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Conserved domains on  [gi|1252414522|ref|NP_001343458|]
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UBX domain-containing protein 4 isoform 2 [Mus musculus]

Protein Classification

Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold and UBX_UBXN4 domain-containing protein( domain architecture ID 13051569)

Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold and UBX_UBXN4 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UBX_UBXN4 cd16117
Ubiquitin regulatory domain X (UBX) found in UBX domain protein 4 (UBXN4) and similar proteins; ...
 318-394 9.14e-45

Ubiquitin regulatory domain X (UBX) found in UBX domain protein 4 (UBXN4) and similar proteins; UBXN4, also termed ERAD (endoplasmic-reticulum-associated protein degradation) substrate erasing protein (erasin), or UBX domain-containing protein 2 (UBXD2), or UBXDC1, belongs to the UBXD family of proteins that contains the ubiquitin regulatory domain X (UBX) with a beta-grasp ubiquitin-like fold, but without the C-terminal double glycine motif. UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. UBXN4 is an endoplasmic reticulum (ER) localized protein that interacts with p97 (also known as VCP or Cdc48) via its UBX domain. Erasin exists in a complex with other p97/VCP-associated factors involved in endoplasmic-reticulum-associated protein degradation (ERAD). p97 is a homohexameric AAA ATPase (ATPase associated with a variety of activities) involved in a variety of functions ranging from cell-cycle regulation to membrane fusion and protein degradation. The overexpression of UBXN4 increases degradation of a classical ERAD substrate and UBXN4 levels are increased in ER stressed cells. Anti-UBXN4 staining is increased in neuropathological lesions in brains of patients with Alzheimer's disease.


:

Pssm-ID: 340534 [Multi-domain]  Cd Length: 77  Bit Score: 151.71  E-value: 9.14e-45
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1252414522 318 IARIQFRLPDGSSFTNQFPSDAPLEEARQFAAQTVGNTYGNFSLATMFPRREFTREDYKRRLLDLELAPSASVVLLP 394
Cdd:cd16117     1 TARIQFRLPDGSSFTNQFPSDAPLEEARQFVAQTVGPAYGPFSLATTFPRREFTDDDYQKTLLELELAPSAALVVLP 77
Thioredoxin_like super family cl00388
Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin ...
 4-113 3.00e-04

Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin (TRX)-like superfamily is a large, diverse group of proteins containing a TRX fold. Many members contain a classic TRX domain with a redox active CXXC motif. They function as protein disulfide oxidoreductases (PDOs), altering the redox state of target proteins via the reversible oxidation of their active site dithiol. The PDO members of this superfamily include the families of TRX, protein disulfide isomerase (PDI), tlpA, glutaredoxin, NrdH redoxin, and bacterial Dsb proteins (DsbA, DsbC, DsbG, DsbE, DsbDgamma). Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins, glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others.


The actual alignment was detected with superfamily member cd02958:

Pssm-ID: 469754 [Multi-domain]  Cd Length: 114  Bit Score: 40.28  E-value: 3.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414522   4 FQGAIPAAIASAKRSGAVFVVFVAGDDEQSIQMAAS--WEDEKVTQASSNNFVAIKID-TKSEAcLQFSQIYPVVCVPSS 80
Cdd:cd02958     2 FQGSFEDAKQEAKSEKKWLLVYLQSEDEFDSQVLNRdlWSNESVKEFIRENFIFWQCDiDSSEG-QRFLQSYKVDKYPHI 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1252414522  81 FFIG-DSGIPLEVIAGSVSADELVTRIHKVQQMH 113
Cdd:cd02958    81 AIIDpRTGEVLKVWSGNITPEDLLSQLIEFLEEF 114
 
Name Accession Description Interval E-value
UBX_UBXN4 cd16117
Ubiquitin regulatory domain X (UBX) found in UBX domain protein 4 (UBXN4) and similar proteins; ...
 318-394 9.14e-45

Ubiquitin regulatory domain X (UBX) found in UBX domain protein 4 (UBXN4) and similar proteins; UBXN4, also termed ERAD (endoplasmic-reticulum-associated protein degradation) substrate erasing protein (erasin), or UBX domain-containing protein 2 (UBXD2), or UBXDC1, belongs to the UBXD family of proteins that contains the ubiquitin regulatory domain X (UBX) with a beta-grasp ubiquitin-like fold, but without the C-terminal double glycine motif. UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. UBXN4 is an endoplasmic reticulum (ER) localized protein that interacts with p97 (also known as VCP or Cdc48) via its UBX domain. Erasin exists in a complex with other p97/VCP-associated factors involved in endoplasmic-reticulum-associated protein degradation (ERAD). p97 is a homohexameric AAA ATPase (ATPase associated with a variety of activities) involved in a variety of functions ranging from cell-cycle regulation to membrane fusion and protein degradation. The overexpression of UBXN4 increases degradation of a classical ERAD substrate and UBXN4 levels are increased in ER stressed cells. Anti-UBXN4 staining is increased in neuropathological lesions in brains of patients with Alzheimer's disease.


Pssm-ID: 340534 [Multi-domain]  Cd Length: 77  Bit Score: 151.71  E-value: 9.14e-45
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1252414522 318 IARIQFRLPDGSSFTNQFPSDAPLEEARQFAAQTVGNTYGNFSLATMFPRREFTREDYKRRLLDLELAPSASVVLLP 394
Cdd:cd16117     1 TARIQFRLPDGSSFTNQFPSDAPLEEARQFVAQTVGPAYGPFSLATTFPRREFTDDDYQKTLLELELAPSAALVVLP 77
UBX smart00166
Domain present in ubiquitin-regulatory proteins; Present in FAF1 and Shp1p.
 319-394 5.77e-23

Domain present in ubiquitin-regulatory proteins; Present in FAF1 and Shp1p.


Pssm-ID: 197552 [Multi-domain]  Cd Length: 77  Bit Score: 92.37  E-value: 5.77e-23
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1252414522  319 ARIQFRLPDGSSFTNQFPSDAPLEEARQF--AAQTVGNTygNFSLATMFPRREFTREDYKRRLLDLELAPSASVVLLP 394
Cdd:smart00166   2 CRLQIRLPDGSRLVRRFPSSDTLRTVYEFvsAALGDGND--PFTLNSPFPRRTFTKDDYSKKLLELALLPSSTLVLEP 77
UBX pfam00789
UBX domain; This domain is present in ubiquitin-regulatory proteins and is a general ...
 319-394 3.59e-21

UBX domain; This domain is present in ubiquitin-regulatory proteins and is a general Cdc48-interacting module.


Pssm-ID: 395637 [Multi-domain]  Cd Length: 80  Bit Score: 87.35  E-value: 3.59e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1252414522 319 ARIQFRLPDGSSFTNQFPSDAPLEEARQF-AAQTVGNTYgNFSLATMFPRREFTREDYKRRLLDLELAPSASVVLLP 394
Cdd:pfam00789   5 TRLQIRLPDGSRLVRRFNSSDKLQTVYDFvDSNRYDDLE-PFSLNTPFPRRPLTDLDYSKTLKEAGLLPNSTLVLEP 80
UAS cd02958
UAS family; UAS is a domain of unknown function. Most members of this family are ...
 4-113 3.00e-04

UAS family; UAS is a domain of unknown function. Most members of this family are uncharacterized proteins with similarity to FAS-associated factor 1 (FAF1) and ETEA because of the presence of a UAS domain N-terminal to a ubiquitin-associated UBX domain. FAF1 is a longer protein, compared to the other members of this family, having additional N-terminal domains, a ubiquitin-associated UBA domain and a nuclear targeting domain. FAF1 is an apoptotic signaling molecule that acts downstream in the Fas signal transduction pathway. It interacts with the cytoplasmic domain of Fas, but not to a Fas mutant that is deficient in signal transduction. ETEA is the protein product of a highly expressed gene in T-cells and eosinophils of atopic dermatitis patients. The presence of the ubiquitin-associated UBX domain in the proteins of this family suggests the possibility of their involvement in ubiquitination. Recently, FAF1 has been shown to interact with valosin-containing protein (VCP), which is involved in the ubiquitin-proteosome pathway. Some members of this family are uncharacterized proteins containing only a UAS domain.


Pssm-ID: 239256 [Multi-domain]  Cd Length: 114  Bit Score: 40.28  E-value: 3.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414522   4 FQGAIPAAIASAKRSGAVFVVFVAGDDEQSIQMAAS--WEDEKVTQASSNNFVAIKID-TKSEAcLQFSQIYPVVCVPSS 80
Cdd:cd02958     2 FQGSFEDAKQEAKSEKKWLLVYLQSEDEFDSQVLNRdlWSNESVKEFIRENFIFWQCDiDSSEG-QRFLQSYKVDKYPHI 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1252414522  81 FFIG-DSGIPLEVIAGSVSADELVTRIHKVQQMH 113
Cdd:cd02958    81 AIIDpRTGEVLKVWSGNITPEDLLSQLIEFLEEF 114
DsbD COG4232
Thiol:disulfide interchange protein DsbD [Posttranslational modification, protein turnover, ...
 2-111 7.00e-03

Thiol:disulfide interchange protein DsbD [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443376 [Multi-domain]  Cd Length: 416  Bit Score: 38.63  E-value: 7.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414522   2 LWFQGAIPAAIASAKRSG-AVFVVFVAgdD--------EQSIqmaasWEDEKVTQASSNNFVAIKIDT--KSEACLQFSQ 70
Cdd:COG4232   303 LAWQADLEAALAEARAEGkPVFVDFTA--DwcvtckenERTV-----FSDPEVQAALADDVVLLKADVtdNDPEITALLK 375

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1252414522  71 IYPVVCVPSSFFIGDSGIPLEVIAGSVSADELVTRIHKVQQ 111
Cdd:COG4232   376 RFGRFGVPTYVFYDPDGEELPRLGFMLTADEFLAALEKAKG 416
 
Name Accession Description Interval E-value
UBX_UBXN4 cd16117
Ubiquitin regulatory domain X (UBX) found in UBX domain protein 4 (UBXN4) and similar proteins; ...
 318-394 9.14e-45

Ubiquitin regulatory domain X (UBX) found in UBX domain protein 4 (UBXN4) and similar proteins; UBXN4, also termed ERAD (endoplasmic-reticulum-associated protein degradation) substrate erasing protein (erasin), or UBX domain-containing protein 2 (UBXD2), or UBXDC1, belongs to the UBXD family of proteins that contains the ubiquitin regulatory domain X (UBX) with a beta-grasp ubiquitin-like fold, but without the C-terminal double glycine motif. UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. UBXN4 is an endoplasmic reticulum (ER) localized protein that interacts with p97 (also known as VCP or Cdc48) via its UBX domain. Erasin exists in a complex with other p97/VCP-associated factors involved in endoplasmic-reticulum-associated protein degradation (ERAD). p97 is a homohexameric AAA ATPase (ATPase associated with a variety of activities) involved in a variety of functions ranging from cell-cycle regulation to membrane fusion and protein degradation. The overexpression of UBXN4 increases degradation of a classical ERAD substrate and UBXN4 levels are increased in ER stressed cells. Anti-UBXN4 staining is increased in neuropathological lesions in brains of patients with Alzheimer's disease.


Pssm-ID: 340534 [Multi-domain]  Cd Length: 77  Bit Score: 151.71  E-value: 9.14e-45
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1252414522 318 IARIQFRLPDGSSFTNQFPSDAPLEEARQFAAQTVGNTYGNFSLATMFPRREFTREDYKRRLLDLELAPSASVVLLP 394
Cdd:cd16117     1 TARIQFRLPDGSSFTNQFPSDAPLEEARQFVAQTVGPAYGPFSLATTFPRREFTDDDYQKTLLELELAPSAALVVLP 77
UBX smart00166
Domain present in ubiquitin-regulatory proteins; Present in FAF1 and Shp1p.
 319-394 5.77e-23

Domain present in ubiquitin-regulatory proteins; Present in FAF1 and Shp1p.


Pssm-ID: 197552 [Multi-domain]  Cd Length: 77  Bit Score: 92.37  E-value: 5.77e-23
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1252414522  319 ARIQFRLPDGSSFTNQFPSDAPLEEARQF--AAQTVGNTygNFSLATMFPRREFTREDYKRRLLDLELAPSASVVLLP 394
Cdd:smart00166   2 CRLQIRLPDGSRLVRRFPSSDTLRTVYEFvsAALGDGND--PFTLNSPFPRRTFTKDDYSKKLLELALLPSSTLVLEP 77
UBX pfam00789
UBX domain; This domain is present in ubiquitin-regulatory proteins and is a general ...
 319-394 3.59e-21

UBX domain; This domain is present in ubiquitin-regulatory proteins and is a general Cdc48-interacting module.


Pssm-ID: 395637 [Multi-domain]  Cd Length: 80  Bit Score: 87.35  E-value: 3.59e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1252414522 319 ARIQFRLPDGSSFTNQFPSDAPLEEARQF-AAQTVGNTYgNFSLATMFPRREFTREDYKRRLLDLELAPSASVVLLP 394
Cdd:pfam00789   5 TRLQIRLPDGSRLVRRFNSSDKLQTVYDFvDSNRYDDLE-PFSLNTPFPRRPLTDLDYSKTLKEAGLLPNSTLVLEP 80
UBX cd01767
Ubiquitin regulatory domain X (UBX) structurally similar to a beta-grasp ubiquitin-like fold; ...
 320-392 1.91e-20

Ubiquitin regulatory domain X (UBX) structurally similar to a beta-grasp ubiquitin-like fold; The UBXD family of proteins contains the ubiquitin regulatory domain X (UBX) with a beta-grasp ubiquitin-like fold, but without the C-terminal double glycine motif. UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. Members in this family function as cofactors of p97 (also known as VCP or Cdc48), which is a homohexameric AAA ATPase (ATPase associated with a variety of activities) involved in a variety of functions ranging from cell-cycle regulation to membrane fusion and protein degradation. Based on domain composition, UBXD proteins can be divided into two main groups, with and without ubiquitin-associated (UBA) domain.


Pssm-ID: 340466 [Multi-domain]  Cd Length: 74  Bit Score: 85.39  E-value: 1.91e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1252414522 320 RIQFRLPDGSSFTNQFPSDAPLEEARQFAAQTVGNTYGNFSLATMFPRREFTREDYKRRLLDLELAPSASVVL 392
Cdd:cd01767     1 RIQIRLPDGSRIQRRFSKSDTLQDLYDFVESNLGDSPSSFSLVTSFPRRVLTDEDSDKTLEELGLTPNAVLFV 73
UBX_UBXN1 cd01772
Ubiquitin regulatory domain X (UBX) found in UBX domain protein 1 (UBXN1) and similar proteins; ...
 319-392 9.61e-15

Ubiquitin regulatory domain X (UBX) found in UBX domain protein 1 (UBXN1) and similar proteins; UBXN1, also termed SAPK substrate protein 1 (SAKS1), UBA/UBX 33.3 kDa protein (Y33K), or UBXD10, is a widely expressed protein containing an N-terminal ubiquitin-associated (UBA) domain, a coiled-coil region, and a C-terminal ubiquitin-like (Ubl or UBX) domain that has a beta-grasp ubiquitin-like fold without the C-terminal double glycine motif. UBXN1 has been identified as a substrate for stress-activated protein kinases (SAPKs). It binds polyubiquitin and valosin-containing protein (VCP), suggesting a role as an adaptor that directs VCP to polyubiquitinated proteins facilitating its destruction by the proteasome. In addition, UBXN1 specifically binds to Homer2b. It may also interact with ubiquitin (Ub) and be involved in the Ub-proteasome proteolytic pathways. UBXN1 can also associate with autoubiquitinated BRCA1 tumor suppressor and inhibit its enzymatic function through its UBA domains.


Pssm-ID: 340470 [Multi-domain]  Cd Length: 81  Bit Score: 69.26  E-value: 9.61e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1252414522 319 ARIQFRLPDGSSFTNQFPSDAPLEEARQFAAQTVGNTYGNFSLATMFPRREFTREDYKRRLLDLELAPSASVVL 392
Cdd:cd01772     7 CRLQVRLTNGSTLTQTFGAKEQLAAVRLYVELNRTDGDGPFSLMTTFPRKVFTEEDMEKPLKELGLVPSAVLIV 80
UBX_UBXN2 cd01770
Ubiquitin regulatory domain X (UBX) found in UBX domain-containing proteins UBXN2A, UBXN2B, ...
 320-374 4.28e-08

Ubiquitin regulatory domain X (UBX) found in UBX domain-containing proteins UBXN2A, UBXN2B, NSFL1C/UBXN2C, and similar proteins; This family includes UBX domain-containing proteins UBXN2A, UBXN2B, and NSFL1C/UBXN2C, which contain a SEP (Saccharomyces cerevisiae Shp1, Drosophila melanogaster eyes closed gene (eyc), and vertebrate p47) domain, and a ubiquitin regulatory domain X (UBX) with a beta-grasp ubiquitin-like fold at the C-terminus. UBX domain participates broadly in the regulation of protein degradation. UBXN2A, UBXN2B, and UBXN2C function as the adaptor proteins of p97 (also known as VCP or Cdc48), which is a homohexameric AAA ATPase (ATPase associated with a variety of activities) involved in a variety of functions ranging from cell-cycle regulation to membrane fusion and protein degradation.


Pssm-ID: 340468  Cd Length: 71  Bit Score: 50.26  E-value: 4.28e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1252414522 320 RIQFRLPDGSSFTNQFPSDAPLEEARQFAAQTVGNTYGNFSLATMFPRREFTRED 374
Cdd:cd01770     1 SIQIRLADGSRLVARFNLTHTVGDIRQFIDSARPGYSRPFVLMTGFPPKELTDES 55
UBX_UBXN3A cd01771
Ubiquitin regulatory domain X (UBX) found in FAS associated factor 1 (FAF1, also known as ...
 318-392 4.93e-06

Ubiquitin regulatory domain X (UBX) found in FAS associated factor 1 (FAF1, also known as UBXN3A) and similar proteins; UBX domain-containing protein 3A (UBXN3A),also termed UBX domain-containing protein 12 (UBXD12), or FAF1, belongs to the UBXD family of proteins that contains the ubiquitin regulatory domain X (UBX) with a beta-grasp ubiquitin-like fold, but without the C-terminal double glycine motif. UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. In addition, FAF1 contains two tandem ubiquitin-like (Ubl) domains, which shows high structural similarity with UBX domain. FAF1 functions as a cofactor of p97 (also known as VCP or Cdc48), which is a homohexameric AAA ATPase (ATPase associated with a variety of activities) involved in a variety of functions ranging from cell-cycle regulation to membrane fusion and protein degradation. The FAF1-p97 complex inhibits the proteasomal protein degradation in which p97 acts as a co-chaperone. Moreover, FAF1 is an apoptotic signaling molecule that acts downstream in the Fas signal transduction pathway. It interacts with the cytoplasmic domain of Fas, but not to a Fas mutant that is deficient in signal transduction. FAF1 is widely expressed in adult and embryonic tissues, and in tumor cell lines, and is localized not only in the cytoplasm where it interacts with Fas, but also in the nucleus. FAF1 contains phosphorylation sites for protein kinase CK2 within the nuclear targeting domain. Phosphorylation influences nuclear localization of FAF1 but does not affect its potentiation of Fas-induced apoptosis. Other functions have also been attributed to FAF1. It inhibits nuclear factor-kappaB (NF-kappaB) by interfering with the nuclear translocation of the p65 subunit. Although the precise role of FAF1 in the ubiquitination pathway remains unclear, FAF1 interacts with valosin-containing protein (VCP), which is involved in the ubiquitin-proteosome pathway. This family corresponds to UBX domain.


Pssm-ID: 340469  Cd Length: 80  Bit Score: 44.53  E-value: 4.93e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1252414522 318 IARIQFRLPDGSSFTNQFPSDAPLEEARQFAAqTVGNTYGNFSLATMFPRREFTREDYKRRLLDLELAPSASVVL 392
Cdd:cd01771     4 ISKLRFRLPGGEFLTRRFLASEPLQVLLNFVA-SKGYPPDEYKLLTTFPRRDLTQLDPSKTLEELKLFPQETLFL 77
UBX_UBXN7 cd01773
Ubiquitin regulatory domain X (UBX) found in UBX domain protein 7 (UBXN7) and similar proteins; ...
 319-390 2.38e-05

Ubiquitin regulatory domain X (UBX) found in UBX domain protein 7 (UBXN7) and similar proteins; UBXN7, also termed UBX domain-containing protein 7 (UBXD7), belongs to the UBXD family of proteins that contains the ubiquitin regulatory domain X (UBX) with a beta-grasp ubiquitin-like fold, but without the C-terminal double glycine motif. UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. UBXN7 functions as a ubiquitin-binding adaptor that mediates the interaction between the AAA+ ATPase p97 (also known as VCP or Cdc48) and the transcription factor HIF1-alpha. It binds only to the active, NEDD8- or Rub1-modified form of cullins. In addition to having a UBX domain, UBXD7 contains a ubiquitin-associated (UBA), ubiquitin-associating (UAS), and ubiquitin-interacting motif (UIM) domains. Either UBA or UIM could serve as a docking site for neddylated-cullins. UBA domain is required for binding ubiquitylated-protein substrates, while the UIM motif is responsible for the binding to cullin RING ligases (CRLs), and the UBX domain is essential for p97 binding.


Pssm-ID: 340471  Cd Length: 76  Bit Score: 42.62  E-value: 2.38e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1252414522 319 ARIQFRLPDGSSFTNQFPSDAPLEEARQFAaQTVGNTYGNFSLATMFPRREFTREDYKRRLLDLELAPSASV 390
Cdd:cd01773     2 SKLMLRFPDGKREQLSLPASAKLKALVKYV-SSKGYPNERYELVTNFPRRKLSHLDYDITLKEAGLCPQETI 72
UAS cd02958
UAS family; UAS is a domain of unknown function. Most members of this family are ...
 4-113 3.00e-04

UAS family; UAS is a domain of unknown function. Most members of this family are uncharacterized proteins with similarity to FAS-associated factor 1 (FAF1) and ETEA because of the presence of a UAS domain N-terminal to a ubiquitin-associated UBX domain. FAF1 is a longer protein, compared to the other members of this family, having additional N-terminal domains, a ubiquitin-associated UBA domain and a nuclear targeting domain. FAF1 is an apoptotic signaling molecule that acts downstream in the Fas signal transduction pathway. It interacts with the cytoplasmic domain of Fas, but not to a Fas mutant that is deficient in signal transduction. ETEA is the protein product of a highly expressed gene in T-cells and eosinophils of atopic dermatitis patients. The presence of the ubiquitin-associated UBX domain in the proteins of this family suggests the possibility of their involvement in ubiquitination. Recently, FAF1 has been shown to interact with valosin-containing protein (VCP), which is involved in the ubiquitin-proteosome pathway. Some members of this family are uncharacterized proteins containing only a UAS domain.


Pssm-ID: 239256 [Multi-domain]  Cd Length: 114  Bit Score: 40.28  E-value: 3.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414522   4 FQGAIPAAIASAKRSGAVFVVFVAGDDEQSIQMAAS--WEDEKVTQASSNNFVAIKID-TKSEAcLQFSQIYPVVCVPSS 80
Cdd:cd02958     2 FQGSFEDAKQEAKSEKKWLLVYLQSEDEFDSQVLNRdlWSNESVKEFIRENFIFWQCDiDSSEG-QRFLQSYKVDKYPHI 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1252414522  81 FFIG-DSGIPLEVIAGSVSADELVTRIHKVQQMH 113
Cdd:cd02958    81 AIIDpRTGEVLKVWSGNITPEDLLSQLIEFLEEF 114
UBX_UBXN10 cd17076
Ubiquitin regulatory domain X (UBX) found in UBX domain protein 10 (UBXN10) and similar ...
 324-393 1.93e-03

Ubiquitin regulatory domain X (UBX) found in UBX domain protein 10 (UBXN10) and similar proteins; UBXN10, also termed UBX domain-containing protein 3 (UBXD3), belongs to the UBXD family of proteins that contains the ubiquitin regulatory domain X (UBX) with a beta-grasp ubiquitin-like fold, but without the C-terminal double glycine motif. UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. UBXN10 functions as a cofactor of p97 (also known as VCP or Cdc48), which is a homohexameric AAA ATPase (ATPase associated with a variety of activities) involved in a variety of functions ranging from cell-cycle regulation to membrane fusion and protein degradation. UBXN10 localizes to cilia in a p97-dependent manner, and both p97 and UBXN10 are required for ciliogenesis. Additionally, UBXN10 interacts with the intraflagellar transport B (IFT-B) and regulates anterograde transport into cilia.


Pssm-ID: 340596  Cd Length: 76  Bit Score: 37.22  E-value: 1.93e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1252414522 324 RLPDGSSFTNQF-PSDApLEEARQFAAQTVGNTYGNFSLATM-FPRREFTreDYKRRLLDLELaPSASVVLL 393
Cdd:cd17076     8 RLPDGQRFQRFFrPSDT-LQDVLAFAESQSGLDLSNCIIETNeVPRRVFS--DLSKTIAECGI-QDKTVLYI 75
UBX_UBXN2B cd17161
Ubiquitin regulatory domain X (UBX) found in UBX domain protein 2B (UBXN2B) and similar ...
 320-382 2.62e-03

Ubiquitin regulatory domain X (UBX) found in UBX domain protein 2B (UBXN2B) and similar proteins; UBXN2B, also termed NSFL1 cofactor p37, or p97 cofactor p37, belongs to the UBXD family of proteins that contains the ubiquitin regulatory domain X (UBX) with a beta-grasp ubiquitin-like fold, but without the C-terminal double glycine motif. UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. UBXN2B is an adaptor protein of p97 (also known as VCP or Cdc48), which is a homohexameric AAA ATPase (ATPase associated with a variety of activities) involved in a variety of functions ranging from cell-cycle regulation to membrane fusion and protein degradation. UBXN2B forms a tight complex with p97 in the cytosol and localizes to the Golgi and endoplasmic reticulum (ER).


Pssm-ID: 340681  Cd Length: 82  Bit Score: 36.79  E-value: 2.62e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1252414522 320 RIQFRLPDGSSFTNQFPSDAPLEEARQFAAQTVGN-TYGNFSLATMFPRREFTREDYKRRLLDL 382
Cdd:cd17161     9 KIQIRLADGSRLIQRFNQSHRIHDIRQFIVQSRPVfAASDFLLVTTFPNKELTDESQTLQEADI 72
UBX_UBXN2C cd17162
Ubiquitin regulatory domain X (UBX) found in NSFL1 cofactor (also known as UBX ...
 314-374 3.89e-03

Ubiquitin regulatory domain X (UBX) found in NSFL1 cofactor (also known as UBX domain-containing protein 2C (UBXN2C) and similar proteins; UBXN2C, also termed NSFL1C, or NSFL1 cofactor p47, or p97 cofactor p47, UBX1, or UBXD10, belongs to the UBXD family of proteins that contains the ubiquitin regulatory domain X (UBX) with a beta-grasp ubiquitin-like fold, but without the C-terminal double glycine motif. UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. UBXN2C is a major adaptor of p97 (also known as VCP or Cdc48), which is a homohexameric AAA ATPase (ATPase associated with a variety of activities) involved in a variety of functions ranging from cell-cycle regulation to membrane fusion and protein degradation. The main role of the UBXN2C/p97 complex is in regulation of membrane fusion events. It plays an essential role in the reassembly of Golgi stacks at the end of mitosis. UBXN2C also functions as an essential factor for Golgi membrane fusion, which associates with the nuclear factor-kappaB essential modulator (NEMO) subunit of the IkappaB kinase (IKK) complex upon tumor necrosis factor (TNF)-alpha or interleukin (IL)-1 stimulation, induces the lysosome-dependent degradation of polyubiquitinated NEMO without p97, and thus inhibits IKK activation. Moreover, UBXN2C regulates a membrane fusion process, which is required by the maintenance of the endoplasmic reticulum (ER) network, through phosphorylation by Cdc2 kinase.


Pssm-ID: 340682  Cd Length: 82  Bit Score: 36.45  E-value: 3.89e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1252414522 314 DRSTIARIQFRLPDGSSFTNQFPSDAPLEEARQFAAQT-VGNTYGNFSLATMFPRREFTRED 374
Cdd:cd17162     3 DSEPVTNIQIRLADGGRLVQKFNHSHRIRDIRLFIVDArPAMAATSFVLMTTFPNKELTDEN 64
DsbD COG4232
Thiol:disulfide interchange protein DsbD [Posttranslational modification, protein turnover, ...
 2-111 7.00e-03

Thiol:disulfide interchange protein DsbD [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443376 [Multi-domain]  Cd Length: 416  Bit Score: 38.63  E-value: 7.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414522   2 LWFQGAIPAAIASAKRSG-AVFVVFVAgdD--------EQSIqmaasWEDEKVTQASSNNFVAIKIDT--KSEACLQFSQ 70
Cdd:COG4232   303 LAWQADLEAALAEARAEGkPVFVDFTA--DwcvtckenERTV-----FSDPEVQAALADDVVLLKADVtdNDPEITALLK 375

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1252414522  71 IYPVVCVPSSFFIGDSGIPLEVIAGSVSADELVTRIHKVQQ 111
Cdd:COG4232   376 RFGRFGVPTYVFYDPDGEELPRLGFMLTADEFLAALEKAKG 416
 
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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