                   ....*....|....*....
gi 442622389   553 NLKVKSYNLVFETKTFGDG 571
Cdd:smart00613  71 GKSVEKVVIRMSGIEEIAN 89
PUB cd09212
PNGase/UBA or UBX (PUB) domain of p97 adaptor proteins; The PUB domain is found in p97 adaptor ...
 30-113 5.73e-18

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.


Pssm-ID: 198416  Cd Length: 96  Bit Score: 79.35  E-value: 5.73e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622389  30 EAYLEAVRILLVLLENILAQPENSMFRTIRQENKAIKEKLLSLPGCERLLEAIGFVRAPSS--NAYTLPTEVSLQQVKKY 107
Cdd:cd09212   11 EAFKEALKTLLKILDNILSNPTEEKYRRIRLSNKAFQEKVLPVPGGLELLLALGFVEETESgeSFLVLPDDADVDLLKDA 90


                 ....*.
gi 442622389 108 RDALSE 113
Cdd:cd09212   91 KAALEE 96
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
 278-341 4.42e-14

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: 68.59  E-value: 4.42e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442622389  278 KFYRYNDISQLLVSRKGRCGEYANCFTFLCRALDYDARIVH---------SHFD-HVWTEVYSEAQmRWLHVDP 341
Cdd:pfam01841  36 RSPGDGDAEEFLFTGKGDCEDFASLFVALLRALGIPARYVTgylrgpdtvRGGDaHAWVEVYLPGY-GWVPVDP 108
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
 288-342 6.07e-14

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: 67.02  E-value: 6.07e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442622389   288 LLVSRKGRCGEYANCFTFLCRALDYDARIV--------------HSHFDHVWTEVYSEAqmRWLHVDPS 342
Cdd:smart00460   1 LLKTKYGTCGEFAALFVALLRSLGIPARVVsgylkapdtigglrSIWEAHAWAEVYLEG--GWVPVDPT 67
PUG smart00580
domain in protein kinases, N-glycanases and other nuclear proteins;
35-97 1.57e-13

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


Pssm-ID: 197798  Cd Length: 57  Bit Score: 65.40  E-value: 1.57e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442622389    35 AVRILLVLLENILAQPENSMfrtirqENKAIKEKLLSLPGCERLLEAIGFVRAPSSNAYTLPT 97
Cdd:smart00580   1 SVRDLLRALRNILHHPREEK------GNPAIKERLGPVPGGFELYFTVGFPRLLISEVYTLPK 57
YebA COG1305
Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, ...
 284-342 4.57e-08

Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440916 [Multi-domain]  Cd Length: 174  Bit Score: 53.08  E-value: 4.57e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442622389 284 DISQLLVSRKGRCGEYANCFTFLCRALDYDARIV-------------HSHFDHVWTEVYSEAQmRWLHVDPS 342
Cdd:COG1305  104 TALETLERRRGVCRDFAHLLVALLRALGIPARYVsgylpgepppgggRADDAHAWVEVYLPGA-GWVPFDPT 174
Rad4 pfam03835
Rad4 transglutaminase-like domain;
325-383 2.21e-04

Rad4 transglutaminase-like domain;


Pssm-ID: 427539 [Multi-domain]  Cd Length: 146  Bit Score: 42.01  E-value: 2.21e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442622389  325 WTEVYSEAQMRWLHVDP--SENV----IDSPLMYQHGwKRHIDYILAYSRDD-IQDVTWRYTNDHQ 383
Cdd:pfam03835  39 WVEVFNPETKKWISVDPlvLKTIelksKFEPRIAEKA-LNVMTYVVAFDSDGgAKDVTRRYCSTYN 103
 
Name Accession Description Interval E-value
PAW pfam04721
PNGase C-terminal domain, mannose-binding module PAW; The PAW domain is found at the ...
 444-630 1.71e-88

PNGase C-terminal domain, mannose-binding module PAW; The PAW domain is found at the C-terminus of PGNase, or peptide-N-glycanase, enzymes. It was named for 'domain present in PNGases and other worm proteins'. PNGase catalyzes the deglycosylation of several misfolded N-linked glycoproteins by cleaving off the bulky glycan chain before these proteins are degraded by the proteasome. PNGase specifically acts on the unfolded form of high-mannose type N-glycosylated proteins, and this domain appears to be the mannose-binding domain, which contributes to the oligosaccharide-binding specificity of PNGase.


Pssm-ID: 461409  Cd Length: 197  Bit Score: 273.39  E-value: 1.71e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622389  444 GRSSGSLSWRQSRGEHTF---TNIFVFNLSATELQKRQLNVRYSCATDTYERYAKEGEhitildSYKTWQKAQFSSKNIF 520
Cdd:pfam04721   1 GRTSGSLAWRLARGETGSatqEKEFVFKPTEKEKKAKLFHLRYSIVKDIYTRVSNNNE------TIKGWESGVFSSENIF 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622389  521 RKVERDWKMAYLARLEDTDCGEIAWTFDFSKTNLKVKSYNLVFETKTFGDGKISVTVDATDGS------------ASVEN 588
Cdd:pfam04721  75 RKVEHDWKMVYLARTEGTSSGSISWKFDLSSSGLKIKSISLKASSQTFESGKVSWRLQSDKTTveipgdktlqslSSLSG 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 442622389  589 ATGFKIVAKLTGGKGDVAWQHTQLFRQSLNS-RDYPFDLQVQL 630
Cdd:pfam04721 155 ATELTLTAELSGGDGDVAWQHAQLFRQSLDDtEEYSLEIIITL 197
PUB pfam09409
PUB domain; The PUB (also known as PUG) domain is found in peptide N-glycanase where it ...
 29-109 6.49e-22

PUB domain; The PUB (also known as PUG) domain is found in peptide N-glycanase where it functions as a AAA ATPase binding domain. This domain is also found on other proteins linked to the ubiquitin-proteasome system.


Pssm-ID: 462790  Cd Length: 80  Bit Score: 90.02  E-value: 6.49e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622389   29 KEAYLEAVRILLVLLENILAQPENSMFRTIRQENKAIKEKLLSLPGCERLLEAIGFVRaPSSNAYTLPTEVSLQQVKKYR 108
Cdd:pfam09409   1 KEKVKEALETLLKYLNNILSNPNEEKYRKIRLSNKAFQEKVLPLEGALELLLAIGFEK-EDEEEFLLLEEESLKQLAVLL 79


                  .
gi 442622389  109 D 109
Cdd:pfam09409  80 E 80
PAW smart00613
domain present in PNGases and other hypothetical proteins; present in several copies in ...
 473-571 3.81e-20

domain present in PNGases and other hypothetical proteins; present in several copies in proteins with unknown function in C. elegans


Pssm-ID: 214745  Cd Length: 89  Bit Score: 85.40  E-value: 3.81e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622389   473 ELQKRQLNVRYSCATDTYERYAKEGEHITILDsYKTWQKAQFSsknifrkvERDWKMAYLARLEDTDCGeIAWTFDFSKT 552
Cdd:smart00613   1 ESGENYVKFTYDIINDTYSHTNEDGSPVQPYE-VKNIERVVDK--------ELNEVYLHKKRPEEEGNY-IYWKFDLKST 70

                           90
                   ....*....|....*....
gi 442622389   553 NLKVKSYNLVFETKTFGDG 571
Cdd:smart00613  71 GKSVEKVVIRMSGIEEIAN 89
PUB cd09212
PNGase/UBA or UBX (PUB) domain of p97 adaptor proteins; The PUB domain is found in p97 adaptor ...
 30-113 5.73e-18

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.


Pssm-ID: 198416  Cd Length: 96  Bit Score: 79.35  E-value: 5.73e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622389  30 EAYLEAVRILLVLLENILAQPENSMFRTIRQENKAIKEKLLSLPGCERLLEAIGFVRAPSS--NAYTLPTEVSLQQVKKY 107
Cdd:cd09212   11 EAFKEALKTLLKILDNILSNPTEEKYRRIRLSNKAFQEKVLPVPGGLELLLALGFVEETESgeSFLVLPDDADVDLLKDA 90


                 ....*.
gi 442622389 108 RDALSE 113
Cdd:cd09212   91 KAALEE 96
PUB_PNGase cd10459
PNGase/UBA or UBX (PUB) domain of the P97 adaptor protein Peptide:N-glycanase (PNGase); This ...
 30-115 1.22e-14

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.


Pssm-ID: 198417  Cd Length: 93  Bit Score: 69.61  E-value: 1.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622389  30 EAYLEAVRILLVLLENILAQPENSMFRTIRQENKAIKEKLLSLPGCERLLEAIGFVRApsSNAYTLPTEVSLQQVKKYRD 109
Cdd:cd10459   10 DVFLEASEALLTYANNILRNPNDPKYRSIRLDNPVFSTKLLPARGAIECLFEMGFVED--EDRLFLPRNASLEKLQDLRD 87


                 ....*.
gi 442622389 110 ALSERR 115
Cdd:cd10459   88 LLAAER 93
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
 278-341 4.42e-14

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: 68.59  E-value: 4.42e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442622389  278 KFYRYNDISQLLVSRKGRCGEYANCFTFLCRALDYDARIVH---------SHFD-HVWTEVYSEAQmRWLHVDP 341
Cdd:pfam01841  36 RSPGDGDAEEFLFTGKGDCEDFASLFVALLRALGIPARYVTgylrgpdtvRGGDaHAWVEVYLPGY-GWVPVDP 108
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
 288-342 6.07e-14

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: 67.02  E-value: 6.07e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442622389   288 LLVSRKGRCGEYANCFTFLCRALDYDARIV--------------HSHFDHVWTEVYSEAqmRWLHVDPS 342
Cdd:smart00460   1 LLKTKYGTCGEFAALFVALLRSLGIPARVVsgylkapdtigglrSIWEAHAWAEVYLEG--GWVPVDPT 67
PUG smart00580
domain in protein kinases, N-glycanases and other nuclear proteins;
35-97 1.57e-13

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


Pssm-ID: 197798  Cd Length: 57  Bit Score: 65.40  E-value: 1.57e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442622389    35 AVRILLVLLENILAQPENSMfrtirqENKAIKEKLLSLPGCERLLEAIGFVRAPSSNAYTLPT 97
Cdd:smart00580   1 SVRDLLRALRNILHHPREEK------GNPAIKERLGPVPGGFELYFTVGFPRLLISEVYTLPK 57
PUB_UBXD1 cd10460
PNGase/UBA or UBX (PUB) domain of UBXD1; This PUB domain is found in p97 adaptor protein ...
 29-112 1.91e-09

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.


Pssm-ID: 198418  Cd Length: 102  Bit Score: 55.33  E-value: 1.91e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622389  29 KEAYLEAVRILLVLLENILAQPENSMFRTIRQENKAIKEKLLSLPGCERLLEAIGFVRAPSSNA------YTLPTEVSLQ 102
Cdd:cd10460   11 REKVEECVDTLCKYLENIIDHPDEEKYRKIRLSNKVFQEKVLPVEGALEFLEAAGFEEKTLPEQedeedfLVLSEECDID 90

                         90
                 ....*....|
gi 442622389 103 QVKKYRDALS 112
Cdd:cd10460   91 SLELAKDLLQ 100
PUB_WLM cd10463
PNGase/UBA or UBX (PUB) domain of the Wss1p-like metalloprotease (WLM) family; The PUB domain ...
 34-86 1.51e-08

PNGase/UBA or UBX (PUB) domain of the Wss1p-like metalloprotease (WLM) family; 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. WLM domains are found mostly in plant proteins, belonging to the Zincin-like superfamily of Zn-dependent peptidases that are linked to the ubiquitin signaling pathway through its fusion with the ubiquitin-binding PUB, ubiquitin-like, and Little Finger domains. More specifically, genetic evidence implicates the WLM family in de-SUMOylation.


Pssm-ID: 198421  Cd Length: 96  Bit Score: 52.39  E-value: 1.51e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 442622389  34 EAVRILLVLLENILAQPENSMFRTIRQENKAIKEKLLSLPGCERLLEAIGFVR 86
Cdd:cd10463   16 SALQTLFKILGNAIEHPNEDKFRRLRKSNPAFQRRVARFPGAVELLLAAGFAE 68
YebA COG1305
Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, ...
 284-342 4.57e-08

Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440916 [Multi-domain]  Cd Length: 174  Bit Score: 53.08  E-value: 4.57e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442622389 284 DISQLLVSRKGRCGEYANCFTFLCRALDYDARIV-------------HSHFDHVWTEVYSEAQmRWLHVDPS 342
Cdd:COG1305  104 TALETLERRRGVCRDFAHLLVALLRALGIPARYVsgylpgepppgggRADDAHAWVEVYLPGA-GWVPFDPT 174
PUB_UBA_plant cd10461
PNGase/UBA or UBX (PUB) domain of plant Ubiquitin-associated (UBA) domain containing proteins; ...
 24-96 3.97e-06

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.


Pssm-ID: 198419  Cd Length: 107  Bit Score: 45.89  E-value: 3.97e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442622389  24 QERGLKEAYleavRILLVLLENILAQPENSMFRTIRQENKAIKEKLLSLPGCERLLEAIGFVRAPSSNAYTLP 96
Cdd:cd10461   11 DPDAVKTAF----QTLLTYLGNVAKNPDEEKFRRIRLTNAAFQERVGALRGGIEFLELCGFERDEGDEALVLP 79
Rad4 pfam03835
Rad4 transglutaminase-like domain;
325-383 2.21e-04

Rad4 transglutaminase-like domain;


Pssm-ID: 427539 [Multi-domain]  Cd Length: 146  Bit Score: 42.01  E-value: 2.21e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442622389  325 WTEVYSEAQMRWLHVDP--SENV----IDSPLMYQHGwKRHIDYILAYSRDD-IQDVTWRYTNDHQ 383
Cdd:pfam03835  39 WVEVFNPETKKWISVDPlvLKTIelksKFEPRIAEKA-LNVMTYVVAFDSDGgAKDVTRRYCSTYN 103
PUB_UBA cd10462
PNGase/UBA or UBX (PUB) domain of Ubiquitin-associated (UBA) domain containing proteins; The ...
 29-113 5.46e-04

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.


Pssm-ID: 198420  Cd Length: 100  Bit Score: 39.78  E-value: 5.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622389  29 KEAYLEAVRILLVLLENILAQPENSMFRTIRQENKAIKEKLLSLPGCERLLEAIGFVRAPSSNAYT--LPTEVSLQQVKK 106
Cdd:cd10462   13 KQGLMTCLNTLRTYISNAHDHPLEEKYKKIRKENKAFVSKVLIFEGAIEILLACGFEDTGDFLFIInkIPDTFLCSQAIK 92


                 ....*..
gi 442622389 107 YRDALSE 113
Cdd:cd10462   93 FIDLILQ 99
 
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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