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Conserved domains on  [gi|658753000|ref|WP_029772546|]
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class I SAM-dependent DNA methyltransferase [Pseudoalteromonas sp. TB51]

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];
151-404 2.36e-96

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


:

Pssm-ID: 440055 [Multi-domain]  Cd Length: 243  Bit Score: 292.86  E-value: 2.36e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753000 151 DIFGRIYEYFLNEFAKTEGQGGGEFFTPSALVKLITEVIEPYHG-KVFDPACGSGGMFISSADFVAKHNKDASDELSVFG 229
Cdd:COG0286    1 DVLGDAYEYLLRKFAEESGKKAGEFYTPREVVRLMVELLDPKPGeTVYDPACGSGGFLVEAAEYLKEHGGDERKKLSLYG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753000 230 QEKTGDTVRLSKLNLAVHGL-QGDIREGNSYYEDPFDLakgevidgkqyGQFDYVMANPPFNVnEIQKDRLEGDKH-RFP 307
Cdd:COG0286   81 QEINPTTYRLAKMNLLLHGIgDPNIELGDTLSNDGDEL-----------EKFDVVLANPPFGG-KWKKEELKDDLLgRFG 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753000 308 YGMPRNDNGNYLWIQMFYSALNQKGRAGFVMANSASDaRGSEQEIRQKLIEEDGVDVMVAVSSNFFYTVTLPCALWFLDK 387
Cdd:COG0286  149 YGLPPKSNADLLFLQHILSLLKPGGRAAVVLPDGVLF-RGAEKEIRKKLLENDLLEAIIGLPSNLFYNTGIPTCILFLTK 227
                        250
                 ....*....|....*..
gi 658753000 388 NKPAHnKDKVLFIDARH 404
Cdd:COG0286  228 GKPER-TGKVLFIDASK 243
HsdM_N pfam12161
HsdM N-terminal domain; This domain is found at the N-terminus of the methylase subunit of ...
10-141 7.12e-17

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: 76.95  E-value: 7.12e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753000   10 LEKRLWSAADSLRANtgLTAQEYSRPILGLIFLKYAEYRFTLAKSKIEEqsssrrrgssdIKSKIQAEGAMYVPSEALYS 89
Cdd:pfam12161   1 LESFLWNAADILRGD--VDASEYKEYILPLLFLKRLDDVLEEREEEVLE-----------LIEPLDSGFGFYIPSELRWS 67
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 658753000   90 NLLALPEGSNIGVQVNDAMKALEADNEAIKDALPKTY----SRFENDMLKSLLKNF 141
Cdd:pfam12161  68 KLANNLDNDELGENLNDAFPGLEELNPDLRGVFMKDArgiiTLKSPDLLKKVIQKF 123
 
Name Accession Description Interval E-value
HsdM COG0286
Type I restriction-modification system, DNA methylase subunit [Defense mechanisms];
151-404 2.36e-96

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


Pssm-ID: 440055 [Multi-domain]  Cd Length: 243  Bit Score: 292.86  E-value: 2.36e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753000 151 DIFGRIYEYFLNEFAKTEGQGGGEFFTPSALVKLITEVIEPYHG-KVFDPACGSGGMFISSADFVAKHNKDASDELSVFG 229
Cdd:COG0286    1 DVLGDAYEYLLRKFAEESGKKAGEFYTPREVVRLMVELLDPKPGeTVYDPACGSGGFLVEAAEYLKEHGGDERKKLSLYG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753000 230 QEKTGDTVRLSKLNLAVHGL-QGDIREGNSYYEDPFDLakgevidgkqyGQFDYVMANPPFNVnEIQKDRLEGDKH-RFP 307
Cdd:COG0286   81 QEINPTTYRLAKMNLLLHGIgDPNIELGDTLSNDGDEL-----------EKFDVVLANPPFGG-KWKKEELKDDLLgRFG 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753000 308 YGMPRNDNGNYLWIQMFYSALNQKGRAGFVMANSASDaRGSEQEIRQKLIEEDGVDVMVAVSSNFFYTVTLPCALWFLDK 387
Cdd:COG0286  149 YGLPPKSNADLLFLQHILSLLKPGGRAAVVLPDGVLF-RGAEKEIRKKLLENDLLEAIIGLPSNLFYNTGIPTCILFLTK 227
                        250
                 ....*....|....*..
gi 658753000 388 NKPAHnKDKVLFIDARH 404
Cdd:COG0286  228 GKPER-TGKVLFIDASK 243
N6_Mtase pfam02384
N-6 DNA Methylase; Restriction-modification (R-M) systems protect a bacterial cell against ...
151-503 3.18e-86

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: 269.19  E-value: 3.18e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753000  151 DIFGRIYEYFLNEFAKTEGQGGGEFFTPSALVKLITEVIEPYHGK-VFDPACGSGGMFISSADFVAKHNKDASDeLSVFG 229
Cdd:pfam02384   3 DLFGDAYEYLLRKFAPNAGKSGGEFFTPREVSKLIVELLDPKPGEsIYDPACGSGGFLIQAEKFVKEHDGDTND-LSIYG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753000  230 QEKTGDTVRLSKLNLAVHGLQGD---IREGNSYYEDPFDLAKgevidgkqygQFDYVMANPPFNVNEIQKDRLEGD-KHR 305
Cdd:pfam02384  82 QEKNPTTYRLARMNMILHGIEYDdfhIRHGDTLTSPKFEDDK----------KFDVVVANPPFSDKWDANDTLENDpRFR 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753000  306 FPYGMPRNDNGNYLWIQMFYSALNQKGRAGFVMANSASDARGSEQEIRQKLIEEDGVDVMVAVSSNFFYTVTLPCALWFL 385
Cdd:pfam02384 152 PAYGVAPKSNADLAFLQHIIYYLAPGGRAAVVLPNGVLFRGGAEGKIRKALVDKDLVETVIALPPNLFYNTSIPTCILFL 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753000  386 DKNKPAhNKDKVLFIDARHIFRQVTRAvRDYTSEQlnfIANIVRLYRGqdidntylgsypdagnngkfklddhftndvge 465
Cdd:pfam02384 232 TKNKAE-RKGKVLFIDASNEFKKEGKL-NILTDEH---IEKIIDTFGE-------------------------------- 274
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 658753000  466 liYQDIAGLCKVATKEEIIEQGYSLNPGRYVGVAEGEH 503
Cdd:pfam02384 275 --FKDVDGFSKSATLEEIAANDYNLNVGRYVGTEEEEE 310
hsdM TIGR00497
type I restriction system adenine methylase (hsdM); Function: methylation of specific adenine ...
9-507 1.64e-31

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: 127.76  E-value: 1.64e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753000    9 ELEKRLWSAADSLRANtgLTAQEYSRPILGLIFLKYAEYRFT--LAKSKIEEQSSSRRRGSSDIKSKIQ-------AEGA 79
Cdd:TIGR00497   4 ELEKKIWEIANKLRGS--VDGWDFKQYVLGGLFYRFISENLCkyINDSERRNDPSFSYANLTDDYEAIDalkdaaiASKG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753000   80 MYVPSEALYSNLLALP-----------------EGSNIGVQVNDAMKALEADNEAIKDALPKTYS-RFENdmLKSLLKNF 141
Cdd:TIGR00497  82 FFIKPSQLFQNVVKSIrenedlnttlrdifddiEKSELGDGSKESFKGLFKDFNVSEVKLGSTLTiRTEK--LKELLTSI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753000  142 NDIDF----TLGSDIFGRIYEYFLNEFAKTEGQGGGEFFTPSALVKLITEViePYHGK-----VFDPACGSGGMFISsad 212
Cdd:TIGR00497 160 DTMELdefeKNSIDAFGDAYEFLISMYAQNAGKSGGEFFTPQDISELLARI--AIGKKdtvddVYDMACGSGSLLLQ--- 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753000  213 fVAKHNKDASDELSVFGQEKTGDTVRLSKLNLAVHglqgDIREGNsyyedpFDLAKGEVIDGKQYGQ---FDYVMANPPF 289
Cdd:TIGR00497 235 -VIKVLGEKTSLVSYYGQEINHTTYNLCRMNMILH----NIDYAN------FNIINADTLTTKEWENengFEVVVSNPPY 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753000  290 NVNEI--QKDRLEGDKHRFPYG-MPRNDNGNYLWIQMFYSALNQKGRAGFVMANSASDARGSEQEIRQKLIEEDGVDVMV 366
Cdd:TIGR00497 304 SISWAgdKKSNLVSDVRFKDAGtLAPNSKADLAFVLHALYVLGQEGTAAIVCFPGILYREGKEQTIRKYLVDQNFVDAVI 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753000  367 AVSSNFFYTVTLPCALWFLDKNKpahNKDKVLFIDARHIFrqvtraVRDYTSEQLN--FIANIVRLYRGQdidntylgsy 444
Cdd:TIGR00497 384 QLPSNLFSTTSIATSILVLKKNR---KKDPIFFIDGSNEF------VREKKNNRLSpkNIEKIVDCFNSK---------- 444
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658753000  445 pdagnngkfklddhftndvgeliyQDIAGLCKVATKEEIIEQGYSLNPGRYVgvaEGEHESDE 507
Cdd:TIGR00497 445 ------------------------KEEANFAKSVERDKIRESNYDLTVGKYV---NSEAEKEE 480
HsdM_N pfam12161
HsdM N-terminal domain; This domain is found at the N-terminus of the methylase subunit of ...
10-141 7.12e-17

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: 76.95  E-value: 7.12e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753000   10 LEKRLWSAADSLRANtgLTAQEYSRPILGLIFLKYAEYRFTLAKSKIEEqsssrrrgssdIKSKIQAEGAMYVPSEALYS 89
Cdd:pfam12161   1 LESFLWNAADILRGD--VDASEYKEYILPLLFLKRLDDVLEEREEEVLE-----------LIEPLDSGFGFYIPSELRWS 67
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 658753000   90 NLLALPEGSNIGVQVNDAMKALEADNEAIKDALPKTY----SRFENDMLKSLLKNF 141
Cdd:pfam12161  68 KLANNLDNDELGENLNDAFPGLEELNPDLRGVFMKDArgiiTLKSPDLLKKVIQKF 123
rsmC PRK09489
16S rRNA (guanine(1207)-N(2))-methyltransferase RsmC;
194-289 3.99e-03

16S rRNA (guanine(1207)-N(2))-methyltransferase RsmC;


Pssm-ID: 181902 [Multi-domain]  Cd Length: 342  Bit Score: 39.54  E-value: 3.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753000 194 GKVFDPACGSGgmFISSAdfVAKHNKDASDELSvfgqektgD----TVRLSKLNLAVHGLQGDIREGNSYYEdpfdlakg 269
Cdd:PRK09489 198 GKVLDVGCGAG--VLSAV--LARHSPKIRLTLS--------DvsaaALESSRATLAANGLEGEVFASNVFSD-------- 257
                         90       100
                 ....*....|....*....|
gi 658753000 270 evIDGKqygqFDYVMANPPF 289
Cdd:PRK09489 258 --IKGR----FDMIISNPPF 271
 
Name Accession Description Interval E-value
HsdM COG0286
Type I restriction-modification system, DNA methylase subunit [Defense mechanisms];
151-404 2.36e-96

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


Pssm-ID: 440055 [Multi-domain]  Cd Length: 243  Bit Score: 292.86  E-value: 2.36e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753000 151 DIFGRIYEYFLNEFAKTEGQGGGEFFTPSALVKLITEVIEPYHG-KVFDPACGSGGMFISSADFVAKHNKDASDELSVFG 229
Cdd:COG0286    1 DVLGDAYEYLLRKFAEESGKKAGEFYTPREVVRLMVELLDPKPGeTVYDPACGSGGFLVEAAEYLKEHGGDERKKLSLYG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753000 230 QEKTGDTVRLSKLNLAVHGL-QGDIREGNSYYEDPFDLakgevidgkqyGQFDYVMANPPFNVnEIQKDRLEGDKH-RFP 307
Cdd:COG0286   81 QEINPTTYRLAKMNLLLHGIgDPNIELGDTLSNDGDEL-----------EKFDVVLANPPFGG-KWKKEELKDDLLgRFG 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753000 308 YGMPRNDNGNYLWIQMFYSALNQKGRAGFVMANSASDaRGSEQEIRQKLIEEDGVDVMVAVSSNFFYTVTLPCALWFLDK 387
Cdd:COG0286  149 YGLPPKSNADLLFLQHILSLLKPGGRAAVVLPDGVLF-RGAEKEIRKKLLENDLLEAIIGLPSNLFYNTGIPTCILFLTK 227
                        250
                 ....*....|....*..
gi 658753000 388 NKPAHnKDKVLFIDARH 404
Cdd:COG0286  228 GKPER-TGKVLFIDASK 243
N6_Mtase pfam02384
N-6 DNA Methylase; Restriction-modification (R-M) systems protect a bacterial cell against ...
151-503 3.18e-86

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: 269.19  E-value: 3.18e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753000  151 DIFGRIYEYFLNEFAKTEGQGGGEFFTPSALVKLITEVIEPYHGK-VFDPACGSGGMFISSADFVAKHNKDASDeLSVFG 229
Cdd:pfam02384   3 DLFGDAYEYLLRKFAPNAGKSGGEFFTPREVSKLIVELLDPKPGEsIYDPACGSGGFLIQAEKFVKEHDGDTND-LSIYG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753000  230 QEKTGDTVRLSKLNLAVHGLQGD---IREGNSYYEDPFDLAKgevidgkqygQFDYVMANPPFNVNEIQKDRLEGD-KHR 305
Cdd:pfam02384  82 QEKNPTTYRLARMNMILHGIEYDdfhIRHGDTLTSPKFEDDK----------KFDVVVANPPFSDKWDANDTLENDpRFR 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753000  306 FPYGMPRNDNGNYLWIQMFYSALNQKGRAGFVMANSASDARGSEQEIRQKLIEEDGVDVMVAVSSNFFYTVTLPCALWFL 385
Cdd:pfam02384 152 PAYGVAPKSNADLAFLQHIIYYLAPGGRAAVVLPNGVLFRGGAEGKIRKALVDKDLVETVIALPPNLFYNTSIPTCILFL 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753000  386 DKNKPAhNKDKVLFIDARHIFRQVTRAvRDYTSEQlnfIANIVRLYRGqdidntylgsypdagnngkfklddhftndvge 465
Cdd:pfam02384 232 TKNKAE-RKGKVLFIDASNEFKKEGKL-NILTDEH---IEKIIDTFGE-------------------------------- 274
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 658753000  466 liYQDIAGLCKVATKEEIIEQGYSLNPGRYVGVAEGEH 503
Cdd:pfam02384 275 --FKDVDGFSKSATLEEIAANDYNLNVGRYVGTEEEEE 310
hsdM TIGR00497
type I restriction system adenine methylase (hsdM); Function: methylation of specific adenine ...
9-507 1.64e-31

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: 127.76  E-value: 1.64e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753000    9 ELEKRLWSAADSLRANtgLTAQEYSRPILGLIFLKYAEYRFT--LAKSKIEEQSSSRRRGSSDIKSKIQ-------AEGA 79
Cdd:TIGR00497   4 ELEKKIWEIANKLRGS--VDGWDFKQYVLGGLFYRFISENLCkyINDSERRNDPSFSYANLTDDYEAIDalkdaaiASKG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753000   80 MYVPSEALYSNLLALP-----------------EGSNIGVQVNDAMKALEADNEAIKDALPKTYS-RFENdmLKSLLKNF 141
Cdd:TIGR00497  82 FFIKPSQLFQNVVKSIrenedlnttlrdifddiEKSELGDGSKESFKGLFKDFNVSEVKLGSTLTiRTEK--LKELLTSI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753000  142 NDIDF----TLGSDIFGRIYEYFLNEFAKTEGQGGGEFFTPSALVKLITEViePYHGK-----VFDPACGSGGMFISsad 212
Cdd:TIGR00497 160 DTMELdefeKNSIDAFGDAYEFLISMYAQNAGKSGGEFFTPQDISELLARI--AIGKKdtvddVYDMACGSGSLLLQ--- 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753000  213 fVAKHNKDASDELSVFGQEKTGDTVRLSKLNLAVHglqgDIREGNsyyedpFDLAKGEVIDGKQYGQ---FDYVMANPPF 289
Cdd:TIGR00497 235 -VIKVLGEKTSLVSYYGQEINHTTYNLCRMNMILH----NIDYAN------FNIINADTLTTKEWENengFEVVVSNPPY 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753000  290 NVNEI--QKDRLEGDKHRFPYG-MPRNDNGNYLWIQMFYSALNQKGRAGFVMANSASDARGSEQEIRQKLIEEDGVDVMV 366
Cdd:TIGR00497 304 SISWAgdKKSNLVSDVRFKDAGtLAPNSKADLAFVLHALYVLGQEGTAAIVCFPGILYREGKEQTIRKYLVDQNFVDAVI 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753000  367 AVSSNFFYTVTLPCALWFLDKNKpahNKDKVLFIDARHIFrqvtraVRDYTSEQLN--FIANIVRLYRGQdidntylgsy 444
Cdd:TIGR00497 384 QLPSNLFSTTSIATSILVLKKNR---KKDPIFFIDGSNEF------VREKKNNRLSpkNIEKIVDCFNSK---------- 444
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658753000  445 pdagnngkfklddhftndvgeliyQDIAGLCKVATKEEIIEQGYSLNPGRYVgvaEGEHESDE 507
Cdd:TIGR00497 445 ------------------------KEEANFAKSVERDKIRESNYDLTVGKYV---NSEAEKEE 480
HsdM_N pfam12161
HsdM N-terminal domain; This domain is found at the N-terminus of the methylase subunit of ...
10-141 7.12e-17

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: 76.95  E-value: 7.12e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753000   10 LEKRLWSAADSLRANtgLTAQEYSRPILGLIFLKYAEYRFTLAKSKIEEqsssrrrgssdIKSKIQAEGAMYVPSEALYS 89
Cdd:pfam12161   1 LESFLWNAADILRGD--VDASEYKEYILPLLFLKRLDDVLEEREEEVLE-----------LIEPLDSGFGFYIPSELRWS 67
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 658753000   90 NLLALPEGSNIGVQVNDAMKALEADNEAIKDALPKTY----SRFENDMLKSLLKNF 141
Cdd:pfam12161  68 KLANNLDNDELGENLNDAFPGLEELNPDLRGVFMKDArgiiTLKSPDLLKKVIQKF 123
YeeA COG1002
Type II restriction/modification system, endonuclease and methylase domains [Defense ...
195-409 4.09e-04

Type II restriction/modification system, endonuclease and methylase domains [Defense mechanisms];


Pssm-ID: 440626 [Multi-domain]  Cd Length: 838  Bit Score: 43.16  E-value: 4.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753000 195 KVFDPACGSGGmFISSAdfvAKHNKDASDELSVFGQEKTGDTV-------------------------RLS------KLN 243
Cdd:COG1002  300 RVLDPACGSGN-FLVIA---YKELKAIEGEVLIRLEELDGLSQfhrkstiipnnfygieinpfaaeiaRLAlwiaelQWN 375
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753000 244 LAVHG----------LQGDIREGNS---YYEDPFDLAKGevidGKQYGQFDYVMANPPFNVNEIQKDRLEGD-KHRFPYG 309
Cdd:COG1002  376 YRYRGqlapflpllnDDNNIECGNAlrlRDGNAADWRFV----CPETGGEDYIIGNPPFLGQKEQREELKDDyVAVFPGK 451
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753000 310 MPRN-DNGNYLWIQMFYSALNQKGRAGFVMANSASdaRGSEQEIRQKLIEEDGVDVMVAVSS----NFFYTVTLPCALWF 384
Cdd:COG1002  452 VPGSaDYVAYWFEKAADYLRAGRGRFGFVTTNSIC--QGEQRKVLWPLLFATGLEIFFAIPDfpwaNASDNAAVRVSIVG 529
                        250       260
                 ....*....|....*....|....*
gi 658753000 385 LDKNKPAHNKDKVLFIDARHIFRQV 409
Cdd:COG1002  530 LSKGKPAGPKTLFSELEGVLFGREV 554
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
194-289 6.38e-04

Methyltransferase small domain; This domain is found in ribosomal RNA small subunit methyltransferase C as well as other methyltransferases.


Pssm-ID: 428349 [Multi-domain]  Cd Length: 170  Bit Score: 40.65  E-value: 6.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753000  194 GKVFDPACGSGGMFISSADFVAKHNKDASDElsvfgqektgDT--VRLSKLNLAVHGLQ-GDIREGNsyyedpfdlakge 270
Cdd:pfam05175  33 GKVLDLGCGAGVLGAALAKESPDAELTMVDI----------NAraLESARENLAANGLEnGEVVASD------------- 89
                          90
                  ....*....|....*....
gi 658753000  271 VIDGKQYGQFDYVMANPPF 289
Cdd:pfam05175  90 VYSGVEDGKFDLIISNPPF 108
rsmC PRK09489
16S rRNA (guanine(1207)-N(2))-methyltransferase RsmC;
194-289 3.99e-03

16S rRNA (guanine(1207)-N(2))-methyltransferase RsmC;


Pssm-ID: 181902 [Multi-domain]  Cd Length: 342  Bit Score: 39.54  E-value: 3.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753000 194 GKVFDPACGSGgmFISSAdfVAKHNKDASDELSvfgqektgD----TVRLSKLNLAVHGLQGDIREGNSYYEdpfdlakg 269
Cdd:PRK09489 198 GKVLDVGCGAG--VLSAV--LARHSPKIRLTLS--------DvsaaALESSRATLAANGLEGEVFASNVFSD-------- 257
                         90       100
                 ....*....|....*....|
gi 658753000 270 evIDGKqygqFDYVMANPPF 289
Cdd:PRK09489 258 --IKGR----FDMIISNPPF 271
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
184-289 5.36e-03

16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA G1207 methylase RsmC is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 442062 [Multi-domain]  Cd Length: 191  Bit Score: 38.25  E-value: 5.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658753000 184 LITEVIEPYHGKVFDPACGSGgmFISSAdfVAKHNKDAS------DELSVfgqektgdtvRLSKLNLAVHGLQ-GDIREG 256
Cdd:COG2813   41 LLEHLPEPLGGRVLDLGCGYG--VIGLA--LAKRNPEARvtlvdvNARAV----------ELARANAAANGLEnVEVLWS 106
                         90       100       110
                 ....*....|....*....|....*....|...
gi 658753000 257 NsYYEDPFDlakgevidgkqyGQFDYVMANPPF 289
Cdd:COG2813  107 D-GLSGVPD------------GSFDLILSNPPF 126
 
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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