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Conserved domains on  [gi|1191888642|ref|XP_020951070|]
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protein FAM131C isoform X3 [Sus scrofa]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FAM131 super family cl20887
Putative cell signalling; The precise function of this protein family is unknown, however ...
 68-277 2.64e-37

Putative cell signalling; The precise function of this protein family is unknown, however studies have shown it undergoes Protein N-myristoylation; a type of lipid modification in eukaryotic and viral proteins. Protein N-myristoylation is usually an irreversible co-translational protein modification which is useful in cell signal transduction pathways. This indicates that FAM131 may have some sort of role in cell signalling due to its ability to be myristoylated. This family of proteins is found in eukaryotes and are typically between 257 and 361 amino acids in length.


The actual alignment was detected with superfamily member pfam15010:

Pssm-ID: 464442  Cd Length: 292  Bit Score: 133.55  E-value: 2.64e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191888642  68 LSDSRSCSSNYNVAALATSSLVGVVQSIKDHITKPTAMARGRVAHLIEWKGWSAQRSGWELSPAEDEHYCCLPDELREAR 147
Cdd:pfam15010   2 LPKSRRALTIQEIAALARSSLHGISQVVKDHVTKPTAMAQGRVAHLIEWKGWSKPQDSPAALESDFNSYSDLSEGEQEAR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191888642 148 FAAGVAEQFAITEATLSAWSSLDDEELNPE-------NSPQDVVQLQDLES-----IYLQDSLLSVPSQDDSLLAFSSSG 215
Cdd:pfam15010  82 FAAGVAEQFAIAEAKLRAWSSVDGEDSNDDsydedfaPATEPTMQSQDNAAqyplgPWLHDYLHSGRCQSRPLRQGSCEP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191888642 216 --------LSPDGW-------------PSPEEPPITAVGPQppSPEQQHRQRLPGAPGPEGGAHLQGSLPSVDSG----- 269
Cdd:pfam15010 162 esdgsqtvGSPDTLcsslcsliedhllGSPAELAGSLLGQG--GEELLPRLQREGPPSQESAFRSLGPLERQDSLysvsy 239

                         250
                  ....*....|.
gi 1191888642 270 ---SLSEEEDE 277
Cdd:pfam15010 240 sesCLSPAEEE 250
 
Name Accession Description Interval E-value
FAM131 pfam15010
Putative cell signalling; The precise function of this protein family is unknown, however ...
 68-277 2.64e-37

Putative cell signalling; The precise function of this protein family is unknown, however studies have shown it undergoes Protein N-myristoylation; a type of lipid modification in eukaryotic and viral proteins. Protein N-myristoylation is usually an irreversible co-translational protein modification which is useful in cell signal transduction pathways. This indicates that FAM131 may have some sort of role in cell signalling due to its ability to be myristoylated. This family of proteins is found in eukaryotes and are typically between 257 and 361 amino acids in length.


Pssm-ID: 464442  Cd Length: 292  Bit Score: 133.55  E-value: 2.64e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191888642  68 LSDSRSCSSNYNVAALATSSLVGVVQSIKDHITKPTAMARGRVAHLIEWKGWSAQRSGWELSPAEDEHYCCLPDELREAR 147
Cdd:pfam15010   2 LPKSRRALTIQEIAALARSSLHGISQVVKDHVTKPTAMAQGRVAHLIEWKGWSKPQDSPAALESDFNSYSDLSEGEQEAR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191888642 148 FAAGVAEQFAITEATLSAWSSLDDEELNPE-------NSPQDVVQLQDLES-----IYLQDSLLSVPSQDDSLLAFSSSG 215
Cdd:pfam15010  82 FAAGVAEQFAIAEAKLRAWSSVDGEDSNDDsydedfaPATEPTMQSQDNAAqyplgPWLHDYLHSGRCQSRPLRQGSCEP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191888642 216 --------LSPDGW-------------PSPEEPPITAVGPQppSPEQQHRQRLPGAPGPEGGAHLQGSLPSVDSG----- 269
Cdd:pfam15010 162 esdgsqtvGSPDTLcsslcsliedhllGSPAELAGSLLGQG--GEELLPRLQREGPPSQESAFRSLGPLERQDSLysvsy 239

                         250
                  ....*....|.
gi 1191888642 270 ---SLSEEEDE 277
Cdd:pfam15010 240 sesCLSPAEEE 250
CD_Cbx6 cd18648
chromodomain of chromobox homolog 6; CHRomatin Organization Modifier (chromo) domain of ...
 107-133 2.94e-03

chromodomain of chromobox homolog 6; CHRomatin Organization Modifier (chromo) domain of chromobox homolog 6 (CBX6), a component of the PcG repressive complex PRC1, one of the two classes of PRCs. PcG proteins form large multiprotein complexes (PcG bodies) which are involved in the stable repression of genes involved in development, signaling or cancer via chromatin-based epigenetic modifications. Mammalian PRC1 includes canonical (cPRC1) and non-canonical complexes; cPRC1, contains four core subunits including one CBX protein (CBX2, CBX4, and CBX6-CBX8) that binds H3K27me3. CBX family members have different affinity for H3K27me3, with CBX7 having the highest binding capability. The human CBX proteins show distinct nuclear localizations and contribute differently to transcriptional repression. Some CBX proteins of the PRC1 complex have been implicated in transcriptional activation as well as in PRC1-independent roles in embryonic stem cells and in somatic cells.


Pssm-ID: 349295  Cd Length: 58  Bit Score: 35.42  E-value: 2.94e-03
                          10        20
                  ....*....|....*....|....*..
gi 1191888642 107 RGRVAHLIEWKGWSAQRSGWElsPAED 133
Cdd:cd18648    16 KGRIEYLVKWKGWAIKYSTWE--PEEN 40
 
Name Accession Description Interval E-value
FAM131 pfam15010
Putative cell signalling; The precise function of this protein family is unknown, however ...
 68-277 2.64e-37

Putative cell signalling; The precise function of this protein family is unknown, however studies have shown it undergoes Protein N-myristoylation; a type of lipid modification in eukaryotic and viral proteins. Protein N-myristoylation is usually an irreversible co-translational protein modification which is useful in cell signal transduction pathways. This indicates that FAM131 may have some sort of role in cell signalling due to its ability to be myristoylated. This family of proteins is found in eukaryotes and are typically between 257 and 361 amino acids in length.


Pssm-ID: 464442  Cd Length: 292  Bit Score: 133.55  E-value: 2.64e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191888642  68 LSDSRSCSSNYNVAALATSSLVGVVQSIKDHITKPTAMARGRVAHLIEWKGWSAQRSGWELSPAEDEHYCCLPDELREAR 147
Cdd:pfam15010   2 LPKSRRALTIQEIAALARSSLHGISQVVKDHVTKPTAMAQGRVAHLIEWKGWSKPQDSPAALESDFNSYSDLSEGEQEAR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191888642 148 FAAGVAEQFAITEATLSAWSSLDDEELNPE-------NSPQDVVQLQDLES-----IYLQDSLLSVPSQDDSLLAFSSSG 215
Cdd:pfam15010  82 FAAGVAEQFAIAEAKLRAWSSVDGEDSNDDsydedfaPATEPTMQSQDNAAqyplgPWLHDYLHSGRCQSRPLRQGSCEP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191888642 216 --------LSPDGW-------------PSPEEPPITAVGPQppSPEQQHRQRLPGAPGPEGGAHLQGSLPSVDSG----- 269
Cdd:pfam15010 162 esdgsqtvGSPDTLcsslcsliedhllGSPAELAGSLLGQG--GEELLPRLQREGPPSQESAFRSLGPLERQDSLysvsy 239

                         250
                  ....*....|.
gi 1191888642 270 ---SLSEEEDE 277
Cdd:pfam15010 240 sesCLSPAEEE 250
CD_Cbx6 cd18648
chromodomain of chromobox homolog 6; CHRomatin Organization Modifier (chromo) domain of ...
 107-133 2.94e-03

chromodomain of chromobox homolog 6; CHRomatin Organization Modifier (chromo) domain of chromobox homolog 6 (CBX6), a component of the PcG repressive complex PRC1, one of the two classes of PRCs. PcG proteins form large multiprotein complexes (PcG bodies) which are involved in the stable repression of genes involved in development, signaling or cancer via chromatin-based epigenetic modifications. Mammalian PRC1 includes canonical (cPRC1) and non-canonical complexes; cPRC1, contains four core subunits including one CBX protein (CBX2, CBX4, and CBX6-CBX8) that binds H3K27me3. CBX family members have different affinity for H3K27me3, with CBX7 having the highest binding capability. The human CBX proteins show distinct nuclear localizations and contribute differently to transcriptional repression. Some CBX proteins of the PRC1 complex have been implicated in transcriptional activation as well as in PRC1-independent roles in embryonic stem cells and in somatic cells.


Pssm-ID: 349295  Cd Length: 58  Bit Score: 35.42  E-value: 2.94e-03
                          10        20
                  ....*....|....*....|....*..
gi 1191888642 107 RGRVAHLIEWKGWSAQRSGWElsPAED 133
Cdd:cd18648    16 KGRIEYLVKWKGWAIKYSTWE--PEEN 40
CD_polycomb_like cd18627
chromodomain of polycomb and chromobox family proteins; CHRomatin Organization Modifier ...
 107-127 3.32e-03

chromodomain of polycomb and chromobox family proteins; CHRomatin Organization Modifier (chromo) domain of Polycomb and Polycomb-group (PcG) chromobox (CBX) family proteins such as CBX2, CBX4, CBX6, CBX7, and CBX8. These CBX proteins are components of the PcG repressive complex PRC1, one of the two classes of PRCs. PcG proteins form large multiprotein complexes (PcG bodies) which are involved in the stable repression of genes involved in development, signaling or cancer via chromatin-based epigenetic modifications. Mammalian PRC1 includes canonical (cPRC1) and non-canonical complexes; cPRC1, contains four core subunits including one CBX protein (CBX2, CBX4, and CBX6-CBX8) that binds H3K27me3. CBX family members have different affinity for H3K27me3, with CBX7 having the highest binding capability. The human CBX proteins show distinct nuclear localizations and contribute differently to transcriptional repression. Some CBX proteins of the PRC1 complex have been implicated in transcriptional activation as well as in PRC1-independent roles in embryonic stem cells and in somatic cells.


Pssm-ID: 349277  Cd Length: 49  Bit Score: 35.06  E-value: 3.32e-03
                          10        20
                  ....*....|....*....|.
gi 1191888642 107 RGRVAHLIEWKGWSAQRSGWE 127
Cdd:cd18627    13 KGKVEYLVKWKGWSQKYNTWE 33
CD_polycomb cd18644
chromodomain of polycomb; CHRomatin Organization Modifier (chromo) domain of the PcG ...
 107-127 6.38e-03

chromodomain of polycomb; CHRomatin Organization Modifier (chromo) domain of the PcG (polycomb-group) chromodomain protein Polycomb (Pc) from Drosophila melanogaster, anthropod, worm, and sea cucumber, and similar proteins. Pc is a component of the Polycomb-group (PcG) multiprotein PRC1 complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. The core subunits of PRC1 are polycomb (Pc), polyhomeotic (Ph), posterior sex combs (Psc), and sex comb extra (Sce, also known as dRing). Polycomb (Pc) plays a role in modulating life span in flies, it negatively regulates longevity.


Pssm-ID: 349291  Cd Length: 54  Bit Score: 34.36  E-value: 6.38e-03
                          10        20
                  ....*....|....*....|.
gi 1191888642 107 RGRVAHLIEWKGWSAQRSGWE 127
Cdd:cd18644    16 KGKVEYLVKWKGWSNKHNTWE 36
CD_Cbx4 cd18645
chromodomain of chromobox homolog 4; CHRomatin Organization Modifier (chromo) domain of ...
 105-133 7.57e-03

chromodomain of chromobox homolog 4; CHRomatin Organization Modifier (chromo) domain of chromobox homolog 4 (CBX4), a component of the PcG repressive complex PRC1, one of the two classes of PRCs. PcG proteins form large multiprotein complexes (PcG bodies) which are involved in the stable repression of genes involved in development, signaling or cancer via chromatin-based epigenetic modifications. Mammalian PRC1 includes canonical (cPRC1) and non-canonical complexes; cPRC1, contains four core subunits including one CBX protein (CBX2, CBX4, and CBX6-CBX8) that binds H3K27me3. CBX family members have different affinity for H3K27me3, with CBX7 having the highest binding capability. The human CBX proteins show distinct nuclear localizations and contribute differently to transcriptional repression. Some CBX proteins of the PRC1 complex have been implicated in transcriptional activation as well as in PRC1-independent roles in embryonic stem cells and in somatic cells. In addition to a chromodomain with H3K27me3-binding activity, Cbx4 contains two SUMO-interacting motifs responsible for its small ubiquitin-related modifier (SUMO) E3 ligase activity. CBX proteins may act as an oncogene or tumor suppressor in a cell-type-dependent manner, for example CBX8 promotes proliferation while suppressing metastasis, in colorectal carcinoma progression. CBX4 may serve as a tumor suppressor in colorectal carcinoma, and has been shown to be an oncogene in osteosarcoma and breast cancer.


Pssm-ID: 349292  Cd Length: 55  Bit Score: 34.26  E-value: 7.57e-03
                          10        20
                  ....*....|....*....|....*....
gi 1191888642 105 MARGRVAHLIEWKGWSAQRSGWElsPAED 133
Cdd:cd18645    14 IRKGRVEYLVKWRGWSPKYNTWE--PEEN 40
CD_Cbx8 cd18649
chromodomain of chromobox homolog 8; CHRomatin Organization Modifier (chromo) domain of ...
 107-133 8.17e-03

chromodomain of chromobox homolog 8; CHRomatin Organization Modifier (chromo) domain of chromobox homolog 8 (CBX8), a component of the PcG repressive complex PRC1, one of the two classes of PRCs. PcG proteins form large multiprotein complexes (PcG bodies) which are involved in the stable repression of genes involved in development, signaling or cancer via chromatin-based epigenetic modifications. Mammalian PRC1 includes canonical (cPRC1) and non-canonical complexes; cPRC1, contains four core subunits including one CBX protein (CBX2, CBX4, and CBX6-CBX8) that binds H3K27me3. CBX family members have different affinity for H3K27me3, with CBX7 having the highest binding capability. The human CBX proteins show distinct nuclear localizations and contribute differently to transcriptional repression. Some CBX proteins of the PRC1 complex have been implicated in transcriptional activation as well as in PRC1-independent roles in embryonic stem cells and in somatic cells. CBX proteins may act as an oncogene or tumor suppressor in a cell-type-dependent manner, CBX8 for example promotes proliferation while suppressing metastasis, in colorectal carcinoma progression.


Pssm-ID: 349296  Cd Length: 55  Bit Score: 33.92  E-value: 8.17e-03
                          10        20
                  ....*....|....*....|....*..
gi 1191888642 107 RGRVAHLIEWKGWSAQRSGWElsPAED 133
Cdd:cd18649    17 KGRMEYLVKWKGWSQKYSTWE--PEEN 41
 
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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