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Conserved domains on  [gi|5805208|gb|AAD51886|]
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fas-associated factor 1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
UAS_FAF1 cd02990
UAS family, FAS-associated factor 1 (FAF1) subfamily; FAF1 contains a UAS domain of unknown ...
352-487 8.05e-88

UAS family, FAS-associated factor 1 (FAF1) subfamily; FAF1 contains a UAS domain of unknown function N-terminal to a ubiquitin-associated UBX domain. FAF1 also contains ubiquitin-associated UBA and nuclear targeting domains, N-terminal to the UAS 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. It 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-kB (NF-kB) by interfering with the nuclear translocation of the p65 subunit. FAF1 also interacts with valosin-containing protein (VCP), which is involved in the ubiquitin-proteosome pathway.


:

Pssm-ID: 239288  Cd Length: 136  Bit Score: 269.75  E-value: 8.05e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5805208  352 FFIGSLEAAFQEAFYVKARDRKLLAIYLHHDESVLTNVFCSQMLCAESIVSYLSQNFITWAWDLTKDSNRARFLTMCNRH 431
Cdd:cd02990   1 FFIGSLEAAFQEACYRKARDRKLLAIYLHHDESVLSNVFCSQLLCAESIVQYLSQNFITWGWDMTKESNKARFLSSCTRH 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 5805208  432 FGSVVAQTIRTQKTDQKPLFLIIMGKRSSNEVLNVIQGNTTVDELMMRLMAAMEIF 487
Cdd:cd02990  81 FGSVAAQTIRNIKTDQLPAILIIMGKRSSNEVLNVIQGNTGVDELLMRLIEAMEMF 136
UBX_UBXN3A cd01771
Ubiquitin regulatory domain X (UBX) found in FAS associated factor 1 (FAF1, also known as ...
571-649 3.56e-46

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: 157.77  E-value: 3.56e-46
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5805208  571 EPVSKLRIRTPSGEFLERRFLASNKLQIVFDFVASKGFPWDEYKLLSTFPRRDVTQLDPNKSLLEVKLFPQETLFLEAK 649
Cdd:cd01771   2 EPISKLRFRLPGGEFLTRRFLASEPLQVLLNFVASKGYPPDEYKLLTTFPRRDLTQLDPSKTLEELKLFPQETLFLEER 80
Ubl_FAF1 cd17056
ubiquitin-like (Ubl) domain found in FAS-associated factor 1 (FAF1) and similar proteins; FAF1, ...
195-268 6.50e-44

ubiquitin-like (Ubl) domain found in FAS-associated factor 1 (FAF1) and similar proteins; FAF1, also termed UBX domain-containing protein 12 (UBXD12), or UBX domain-containing protein 3A (UBXN3A), belongs to the UBXD family of proteins that contains the ubiquitin regulatory domain X (UBX) with a beta-grasp ubiquitin-like (Ubl) 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 Ubl domains, which show 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 Ubl domains.


:

Pssm-ID: 340576  Cd Length: 71  Bit Score: 151.43  E-value: 6.50e-44
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5805208  195 MLIITHRevQREYNLNFSGSSTIQEVKRNVYDLTSIPVRHQLWEGWPTSATDDSMCLaESGLSYPCHRLTVGRR 268
Cdd:cd17056   1 DFRVEYR--DRNVDVVLEDTCTVGEIKQILENELQIPVSKMLLKGWKTGDVEDSTVL-KSLHLPKNNSLYVLTP 71
Ubl1_FAF1 cd17129
ubiquitin-like (Ubl) domain 1 found in FAS-associated factor 1 (FAF1) and similar proteins; ...
100-172 1.53e-38

ubiquitin-like (Ubl) domain 1 found in FAS-associated factor 1 (FAF1) and similar proteins; FAF1, also termed UBX domain-containing protein 12 (UBXD12), or UBX domain-containing protein 3A (UBXN3A), belongs to the UBXD family of proteins that contains the ubiquitin (Ub) regulatory domain X (UBX) with a beta-grasp ubiquitin-like (Ubl) fold, but without the C-terminal double glycine motif. The 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 Ubl domains, which show high structural similarity with the 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. The family corresponds to the first Ubl domain.


:

Pssm-ID: 340649  Cd Length: 73  Bit Score: 136.62  E-value: 1.53e-38
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5805208  100 MLDFRVEYRDRNVDVVLEDTCTVGEIKQILENELQIPVSKMLLKGWKTGDVEDSTVLKSLHLPKNNSLYVLTP 172
Cdd:cd17129   1 MLTFNVEYRDRTIDVVLPDTETVGDIKQILENELGIPPCKQILKGWKARTVSDSTVLRSLHLPKENSLYLLTP 73
UBA_FAF1 cd14413
UBA-like domain found in FAS-associated factor 1 (FAF1) and similar proteins; FAF1, also ...
14-46 2.95e-16

UBA-like domain found in FAS-associated factor 1 (FAF1) and similar proteins; FAF1, also called UBX domain-containing protein 12 or UBX domain-containing protein 3A, is a multi-functional Fas associating protein that contains an N-terminal ubiquitin-associated (UBA)-like domain, UAS and ubiquitin-like (UBX) domains, p150 subunit of a chromatin assembly factor like domain (CAF) and a novel nuclear localization signal (NLS). 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.


:

Pssm-ID: 270596  Cd Length: 33  Bit Score: 72.37  E-value: 2.95e-16
                        10        20        30
                ....*....|....*....|....*....|...
gi 5805208   14 FQACTGIENIDEAITLLEQNNWDLVAAINGVIP 46
Cdd:cd14413   1 FQACTGIEDIDECIMLLEQNNWNLVAAVNAVIP 33
Mitofilin super family cl26613
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
490-595 9.15e-05

Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.


The actual alignment was detected with superfamily member pfam09731:

Pssm-ID: 430783 [Multi-domain]  Cd Length: 618  Bit Score: 45.52  E-value: 9.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5805208    490 QQQEDIKDGDEREARENVKrEQDEAYRlslEADRAKREAREREMAEQfrLEQIRKEQEEEREAIRLSLEQALPPEPKEEN 569
Cdd:pfam09731 301 KKLAELKKREEKHIERALE-KQKEELD---KLAEELSARLEEVRAAD--EAQLRLEFEREREEIRESYEEKLRTELERQA 374
                          90       100
                  ....*....|....*....|....*...
gi 5805208    570 AEPVSKLR--IRTPSGEfLERRFLASNK 595
Cdd:pfam09731 375 EAHEEHLKdvLVEQEIE-LQREFLQDIK 401
 
Name Accession Description Interval E-value
UAS_FAF1 cd02990
UAS family, FAS-associated factor 1 (FAF1) subfamily; FAF1 contains a UAS domain of unknown ...
352-487 8.05e-88

UAS family, FAS-associated factor 1 (FAF1) subfamily; FAF1 contains a UAS domain of unknown function N-terminal to a ubiquitin-associated UBX domain. FAF1 also contains ubiquitin-associated UBA and nuclear targeting domains, N-terminal to the UAS 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. It 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-kB (NF-kB) by interfering with the nuclear translocation of the p65 subunit. FAF1 also interacts with valosin-containing protein (VCP), which is involved in the ubiquitin-proteosome pathway.


Pssm-ID: 239288  Cd Length: 136  Bit Score: 269.75  E-value: 8.05e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5805208  352 FFIGSLEAAFQEAFYVKARDRKLLAIYLHHDESVLTNVFCSQMLCAESIVSYLSQNFITWAWDLTKDSNRARFLTMCNRH 431
Cdd:cd02990   1 FFIGSLEAAFQEACYRKARDRKLLAIYLHHDESVLSNVFCSQLLCAESIVQYLSQNFITWGWDMTKESNKARFLSSCTRH 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 5805208  432 FGSVVAQTIRTQKTDQKPLFLIIMGKRSSNEVLNVIQGNTTVDELMMRLMAAMEIF 487
Cdd:cd02990  81 FGSVAAQTIRNIKTDQLPAILIIMGKRSSNEVLNVIQGNTGVDELLMRLIEAMEMF 136
UBX_UBXN3A cd01771
Ubiquitin regulatory domain X (UBX) found in FAS associated factor 1 (FAF1, also known as ...
571-649 3.56e-46

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: 157.77  E-value: 3.56e-46
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5805208  571 EPVSKLRIRTPSGEFLERRFLASNKLQIVFDFVASKGFPWDEYKLLSTFPRRDVTQLDPNKSLLEVKLFPQETLFLEAK 649
Cdd:cd01771   2 EPISKLRFRLPGGEFLTRRFLASEPLQVLLNFVASKGYPPDEYKLLTTFPRRDLTQLDPSKTLEELKLFPQETLFLEER 80
Ubl_FAF1 cd17056
ubiquitin-like (Ubl) domain found in FAS-associated factor 1 (FAF1) and similar proteins; FAF1, ...
195-268 6.50e-44

ubiquitin-like (Ubl) domain found in FAS-associated factor 1 (FAF1) and similar proteins; FAF1, also termed UBX domain-containing protein 12 (UBXD12), or UBX domain-containing protein 3A (UBXN3A), belongs to the UBXD family of proteins that contains the ubiquitin regulatory domain X (UBX) with a beta-grasp ubiquitin-like (Ubl) 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 Ubl domains, which show 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 Ubl domains.


Pssm-ID: 340576  Cd Length: 71  Bit Score: 151.43  E-value: 6.50e-44
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5805208  195 MLIITHRevQREYNLNFSGSSTIQEVKRNVYDLTSIPVRHQLWEGWPTSATDDSMCLaESGLSYPCHRLTVGRR 268
Cdd:cd17056   1 DFRVEYR--DRNVDVVLEDTCTVGEIKQILENELQIPVSKMLLKGWKTGDVEDSTVL-KSLHLPKNNSLYVLTP 71
Ubl1_FAF1 cd17129
ubiquitin-like (Ubl) domain 1 found in FAS-associated factor 1 (FAF1) and similar proteins; ...
100-172 1.53e-38

ubiquitin-like (Ubl) domain 1 found in FAS-associated factor 1 (FAF1) and similar proteins; FAF1, also termed UBX domain-containing protein 12 (UBXD12), or UBX domain-containing protein 3A (UBXN3A), belongs to the UBXD family of proteins that contains the ubiquitin (Ub) regulatory domain X (UBX) with a beta-grasp ubiquitin-like (Ubl) fold, but without the C-terminal double glycine motif. The 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 Ubl domains, which show high structural similarity with the 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. The family corresponds to the first Ubl domain.


Pssm-ID: 340649  Cd Length: 73  Bit Score: 136.62  E-value: 1.53e-38
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5805208  100 MLDFRVEYRDRNVDVVLEDTCTVGEIKQILENELQIPVSKMLLKGWKTGDVEDSTVLKSLHLPKNNSLYVLTP 172
Cdd:cd17129   1 MLTFNVEYRDRTIDVVLPDTETVGDIKQILENELGIPPCKQILKGWKARTVSDSTVLRSLHLPKENSLYLLTP 73
UAS smart00594
UAS domain;
339-481 3.52e-33

UAS domain;


Pssm-ID: 214737 [Multi-domain]  Cd Length: 122  Bit Score: 123.59  E-value: 3.52e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5805208     339 AEFSSRYGdchPVFFIGSLEAAFQEAFyvkaRDRKLLAIYLHHDESVLTNVFCSQMLCAESIVSYLSQNFITWAWDLTKD 418
Cdd:smart00594   1 KLFRPPYG---PLFYQGSLEAAKQEAS----RQRRLLWLYLHSQDSPDSQVFNRDVLCNEAVKSLIRENFIFWQVDVDTS 73
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5805208     419 SNRARFLTMcnrhfgsvvaqtirtqKTDQKPLFLIIMGKR--SSNEVLNVIQGNTTVDELMMRLM 481
Cdd:smart00594  74 EGQRVSQFY----------------KLDSFPYVAIVDPRTgqRVIEWVGVVEGEISPEELMTFLE 122
UBX pfam00789
UBX domain; This domain is present in ubiquitin-regulatory proteins and is a general ...
570-647 1.90e-25

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: 100.06  E-value: 1.90e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5805208    570 AEPVSKLRIRTPSGEFLERRFLASNKLQIVFDFVASKGFPWDE-YKLLSTFPRRDVTQLDPNKSLLEVKLFPQETLFLE 647
Cdd:pfam00789   1 AEDVTRLQIRLPDGSRLVRRFNSSDKLQTVYDFVDSNRYDDLEpFSLNTPFPRRPLTDLDYSKTLKEAGLLPNSTLVLE 79
UBX smart00166
Domain present in ubiquitin-regulatory proteins; Present in FAF1 and Shp1p.
573-648 5.05e-24

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


Pssm-ID: 197552 [Multi-domain]  Cd Length: 77  Bit Score: 95.83  E-value: 5.05e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5805208     573 VSKLRIRTPSGEFLERRFLASNKLQIVFDFV-ASKGFPWDEYKLLSTFPRRDVTQLDPNKSLLEVKLFPQETLFLEA 648
Cdd:smart00166   1 VCRLQIRLPDGSRLVRRFPSSDTLRTVYEFVsAALGDGNDPFTLNSPFPRRTFTKDDYSKKLLELALLPSSTLVLEP 77
UBA_FAF1 cd14413
UBA-like domain found in FAS-associated factor 1 (FAF1) and similar proteins; FAF1, also ...
14-46 2.95e-16

UBA-like domain found in FAS-associated factor 1 (FAF1) and similar proteins; FAF1, also called UBX domain-containing protein 12 or UBX domain-containing protein 3A, is a multi-functional Fas associating protein that contains an N-terminal ubiquitin-associated (UBA)-like domain, UAS and ubiquitin-like (UBX) domains, p150 subunit of a chromatin assembly factor like domain (CAF) and a novel nuclear localization signal (NLS). 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.


Pssm-ID: 270596  Cd Length: 33  Bit Score: 72.37  E-value: 2.95e-16
                        10        20        30
                ....*....|....*....|....*....|...
gi 5805208   14 FQACTGIENIDEAITLLEQNNWDLVAAINGVIP 46
Cdd:cd14413   1 FQACTGIEDIDECIMLLEQNNWNLVAAVNAVIP 33
UBA_4 pfam14555
UBA-like domain;
8-42 1.99e-05

UBA-like domain;


Pssm-ID: 464207  Cd Length: 43  Bit Score: 42.05  E-value: 1.99e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 5805208      8 EMILADFQACTGIENiDEAITLLEQNNWDLVAAIN 42
Cdd:pfam14555   1 DELIAQFQAITGADE-EVARQYLEAHNWDLEAAVN 34
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
490-595 9.15e-05

Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.


Pssm-ID: 430783 [Multi-domain]  Cd Length: 618  Bit Score: 45.52  E-value: 9.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5805208    490 QQQEDIKDGDEREARENVKrEQDEAYRlslEADRAKREAREREMAEQfrLEQIRKEQEEEREAIRLSLEQALPPEPKEEN 569
Cdd:pfam09731 301 KKLAELKKREEKHIERALE-KQKEELD---KLAEELSARLEEVRAAD--EAQLRLEFEREREEIRESYEEKLRTELERQA 374
                          90       100
                  ....*....|....*....|....*...
gi 5805208    570 AEPVSKLR--IRTPSGEfLERRFLASNK 595
Cdd:pfam09731 375 EAHEEHLKdvLVEQEIE-LQREFLQDIK 401
PTZ00121 PTZ00121
MAEBL; Provisional
483-577 6.61e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 6.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5805208    483 AMEIFTAQQQEDIKDGDEREARENVKREQDEAyRLSLEADRAKREAREREMAEQFRLEQIRKEQEEE-REAIRLSLEQal 561
Cdd:PTZ00121 1649 AEELKKAEEENKIKAAEEAKKAEEDKKKAEEA-KKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEkKKAEELKKAE-- 1725
                          90
                  ....*....|....*.
gi 5805208    562 ppepkEENAEPVSKLR 577
Cdd:PTZ00121 1726 -----EENKIKAEEAK 1736
 
Name Accession Description Interval E-value
UAS_FAF1 cd02990
UAS family, FAS-associated factor 1 (FAF1) subfamily; FAF1 contains a UAS domain of unknown ...
352-487 8.05e-88

UAS family, FAS-associated factor 1 (FAF1) subfamily; FAF1 contains a UAS domain of unknown function N-terminal to a ubiquitin-associated UBX domain. FAF1 also contains ubiquitin-associated UBA and nuclear targeting domains, N-terminal to the UAS 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. It 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-kB (NF-kB) by interfering with the nuclear translocation of the p65 subunit. FAF1 also interacts with valosin-containing protein (VCP), which is involved in the ubiquitin-proteosome pathway.


Pssm-ID: 239288  Cd Length: 136  Bit Score: 269.75  E-value: 8.05e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5805208  352 FFIGSLEAAFQEAFYVKARDRKLLAIYLHHDESVLTNVFCSQMLCAESIVSYLSQNFITWAWDLTKDSNRARFLTMCNRH 431
Cdd:cd02990   1 FFIGSLEAAFQEACYRKARDRKLLAIYLHHDESVLSNVFCSQLLCAESIVQYLSQNFITWGWDMTKESNKARFLSSCTRH 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 5805208  432 FGSVVAQTIRTQKTDQKPLFLIIMGKRSSNEVLNVIQGNTTVDELMMRLMAAMEIF 487
Cdd:cd02990  81 FGSVAAQTIRNIKTDQLPAILIIMGKRSSNEVLNVIQGNTGVDELLMRLIEAMEMF 136
UBX_UBXN3A cd01771
Ubiquitin regulatory domain X (UBX) found in FAS associated factor 1 (FAF1, also known as ...
571-649 3.56e-46

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: 157.77  E-value: 3.56e-46
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5805208  571 EPVSKLRIRTPSGEFLERRFLASNKLQIVFDFVASKGFPWDEYKLLSTFPRRDVTQLDPNKSLLEVKLFPQETLFLEAK 649
Cdd:cd01771   2 EPISKLRFRLPGGEFLTRRFLASEPLQVLLNFVASKGYPPDEYKLLTTFPRRDLTQLDPSKTLEELKLFPQETLFLEER 80
Ubl_FAF1 cd17056
ubiquitin-like (Ubl) domain found in FAS-associated factor 1 (FAF1) and similar proteins; FAF1, ...
195-268 6.50e-44

ubiquitin-like (Ubl) domain found in FAS-associated factor 1 (FAF1) and similar proteins; FAF1, also termed UBX domain-containing protein 12 (UBXD12), or UBX domain-containing protein 3A (UBXN3A), belongs to the UBXD family of proteins that contains the ubiquitin regulatory domain X (UBX) with a beta-grasp ubiquitin-like (Ubl) 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 Ubl domains, which show 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 Ubl domains.


Pssm-ID: 340576  Cd Length: 71  Bit Score: 151.43  E-value: 6.50e-44
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5805208  195 MLIITHRevQREYNLNFSGSSTIQEVKRNVYDLTSIPVRHQLWEGWPTSATDDSMCLaESGLSYPCHRLTVGRR 268
Cdd:cd17056   1 DFRVEYR--DRNVDVVLEDTCTVGEIKQILENELQIPVSKMLLKGWKTGDVEDSTVL-KSLHLPKNNSLYVLTP 71
Ubl2_FAF1 cd17130
ubiquitin-like (Ubl) domain 2 found in FAS-associated factor 1 (FAF1) and similar proteins; ...
193-268 1.18e-40

ubiquitin-like (Ubl) domain 2 found in FAS-associated factor 1 (FAF1) and similar proteins; FAF1, also termed UBX domain-containing protein 12 (UBXD12), or UBX domain-containing protein 3A (UBXN3A), belongs to the UBXD family of proteins that contains the ubiquitin regulatory domain X (UBX) with a beta-grasp ubiquitin-like (Ubl) fold, but without the C-terminal double glycine motif. The 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 Ubl domains, which show high structural similarity with the 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. The family corresponds to the second Ubl domain.


Pssm-ID: 340650  Cd Length: 75  Bit Score: 142.46  E-value: 1.18e-40
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5805208  193 NFMLIITHREVQREYNLNFSGSSTIQEVKRNVYDLTSIPVRHQLWEGWPTSATDDSMcLAESGLSYPCHRLTVGRR 268
Cdd:cd17130   1 NYTLNITDTTSQREYNLNFPGSKTIQEVKQDVSDLTSIPVRHQRWTGWPSGASDDTM-LLALGLDFPCHRLTVSRR 75
Ubl1_FAF1 cd17129
ubiquitin-like (Ubl) domain 1 found in FAS-associated factor 1 (FAF1) and similar proteins; ...
100-172 1.53e-38

ubiquitin-like (Ubl) domain 1 found in FAS-associated factor 1 (FAF1) and similar proteins; FAF1, also termed UBX domain-containing protein 12 (UBXD12), or UBX domain-containing protein 3A (UBXN3A), belongs to the UBXD family of proteins that contains the ubiquitin (Ub) regulatory domain X (UBX) with a beta-grasp ubiquitin-like (Ubl) fold, but without the C-terminal double glycine motif. The 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 Ubl domains, which show high structural similarity with the 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. The family corresponds to the first Ubl domain.


Pssm-ID: 340649  Cd Length: 73  Bit Score: 136.62  E-value: 1.53e-38
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5805208  100 MLDFRVEYRDRNVDVVLEDTCTVGEIKQILENELQIPVSKMLLKGWKTGDVEDSTVLKSLHLPKNNSLYVLTP 172
Cdd:cd17129   1 MLTFNVEYRDRTIDVVLPDTETVGDIKQILENELGIPPCKQILKGWKARTVSDSTVLRSLHLPKENSLYLLTP 73
UAS cd02958
UAS family; UAS is a domain of unknown function. Most members of this family are ...
352-487 4.18e-35

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: 128.49  E-value: 4.18e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5805208  352 FFIGSLEAAFQEAFyvkaRDRKLLAIYLHHDESVLTNVFCSQMLCAESIVSYLSQNFITWAWDLTKdSNRARFLTMCnrh 431
Cdd:cd02958   1 FFQGSFEDAKQEAK----SEKKWLLVYLQSEDEFDSQVLNRDLWSNESVKEFIRENFIFWQCDIDS-SEGQRFLQSY--- 72
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 5805208  432 fgsvvaqtirtqKTDQKPLFLIIMGKrsSNEVLNVIQGNTTVDELMMRLMAAMEIF 487
Cdd:cd02958  73 ------------KVDKYPHIAIIDPR--TGEVLKVWSGNITPEDLLSQLIEFLEEF 114
UAS smart00594
UAS domain;
339-481 3.52e-33

UAS domain;


Pssm-ID: 214737 [Multi-domain]  Cd Length: 122  Bit Score: 123.59  E-value: 3.52e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5805208     339 AEFSSRYGdchPVFFIGSLEAAFQEAFyvkaRDRKLLAIYLHHDESVLTNVFCSQMLCAESIVSYLSQNFITWAWDLTKD 418
Cdd:smart00594   1 KLFRPPYG---PLFYQGSLEAAKQEAS----RQRRLLWLYLHSQDSPDSQVFNRDVLCNEAVKSLIRENFIFWQVDVDTS 73
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5805208     419 SNRARFLTMcnrhfgsvvaqtirtqKTDQKPLFLIIMGKR--SSNEVLNVIQGNTTVDELMMRLM 481
Cdd:smart00594  74 EGQRVSQFY----------------KLDSFPYVAIVDPRTgqRVIEWVGVVEGEISPEELMTFLE 122
UBX pfam00789
UBX domain; This domain is present in ubiquitin-regulatory proteins and is a general ...
570-647 1.90e-25

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: 100.06  E-value: 1.90e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5805208    570 AEPVSKLRIRTPSGEFLERRFLASNKLQIVFDFVASKGFPWDE-YKLLSTFPRRDVTQLDPNKSLLEVKLFPQETLFLE 647
Cdd:pfam00789   1 AEDVTRLQIRLPDGSRLVRRFNSSDKLQTVYDFVDSNRYDDLEpFSLNTPFPRRPLTDLDYSKTLKEAGLLPNSTLVLE 79
UBX smart00166
Domain present in ubiquitin-regulatory proteins; Present in FAF1 and Shp1p.
573-648 5.05e-24

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


Pssm-ID: 197552 [Multi-domain]  Cd Length: 77  Bit Score: 95.83  E-value: 5.05e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5805208     573 VSKLRIRTPSGEFLERRFLASNKLQIVFDFV-ASKGFPWDEYKLLSTFPRRDVTQLDPNKSLLEVKLFPQETLFLEA 648
Cdd:smart00166   1 VCRLQIRLPDGSRLVRRFPSSDTLRTVYEFVsAALGDGNDPFTLNSPFPRRTFTKDDYSKKLLELALLPSSTLVLEP 77
UBX cd01767
Ubiquitin regulatory domain X (UBX) structurally similar to a beta-grasp ubiquitin-like fold; ...
575-647 6.20e-19

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: 81.16  E-value: 6.20e-19
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5805208  575 KLRIRTPSGEFLERRFLASNKLQIVFDFVASK-GFPWDEYKLLSTFPRRDVTQLDPNKSLLEVKLFPQETLFLE 647
Cdd:cd01767   1 RIQIRLPDGSRIQRRFSKSDTLQDLYDFVESNlGDSPSSFSLVTSFPRRVLTDEDSDKTLEELGLTPNAVLFVE 74
UBA_FAF1 cd14413
UBA-like domain found in FAS-associated factor 1 (FAF1) and similar proteins; FAF1, also ...
14-46 2.95e-16

UBA-like domain found in FAS-associated factor 1 (FAF1) and similar proteins; FAF1, also called UBX domain-containing protein 12 or UBX domain-containing protein 3A, is a multi-functional Fas associating protein that contains an N-terminal ubiquitin-associated (UBA)-like domain, UAS and ubiquitin-like (UBX) domains, p150 subunit of a chromatin assembly factor like domain (CAF) and a novel nuclear localization signal (NLS). 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.


Pssm-ID: 270596  Cd Length: 33  Bit Score: 72.37  E-value: 2.95e-16
                        10        20        30
                ....*....|....*....|....*....|...
gi 5805208   14 FQACTGIENIDEAITLLEQNNWDLVAAINGVIP 46
Cdd:cd14413   1 FQACTGIEDIDECIMLLEQNNWNLVAAVNAVIP 33
UBX_UBXN7 cd01773
Ubiquitin regulatory domain X (UBX) found in UBX domain protein 7 (UBXN7) and similar proteins; ...
574-648 6.85e-16

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: 72.66  E-value: 6.85e-16
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5805208  574 SKLRIRTPSGEFLERRFLASNKLQIVFDFVASKGFPWDEYKLLSTFPRRDVTQLDPNKSLLEVKLFPQETLFLEA 648
Cdd:cd01773   2 SKLMLRFPDGKREQLSLPASAKLKALVKYVSSKGYPNERYELVTNFPRRKLSHLDYDITLKEAGLCPQETIFVQE 76
UBX_UBXN3B cd16120
Ubiquitin regulatory domain X (UBX) found in FAS associated factor 2 (FAF2, also known as ...
575-645 3.52e-11

Ubiquitin regulatory domain X (UBX) found in FAS associated factor 2 (FAF2, also known as UBXN3B) and similar proteins; UBX domain-containing protein 3B (UBXN3B), also termed protein ETEA, or FAF2, or UBX domain-containing protein 8 (UBXD8), 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. FAF2 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 p97-UBXD8 complex destabilizes mRNA by promoting release of ubiquitinated the RNA-binding protein HuR from messenger ribonucleoprotein (mRNP). Moreover, FAF2 is the translation product of a highly expressed gene in the T-cells and eosinophils of atopic dermatitis patients compared with those of normal individuals. A yeast two-hybrid assay showed that FAF2 can interact with Fas.


Pssm-ID: 340537  Cd Length: 80  Bit Score: 59.59  E-value: 3.52e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5805208  575 KLRIRTPSGEFLERRFLASNKLQIVFDFVASKGFPWDEYKLLSTFPRRDVT-----QLDPNKSLLEVKLFPQETLF 645
Cdd:cd16120   2 KILFKLPNGTRLERRFLKSDSLKVLYDFVFSHEDSPDKFQLVTNFPRRVLPcqpteEQPNPPTLEEAGLGKSEVLF 77
UBA_FAF cd14353
UBA-like domain found in FAS-associated factor FAF1, FAF2 and similar proteins; FAF1, also ...
14-45 1.04e-10

UBA-like domain found in FAS-associated factor FAF1, FAF2 and similar proteins; FAF1, also called UBX domain-containing protein 12 or UBX domain-containing protein 3A, 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. FAF2, also called protein ETEA, UBX domain-containing protein 3B, or UBX domain-containing protein 8, is the translation product of a highly expressed gene in the T-cells and eosinophils of atopic dermatitis patients compared with those of normal individuals. FAF2 shows homology to Fas-associated factor 1 (FAF1). Both of them contain N-terminal ubiquitin-associated (UBA)-like domain, UAS and ubiquitin-like (UBX) domains. Compared to FAF1, however, FAF2 lacks the nuclear targeting domain. The function of FAF2 remains unclear. A yeast two-hybrid assay showed that it can interact with Fas. Because of its homology to FAF1, it is postulated that FAF2 could be involved in modulating Fas-mediated apoptosis of T-cells and eosinophils of atopic dermatitis patients, making them more resistant to apoptosis.


Pssm-ID: 270538  Cd Length: 32  Bit Score: 56.81  E-value: 1.04e-10
                        10        20        30
                ....*....|....*....|....*....|..
gi 5805208   14 FQACTGIENIDEAITLLEQNNWDLVAAINGVI 45
Cdd:cd14353   1 FQSITGIEDSDQCRQILEAHNWDLEAAIQTAL 32
UBX_UBXN8 cd01774
Ubiquitin regulatory domain X (UBX) found in UBX domain protein 8 (UBXN8) and similar proteins; ...
573-647 1.54e-10

Ubiquitin regulatory domain X (UBX) found in UBX domain protein 8 (UBXN8) and similar proteins; UBXN8, also termed reproduction 8 protein (Rep8), or UBX domain-containing protein 6 (UBXD6), or D8S2298E, 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. UBXN8 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. UBXN8 is a transmembrane protein that localizes to the endoplasmic reticulum (ER) membrane with its UBX domain facing the cytoplasm. It facilitates efficient ER-associated degradation (ERAD) by tethering p97 to the ER membrane.


Pssm-ID: 340472  Cd Length: 76  Bit Score: 57.35  E-value: 1.54e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5805208  573 VSKLRIRTPSGEFLERRFLASNKLQIVFDFVASKGFPWDEYKLLSTFPRRDVTQlDPNKSLLEVKLFPQETLFLE 647
Cdd:cd01774   2 AVTIALRFPGGRVHRRRFLTTENIQVLLDWMTKLGYHQTLYTLSTTYPRTILSD-DADKTLEDLGITKDVALNVE 75
Ubiquitin_like_fold cd00196
Beta-grasp ubiquitin-like fold; Ubiquitin is a protein modifier that is involved in various ...
576-647 2.44e-08

Beta-grasp ubiquitin-like fold; Ubiquitin is a protein modifier that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair in eukaryotes. The ubiquitination process comprises a cascade of E1, E2 and E3 enzymes that results in a covalent bond between the C-terminus of ubiquitin and the epsilon-amino group of a substrate lysine. Ubiquitin-like proteins have similar ubiquitin beta-grasp fold and attach to other proteins in a ubiquitin-like manner but with biochemically distinct roles. Ubiquitin and ubiquitin-like proteins conjugate and deconjugate via ligases and peptidases to covalently modify target polypeptides. Some other ubiquitin-like domains have adaptor roles in ubiquitin-signaling by mediating protein-protein interaction. In addition to Ubiquitin-like (Ubl) domain, Ras-associating (RA) domain, F0/F1 sub-domain of FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, TGS (ThrRS, GTPase and SpoT) domain, Ras-binding domain (RBD), Ubiquitin regulatory domain X (UBX), Dublecortin-like domain, and RING finger- and WD40-associated ubiquitin-like (RAWUL) domain have beta-grasp ubiquitin-like folds, and are included in this superfamily.


Pssm-ID: 340450  Cd Length: 68  Bit Score: 51.17  E-value: 2.44e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5805208  576 LRIRTPSGEFLERRFLASNKLQIVFDFVASK-GFPWDEYKLLstfprRDVTQLDPNKSLLEVKLFPQETLFLE 647
Cdd:cd00196   1 VKVETPSLKKIVVAVPPSTTLRQVLEKVAKRiGLPPDVIRLL-----FNGQVLDDLMTAKQVGLEPGEELHFV 68
UAS_ETEA cd02991
UAS family, ETEA subfamily; composed of proteins similar to human ETEA protein, the ...
352-485 5.95e-08

UAS family, ETEA subfamily; composed of proteins similar to human ETEA protein, the translation product of a highly expressed gene in the T-cells and eosinophils of atopic dermatitis patients compared with those of normal individuals. ETEA shows homology to Fas-associated factor 1 (FAF1); both containing UAS and UBX (ubiquitin-associated) domains. Compared to FAF1, however, ETEA lacks the ubiquitin-associated UBA domain and a nuclear targeting domain. The function of ETEA is still unknown. A yeast two-hybrid assay showed that it can interact with Fas. Because of its homology to FAF1, it is postulated that ETEA could be involved in modulating Fas-mediated apoptosis of T-cells and eosinophils of atopic dermatitis patients, making them more resistant to apoptosis.


Pssm-ID: 239289  Cd Length: 116  Bit Score: 51.33  E-value: 5.95e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5805208  352 FFIGSLEAAFQEAfyvkARDRKLLAIYLHHDESVLTNVFCSQMLCAESIVSYLSQNFITWAWDLtkdsnrarfltmcNRH 431
Cdd:cd02991   1 FYQGTYSQALNDA----KQELRFLLVYLHGDDHQDTDEFCRNTLCAPEVIEYINTRMLFWACSV-------------AKP 63
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 5805208  432 FGSVVAQTIRTQktdQKPLFLIIMGKRSSNEVLNVIQGNTTVDELMMRLMAAME 485
Cdd:cd02991  64 EGYRVSQALRER---TYPFLAMIMLKDNRMTIVGRLEGLIQPEDLINRLTFIMD 114
UBX_UBXN4 cd16117
Ubiquitin regulatory domain X (UBX) found in UBX domain protein 4 (UBXN4) and similar proteins; ...
573-646 4.02e-07

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: 47.71  E-value: 4.02e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5805208  573 VSKLRIRTPSGEFLERRFLASNKLQIVFDFVASK-GFPWDEYKLLSTFPRRDVTQLDPNKSLLEVKLFPQETLFL 646
Cdd:cd16117   1 TARIQFRLPDGSSFTNQFPSDAPLEEARQFVAQTvGPAYGPFSLATTFPRREFTDDDYQKTLLELELAPSAALVV 75
UBX2_UBXN9 cd16118
Ubiquitin regulatory domain X (UBX) 2 found in UBX domain protein 9 (UBXN9, UBXD9, or ASPSCR1) ...
576-640 1.93e-05

Ubiquitin regulatory domain X (UBX) 2 found in UBX domain protein 9 (UBXN9, UBXD9, or ASPSCR1) and similar proteins; UBXN9, also termed tether containing UBX domain for GLUT4 (TUG), or alveolar soft part sarcoma chromosomal region candidate gene 1 protein (ASPSCR1), or alveolar soft part sarcoma locus (ASPL), or renal papillary cell carcinoma protein 17 (RCC17), belongs to the UBXD family of proteins that contains two ubiquitin regulatory domains 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, UBXN9 contains an N-terminal ubiquitin-like (Ubl) domain. UBXN9 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. However, high-affinity interacting protein ASPL efficiently promotes p97 hexamer disassembly, resulting in the formation of stable p97:ASPL heterotetramers; the extended UBX domain (eUBX) in ASPL is critical for p97 hexamer disassembly and facilitates the assembly of p97:ASPL heterotetramers.UBXN9 is involved in insulin-stimulated redistribution of the glucose transporter GLUT4, assembly of the Golgi apparatus. In addition to GLUT4, UBXN9 also controls vesicle translocation by interacting with insulin-regulated aminopeptidase (IRAP), a transmembrane aminopeptidase. UBXN9 and its budding yeast ortholog, Ubx4p, are multifunctional proteins that share some, but not all functions. Yeast Ubx4p is important for endoplasmic reticulum-associated protein degradation (ERAD) but UBXN9 appears not to share this function.


Pssm-ID: 340535  Cd Length: 74  Bit Score: 42.94  E-value: 1.93e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5805208  576 LRIRTPSGEFLERRFLASNKLQIVFDFV----ASKGFPWdeyKLLSTFPRRDVTqlDPNKSLLEVKLFP 640
Cdd:cd16118   3 IRVQFPDRLVLQAFFRPLETVRALYDFVkshlADPDLPF---YLYTTPPKRVLK--DKNKTLYQAGLVP 66
UBA_4 pfam14555
UBA-like domain;
8-42 1.99e-05

UBA-like domain;


Pssm-ID: 464207  Cd Length: 43  Bit Score: 42.05  E-value: 1.99e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 5805208      8 EMILADFQACTGIENiDEAITLLEQNNWDLVAAIN 42
Cdd:pfam14555   1 DELIAQFQAITGADE-EVARQYLEAHNWDLEAAVN 34
UBX_UBXN6 cd16119
Ubiquitin regulatory domain X (UBX) found in UBX domain protein 6 (UBXN6) and similar proteins; ...
576-644 6.91e-05

Ubiquitin regulatory domain X (UBX) found in UBX domain protein 6 (UBXN6) and similar proteins; UBXN6, also termed UBX domain-containing protein 1 (UBXD1), and UBXDC2, 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. UBXN6 acts 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. Unlike other p97 cofactors that binds the N-domain of p97 through their UBX domain, UBXN6 binds p97 in two regions, at the p97 C terminus via a PUB domain and at the p97 N-domain with a short linear interaction motif termed VIM. Its UBX domain is not functional for the binding of p97. The UBXN6-p97 complex regulates the endolysosomal sorting of ubiquitylated plasma membrane protein caveolin-1 (CAV1), as well as the trafficking of ERGIC-53-containing vesicles by controlling the interaction of transport factors with the cytoplasmic tail of ERGIC-53. In addition, UBXN6 is a regulatory component of endoplasmic reticulum-associated degradation (ERAD) that may modulate the adaptor binding to p97.


Pssm-ID: 340536  Cd Length: 73  Bit Score: 41.39  E-value: 6.91e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5805208  576 LRIRTPSGEFLERRFLASNKLQIVFDFVASK-GFPWDEYKLlsTFPRRDVTQLDpNKSLLEVKLFPQETL 644
Cdd:cd16119   4 IRVRFPDGVILQGTFYAREKLSAVREFVREAlANDWLPFEL--VTPGGQKLTDE-DATLAELGLVPAALL 70
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
490-595 9.15e-05

Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.


Pssm-ID: 430783 [Multi-domain]  Cd Length: 618  Bit Score: 45.52  E-value: 9.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5805208    490 QQQEDIKDGDEREARENVKrEQDEAYRlslEADRAKREAREREMAEQfrLEQIRKEQEEEREAIRLSLEQALPPEPKEEN 569
Cdd:pfam09731 301 KKLAELKKREEKHIERALE-KQKEELD---KLAEELSARLEEVRAAD--EAQLRLEFEREREEIRESYEEKLRTELERQA 374
                          90       100
                  ....*....|....*....|....*...
gi 5805208    570 AEPVSKLR--IRTPSGEfLERRFLASNK 595
Cdd:pfam09731 375 EAHEEHLKdvLVEQEIE-LQREFLQDIK 401
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
461-578 1.04e-04

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 45.50  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5805208    461 NEVLNVIQGNTTVDELMMRlmaamEIFTAQQQEDIKDGDEREARENVKREQ-------------------DEAYRLSLEA 521
Cdd:pfam17380 272 NQLLHIVQHQKAVSERQQQ-----EKFEKMEQERLRQEKEEKAREVERRRKleeaekarqaemdrqaaiyAEQERMAMER 346
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5805208    522 ----DRAKREAREREMaEQFRLEQIRKEQEEEREAIRLSLEQALPPEPKEENAEPVSKLRI 578
Cdd:pfam17380 347 erelERIRQEERKREL-ERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKI 406
Ubl_ubiquitin_like cd17039
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ...
103-170 3.32e-04

ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like (Ubl) proteins have a similar ubiquitin (Ub) beta-grasp fold and attach to other proteins in a Ubl manner but with biochemically distinct roles. Ub and Ubl proteins conjugate and deconjugate via ligases and peptidases to covalently modify target polypeptides. Some Ubl domains have adaptor roles in Ub-signaling by mediating protein-protein interaction. Prokaryotic sulfur carrier proteins are Ub-related proteins that can be activated in an ATP-dependent manner. Polyubiquitination signals for a diverse set of cellular events via different isopeptide linkages formed between the C terminus of one ubiquitin (Ub) and the epsilon-amine of K6, K11, K27, K29, K33, K48, or K63 of a second Ub. One of these seven lysine residues (K27, Ub numbering) is conserved in this Ubl_ubiquitin_like family. K27-linked Ub chains are versatile and can be recognized by several downstream receptor proteins. K27 has roles beyond chain linkage, such as in Ubl NEDD8 (which contains many of the same lysines (K6, K11, K27, K33, K48) as Ub) where K27 has a role (other than conjugation) in the mechanism of protein neddylation.


Pssm-ID: 340559 [Multi-domain]  Cd Length: 68  Bit Score: 39.12  E-value: 3.32e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5805208  103 FRVEYRD-RNVDVVLEDTCTVGEIKQILENELQIPVSKMLLKGWKTGdVEDSTVLKSLHLPKNNSLYVL 170
Cdd:cd17039   1 ITVKTLDgKTYTVEVDPDDTVADLKEKIEEKTGIPVEQQRLIYNGKE-LKDDKTLSDYGIKDGSTIHLV 68
UBA_TAP-C_like cd14273
UBA-like domain found in the NXF family of mRNA nuclear export factors and similar proteins; ...
14-42 3.89e-04

UBA-like domain found in the NXF family of mRNA nuclear export factors and similar proteins; This family includes nuclear RNA export factors (NXF1/NXF2), FAS-associated factors (FAF1/2), tyrosyl-DNA phosphodiesterase 2 (TDP2), OTU domain-containing proteins (OTU7A/OTU7B), NSFL1 cofactor p47, defective in cullin neddylation protein 1 (DCN1)-like protein (DCNL1/DCNL2), yeast defective in cullin neddylation protein 1 (DCN1) and similar proteins. NXF proteins can stimulate nuclear export of mRNAs and facilitate the export of unspliced viral mRNA containing the constitutive transport element. 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. FAF2 is the translation product of a highly expressed gene in the T-cells and eosinophils of atopic dermatitis patients compared with those of normal individuals. Its biological function remains unclear. TDP2 is a 5'-Tyr-DNA phosphodiesterase required for the efficient repair of topoisomerase II-induced DNA double strand breaks. OTU7A and OTU7B are zinc finger proteins that function as deubiquitinating enzymes. p47 is a major cofactor of the cytosolic AAA ATPase p97. It is required for the p97-regulated membrane reassembly of the endoplasmic reticulum (ER), the nuclear envelope and the Golgi apparatus. DCNL1 plays an essential role in the neddylation E3 complex and participates in the release of inhibitory effects of CAND1 on cullin-RING ligase E3 complex assembly and activity. The biological function of DCNL2 remains unclear. Yeast DCN1 is a scaffold-type E3 ligase for cullin neddylation. It can bind directly to cullins and the ubiquitin-like protein Nedd8-specific E2 (Ubc12), and regulate cullin neddylation and thus display ubiquitin ligase activity.


Pssm-ID: 270459  Cd Length: 31  Bit Score: 38.15  E-value: 3.89e-04
                        10        20
                ....*....|....*....|....*....
gi 5805208   14 FQACTGIeNIDEAITLLEQNNWDLVAAIN 42
Cdd:cd14273   1 FMEITGA-DPETARQYLESNNWDLEAAIN 28
PTZ00121 PTZ00121
MAEBL; Provisional
483-577 6.61e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 6.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5805208    483 AMEIFTAQQQEDIKDGDEREARENVKREQDEAyRLSLEADRAKREAREREMAEQFRLEQIRKEQEEE-REAIRLSLEQal 561
Cdd:PTZ00121 1649 AEELKKAEEENKIKAAEEAKKAEEDKKKAEEA-KKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEkKKAEELKKAE-- 1725
                          90
                  ....*....|....*.
gi 5805208    562 ppepkEENAEPVSKLR 577
Cdd:PTZ00121 1726 -----EENKIKAEEAK 1736
UBX_UBXN1 cd01772
Ubiquitin regulatory domain X (UBX) found in UBX domain protein 1 (UBXN1) and similar proteins; ...
575-646 1.28e-03

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: 38.06  E-value: 1.28e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5805208  575 KLRIRTPSGEFLERRFLASNKLQIVFDFVASKGFPWDE-YKLLSTFPRRDVTQLDPNKSLLEVKLFPQETLFL 646
Cdd:cd01772   8 RLQVRLTNGSTLTQTFGAKEQLAAVRLYVELNRTDGDGpFSLMTTFPRKVFTEEDMEKPLKELGLVPSAVLIV 80
Ubl_AtNPL4_like cd17055
ubiquitin-like (Ubl) domain found in Arabidopsis thaliana NPL4-like proteins NPL4-1, NPL4-2, ...
104-143 1.53e-03

ubiquitin-like (Ubl) domain found in Arabidopsis thaliana NPL4-like proteins NPL4-1, NPL4-2, and similar proteins; The family includes a group of uncharacterized plant ubiquitin-like (Ubl) domain-containing proteins, including Arabidopsis thaliana NPL4-like protein 1 and NPL4-like protein 2.


Pssm-ID: 340575  Cd Length: 73  Bit Score: 37.58  E-value: 1.53e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 5805208  104 RVEYRDRNVDVVLEDTCTVGEIKQILENELQIPVSKMLLK 143
Cdd:cd17055   4 RVRSRDGTERVEVPDDATVGDLKEKIAEQLSVPVSDQTLS 43
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
492-599 1.68e-03

Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.


Pssm-ID: 402959 [Multi-domain]  Cd Length: 164  Bit Score: 39.67  E-value: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5805208    492 QEDIKDGDEReARENVKREQDEAYRLSLEADRAKREAREREMAEQFRL-EQIRKEQEEEREAirlSLEQALPPEpkEENA 570
Cdd:pfam11600  42 KEEAKAEKER-AKEEARRKKEEEKELKEKERREKKEKDEKEKAEKLRLkEEKRKEKQEALEA---KLEEKRKKE--EEKR 115
                          90       100
                  ....*....|....*....|....*....
gi 5805208    571 EPVSKLRIRTPSGEFleRRFLASNKLQIV 599
Cdd:pfam11600 116 LKEEEKRIKAEKAEI--TRFLQKPKTQQA 142
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
500-571 1.81e-03

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 39.25  E-value: 1.81e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5805208    500 EREAREnvKREQDEAYRLSLEADRAKR-EAREREMAEQFRLEQIRKEQEEEREAIRLSLEQALPPEPKEENAE 571
Cdd:pfam05672  28 EREEQE--RLEKEEEERLRKEELRRRAeEERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQER 98
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
478-560 1.84e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 41.48  E-value: 1.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5805208    478 MRLMAAMEIFTAQQQEDIKDGDEREArenvKREQDEAYRLSLEADRAKRE----ARER----EMAEQFRLEQIRKEQEEE 549
Cdd:pfam15709 412 LQLQAAQERARQQQEEFRRKLQELQR----KKQQEEAERAEAEKQRQKELemqlAEEQkrlmEMAEEERLEYQRQKQEAE 487
                          90       100
                  ....*....|....*....|....*
gi 5805208    550 --------------REAIRLSLEQA 560
Cdd:pfam15709 488 ekarleaeerrqkeEEAARLALEEA 512
UBA_CF106 cd14349
UBA-like domain found in uncharacterized protein C6orf106 and similar proteins; The family ...
6-42 2.07e-03

UBA-like domain found in uncharacterized protein C6orf106 and similar proteins; The family corresponds to a group of uncharacterized protein C6orf106 and its homologs mainly found in Metazoa. All family members contain a ubiquitin-associated (UBA)-like domain.


Pssm-ID: 270534  Cd Length: 41  Bit Score: 36.43  E-value: 2.07e-03
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 5805208    6 DREMILADFQACTGIENIDEAITLLEQNNWDLVAAIN 42
Cdd:cd14349   1 DHEELISQFQSILGAQNESEAAFFLEMNNWNLQAAVG 37
UBX_UBXN2C cd17162
Ubiquitin regulatory domain X (UBX) found in NSFL1 cofactor (also known as UBX ...
568-639 2.70e-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: 37.22  E-value: 2.70e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5805208  568 ENAEPVSKLRIRTPSGEFLERRFLASNKLQIVFDFVASK--GFPWDEYKLLSTFPRRDVTqlDPNKSLLEVKLF 639
Cdd:cd17162   2 NDSEPVTNIQIRLADGGRLVQKFNHSHRIRDIRLFIVDArpAMAATSFVLMTTFPNKELT--DENQTLKEANLL 73
DDRGK pfam09756
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ...
482-548 3.28e-03

DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and vertebrates. They contain a highly conserved DDRGK motif.


Pssm-ID: 370664 [Multi-domain]  Cd Length: 188  Bit Score: 39.25  E-value: 3.28e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5805208    482 AAMEIFTAQQQEDIKDGDEREARENVKREQDEAYRLSLEADRAKREAREREMAEQfRLEQIRKEQEE 548
Cdd:pfam09756   9 AKLELKEAKRQQREAEEEEREEREKLEEKREEEYKEREEREEEAEKEKEEEERKQ-EEEQERKEQEE 74
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
458-571 3.47e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 40.32  E-value: 3.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5805208    458 RSSNEVLNVIQGNTTVDELMMRLMAAMEIFTAQQQEdikdgdeREARENVKREQDEAYRLSLEADRAKREAREREMAEQF 537
Cdd:pfam15709 296 RSSPTQTFVVTGNMESEEERSEEDPSKALLEKREQE-------KASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEQL 368
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 5805208    538 -RLEQIRKEQEEER----EAIRLSLEQALPPEPKEENAE 571
Cdd:pfam15709 369 eRAEKMREELELEQqrrfEEIRLRKQRLEEERQRQEEEE 407
V-ATPase_G_2 pfam16999
Vacuolar (H+)-ATPase G subunit; This family represents vacuolar (H+)-ATPase G subunit from ...
489-554 4.23e-03

Vacuolar (H+)-ATPase G subunit; This family represents vacuolar (H+)-ATPase G subunit from several bacterial and archaeal species. Subunit G is a component of the peripheral stalk of the ATPase complex


Pssm-ID: 339878 [Multi-domain]  Cd Length: 104  Bit Score: 37.42  E-value: 4.23e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5805208    489 AQQQEDIKdgdeREARENVKREQDEAYRLSLEAdrakrEAREREMAEQFRlEQIRKEQEEEREAIR 554
Cdd:pfam16999  18 DQQIEAAR----KEAEREVEAAEAEAARILREA-----EAKAKALQAEYR-QELAAETARIREEAR 73
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
490-551 7.62e-03

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 37.71  E-value: 7.62e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5805208    490 QQQEDIKDGDEREARENVKREQDEAYRLSLEADRAkrEAREREMAEQFRLEQIRKEQEEERE 551
Cdd:pfam05672  72 REEEERQRKAEEEAEEREQREQEEQERLQKQKEEA--EAKAREEAERQRQEREKIMQQEEQE 131
 
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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