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Conserved domains on  [gi|968558447|ref|WP_058585631|]
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N-6 DNA methylase [Pseudoalteromonas sp. XI10]

Protein Classification

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];
161-414 6.90e-76

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


:

Pssm-ID: 440055 [Multi-domain]  Cd Length: 243  Bit Score: 241.63  E-value: 6.90e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558447 161 IGDVYEQLLNDL--RGAGNAGEFYTPRAITAFMADRVNPrlDKRETVMDPACGTGGFLTAAIDHLRNQlttksGAEDKRA 238
Cdd:COG0286    3 LGDAYEYLLRKFaeESGKKAGEFYTPREVVRLMVELLDP--KPGETVYDPACGSGGFLVEAAEYLKEH-----GGDERKK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558447 239 IEalIHGIEKKQLPHLLCTTNMLLHGIDVPsQIEHKNTLGkgwNEWNNNDKVDCIITNPPFGG-YEDDTVGGDYPTDLK- 316
Cdd:COG0286   76 LS--LYGQEINPTTYRLAKMNLLLHGIGDP-NIELGDTLS---NDGDELEKFDVVLANPPFGGkWKKEELKDDLLGRFGy 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558447 317 ----TRETADMFMALIIKKlLKENGRAAVVLPDGFLFgDGIKGTLKKLLLQECNLHTIIRLPKGVFaPYTTIKTNLLFFT 392
Cdd:COG0286  150 glppKSNADLLFLQHILSL-LKPGGRAAVVLPDGVLF-RGAEKEIRKKLLENDLLEAIIGLPSNLF-YNTGIPTCILFLT 226
                        250       260
                 ....*....|....*....|..
gi 968558447 393 KGARVddgsehfHTDTIWFYEH 414
Cdd:COG0286  227 KGKPE-------RTGKVLFIDA 241
HsdM_N super family cl13579
HsdM N-terminal domain; This domain is found at the N-terminus of the methylase subunit of ...
3-123 2.58e-08

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.


The actual alignment was detected with superfamily member pfam12161:

Pssm-ID: 463478  Cd Length: 123  Bit Score: 52.68  E-value: 2.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558447    3 LSSTIKSIQDIMRKDdgVDgDAQRLGQLTWMLFLKVFDQREEEWEDDDASYKSPL--------PEALRWRNWAAyvpgvd 74
Cdd:pfam12161   1 LESFLWNAADILRGD--VD-ASEYKEYILPLLFLKRLDDVLEEREEEVLELIEPLdsgfgfyiPSELRWSKLAN------ 71
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 968558447   75 gkkapQKAASDIIGFVNNqLFPALKELEIPVFD-------AEKDNATSVALYKVIR 123
Cdd:pfam12161  72 -----NLDNDELGENLND-AFPGLEELNPDLRGvfmkdarGIITLKSPDLLKKVIQ 121
 
Name Accession Description Interval E-value
HsdM COG0286
Type I restriction-modification system, DNA methylase subunit [Defense mechanisms];
161-414 6.90e-76

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


Pssm-ID: 440055 [Multi-domain]  Cd Length: 243  Bit Score: 241.63  E-value: 6.90e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558447 161 IGDVYEQLLNDL--RGAGNAGEFYTPRAITAFMADRVNPrlDKRETVMDPACGTGGFLTAAIDHLRNQlttksGAEDKRA 238
Cdd:COG0286    3 LGDAYEYLLRKFaeESGKKAGEFYTPREVVRLMVELLDP--KPGETVYDPACGSGGFLVEAAEYLKEH-----GGDERKK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558447 239 IEalIHGIEKKQLPHLLCTTNMLLHGIDVPsQIEHKNTLGkgwNEWNNNDKVDCIITNPPFGG-YEDDTVGGDYPTDLK- 316
Cdd:COG0286   76 LS--LYGQEINPTTYRLAKMNLLLHGIGDP-NIELGDTLS---NDGDELEKFDVVLANPPFGGkWKKEELKDDLLGRFGy 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558447 317 ----TRETADMFMALIIKKlLKENGRAAVVLPDGFLFgDGIKGTLKKLLLQECNLHTIIRLPKGVFaPYTTIKTNLLFFT 392
Cdd:COG0286  150 glppKSNADLLFLQHILSL-LKPGGRAAVVLPDGVLF-RGAEKEIRKKLLENDLLEAIIGLPSNLF-YNTGIPTCILFLT 226
                        250       260
                 ....*....|....*....|..
gi 968558447 393 KGARVddgsehfHTDTIWFYEH 414
Cdd:COG0286  227 KGKPE-------RTGKVLFIDA 241
N6_Mtase pfam02384
N-6 DNA Methylase; Restriction-modification (R-M) systems protect a bacterial cell against ...
162-462 2.28e-71

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: 232.21  E-value: 2.28e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558447  162 GDVYEQLLNDLRG--AGNAGEFYTPRAITAFMADRVNPRLDkrETVMDPACGTGGFLTAAIDHLrnqlttksGAEDKRAI 239
Cdd:pfam02384   6 GDAYEYLLRKFAPnaGKSGGEFFTPREVSKLIVELLDPKPG--ESIYDPACGSGGFLIQAEKFV--------KEHDGDTN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558447  240 EALIHGIEKKQLPHLLCTTNMLLHGIDVPS-QIEHKNTLGKGWNEWNNndKVDCIITNPPFG--GYEDDTVGGD------ 310
Cdd:pfam02384  76 DLSIYGQEKNPTTYRLARMNMILHGIEYDDfHIRHGDTLTSPKFEDDK--KFDVVVANPPFSdkWDANDTLENDprfrpa 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558447  311 YPTDLKTreTAD-MFMALIIKKLlKENGRAAVVLPDGFLFGDGIKGTLKKLLLQECNLHTIIRLPKGVFAPyTTIKTNLL 389
Cdd:pfam02384 154 YGVAPKS--NADlAFLQHIIYYL-APGGRAAVVLPNGVLFRGGAEGKIRKALVDKDLVETVIALPPNLFYN-TSIPTCIL 229
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 968558447  390 FFTKGaRVDdgsehfHTDTIWFYEHPYPagYKSYSKTKPIRLEEFKPEQDWWGDEsddfasREENEFAWKVDF 462
Cdd:pfam02384 230 FLTKN-KAE------RKGKVLFIDASNE--FKKEGKLNILTDEHIEKIIDTFGEF------KDVDGFSKSATL 287
hsdM TIGR00497
type I restriction system adenine methylase (hsdM); Function: methylation of specific adenine ...
122-404 4.14e-20

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: 93.86  E-value: 4.14e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558447  122 IRGVFEDAN-NYMKSGTQLLAVIEKLE------DAINFHDFKTRA--NIGDVYEQLLNDLrgAGNAG----EFYTPRAIT 188
Cdd:TIGR00497 127 FKGLFKDFNvSEVKLGSTLTIRTEKLKelltsiDTMELDEFEKNSidAFGDAYEFLISMY--AQNAGksggEFFTPQDIS 204
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558447  189 AFMADRVNPRLDKRETVMDPACGTGGFLTAAIDHLRNQLTTKSgaedkraiealIHGIEKKQLPHLLCTTNMLLHGIDVP 268
Cdd:TIGR00497 205 ELLARIAIGKKDTVDDVYDMACGSGSLLLQVIKVLGEKTSLVS-----------YYGQEINHTTYNLCRMNMILHNIDYA 273
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558447  269 S-QIEHKNTLGKgwNEWNNNDKVDCIITNPPfggYEDDTVGGDYPT-----------DLKTRETADMFMALIIKKLLKEN 336
Cdd:TIGR00497 274 NfNIINADTLTT--KEWENENGFEVVVSNPP---YSISWAGDKKSNlvsdvrfkdagTLAPNSKADLAFVLHALYVLGQE 348
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 968558447  337 GRAAVVLPDGFLFGDGIKGTLKKLLLQECNLHTIIRLPKGVFAPyTTIKTNLLFFTKGARVD-----DGSEHF 404
Cdd:TIGR00497 349 GTAAIVCFPGILYREGKEQTIRKYLVDQNFVDAVIQLPSNLFST-TSIATSILVLKKNRKKDpiffiDGSNEF 420
HsdM_N pfam12161
HsdM N-terminal domain; This domain is found at the N-terminus of the methylase subunit of ...
3-123 2.58e-08

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: 52.68  E-value: 2.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558447    3 LSSTIKSIQDIMRKDdgVDgDAQRLGQLTWMLFLKVFDQREEEWEDDDASYKSPL--------PEALRWRNWAAyvpgvd 74
Cdd:pfam12161   1 LESFLWNAADILRGD--VD-ASEYKEYILPLLFLKRLDDVLEEREEEVLELIEPLdsgfgfyiPSELRWSKLAN------ 71
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 968558447   75 gkkapQKAASDIIGFVNNqLFPALKELEIPVFD-------AEKDNATSVALYKVIR 123
Cdd:pfam12161  72 -----NLDNDELGENLND-AFPGLEELNPDLRGvfmkdarGIITLKSPDLLKKVIQ 121
 
Name Accession Description Interval E-value
HsdM COG0286
Type I restriction-modification system, DNA methylase subunit [Defense mechanisms];
161-414 6.90e-76

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


Pssm-ID: 440055 [Multi-domain]  Cd Length: 243  Bit Score: 241.63  E-value: 6.90e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558447 161 IGDVYEQLLNDL--RGAGNAGEFYTPRAITAFMADRVNPrlDKRETVMDPACGTGGFLTAAIDHLRNQlttksGAEDKRA 238
Cdd:COG0286    3 LGDAYEYLLRKFaeESGKKAGEFYTPREVVRLMVELLDP--KPGETVYDPACGSGGFLVEAAEYLKEH-----GGDERKK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558447 239 IEalIHGIEKKQLPHLLCTTNMLLHGIDVPsQIEHKNTLGkgwNEWNNNDKVDCIITNPPFGG-YEDDTVGGDYPTDLK- 316
Cdd:COG0286   76 LS--LYGQEINPTTYRLAKMNLLLHGIGDP-NIELGDTLS---NDGDELEKFDVVLANPPFGGkWKKEELKDDLLGRFGy 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558447 317 ----TRETADMFMALIIKKlLKENGRAAVVLPDGFLFgDGIKGTLKKLLLQECNLHTIIRLPKGVFaPYTTIKTNLLFFT 392
Cdd:COG0286  150 glppKSNADLLFLQHILSL-LKPGGRAAVVLPDGVLF-RGAEKEIRKKLLENDLLEAIIGLPSNLF-YNTGIPTCILFLT 226
                        250       260
                 ....*....|....*....|..
gi 968558447 393 KGARVddgsehfHTDTIWFYEH 414
Cdd:COG0286  227 KGKPE-------RTGKVLFIDA 241
N6_Mtase pfam02384
N-6 DNA Methylase; Restriction-modification (R-M) systems protect a bacterial cell against ...
162-462 2.28e-71

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: 232.21  E-value: 2.28e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558447  162 GDVYEQLLNDLRG--AGNAGEFYTPRAITAFMADRVNPRLDkrETVMDPACGTGGFLTAAIDHLrnqlttksGAEDKRAI 239
Cdd:pfam02384   6 GDAYEYLLRKFAPnaGKSGGEFFTPREVSKLIVELLDPKPG--ESIYDPACGSGGFLIQAEKFV--------KEHDGDTN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558447  240 EALIHGIEKKQLPHLLCTTNMLLHGIDVPS-QIEHKNTLGKGWNEWNNndKVDCIITNPPFG--GYEDDTVGGD------ 310
Cdd:pfam02384  76 DLSIYGQEKNPTTYRLARMNMILHGIEYDDfHIRHGDTLTSPKFEDDK--KFDVVVANPPFSdkWDANDTLENDprfrpa 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558447  311 YPTDLKTreTAD-MFMALIIKKLlKENGRAAVVLPDGFLFGDGIKGTLKKLLLQECNLHTIIRLPKGVFAPyTTIKTNLL 389
Cdd:pfam02384 154 YGVAPKS--NADlAFLQHIIYYL-APGGRAAVVLPNGVLFRGGAEGKIRKALVDKDLVETVIALPPNLFYN-TSIPTCIL 229
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 968558447  390 FFTKGaRVDdgsehfHTDTIWFYEHPYPagYKSYSKTKPIRLEEFKPEQDWWGDEsddfasREENEFAWKVDF 462
Cdd:pfam02384 230 FLTKN-KAE------RKGKVLFIDASNE--FKKEGKLNILTDEHIEKIIDTFGEF------KDVDGFSKSATL 287
hsdM TIGR00497
type I restriction system adenine methylase (hsdM); Function: methylation of specific adenine ...
122-404 4.14e-20

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: 93.86  E-value: 4.14e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558447  122 IRGVFEDAN-NYMKSGTQLLAVIEKLE------DAINFHDFKTRA--NIGDVYEQLLNDLrgAGNAG----EFYTPRAIT 188
Cdd:TIGR00497 127 FKGLFKDFNvSEVKLGSTLTIRTEKLKelltsiDTMELDEFEKNSidAFGDAYEFLISMY--AQNAGksggEFFTPQDIS 204
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558447  189 AFMADRVNPRLDKRETVMDPACGTGGFLTAAIDHLRNQLTTKSgaedkraiealIHGIEKKQLPHLLCTTNMLLHGIDVP 268
Cdd:TIGR00497 205 ELLARIAIGKKDTVDDVYDMACGSGSLLLQVIKVLGEKTSLVS-----------YYGQEINHTTYNLCRMNMILHNIDYA 273
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558447  269 S-QIEHKNTLGKgwNEWNNNDKVDCIITNPPfggYEDDTVGGDYPT-----------DLKTRETADMFMALIIKKLLKEN 336
Cdd:TIGR00497 274 NfNIINADTLTT--KEWENENGFEVVVSNPP---YSISWAGDKKSNlvsdvrfkdagTLAPNSKADLAFVLHALYVLGQE 348
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 968558447  337 GRAAVVLPDGFLFGDGIKGTLKKLLLQECNLHTIIRLPKGVFAPyTTIKTNLLFFTKGARVD-----DGSEHF 404
Cdd:TIGR00497 349 GTAAIVCFPGILYREGKEQTIRKYLVDQNFVDAVIQLPSNLFST-TSIATSILVLKKNRKKDpiffiDGSNEF 420
YtxK COG0827
Adenine-specific DNA N6-methylase [Replication, recombination and repair];
182-379 8.42e-18

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


Pssm-ID: 440589 [Multi-domain]  Cd Length: 327  Bit Score: 84.62  E-value: 8.42e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558447 182 YTPRAITAFMADRVNpRLDKRE--TVMDPACGTGGFLTAAIDHLRNQLTtksgaedkraiealIHGIEKkqLPHLLCTTN 259
Cdd:COG0827   95 MTPDAIGLLIGYLVE-KFTKKEglRILDPAVGTGNLLTTVLNQLKKKVN--------------AYGVEV--DDLLIRLAA 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558447 260 MLLHGIDVPSQIEHKNTLgkgwnEWNNNDKVDCIITNPPFGGYEDDTVGGDYptdlKTRETADMFMA---LIIK--KLLK 334
Cdd:COG0827  158 VLANLQGHPVELFHQDAL-----QPLLIDPVDVVISDLPVGYYPNDERAKRF----KLKADEGHSYAhhlFIEQslNYLK 228
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 968558447 335 ENGRAAVVLPDgFLFGDGIKGTLKKLLLQECNLHTIIRLPKGVFA 379
Cdd:COG0827  229 PGGYLFFLVPS-NLFESDQAAQLREFLKEKAHIQGLIQLPESLFK 272
HsdM_N pfam12161
HsdM N-terminal domain; This domain is found at the N-terminus of the methylase subunit of ...
3-123 2.58e-08

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: 52.68  E-value: 2.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558447    3 LSSTIKSIQDIMRKDdgVDgDAQRLGQLTWMLFLKVFDQREEEWEDDDASYKSPL--------PEALRWRNWAAyvpgvd 74
Cdd:pfam12161   1 LESFLWNAADILRGD--VD-ASEYKEYILPLLFLKRLDDVLEEREEEVLELIEPLdsgfgfyiPSELRWSKLAN------ 71
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 968558447   75 gkkapQKAASDIIGFVNNqLFPALKELEIPVFD-------AEKDNATSVALYKVIR 123
Cdd:pfam12161  72 -----NLDNDELGENLND-AFPGLEELNPDLRGvfmkdarGIITLKSPDLLKKVIQ 121
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
198-344 9.17e-05

tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443299 [Multi-domain]  Cd Length: 238  Bit Score: 44.37  E-value: 9.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558447 198 RLDKRETVMDPACGTG--GFLTAAidhlrnqlttksgaedkRAIEALIHGIEKKQLPHLLCTTNMLLHGIDvpSQIE-HK 274
Cdd:COG4123   34 PVKKGGRVLDLGTGTGviALMLAQ-----------------RSPGARITGVEIQPEAAELARRNVALNGLE--DRITvIH 94
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 968558447 275 NTLgKGWNEWNNNDKVDCIITNPPFggYEDdtvGGDYPTDLKTRETA-----DMFMALI--IKKLLKENGRAAVVLP 344
Cdd:COG4123   95 GDL-KEFAAELPPGSFDLVVSNPPY--FKA---GSGRKSPDEARAIArhedaLTLEDLIraAARLLKPGGRFALIHP 165
YhdJ COG0863
DNA modification methylase [Replication, recombination and repair];
287-431 6.70e-04

DNA modification methylase [Replication, recombination and repair];


Pssm-ID: 440623  Cd Length: 236  Bit Score: 41.45  E-value: 6.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558447 287 NDKVDCIITNPPFG-GYEDDTVGGDYPTDLKTRETADMFMALI--IKKLLKENGRAAVVLpdGFLFGDGIKGTLKKL--- 360
Cdd:COG0863   16 DESVDLIVTDPPYNlGKKYGLGRREIGNELSFEEYLEFLREWLaeCYRVLKPGGSLYVNI--GDRYISRLIAALRDAgfk 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558447 361 LLQECnlhtIIRLPKGVFAPYTTIKTN----LLFFTKGAR-------VDDGSEHFHTDTIWFYEHPYPAGYKSYSKTKPI 429
Cdd:COG0863   94 LRNEI----IWRKPNGVPGPSKRRFRNsheyILWFTKGKKytfnvdaVKSIEDGRNPSDVWDIPGVTPKERKGHPTQKPV 169

                 ..
gi 968558447 430 RL 431
Cdd:COG0863  170 EL 171
 
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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