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Conserved domains on  [gi|1958497378|ref|WP_201345023|]
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class I SAM-dependent DNA methyltransferase [Thiohalobacter sp. COW1]

Protein Classification

type I restriction-modification system subunit M( domain architecture ID 12114514)

type I restriction-modification system modification (M) subunit (HsdM), together with specificity (S) subunit (HsdS), forms a methyltransferase that methylates two adenine residues in complementary strands of a bipartite DNA recognition sequence

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HsdM COG0286
Type I restriction-modification system, DNA methylase subunit [Defense mechanisms];
174-448 5.12e-85

Type I restriction-modification system, DNA methylase subunit [Defense mechanisms];


:

Pssm-ID: 440055 [Multi-domain]  Cd Length: 243  Bit Score: 268.21  E-value: 5.12e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958497378 174 MGTIFEELIRRFNEENNEEAGEHFTPRDVVKLMADLIFlPVADDIesgtylVYDGACGTGGMLTVAEERLAELAQSHDKD 253
Cdd:COG0286     3 LGDAYEYLLRKFAEESGKKAGEFYTPREVVRLMVELLD-PKPGET------VYDPACGSGGFLVEAAEYLKEHGGDERKK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958497378 254 vsIHLFGQEVQPETYAISKADLLLKGegAEAENMKYGSTLSSDAFPSQEFDFMLSNPPYGKSWKTDLERlggkgDIKDPR 333
Cdd:COG0286    76 --LSLYGQEINPTTYRLAKMNLLLHG--IGDPNIELGDTLSNDGDELEKFDVVLANPPFGGKWKKEELK-----DDLLGR 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958497378 334 FVTQhggdpeykmITRSSDGQLMFLVNKLSKMKHttrlGSRIAEVHNGSSLFTGdagqGESNIRRWIIENDWLEAIIALP 413
Cdd:COG0286   147 FGYG---------LPPKSNADLLFLQHILSLLKP----GGRAAVVLPDGVLFRG----AEKEIRKKLLENDLLEAIIGLP 209
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1958497378 414 DNMFYNTGIATYIWMLTNRKSeERKGKVQLIDATE 448
Cdd:COG0286   210 SNLFYNTGIPTCILFLTKGKP-ERTGKVLFIDASK 243
HsdM_N pfam12161
HsdM N-terminal domain; This domain is found at the N-terminus of the methylase subunit of ...
9-145 4.18e-22

HsdM N-terminal domain; This domain is found at the N-terminus of the methylase subunit of Type I DNA methyltransferases. This domain family is found in bacteria and archaea, and is typically between 123 and 138 amino acids in length. The family is found in association with pfam02384. Mutations in this region of EcoKI methyltransferase abolish the normally strong preference of this system for methylating hemimethylated substrate. The structure of this domain has been shown to be all alpha-helical.


:

Pssm-ID: 463478  Cd Length: 123  Bit Score: 91.98  E-value: 4.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958497378   9 IVNFIWGIADdVLRDVYVRGKYRDVILPMTVIRRLDALLEPSKEKVLgmkkqldgagianqHAALCQASGEAFYNVSPFT 88
Cdd:pfam12161   1 LESFLWNAAD-ILRGDVDASEYKEYILPLLFLKRLDDVLEEREEEVL--------------ELIEPLDSGFGFYIPSELR 65
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958497378  89 LRDLKNRAKQQQLKADFEAYLDGFS---PNVQEILDKfKFRNQIpTLIEADILGHLIEKF 145
Cdd:pfam12161  66 WSKLANNLDNDELGENLNDAFPGLEelnPDLRGVFMK-DARGII-TLKSPDLLKKVIQKF 123
 
Name Accession Description Interval E-value
HsdM COG0286
Type I restriction-modification system, DNA methylase subunit [Defense mechanisms];
174-448 5.12e-85

Type I restriction-modification system, DNA methylase subunit [Defense mechanisms];


Pssm-ID: 440055 [Multi-domain]  Cd Length: 243  Bit Score: 268.21  E-value: 5.12e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958497378 174 MGTIFEELIRRFNEENNEEAGEHFTPRDVVKLMADLIFlPVADDIesgtylVYDGACGTGGMLTVAEERLAELAQSHDKD 253
Cdd:COG0286     3 LGDAYEYLLRKFAEESGKKAGEFYTPREVVRLMVELLD-PKPGET------VYDPACGSGGFLVEAAEYLKEHGGDERKK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958497378 254 vsIHLFGQEVQPETYAISKADLLLKGegAEAENMKYGSTLSSDAFPSQEFDFMLSNPPYGKSWKTDLERlggkgDIKDPR 333
Cdd:COG0286    76 --LSLYGQEINPTTYRLAKMNLLLHG--IGDPNIELGDTLSNDGDELEKFDVVLANPPFGGKWKKEELK-----DDLLGR 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958497378 334 FVTQhggdpeykmITRSSDGQLMFLVNKLSKMKHttrlGSRIAEVHNGSSLFTGdagqGESNIRRWIIENDWLEAIIALP 413
Cdd:COG0286   147 FGYG---------LPPKSNADLLFLQHILSLLKP----GGRAAVVLPDGVLFRG----AEKEIRKKLLENDLLEAIIGLP 209
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1958497378 414 DNMFYNTGIATYIWMLTNRKSeERKGKVQLIDATE 448
Cdd:COG0286   210 SNLFYNTGIPTCILFLTKGKP-ERTGKVLFIDASK 243
N6_Mtase pfam02384
N-6 DNA Methylase; Restriction-modification (R-M) systems protect a bacterial cell against ...
170-474 7.01e-49

N-6 DNA Methylase; Restriction-modification (R-M) systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The R-M system is a complex containing three polypeptides: M (this family), S (pfam01420), and R. This family consists of N-6 adenine-specific DNA methylase EC:2.1.1.72 from Type I and Type IC restriction systems. These methylases have the same sequence specificity as their corresponding restriction enzymes.


Pssm-ID: 426749 [Multi-domain]  Cd Length: 310  Bit Score: 174.05  E-value: 7.01e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958497378 170 DNHSMGTIFEELIRRFNEENNEEAGEHFTPRDVVKLMADLIflpvadDIESGTyLVYDGACGTGGMLTVAEERLAELaQS 249
Cdd:pfam02384   1 SRDLFGDAYEYLLRKFAPNAGKSGGEFFTPREVSKLIVELL------DPKPGE-SIYDPACGSGGFLIQAEKFVKEH-DG 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958497378 250 HDKDVSIhlFGQEVQPETYAISKADLLLKGEGAEAENMKYGSTLSSDAFPSQE-FDFMLSNPPYGKSWKtdlerlGGKGD 328
Cdd:pfam02384  73 DTNDLSI--YGQEKNPTTYRLARMNMILHGIEYDDFHIRHGDTLTSPKFEDDKkFDVVVANPPFSDKWD------ANDTL 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958497378 329 IKDPRFVTQHGGDPEykmitrsSDGQLMFLVNKLSKMKHttrlGSRIAEVHNGSSLFTGDAgqgESNIRRWIIENDWLEA 408
Cdd:pfam02384 145 ENDPRFRPAYGVAPK-------SNADLAFLQHIIYYLAP----GGRAAVVLPNGVLFRGGA---EGKIRKALVDKDLVET 210
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958497378 409 IIALPDNMFYNTGIATYIWMLTNRKSeERKGKVQLIDATEWYVplrrnLGKKNCEYSEEHIRAICD 474
Cdd:pfam02384 211 VIALPPNLFYNTSIPTCILFLTKNKA-ERKGKVLFIDASNEFK-----KEGKLNILTDEHIEKIID 270
hsdM TIGR00497
type I restriction system adenine methylase (hsdM); Function: methylation of specific adenine ...
149-474 7.69e-24

type I restriction system adenine methylase (hsdM); Function: methylation of specific adenine residues; required for both restriction and modification activities. The ECOR124/3 I enzyme recognizes 5'GAA(N7)RTCG. for E.coli see (J. Mol. Biol. 257: 960-969 (1996)). [DNA metabolism, Restriction/modification]


Pssm-ID: 211578 [Multi-domain]  Cd Length: 501  Bit Score: 105.81  E-value: 7.69e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958497378 149 RVNLSPKPVQDVDGNEILPALDN--HSMGTIFEELIRRFNEENNEEAGEHFTPRDVVKLMADlIFLPVADDIESgtylVY 226
Cdd:TIGR00497 148 RTEKLKELLTSIDTMELDEFEKNsiDAFGDAYEFLISMYAQNAGKSGGEFFTPQDISELLAR-IAIGKKDTVDD----VY 222
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958497378 227 DGACGTGGMLTVAEERLAelaqshDKDVSIHLFGQEVQPETYAISKADLLLKGEGAEAENMKYGSTLSSDAFPSQE-FDF 305
Cdd:TIGR00497 223 DMACGSGSLLLQVIKVLG------EKTSLVSYYGQEINHTTYNLCRMNMILHNIDYANFNIINADTLTTKEWENENgFEV 296
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958497378 306 MLSNPPYGKSWKTDLERLggkgDIKDPRFvtqhggdPEYKMITRSSDGQLMFLVNKLSKMKHTtrlgSRIAEVHNGSSLF 385
Cdd:TIGR00497 297 VVSNPPYSISWAGDKKSN----LVSDVRF-------KDAGTLAPNSKADLAFVLHALYVLGQE----GTAAIVCFPGILY 361
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958497378 386 TGDAgqgESNIRRWIIENDWLEAIIALPDNMFYNTGIATYIWMLtnrKSEERKGKVQLIDATEWYVPlrrnlGKKNCEYS 465
Cdd:TIGR00497 362 REGK---EQTIRKYLVDQNFVDAVIQLPSNLFSTTSIATSILVL---KKNRKKDPIFFIDGSNEFVR-----EKKNNRLS 430

                  ....*....
gi 1958497378 466 EEHIRAICD 474
Cdd:TIGR00497 431 PKNIEKIVD 439
HsdM_N pfam12161
HsdM N-terminal domain; This domain is found at the N-terminus of the methylase subunit of ...
9-145 4.18e-22

HsdM N-terminal domain; This domain is found at the N-terminus of the methylase subunit of Type I DNA methyltransferases. This domain family is found in bacteria and archaea, and is typically between 123 and 138 amino acids in length. The family is found in association with pfam02384. Mutations in this region of EcoKI methyltransferase abolish the normally strong preference of this system for methylating hemimethylated substrate. The structure of this domain has been shown to be all alpha-helical.


Pssm-ID: 463478  Cd Length: 123  Bit Score: 91.98  E-value: 4.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958497378   9 IVNFIWGIADdVLRDVYVRGKYRDVILPMTVIRRLDALLEPSKEKVLgmkkqldgagianqHAALCQASGEAFYNVSPFT 88
Cdd:pfam12161   1 LESFLWNAAD-ILRGDVDASEYKEYILPLLFLKRLDDVLEEREEEVL--------------ELIEPLDSGFGFYIPSELR 65
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958497378  89 LRDLKNRAKQQQLKADFEAYLDGFS---PNVQEILDKfKFRNQIpTLIEADILGHLIEKF 145
Cdd:pfam12161  66 WSKLANNLDNDELGENLNDAFPGLEelnPDLRGVFMK-DARGII-TLKSPDLLKKVIQKF 123
 
Name Accession Description Interval E-value
HsdM COG0286
Type I restriction-modification system, DNA methylase subunit [Defense mechanisms];
174-448 5.12e-85

Type I restriction-modification system, DNA methylase subunit [Defense mechanisms];


Pssm-ID: 440055 [Multi-domain]  Cd Length: 243  Bit Score: 268.21  E-value: 5.12e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958497378 174 MGTIFEELIRRFNEENNEEAGEHFTPRDVVKLMADLIFlPVADDIesgtylVYDGACGTGGMLTVAEERLAELAQSHDKD 253
Cdd:COG0286     3 LGDAYEYLLRKFAEESGKKAGEFYTPREVVRLMVELLD-PKPGET------VYDPACGSGGFLVEAAEYLKEHGGDERKK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958497378 254 vsIHLFGQEVQPETYAISKADLLLKGegAEAENMKYGSTLSSDAFPSQEFDFMLSNPPYGKSWKTDLERlggkgDIKDPR 333
Cdd:COG0286    76 --LSLYGQEINPTTYRLAKMNLLLHG--IGDPNIELGDTLSNDGDELEKFDVVLANPPFGGKWKKEELK-----DDLLGR 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958497378 334 FVTQhggdpeykmITRSSDGQLMFLVNKLSKMKHttrlGSRIAEVHNGSSLFTGdagqGESNIRRWIIENDWLEAIIALP 413
Cdd:COG0286   147 FGYG---------LPPKSNADLLFLQHILSLLKP----GGRAAVVLPDGVLFRG----AEKEIRKKLLENDLLEAIIGLP 209
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1958497378 414 DNMFYNTGIATYIWMLTNRKSeERKGKVQLIDATE 448
Cdd:COG0286   210 SNLFYNTGIPTCILFLTKGKP-ERTGKVLFIDASK 243
N6_Mtase pfam02384
N-6 DNA Methylase; Restriction-modification (R-M) systems protect a bacterial cell against ...
170-474 7.01e-49

N-6 DNA Methylase; Restriction-modification (R-M) systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The R-M system is a complex containing three polypeptides: M (this family), S (pfam01420), and R. This family consists of N-6 adenine-specific DNA methylase EC:2.1.1.72 from Type I and Type IC restriction systems. These methylases have the same sequence specificity as their corresponding restriction enzymes.


Pssm-ID: 426749 [Multi-domain]  Cd Length: 310  Bit Score: 174.05  E-value: 7.01e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958497378 170 DNHSMGTIFEELIRRFNEENNEEAGEHFTPRDVVKLMADLIflpvadDIESGTyLVYDGACGTGGMLTVAEERLAELaQS 249
Cdd:pfam02384   1 SRDLFGDAYEYLLRKFAPNAGKSGGEFFTPREVSKLIVELL------DPKPGE-SIYDPACGSGGFLIQAEKFVKEH-DG 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958497378 250 HDKDVSIhlFGQEVQPETYAISKADLLLKGEGAEAENMKYGSTLSSDAFPSQE-FDFMLSNPPYGKSWKtdlerlGGKGD 328
Cdd:pfam02384  73 DTNDLSI--YGQEKNPTTYRLARMNMILHGIEYDDFHIRHGDTLTSPKFEDDKkFDVVVANPPFSDKWD------ANDTL 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958497378 329 IKDPRFVTQHGGDPEykmitrsSDGQLMFLVNKLSKMKHttrlGSRIAEVHNGSSLFTGDAgqgESNIRRWIIENDWLEA 408
Cdd:pfam02384 145 ENDPRFRPAYGVAPK-------SNADLAFLQHIIYYLAP----GGRAAVVLPNGVLFRGGA---EGKIRKALVDKDLVET 210
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958497378 409 IIALPDNMFYNTGIATYIWMLTNRKSeERKGKVQLIDATEWYVplrrnLGKKNCEYSEEHIRAICD 474
Cdd:pfam02384 211 VIALPPNLFYNTSIPTCILFLTKNKA-ERKGKVLFIDASNEFK-----KEGKLNILTDEHIEKIID 270
hsdM TIGR00497
type I restriction system adenine methylase (hsdM); Function: methylation of specific adenine ...
149-474 7.69e-24

type I restriction system adenine methylase (hsdM); Function: methylation of specific adenine residues; required for both restriction and modification activities. The ECOR124/3 I enzyme recognizes 5'GAA(N7)RTCG. for E.coli see (J. Mol. Biol. 257: 960-969 (1996)). [DNA metabolism, Restriction/modification]


Pssm-ID: 211578 [Multi-domain]  Cd Length: 501  Bit Score: 105.81  E-value: 7.69e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958497378 149 RVNLSPKPVQDVDGNEILPALDN--HSMGTIFEELIRRFNEENNEEAGEHFTPRDVVKLMADlIFLPVADDIESgtylVY 226
Cdd:TIGR00497 148 RTEKLKELLTSIDTMELDEFEKNsiDAFGDAYEFLISMYAQNAGKSGGEFFTPQDISELLAR-IAIGKKDTVDD----VY 222
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958497378 227 DGACGTGGMLTVAEERLAelaqshDKDVSIHLFGQEVQPETYAISKADLLLKGEGAEAENMKYGSTLSSDAFPSQE-FDF 305
Cdd:TIGR00497 223 DMACGSGSLLLQVIKVLG------EKTSLVSYYGQEINHTTYNLCRMNMILHNIDYANFNIINADTLTTKEWENENgFEV 296
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958497378 306 MLSNPPYGKSWKTDLERLggkgDIKDPRFvtqhggdPEYKMITRSSDGQLMFLVNKLSKMKHTtrlgSRIAEVHNGSSLF 385
Cdd:TIGR00497 297 VVSNPPYSISWAGDKKSN----LVSDVRF-------KDAGTLAPNSKADLAFVLHALYVLGQE----GTAAIVCFPGILY 361
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958497378 386 TGDAgqgESNIRRWIIENDWLEAIIALPDNMFYNTGIATYIWMLtnrKSEERKGKVQLIDATEWYVPlrrnlGKKNCEYS 465
Cdd:TIGR00497 362 REGK---EQTIRKYLVDQNFVDAVIQLPSNLFSTTSIATSILVL---KKNRKKDPIFFIDGSNEFVR-----EKKNNRLS 430

                  ....*....
gi 1958497378 466 EEHIRAICD 474
Cdd:TIGR00497 431 PKNIEKIVD 439
HsdM_N pfam12161
HsdM N-terminal domain; This domain is found at the N-terminus of the methylase subunit of ...
9-145 4.18e-22

HsdM N-terminal domain; This domain is found at the N-terminus of the methylase subunit of Type I DNA methyltransferases. This domain family is found in bacteria and archaea, and is typically between 123 and 138 amino acids in length. The family is found in association with pfam02384. Mutations in this region of EcoKI methyltransferase abolish the normally strong preference of this system for methylating hemimethylated substrate. The structure of this domain has been shown to be all alpha-helical.


Pssm-ID: 463478  Cd Length: 123  Bit Score: 91.98  E-value: 4.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958497378   9 IVNFIWGIADdVLRDVYVRGKYRDVILPMTVIRRLDALLEPSKEKVLgmkkqldgagianqHAALCQASGEAFYNVSPFT 88
Cdd:pfam12161   1 LESFLWNAAD-ILRGDVDASEYKEYILPLLFLKRLDDVLEEREEEVL--------------ELIEPLDSGFGFYIPSELR 65
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958497378  89 LRDLKNRAKQQQLKADFEAYLDGFS---PNVQEILDKfKFRNQIpTLIEADILGHLIEKF 145
Cdd:pfam12161  66 WSKLANNLDNDELGENLNDAFPGLEelnPDLRGVFMK-DARGII-TLKSPDLLKKVIQKF 123
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
224-323 4.14e-03

tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 N-methylase Trm11 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440663 [Multi-domain]  Cd Length: 172  Bit Score: 38.78  E-value: 4.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958497378 224 LVYDGACGTGGMLTVAEErlaelaqshdkdVSIHLFGQEVQPETYAISKADLllkgegaEAENMKYGSTLSSDA----FP 299
Cdd:COG1041    29 TVLDPFCGTGTILIEAGL------------LGRRVIGSDIDPKMVEGARENL-------EHYGYEDADVIRGDArdlpLA 89
                          90       100
                  ....*....|....*....|....
gi 1958497378 300 SQEFDFMLSNPPYGKSWKTDLERL 323
Cdd:COG1041    90 DESVDAIVTDPPYGRSSKISGEEL 113
 
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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