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Conserved domains on  [gi|334724470|ref|NP_001229338|]
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GRB2-associated and regulator of MAPK protein 1 isoform 1 [Homo sapiens]

Protein Classification

CABIT and SAM_GAREM domain-containing protein( domain architecture ID 13785675)

protein containing domains CABIT, PHA03307, and SAM_GAREM

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CABIT pfam12736
Cell-cycle sustaining, positive selection,; The 'CABIT' domain (for 'cysteine-containing, all- ...
 32-323 8.16e-74

Cell-cycle sustaining, positive selection,; The 'CABIT' domain (for 'cysteine-containing, all- in Themis') is found in a newly identified gene family that has three mammalian homologs (Themis, Icb1 and 9130404H23Rik) that encode proteins with two CABIT domains and a highly conserved proline-rich region. In contrast, Fam59A, Fam59B and related proteins from mammals to cnidarians, including the insect Serrano proteins, have a single copy of the CABIT domain, a proline-rich region and often a C-terminal SAM (sterile-motif) domain. Multiple-sequence alignment has predicted that the CABIT domain adopts an all-strand structure with at least 12 strands, ie a dyad of six-stranded beta-barrel units. The CABIT domain contains a nearly absolutely conserved cysteine residue which is likely to be central to its function. CABIT domain proteins function downstream of tyrosine kinase signalling and interact with GRB2.


:

Pssm-ID: 463686  Cd Length: 261  Bit Score: 242.35  E-value: 8.16e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334724470   32 LPQIARLDNGECVEG----LRENDYLLIHSCRQWTTITAHSLEEGHYVIGPKIEIPVHYAGQFKLLEQDRDikepvqyFN 107
Cdd:pfam12736   1 LPQVVKVTSGIYGEGsvycLSKGDVLLIHGLKQAKKVVAQEVEEGRGVVGPKLLIPLSYPGLFKLLADEGP-------FE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334724470  108 SVEEVAKAFPERVYVMEDITFNVKVASGECNEDTEVYNITLCTGDELTLMGQAEILyakTFKEKSRLNTIFKkigklnsi 187
Cdd:pfam12736  74 SVEELARSFPIRVLAKEEGPDSVGVPMFRSSDDMSLANFTLQAGEELTLLGVEESS---GGKEELASVTVGD-------- 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334724470  188 sklgkgkmpCLICMNHRTNESISLPFQCKGRFStrsplELQMQEGEHTIRNIVEKTRLPVNVTVPS-PPPRNPYDlhfiR 266
Cdd:pfam12736 143 ---------YLICLVNQTGESVLLPLSCRGRFS-----EECEDEGEYTLREIVEKFKLPLNVKVVVgDPPRGDLD----A 204

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 334724470  267 EGHRYKFVNIQTKTVVVCCVLR---NNKILPMHFPLHLtvpKFSLPEHLVKGESWPETLV 323
Cdd:pfam12736 205 FTGELRLEPVYEEQAVVASPLLipvPFRKLEVPIPSDL---DVEVAEVTSADNKDYEEFL 261
SAM_GAREM cd09525
SAM domain of GAREM subfamily; SAM (sterile alpha motif) domain of GAREM (Grb2-associated and ...
 808-874 3.81e-39

SAM domain of GAREM subfamily; SAM (sterile alpha motif) domain of GAREM (Grb2-associated and regulator of Erk/MARK) protein subfamily (also known as FAM59A) is a putative protein-protein interaction domain. SAM domain is a widespread domain in signaling proteins. Proteins of this group have SAM at the C-terminus. Human GAREM protein is known to play a role in regulation of the EGF (Epidermal Growth Factor) receptor and of Gab or insulin preceptor substrate-1 family proteins. Grb2 (Growth factor receptor-bound) protein was identified as a binding partner of human GAREM. Proline-rich motifs and phosphorylation of two conserved tyrosines in GAREM are important for the interaction with the SH3 domains of Grb2 protein; however these motifs and residues do not belong to the SAM domain.


:

Pssm-ID: 188924  Cd Length: 67  Bit Score: 139.21  E-value: 3.81e-39
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334724470 808 LSGLSIEEVSKSLRFIGLSEDVISFFVTEKIDGNLLVQLTEEILSEDFKLSKLQVKKIMQFINGWRP 874
Cdd:cd09525    1 LSGLSIEEVSKSLRFIGLSEDVVSFFVTEKIDGNLLVQLTEEILSEDFKLSKLQVKKIMQFINGWRP 67
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
 414-766 7.87e-04

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.24  E-value: 7.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334724470  414 APFPHDILPYQDSGDSGSDylfPEASEESAGIPGKSELPYEELWLEEGKPSHQPLTRSLSeknrcdqfrGSVRSKCATSP 493
Cdd:PHA03307   98 ASPAREGSPTPPGPSSPDP---PPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPA---------AGASPAAVASD 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334724470  494 LPIPGTLGAAVKSSDTALPPPPVPPKSEAVREECRLLNAPPVPPRSAKPLSTSPSIPPRTVKPARQQTRSPSPTLSYYSS 573
Cdd:PHA03307  166 AASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESS 245

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334724470  574 GLHNISVTKT-DTNPSESTPVSCY----PCNRVKTDSVDLKS------PFGSPSAEAVSSRLSWPNHYSGASESQTRSDF 642
Cdd:PHA03307  246 GCGWGPENECpLPRPAPITLPTRIweasGWNGPSSRPGPASSssspreRSPSPSPSSPGSGPAPSSPRASSSSSSSRESS 325

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334724470  643 LLDPSRSYSYPRQKTPGTPKRNCPAPFDFDGCELLASPtSPVTAEFSSSVSGCPKSASYSLESTDVKSLAAGVTKQSTSC 722
Cdd:PHA03307  326 SSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPS-SPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDAT 404

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 334724470  723 PALPprapklveekvASETSPLPLKIDGAEEDPKSGSPDLSEDQ 766
Cdd:PHA03307  405 GRFP-----------AGRPRPSPLDAGAASGAFYARYPLLTPSG 437
 
Name Accession Description Interval E-value
CABIT pfam12736
Cell-cycle sustaining, positive selection,; The 'CABIT' domain (for 'cysteine-containing, all- ...
 32-323 8.16e-74

Cell-cycle sustaining, positive selection,; The 'CABIT' domain (for 'cysteine-containing, all- in Themis') is found in a newly identified gene family that has three mammalian homologs (Themis, Icb1 and 9130404H23Rik) that encode proteins with two CABIT domains and a highly conserved proline-rich region. In contrast, Fam59A, Fam59B and related proteins from mammals to cnidarians, including the insect Serrano proteins, have a single copy of the CABIT domain, a proline-rich region and often a C-terminal SAM (sterile-motif) domain. Multiple-sequence alignment has predicted that the CABIT domain adopts an all-strand structure with at least 12 strands, ie a dyad of six-stranded beta-barrel units. The CABIT domain contains a nearly absolutely conserved cysteine residue which is likely to be central to its function. CABIT domain proteins function downstream of tyrosine kinase signalling and interact with GRB2.


Pssm-ID: 463686  Cd Length: 261  Bit Score: 242.35  E-value: 8.16e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334724470   32 LPQIARLDNGECVEG----LRENDYLLIHSCRQWTTITAHSLEEGHYVIGPKIEIPVHYAGQFKLLEQDRDikepvqyFN 107
Cdd:pfam12736   1 LPQVVKVTSGIYGEGsvycLSKGDVLLIHGLKQAKKVVAQEVEEGRGVVGPKLLIPLSYPGLFKLLADEGP-------FE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334724470  108 SVEEVAKAFPERVYVMEDITFNVKVASGECNEDTEVYNITLCTGDELTLMGQAEILyakTFKEKSRLNTIFKkigklnsi 187
Cdd:pfam12736  74 SVEELARSFPIRVLAKEEGPDSVGVPMFRSSDDMSLANFTLQAGEELTLLGVEESS---GGKEELASVTVGD-------- 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334724470  188 sklgkgkmpCLICMNHRTNESISLPFQCKGRFStrsplELQMQEGEHTIRNIVEKTRLPVNVTVPS-PPPRNPYDlhfiR 266
Cdd:pfam12736 143 ---------YLICLVNQTGESVLLPLSCRGRFS-----EECEDEGEYTLREIVEKFKLPLNVKVVVgDPPRGDLD----A 204

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 334724470  267 EGHRYKFVNIQTKTVVVCCVLR---NNKILPMHFPLHLtvpKFSLPEHLVKGESWPETLV 323
Cdd:pfam12736 205 FTGELRLEPVYEEQAVVASPLLipvPFRKLEVPIPSDL---DVEVAEVTSADNKDYEEFL 261
SAM_GAREM cd09525
SAM domain of GAREM subfamily; SAM (sterile alpha motif) domain of GAREM (Grb2-associated and ...
 808-874 3.81e-39

SAM domain of GAREM subfamily; SAM (sterile alpha motif) domain of GAREM (Grb2-associated and regulator of Erk/MARK) protein subfamily (also known as FAM59A) is a putative protein-protein interaction domain. SAM domain is a widespread domain in signaling proteins. Proteins of this group have SAM at the C-terminus. Human GAREM protein is known to play a role in regulation of the EGF (Epidermal Growth Factor) receptor and of Gab or insulin preceptor substrate-1 family proteins. Grb2 (Growth factor receptor-bound) protein was identified as a binding partner of human GAREM. Proline-rich motifs and phosphorylation of two conserved tyrosines in GAREM are important for the interaction with the SH3 domains of Grb2 protein; however these motifs and residues do not belong to the SAM domain.


Pssm-ID: 188924  Cd Length: 67  Bit Score: 139.21  E-value: 3.81e-39
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334724470 808 LSGLSIEEVSKSLRFIGLSEDVISFFVTEKIDGNLLVQLTEEILSEDFKLSKLQVKKIMQFINGWRP 874
Cdd:cd09525    1 LSGLSIEEVSKSLRFIGLSEDVVSFFVTEKIDGNLLVQLTEEILSEDFKLSKLQVKKIMQFINGWRP 67
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 414-766 7.87e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.24  E-value: 7.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334724470  414 APFPHDILPYQDSGDSGSDylfPEASEESAGIPGKSELPYEELWLEEGKPSHQPLTRSLSeknrcdqfrGSVRSKCATSP 493
Cdd:PHA03307   98 ASPAREGSPTPPGPSSPDP---PPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPA---------AGASPAAVASD 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334724470  494 LPIPGTLGAAVKSSDTALPPPPVPPKSEAVREECRLLNAPPVPPRSAKPLSTSPSIPPRTVKPARQQTRSPSPTLSYYSS 573
Cdd:PHA03307  166 AASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESS 245

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334724470  574 GLHNISVTKT-DTNPSESTPVSCY----PCNRVKTDSVDLKS------PFGSPSAEAVSSRLSWPNHYSGASESQTRSDF 642
Cdd:PHA03307  246 GCGWGPENECpLPRPAPITLPTRIweasGWNGPSSRPGPASSssspreRSPSPSPSSPGSGPAPSSPRASSSSSSSRESS 325

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334724470  643 LLDPSRSYSYPRQKTPGTPKRNCPAPFDFDGCELLASPtSPVTAEFSSSVSGCPKSASYSLESTDVKSLAAGVTKQSTSC 722
Cdd:PHA03307  326 SSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPS-SPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDAT 404

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 334724470  723 PALPprapklveekvASETSPLPLKIDGAEEDPKSGSPDLSEDQ 766
Cdd:PHA03307  405 GRFP-----------AGRPRPSPLDAGAASGAFYARYPLLTPSG 437
 
Name Accession Description Interval E-value
CABIT pfam12736
Cell-cycle sustaining, positive selection,; The 'CABIT' domain (for 'cysteine-containing, all- ...
 32-323 8.16e-74

Cell-cycle sustaining, positive selection,; The 'CABIT' domain (for 'cysteine-containing, all- in Themis') is found in a newly identified gene family that has three mammalian homologs (Themis, Icb1 and 9130404H23Rik) that encode proteins with two CABIT domains and a highly conserved proline-rich region. In contrast, Fam59A, Fam59B and related proteins from mammals to cnidarians, including the insect Serrano proteins, have a single copy of the CABIT domain, a proline-rich region and often a C-terminal SAM (sterile-motif) domain. Multiple-sequence alignment has predicted that the CABIT domain adopts an all-strand structure with at least 12 strands, ie a dyad of six-stranded beta-barrel units. The CABIT domain contains a nearly absolutely conserved cysteine residue which is likely to be central to its function. CABIT domain proteins function downstream of tyrosine kinase signalling and interact with GRB2.


Pssm-ID: 463686  Cd Length: 261  Bit Score: 242.35  E-value: 8.16e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334724470   32 LPQIARLDNGECVEG----LRENDYLLIHSCRQWTTITAHSLEEGHYVIGPKIEIPVHYAGQFKLLEQDRDikepvqyFN 107
Cdd:pfam12736   1 LPQVVKVTSGIYGEGsvycLSKGDVLLIHGLKQAKKVVAQEVEEGRGVVGPKLLIPLSYPGLFKLLADEGP-------FE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334724470  108 SVEEVAKAFPERVYVMEDITFNVKVASGECNEDTEVYNITLCTGDELTLMGQAEILyakTFKEKSRLNTIFKkigklnsi 187
Cdd:pfam12736  74 SVEELARSFPIRVLAKEEGPDSVGVPMFRSSDDMSLANFTLQAGEELTLLGVEESS---GGKEELASVTVGD-------- 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334724470  188 sklgkgkmpCLICMNHRTNESISLPFQCKGRFStrsplELQMQEGEHTIRNIVEKTRLPVNVTVPS-PPPRNPYDlhfiR 266
Cdd:pfam12736 143 ---------YLICLVNQTGESVLLPLSCRGRFS-----EECEDEGEYTLREIVEKFKLPLNVKVVVgDPPRGDLD----A 204

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 334724470  267 EGHRYKFVNIQTKTVVVCCVLR---NNKILPMHFPLHLtvpKFSLPEHLVKGESWPETLV 323
Cdd:pfam12736 205 FTGELRLEPVYEEQAVVASPLLipvPFRKLEVPIPSDL---DVEVAEVTSADNKDYEEFL 261
SAM_GAREM cd09525
SAM domain of GAREM subfamily; SAM (sterile alpha motif) domain of GAREM (Grb2-associated and ...
 808-874 3.81e-39

SAM domain of GAREM subfamily; SAM (sterile alpha motif) domain of GAREM (Grb2-associated and regulator of Erk/MARK) protein subfamily (also known as FAM59A) is a putative protein-protein interaction domain. SAM domain is a widespread domain in signaling proteins. Proteins of this group have SAM at the C-terminus. Human GAREM protein is known to play a role in regulation of the EGF (Epidermal Growth Factor) receptor and of Gab or insulin preceptor substrate-1 family proteins. Grb2 (Growth factor receptor-bound) protein was identified as a binding partner of human GAREM. Proline-rich motifs and phosphorylation of two conserved tyrosines in GAREM are important for the interaction with the SH3 domains of Grb2 protein; however these motifs and residues do not belong to the SAM domain.


Pssm-ID: 188924  Cd Length: 67  Bit Score: 139.21  E-value: 3.81e-39
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334724470 808 LSGLSIEEVSKSLRFIGLSEDVISFFVTEKIDGNLLVQLTEEILSEDFKLSKLQVKKIMQFINGWRP 874
Cdd:cd09525    1 LSGLSIEEVSKSLRFIGLSEDVVSFFVTEKIDGNLLVQLTEEILSEDFKLSKLQVKKIMQFINGWRP 67
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 815-870 6.26e-07

SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.


Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 46.85  E-value: 6.26e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 334724470 815 EVSKSLRFIGLsEDVISFFVTEKIDGNLLVQLTEEILSEDFKLSKLQVKKIMQFIN 870
Cdd:cd09487    1 DVAEWLESLGL-EQYADLFRKNEIDGDALLLLTDEDLKELGITSPGHRKKILRAIQ 55
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
 808-870 4.14e-06

SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins is a putative protein-protein interaction domain. Proteins of this group contain multiple domains: SAM, one or more WD40 repeats and U-box (derived version of the RING-finger domain). Apparently the WDSUB1 subfamily proteins participate in protein degradation through ubiquitination, since U-box domain are known as a member of E3 ubiquitin ligase family, while SAM and WD40 domains most probably are responsible for an E2 ubiquitin-conjugating enzyme binding and a target protein binding.


Pssm-ID: 188904  Cd Length: 72  Bit Score: 45.39  E-value: 4.14e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334724470 808 LSGLSIEEVSKSLRFIGLsEDVISFFVTEKIDGNLLVQLTEEILSEDFKLSKL-QVKKIMQFIN 870
Cdd:cd09505    2 LQDWSEEDVCTWLRSIGL-EQYVEVFRANNIDGKELLNLTKESLSKDLKIESLgHRNKILRKIE 64
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 414-766 7.87e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.24  E-value: 7.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334724470  414 APFPHDILPYQDSGDSGSDylfPEASEESAGIPGKSELPYEELWLEEGKPSHQPLTRSLSeknrcdqfrGSVRSKCATSP 493
Cdd:PHA03307   98 ASPAREGSPTPPGPSSPDP---PPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPA---------AGASPAAVASD 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334724470  494 LPIPGTLGAAVKSSDTALPPPPVPPKSEAVREECRLLNAPPVPPRSAKPLSTSPSIPPRTVKPARQQTRSPSPTLSYYSS 573
Cdd:PHA03307  166 AASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESS 245

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334724470  574 GLHNISVTKT-DTNPSESTPVSCY----PCNRVKTDSVDLKS------PFGSPSAEAVSSRLSWPNHYSGASESQTRSDF 642
Cdd:PHA03307  246 GCGWGPENECpLPRPAPITLPTRIweasGWNGPSSRPGPASSssspreRSPSPSPSSPGSGPAPSSPRASSSSSSSRESS 325

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334724470  643 LLDPSRSYSYPRQKTPGTPKRNCPAPFDFDGCELLASPtSPVTAEFSSSVSGCPKSASYSLESTDVKSLAAGVTKQSTSC 722
Cdd:PHA03307  326 SSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPS-SPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDAT 404

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 334724470  723 PALPprapklveekvASETSPLPLKIDGAEEDPKSGSPDLSEDQ 766
Cdd:PHA03307  405 GRFP-----------AGRPRPSPLDAGAASGAFYARYPLLTPSG 437
SAM_SGMS1-like cd09515
SAM domain of sphingomyelin synthase related subfamily; SAM (sterile alpha motif) domain of ...
 812-865 1.14e-03

SAM domain of sphingomyelin synthase related subfamily; SAM (sterile alpha motif) domain of SGMS-like (sphingomyelin synthase) subfamily is a potential protein-protein interaction domain. This group of proteins is related to sphingomyelin synthase 1, and contains an N-terminal SAM domain. The function of SGMS1-like proteins is unknown; they may play a role in sphingolipid metabolism.


Pssm-ID: 188914  Cd Length: 70  Bit Score: 38.38  E-value: 1.14e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 334724470 812 SIEEVSKSLRFIGLSEDVISFFVTEKIDGNLLVQLTEeilsEDFKLSKLQVKKI 865
Cdd:cd09515    5 TCEDVAKWLKKEGFSKYVDLLCNKHRIDGKVLLSLTE----EDLRSPPLEIKVL 54
 
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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