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Conserved domains on  [gi|946809932|ref|XP_014388950|]
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PREDICTED: diacylglycerol kinase theta [Myotis brandtii]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DAGK_acc super family cl02440
Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts ...
 503-655 6.48e-70

Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. This domain is assumed to be an accessory domain: its function is unknown.


The actual alignment was detected with superfamily member smart00045:

Pssm-ID: 470579  Cd Length: 160  Bit Score: 225.29  E-value: 6.48e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946809932   503 QMSNYCGIGIDAELSLDFHQAREEEPSKFTSRFHNKGVYVRVGLQKMNHA--RSLHKEIRLQVEQQEVELP-SIEGLIFI 579
Cdd:smart00045   1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRtcKDLHERIELECDGVDVDLPnSLEGIAVL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946809932   580 NIPSWGSGADLWG--SDSDSRFEKPRMDDGLLEVVGVTGVMHMVSM**GLRSGIRIAQGAYFRVTLL--KATPVQVDGEP 655
Cdd:smart00045  81 NIPSYGGGTNLWGttDKEDLNFSKQSHDDGLLEVVGLTGAMHMAQIRQVGLAGRRIAQCSEVRITIKtsKTIPMQVDGEP 160
Ubl1_cv_Nsp3_N-like super family cl28922
first ubiquitin-like (Ubl) domain located at the N-terminus of coronavirus SARS-CoV ...
 210-304 6.77e-37

first ubiquitin-like (Ubl) domain located at the N-terminus of coronavirus SARS-CoV non-structural protein 3 (Nsp3) and related proteins; This ubiquitin-like (Ubl) domain (Ubl1) is found at the N-terminus of coronavirus Nsp3, a large multi-functional multi-domain protein which is an essential component of the replication/transcription complex (RTC). The functions of Ubl1 in CoVs are related to single-stranded RNA (ssRNA) binding and to interacting with the nucleocapsid (N) protein. SARS-CoV Ubl1 has been shown to bind ssRNA having AUA patterns, and since the 5'-UTR of the SARS-CoV genome has a number of AUA repeats, it may bind there. In mouse hepatitis virus (MHV), this Ubl1 domain binds the cognate N protein. Adjacent to Ubl1 is a Glu-rich acidic region (also referred to as hypervariable region, HVR); Ubl1 together with HVR has been called Nsp3a. Currently, the function of HVR in CoVs is unknown. This model corresponds to one of two Ubl domains in Nsp3; the other is located N-terminal to the papain-like protease (PLpro) and is not represented by this model.


The actual alignment was detected with superfamily member cd01783:

Pssm-ID: 475130  Cd Length: 95  Bit Score: 133.12  E-value: 6.77e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946809932 210 VLKIYPAWLKVGVAYVSIRVTPESTARTVVLEVLPLLGRQAEGPESFQLEEVYMGSRQVQRTVLADEESLLSRLrDIRQT 289
Cdd:cd01783    2 YIRVYPGWLKVGVAYKSIPVTKETTVEEVIKEALPKFGLQDEDPEDFRLVEVLMDKGVVERVMLRDECPWLILL-DIRKE 80

                         90
                 ....*....|....*
gi 946809932 290 SLRQMSQTRFYVAES 304
Cdd:cd01783   81 SLRQMRQTRFYLQQK 95
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 402-489 3.00e-30

Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. DAG can be produced from the hydrolysis of phosphatidylinositol 4,5-bisphosphate (PIP2) by a phosphoinositide-specific phospholipase C and by the degradation of phosphatidylcholine (PC) by a phospholipase C or the concerted actions of phospholipase D and phosphatidate phosphohydrolase. This domain is presumed to be the catalytic domain. Bacterial homologues areknown.


:

Pssm-ID: 214487 [Multi-domain]  Cd Length: 124  Bit Score: 115.47  E-value: 3.00e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946809932   402 LVFVNPKSGGLKGRDLLCSFRKLLNPHQVFELTNGGPLPGLHVFAQMPRF-RVLVCGGDGTVGWVLAALeeMRHQLACPE 480
Cdd:smart00046   1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVPDFnRVLVCGGDGTVGWVLNAL--DKRELPLPE 78


                   ....*....
gi 946809932   481 PPGAGAPGG 489
Cdd:smart00046  79 PPVAVLPLG 87
RA1_DAGK-theta cd17111
Ras-associating (RA) domain 1 found in diacylgylcerol kinase theta (DAGK-theta) and similar ...
 123-206 1.82e-22

Ras-associating (RA) domain 1 found in diacylgylcerol kinase theta (DAGK-theta) and similar proteins; DAGK phosphorylates the second messenger diacylglycerol to phosphatidic acid as part of a protein kinase C pathway. DAGK-theta is characterized as a type V DAGK that has three cysteine-rich domains (all other isoforms have two), a proline/glycine-rich domain at its N-terminal, and a proposed Ras-associating (RA) domain. RA domain-containing proteins function by interacting with Ras proteins directly or indirectly and are involved in several different functions ranging from tumor suppression to being oncoproteins. Ras proteins are small GTPases that are involved in cellular signal transduction. The RA domain has a beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub). Ub is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair in eukaryotes. Ten mammalian isoforms of DAGK have been identified to date which are organized into five categories based on the domain architecture. DAGK-theta also contains a pleckstrin homology (PH) domain. The subcellular localization and the activity of DAGK-theta are regulated in a complex (stimulation- and cell type-dependent) manner. This family corresponds to the first RA domain of DAGK-theta.


:

Pssm-ID: 340631  Cd Length: 91  Bit Score: 91.88  E-value: 1.82e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946809932 123 KQTLKIFDGSDAVHRNRFRVVSVPRLARSEEVLEAALRAYYITEDPRGFELQAL--PWPLSEEE-----GGRGPRSREVS 195
Cdd:cd17111    1 KEIVKVFDGNASLKRNQFRLITVPRNASVEQVLEAALRAFHIPDDPENYYLTDAyeSSLGDEREledpgPLRNLVRREGK 80

                         90
                 ....*....|.
gi 946809932 196 PEAWIIRTLPR 206
Cdd:cd17111   81 RPAIFLRYKEK 91
C1 super family cl00040
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ...
 51-81 1.16e-10

protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains. It contains the motif HX12CX2CXnCX2CX4HX2CX7C, where C and H are cysteine and histidine, respectively; X represents other residues; and n is either 13 or 14. C1 has a globular fold with two separate Zn(2+)-binding sites. It was originally discovered as lipid-binding modules in protein kinase C (PKC) isoforms. C1 domains that bind and respond to phorbol esters (PE) and diacylglycerol (DAG) are referred to as typical, and those that do not respond to PE and DAG are deemed atypical. A C1 domain may also be referred to as PKC or non-PKC C1, based on the parent protein's activity. Most C1 domain-containing non-PKC proteins act as lipid kinases and scaffolds, except PKD which acts as a protein kinase. PKC C1 domains play roles in membrane translocation and activation of the enzyme.


The actual alignment was detected with superfamily member cd20803:

Pssm-ID: 412127  Cd Length: 56  Bit Score: 57.32  E-value: 1.16e-10
                         10        20        30
                 ....*....|....*....|....*....|.
gi 946809932  51 LTPGFVPTVCNFMSHEKCLRQVKTPCTSLAP 81
Cdd:cd20803   26 LNQGYQCEVCNFVSHERCLKTVVTPCSSIAP 56
 
Name Accession Description Interval E-value
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 503-655 6.48e-70

Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. DAG can be produced from the hydrolysis of phosphatidylinositol 4,5-bisphosphate (PIP2) by a phosphoinositide-specific phospholipase C and by the degradation of phosphatidylcholine (PC) by a phospholipase C or the concerted actions of phospholipase D and phosphatidate phosphohydrolase. This domain might either be an accessory domain or else contribute to the catalytic domain. Bacterial homologues are known.


Pssm-ID: 214486  Cd Length: 160  Bit Score: 225.29  E-value: 6.48e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946809932   503 QMSNYCGIGIDAELSLDFHQAREEEPSKFTSRFHNKGVYVRVGLQKMNHA--RSLHKEIRLQVEQQEVELP-SIEGLIFI 579
Cdd:smart00045   1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRtcKDLHERIELECDGVDVDLPnSLEGIAVL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946809932   580 NIPSWGSGADLWG--SDSDSRFEKPRMDDGLLEVVGVTGVMHMVSM**GLRSGIRIAQGAYFRVTLL--KATPVQVDGEP 655
Cdd:smart00045  81 NIPSYGGGTNLWGttDKEDLNFSKQSHDDGLLEVVGLTGAMHMAQIRQVGLAGRRIAQCSEVRITIKtsKTIPMQVDGEP 160
DAGK_acc pfam00609
Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts ...
 503-655 9.94e-67

Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. This domain is assumed to be an accessory domain: its function is unknown.


Pssm-ID: 459866  Cd Length: 158  Bit Score: 216.70  E-value: 9.94e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946809932  503 QMSNYCGIGIDAELSLDFHQAREEEPSKFTSRFHNKGVYVRVGLQKM--NHARSLHKEIRLQVEQQEVELP-SIEGLIFI 579
Cdd:pfam00609   1 VMNNYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDMfqRSCKNLIEKVELEVDGKDLPLPkSLEGIVVL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 946809932  580 NIPSWGSGADLWGSDSDSR--FEKPRMDDGLLEVVGVTGVMHMVSM**GLRSGIRIAQGAYFRVTLLKATPVQVDGEP 655
Cdd:pfam00609  81 NIPSYAGGTDLWGNSKEDGlgFAPQSVDDGLLEVVGLTGALHLGQVQVGLGSAKRIAQGGPIRITTKKKIPMQVDGEP 158
RA2_DAGK-theta cd01783
Ras-associating (RA) domain 2 found in diacylgylcerol kinase theta (DAGK-theta) and similar ...
 210-304 6.77e-37

Ras-associating (RA) domain 2 found in diacylgylcerol kinase theta (DAGK-theta) and similar proteins; DAGK phosphorylates the second messenger diacylglycerol to phosphatidic acid as part of a protein kinase C pathway. DAGK-theta is characterized as a type V DAGK that has three cysteine-rich domains (all other isoforms have two), a proline/glycine-rich domain at its N-terminal, and a proposed Ras-associating (RA) domain. RA domain-containing proteins function by interacting with Ras proteins directly or indirectly and are involved in several different functions ranging from tumor suppression to being oncoproteins. Ras proteins are small GTPases that are involved in cellular signal transduction. The RA domain has a beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub). Ub is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair in eukaryotes. There are ten mammalian isoforms of DAGK have been identified to date, these are organized into five categories based on the domain architecture. DAGK-theta also contains a pleckstrin homology (PH) domain. The subcellular localization and the activity of DAGK-theta are regulated in a complex (stimulation- and cell type-dependent) manner. This family corresponds to the second RA domain of DAGK-theta.


Pssm-ID: 340481  Cd Length: 95  Bit Score: 133.12  E-value: 6.77e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946809932 210 VLKIYPAWLKVGVAYVSIRVTPESTARTVVLEVLPLLGRQAEGPESFQLEEVYMGSRQVQRTVLADEESLLSRLrDIRQT 289
Cdd:cd01783    2 YIRVYPGWLKVGVAYKSIPVTKETTVEEVIKEALPKFGLQDEDPEDFRLVEVLMDKGVVERVMLRDECPWLILL-DIRKE 80

                         90
                 ....*....|....*
gi 946809932 290 SLRQMSQTRFYVAES 304
Cdd:cd01783   81 SLRQMRQTRFYLQQK 95
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 402-489 3.00e-30

Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. DAG can be produced from the hydrolysis of phosphatidylinositol 4,5-bisphosphate (PIP2) by a phosphoinositide-specific phospholipase C and by the degradation of phosphatidylcholine (PC) by a phospholipase C or the concerted actions of phospholipase D and phosphatidate phosphohydrolase. This domain is presumed to be the catalytic domain. Bacterial homologues areknown.


Pssm-ID: 214487 [Multi-domain]  Cd Length: 124  Bit Score: 115.47  E-value: 3.00e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946809932   402 LVFVNPKSGGLKGRDLLCSFRKLLNPHQVFELTNGGPLPGLHVFAQMPRF-RVLVCGGDGTVGWVLAALeeMRHQLACPE 480
Cdd:smart00046   1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVPDFnRVLVCGGDGTVGWVLNAL--DKRELPLPE 78


                   ....*....
gi 946809932   481 PPGAGAPGG 489
Cdd:smart00046  79 PPVAVLPLG 87
RA1_DAGK-theta cd17111
Ras-associating (RA) domain 1 found in diacylgylcerol kinase theta (DAGK-theta) and similar ...
 123-206 1.82e-22

Ras-associating (RA) domain 1 found in diacylgylcerol kinase theta (DAGK-theta) and similar proteins; DAGK phosphorylates the second messenger diacylglycerol to phosphatidic acid as part of a protein kinase C pathway. DAGK-theta is characterized as a type V DAGK that has three cysteine-rich domains (all other isoforms have two), a proline/glycine-rich domain at its N-terminal, and a proposed Ras-associating (RA) domain. RA domain-containing proteins function by interacting with Ras proteins directly or indirectly and are involved in several different functions ranging from tumor suppression to being oncoproteins. Ras proteins are small GTPases that are involved in cellular signal transduction. The RA domain has a beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub). Ub is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair in eukaryotes. Ten mammalian isoforms of DAGK have been identified to date which are organized into five categories based on the domain architecture. DAGK-theta also contains a pleckstrin homology (PH) domain. The subcellular localization and the activity of DAGK-theta are regulated in a complex (stimulation- and cell type-dependent) manner. This family corresponds to the first RA domain of DAGK-theta.


Pssm-ID: 340631  Cd Length: 91  Bit Score: 91.88  E-value: 1.82e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946809932 123 KQTLKIFDGSDAVHRNRFRVVSVPRLARSEEVLEAALRAYYITEDPRGFELQAL--PWPLSEEE-----GGRGPRSREVS 195
Cdd:cd17111    1 KEIVKVFDGNASLKRNQFRLITVPRNASVEQVLEAALRAFHIPDDPENYYLTDAyeSSLGDEREledpgPLRNLVRREGK 80

                         90
                 ....*....|.
gi 946809932 196 PEAWIIRTLPR 206
Cdd:cd17111   81 RPAIFLRYKEK 91
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 400-477 1.39e-18

Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. The catalytic domain is assumed from the finding of bacterial homologs. YegS is the Escherichia coli protein in this family whose crystal structure reveals an active site in the inter-domain cleft formed by four conserved sequence motifs, revealing a novel metal-binding site. The residues of this site are conserved across the family.


Pssm-ID: 425868 [Multi-domain]  Cd Length: 125  Bit Score: 82.25  E-value: 1.39e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946809932  400 PLLVFVNPKSGGLKGRDLLCSFRKLLNPHQV-FELTN-GGPLPGLHVFAQMPR---FRVLVCGGDGTVGWVLAALEEMRH 474
Cdd:pfam00781   1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVeVELVLtEGPGDALELAREAAEdgyDRIVVAGGDGTVNEVLNGLAGLAT 80


                  ...
gi 946809932  475 QLA 477
Cdd:pfam00781  81 RPP 83
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 401-655 3.89e-17

Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, General function prediction only];


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 82.59  E-value: 3.89e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946809932 401 LLVFVNPKSGGLKGRDLLCSFRKLLNPH----QVFELTNGGPLPGLHVFAQMPRFRVLV-CGGDGTVGWVLAALEEMRHQ 475
Cdd:COG1597    5 ALLIVNPASGRGRAARLLERLVAALRAAglevEVLETESPGDATELAREAAAEGADLVVaAGGDGTVNEVANGLAGTGPP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946809932 476 LACpeppgagAPGG----------LP-------------RPRRVvcpQIVQMS-----NYCGIGIDAELSLDFHQAReee 527
Cdd:COG1597   85 LGI-------LPLGtgndfaralgIPldpeaalealltgRTRRI---DLGRVNgryflNVAGIGFDAEVVERANRAL--- 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946809932 528 pskftSRFHNKGVYVRVGLQKMNHARSLHkeIRLQVEQQEVELPSIegLIFI-NIPSWGSGADLwgsdsdsrFEKPRMDD 606
Cdd:COG1597  152 -----KRRLGKLAYVLAALRALLRYRPFR--LRIELDGEEIEGEAL--LVAVgNGPYYGGGLRL--------APDASLDD 214

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 946809932 607 GLLEVVGVT--GVMHMVSM**GLRSG-------IRIAQGAYFRVTLLKATPVQVDGEP 655
Cdd:COG1597  215 GLLDVVVVRplSRLRLLRLLPRLLRGrhlrhpgVRYFRAREVEIESDRPLPVQLDGEP 272
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 208-306 9.60e-11

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Recent evidence (not yet in MEDLINE) shows that some RA domains do NOT bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase.


Pssm-ID: 425871  Cd Length: 93  Bit Score: 58.88  E-value: 9.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946809932  208 QDVLKIYPAWLKVGVAYVSIRVTPESTARTVVLEVLPLLGRqAEGPESFQLEEVYmGSRQVQRTVLADEesllsRLRDIR 287
Cdd:pfam00788   2 DGVLKVYTEDGKPGTTYKTILVSSSTTAEEVIEALLEKFGL-EDDPRDYVLVEVL-ERGGGERRLPDDE-----CPLQIQ 74

                          90
                  ....*....|....*....
gi 946809932  288 QTSLRQMSQTRFYVAESKA 306
Cdd:pfam00788  75 LQWPRDASDSRFLLRKRDD 93
C1_DGKtheta_typeV_rpt1 cd20803
first protein kinase C conserved region 1 (C1 domain) found in type V diacylglycerol kinase, ...
 51-81 1.16e-10

first protein kinase C conserved region 1 (C1 domain) found in type V diacylglycerol kinase, DAG kinase theta, and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase theta, also called diglyceride kinase theta (DGK-theta), is the only isoform classified as type V; it contains a pleckstrin homology (PH)-like domain and an additional C1 domain, compared to other DGKs. It may regulate the activity of protein kinase C by controlling the balance between the two signaling lipids, diacylglycerol and phosphatidic acid. DAG kinase theta contains three copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410353  Cd Length: 56  Bit Score: 57.32  E-value: 1.16e-10
                         10        20        30
                 ....*....|....*....|....*....|.
gi 946809932  51 LTPGFVPTVCNFMSHEKCLRQVKTPCTSLAP 81
Cdd:cd20803   26 LNQGYQCEVCNFVSHERCLKTVVTPCSSIAP 56
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 208-304 5.97e-08

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Kalhammer et al. have shown that not all RA domains bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase. Predicted RA domains in PLC210 and nore1 found to bind RasGTP. Included outliers (Grb7, Grb14, adenylyl cyclases etc.)


Pssm-ID: 214612  Cd Length: 90  Bit Score: 50.76  E-value: 5.97e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946809932   208 QDVLKIYPAWLkVGVAYVSIRVTPESTARTVVLEVLPLLGRQAEgPESFQLEEVYmgSRQVQRTVLADEESLLSRLRDIR 287
Cdd:smart00314   2 TFVLRVYVDDL-PGGTYKTLRVSSRTTARDVIQQLLEKFHLTDD-PEEYVLVEVL--PDGKERVLPDDENPLQLQKLWPR 77

                           90
                   ....*....|....*..
gi 946809932   288 QTSLRqmsqtRFYVAES 304
Cdd:smart00314  78 RGPNL-----RFVLRKR 89
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 122-184 2.92e-04

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Recent evidence (not yet in MEDLINE) shows that some RA domains do NOT bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase.


Pssm-ID: 425871  Cd Length: 93  Bit Score: 40.39  E-value: 2.92e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 946809932  122 DKQTLKIFDGSDAVhRNRFRVVSVPRLARSEEVLEAALRAYYITEDPRGFEL------QALPWPLSEEE 184
Cdd:pfam00788   1 DDGVLKVYTEDGKP-GTTYKTILVSSSTTAEEVIEALLEKFGLEDDPRDYVLvevlerGGGERRLPDDE 68
 
Name Accession Description Interval E-value
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 503-655 6.48e-70

Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. DAG can be produced from the hydrolysis of phosphatidylinositol 4,5-bisphosphate (PIP2) by a phosphoinositide-specific phospholipase C and by the degradation of phosphatidylcholine (PC) by a phospholipase C or the concerted actions of phospholipase D and phosphatidate phosphohydrolase. This domain might either be an accessory domain or else contribute to the catalytic domain. Bacterial homologues are known.


Pssm-ID: 214486  Cd Length: 160  Bit Score: 225.29  E-value: 6.48e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946809932   503 QMSNYCGIGIDAELSLDFHQAREEEPSKFTSRFHNKGVYVRVGLQKMNHA--RSLHKEIRLQVEQQEVELP-SIEGLIFI 579
Cdd:smart00045   1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRtcKDLHERIELECDGVDVDLPnSLEGIAVL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946809932   580 NIPSWGSGADLWG--SDSDSRFEKPRMDDGLLEVVGVTGVMHMVSM**GLRSGIRIAQGAYFRVTLL--KATPVQVDGEP 655
Cdd:smart00045  81 NIPSYGGGTNLWGttDKEDLNFSKQSHDDGLLEVVGLTGAMHMAQIRQVGLAGRRIAQCSEVRITIKtsKTIPMQVDGEP 160
DAGK_acc pfam00609
Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts ...
 503-655 9.94e-67

Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. This domain is assumed to be an accessory domain: its function is unknown.


Pssm-ID: 459866  Cd Length: 158  Bit Score: 216.70  E-value: 9.94e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946809932  503 QMSNYCGIGIDAELSLDFHQAREEEPSKFTSRFHNKGVYVRVGLQKM--NHARSLHKEIRLQVEQQEVELP-SIEGLIFI 579
Cdd:pfam00609   1 VMNNYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDMfqRSCKNLIEKVELEVDGKDLPLPkSLEGIVVL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 946809932  580 NIPSWGSGADLWGSDSDSR--FEKPRMDDGLLEVVGVTGVMHMVSM**GLRSGIRIAQGAYFRVTLLKATPVQVDGEP 655
Cdd:pfam00609  81 NIPSYAGGTDLWGNSKEDGlgFAPQSVDDGLLEVVGLTGALHLGQVQVGLGSAKRIAQGGPIRITTKKKIPMQVDGEP 158
RA2_DAGK-theta cd01783
Ras-associating (RA) domain 2 found in diacylgylcerol kinase theta (DAGK-theta) and similar ...
 210-304 6.77e-37

Ras-associating (RA) domain 2 found in diacylgylcerol kinase theta (DAGK-theta) and similar proteins; DAGK phosphorylates the second messenger diacylglycerol to phosphatidic acid as part of a protein kinase C pathway. DAGK-theta is characterized as a type V DAGK that has three cysteine-rich domains (all other isoforms have two), a proline/glycine-rich domain at its N-terminal, and a proposed Ras-associating (RA) domain. RA domain-containing proteins function by interacting with Ras proteins directly or indirectly and are involved in several different functions ranging from tumor suppression to being oncoproteins. Ras proteins are small GTPases that are involved in cellular signal transduction. The RA domain has a beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub). Ub is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair in eukaryotes. There are ten mammalian isoforms of DAGK have been identified to date, these are organized into five categories based on the domain architecture. DAGK-theta also contains a pleckstrin homology (PH) domain. The subcellular localization and the activity of DAGK-theta are regulated in a complex (stimulation- and cell type-dependent) manner. This family corresponds to the second RA domain of DAGK-theta.


Pssm-ID: 340481  Cd Length: 95  Bit Score: 133.12  E-value: 6.77e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946809932 210 VLKIYPAWLKVGVAYVSIRVTPESTARTVVLEVLPLLGRQAEGPESFQLEEVYMGSRQVQRTVLADEESLLSRLrDIRQT 289
Cdd:cd01783    2 YIRVYPGWLKVGVAYKSIPVTKETTVEEVIKEALPKFGLQDEDPEDFRLVEVLMDKGVVERVMLRDECPWLILL-DIRKE 80

                         90
                 ....*....|....*
gi 946809932 290 SLRQMSQTRFYVAES 304
Cdd:cd01783   81 SLRQMRQTRFYLQQK 95
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 402-489 3.00e-30

Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. DAG can be produced from the hydrolysis of phosphatidylinositol 4,5-bisphosphate (PIP2) by a phosphoinositide-specific phospholipase C and by the degradation of phosphatidylcholine (PC) by a phospholipase C or the concerted actions of phospholipase D and phosphatidate phosphohydrolase. This domain is presumed to be the catalytic domain. Bacterial homologues areknown.


Pssm-ID: 214487 [Multi-domain]  Cd Length: 124  Bit Score: 115.47  E-value: 3.00e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946809932   402 LVFVNPKSGGLKGRDLLCSFRKLLNPHQVFELTNGGPLPGLHVFAQMPRF-RVLVCGGDGTVGWVLAALeeMRHQLACPE 480
Cdd:smart00046   1 LVFVNPKSGGGKGEKLLRKFRLLLNPRQVFDLTKKGPAVALVIFRDVPDFnRVLVCGGDGTVGWVLNAL--DKRELPLPE 78


                   ....*....
gi 946809932   481 PPGAGAPGG 489
Cdd:smart00046  79 PPVAVLPLG 87
RA1_DAGK-theta cd17111
Ras-associating (RA) domain 1 found in diacylgylcerol kinase theta (DAGK-theta) and similar ...
 123-206 1.82e-22

Ras-associating (RA) domain 1 found in diacylgylcerol kinase theta (DAGK-theta) and similar proteins; DAGK phosphorylates the second messenger diacylglycerol to phosphatidic acid as part of a protein kinase C pathway. DAGK-theta is characterized as a type V DAGK that has three cysteine-rich domains (all other isoforms have two), a proline/glycine-rich domain at its N-terminal, and a proposed Ras-associating (RA) domain. RA domain-containing proteins function by interacting with Ras proteins directly or indirectly and are involved in several different functions ranging from tumor suppression to being oncoproteins. Ras proteins are small GTPases that are involved in cellular signal transduction. The RA domain has a beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub). Ub is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair in eukaryotes. Ten mammalian isoforms of DAGK have been identified to date which are organized into five categories based on the domain architecture. DAGK-theta also contains a pleckstrin homology (PH) domain. The subcellular localization and the activity of DAGK-theta are regulated in a complex (stimulation- and cell type-dependent) manner. This family corresponds to the first RA domain of DAGK-theta.


Pssm-ID: 340631  Cd Length: 91  Bit Score: 91.88  E-value: 1.82e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946809932 123 KQTLKIFDGSDAVHRNRFRVVSVPRLARSEEVLEAALRAYYITEDPRGFELQAL--PWPLSEEE-----GGRGPRSREVS 195
Cdd:cd17111    1 KEIVKVFDGNASLKRNQFRLITVPRNASVEQVLEAALRAFHIPDDPENYYLTDAyeSSLGDEREledpgPLRNLVRREGK 80

                         90
                 ....*....|.
gi 946809932 196 PEAWIIRTLPR 206
Cdd:cd17111   81 RPAIFLRYKEK 91
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 400-477 1.39e-18

Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. The catalytic domain is assumed from the finding of bacterial homologs. YegS is the Escherichia coli protein in this family whose crystal structure reveals an active site in the inter-domain cleft formed by four conserved sequence motifs, revealing a novel metal-binding site. The residues of this site are conserved across the family.


Pssm-ID: 425868 [Multi-domain]  Cd Length: 125  Bit Score: 82.25  E-value: 1.39e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946809932  400 PLLVFVNPKSGGLKGRDLLCSFRKLLNPHQV-FELTN-GGPLPGLHVFAQMPR---FRVLVCGGDGTVGWVLAALEEMRH 474
Cdd:pfam00781   1 KLLVIVNPKSGGGKGKKLLRKVRPLLNKAGVeVELVLtEGPGDALELAREAAEdgyDRIVVAGGDGTVNEVLNGLAGLAT 80


                  ...
gi 946809932  475 QLA 477
Cdd:pfam00781  81 RPP 83
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 401-655 3.89e-17

Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, General function prediction only];


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 82.59  E-value: 3.89e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946809932 401 LLVFVNPKSGGLKGRDLLCSFRKLLNPH----QVFELTNGGPLPGLHVFAQMPRFRVLV-CGGDGTVGWVLAALEEMRHQ 475
Cdd:COG1597    5 ALLIVNPASGRGRAARLLERLVAALRAAglevEVLETESPGDATELAREAAAEGADLVVaAGGDGTVNEVANGLAGTGPP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946809932 476 LACpeppgagAPGG----------LP-------------RPRRVvcpQIVQMS-----NYCGIGIDAELSLDFHQAReee 527
Cdd:COG1597   85 LGI-------LPLGtgndfaralgIPldpeaalealltgRTRRI---DLGRVNgryflNVAGIGFDAEVVERANRAL--- 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946809932 528 pskftSRFHNKGVYVRVGLQKMNHARSLHkeIRLQVEQQEVELPSIegLIFI-NIPSWGSGADLwgsdsdsrFEKPRMDD 606
Cdd:COG1597  152 -----KRRLGKLAYVLAALRALLRYRPFR--LRIELDGEEIEGEAL--LVAVgNGPYYGGGLRL--------APDASLDD 214

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 946809932 607 GLLEVVGVT--GVMHMVSM**GLRSG-------IRIAQGAYFRVTLLKATPVQVDGEP 655
Cdd:COG1597  215 GLLDVVVVRplSRLRLLRLLPRLLRGrhlrhpgVRYFRAREVEIESDRPLPVQLDGEP 272
RA cd17043
Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA ...
 210-303 5.28e-12

Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA domain-containing proteins function by interacting with Ras proteins directly or indirectly and are involved in various functions ranging from tumor suppression to being oncoproteins. Ras proteins are small GTPases that are involved in cellular signal transduction. The RA domain has the beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub); Ub is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. RA-containing proteins include RalGDS, AF6, RIN, RASSF1, SNX27, CYR1, STE50, and phospholipase C epsilon.


Pssm-ID: 340563  Cd Length: 87  Bit Score: 61.95  E-value: 5.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946809932 210 VLKIYPAWLKVGVAYVSIRVTPESTARTVVLEVLPLLGRqAEGPESFQLEEVYMGsRQVQRTVLADEESLLsrlrdIRQT 289
Cdd:cd17043    1 VLKVYDDDLAPGSAYKSILVSSTTTAREVVQLLLEKYGL-EEDPEDYSLYEVSEK-QETERVLHDDECPLL-----IQLE 73

                         90
                 ....*....|....
gi 946809932 290 SLRQMSQTRFYVAE 303
Cdd:cd17043   74 WGPQGTEFRFVLKR 87
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 208-306 9.60e-11

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Recent evidence (not yet in MEDLINE) shows that some RA domains do NOT bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase.


Pssm-ID: 425871  Cd Length: 93  Bit Score: 58.88  E-value: 9.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946809932  208 QDVLKIYPAWLKVGVAYVSIRVTPESTARTVVLEVLPLLGRqAEGPESFQLEEVYmGSRQVQRTVLADEesllsRLRDIR 287
Cdd:pfam00788   2 DGVLKVYTEDGKPGTTYKTILVSSSTTAEEVIEALLEKFGL-EDDPRDYVLVEVL-ERGGGERRLPDDE-----CPLQIQ 74

                          90
                  ....*....|....*....
gi 946809932  288 QTSLRQMSQTRFYVAESKA 306
Cdd:pfam00788  75 LQWPRDASDSRFLLRKRDD 93
C1_DGKtheta_typeV_rpt1 cd20803
first protein kinase C conserved region 1 (C1 domain) found in type V diacylglycerol kinase, ...
 51-81 1.16e-10

first protein kinase C conserved region 1 (C1 domain) found in type V diacylglycerol kinase, DAG kinase theta, and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase theta, also called diglyceride kinase theta (DGK-theta), is the only isoform classified as type V; it contains a pleckstrin homology (PH)-like domain and an additional C1 domain, compared to other DGKs. It may regulate the activity of protein kinase C by controlling the balance between the two signaling lipids, diacylglycerol and phosphatidic acid. DAG kinase theta contains three copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410353  Cd Length: 56  Bit Score: 57.32  E-value: 1.16e-10
                         10        20        30
                 ....*....|....*....|....*....|.
gi 946809932  51 LTPGFVPTVCNFMSHEKCLRQVKTPCTSLAP 81
Cdd:cd20803   26 LNQGYQCEVCNFVSHERCLKTVVTPCSSIAP 56
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 208-304 5.97e-08

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Kalhammer et al. have shown that not all RA domains bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase. Predicted RA domains in PLC210 and nore1 found to bind RasGTP. Included outliers (Grb7, Grb14, adenylyl cyclases etc.)


Pssm-ID: 214612  Cd Length: 90  Bit Score: 50.76  E-value: 5.97e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946809932   208 QDVLKIYPAWLkVGVAYVSIRVTPESTARTVVLEVLPLLGRQAEgPESFQLEEVYmgSRQVQRTVLADEESLLSRLRDIR 287
Cdd:smart00314   2 TFVLRVYVDDL-PGGTYKTLRVSSRTTARDVIQQLLEKFHLTDD-PEEYVLVEVL--PDGKERVLPDDENPLQLQKLWPR 77

                           90
                   ....*....|....*..
gi 946809932   288 QTSLRqmsqtRFYVAES 304
Cdd:smart00314  78 RGPNL-----RFVLRKR 89
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 122-184 2.92e-04

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Recent evidence (not yet in MEDLINE) shows that some RA domains do NOT bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase.


Pssm-ID: 425871  Cd Length: 93  Bit Score: 40.39  E-value: 2.92e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 946809932  122 DKQTLKIFDGSDAVhRNRFRVVSVPRLARSEEVLEAALRAYYITEDPRGFEL------QALPWPLSEEE 184
Cdd:pfam00788   1 DDGVLKVYTEDGKP-GTTYKTILVSSSTTAEEVIEALLEKFGLEDDPRDYVLvevlerGGGERRLPDDE 68
RA2_Afadin cd01781
Ras-associating (RA) domain 2 found in Afadin; Afadin, also termed ALL1-fused gene from ...
 209-286 4.14e-04

Ras-associating (RA) domain 2 found in Afadin; Afadin, also termed ALL1-fused gene from chromosome 6 protein (AF-6), or canoe, is involved in many fundamental signaling cascades in cells. In addition, it is involved in oncogenesis and metastasis. Afadin has multiple domains: from the N-terminus to the C-terminus it has two Ras-associated (RA) domains, a forkhead-associated domain, a dilute domain, a PDZ domain, three proline-rich domains, and an F-actin binding domain. RA domain-containing proteins function by interacting with Ras proteins directly or indirectly and are involved in several different functions ranging from tumor suppression to being oncoproteins. Ras proteins are small GTPases that are involved in cellular signal transduction. The RA domain has a beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub). Ub is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair in eukaryotes. Afadin is abundant at cadherin-based adherens junctions in epithelial cells, endothelial cells, and fibroblasts. This family corresponds to the second RA domain of afadin.


Pssm-ID: 340479  Cd Length: 102  Bit Score: 39.95  E-value: 4.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 946809932 209 DVLKIYPAWLKVGVAYVSIRVTPESTARTVVLEVLPLLGRQAEGPESFQLEEVYMGSRQVQRT--------VLADEESLL 280
Cdd:cd01781    2 GTLKIYGDSLKPEVPYKTLLLSTNDTADFVVREALEKYGLEKENPKDYCLVQVVLPPGGSPRLdggggkerILDDDECPL 81


                 ....*.
gi 946809932 281 SRLRDI 286
Cdd:cd01781   82 AILMRW 87
 
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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