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Conserved domains on  [gi|2112719293|gb|KAH1024437|]
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hypothetical protein HUJ05_003922 [Dendroctonus ponderosae]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 667-824 3.75e-74

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: 243.40  E-value: 3.75e-74
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112719293   667 VMNNYFGIGIDAKISLDFHHKREEHPEKCRSRAKNYLWYGVLGGKELLQRTFKNLEQRVQLECDGQRIPLP-SLQGIVIL 745
Cdd:smart00045    1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLPnSLEGIAVL 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112719293   746 NIPRFMGGINFWGGS-KMDDVFIAPSFDDKILEVVAVFGSMQMAASRMMKFQHHRIAQCQSIQINILGDEGVPIQVDGEA 824
Cdd:smart00045   81 NIPSYGGGTNLWGTTdKEDLNFSKQSHDDGLLEVVGLTGAMHMAQIRQVGLAGRRIAQCSEVRITIKTSKTIPMQVDGEP 160
Cullin_binding pfam03556
Cullin binding; This domain binds to cullins and to Rbx-1, components of an E3 ubiquitin ...
 1282-1392 2.39e-54

Cullin binding; This domain binds to cullins and to Rbx-1, components of an E3 ubiquitin ligase complex for neddylation. Neddylation is the process by which the C-terminal glycine of the ubiquitin-like protein Nedd8 is covalently linked to lysine residues in a protein through an isopeptide bond. The structure of this domain is composed entirely of alpha helices.


:

Pssm-ID: 460971  Cd Length: 117  Bit Score: 185.10  E-value: 2.39e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112719293 1282 KLKQRLPSMENELRD-AFKFKDFYQFTFNFAKNPNQKGIDLDMAIAYWNIVLKGRF---KFLELWCTFLQENHKRSIPKD 1357
Cdd:pfam03556    1 KLKAKLPELRKELTDpSEYFKKVYRFTFDFAKEPGQKSLDLETAIEYWKLLLGGRFrifPLLDLWIEFLEEEKKVKISKD 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2112719293 1358 TWNLLLDFAQQIS--DDMSNYDEEGAWPVLIDDFVEW 1392
Cdd:pfam03556   81 TWNMFLEFARKVDedEDLSNYDEDGAWPSLIDEFVEW 117
UBA_like_SF super family cl21463
UBA domain-like superfamily; The ubiquitin-associated (UBA) domain-like superfamily contains ...
 1150-1196 1.29e-24

UBA domain-like superfamily; The ubiquitin-associated (UBA) domain-like superfamily contains alpha-helical structural homology ubiquitin-binding domains, including UBA domains and coupling of ubiquitin conjugation to endoplasmic reticulum degradation (CUE) domains which share a common three-helical bundle architecture. UBA domains are commonly occurring sequence motifs found in proteins involved in ubiquitin-mediated proteolysis. They contribute to ubiquitin (Ub) binding or ubiquitin-like (UbL) domain binding. However, some kinds of UBA domains can only bind the UbL domain, but not the Ub domain. UBA domains are normally comprised of compact three-helix bundles which contain a conserved GF/Y-loop. They can bind polyubiquitin with high affinity. They also bind monoubiquitin and other proteins. Most UBA domain-containing proteins have one UBA domain, but some harbor two or three UBA domains. CUE domain containing proteins are characterized by an FP and a di-leucine-like sequence and bind to monoubiquitin with varying affinities. Some higher eukaryotic CUE domain proteins do not bind monoubiquitin efficiently, since they carry LP, rather than FP among CUE domains. This superfamily also includes many UBA-like domains found in AMP-activated protein kinase (AMPK) related kinases, the NXF family of mRNA nuclear export factors, elongation factor Ts (EF-Ts), nascent polypeptide-associated complex subunit alpha (NACA) and similar proteins. Although many UBA-like domains may have a conserved TG but not GF/Y-loop, they still show a high level of structural and sequence similarity with three-helical ubiquitin binding domains.


The actual alignment was detected with superfamily member cd14412:

Pssm-ID: 473871  Cd Length: 47  Bit Score: 97.46  E-value: 1.29e-24
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2112719293 1150 HKLKSSQRDKVKKFISFTQTGESTAIYCLTQNDWKLDLASDNYFQNP 1196
Cdd:cd14412      1 HKLKSSQKDKVRQFMAFTQAGERTAIYCLTQNEWKLEVATDNYFQNP 47
SAM_superfamily super family cl15755
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 1100-1149 3.07e-21

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.


The actual alignment was detected with superfamily member cd09507:

Pssm-ID: 472832  Cd Length: 65  Bit Score: 88.62  E-value: 3.07e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2112719293 1100 VASWGTHEVATWLDTLQLTEYIDSFEKNDIRGRELLTLARRDLKDLGVTK 1149
Cdd:cd09507      2 VTNWTTEEVGAWLESLQLGEYRDIFARNDIRGSELLHLERRDLKDLGITK 51
DAGK_cat super family cl01255
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 6-51 8.45e-11

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.


The actual alignment was detected with superfamily member smart00046:

Pssm-ID: 445337 [Multi-domain]  Cd Length: 124  Bit Score: 60.77  E-value: 8.45e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 2112719293     6 QVAVLPLGTGNDLARVLGWGASCDSDAHLPQLLEKyERASVQMLDR 51
Cdd:smart00046   80 PVAVLPLGTGNDLARSLGWGGGYDGEKLLKTLRDA-LESDTVKLDR 124
 
Name Accession Description Interval E-value
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 667-824 3.75e-74

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: 243.40  E-value: 3.75e-74
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112719293   667 VMNNYFGIGIDAKISLDFHHKREEHPEKCRSRAKNYLWYGVLGGKELLQRTFKNLEQRVQLECDGQRIPLP-SLQGIVIL 745
Cdd:smart00045    1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLPnSLEGIAVL 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112719293   746 NIPRFMGGINFWGGS-KMDDVFIAPSFDDKILEVVAVFGSMQMAASRMMKFQHHRIAQCQSIQINILGDEGVPIQVDGEA 824
Cdd:smart00045   81 NIPSYGGGTNLWGTTdKEDLNFSKQSHDDGLLEVVGLTGAMHMAQIRQVGLAGRRIAQCSEVRITIKTSKTIPMQVDGEP 160
DAGK_acc pfam00609
Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts ...
 667-824 8.07e-66

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: 219.39  E-value: 8.07e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112719293  667 VMNNYFGIGIDAKISLDFHHKREEHPEKCRSRAKNYLWYGVLGGKELLQRTFKNLEQRVQLECDGQRIPLP-SLQGIVIL 745
Cdd:pfam00609    1 VMNNYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDMFQRSCKNLIEKVELEVDGKDLPLPkSLEGIVVL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112719293  746 NIPRFMGGINFWGGSKMDDV-FIAPSFDDKILEVVAVFGSMQMAASRMMKFQHHRIAQCQSIQINIlgDEGVPIQVDGEA 824
Cdd:pfam00609   81 NIPSYAGGTDLWGNSKEDGLgFAPQSVDDGLLEVVGLTGALHLGQVQVGLGSAKRIAQGGPIRITT--KKKIPMQVDGEP 158
Cullin_binding pfam03556
Cullin binding; This domain binds to cullins and to Rbx-1, components of an E3 ubiquitin ...
 1282-1392 2.39e-54

Cullin binding; This domain binds to cullins and to Rbx-1, components of an E3 ubiquitin ligase complex for neddylation. Neddylation is the process by which the C-terminal glycine of the ubiquitin-like protein Nedd8 is covalently linked to lysine residues in a protein through an isopeptide bond. The structure of this domain is composed entirely of alpha helices.


Pssm-ID: 460971  Cd Length: 117  Bit Score: 185.10  E-value: 2.39e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112719293 1282 KLKQRLPSMENELRD-AFKFKDFYQFTFNFAKNPNQKGIDLDMAIAYWNIVLKGRF---KFLELWCTFLQENHKRSIPKD 1357
Cdd:pfam03556    1 KLKAKLPELRKELTDpSEYFKKVYRFTFDFAKEPGQKSLDLETAIEYWKLLLGGRFrifPLLDLWIEFLEEEKKVKISKD 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2112719293 1358 TWNLLLDFAQQIS--DDMSNYDEEGAWPVLIDDFVEW 1392
Cdd:pfam03556   81 TWNMFLEFARKVDedEDLSNYDEDGAWPSLIDEFVEW 117
UBA_DCNL2 cd14412
UBA-like domain found in DCN1-like protein 2 (DCNL2) and similar proteins; DCNL2 (defective in ...
 1150-1196 1.29e-24

UBA-like domain found in DCN1-like protein 2 (DCNL2) and similar proteins; DCNL2 (defective in cullin neddylation protein 1-like protein 2), also called DCUN1 domain-containing protein 2, is encoded by gene DCUN1D2. Although its biological function remains unclear, DCNL2 shows high sequence similarity with DCNL1, a protein that plays an essential role in the neddylation E3 complex and participates in the release of inhibitory effects of CAND1 on cullin-RING ligase E3 complex assembly and activity. At this point, DCNL2 may also contribute to neddylation of cullin components of SCF-type E3 ubiquitin ligase complexes. Like DCNL1, DCNL2 contains an N-terminal ubiquitin-associated (UBA)-like domain and a C-terminal cullin binding domain that is responsible for the binding to cullins and Rbx-1, components of an E3 ubiquitin ligase complex for neddylation.


Pssm-ID: 270595  Cd Length: 47  Bit Score: 97.46  E-value: 1.29e-24
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2112719293 1150 HKLKSSQRDKVKKFISFTQTGESTAIYCLTQNDWKLDLASDNYFQNP 1196
Cdd:cd14412      1 HKLKSSQKDKVRQFMAFTQAGERTAIYCLTQNEWKLEVATDNYFQNP 47
SAM_DGK-delta-eta cd09507
SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain ...
 1100-1149 3.07e-21

SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain of DGK-eta-delta subfamily proteins is a protein-protein interaction domain. Proteins of this subfamily are multidomain diacylglycerol kinases with a SAM domain located at the C-terminus. DGK proteins participate in signal transduction. They regulate the level of second messengers such as diacylglycerol and phosphatidic acid. The SAM domain of DGK proteins can form high molecular weight homooligomers through head-to-tail interactions as well as heterooligomers between the SAM domains of DGK delta and eta proteins. The oligomerization plays a role in the regulation of DGK intracellular localization.


Pssm-ID: 188906  Cd Length: 65  Bit Score: 88.62  E-value: 3.07e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2112719293 1100 VASWGTHEVATWLDTLQLTEYIDSFEKNDIRGRELLTLARRDLKDLGVTK 1149
Cdd:cd09507      2 VTNWTTEEVGAWLESLQLGEYRDIFARNDIRGSELLHLERRDLKDLGITK 51
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 6-51 8.45e-11

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: 60.77  E-value: 8.45e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 2112719293     6 QVAVLPLGTGNDLARVLGWGASCDSDAHLPQLLEKyERASVQMLDR 51
Cdd:smart00046   80 PVAVLPLGTGNDLARSLGWGGGYDGEKLLKTLRDA-LESDTVKLDR 124
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 664-837 1.09e-09

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


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 61.41  E-value: 1.09e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112719293  664 ERCVMNNyFGIGIDAKISLDFHHKReehpeKCRSRAKNYLWYGVlggKELLQRTFknleQRVQLECDGQRIPLPSLQgIV 743
Cdd:COG1597    128 GRYFLNV-AGIGFDAEVVERANRAL-----KRRLGKLAYVLAAL---RALLRYRP----FRLRIELDGEEIEGEALL-VA 193

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112719293  744 ILNIPRFMGGINFWGGSKMDD----VFIAPSFDdkILEVVAVFgsMQMAASRMMKFQHHRIAQCQSIQINilGDEGVPIQ 819
Cdd:COG1597    194 VGNGPYYGGGLRLAPDASLDDglldVVVVRPLS--RLRLLRLL--PRLLRGRHLRHPGVRYFRAREVEIE--SDRPLPVQ 267

                          170
                   ....*....|....*....
gi 2112719293  820 VDGEA-WIQPPGIIRILHK 837
Cdd:COG1597    268 LDGEPlGLATPLEFEVLPG 286
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 1100-1153 1.40e-09

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 55.38  E-value: 1.40e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 2112719293  1100 VASWGTHEVATWLDTLQLTEYIDSFEKNDIRGRELLTLARR-DLKDLGVTK--HKLK 1153
Cdd:smart00454    1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEeDLKELGITKlgHRKK 57
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 1102-1153 1.31e-08

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 52.66  E-value: 1.31e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2112719293 1102 SWGTHEVATWLDTLQLTEYIDSFEKNDIRGRELLTLARRDLKDLGVTK--HKLK 1153
Cdd:pfam00536    2 GWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLlgHRKK 55
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 4-32 4.68e-06

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: 47.19  E-value: 4.68e-06
                           10        20
                   ....*....|....*....|....*....
gi 2112719293    4 QCQVAVLPLGTGNDLARVLGWGASCDSDA 32
Cdd:pfam00781   81 RPPLGIIPLGTGNDFARALGIPGDPEEAL 109
UBA_4 pfam14555
UBA-like domain;
1157-1198 4.11e-05

UBA-like domain;


Pssm-ID: 464207  Cd Length: 43  Bit Score: 42.05  E-value: 4.11e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 2112719293 1157 RDKVKKFISFTQTGESTAIYCLTQNDWKLDLASDNYFQNPDA 1198
Cdd:pfam14555    1 DELIAQFQAITGADEEVARQYLEAHNWDLEAAVNAFFDDGEA 42
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 1-23 3.80e-03

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


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 40.99  E-value: 3.80e-03
                           10        20
                   ....*....|....*....|...
gi 2112719293    1 MHKQCQVAVLPLGTGNDLARVLG 23
Cdd:COG1597     79 AGTGPPLGILPLGTGNDFARALG 101
 
Name Accession Description Interval E-value
DAGKa smart00045
Diacylglycerol kinase accessory domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 667-824 3.75e-74

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: 243.40  E-value: 3.75e-74
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112719293   667 VMNNYFGIGIDAKISLDFHHKREEHPEKCRSRAKNYLWYGVLGGKELLQRTFKNLEQRVQLECDGQRIPLP-SLQGIVIL 745
Cdd:smart00045    1 VMNNYFSIGVDAHIALEFHNKREANPEKFNSRLKNKMWYFELGTKDLFFRTCKDLHERIELECDGVDVDLPnSLEGIAVL 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112719293   746 NIPRFMGGINFWGGS-KMDDVFIAPSFDDKILEVVAVFGSMQMAASRMMKFQHHRIAQCQSIQINILGDEGVPIQVDGEA 824
Cdd:smart00045   81 NIPSYGGGTNLWGTTdKEDLNFSKQSHDDGLLEVVGLTGAMHMAQIRQVGLAGRRIAQCSEVRITIKTSKTIPMQVDGEP 160
DAGK_acc pfam00609
Diacylglycerol kinase accessory domain; Diacylglycerol (DAG) is a second messenger that acts ...
 667-824 8.07e-66

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: 219.39  E-value: 8.07e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112719293  667 VMNNYFGIGIDAKISLDFHHKREEHPEKCRSRAKNYLWYGVLGGKELLQRTFKNLEQRVQLECDGQRIPLP-SLQGIVIL 745
Cdd:pfam00609    1 VMNNYFSIGVDARIALGFHRLREEHPELFNSRLKNKLIYGVFGFKDMFQRSCKNLIEKVELEVDGKDLPLPkSLEGIVVL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112719293  746 NIPRFMGGINFWGGSKMDDV-FIAPSFDDKILEVVAVFGSMQMAASRMMKFQHHRIAQCQSIQINIlgDEGVPIQVDGEA 824
Cdd:pfam00609   81 NIPSYAGGTDLWGNSKEDGLgFAPQSVDDGLLEVVGLTGALHLGQVQVGLGSAKRIAQGGPIRITT--KKKIPMQVDGEP 158
Cullin_binding pfam03556
Cullin binding; This domain binds to cullins and to Rbx-1, components of an E3 ubiquitin ...
 1282-1392 2.39e-54

Cullin binding; This domain binds to cullins and to Rbx-1, components of an E3 ubiquitin ligase complex for neddylation. Neddylation is the process by which the C-terminal glycine of the ubiquitin-like protein Nedd8 is covalently linked to lysine residues in a protein through an isopeptide bond. The structure of this domain is composed entirely of alpha helices.


Pssm-ID: 460971  Cd Length: 117  Bit Score: 185.10  E-value: 2.39e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112719293 1282 KLKQRLPSMENELRD-AFKFKDFYQFTFNFAKNPNQKGIDLDMAIAYWNIVLKGRF---KFLELWCTFLQENHKRSIPKD 1357
Cdd:pfam03556    1 KLKAKLPELRKELTDpSEYFKKVYRFTFDFAKEPGQKSLDLETAIEYWKLLLGGRFrifPLLDLWIEFLEEEKKVKISKD 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2112719293 1358 TWNLLLDFAQQIS--DDMSNYDEEGAWPVLIDDFVEW 1392
Cdd:pfam03556   81 TWNMFLEFARKVDedEDLSNYDEDGAWPSLIDEFVEW 117
UBA_DCNL2 cd14412
UBA-like domain found in DCN1-like protein 2 (DCNL2) and similar proteins; DCNL2 (defective in ...
 1150-1196 1.29e-24

UBA-like domain found in DCN1-like protein 2 (DCNL2) and similar proteins; DCNL2 (defective in cullin neddylation protein 1-like protein 2), also called DCUN1 domain-containing protein 2, is encoded by gene DCUN1D2. Although its biological function remains unclear, DCNL2 shows high sequence similarity with DCNL1, a protein that plays an essential role in the neddylation E3 complex and participates in the release of inhibitory effects of CAND1 on cullin-RING ligase E3 complex assembly and activity. At this point, DCNL2 may also contribute to neddylation of cullin components of SCF-type E3 ubiquitin ligase complexes. Like DCNL1, DCNL2 contains an N-terminal ubiquitin-associated (UBA)-like domain and a C-terminal cullin binding domain that is responsible for the binding to cullins and Rbx-1, components of an E3 ubiquitin ligase complex for neddylation.


Pssm-ID: 270595  Cd Length: 47  Bit Score: 97.46  E-value: 1.29e-24
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2112719293 1150 HKLKSSQRDKVKKFISFTQTGESTAIYCLTQNDWKLDLASDNYFQNP 1196
Cdd:cd14412      1 HKLKSSQKDKVRQFMAFTQAGERTAIYCLTQNEWKLEVATDNYFQNP 47
SAM_DGK-delta-eta cd09507
SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain ...
 1100-1149 3.07e-21

SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain of DGK-eta-delta subfamily proteins is a protein-protein interaction domain. Proteins of this subfamily are multidomain diacylglycerol kinases with a SAM domain located at the C-terminus. DGK proteins participate in signal transduction. They regulate the level of second messengers such as diacylglycerol and phosphatidic acid. The SAM domain of DGK proteins can form high molecular weight homooligomers through head-to-tail interactions as well as heterooligomers between the SAM domains of DGK delta and eta proteins. The oligomerization plays a role in the regulation of DGK intracellular localization.


Pssm-ID: 188906  Cd Length: 65  Bit Score: 88.62  E-value: 3.07e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2112719293 1100 VASWGTHEVATWLDTLQLTEYIDSFEKNDIRGRELLTLARRDLKDLGVTK 1149
Cdd:cd09507      2 VTNWTTEEVGAWLESLQLGEYRDIFARNDIRGSELLHLERRDLKDLGITK 51
UBA_DCNL cd14350
UBA-like domain found in DCN1-like protein DCNL1, DCNL2 and similar proteins; DCNL1 (defective ...
 1155-1196 3.75e-19

UBA-like domain found in DCN1-like protein DCNL1, DCNL2 and similar proteins; DCNL1 (defective in cullin neddylation protein 1-like protein 1), also called DCUN1 domain-containing protein 1, is encoded by squamous cell carcinoma-related oncogene SCCRO (DCUN1D1). It interacts with known cullin isoforms as well as ROC1, Ubc12 and CAND1, the components of the neddylation pathway. It plays an essential role in the neddylation E3 complex and participates in the release of inhibitory effects of CAND1 on cullin-RING ligase E3 complex assembly and activity. DCNL1 contains an N-terminal ubiquitin-associated (UBA)-like domain and a C-terminal cullin binding domain that binds to cullins and Rbx-1, components of an E3 ubiquitin ligase complex for neddylation. DCNL2 (defective in cullin neddylation protein 1-like protein 2), also called DCUN1 domain-containing protein 2, is encoded by gene DCUN1D2. Although its biological function remains unclear, DCNL2 shows high sequence similarity with DCNL1 and may also contribute to neddylation of cullin components of SCF-type E3 ubiquitin ligase complexes. Like DCNL1, DCNL2 contains an N-terminal UBA-like domain and a C-terminal cullin binding domain.


Pssm-ID: 270535  Cd Length: 42  Bit Score: 81.92  E-value: 3.75e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 2112719293 1155 SQRDKVKKFISFTQTGESTAIYCLTQNDWKLDLASDNYFQNP 1196
Cdd:cd14350      1 SQKDKVRQFMSITQANEKTAIQCLKDADWNLELAVDAYFQNP 42
UBA_DCNL1 cd14411
UBA-like domain found in DCN1-like protein 1 (DCNL1) and similar proteins; DCNL1 (defective in ...
 1150-1199 7.74e-18

UBA-like domain found in DCN1-like protein 1 (DCNL1) and similar proteins; DCNL1 (defective in cullin neddylation protein 1-like protein 1), also called DCUN1 domain-containing protein 1, is encoded by squamous cell carcinoma-related oncogene SCCRO (DCUN1D1). It interacts with known cullin isoforms as well as ROC1, Ubc12 and CAND1, the components of the neddylation pathway. It plays an essential role in the neddylation E3 complex and participates in the release of inhibitory effects of CAND1 on cullin-RING ligase E3 complex assembly and activity. DCNL1 contains an N-terminal ubiquitin-associated (UBA)-like domain and a C-terminal cullin binding domain that binds to cullins and Rbx-1, components of an E3 ubiquitin ligase complex for neddylation.


Pssm-ID: 270594  Cd Length: 51  Bit Score: 78.27  E-value: 7.74e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2112719293 1150 HKLKSSQRDKVKKFISFTQTGESTAIYCLTQNDWKLDLASDNYFQNPDAY 1199
Cdd:cd14411      2 NKLKSSQKDKVRQFMIFTQSSEKTAVSCLSQNDWKLDVATDNFFQNPELY 51
SAM_DGK-delta cd09575
SAM domain of diacylglycerol kinase delta; SAM (sterile alpha motif) domain of DGK-delta ...
 1100-1149 5.96e-17

SAM domain of diacylglycerol kinase delta; SAM (sterile alpha motif) domain of DGK-delta subfamily proteins is a protein-protein interaction domain. Proteins of this subfamily are multidomain diacylglycerol kinases with a SAM domain located at the C-terminus. DGK-delta proteins participate in signal transduction. They regulate the level of second messengers such as diacylglycerol and phosphatidic acid. In particular DGK-delta is involved in the regulation of clathrin-dependent endocytosis. The SAM domain of DGK-delta proteins can form high molecular weight homooligomers through head-to-tail interactions as well as heterooligomers with the SAM domain of DGK-eta proteins. The oligomerization plays a role in the regulation of the DGK-delta intracellular localization: it inhibits the translocation of the protein to the plasma membrane from the cytoplasm. The SAM domain also can bind Zn at multiple (not conserved) sites driving the formation of highly ordered large sheets of polymers, thus suggesting that Zn may play important role in the function of DCK-delta.


Pssm-ID: 188974  Cd Length: 65  Bit Score: 76.53  E-value: 5.96e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2112719293 1100 VASWGTHEVATWLDTLQLTEYIDSFEKNDIRGRELLTLARRDLKDLGVTK 1149
Cdd:cd09575      2 VHLWGTEEVAAWLEHLSLCEYKDIFTRHDVRGSELLHLERRDLKDLGVTK 51
SAM_DGK-eta cd09576
SAM domain of diacylglycerol kinase eta; SAM (sterile alpha motif) domain of DGK-eta subfamily ...
 1100-1149 4.64e-15

SAM domain of diacylglycerol kinase eta; SAM (sterile alpha motif) domain of DGK-eta subfamily proteins is a protein-protein interaction domain. Proteins of this subfamily are multidomain diacylglycerol kinases. The SAM domain is located at the C-terminus of two out of three isoforms of DGK-eta protein. DGK-eta proteins participate in signal transduction. They regulate the level of second messengers such as diacylglycerol and phosphatidic acid. The SAM domain of DCK-eta proteins can form high molecular weight homooligomers through head-to-tail interactions as well as heterooligomers with the SAM domain of DGK-delta proteins. The oligomerization plays a role in the regulation of the DGK-delta intracellular localization: it is responsible for sustained endosomal localization of the protein and resulted in negative regulation of DCK-eta catalytic activity.


Pssm-ID: 188975  Cd Length: 65  Bit Score: 71.16  E-value: 4.64e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2112719293 1100 VASWGTHEVATWLDTLQLTEYIDSFEKNDIRGRELLTLARRDLKDLGVTK 1149
Cdd:cd09576      2 VQKWGTDEVAAWLDLLSLGEYKEIFIRHDIRGSELLHLERRDLKDLGIPK 51
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 6-51 8.45e-11

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: 60.77  E-value: 8.45e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 2112719293     6 QVAVLPLGTGNDLARVLGWGASCDSDAHLPQLLEKyERASVQMLDR 51
Cdd:smart00046   80 PVAVLPLGTGNDLARSLGWGGGYDGEKLLKTLRDA-LESDTVKLDR 124
SAM_Shank1,2,3 cd09506
SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 ...
 1100-1149 8.46e-10

SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 family proteins is a protein-protein interaction domain. Shank1,2,3 proteins are scaffold proteins that are known to interact with a variety of cytoplasmic and membrane proteins. SAM domains of the Shank1,2,3 family are prone to homooligomerization. They are highly enriched in the postsynaptic density, acting as scaffolds to organize assembly of postsynaptic proteins. SAM domains of Shank3 proteins can form large sheets of helical fibers. Shank genes show distinct patterns of expression, in rat Shank1 mRNA is found almost exclusively in brain, Shank2 in brain, kidney and liver, and Shank3 in heart, brain and spleen.


Pssm-ID: 188905  Cd Length: 66  Bit Score: 56.17  E-value: 8.46e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2112719293 1100 VASWGTHEVATWLDTLQLTEYIDSFEKNDIRGRELLTLARRDLKDLGVTK 1149
Cdd:cd09506      2 VHEWTVDDVGDWLESLNLGEHRERFMDNEIDGSHLPNLDKEDLTELGVTR 51
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 664-837 1.09e-09

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


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 61.41  E-value: 1.09e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112719293  664 ERCVMNNyFGIGIDAKISLDFHHKReehpeKCRSRAKNYLWYGVlggKELLQRTFknleQRVQLECDGQRIPLPSLQgIV 743
Cdd:COG1597    128 GRYFLNV-AGIGFDAEVVERANRAL-----KRRLGKLAYVLAAL---RALLRYRP----FRLRIELDGEEIEGEALL-VA 193

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112719293  744 ILNIPRFMGGINFWGGSKMDD----VFIAPSFDdkILEVVAVFgsMQMAASRMMKFQHHRIAQCQSIQINilGDEGVPIQ 819
Cdd:COG1597    194 VGNGPYYGGGLRLAPDASLDDglldVVVVRPLS--RLRLLRLL--PRLLRGRHLRHPGVRYFRAREVEIE--SDRPLPVQ 267

                          170
                   ....*....|....*....
gi 2112719293  820 VDGEA-WIQPPGIIRILHK 837
Cdd:COG1597    268 LDGEPlGLATPLEFEVLPG 286
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 1100-1153 1.40e-09

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 55.38  E-value: 1.40e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 2112719293  1100 VASWGTHEVATWLDTLQLTEYIDSFEKNDIRGRELLTLARR-DLKDLGVTK--HKLK 1153
Cdd:smart00454    1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEeDLKELGITKlgHRKK 57
SAM_Ste11_fungal cd09534
SAM domain of Ste11_fungal subfamily; SAM (sterile alpha motif) domain of Ste11 subfamily is a ...
 1103-1149 1.21e-08

SAM domain of Ste11_fungal subfamily; SAM (sterile alpha motif) domain of Ste11 subfamily is a protein-protein interaction domain. Proteins of this subfamily have SAM domain at the N-terminus and protein kinase domain at the C-terminus. They participate in regulation of mating pheromone response, invasive growth and high osmolarity growth response. MAP triple kinase Ste11 from S.cerevisia is known to interact with Ste20 kinase and Ste50 regulator. These kinases are able to form homodimers interacting through their SAM domains as well as heterodimers or heterogenous complexes when either SAM domain of monomeric or homodimeric form of Ste11 interacts with Ste50 regulator.


Pssm-ID: 188933  Cd Length: 62  Bit Score: 52.60  E-value: 1.21e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2112719293 1103 WGTHEVATWLDTLQLTEYIDSFEKNDIRGRELLTLARRDLKDLGVTK 1149
Cdd:cd09534      1 WDEEFVEEWLNELNCGQYLDIFEKNLITGDLLLELDKEALKELGITK 47
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 1102-1153 1.31e-08

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 52.66  E-value: 1.31e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2112719293 1102 SWGTHEVATWLDTLQLTEYIDSFEKNDIRGRELLTLARRDLKDLGVTK--HKLK 1153
Cdd:pfam00536    2 GWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLlgHRKK 55
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 1107-1164 2.11e-08

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: 51.86  E-value: 2.11e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2112719293 1107 EVATWLDTLQLTEYIDSFEKNDIRGRELLTLARRDLKDLGVTkhklKSSQRDKVKKFI 1164
Cdd:cd09487      1 DVAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDLKELGIT----SPGHRKKILRAI 54
SAM_CNK1,2,3-suppressor cd09511
SAM domain of CNK1,2,3-suppressor subfamily; SAM (sterile alpha motif) domain of CNK ...
 1100-1149 1.32e-07

SAM domain of CNK1,2,3-suppressor subfamily; SAM (sterile alpha motif) domain of CNK (connector enhancer of kinase suppressor of ras (Ksr)) subfamily is a protein-protein interaction domain. CNK proteins are multidomain scaffold proteins containing a few protein-protein interaction domains and are required for connecting Rho and Ras signaling pathways. In Drosophila, the SAM domain of CNK is known to interact with the SAM domain of the aveugle protein, forming a heterodimer. Mutation of the SAM domain in human CNK1 abolishes the ability to cooperate with the Ras effector, supporting the idea that this interaction is necessary for proper Ras signal transduction.


Pssm-ID: 188910  Cd Length: 69  Bit Score: 49.98  E-value: 1.32e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2112719293 1100 VASWGTHEVATWLDTLQ--LTEYIDSFEKNDIRGRELLTLARRDLKDLGVTK 1149
Cdd:cd09511      1 VAKWSPKQVTDWLKGLDdcLQQYIYTFEREKVTGEQLLNLSPQDLENLGVTK 52
SAM_Neurabin-like cd09512
SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like ...
 1100-1161 2.21e-07

SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like (Neural actin-binding) subfamily is a putative protein-protein interaction domain. This group currently includes the SAM domains of neurobin-I, SAMD14 and neurobin-I/SAMD14-like proteins. Most are multidomain proteins and in addition to SAM domain they contain other protein-binding domains such as PDZ and actin-binding domains. Members of this subfamily participate in signal transduction. Neurabin-I is involved in the regulation of Ca signaling intensity in alpha-adrenergic receptors; it forms a functional pair of opposing regulators with neurabin-II. Neurabins are expressed almost exclusively in neuronal cells. They are known to interact with protein phosphatase 1 and inhibit its activity; they also can bind actin filaments; however, the exact role of the SAM domain is unclear, since SAM doesn't participate in these interactions.


Pssm-ID: 188911 [Multi-domain]  Cd Length: 70  Bit Score: 49.19  E-value: 2.21e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2112719293 1100 VASWGTHEVATWLDTLQLTEYIDSFEKNDIRGRELLTLARRDLKDLGVTKHKLKSSQRDKVK 1161
Cdd:cd09512      4 VSEWSVQQVCQWLMGLGLEQYIPEFTANNIDGQQLLQLDSSKLKALGITSSSDRSLLKKKLK 65
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
1100-1153 4.35e-06

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 45.72  E-value: 4.35e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2112719293 1100 VASWGTHEVATWLDTLQLTEYIDSFEKNDIRGRE-LLTLARRDLKDLGVTK--HKLK 1153
Cdd:pfam07647    1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAElLLRLTLEDLKRLGITSvgHRRK 57
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 4-32 4.68e-06

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: 47.19  E-value: 4.68e-06
                           10        20
                   ....*....|....*....|....*....
gi 2112719293    4 QCQVAVLPLGTGNDLARVLGWGASCDSDA 32
Cdd:pfam00781   81 RPPLGIIPLGTGNDFARALGIPGDPEEAL 109
SAM_Ste50-like_fungal cd09533
SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or ...
 1107-1152 1.55e-05

SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or Ubc2 for Ustilago bypass of cyclase) subfamily is a putative protein-protein interaction domain. This group includes only fungal proteins. Basidiomycetes have an N-terminal SAM domain, central UBQ domain, and C-terminal SH3 domain, while Ascomycetes lack the SH3 domain. Ubc2 of Ustilago maydis is a major virulence and maize pathogenicity factor. It is required for filamentous growth (the budding haploid form of Ustilago maydis is a saprophyte, while filamentous dikaryotic form is a pathogen). Also the Ubc2 protein is involved in the pheromone-responsive morphogenesis via the MAP kinase cascade. The SAM domain is necessary for ubc2 function; deletion of SAM eliminates this function. A Lys-to-Glu mutation in the SAM domain of ubc2 gene induces temperature sensitivity.


Pssm-ID: 188932  Cd Length: 58  Bit Score: 43.84  E-value: 1.55e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2112719293 1107 EVATWLDTLQLTEYIDSFEKNDIRGRELLTLARRDLKDLGVTK--HKL 1152
Cdd:cd09533      1 DVADWLSSLGLPQYEDQFIENGITGDVLVALDHEDLKEMGITSvgHRL 48
UBA_4 pfam14555
UBA-like domain;
1157-1198 4.11e-05

UBA-like domain;


Pssm-ID: 464207  Cd Length: 43  Bit Score: 42.05  E-value: 4.11e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 2112719293 1157 RDKVKKFISFTQTGESTAIYCLTQNDWKLDLASDNYFQNPDA 1198
Cdd:pfam14555    1 DELIAQFQAITGADEEVARQYLEAHNWDLEAAVNAFFDDGEA 42
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
 1100-1148 4.34e-05

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: 43.07  E-value: 4.34e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2112719293 1100 VASWGTHEVATWLDTLQLTEYIDSFEKNDIRGRELLTLARRDL-KDLGVT 1148
Cdd:cd09505      2 LQDWSEEDVCTWLRSIGLEQYVEVFRANNIDGKELLNLTKESLsKDLKIE 51
SAM_SGMS1-like cd09515
SAM domain of sphingomyelin synthase related subfamily; SAM (sterile alpha motif) domain of ...
 1100-1152 4.36e-05

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: 43.01  E-value: 4.36e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2112719293 1100 VASWGTHEVATWLDTLQLTEYIDSF-EKNDIRGRELLTLARRDLKDLGVTKHKL 1152
Cdd:cd09515      1 VHEWTCEDVAKWLKKEGFSKYVDLLcNKHRIDGKVLLSLTEEDLRSPPLEIKVL 54
SAM_liprin-beta1,2_repeat2 cd09566
SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 1103-1148 1.76e-04

SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-alpha proteins through their SAM domains. It was suggested based on bioinformatic approaches that the second SAM domain of liprin-beta potentially is able to form polymers. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.


Pssm-ID: 188965  Cd Length: 63  Bit Score: 40.76  E-value: 1.76e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2112719293 1103 WGTHEVATWLDTLQLTEYIDSFEKNDIRGRELLTLARRDLKDLGVT 1148
Cdd:cd09566      2 LDTHWVLRWLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDLLHLKVT 47
SAM_MLTK cd09529
SAM domain of MLTK subfamily; SAM (sterile alpha motif) domain of MLTK subfamily is a ...
 1102-1148 1.80e-04

SAM domain of MLTK subfamily; SAM (sterile alpha motif) domain of MLTK subfamily is a protein-protein interaction domain. Besides SAM domain, these proteins have N-terminal protein tyrosine kinase domain and leucine-zipper motif. Proteins of this group act as mitogen-activated protein triple kinase in a number of MAPK cascades. They can be activated by autophosphorylation in response to stress signals. MLTK-alpha is known to phosphorylate histone H3. In mammals, MLTKs participate in the activation of the JNK/SAPK, p38, ERK5 pathways, the transcriptional factor NF-kB, in the regulation of the cell cycle checkpoint, and in the induction of apoptosis in a hepatoma cell line. Some members of this subfamily are proto-oncogenes, thus MLTK-alpha is involved in neoplasmic cell transformation and/or skin cancer development in athymic nude mice. Based on in vivo coprecipitation experiments in mammalian cells, it has been demonstrated that MLTK proteins might form homodimers/oligomers via their SAM domains.


Pssm-ID: 188928  Cd Length: 71  Bit Score: 41.34  E-value: 1.80e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2112719293 1102 SWGTHEVATWLDTL--------QLTEYIDSFEKNDIRGRELLTLARRDLKDLGVT 1148
Cdd:cd09529      1 AWTEEDVHFWMQQLvrkgghpsELSQYADLFKENHITGKRLLLLTEEDLRDMGIG 55
UBA_TAP-C_like cd14273
UBA-like domain found in the NXF family of mRNA nuclear export factors and similar proteins; ...
 1163-1193 1.83e-04

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


Pssm-ID: 270459  Cd Length: 31  Bit Score: 40.08  E-value: 1.83e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 2112719293 1163 FISFTQTGESTAIYCLTQNDWKLDLASDNYF 1193
Cdd:cd14273      1 FMEITGADPETARQYLESNNWDLEAAINLYF 31
SAM_DDHD2 cd09585
SAM domain of DDHD2; SAM (sterile alpha motif) domain of DDHD2 group is a potential ...
 1104-1147 2.00e-04

SAM domain of DDHD2; SAM (sterile alpha motif) domain of DDHD2 group is a potential protein-protein interaction domain. DDHD2 proteins contain at least two domains:a SAM domain and a predicted metal-binding domain. Phospholipase A1 activity was demonstrated for the mammalian DDHD2 protein. Mutation of the putative catalytic serine resulted in elimination of activity. Unlike SEC23IP, DDHD2 proteins do not have an N-terminal proline-rich region and correspondingly they are not able to interact with Sec23p/Sec24p complex. Overexpression of DDHD2 is the cause of dispersion of ER/Golgi intermediate compartment and dispersion of tethering proteins located in the Golgi region, leading to aggregation in the endoplasmic reticulum.


Pssm-ID: 188984  Cd Length: 69  Bit Score: 40.89  E-value: 2.00e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2112719293 1104 GTHEVATWLDTLQLTEYIDSFEKNDIRGRELLTLARRDLKDLGV 1147
Cdd:cd09585      8 DTPTLEETLKKLGLSEYCDVFEKEKIDLEALALCQERDLKDLGI 51
SAM_kazrin_repeat2 cd09567
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ...
 1110-1149 4.86e-04

SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrins contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved in interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.


Pssm-ID: 188966  Cd Length: 65  Bit Score: 39.70  E-value: 4.86e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 2112719293 1110 TWLDTLQLTEYIDSFEKNDIRGRELLTLARRDL-KDLGVTK 1149
Cdd:cd09567     10 EWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLeKHLGVSK 50
SAM_Samd14 cd09530
SAM domain of Samd14 subfamily; SAM (sterile alpha motif) domain of SamD14 (or FAM15A) ...
 1102-1149 1.27e-03

SAM domain of Samd14 subfamily; SAM (sterile alpha motif) domain of SamD14 (or FAM15A) subfamily is a putative protein-protein interaction domain. SAM is widespread domain in proteins involved in signal transduction and regulation. In many cases SAM mediates homodimerization/oligomerization. The exact function of proteins belonging to this subfamily is unknown.


Pssm-ID: 188929  Cd Length: 67  Bit Score: 38.45  E-value: 1.27e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2112719293 1102 SWGTHEVATWLDTLQLTEYIDSFEKNDIRGRELLTLARRDLKDLGVTK 1149
Cdd:cd09530      2 SWDTEDVAEWIEGLGFPQYRECFTTNFIDGRKLILVDASTLPRMGVTD 49
UBA_DCN1 cd14352
UBA-like domain found in yeast defective in cullin neddylation protein 1 (DCN1) and similar ...
 1160-1193 3.29e-03

UBA-like domain found in yeast defective in cullin neddylation protein 1 (DCN1) and similar proteins; DCN1 is a scaffold-type E3 ligase for cullin neddylation. It can bind directly to cullins and the ubiquitin-like protein Nedd8-specific E2 (Ubc12), and regulate cullin neddylation and thus display ubiquitin ligase activity. It contains an N-terminal ubiquitin-associated (UBA)-like domain and a unique C-terminal PONY domain that is essential for the neddylation function of DCN1.


Pssm-ID: 270537  Cd Length: 36  Bit Score: 36.49  E-value: 3.29e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2112719293 1160 VKKFISFTQTGESTAIYCLTQNDWKLDLASDNYF 1193
Cdd:cd14352      3 IKQFREITATSPEVARDYLQRSNWNLNYAVDDFY 36
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 1-23 3.80e-03

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


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 40.99  E-value: 3.80e-03
                           10        20
                   ....*....|....*....|...
gi 2112719293    1 MHKQCQVAVLPLGTGNDLARVLG 23
Cdd:COG1597     79 AGTGPPLGILPLGTGNDFARALG 101
SAM_SARM1-like_repeat1 cd09501
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 1100-1148 5.57e-03

SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of SARM1-like adaptor proteins is a protein-protein interaction domain. SARM1-like proteins contain two tandem SAM domains. SARM1-like proteins are involved in TLR (Toll-like receptor) signaling. They are responsible for targeted localization of the whole protein to post-synaptic regions of axons. In humans SARM1 expression is detected in kidney and liver.


Pssm-ID: 188900 [Multi-domain]  Cd Length: 69  Bit Score: 36.90  E-value: 5.57e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2112719293 1100 VASWGTHEVATWLDTLQLTEYIDSFEKNDIRGRELLTLARRDLK-DLGVT 1148
Cdd:cd09501      1 VPLWSVADVQTWLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKqDLGMS 50
SAM_BOI-like_fungal cd09535
SAM domain of BOI-like fungal subfamily; SAM (sterile alpha motif) domain of BOI-like fungal ...
 1102-1148 5.68e-03

SAM domain of BOI-like fungal subfamily; SAM (sterile alpha motif) domain of BOI-like fungal subfamily is a potential protein-protein interaction domain. Proteins of this subfamily are apparently scaffold proteins, since most contain SH3 and PH domains, which are also protein-protein interaction domains, in addition to SAM domain. BOI-like proteins participate in cell cycle regulation. In particular BOI1 and BOI2 proteins of budding yeast S.cerevisiae are involved in bud formation, and POB1 protein of fission yeast S.pombe plays a role in cell elongation and separation. Among binding partners of BOI-like fungal subfamily members are such proteins as Bem1 and Cdc42 (they are known to be involved in cell polarization and bud formation).


Pssm-ID: 188934  Cd Length: 65  Bit Score: 36.76  E-value: 5.68e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2112719293 1102 SWGTHEVATWLDTLQLTEYI-DSFEKNDIRGRELLTLARRDLKDLGVT 1148
Cdd:cd09535      2 SWSPEQVAEWLLSAGFDDSVcEKFRENEITGDILLELDLEDLKELDIG 49
SAM_caskin1,2_repeat1 cd09497
SAM domain of caskin protein repeat 1; SAM (sterile alpha motif) domain repeat 1 of caskin1,2 ...
 1107-1154 7.81e-03

SAM domain of caskin protein repeat 1; SAM (sterile alpha motif) domain repeat 1 of caskin1,2 proteins is a protein-protein interaction domain. Caskin has two tandem SAM domains. Caskin protein is known to interact with membrane-associated guanylate kinase CASK, and apparently may play a role in neural development, synaptic protein targeting, and regulation of gene expression.


Pssm-ID: 188896  Cd Length: 66  Bit Score: 36.47  E-value: 7.81e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2112719293 1107 EVATWLDTLQLTEYIDSFEKNdirGRELLTLAR---RDLKDLGVTK--H--KLKS 1154
Cdd:cd09497      6 AIFDWLREFGLEEYTPNFIKA---GYDLPTISRmtpEDLTAIGITKpgHrkKLKS 57
 
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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