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Conserved domains on  [gi|270265910|ref|NP_001161713|]
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GRB2-associated and regulator of MAPK protein 2 isoform 1 [Homo sapiens]

Protein Classification

CABIT and SAM_GAREM domain-containing protein( domain architecture ID 12119424)

CABIT and SAM_GAREM domain-containing protein

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- ...
29-341 4.95e-71

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: 235.03  E-value: 4.95e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265910   29 LPTLACLGPGEYAEG----VSERDILLIHSCRQWTTVTAHTLEEGHYVIGPKIDIPLQYPGKFKLLEQARDvrepvryFS 104
Cdd:pfam12736   1 LPQVVKVTSGIYGEGsvycLSKGDVLLIHGLKQAKKVVAQEVEEGRGVVGPKLLIPLSYPGLFKLLADEGP-------FE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265910  105 SVEEVASVFPDRIFVMEAITFSVKVVSGEFSEDSEVYNFTLHAGDELTLMGQAEILCAkttKERSRFTTLLRklgragal 184
Cdd:pfam12736  74 SVEELARSFPIRVLAKEEGPDSVGVPMFRSSDDMSLANFTLQAGEELTLLGVEESSGG---KEELASVTVGD-------- 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265910  185 agvggggpasagaaggtggggarpvkgkmpCLICMNHRTNESLSLPFQCQGRFStrsplELQMQEGEHTVRAIIERVRLP 264
Cdd:pfam12736 143 ------------------------------YLICLVNQTGESVLLPLSCRGRFS-----EECEDEGEYTLREIVEKFKLP 187
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 270265910  265 VNVLVPSR-PPRNPYDlhpvREGHCYKLVSIISKTVVLGLALRREGPAPLHFLLLTDTPRFALPQGLLAGDPRVERLV 341
Cdd:pfam12736 188 LNVKVVVGdPPRGDLD----AFTGELRLEPVYEEQAVVASPLLIPVPFRKLEVPIPSDLDVEVAEVTSADNKDYEEFL 261
SAM_GAREM cd09525
SAM domain of GAREM subfamily; SAM (sterile alpha motif) domain of GAREM (Grb2-associated and ...
806-872 1.21e-31

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: 117.64  E-value: 1.21e-31
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 270265910 806 LSALSLEEVSRSLRFIGLSEDVVSFFARERIDGSIFVQLSEDILADDFHLTKLQVKKIMQFIKGWRP 872
Cdd:cd09525    1 LSGLSIEEVSKSLRFIGLSEDVVSFFVTEKIDGNLLVQLTEEILSEDFKLSKLQVKKIMQFINGWRP 67
PHA03247 super family cl33720
large tegument protein UL36; Provisional
568-813 2.31e-06

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.86  E-value: 2.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265910  568 RPAPGPLPSTTQPSQASRALTEPLSGRAASLLGADTPVKTYHSCPPLFKPSHPQKRFAPFGALNPFSGPAYPSGPSAALS 647
Cdd:PHA03247 2768 APAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPP 2847
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265910  648 SgPRTTSGPVATSGPAYSPGPASPGQAYSAAPPSSCAP--SSSSSSEWQEPVLEPFDPFELGQGSSPEPELLRSQEPRAV 725
Cdd:PHA03247 2848 P-SLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRrlARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPP 2926
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265910  726 GTPGPGPRLSPLGPSKAFEPEGLVLHQVPTPLSPAALQGPEAGGALFLTQGRLEGP------PASPRDGATGFGVRDASS 799
Cdd:PHA03247 2927 PQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPapsreaPASSTPPLTGHSLSRVSS 3006
                         250
                  ....*....|....
gi 270265910  800 WQppadlSALSLEE 813
Cdd:PHA03247 3007 WA-----SSLALHE 3015
 
Name Accession Description Interval E-value
CABIT pfam12736
Cell-cycle sustaining, positive selection,; The 'CABIT' domain (for 'cysteine-containing, all- ...
29-341 4.95e-71

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: 235.03  E-value: 4.95e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265910   29 LPTLACLGPGEYAEG----VSERDILLIHSCRQWTTVTAHTLEEGHYVIGPKIDIPLQYPGKFKLLEQARDvrepvryFS 104
Cdd:pfam12736   1 LPQVVKVTSGIYGEGsvycLSKGDVLLIHGLKQAKKVVAQEVEEGRGVVGPKLLIPLSYPGLFKLLADEGP-------FE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265910  105 SVEEVASVFPDRIFVMEAITFSVKVVSGEFSEDSEVYNFTLHAGDELTLMGQAEILCAkttKERSRFTTLLRklgragal 184
Cdd:pfam12736  74 SVEELARSFPIRVLAKEEGPDSVGVPMFRSSDDMSLANFTLQAGEELTLLGVEESSGG---KEELASVTVGD-------- 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265910  185 agvggggpasagaaggtggggarpvkgkmpCLICMNHRTNESLSLPFQCQGRFStrsplELQMQEGEHTVRAIIERVRLP 264
Cdd:pfam12736 143 ------------------------------YLICLVNQTGESVLLPLSCRGRFS-----EECEDEGEYTLREIVEKFKLP 187
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 270265910  265 VNVLVPSR-PPRNPYDlhpvREGHCYKLVSIISKTVVLGLALRREGPAPLHFLLLTDTPRFALPQGLLAGDPRVERLV 341
Cdd:pfam12736 188 LNVKVVVGdPPRGDLD----AFTGELRLEPVYEEQAVVASPLLIPVPFRKLEVPIPSDLDVEVAEVTSADNKDYEEFL 261
SAM_GAREM cd09525
SAM domain of GAREM subfamily; SAM (sterile alpha motif) domain of GAREM (Grb2-associated and ...
806-872 1.21e-31

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: 117.64  E-value: 1.21e-31
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 270265910 806 LSALSLEEVSRSLRFIGLSEDVVSFFARERIDGSIFVQLSEDILADDFHLTKLQVKKIMQFIKGWRP 872
Cdd:cd09525    1 LSGLSIEEVSKSLRFIGLSEDVVSFFVTEKIDGNLLVQLTEEILSEDFKLSKLQVKKIMQFINGWRP 67
PHA03247 PHA03247
large tegument protein UL36; Provisional
568-813 2.31e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.86  E-value: 2.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265910  568 RPAPGPLPSTTQPSQASRALTEPLSGRAASLLGADTPVKTYHSCPPLFKPSHPQKRFAPFGALNPFSGPAYPSGPSAALS 647
Cdd:PHA03247 2768 APAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPP 2847
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265910  648 SgPRTTSGPVATSGPAYSPGPASPGQAYSAAPPSSCAP--SSSSSSEWQEPVLEPFDPFELGQGSSPEPELLRSQEPRAV 725
Cdd:PHA03247 2848 P-SLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRrlARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPP 2926
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265910  726 GTPGPGPRLSPLGPSKAFEPEGLVLHQVPTPLSPAALQGPEAGGALFLTQGRLEGP------PASPRDGATGFGVRDASS 799
Cdd:PHA03247 2927 PQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPapsreaPASSTPPLTGHSLSRVSS 3006
                         250
                  ....*....|....
gi 270265910  800 WQppadlSALSLEE 813
Cdd:PHA03247 3007 WA-----SSLALHE 3015
 
Name Accession Description Interval E-value
CABIT pfam12736
Cell-cycle sustaining, positive selection,; The 'CABIT' domain (for 'cysteine-containing, all- ...
29-341 4.95e-71

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: 235.03  E-value: 4.95e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265910   29 LPTLACLGPGEYAEG----VSERDILLIHSCRQWTTVTAHTLEEGHYVIGPKIDIPLQYPGKFKLLEQARDvrepvryFS 104
Cdd:pfam12736   1 LPQVVKVTSGIYGEGsvycLSKGDVLLIHGLKQAKKVVAQEVEEGRGVVGPKLLIPLSYPGLFKLLADEGP-------FE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265910  105 SVEEVASVFPDRIFVMEAITFSVKVVSGEFSEDSEVYNFTLHAGDELTLMGQAEILCAkttKERSRFTTLLRklgragal 184
Cdd:pfam12736  74 SVEELARSFPIRVLAKEEGPDSVGVPMFRSSDDMSLANFTLQAGEELTLLGVEESSGG---KEELASVTVGD-------- 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265910  185 agvggggpasagaaggtggggarpvkgkmpCLICMNHRTNESLSLPFQCQGRFStrsplELQMQEGEHTVRAIIERVRLP 264
Cdd:pfam12736 143 ------------------------------YLICLVNQTGESVLLPLSCRGRFS-----EECEDEGEYTLREIVEKFKLP 187
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 270265910  265 VNVLVPSR-PPRNPYDlhpvREGHCYKLVSIISKTVVLGLALRREGPAPLHFLLLTDTPRFALPQGLLAGDPRVERLV 341
Cdd:pfam12736 188 LNVKVVVGdPPRGDLD----AFTGELRLEPVYEEQAVVASPLLIPVPFRKLEVPIPSDLDVEVAEVTSADNKDYEEFL 261
SAM_GAREM cd09525
SAM domain of GAREM subfamily; SAM (sterile alpha motif) domain of GAREM (Grb2-associated and ...
806-872 1.21e-31

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: 117.64  E-value: 1.21e-31
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 270265910 806 LSALSLEEVSRSLRFIGLSEDVVSFFARERIDGSIFVQLSEDILADDFHLTKLQVKKIMQFIKGWRP 872
Cdd:cd09525    1 LSGLSIEEVSKSLRFIGLSEDVVSFFVTEKIDGNLLVQLTEEILSEDFKLSKLQVKKIMQFINGWRP 67
PHA03247 PHA03247
large tegument protein UL36; Provisional
568-813 2.31e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.86  E-value: 2.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265910  568 RPAPGPLPSTTQPSQASRALTEPLSGRAASLLGADTPVKTYHSCPPLFKPSHPQKRFAPFGALNPFSGPAYPSGPSAALS 647
Cdd:PHA03247 2768 APAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPP 2847
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265910  648 SgPRTTSGPVATSGPAYSPGPASPGQAYSAAPPSSCAP--SSSSSSEWQEPVLEPFDPFELGQGSSPEPELLRSQEPRAV 725
Cdd:PHA03247 2848 P-SLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRrlARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPP 2926
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265910  726 GTPGPGPRLSPLGPSKAFEPEGLVLHQVPTPLSPAALQGPEAGGALFLTQGRLEGP------PASPRDGATGFGVRDASS 799
Cdd:PHA03247 2927 PQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPapsreaPASSTPPLTGHSLSRVSS 3006
                         250
                  ....*....|....
gi 270265910  800 WQppadlSALSLEE 813
Cdd:PHA03247 3007 WA-----SSLALHE 3015
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
806-868 4.34e-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: 45.00  E-value: 4.34e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 270265910 806 LSALSLEEVSRSLRFIGLsEDVVSFFARERIDGSIFVQLSEDILADDFHLTKL-QVKKIMQFIK 868
Cdd:cd09505    2 LQDWSEEDVCTWLRSIGL-EQYVEVFRANNIDGKELLNLTKESLSKDLKIESLgHRNKILRKIE 64
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
813-868 8.30e-05

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: 41.07  E-value: 8.30e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 270265910 813 EVSRSLRFIGLsEDVVSFFARERIDGSIFVQLSEDILADDFHLTKLQVKKIMQFIK 868
Cdd:cd09487    1 DVAEWLESLGL-EQYADLFRKNEIDGDALLLLTDEDLKELGITSPGHRKKILRAIQ 55
PHA03247 PHA03247
large tegument protein UL36; Provisional
476-765 2.54e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.93  E-value: 2.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265910  476 AVKEECRLLNAPPVP-----PRGGNGSGRLSSSP-PVPPRFPKLQPVHSPSSSLSYYSSGLQDGAGSRSGSGSPSPDTys 549
Cdd:PHA03247 2581 AVTSRARRPDAPPQSarpraPVDDRGDPRGPAPPsPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAP-- 2658
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265910  550 lycypctwGDCKVGESSSRPAPGPLPSTTQPSQASRALTEPLsGRAASLLGADTPVKTYHSCPPLFKPSHPQKRFAPFGA 629
Cdd:PHA03247 2659 --------GRVSRPRRARRLGRAAQASSPPQRPRRRAARPTV-GSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAAR 2729
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265910  630 LNPFSGPAYPSGP----SAALSSGPRTTSGPVATSGPAYSPGPASPGQAYSAAPPSSCAPSSSSSSEWQEPVLEPFDPfe 705
Cdd:PHA03247 2730 QASPALPAAPAPPavpaGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADP-- 2807
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265910  706 LGQGSSPEPELLRSQEPRAVGTPGPGPRLSPLGPSKAFEPEGLVLHQVPTPLSPAALQGP 765
Cdd:PHA03247 2808 PAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPP 2867
PHA03378 PHA03378
EBNA-3B; Provisional
566-784 3.68e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 41.21  E-value: 3.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265910 566 SSRPAPGPLPSTTQPSQASRALT-EPLSGRAASLLGADTPVKTYHSCPPLFK------PSHPQKRFAPFGALNPFSGPAY 638
Cdd:PHA03378 593 AQTPWPVPHPSQTPEPPTTQSHIpETSAPRQWPMPLRPIPMRPLRMQPITFNvlvfptPHQPPQVEITPYKPTWTQIGHI 672
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265910 639 PSGPSAALSSGPRTTS-GPVATSGPAYSPGPASPGQAYSAAPPSSCAPSSSSSSEWQEPVLEPFDPFELGQGSSPEPELL 717
Cdd:PHA03378 673 PYQPSPTGANTMLPIQwAPGTMQPPPRAPTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPG 752
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 270265910 718 RSQEPRAVGTPGPGPRLSPLGPSKAFEPEGlvlhqvptplSPAALQGPEAGGAlflTQGRLEGPPAS 784
Cdd:PHA03378 753 RARPPAAAPGRARPPAAAPGAPTPQPPPQA----------PPAPQQRPRGAPT---PQPPPQAGPTS 806
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
563-787 9.69e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 39.47  E-value: 9.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265910 563 GESSSRPAPGPLPSTTQPSQASRALTEPLSGRAAsllgadtpvktyhscPPLFKPSHPQKRFAPFGALNPFSgPAYPSGP 642
Cdd:PRK12323 371 GAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPA---------------APAAAPAAAAAARAVAAAPARRS-PAPEALA 434
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265910 643 SAALSSGPRTTSGPVATSGPAYSPGPASPGQAYSAAPPSSCAPSSSSSSE---WQEPVLEPFDPFELGQGSSPEPELLRS 719
Cdd:PRK12323 435 AARQASARGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAApaaAPAPADDDPPPWEELPPEFASPAPAQP 514
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 270265910 720 QEPRAVGTPGPGPRLSPLGPSKAFEPEGLVLHQVPTPLSPAALQGPEAGGALFLTQGRLegPPASPRD 787
Cdd:PRK12323 515 DAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGL--PDMFDGD 580
 
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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