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Conserved domains on  [gi|491959767|ref|WP_005692718|]
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type I restriction-modification system subunit M [Lacticaseibacillus rhamnosus]

Protein Classification

type I restriction-modification system subunit M( domain architecture ID 12114586)

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
N6_Mtase pfam02384
N-6 DNA Methylase; Restriction-modification (R-M) systems protect a bacterial cell against ...
180-496 5.47e-130

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: 381.67  E-value: 5.47e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491959767  180 GRDILGDVYEYLIAQFAGNSGKKAGEFYTPHQVSKVLAKLValgvqKDQEIFTVYDPTMGSGSLLLTVRDELPAT---VK 256
Cdd:pfam02384   1 SRDLFGDAYEYLLRKFAPNAGKSGGEFFTPREVSKLIVELL-----DPKPGESIYDPACGSGGFLIQAEKFVKEHdgdTN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491959767  257 AVMFHGQELNTTTFNLARMNLMMHNVPYTNMSLRNADTLEDDWPDGvvggvdsPRSFDAVVANPPYSIHWDNSENKLKDP 336
Cdd:pfam02384  76 DLSIYGQEKNPTTYRLARMNMILHGIEYDDFHIRHGDTLTSPKFED-------DKKFDVVVANPPFSDKWDANDTLENDP 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491959767  337 RFKPFGALAPKSKADFAFVEHGLYHLNDTGTMAIVLPHGVLFRGAAEGKIRKAIIEKNYLDAVIGMPAGLFFSTGIPTVV 416
Cdd:pfam02384 149 RFRPAYGVAPKSNADLAFLQHIIYYLAPGGRAAVVLPNGVLFRGGAEGKIRKALVDKDLVETVIALPPNLFYNTSIPTCI 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491959767  417 LVFKKNRTNR--DIFFIDASNNFEKGKNQNILRDSDIDKIIEAYSKREDVDKYAHKAELDEIVENEYNLNIPRYVDTTEP 494
Cdd:pfam02384 229 LFLTKNKAERkgKVLFIDASNEFKKEGKLNILTDEHIEKIIDTFGEFKDVDGFSKSATLEEIAANDYNLNVGRYVGTEEE 308

                  ..
gi 491959767  495 EK 496
Cdd:pfam02384 309 EE 310
HsdM_N pfam12161
HsdM N-terminal domain; This domain is found at the N-terminus of the methylase subunit of ...
10-170 2.08e-16

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: 75.41  E-value: 2.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491959767   10 ITSQLWAMANELRGNMDASEFRNYILGFMFYRYLSEHQERYLQETnlfepeagqtwndafrevasdpesrKEYLEDISSE 89
Cdd:pfam12161   1 LESFLWNAADILRGDVDASEYKEYILPLLFLKRLDDVLEEREEEV-------------------------LELIEPLDSG 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491959767   90 LGYAIAPEQTWASLVQkVNDDKIVPSDYQDLFDDFnknAALNPnseaDFRGIF-ADINLGDsrlgssTTARAKALNGVVR 168
Cdd:pfam12161  56 FGFYIPSELRWSKLAN-NLDNDELGENLNDAFPGL---EELNP----DLRGVFmKDARGII------TLKSPDLLKKVIQ 121

                  ..
gi 491959767  169 LV 170
Cdd:pfam12161 122 KF 123
 
Name Accession Description Interval E-value
N6_Mtase pfam02384
N-6 DNA Methylase; Restriction-modification (R-M) systems protect a bacterial cell against ...
180-496 5.47e-130

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: 381.67  E-value: 5.47e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491959767  180 GRDILGDVYEYLIAQFAGNSGKKAGEFYTPHQVSKVLAKLValgvqKDQEIFTVYDPTMGSGSLLLTVRDELPAT---VK 256
Cdd:pfam02384   1 SRDLFGDAYEYLLRKFAPNAGKSGGEFFTPREVSKLIVELL-----DPKPGESIYDPACGSGGFLIQAEKFVKEHdgdTN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491959767  257 AVMFHGQELNTTTFNLARMNLMMHNVPYTNMSLRNADTLEDDWPDGvvggvdsPRSFDAVVANPPYSIHWDNSENKLKDP 336
Cdd:pfam02384  76 DLSIYGQEKNPTTYRLARMNMILHGIEYDDFHIRHGDTLTSPKFED-------DKKFDVVVANPPFSDKWDANDTLENDP 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491959767  337 RFKPFGALAPKSKADFAFVEHGLYHLNDTGTMAIVLPHGVLFRGAAEGKIRKAIIEKNYLDAVIGMPAGLFFSTGIPTVV 416
Cdd:pfam02384 149 RFRPAYGVAPKSNADLAFLQHIIYYLAPGGRAAVVLPNGVLFRGGAEGKIRKALVDKDLVETVIALPPNLFYNTSIPTCI 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491959767  417 LVFKKNRTNR--DIFFIDASNNFEKGKNQNILRDSDIDKIIEAYSKREDVDKYAHKAELDEIVENEYNLNIPRYVDTTEP 494
Cdd:pfam02384 229 LFLTKNKAERkgKVLFIDASNEFKKEGKLNILTDEHIEKIIDTFGEFKDVDGFSKSATLEEIAANDYNLNVGRYVGTEEE 308

                  ..
gi 491959767  495 EK 496
Cdd:pfam02384 309 EE 310
hsdM TIGR00497
type I restriction system adenine methylase (hsdM); Function: methylation of specific adenine ...
9-517 9.95e-130

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: 388.16  E-value: 9.95e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491959767    9 EITSQLWAMANELRGNMDASEFRNYILGFMFYRYLSEHQERYLqetnlfepEAGQTWND---AFREVASDPESRKEYLED 85
Cdd:TIGR00497   4 ELEKKIWEIANKLRGSVDGWDFKQYVLGGLFYRFISENLCKYI--------NDSERRNDpsfSYANLTDDYEAIDALKDA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491959767   86 ISSELGYAIAPEQTWASLVQKVNDDKIVPSDYQDLFDDFNKnAALNPNSEADFRGIFADINLGDSRLGSSTTARAKALNG 165
Cdd:TIGR00497  76 AIASKGFFIKPSQLFQNVVKSIRENEDLNTTLRDIFDDIEK-SELGDGSKESFKGLFKDFNVSEVKLGSTLTIRTEKLKE 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491959767  166 VVRLVDQFEYND--KQGRDILGDVYEYLIAQFAGNSGKKAGEFYTPHQVSKVLAKlVALGvqKDQEIFTVYDPTMGSGSL 243
Cdd:TIGR00497 155 LLTSIDTMELDEfeKNSIDAFGDAYEFLISMYAQNAGKSGGEFFTPQDISELLAR-IAIG--KKDTVDDVYDMACGSGSL 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491959767  244 LLTVRDELPATVKAVMFHGQELNTTTFNLARMNLMMHNVPYTNMSLRNADTLED-DWPDgvvggvDSPrsFDAVVANPPY 322
Cdd:TIGR00497 232 LLQVIKVLGEKTSLVSYYGQEINHTTYNLCRMNMILHNIDYANFNIINADTLTTkEWEN------ENG--FEVVVSNPPY 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491959767  323 SIHW--DNSENKLKDPRFKPFGALAPKSKADFAFVEHGLYHLNDTGTMAIVLPHGVLFRGAAEGKIRKAIIEKNYLDAVI 400
Cdd:TIGR00497 304 SISWagDKKSNLVSDVRFKDAGTLAPNSKADLAFVLHALYVLGQEGTAAIVCFPGILYREGKEQTIRKYLVDQNFVDAVI 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491959767  401 GMPAGLFFSTGIPTVVLVFKKNRTNRDIFFIDASNNFEKGKNQNILRDSDIDKIIEAYSKREDVDKYAHKAELDEIVENE 480
Cdd:TIGR00497 384 QLPSNLFSTTSIATSILVLKKNRKKDPIFFIDGSNEFVREKKNNRLSPKNIEKIVDCFNSKKEEANFAKSVERDKIRESN 463
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 491959767  481 YNLNIPRYVDTTEPEKPIDVVQVVADIKETDKKIAKL 517
Cdd:TIGR00497 464 YDLTVGKYVNSEAEKEELDIKVLNHSIDEIVDKQKDL 500
HsdM COG0286
Type I restriction-modification system, DNA methylase subunit [Defense mechanisms];
182-435 7.19e-103

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


Pssm-ID: 440055 [Multi-domain]  Cd Length: 243  Bit Score: 309.42  E-value: 7.19e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491959767 182 DILGDVYEYLIAQFAGNSGKKAGEFYTPHQVSKVLAKLValgvqKDQEIFTVYDPTMGSGSLLLT----VRDELPATVKA 257
Cdd:COG0286    1 DVLGDAYEYLLRKFAEESGKKAGEFYTPREVVRLMVELL-----DPKPGETVYDPACGSGGFLVEaaeyLKEHGGDERKK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491959767 258 VMFHGQELNTTTFNLARMNLMMHNVPytNMSLRNADTLEDDWpdgvvggvDSPRSFDAVVANPPYSIHWDNSENKlKDPR 337
Cdd:COG0286   76 LSLYGQEINPTTYRLAKMNLLLHGIG--DPNIELGDTLSNDG--------DELEKFDVVLANPPFGGKWKKEELK-DDLL 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491959767 338 FKPFGALAPKSKADFAFVEHGLYHLNDTGTMAIVLPHGVLFRGAaEGKIRKAIIEKNYLDAVIGMPAGLFFSTGIPTVVL 417
Cdd:COG0286  145 GRFGYGLPPKSNADLLFLQHILSLLKPGGRAAVVLPDGVLFRGA-EKEIRKKLLENDLLEAIIGLPSNLFYNTGIPTCIL 223
                        250       260
                 ....*....|....*....|
gi 491959767 418 VFKKNRTNR--DIFFIDASN 435
Cdd:COG0286  224 FLTKGKPERtgKVLFIDASK 243
HsdM_N pfam12161
HsdM N-terminal domain; This domain is found at the N-terminus of the methylase subunit of ...
10-170 2.08e-16

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: 75.41  E-value: 2.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491959767   10 ITSQLWAMANELRGNMDASEFRNYILGFMFYRYLSEHQERYLQETnlfepeagqtwndafrevasdpesrKEYLEDISSE 89
Cdd:pfam12161   1 LESFLWNAADILRGDVDASEYKEYILPLLFLKRLDDVLEEREEEV-------------------------LELIEPLDSG 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491959767   90 LGYAIAPEQTWASLVQkVNDDKIVPSDYQDLFDDFnknAALNPnseaDFRGIF-ADINLGDsrlgssTTARAKALNGVVR 168
Cdd:pfam12161  56 FGFYIPSELRWSKLAN-NLDNDELGENLNDAFPGL---EELNP----DLRGVFmKDARGII------TLKSPDLLKKVIQ 121

                  ..
gi 491959767  169 LV 170
Cdd:pfam12161 122 KF 123
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
219-322 2.27e-03

N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 40.15  E-value: 2.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491959767 219 LV--ALGVQKDQEIFTVYDPTMGSGSLLLTVRDELP-ATVKAVmfhgqELNTTTFNLARMNLMMHNvpytnmsLRNADTL 295
Cdd:PRK09328  96 LVewALEALLLKEPLRVLDLGTGSGAIALALAKERPdAEVTAV-----DISPEALAVARRNAKHGL-------GARVEFL 163
                         90       100
                 ....*....|....*....|....*..
gi 491959767 296 EDDWPDGVVGGvdsprSFDAVVANPPY 322
Cdd:PRK09328 164 QGDWFEPLPGG-----RFDLIVSNPPY 185
 
Name Accession Description Interval E-value
N6_Mtase pfam02384
N-6 DNA Methylase; Restriction-modification (R-M) systems protect a bacterial cell against ...
180-496 5.47e-130

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: 381.67  E-value: 5.47e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491959767  180 GRDILGDVYEYLIAQFAGNSGKKAGEFYTPHQVSKVLAKLValgvqKDQEIFTVYDPTMGSGSLLLTVRDELPAT---VK 256
Cdd:pfam02384   1 SRDLFGDAYEYLLRKFAPNAGKSGGEFFTPREVSKLIVELL-----DPKPGESIYDPACGSGGFLIQAEKFVKEHdgdTN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491959767  257 AVMFHGQELNTTTFNLARMNLMMHNVPYTNMSLRNADTLEDDWPDGvvggvdsPRSFDAVVANPPYSIHWDNSENKLKDP 336
Cdd:pfam02384  76 DLSIYGQEKNPTTYRLARMNMILHGIEYDDFHIRHGDTLTSPKFED-------DKKFDVVVANPPFSDKWDANDTLENDP 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491959767  337 RFKPFGALAPKSKADFAFVEHGLYHLNDTGTMAIVLPHGVLFRGAAEGKIRKAIIEKNYLDAVIGMPAGLFFSTGIPTVV 416
Cdd:pfam02384 149 RFRPAYGVAPKSNADLAFLQHIIYYLAPGGRAAVVLPNGVLFRGGAEGKIRKALVDKDLVETVIALPPNLFYNTSIPTCI 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491959767  417 LVFKKNRTNR--DIFFIDASNNFEKGKNQNILRDSDIDKIIEAYSKREDVDKYAHKAELDEIVENEYNLNIPRYVDTTEP 494
Cdd:pfam02384 229 LFLTKNKAERkgKVLFIDASNEFKKEGKLNILTDEHIEKIIDTFGEFKDVDGFSKSATLEEIAANDYNLNVGRYVGTEEE 308

                  ..
gi 491959767  495 EK 496
Cdd:pfam02384 309 EE 310
hsdM TIGR00497
type I restriction system adenine methylase (hsdM); Function: methylation of specific adenine ...
9-517 9.95e-130

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: 388.16  E-value: 9.95e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491959767    9 EITSQLWAMANELRGNMDASEFRNYILGFMFYRYLSEHQERYLqetnlfepEAGQTWND---AFREVASDPESRKEYLED 85
Cdd:TIGR00497   4 ELEKKIWEIANKLRGSVDGWDFKQYVLGGLFYRFISENLCKYI--------NDSERRNDpsfSYANLTDDYEAIDALKDA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491959767   86 ISSELGYAIAPEQTWASLVQKVNDDKIVPSDYQDLFDDFNKnAALNPNSEADFRGIFADINLGDSRLGSSTTARAKALNG 165
Cdd:TIGR00497  76 AIASKGFFIKPSQLFQNVVKSIRENEDLNTTLRDIFDDIEK-SELGDGSKESFKGLFKDFNVSEVKLGSTLTIRTEKLKE 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491959767  166 VVRLVDQFEYND--KQGRDILGDVYEYLIAQFAGNSGKKAGEFYTPHQVSKVLAKlVALGvqKDQEIFTVYDPTMGSGSL 243
Cdd:TIGR00497 155 LLTSIDTMELDEfeKNSIDAFGDAYEFLISMYAQNAGKSGGEFFTPQDISELLAR-IAIG--KKDTVDDVYDMACGSGSL 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491959767  244 LLTVRDELPATVKAVMFHGQELNTTTFNLARMNLMMHNVPYTNMSLRNADTLED-DWPDgvvggvDSPrsFDAVVANPPY 322
Cdd:TIGR00497 232 LLQVIKVLGEKTSLVSYYGQEINHTTYNLCRMNMILHNIDYANFNIINADTLTTkEWEN------ENG--FEVVVSNPPY 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491959767  323 SIHW--DNSENKLKDPRFKPFGALAPKSKADFAFVEHGLYHLNDTGTMAIVLPHGVLFRGAAEGKIRKAIIEKNYLDAVI 400
Cdd:TIGR00497 304 SISWagDKKSNLVSDVRFKDAGTLAPNSKADLAFVLHALYVLGQEGTAAIVCFPGILYREGKEQTIRKYLVDQNFVDAVI 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491959767  401 GMPAGLFFSTGIPTVVLVFKKNRTNRDIFFIDASNNFEKGKNQNILRDSDIDKIIEAYSKREDVDKYAHKAELDEIVENE 480
Cdd:TIGR00497 384 QLPSNLFSTTSIATSILVLKKNRKKDPIFFIDGSNEFVREKKNNRLSPKNIEKIVDCFNSKKEEANFAKSVERDKIRESN 463
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 491959767  481 YNLNIPRYVDTTEPEKPIDVVQVVADIKETDKKIAKL 517
Cdd:TIGR00497 464 YDLTVGKYVNSEAEKEELDIKVLNHSIDEIVDKQKDL 500
HsdM COG0286
Type I restriction-modification system, DNA methylase subunit [Defense mechanisms];
182-435 7.19e-103

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


Pssm-ID: 440055 [Multi-domain]  Cd Length: 243  Bit Score: 309.42  E-value: 7.19e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491959767 182 DILGDVYEYLIAQFAGNSGKKAGEFYTPHQVSKVLAKLValgvqKDQEIFTVYDPTMGSGSLLLT----VRDELPATVKA 257
Cdd:COG0286    1 DVLGDAYEYLLRKFAEESGKKAGEFYTPREVVRLMVELL-----DPKPGETVYDPACGSGGFLVEaaeyLKEHGGDERKK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491959767 258 VMFHGQELNTTTFNLARMNLMMHNVPytNMSLRNADTLEDDWpdgvvggvDSPRSFDAVVANPPYSIHWDNSENKlKDPR 337
Cdd:COG0286   76 LSLYGQEINPTTYRLAKMNLLLHGIG--DPNIELGDTLSNDG--------DELEKFDVVLANPPFGGKWKKEELK-DDLL 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491959767 338 FKPFGALAPKSKADFAFVEHGLYHLNDTGTMAIVLPHGVLFRGAaEGKIRKAIIEKNYLDAVIGMPAGLFFSTGIPTVVL 417
Cdd:COG0286  145 GRFGYGLPPKSNADLLFLQHILSLLKPGGRAAVVLPDGVLFRGA-EKEIRKKLLENDLLEAIIGLPSNLFYNTGIPTCIL 223
                        250       260
                 ....*....|....*....|
gi 491959767 418 VFKKNRTNR--DIFFIDASN 435
Cdd:COG0286  224 FLTKGKPERtgKVLFIDASK 243
HsdM_N pfam12161
HsdM N-terminal domain; This domain is found at the N-terminus of the methylase subunit of ...
10-170 2.08e-16

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: 75.41  E-value: 2.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491959767   10 ITSQLWAMANELRGNMDASEFRNYILGFMFYRYLSEHQERYLQETnlfepeagqtwndafrevasdpesrKEYLEDISSE 89
Cdd:pfam12161   1 LESFLWNAADILRGDVDASEYKEYILPLLFLKRLDDVLEEREEEV-------------------------LELIEPLDSG 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491959767   90 LGYAIAPEQTWASLVQkVNDDKIVPSDYQDLFDDFnknAALNPnseaDFRGIF-ADINLGDsrlgssTTARAKALNGVVR 168
Cdd:pfam12161  56 FGFYIPSELRWSKLAN-NLDNDELGENLNDAFPGL---EELNP----DLRGVFmKDARGII------TLKSPDLLKKVIQ 121

                  ..
gi 491959767  169 LV 170
Cdd:pfam12161 122 KF 123
YtxK COG0827
Adenine-specific DNA N6-methylase [Replication, recombination and repair];
147-407 5.01e-09

Adenine-specific DNA N6-methylase [Replication, recombination and repair];


Pssm-ID: 440589 [Multi-domain]  Cd Length: 327  Bit Score: 58.04  E-value: 5.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491959767 147 LGDSRLGSSTTARAKALNGVVRLVDQFEYNDKQGRDILgdvyeyliaQFAGNSGKK----AGEFYTPHQVSKVLAKLVA- 221
Cdd:COG0827   40 LDGEVEGKPTEEAKKKLKKNYQKLQLESLSKEEIRKAL---------QLALLKGMKesvqPNHQMTPDAIGLLIGYLVEk 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491959767 222 LGVQKDQEIFtvyDPTMGSGSLLLTVRDELPATVKAvmfHGQELNTTtfnLARMNLMMHNVPYTNMSLRNADTLEDDWPD 301
Cdd:COG0827  111 FTKKEGLRIL---DPAVGTGNLLTTVLNQLKKKVNA---YGVEVDDL---LIRLAAVLANLQGHPVELFHQDALQPLLID 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491959767 302 gvvggvdsprSFDAVVANPP--YSIHWDNSENklkdprFKpfgaLAPKSKADFA---FVEHGLYHLNDTGTMAIVLPHGv 376
Cdd:COG0827  182 ----------PVDVVISDLPvgYYPNDERAKR------FK----LKADEGHSYAhhlFIEQSLNYLKPGGYLFFLVPSN- 240
                        250       260       270
                 ....*....|....*....|....*....|.
gi 491959767 377 LFRGAAEGKIRKAIIEKNYLDAVIGMPAGLF 407
Cdd:COG0827  241 LFESDQAAQLREFLKEKAHIQGLIQLPESLF 271
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
239-322 9.68e-05

Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 44.37  E-value: 9.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491959767 239 GSGSLLLTVRDELP-ATVKAVmfhgqELNTTTFNLARMNLMMHNVPytnmslRNADTLEDDWPDGVvggvDSPRSFDAVV 317
Cdd:COG2890  122 GSGAIALALAKERPdARVTAV-----DISPDALAVARRNAERLGLE------DRVRFLQGDLFEPL----PGDGRFDLIV 186

                 ....*
gi 491959767 318 ANPPY 322
Cdd:COG2890  187 SNPPY 191
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
219-322 2.27e-03

N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 40.15  E-value: 2.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491959767 219 LV--ALGVQKDQEIFTVYDPTMGSGSLLLTVRDELP-ATVKAVmfhgqELNTTTFNLARMNLMMHNvpytnmsLRNADTL 295
Cdd:PRK09328  96 LVewALEALLLKEPLRVLDLGTGSGAIALALAKERPdAEVTAV-----DISPEALAVARRNAKHGL-------GARVEFL 163
                         90       100
                 ....*....|....*....|....*..
gi 491959767 296 EDDWPDGVVGGvdsprSFDAVVANPPY 322
Cdd:PRK09328 164 QGDWFEPLPGG-----RFDLIVSNPPY 185
 
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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