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Conserved domains on  [gi|38016914|ref|NP_056289|]
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deoxynucleoside triphosphate triphosphohydrolase SAMHD1 isoform 1 [Homo sapiens]

Protein Classification

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

SAM_HD and HDc domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YdhJ COG1078
HD superfamily phosphohydrolase [General function prediction only];
115-472 2.44e-77

HD superfamily phosphohydrolase [General function prediction only];


:

Pssm-ID: 440696 [Multi-domain]  Cd Length: 340  Bit Score: 249.33  E-value: 2.44e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38016914 115 MKVINDPIHGHIELHPLLVRIIDTPQFQRLRYIKQLGGGYYVFPGASHNRFEHSLGVGYLAGCLVHALGEKQPElqISER 194
Cdd:COG1078   1 MKIIRDPVHGYIEVDELELDLIDTPEFQRLRRIKQLGLAYLVYPGAEHTRFEHSLGVMHLARRALDRLRRKGVE--IDEE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38016914 195 DVLCVQIAGLCHDLGHGPFSHMFDGRFiplarpEVKWTHEQGSVMmfehLINSNGIKPVMEQYGLIPEEDICFIkeqivg 274
Cdd:COG1078  79 ERELVRAAALLHDIGHGPFSHAFEEVL------LTGVDHEEITLR----IIEENEINGILEKHGIDPELVADII------ 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38016914 275 plespvedslwpyKGRPENKsFLYEIVSnkrNGIDVDKWDYFARDCHHLGIQN-NFDYKRFIKFARVceVDNELRIcaRD 353
Cdd:COG1078 143 -------------KGEYPNK-FLRQLIS---SQLDADRMDYLLRDSYYTGVSYgNIDLERLIRMLRV--VDDELVV--EE 201

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38016914 354 KEVGNLYDMFHTRNSLHRRAYQHKVGNIIDTMITDAFLKAddyIEITGAGGKKYRIstaidDMEAYTKLTDNIFLEIL-- 431
Cdd:COG1078 202 KGIYAVESFLIARYLMYWQVYFHKTSRAAEVMLRRALERA---KELYDEGELENPL-----DLEDFLRLDDYDLLSALke 273

                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 38016914 432 --YSTDPKLKDareILKQIEYRNLFKYVgetqptgqIKIKRED 472
Cdd:COG1078 274 wqDHPDPILSD---LARRLLNRKLFKRV--------ILIVDKN 305
SAM_HD cd09508
SAM domain of HD-phosphohydrolase; SAM (sterile alpha motif) domain of SAM_HD subfamily ...
 41-110 8.09e-33

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: 120.50  E-value: 8.09e-33
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38016914  41 DYKTWGPEQVCSFLRRGGFEEPVLLKNIRENEITGALLPCLDESRFENLGVSSLGERKKLLSYIQRLVQI 110
Cdd:cd09508   1 DFRSWDPEDVCQFLRGNGFGEPELLEIFRENEITGAHLPDLTESRLEKLGVSSLGERLKLLKCLQKLSQI 70
 
Name Accession Description Interval E-value
YdhJ COG1078
HD superfamily phosphohydrolase [General function prediction only];
115-472 2.44e-77

HD superfamily phosphohydrolase [General function prediction only];


Pssm-ID: 440696 [Multi-domain]  Cd Length: 340  Bit Score: 249.33  E-value: 2.44e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38016914 115 MKVINDPIHGHIELHPLLVRIIDTPQFQRLRYIKQLGGGYYVFPGASHNRFEHSLGVGYLAGCLVHALGEKQPElqISER 194
Cdd:COG1078   1 MKIIRDPVHGYIEVDELELDLIDTPEFQRLRRIKQLGLAYLVYPGAEHTRFEHSLGVMHLARRALDRLRRKGVE--IDEE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38016914 195 DVLCVQIAGLCHDLGHGPFSHMFDGRFiplarpEVKWTHEQGSVMmfehLINSNGIKPVMEQYGLIPEEDICFIkeqivg 274
Cdd:COG1078  79 ERELVRAAALLHDIGHGPFSHAFEEVL------LTGVDHEEITLR----IIEENEINGILEKHGIDPELVADII------ 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38016914 275 plespvedslwpyKGRPENKsFLYEIVSnkrNGIDVDKWDYFARDCHHLGIQN-NFDYKRFIKFARVceVDNELRIcaRD 353
Cdd:COG1078 143 -------------KGEYPNK-FLRQLIS---SQLDADRMDYLLRDSYYTGVSYgNIDLERLIRMLRV--VDDELVV--EE 201

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38016914 354 KEVGNLYDMFHTRNSLHRRAYQHKVGNIIDTMITDAFLKAddyIEITGAGGKKYRIstaidDMEAYTKLTDNIFLEIL-- 431
Cdd:COG1078 202 KGIYAVESFLIARYLMYWQVYFHKTSRAAEVMLRRALERA---KELYDEGELENPL-----DLEDFLRLDDYDLLSALke 273

                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 38016914 432 --YSTDPKLKDareILKQIEYRNLFKYVgetqptgqIKIKRED 472
Cdd:COG1078 274 wqDHPDPILSD---LARRLLNRKLFKRV--------ILIVDKN 305
SAM_HD cd09508
SAM domain of HD-phosphohydrolase; SAM (sterile alpha motif) domain of SAM_HD subfamily ...
 41-110 8.09e-33

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: 120.50  E-value: 8.09e-33
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38016914  41 DYKTWGPEQVCSFLRRGGFEEPVLLKNIRENEITGALLPCLDESRFENLGVSSLGERKKLLSYIQRLVQI 110
Cdd:cd09508   1 DFRSWDPEDVCQFLRGNGFGEPELLEIFRENEITGAHLPDLTESRLEKLGVSSLGERLKLLKCLQKLSQI 70
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
 162-335 1.46e-14

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 71.22  E-value: 1.46e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38016914 162 HNRFEHSLGVGYLAgclvHALGEKqpeLQISERDVLCVQIAGLCHDLGHGPFSHMFdgrfiplarpevkwtHEQGSVMMF 241
Cdd:cd00077   1 EHRFEHSLRVAQLA----RRLAEE---LGLSEEDIELLRLAALLHDIGKPGTPDAI---------------TEEESELEK 58

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38016914 242 EHLINSNGIKpvmeqYGLIPEEDICFIKEqIVGPLESPVEDSLWPYKGRPENKSflYEIVSNKRNGIDVDKWDYFARDCH 321
Cdd:cd00077  59 DHAIVGAEIL-----RELLLEEVIKLIDE-LILAVDASHHERLDGLGYPDGLKG--EEITLEARIVKLADRLDALRRDSR 130

                       170
                ....*....|....*
gi 38016914 322 HLGIQ-NNFDYKRFI 335
Cdd:cd00077 131 EKRRRiAEEDLEELL 145
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
 160-245 9.65e-12

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: 62.31  E-value: 9.65e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38016914    160 ASHNRFEHSLGVGYLAGCLVHALGEKqpelqiserDVLCVQIAGLCHDLGHGPFSHMFDGRFIPLarpevkWTHEQGSVM 239
Cdd:smart00471   1 SDYHVFEHSLRVAQLAAALAEELGLL---------DIELLLLAALLHDIGKPGTPDSFLVKTSVL------EDHHFIGAE 65


                   ....*.
gi 38016914    240 MFEHLI 245
Cdd:smart00471  66 ILLEEE 71
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 42-109 2.86e-11

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: 59.23  E-value: 2.86e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38016914     42 YKTWGPEQVCSFLRRGGFEEpvLLKNIRENEITGALLPCLD-ESRFENLGVSSLGERKKLLSYIQRLVQ 109
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQ--YADNFRKNGIDGALLLLLTsEEDLKELGITKLGHRKKILKAIQKLKE 67
HD pfam01966
HD domain; HD domains are metal dependent phosphohydrolases.
 164-266 2.27e-09

HD domain; HD domains are metal dependent phosphohydrolases.


Pssm-ID: 460398 [Multi-domain]  Cd Length: 110  Bit Score: 55.32  E-value: 2.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38016914   164 RFEHSLGVGYLAGCLVHALGEKqpelqiserDVLCVQIAGLCHDLGHGPFS-----------HMFDGRFIPLARPEVKWt 232
Cdd:pfam01966   1 RLEHSLRVALLARELAEELGEL---------DRELLLLAALLHDIGKGPFGdekpefeiflgHAVVGAEILRELEKRLG- 70

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 38016914   233 heqgsVMMFEHLINSNGIKPVMEQYGL-IPEEDIC 266
Cdd:pfam01966  71 -----LEDVLKLILEHHESWEGAGYPEeISLEARI 100
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 44-107 9.63e-09

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: 51.89  E-value: 9.63e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 38016914    44 TWGPEQVCSFLRRGGFEEpvLLKNIRENEITGALLPCLDESRFENLGVSSLGERKKLLSYIQRL 107
Cdd:pfam00536   2 GWSVEDVGEWLESIGLGQ--YIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRL 63
PRK01096 PRK01096
deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional
 134-215 7.61e-05

deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional


Pssm-ID: 234897 [Multi-domain]  Cd Length: 440  Bit Score: 45.68  E-value: 7.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38016914  134 RIIDTPQFQRLRYIKQlgggyyVFPGAS----HNRFEHSLGV-------GYLAGclvHALGEKQPELQISERDV-LCVQI 201
Cdd:PRK01096  34 RIIFSGSFRRLQRKTQ------VHPLAKndhiHTRLTHSLEVscvgrslGMRVG---ETLKEEKLPDWISPADIgAIVQS 104

                         90
                 ....*....|....
gi 38016914  202 AGLCHDLGHGPFSH 215
Cdd:PRK01096 105 ACLAHDIGNPPFGH 118
 
Name Accession Description Interval E-value
YdhJ COG1078
HD superfamily phosphohydrolase [General function prediction only];
115-472 2.44e-77

HD superfamily phosphohydrolase [General function prediction only];


Pssm-ID: 440696 [Multi-domain]  Cd Length: 340  Bit Score: 249.33  E-value: 2.44e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38016914 115 MKVINDPIHGHIELHPLLVRIIDTPQFQRLRYIKQLGGGYYVFPGASHNRFEHSLGVGYLAGCLVHALGEKQPElqISER 194
Cdd:COG1078   1 MKIIRDPVHGYIEVDELELDLIDTPEFQRLRRIKQLGLAYLVYPGAEHTRFEHSLGVMHLARRALDRLRRKGVE--IDEE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38016914 195 DVLCVQIAGLCHDLGHGPFSHMFDGRFiplarpEVKWTHEQGSVMmfehLINSNGIKPVMEQYGLIPEEDICFIkeqivg 274
Cdd:COG1078  79 ERELVRAAALLHDIGHGPFSHAFEEVL------LTGVDHEEITLR----IIEENEINGILEKHGIDPELVADII------ 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38016914 275 plespvedslwpyKGRPENKsFLYEIVSnkrNGIDVDKWDYFARDCHHLGIQN-NFDYKRFIKFARVceVDNELRIcaRD 353
Cdd:COG1078 143 -------------KGEYPNK-FLRQLIS---SQLDADRMDYLLRDSYYTGVSYgNIDLERLIRMLRV--VDDELVV--EE 201

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38016914 354 KEVGNLYDMFHTRNSLHRRAYQHKVGNIIDTMITDAFLKAddyIEITGAGGKKYRIstaidDMEAYTKLTDNIFLEIL-- 431
Cdd:COG1078 202 KGIYAVESFLIARYLMYWQVYFHKTSRAAEVMLRRALERA---KELYDEGELENPL-----DLEDFLRLDDYDLLSALke 273

                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 38016914 432 --YSTDPKLKDareILKQIEYRNLFKYVgetqptgqIKIKRED 472
Cdd:COG1078 274 wqDHPDPILSD---LARRLLNRKLFKRV--------ILIVDKN 305
SAM_HD cd09508
SAM domain of HD-phosphohydrolase; SAM (sterile alpha motif) domain of SAM_HD subfamily ...
 41-110 8.09e-33

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: 120.50  E-value: 8.09e-33
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38016914  41 DYKTWGPEQVCSFLRRGGFEEPVLLKNIRENEITGALLPCLDESRFENLGVSSLGERKKLLSYIQRLVQI 110
Cdd:cd09508   1 DFRSWDPEDVCQFLRGNGFGEPELLEIFRENEITGAHLPDLTESRLEKLGVSSLGERLKLLKCLQKLSQI 70
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
 162-335 1.46e-14

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 71.22  E-value: 1.46e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38016914 162 HNRFEHSLGVGYLAgclvHALGEKqpeLQISERDVLCVQIAGLCHDLGHGPFSHMFdgrfiplarpevkwtHEQGSVMMF 241
Cdd:cd00077   1 EHRFEHSLRVAQLA----RRLAEE---LGLSEEDIELLRLAALLHDIGKPGTPDAI---------------TEEESELEK 58

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38016914 242 EHLINSNGIKpvmeqYGLIPEEDICFIKEqIVGPLESPVEDSLWPYKGRPENKSflYEIVSNKRNGIDVDKWDYFARDCH 321
Cdd:cd00077  59 DHAIVGAEIL-----RELLLEEVIKLIDE-LILAVDASHHERLDGLGYPDGLKG--EEITLEARIVKLADRLDALRRDSR 130

                       170
                ....*....|....*
gi 38016914 322 HLGIQ-NNFDYKRFI 335
Cdd:cd00077 131 EKRRRiAEEDLEELL 145
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
 160-245 9.65e-12

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: 62.31  E-value: 9.65e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38016914    160 ASHNRFEHSLGVGYLAGCLVHALGEKqpelqiserDVLCVQIAGLCHDLGHGPFSHMFDGRFIPLarpevkWTHEQGSVM 239
Cdd:smart00471   1 SDYHVFEHSLRVAQLAAALAEELGLL---------DIELLLLAALLHDIGKPGTPDSFLVKTSVL------EDHHFIGAE 65


                   ....*.
gi 38016914    240 MFEHLI 245
Cdd:smart00471  66 ILLEEE 71
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 42-109 2.86e-11

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: 59.23  E-value: 2.86e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38016914     42 YKTWGPEQVCSFLRRGGFEEpvLLKNIRENEITGALLPCLD-ESRFENLGVSSLGERKKLLSYIQRLVQ 109
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQ--YADNFRKNGIDGALLLLLTsEEDLKELGITKLGHRKKILKAIQKLKE 67
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 49-106 1.75e-10

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: 56.48  E-value: 1.75e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 38016914  49 QVCSFLRRGGFEEpvLLKNIRENEITGALLPCLDESRFENLGVSSLGERKKLLSYIQR 106
Cdd:cd09487   1 DVAEWLESLGLEQ--YADLFRKNEIDGDALLLLTDEDLKELGITSPGHRKKILRAIQR 56
HD pfam01966
HD domain; HD domains are metal dependent phosphohydrolases.
 164-266 2.27e-09

HD domain; HD domains are metal dependent phosphohydrolases.


Pssm-ID: 460398 [Multi-domain]  Cd Length: 110  Bit Score: 55.32  E-value: 2.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38016914   164 RFEHSLGVGYLAGCLVHALGEKqpelqiserDVLCVQIAGLCHDLGHGPFS-----------HMFDGRFIPLARPEVKWt 232
Cdd:pfam01966   1 RLEHSLRVALLARELAEELGEL---------DRELLLLAALLHDIGKGPFGdekpefeiflgHAVVGAEILRELEKRLG- 70

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 38016914   233 heqgsVMMFEHLINSNGIKPVMEQYGL-IPEEDIC 266
Cdd:pfam01966  71 -----LEDVLKLILEHHESWEGAGYPEeISLEARI 100
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 44-107 9.63e-09

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: 51.89  E-value: 9.63e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 38016914    44 TWGPEQVCSFLRRGGFEEpvLLKNIRENEITGALLPCLDESRFENLGVSSLGERKKLLSYIQRL 107
Cdd:pfam00536   2 GWSVEDVGEWLESIGLGQ--YIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRL 63
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
 44-107 2.74e-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: 2.74e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38016914  44 TWGPEQVCSFLRRGGFEEpvLLKNIRENEITGALLPCL-DESRFENLGVSSLGERKKLLSYIQRL 107
Cdd:cd09505   4 DWSEEDVCTWLRSIGLEQ--YVEVFRANNIDGKELLNLtKESLSKDLKIESLGHRNKILRKIEEL 66
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
42-108 5.25e-08

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 49.96  E-value: 5.25e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 38016914    42 YKTWGPEQVCSFLRRGGFEEpvLLKNIRENEITGA-LLPCLDESRFENLGVSSLGERKKLLSYIQRLV 108
Cdd:pfam07647   1 VESWSLESVADWLRSIGLEQ--YTDNFRDQGITGAeLLLRLTLEDLKRLGITSVGHRRKILKKIQELK 66
SAM_BOI-like_fungal cd09535
SAM domain of BOI-like fungal subfamily; SAM (sterile alpha motif) domain of BOI-like fungal ...
 43-107 1.18e-07

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: 49.09  E-value: 1.18e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38016914  43 KTWGPEQVCSFLRRGGFEEPVLLKnIRENEITGALLPCLDESRFENLGVSSLGERKKLLSYIQRL 107
Cdd:cd09535   1 RSWSPEQVAEWLLSAGFDDSVCEK-FRENEITGDILLELDLEDLKELDIGSFGKRFKLWNEIKSL 64
SAM_Ste11_fungal cd09534
SAM domain of Ste11_fungal subfamily; SAM (sterile alpha motif) domain of Ste11 subfamily is a ...
 45-107 4.94e-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: 47.20  E-value: 4.94e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38016914  45 WGPEQVCSFLRRGGFEEpvLLKNIRENEITGALLPCLDESRFENLGVSSLGERKKLLSYIQRL 107
Cdd:cd09534   1 WDEEFVEEWLNELNCGQ--YLDIFEKNLITGDLLLELDKEALKELGITKVGDRIRLLRAIKSL 61
SAM_Samd3 cd09526
SAM domain of Samd3 subfamily; SAM (sterile alpha motif) domain of the Samd3 subfamily is a ...
 43-109 7.07e-05

SAM domain of Samd3 subfamily; SAM (sterile alpha motif) domain of the Samd3 subfamily is a putative protein-protein interaction domain. Proteins of this subfamily have a SAM domain at the N-terminus. SAM is a widespread domain in signaling and regulatory proteins. In many cases SAM mediates dimerization/oligomerization. Exact function of proteins belonging to this subfamily is unknown.


Pssm-ID: 188925  Cd Length: 66  Bit Score: 41.19  E-value: 7.07e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38016914  43 KTWGPEQVCSFLRRGGFEEpvLLKNIRENEITGALLPCLDESRFENLgVSSLGERKKLLSYIQRLVQ 109
Cdd:cd09526   2 ETWSVEQVCNWLVEKNLGE--LVPRFQEEEVSGAALLALNDRMVQQL-VKKIGHQAVLMDLIKKYKQ 65
PRK01096 PRK01096
deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional
 134-215 7.61e-05

deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional


Pssm-ID: 234897 [Multi-domain]  Cd Length: 440  Bit Score: 45.68  E-value: 7.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38016914  134 RIIDTPQFQRLRYIKQlgggyyVFPGAS----HNRFEHSLGV-------GYLAGclvHALGEKQPELQISERDV-LCVQI 201
Cdd:PRK01096  34 RIIFSGSFRRLQRKTQ------VHPLAKndhiHTRLTHSLEVscvgrslGMRVG---ETLKEEKLPDWISPADIgAIVQS 104

                         90
                 ....*....|....
gi 38016914  202 AGLCHDLGHGPFSH 215
Cdd:PRK01096 105 ACLAHDIGNPPFGH 118
SAM_CNK1,2,3-suppressor cd09511
SAM domain of CNK1,2,3-suppressor subfamily; SAM (sterile alpha motif) domain of CNK ...
 44-107 1.45e-04

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: 40.35  E-value: 1.45e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 38016914  44 TWGPEQVCSFLRrgGFEEPVL--LKNIRENEITGALLPCLDESRFENLGVSSLGERKKLLSYIQRL 107
Cdd:cd09511   3 KWSPKQVTDWLK--GLDDCLQqyIYTFEREKVTGEQLLNLSPQDLENLGVTKIGHQELILEAVELL 66
PRK03007 PRK03007
deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional
 163-215 2.85e-03

deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional


Pssm-ID: 235098 [Multi-domain]  Cd Length: 428  Bit Score: 40.32  E-value: 2.85e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 38016914  163 NRFEHSLGVGYLAGCLVHALGeKQPELqiserdvlcVQIAGLCHDLGHGPFSH 215
Cdd:PRK03007  70 TRLTHSLEVAQIGRGIAAGLG-CDPDL---------VDLAGLAHDIGHPPYGH 112
SAM_DGK-delta-eta cd09507
SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain ...
 45-107 3.71e-03

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: 36.24  E-value: 3.71e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38016914  45 WGPEQVCSFLRRGGFEEPVllKNIRENEITGALLPCLDESRFENLGVSSLGERKKLLSYIQRL 107
Cdd:cd09507   5 WTTEEVGAWLESLQLGEYR--DIFARNDIRGSELLHLERRDLKDLGITKVGHVKRILQAIKDL 65
SAM_Shank1,2,3 cd09506
SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 ...
 69-107 3.86e-03

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: 36.14  E-value: 3.86e-03
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 38016914  69 RENEITGALLPCLDESRFENLGVSSLGERKKLLSYIQRL 107
Cdd:cd09506  27 MDNEIDGSHLPNLDKEDLTELGVTRVGHRMNIERALKKL 65
HD_assoc_2 pfam19276
HD associated region; This entry represents a region that forms part of a larger HD domain. ...
 374-491 4.21e-03

HD associated region; This entry represents a region that forms part of a larger HD domain.According to the original paper describing the HD domain this family represents cluster 1.


Pssm-ID: 466023  Cd Length: 222  Bit Score: 39.01  E-value: 4.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38016914   374 YQHKVGNIIDTMitdaFLKADDYIeitgaggkkyrISTAIDDMEAYTKLTDNIFLEILYSTDPklkDAREILKQIEYRNL 453
Cdd:pfam19276  42 YQHHVARIAKAM----LRRALERL-----------IEEGDLDAEELRRMDDADLLVALRNSEG---YTAEIARRLDERDL 103

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 38016914   454 FK---YVGETQ-PTGQIKIKREDYESLPKEVASA----KPKVLLDV 491
Cdd:pfam19276 104 YKravYAELDDvPDDVLDADHEEIRRAEREIAERagvdPEYVIVDI 149
SAM_Ste50-like_fungal cd09533
SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or ...
 49-107 4.57e-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: 35.75  E-value: 4.57e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 38016914  49 QVCSFLRRGGFEEpvLLKNIRENEITGALLPCLDESRFENLGVSSLGERKKLLSYIQRL 107
Cdd:cd09533   1 DVADWLSSLGLPQ--YEDQFIENGITGDVLVALDHEDLKEMGITSVGHRLTILKAVYEL 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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