NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1650796977|ref|NP_061339|]
View 

deoxynucleoside triphosphate triphosphohydrolase SAMHD1 isoform 1 [Mus musculus]

Protein Classification

SAM_HD and HDc domain-containing protein( domain architecture ID 12966159)

SAM_HD and HDc domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
YdhJ COG1078
HD superfamily phosphohydrolase [General function prediction only];
116-469 1.45e-70

HD superfamily phosphohydrolase [General function prediction only];


:

Pssm-ID: 440696 [Multi-domain]  Cd Length: 340  Bit Score: 231.61  E-value: 1.45e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650796977 116 MKVFNDPIHGHIEFHPLLIRIIDTPQFQRLRYIKQLGGGYYVFPGASHNRFEHSLGVGYLAGCLVRALAEKQPElqISER 195
Cdd:COG1078     1 MKIIRDPVHGYIEVDELELDLIDTPEFQRLRRIKQLGLAYLVYPGAEHTRFEHSLGVMHLARRALDRLRRKGVE--IDEE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650796977 196 DILCVQIAGLCHDLGHGPFSHMFDGRFiprarpEKKWKHEQGSIEmfehLVNSNELKLVMKNYGLVPEEditfIKEQIMG 275
Cdd:COG1078    79 ERELVRAAALLHDIGHGPFSHAFEEVL------LTGVDHEEITLR----IIEENEINGILEKHGIDPEL----VADIIKG 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650796977 276 PPItpvkdslwpykgrpatKSFLYEIVSnkrNGIDVDKWDYFARDCHHLGIQN-NFDYKRFIKFARICEVEYKVKedkty 354
Cdd:COG1078   145 EYP----------------NKFLRQLIS---SQLDADRMDYLLRDSYYTGVSYgNIDLERLIRMLRVVDDELVVE----- 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650796977 355 irkvkhicsrEKEVGNLYDMFHTRNCLHRRAYQHKISNLIDIMITDAFLKADPYVEitgtAGKKFRistaIDDMEAFTKL 434
Cdd:COG1078   201 ----------EKGIYAVESFLIARYLMYWQVYFHKTSRAAEVMLRRALERAKELYD----EGELEN----PLDLEDFLRL 262
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1650796977 435 TDNIFLEVL----HSTDPQLSE-AQSILRniecRNLYKYL 469
Cdd:COG1078   263 DDYDLLSALkewqDHPDPILSDlARRLLN----RKLFKRV 298
SAM_HD cd09508
SAM domain of HD-phosphohydrolase; SAM (sterile alpha motif) domain of SAM_HD subfamily ...
42-111 1.69e-31

SAM domain of HD-phosphohydrolase; SAM (sterile alpha motif) domain of SAM_HD subfamily proteins is a putative protein-protein interaction domain. Proteins of this group, additionally to the SAM domain, contain a HD hydrolase domain. Human SAM-HD1 is a nuclear protein involved in innate immune response and may act as a negative regulator of the cell-intrinsic antiviral response. Mutations in this gene lead to Aicardi-Goutieres syndrome (symptoms include cerebral atrophy, leukoencephalopathy, hepatosplenomegaly, and increased production of alpha-interferon).


:

Pssm-ID: 188907  Cd Length: 70  Bit Score: 116.65  E-value: 1.69e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650796977  42 DLRTWEPEDVCSFLENRGFREKKVLDIFRDNKIAGSFLPFLDEDRLEDLGVSSLEERKKMIECIQQLSQS 111
Cdd:cd09508     1 DFRSWDPEDVCQFLRGNGFGEPELLEIFRENEITGAHLPDLTESRLEKLGVSSLGERLKLLKCLQKLSQI 70
 
Name Accession Description Interval E-value
YdhJ COG1078
HD superfamily phosphohydrolase [General function prediction only];
116-469 1.45e-70

HD superfamily phosphohydrolase [General function prediction only];


Pssm-ID: 440696 [Multi-domain]  Cd Length: 340  Bit Score: 231.61  E-value: 1.45e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650796977 116 MKVFNDPIHGHIEFHPLLIRIIDTPQFQRLRYIKQLGGGYYVFPGASHNRFEHSLGVGYLAGCLVRALAEKQPElqISER 195
Cdd:COG1078     1 MKIIRDPVHGYIEVDELELDLIDTPEFQRLRRIKQLGLAYLVYPGAEHTRFEHSLGVMHLARRALDRLRRKGVE--IDEE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650796977 196 DILCVQIAGLCHDLGHGPFSHMFDGRFiprarpEKKWKHEQGSIEmfehLVNSNELKLVMKNYGLVPEEditfIKEQIMG 275
Cdd:COG1078    79 ERELVRAAALLHDIGHGPFSHAFEEVL------LTGVDHEEITLR----IIEENEINGILEKHGIDPEL----VADIIKG 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650796977 276 PPItpvkdslwpykgrpatKSFLYEIVSnkrNGIDVDKWDYFARDCHHLGIQN-NFDYKRFIKFARICEVEYKVKedkty 354
Cdd:COG1078   145 EYP----------------NKFLRQLIS---SQLDADRMDYLLRDSYYTGVSYgNIDLERLIRMLRVVDDELVVE----- 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650796977 355 irkvkhicsrEKEVGNLYDMFHTRNCLHRRAYQHKISNLIDIMITDAFLKADPYVEitgtAGKKFRistaIDDMEAFTKL 434
Cdd:COG1078   201 ----------EKGIYAVESFLIARYLMYWQVYFHKTSRAAEVMLRRALERAKELYD----EGELEN----PLDLEDFLRL 262
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1650796977 435 TDNIFLEVL----HSTDPQLSE-AQSILRniecRNLYKYL 469
Cdd:COG1078   263 DDYDLLSALkewqDHPDPILSDlARRLLN----RKLFKRV 298
SAM_HD cd09508
SAM domain of HD-phosphohydrolase; SAM (sterile alpha motif) domain of SAM_HD subfamily ...
42-111 1.69e-31

SAM domain of HD-phosphohydrolase; SAM (sterile alpha motif) domain of SAM_HD subfamily proteins is a putative protein-protein interaction domain. Proteins of this group, additionally to the SAM domain, contain a HD hydrolase domain. Human SAM-HD1 is a nuclear protein involved in innate immune response and may act as a negative regulator of the cell-intrinsic antiviral response. Mutations in this gene lead to Aicardi-Goutieres syndrome (symptoms include cerebral atrophy, leukoencephalopathy, hepatosplenomegaly, and increased production of alpha-interferon).


Pssm-ID: 188907  Cd Length: 70  Bit Score: 116.65  E-value: 1.69e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650796977  42 DLRTWEPEDVCSFLENRGFREKKVLDIFRDNKIAGSFLPFLDEDRLEDLGVSSLEERKKMIECIQQLSQS 111
Cdd:cd09508     1 DFRSWDPEDVCQFLRGNGFGEPELLEIFRENEITGAHLPDLTESRLEKLGVSSLGERLKLLKCLQKLSQI 70
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
163-336 7.72e-14

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 69.29  E-value: 7.72e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650796977 163 HNRFEHSLGVGYLAgclvRALAEKqpeLQISERDILCVQIAGLCHDLGHGPFSHMFdgrfiprarpekkwkHEQGSIEMF 242
Cdd:cd00077     1 EHRFEHSLRVAQLA----RRLAEE---LGLSEEDIELLRLAALLHDIGKPGTPDAI---------------TEEESELEK 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650796977 243 EHLVNSNELKLVmknygLVPEEDITFIKEQIMGpPITPVKDSLWPYKGRPATKSflYEIVSNKRNGIDVDKWDYFARDCH 322
Cdd:cd00077    59 DHAIVGAEILRE-----LLLEEVIKLIDELILA-VDASHHERLDGLGYPDGLKG--EEITLEARIVKLADRLDALRRDSR 130
                         170
                  ....*....|....*
gi 1650796977 323 HLGIQ-NNFDYKRFI 336
Cdd:cd00077   131 EKRRRiAEEDLEELL 145
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
161-244 1.65e-11

Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic nucleotide phosphodiesterases (PDEc). This profile/HMM does not detect HD homologues in bacterial glycine aminoacyl-tRNA synthetases (beta subunit).


Pssm-ID: 214679 [Multi-domain]  Cd Length: 124  Bit Score: 61.93  E-value: 1.65e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650796977  161 ASHNRFEHSLGVGYLAgclvRALAEKQPELqiserDILCVQIAGLCHDLGHGPFSHMFDGRFIPrarpekKWKHEQGSIE 240
Cdd:smart00471   1 SDYHVFEHSLRVAQLA----AALAEELGLL-----DIELLLLAALLHDIGKPGTPDSFLVKTSV------LEDHHFIGAE 65

                   ....
gi 1650796977  241 MFEH 244
Cdd:smart00471  66 ILLE 69
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
45-108 1.54e-10

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 57.28  E-value: 1.54e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1650796977  45 TWEPEDVCSFLENRGFREkkVLDIFRDNKIAG-SFLPFLDEDRLEDLGVSSLEERKKMIECIQQL 108
Cdd:pfam07647   3 SWSLESVADWLRSIGLEQ--YTDNFRDQGITGaELLLRLTLEDLKRLGITSVGHRRKILKKIQEL 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
45-111 1.76e-10

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: 56.92  E-value: 1.76e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1650796977   45 TWEPEDVCSFLENRGFreKKVLDIFRDNKIAGSFLPFLD-EDRLEDLGVSSLEERKKMIECIQQLSQS 111
Cdd:smart00454   3 QWSPESVADWLESIGL--EQYADNFRKNGIDGALLLLLTsEEDLKELGITKLGHRKKILKAIQKLKEQ 68
HD pfam01966
HD domain; HD domains are metal dependent phosphohydrolases.
165-258 3.11e-08

HD domain; HD domains are metal dependent phosphohydrolases.


Pssm-ID: 460398 [Multi-domain]  Cd Length: 110  Bit Score: 51.85  E-value: 3.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650796977 165 RFEHSLGVGYLAGCLVRALAEKQPELqiserdilcVQIAGLCHDLGHGPFS-----------HMFDGRFIPRARPEKKWk 233
Cdd:pfam01966   1 RLEHSLRVALLARELAEELGELDREL---------LLLAALLHDIGKGPFGdekpefeiflgHAVVGAEILRELEKRLG- 70
                          90       100
                  ....*....|....*....|....*
gi 1650796977 234 heqgsIEMFEHLVNSNELKLVMKNY 258
Cdd:pfam01966  71 -----LEDVLKLILEHHESWEGAGY 90
PRK01096 PRK01096
deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional
126-216 1.90e-04

deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional


Pssm-ID: 234897 [Multi-domain]  Cd Length: 440  Bit Score: 44.14  E-value: 1.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650796977 126 HIEFHplliRIIDTPQFQRLRYIKQlgggyyVFPGAS----HNRFEHSLGVGylagCLVRALA--------EKQPELQIS 193
Cdd:PRK01096   29 HKDYD----RIIFSGSFRRLQRKTQ------VHPLAKndhiHTRLTHSLEVS----CVGRSLGmrvgetlkEEKLPDWIS 94
                          90       100
                  ....*....|....*....|....
gi 1650796977 194 ERDI-LCVQIAGLCHDLGHGPFSH 216
Cdd:PRK01096   95 PADIgAIVQSACLAHDIGNPPFGH 118
 
Name Accession Description Interval E-value
YdhJ COG1078
HD superfamily phosphohydrolase [General function prediction only];
116-469 1.45e-70

HD superfamily phosphohydrolase [General function prediction only];


Pssm-ID: 440696 [Multi-domain]  Cd Length: 340  Bit Score: 231.61  E-value: 1.45e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650796977 116 MKVFNDPIHGHIEFHPLLIRIIDTPQFQRLRYIKQLGGGYYVFPGASHNRFEHSLGVGYLAGCLVRALAEKQPElqISER 195
Cdd:COG1078     1 MKIIRDPVHGYIEVDELELDLIDTPEFQRLRRIKQLGLAYLVYPGAEHTRFEHSLGVMHLARRALDRLRRKGVE--IDEE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650796977 196 DILCVQIAGLCHDLGHGPFSHMFDGRFiprarpEKKWKHEQGSIEmfehLVNSNELKLVMKNYGLVPEEditfIKEQIMG 275
Cdd:COG1078    79 ERELVRAAALLHDIGHGPFSHAFEEVL------LTGVDHEEITLR----IIEENEINGILEKHGIDPEL----VADIIKG 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650796977 276 PPItpvkdslwpykgrpatKSFLYEIVSnkrNGIDVDKWDYFARDCHHLGIQN-NFDYKRFIKFARICEVEYKVKedkty 354
Cdd:COG1078   145 EYP----------------NKFLRQLIS---SQLDADRMDYLLRDSYYTGVSYgNIDLERLIRMLRVVDDELVVE----- 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650796977 355 irkvkhicsrEKEVGNLYDMFHTRNCLHRRAYQHKISNLIDIMITDAFLKADPYVEitgtAGKKFRistaIDDMEAFTKL 434
Cdd:COG1078   201 ----------EKGIYAVESFLIARYLMYWQVYFHKTSRAAEVMLRRALERAKELYD----EGELEN----PLDLEDFLRL 262
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1650796977 435 TDNIFLEVL----HSTDPQLSE-AQSILRniecRNLYKYL 469
Cdd:COG1078   263 DDYDLLSALkewqDHPDPILSDlARRLLN----RKLFKRV 298
SAM_HD cd09508
SAM domain of HD-phosphohydrolase; SAM (sterile alpha motif) domain of SAM_HD subfamily ...
42-111 1.69e-31

SAM domain of HD-phosphohydrolase; SAM (sterile alpha motif) domain of SAM_HD subfamily proteins is a putative protein-protein interaction domain. Proteins of this group, additionally to the SAM domain, contain a HD hydrolase domain. Human SAM-HD1 is a nuclear protein involved in innate immune response and may act as a negative regulator of the cell-intrinsic antiviral response. Mutations in this gene lead to Aicardi-Goutieres syndrome (symptoms include cerebral atrophy, leukoencephalopathy, hepatosplenomegaly, and increased production of alpha-interferon).


Pssm-ID: 188907  Cd Length: 70  Bit Score: 116.65  E-value: 1.69e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650796977  42 DLRTWEPEDVCSFLENRGFREKKVLDIFRDNKIAGSFLPFLDEDRLEDLGVSSLEERKKMIECIQQLSQS 111
Cdd:cd09508     1 DFRSWDPEDVCQFLRGNGFGEPELLEIFRENEITGAHLPDLTESRLEKLGVSSLGERLKLLKCLQKLSQI 70
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
163-336 7.72e-14

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 69.29  E-value: 7.72e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650796977 163 HNRFEHSLGVGYLAgclvRALAEKqpeLQISERDILCVQIAGLCHDLGHGPFSHMFdgrfiprarpekkwkHEQGSIEMF 242
Cdd:cd00077     1 EHRFEHSLRVAQLA----RRLAEE---LGLSEEDIELLRLAALLHDIGKPGTPDAI---------------TEEESELEK 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650796977 243 EHLVNSNELKLVmknygLVPEEDITFIKEQIMGpPITPVKDSLWPYKGRPATKSflYEIVSNKRNGIDVDKWDYFARDCH 322
Cdd:cd00077    59 DHAIVGAEILRE-----LLLEEVIKLIDELILA-VDASHHERLDGLGYPDGLKG--EEITLEARIVKLADRLDALRRDSR 130
                         170
                  ....*....|....*
gi 1650796977 323 HLGIQ-NNFDYKRFI 336
Cdd:cd00077   131 EKRRRiAEEDLEELL 145
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
161-244 1.65e-11

Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic nucleotide phosphodiesterases (PDEc). This profile/HMM does not detect HD homologues in bacterial glycine aminoacyl-tRNA synthetases (beta subunit).


Pssm-ID: 214679 [Multi-domain]  Cd Length: 124  Bit Score: 61.93  E-value: 1.65e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650796977  161 ASHNRFEHSLGVGYLAgclvRALAEKQPELqiserDILCVQIAGLCHDLGHGPFSHMFDGRFIPrarpekKWKHEQGSIE 240
Cdd:smart00471   1 SDYHVFEHSLRVAQLA----AALAEELGLL-----DIELLLLAALLHDIGKPGTPDSFLVKTSV------LEDHHFIGAE 65

                   ....
gi 1650796977  241 MFEH 244
Cdd:smart00471  66 ILLE 69
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
45-108 1.54e-10

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 57.28  E-value: 1.54e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1650796977  45 TWEPEDVCSFLENRGFREkkVLDIFRDNKIAG-SFLPFLDEDRLEDLGVSSLEERKKMIECIQQL 108
Cdd:pfam07647   3 SWSLESVADWLRSIGLEQ--YTDNFRDQGITGaELLLRLTLEDLKRLGITSVGHRRKILKKIQEL 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
45-111 1.76e-10

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: 56.92  E-value: 1.76e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1650796977   45 TWEPEDVCSFLENRGFreKKVLDIFRDNKIAGSFLPFLD-EDRLEDLGVSSLEERKKMIECIQQLSQS 111
Cdd:smart00454   3 QWSPESVADWLESIGL--EQYADNFRKNGIDGALLLLLTsEEDLKELGITKLGHRKKILKAIQKLKEQ 68
SAM_BOI-like_fungal cd09535
SAM domain of BOI-like fungal subfamily; SAM (sterile alpha motif) domain of BOI-like fungal ...
44-108 8.80e-09

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: 52.17  E-value: 8.80e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1650796977  44 RTWEPEDVCSFLENRGFrEKKVLDIFRDNKIAGSFLPFLDEDRLEDLGVSSLEERKKMIECIQQL 108
Cdd:cd09535     1 RSWSPEQVAEWLLSAGF-DDSVCEKFRENEITGDILLELDLEDLKELDIGSFGKRFKLWNEIKSL 64
HD pfam01966
HD domain; HD domains are metal dependent phosphohydrolases.
165-258 3.11e-08

HD domain; HD domains are metal dependent phosphohydrolases.


Pssm-ID: 460398 [Multi-domain]  Cd Length: 110  Bit Score: 51.85  E-value: 3.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650796977 165 RFEHSLGVGYLAGCLVRALAEKQPELqiserdilcVQIAGLCHDLGHGPFS-----------HMFDGRFIPRARPEKKWk 233
Cdd:pfam01966   1 RLEHSLRVALLARELAEELGELDREL---------LLLAALLHDIGKGPFGdekpefeiflgHAVVGAEILRELEKRLG- 70
                          90       100
                  ....*....|....*....|....*
gi 1650796977 234 heqgsIEMFEHLVNSNELKLVMKNY 258
Cdd:pfam01966  71 -----LEDVLKLILEHHESWEGAGY 90
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
43-114 3.12e-08

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: 50.78  E-value: 3.12e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1650796977  43 LRTWEPEDVCSFLENRGFREkkVLDIFRDNKIAGSFLPFL-DEDRLEDLGVSSLEERKKMIECIQQLSQSRID 114
Cdd:cd09505     2 LQDWSEEDVCTWLRSIGLEQ--YVEVFRANNIDGKELLNLtKESLSKDLKIESLGHRNKILRKIEELKMKSDS 72
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
45-108 2.47e-07

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: 48.03  E-value: 2.47e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1650796977  45 TWEPEDVCSFLENRGFreKKVLDIFRDNKIAGSFLPFLDEDRLEDLGVSSLEERKKMIECIQQL 108
Cdd:pfam00536   2 GWSVEDVGEWLESIGL--GQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRL 63
SAM_Ste11_fungal cd09534
SAM domain of Ste11_fungal subfamily; SAM (sterile alpha motif) domain of Ste11 subfamily is a ...
46-108 5.40e-07

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: 46.82  E-value: 5.40e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1650796977  46 WEPEDVCSFLENRGFREkkVLDIFRDNKIAGSFLPFLDEDRLEDLGVSSLEERKKMIECIQQL 108
Cdd:cd09534     1 WDEEFVEEWLNELNCGQ--YLDIFEKNLITGDLLLELDKEALKELGITKVGDRIRLLRAIKSL 61
SAM_Shank1,2,3 cd09506
SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 ...
46-109 1.26e-06

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: 46.16  E-value: 1.26e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1650796977  46 WEPEDVCSFLENRGFREKKvlDIFRDNKIAGSFLPFLDEDRLEDLGVSSLEERKKMIECIQQLS 109
Cdd:cd09506     5 WTVDDVGDWLESLNLGEHR--ERFMDNEIDGSHLPNLDKEDLTELGVTRVGHRMNIERALKKLL 66
SAM_DGK-delta-eta cd09507
SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain ...
46-108 1.20e-05

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: 43.17  E-value: 1.20e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1650796977  46 WEPEDVCSFLENRGFREKKvlDIFRDNKIAGSFLPFLDEDRLEDLGVSSLEERKKMIECIQQL 108
Cdd:cd09507     5 WTTEEVGAWLESLQLGEYR--DIFARNDIRGSELLHLERRDLKDLGITKVGHVKRILQAIKDL 65
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
50-106 1.47e-05

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


Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 42.61  E-value: 1.47e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1650796977  50 DVCSFLENRGFreKKVLDIFRDNKIAGSFLPFLDEDRLEDLGVSSLEERKKMIECIQ 106
Cdd:cd09487     1 DVAEWLESLGL--EQYADLFRKNEIDGDALLLLTDEDLKELGITSPGHRKKILRAIQ 55
PRK01096 PRK01096
deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional
126-216 1.90e-04

deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional


Pssm-ID: 234897 [Multi-domain]  Cd Length: 440  Bit Score: 44.14  E-value: 1.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650796977 126 HIEFHplliRIIDTPQFQRLRYIKQlgggyyVFPGAS----HNRFEHSLGVGylagCLVRALA--------EKQPELQIS 193
Cdd:PRK01096   29 HKDYD----RIIFSGSFRRLQRKTQ------VHPLAKndhiHTRLTHSLEVS----CVGRSLGmrvgetlkEEKLPDWIS 94
                          90       100
                  ....*....|....*....|....
gi 1650796977 194 ERDI-LCVQIAGLCHDLGHGPFSH 216
Cdd:PRK01096   95 PADIgAIVQSACLAHDIGNPPFGH 118
SAM_DGK-delta cd09575
SAM domain of diacylglycerol kinase delta; SAM (sterile alpha motif) domain of DGK-delta ...
46-108 1.44e-03

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: 37.62  E-value: 1.44e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1650796977  46 WEPEDVCSFLENRGFREKKvlDIFRDNKIAGSFLPFLDEDRLEDLGVSSLEERKKMIECIQQL 108
Cdd:cd09575     5 WGTEEVAAWLEHLSLCEYK--DIFTRHDVRGSELLHLERRDLKDLGVTKVGHMKRILCGIKEL 65
SAM_SARM1-like_repeat1 cd09501
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
45-111 1.69e-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: 37.28  E-value: 1.69e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1650796977  45 TWEPEDVCSFLENRGFreKKVLDIFRDNKIAGSFLPFLDEDRLE-DLGVSSLEERKKMIECIQQLSQS 111
Cdd:cd09501     3 LWSVADVQTWLKQIGF--EDYAEKFSESQVDGDLLLQLTEDELKqDLGMSSGLLRKRFLRELVELKTS 68
SAM_Ste50-like_fungal cd09533
SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or ...
50-108 3.18e-03

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: 36.14  E-value: 3.18e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1650796977  50 DVCSFLENRGFREKKvlDIFRDNKIAGSFLPFLDEDRLEDLGVSSLEERKKMIECIQQL 108
Cdd:cd09533     1 DVADWLSSLGLPQYE--DQFIENGITGDVLVALDHEDLKEMGITSVGHRLTILKAVYEL 57
SAM_Samd7,11 cd09579
SAM domain of Samd7,11 subfamily of Polycomb group; SAM (sterile alpha motif) domain is a ...
43-89 9.18e-03

SAM domain of Samd7,11 subfamily of Polycomb group; SAM (sterile alpha motif) domain is a protein-protein interaction domain. Phylogenetic analysis suggests that proteins of this subfamily are most closely related to SAM-Ph1,2,3 subfamily of Polycomb group. They are predicted transcriptional repressors in photoreceptor cells and pinealocytes of vertebrates. SAM domain containing protein 11 is also known as Mr-s (major retinal SAM) protein. In mouse, it is predominantly expressed in developing retinal photoreceptors and in adult pineal gland. The SAM domain is involved in homooligomerization of whole proteins (it was shown based on immunoprecipitation assay and mutagenesis), however its repression activity is not due to SAM/SAM interactions but to the C-terminal region.


Pssm-ID: 188978  Cd Length: 68  Bit Score: 35.12  E-value: 9.18e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1650796977  43 LRTWEPEDVCSFLEN-RGFREkkVLDIFRDNKIAGSFLPFLDEDRLED 89
Cdd:cd09579     1 IRKWTVDDVCSFIGSlPGCAE--YAQVFREHSIDGETLPLLTEEHLLN 46
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH