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Conserved domains on  [gi|746702580|gb|KIE93255|]
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putative Type I restriction enzyme EcoprrI M protein [Actinobacillus pleuropneumoniae]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
hsdM super family cl33272
type I restriction system adenine methylase (hsdM); Function: methylation of specific adenine ...
 6-502 0e+00

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]


The actual alignment was detected with superfamily member TIGR00497:

Pssm-ID: 211578 [Multi-domain]  Cd Length: 501  Bit Score: 640.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746702580    6 ERAELQRRIWQIANDVRGSVDGWDFKQYVLGTLFYRFISEHFVNYIEGG----DESIKYATWSDDDENIKLGKEHVIKEK 81
Cdd:TIGR00497   1 QRNELEKKIWEIANKLRGSVDGWDFKQYVLGGLFYRFISENLCKYINDSerrnDPSFSYANLTDDYEAIDALKDAAIASK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746702580   82 GYFIYPSQLFENVVKNAHNNPNLNTELKDIFTSIESSAVGYDPENDIKGLFADFDTTSNRLGNTVEDKNKRLAAVLQGVA 161
Cdd:TIGR00497  81 GFFIKPSQLFQNVVKSIRENEDLNTTLRDIFDDIEKSELGDGSKESFKGLFKDFNVSEVKLGSTLTIRTEKLKELLTSID 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746702580  162 GLPFERFEDNQIDLFGDAYEFLISNYAANAGKSGGEFFTPQNVSKLIAQLALHGQKAVNKIYDPACGSGSLLLQAKKQFD 241
Cdd:TIGR00497 161 TMELDEFEKNSIDAFGDAYEFLISMYAQNAGKSGGEFFTPQDISELLARIAIGKKDTVDDVYDMACGSGSLLLQVIKVLG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746702580  242 DHIIEEGFFGQEINHTTYNLARMNMFLHNINYDKFDITLGDTLLKPQFGDSKPFDAIVSNPPYSVKWVGDSDPTLINDER 321
Cdd:TIGR00497 241 EKTSLVSYYGQEINHTTYNLCRMNMILHNIDYANFNIINADTLTTKEWENENGFEVVVSNPPYSISWAGDKKSNLVSDVR 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746702580  322 FAPAGVLAPKSKADFAFILHALSYLSARGRAAIVTFPGIFYRGGAEQKIRQYLVDNNFVETVISLAPNLFFGTSIAVNIL 401
Cdd:TIGR00497 321 FKDAGTLAPNSKADLAFVLHALYVLGQEGTAAIVCFPGILYREGKEQTIRKYLVDQNFVDAVIQLPSNLFSTTSIATSIL 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746702580  402 VLSKNKTDSKTQFIDASGIFKKETNNNVLTDEHIAEILKLFADKADVDHLVKMVDNQAIADNDYNLAVSSYVEAKDEREV 481
Cdd:TIGR00497 401 VLKKNRKKDPIFFIDGSNEFVREKKNNRLSPKNIEKIVDCFNSKKEEANFAKSVERDKIRESNYDLTVGKYVNSEAEKEE 480

                         490       500
                  ....*....|....*....|.
gi 746702580  482 INISELNAEISETVAKIDRLR 502
Cdd:TIGR00497 481 LDIKVLNHSIDEIVDKQKDLR 501
 
Name Accession Description Interval E-value
hsdM TIGR00497
type I restriction system adenine methylase (hsdM); Function: methylation of specific adenine ...
 6-502 0e+00

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: 640.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746702580    6 ERAELQRRIWQIANDVRGSVDGWDFKQYVLGTLFYRFISEHFVNYIEGG----DESIKYATWSDDDENIKLGKEHVIKEK 81
Cdd:TIGR00497   1 QRNELEKKIWEIANKLRGSVDGWDFKQYVLGGLFYRFISENLCKYINDSerrnDPSFSYANLTDDYEAIDALKDAAIASK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746702580   82 GYFIYPSQLFENVVKNAHNNPNLNTELKDIFTSIESSAVGYDPENDIKGLFADFDTTSNRLGNTVEDKNKRLAAVLQGVA 161
Cdd:TIGR00497  81 GFFIKPSQLFQNVVKSIRENEDLNTTLRDIFDDIEKSELGDGSKESFKGLFKDFNVSEVKLGSTLTIRTEKLKELLTSID 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746702580  162 GLPFERFEDNQIDLFGDAYEFLISNYAANAGKSGGEFFTPQNVSKLIAQLALHGQKAVNKIYDPACGSGSLLLQAKKQFD 241
Cdd:TIGR00497 161 TMELDEFEKNSIDAFGDAYEFLISMYAQNAGKSGGEFFTPQDISELLARIAIGKKDTVDDVYDMACGSGSLLLQVIKVLG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746702580  242 DHIIEEGFFGQEINHTTYNLARMNMFLHNINYDKFDITLGDTLLKPQFGDSKPFDAIVSNPPYSVKWVGDSDPTLINDER 321
Cdd:TIGR00497 241 EKTSLVSYYGQEINHTTYNLCRMNMILHNIDYANFNIINADTLTTKEWENENGFEVVVSNPPYSISWAGDKKSNLVSDVR 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746702580  322 FAPAGVLAPKSKADFAFILHALSYLSARGRAAIVTFPGIFYRGGAEQKIRQYLVDNNFVETVISLAPNLFFGTSIAVNIL 401
Cdd:TIGR00497 321 FKDAGTLAPNSKADLAFVLHALYVLGQEGTAAIVCFPGILYREGKEQTIRKYLVDQNFVDAVIQLPSNLFSTTSIATSIL 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746702580  402 VLSKNKTDSKTQFIDASGIFKKETNNNVLTDEHIAEILKLFADKADVDHLVKMVDNQAIADNDYNLAVSSYVEAKDEREV 481
Cdd:TIGR00497 401 VLKKNRKKDPIFFIDGSNEFVREKKNNRLSPKNIEKIVDCFNSKKEEANFAKSVERDKIRESNYDLTVGKYVNSEAEKEE 480

                         490       500
                  ....*....|....*....|.
gi 746702580  482 INISELNAEISETVAKIDRLR 502
Cdd:TIGR00497 481 LDIKVLNHSIDEIVDKQKDLR 501
N6_Mtase pfam02384
N-6 DNA Methylase; Restriction-modification (R-M) systems protect a bacterial cell against ...
 172-480 1.12e-150

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: 432.90  E-value: 1.12e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746702580  172 QIDLFGDAYEFLISNYAANAGKSGGEFFTPQNVSKLIAQLAlhgQKAVNK-IYDPACGSGSLLLQAKKQF---DDHIIEE 247
Cdd:pfam02384   1 SRDLFGDAYEYLLRKFAPNAGKSGGEFFTPREVSKLIVELL---DPKPGEsIYDPACGSGGFLIQAEKFVkehDGDTNDL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746702580  248 GFFGQEINHTTYNLARMNMFLHNINYDKFDITLGDTLLKPQFGDSKPFDAIVSNPPYSVKWvgDSDPTLINDERFAPAGV 327
Cdd:pfam02384  78 SIYGQEKNPTTYRLARMNMILHGIEYDDFHIRHGDTLTSPKFEDDKKFDVVVANPPFSDKW--DANDTLENDPRFRPAYG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746702580  328 LAPKSKADFAFILHALSYLSARGRAAIVTFPGIFYRGGAEQKIRQYLVDNNFVETVISLAPNLFFGTSIAVNILVLSKNK 407
Cdd:pfam02384 156 VAPKSNADLAFLQHIIYYLAPGGRAAVVLPNGVLFRGGAEGKIRKALVDKDLVETVIALPPNLFYNTSIPTCILFLTKNK 235

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 746702580  408 TD--SKTQFIDASGIFKKETNNNVLTDEHIAEILKLFADKADVDHLVKMVDNQAIADNDYNLAVSSYVEAKDERE 480
Cdd:pfam02384 236 AErkGKVLFIDASNEFKKEGKLNILTDEHIEKIIDTFGEFKDVDGFSKSATLEEIAANDYNLNVGRYVGTEEEEE 310
HsdM COG0286
Type I restriction-modification system, DNA methylase subunit [Defense mechanisms];
174-418 1.81e-95

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


Pssm-ID: 440055 [Multi-domain]  Cd Length: 243  Bit Score: 289.39  E-value: 1.81e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746702580 174 DLFGDAYEFLISNYAANAGKSGGEFFTPQNVSKLIAQLALHgqKAVNKIYDPACGSGSLLLQA----KKQFDDHIIEEGF 249
Cdd:COG0286    1 DVLGDAYEYLLRKFAEESGKKAGEFYTPREVVRLMVELLDP--KPGETVYDPACGSGGFLVEAaeylKEHGGDERKKLSL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746702580 250 FGQEINHTTYNLARMNMFLHNInyDKFDITLGDTLLKPQfGDSKPFDAIVSNPPYSVKWVGDSdptLINDERFAPAGVLA 329
Cdd:COG0286   79 YGQEINPTTYRLAKMNLLLHGI--GDPNIELGDTLSNDG-DELEKFDVVLANPPFGGKWKKEE---LKDDLLGRFGYGLP 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746702580 330 PKSKADFAFILHALSYLSARGRAAIVTFPGIFYRGgAEQKIRQYLVDNNFVETVISLAPNLFFGTSIAVNILVLSKNKTD 409
Cdd:COG0286  153 PKSNADLLFLQHILSLLKPGGRAAVVLPDGVLFRG-AEKEIRKKLLENDLLEAIIGLPSNLFYNTGIPTCILFLTKGKPE 231

                        250
                 ....*....|.
gi 746702580 410 --SKTQFIDAS 418
Cdd:COG0286  232 rtGKVLFIDAS 242
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 207-304 1.23e-03

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 40.92  E-value: 1.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746702580 207 LIAQLALHGQKAVN--KIYDPACGSGSLLLQAKKQFDD-HIIeegffGQEINHTTYNLARMNMFLHNInyDKFDITLGDt 283
Cdd:PRK09328  95 ELVEWALEALLLKEplRVLDLGTGSGAIALALAKERPDaEVT-----AVDISPEALAVARRNAKHGLG--ARVEFLQGD- 166

                         90       100
                 ....*....|....*....|.
gi 746702580 284 LLKPQFGDskPFDAIVSNPPY 304
Cdd:PRK09328 167 WFEPLPGG--RFDLIVSNPPY 185
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 221-305 2.48e-03

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 37.79  E-value: 2.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746702580 221 KIYDPACGSGSLLLQAKKQFDDHIIeegffGQEINHTTYNLARMNMFlhNINYDKFDITLGDtLLKPQFGDSKPFDAIVS 300
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGARVT-----GVDISPVALELARKAAA--ALLADNVEVLKGD-AEELPPEADESFDVIIS 72


                 ....*
gi 746702580 301 NPPYS 305
Cdd:cd02440   73 DPPLH 77
 
Name Accession Description Interval E-value
hsdM TIGR00497
type I restriction system adenine methylase (hsdM); Function: methylation of specific adenine ...
 6-502 0e+00

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: 640.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746702580    6 ERAELQRRIWQIANDVRGSVDGWDFKQYVLGTLFYRFISEHFVNYIEGG----DESIKYATWSDDDENIKLGKEHVIKEK 81
Cdd:TIGR00497   1 QRNELEKKIWEIANKLRGSVDGWDFKQYVLGGLFYRFISENLCKYINDSerrnDPSFSYANLTDDYEAIDALKDAAIASK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746702580   82 GYFIYPSQLFENVVKNAHNNPNLNTELKDIFTSIESSAVGYDPENDIKGLFADFDTTSNRLGNTVEDKNKRLAAVLQGVA 161
Cdd:TIGR00497  81 GFFIKPSQLFQNVVKSIRENEDLNTTLRDIFDDIEKSELGDGSKESFKGLFKDFNVSEVKLGSTLTIRTEKLKELLTSID 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746702580  162 GLPFERFEDNQIDLFGDAYEFLISNYAANAGKSGGEFFTPQNVSKLIAQLALHGQKAVNKIYDPACGSGSLLLQAKKQFD 241
Cdd:TIGR00497 161 TMELDEFEKNSIDAFGDAYEFLISMYAQNAGKSGGEFFTPQDISELLARIAIGKKDTVDDVYDMACGSGSLLLQVIKVLG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746702580  242 DHIIEEGFFGQEINHTTYNLARMNMFLHNINYDKFDITLGDTLLKPQFGDSKPFDAIVSNPPYSVKWVGDSDPTLINDER 321
Cdd:TIGR00497 241 EKTSLVSYYGQEINHTTYNLCRMNMILHNIDYANFNIINADTLTTKEWENENGFEVVVSNPPYSISWAGDKKSNLVSDVR 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746702580  322 FAPAGVLAPKSKADFAFILHALSYLSARGRAAIVTFPGIFYRGGAEQKIRQYLVDNNFVETVISLAPNLFFGTSIAVNIL 401
Cdd:TIGR00497 321 FKDAGTLAPNSKADLAFVLHALYVLGQEGTAAIVCFPGILYREGKEQTIRKYLVDQNFVDAVIQLPSNLFSTTSIATSIL 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746702580  402 VLSKNKTDSKTQFIDASGIFKKETNNNVLTDEHIAEILKLFADKADVDHLVKMVDNQAIADNDYNLAVSSYVEAKDEREV 481
Cdd:TIGR00497 401 VLKKNRKKDPIFFIDGSNEFVREKKNNRLSPKNIEKIVDCFNSKKEEANFAKSVERDKIRESNYDLTVGKYVNSEAEKEE 480

                         490       500
                  ....*....|....*....|.
gi 746702580  482 INISELNAEISETVAKIDRLR 502
Cdd:TIGR00497 481 LDIKVLNHSIDEIVDKQKDLR 501
N6_Mtase pfam02384
N-6 DNA Methylase; Restriction-modification (R-M) systems protect a bacterial cell against ...
 172-480 1.12e-150

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: 432.90  E-value: 1.12e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746702580  172 QIDLFGDAYEFLISNYAANAGKSGGEFFTPQNVSKLIAQLAlhgQKAVNK-IYDPACGSGSLLLQAKKQF---DDHIIEE 247
Cdd:pfam02384   1 SRDLFGDAYEYLLRKFAPNAGKSGGEFFTPREVSKLIVELL---DPKPGEsIYDPACGSGGFLIQAEKFVkehDGDTNDL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746702580  248 GFFGQEINHTTYNLARMNMFLHNINYDKFDITLGDTLLKPQFGDSKPFDAIVSNPPYSVKWvgDSDPTLINDERFAPAGV 327
Cdd:pfam02384  78 SIYGQEKNPTTYRLARMNMILHGIEYDDFHIRHGDTLTSPKFEDDKKFDVVVANPPFSDKW--DANDTLENDPRFRPAYG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746702580  328 LAPKSKADFAFILHALSYLSARGRAAIVTFPGIFYRGGAEQKIRQYLVDNNFVETVISLAPNLFFGTSIAVNILVLSKNK 407
Cdd:pfam02384 156 VAPKSNADLAFLQHIIYYLAPGGRAAVVLPNGVLFRGGAEGKIRKALVDKDLVETVIALPPNLFYNTSIPTCILFLTKNK 235

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 746702580  408 TD--SKTQFIDASGIFKKETNNNVLTDEHIAEILKLFADKADVDHLVKMVDNQAIADNDYNLAVSSYVEAKDERE 480
Cdd:pfam02384 236 AErkGKVLFIDASNEFKKEGKLNILTDEHIEKIIDTFGEFKDVDGFSKSATLEEIAANDYNLNVGRYVGTEEEEE 310
HsdM COG0286
Type I restriction-modification system, DNA methylase subunit [Defense mechanisms];
174-418 1.81e-95

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


Pssm-ID: 440055 [Multi-domain]  Cd Length: 243  Bit Score: 289.39  E-value: 1.81e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746702580 174 DLFGDAYEFLISNYAANAGKSGGEFFTPQNVSKLIAQLALHgqKAVNKIYDPACGSGSLLLQA----KKQFDDHIIEEGF 249
Cdd:COG0286    1 DVLGDAYEYLLRKFAEESGKKAGEFYTPREVVRLMVELLDP--KPGETVYDPACGSGGFLVEAaeylKEHGGDERKKLSL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746702580 250 FGQEINHTTYNLARMNMFLHNInyDKFDITLGDTLLKPQfGDSKPFDAIVSNPPYSVKWVGDSdptLINDERFAPAGVLA 329
Cdd:COG0286   79 YGQEINPTTYRLAKMNLLLHGI--GDPNIELGDTLSNDG-DELEKFDVVLANPPFGGKWKKEE---LKDDLLGRFGYGLP 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746702580 330 PKSKADFAFILHALSYLSARGRAAIVTFPGIFYRGgAEQKIRQYLVDNNFVETVISLAPNLFFGTSIAVNILVLSKNKTD 409
Cdd:COG0286  153 PKSNADLLFLQHILSLLKPGGRAAVVLPDGVLFRG-AEKEIRKKLLENDLLEAIIGLPSNLFYNTGIPTCILFLTKGKPE 231

                        250
                 ....*....|.
gi 746702580 410 --SKTQFIDAS 418
Cdd:COG0286  232 rtGKVLFIDAS 242
HsdM_N pfam12161
HsdM N-terminal domain; This domain is found at the N-terminus of the methylase subunit of ...
 10-158 2.53e-11

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: 60.77  E-value: 2.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746702580   10 LQRRIWQIANDVRGSVDGWDFKQYVLGTLFYRFISEHFVNYIEGGDEsikyatwsdddeniklgKEHVIKEKGYFIYPSQ 89
Cdd:pfam12161   1 LESFLWNAADILRGDVDASEYKEYILPLLFLKRLDDVLEEREEEVLE-----------------LIEPLDSGFGFYIPSE 63

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 746702580   90 LFENVVKNAHNNPNLNTELKDIFTSIESSavgydpENDIKGLFAdfdttSNRLGNTVEDKNKRLAAVLQ 158
Cdd:pfam12161  64 LRWSKLANNLDNDELGENLNDAFPGLEEL------NPDLRGVFM-----KDARGIITLKSPDLLKKVIQ 121
YtxK COG0827
Adenine-specific DNA N6-methylase [Replication, recombination and repair];
199-411 8.06e-10

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


Pssm-ID: 440589 [Multi-domain]  Cd Length: 327  Bit Score: 60.35  E-value: 8.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746702580 199 FTPQNVSKLIAQLA--LHGQKAVnKIYDPACGSGSLLLQAKKQFDDHIIEEGFfgqEINHTTYNLARMNMflhNINYDKF 276
Cdd:COG0827   95 MTPDAIGLLIGYLVekFTKKEGL-RILDPAVGTGNLLTTVLNQLKKKVNAYGV---EVDDLLIRLAAVLA---NLQGHPV 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746702580 277 DITLGDTlLKPQFGDskPFDAIVSNPPYSVKwvgdsdPTLINDERFApagvLAPKSKADFA---FILHALSYLSARGRAA 353
Cdd:COG0827  168 ELFHQDA-LQPLLID--PVDVVISDLPVGYY------PNDERAKRFK----LKADEGHSYAhhlFIEQSLNYLKPGGYLF 234

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 746702580 354 IVTFPGIFyRGGAEQKIRQYLVDNNFVETVISLAPNLFFGTSIAVNILVLSKNKTDSK 411
Cdd:COG0827  235 FLVPSNLF-ESDQAAQLREFLKEKAHIQGLIQLPESLFKNEAAAKSILILQKKGEGTK 291
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 222-350 8.07e-08

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: 52.26  E-value: 8.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746702580 222 IYDPACGSGSLLLQAKKQfddhiieeGF--FGQEINHTTYNLARMNM-FLhniNYDKFDITLGDTLLKPQFGDSkpFDAI 298
Cdd:COG1041   30 VLDPFCGTGTILIEAGLL--------GRrvIGSDIDPKMVEGARENLeHY---GYEDADVIRGDARDLPLADES--VDAI 96

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 746702580 299 VSNPPY--SVKWVGDSDPTLIndERFAP--AGVLAPKSKADFAFILHALSYLSARG 350
Cdd:COG1041   97 VTDPPYgrSSKISGEELLELY--EKALEeaARVLKPGGRVVIVTPRDIDELLEEAG 150
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 217-355 1.24e-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: 46.68  E-value: 1.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746702580 217 KAVNKIYDPACGSG--SLLLqAKKQFDDHIIeegffGQEINHTTYNLARMNMFLHNINyDKFDITLGDTLLKPQFGDSKP 294
Cdd:COG4123   36 KKGGRVLDLGTGTGviALML-AQRSPGARIT-----GVEIQPEAAELARRNVALNGLE-DRITVIHGDLKEFAAELPPGS 108

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 746702580 295 FDAIVSNPPYsvkwvgdsdptlindeRFAPAGVLAPKSKADFA----------FILHALSYLSARGRAAIV 355
Cdd:COG4123  109 FDLVVSNPPY----------------FKAGSGRKSPDEARAIArhedaltledLIRAAARLLKPGGRFALI 163
RF_mod_PrmC TIGR03534
protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein ...
 217-354 3.32e-05

protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein family are HemK (PrmC), a protein once thought to be involved in heme biosynthesis but now recognized to be a protein-glutamine methyltransferase that modifies the peptide chain release factors. All members of the seed alignment are encoded next to the release factor 1 gene (prfA) and confirmed by phylogenetic analysis. SIMBAL analysis (manuscript in prep.) shows the motif [LIV]PRx[DE]TE (in Escherichia coli, IPRPDTE) confers specificity for the release factors rather than for ribosomal protein L3. [Protein fate, Protein modification and repair]


Pssm-ID: 274634 [Multi-domain]  Cd Length: 250  Bit Score: 45.54  E-value: 3.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746702580  217 KAVNKIYDPACGSGSLLLQAKKQFDDHIIeegfFGQEINHTTYNLARMNMFLHNInyDKFDITLGDtLLKPqfGDSKPFD 296
Cdd:TIGR03534  85 KKGPRVLDLGTGSGAIALALAKERPDARV----TAVDISPEALAVARKNARRLGL--ENVEFLQGD-WFEP--LPSGKFD 155

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 746702580  297 AIVSNPPYsvkwVGDSDPTLINDE--RFAPAGVL-APKSKADF--AFILHALSYLSARGRAAI 354
Cdd:TIGR03534 156 LIVSNPPY----IPEADIHLLDPEvrDFEPRLALfGGEDGLDFyrRIIAQAPRLLKPGGWLLL 214
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
150-306 3.06e-04

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 41.81  E-value: 3.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746702580 150 NKRLAAVLQGVAGLPFERFEDNQidlfgdayeflisnyaanagksggeFFTPQNVSKLIAQLA-LHGQKAVNKIYDPACG 228
Cdd:COG2263    1 KRELEIILEKLPGFSNPKVELEQ-------------------------YPTPAELAAELLHLAyLRGDIEGKTVLDLGCG 55

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746702580 229 SG-----SLLLQAKKqfddhiieegFFGQEINHTTYNLARMN--MFLHNINYDKFDITlgdtllkpQFGDSKPFDAIVSN 301
Cdd:COG2263   56 TGmlaigAALLGAKK----------VVGVDIDPEALEIARENaeRLGVRVDFIRADVT--------RIPLGGSVDTVVMN 117


                 ....*
gi 746702580 302 PPYSV 306
Cdd:COG2263  118 PPFGA 122
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 207-320 4.37e-04

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 42.06  E-value: 4.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746702580 207 LIAQ-LALHGQKAVNKIYDPACGSGSLLLQAKKQFDDHIIeegfFGQEINHTTYNLARMNMFLHNINyDKFDITLGDtLL 285
Cdd:COG2890  100 LVELaLALLPAGAPPRVLDLGTGSGAIALALAKERPDARV----TAVDISPDALAVARRNAERLGLE-DRVRFLQGD-LF 173

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 746702580 286 KPqFGDSKPFDAIVSNPPYsvkwVGDSDPTLINDE 320
Cdd:COG2890  174 EP-LPGDGRFDLIVSNPPY----IPEDEIALLPPE 203
UPF0020 pfam01170
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ...
 209-304 6.22e-04

Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated with the THUMP domain that also occurs with RNA modification domains.


Pssm-ID: 395932 [Multi-domain]  Cd Length: 184  Bit Score: 40.80  E-value: 6.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746702580  209 AQLALHGQKAVNKIYDPACGSGSLLLQA-------KKQFDDHIIEEGFFGQEINHTTYNLARMNMflhnINYDKFD-ITL 280
Cdd:pfam01170  19 AMVNLAGWKPGDPLLDPMCGSGTILIEAalmganiAPGKFDARVRAPLYGSDIDRRMVQGARLNA----ENAGVGDlIEF 94

                          90       100
                  ....*....|....*....|....
gi 746702580  281 GDTLLKPQFGDSKPFDAIVSNPPY 304
Cdd:pfam01170  95 VQADAADLPLLEGSVDVIVTNPPY 118
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 207-304 1.23e-03

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 40.92  E-value: 1.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746702580 207 LIAQLALHGQKAVN--KIYDPACGSGSLLLQAKKQFDD-HIIeegffGQEINHTTYNLARMNMFLHNInyDKFDITLGDt 283
Cdd:PRK09328  95 ELVEWALEALLLKEplRVLDLGTGSGAIALALAKERPDaEVT-----AVDISPEALAVARRNAKHGLG--ARVEFLQGD- 166

                         90       100
                 ....*....|....*....|.
gi 746702580 284 LLKPQFGDskPFDAIVSNPPY 304
Cdd:PRK09328 167 WFEPLPGG--RFDLIVSNPPY 185
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 221-305 2.48e-03

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 37.79  E-value: 2.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746702580 221 KIYDPACGSGSLLLQAKKQFDDHIIeegffGQEINHTTYNLARMNMFlhNINYDKFDITLGDtLLKPQFGDSKPFDAIVS 300
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGARVT-----GVDISPVALELARKAAA--ALLADNVEVLKGD-AEELPPEADESFDVIIS 72


                 ....*
gi 746702580 301 NPPYS 305
Cdd:cd02440   73 DPPLH 77
 
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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