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Conserved domains on  [gi|573023248|gb|AHF78784|]
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Type I restriction enzyme, modification subunit [Sodalis praecaptivus]

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 ...
 6-501 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: 613.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573023248    6 QRAELHRQIWAIANNVRGSVDGWDFKQYVLGALFYRFISENFSSYIEAG----DDSIHYAALDDSI-ITDDIKDDAIKTK 80
Cdd:TIGR00497   1 QRNELEKKIWEIANKLRGSVDGWDFKQYVLGGLFYRFISENLCKYINDSerrnDPSFSYANLTDDYeAIDALKDAAIASK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573023248   81 GYFIYPSQLFCNVAAKANTNDRLNADLNSIFVAIESSAYGYPSEADIKGLFADFDTTSNRLGNTVKDKNSRLAAVLKGVE 160
Cdd:TIGR00497  81 GFFIKPSQLFQNVVKSIRENEDLNTTLRDIFDDIEKSELGDGSKESFKGLFKDFNVSEVKLGSTLTIRTEKLKELLTSID 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573023248  161 GLNLGNFNDHQIDLFGDAYEFLISNYAANAGKSGGEFFTPQHVSKLIAQLAMHGQTHVNKIYDPAAGSGSLLLQAKKQFD 240
Cdd:TIGR00497 161 TMELDEFEKNSIDAFGDAYEFLISMYAQNAGKSGGEFFTPQDISELLARIAIGKKDTVDDVYDMACGSGSLLLQVIKVLG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573023248  241 DHIIEEGFFGQEINHTTFNLARMNMFLHNINYDKFDIRLGNTLTEPHFGDEKPFDAIVSNPPYSVKWIGSDDPTLINDER 320
Cdd:TIGR00497 241 EKTSLVSYYGQEINHTTYNLCRMNMILHNIDYANFNIINADTLTTKEWENENGFEVVVSNPPYSISWAGDKKSNLVSDVR 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573023248  321 FVPAGVLAPKSKADFAFVLHALNYLSAKGRAAIVCFPGIFYRGGAEQKIRKYLVDNNYVETVISLAPNLFFGTTIAVNIL 400
Cdd:TIGR00497 321 FKDAGTLAPNSKADLAFVLHALYVLGQEGTAAIVCFPGILYREGKEQTIRKYLVDQNFVDAVIQLPSNLFSTTSIATSIL 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573023248  401 VLSKHKTDTSVQFIDASGLFKKETNNNILTDAHIAQIMQVFCSKSDVDHLAKSVAFEEVAGNDYNLSVSSYVEAKDTREI 480
Cdd:TIGR00497 401 VLKKNRKKDPIFFIDGSNEFVREKKNNRLSPKNIEKIVDCFNSKKEEANFAKSVERDKIRESNYDLTVGKYVNSEAEKEE 480

                         490       500
                  ....*....|....*....|.
gi 573023248  481 VDITELNAELNTTVSKIDQLR 501
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 ...
 6-501 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: 613.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573023248    6 QRAELHRQIWAIANNVRGSVDGWDFKQYVLGALFYRFISENFSSYIEAG----DDSIHYAALDDSI-ITDDIKDDAIKTK 80
Cdd:TIGR00497   1 QRNELEKKIWEIANKLRGSVDGWDFKQYVLGGLFYRFISENLCKYINDSerrnDPSFSYANLTDDYeAIDALKDAAIASK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573023248   81 GYFIYPSQLFCNVAAKANTNDRLNADLNSIFVAIESSAYGYPSEADIKGLFADFDTTSNRLGNTVKDKNSRLAAVLKGVE 160
Cdd:TIGR00497  81 GFFIKPSQLFQNVVKSIRENEDLNTTLRDIFDDIEKSELGDGSKESFKGLFKDFNVSEVKLGSTLTIRTEKLKELLTSID 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573023248  161 GLNLGNFNDHQIDLFGDAYEFLISNYAANAGKSGGEFFTPQHVSKLIAQLAMHGQTHVNKIYDPAAGSGSLLLQAKKQFD 240
Cdd:TIGR00497 161 TMELDEFEKNSIDAFGDAYEFLISMYAQNAGKSGGEFFTPQDISELLARIAIGKKDTVDDVYDMACGSGSLLLQVIKVLG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573023248  241 DHIIEEGFFGQEINHTTFNLARMNMFLHNINYDKFDIRLGNTLTEPHFGDEKPFDAIVSNPPYSVKWIGSDDPTLINDER 320
Cdd:TIGR00497 241 EKTSLVSYYGQEINHTTYNLCRMNMILHNIDYANFNIINADTLTTKEWENENGFEVVVSNPPYSISWAGDKKSNLVSDVR 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573023248  321 FVPAGVLAPKSKADFAFVLHALNYLSAKGRAAIVCFPGIFYRGGAEQKIRKYLVDNNYVETVISLAPNLFFGTTIAVNIL 400
Cdd:TIGR00497 321 FKDAGTLAPNSKADLAFVLHALYVLGQEGTAAIVCFPGILYREGKEQTIRKYLVDQNFVDAVIQLPSNLFSTTSIATSIL 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573023248  401 VLSKHKTDTSVQFIDASGLFKKETNNNILTDAHIAQIMQVFCSKSDVDHLAKSVAFEEVAGNDYNLSVSSYVEAKDTREI 480
Cdd:TIGR00497 401 VLKKNRKKDPIFFIDGSNEFVREKKNNRLSPKNIEKIVDCFNSKKEEANFAKSVERDKIRESNYDLTVGKYVNSEAEKEE 480

                         490       500
                  ....*....|....*....|.
gi 573023248  481 VDITELNAELNTTVSKIDQLR 501
Cdd:TIGR00497 481 LDIKVLNHSIDEIVDKQKDLR 501
N6_Mtase pfam02384
N-6 DNA Methylase; Restriction-modification (R-M) systems protect a bacterial cell against ...
 171-479 1.33e-164

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: 468.34  E-value: 1.33e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573023248  171 QIDLFGDAYEFLISNYAANAGKSGGEFFTPQHVSKLIAQLAmhgQTHVNK-IYDPAAGSGSLLLQAKKQF---DDHIIEE 246
Cdd:pfam02384   1 SRDLFGDAYEYLLRKFAPNAGKSGGEFFTPREVSKLIVELL---DPKPGEsIYDPACGSGGFLIQAEKFVkehDGDTNDL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573023248  247 GFFGQEINHTTFNLARMNMFLHNINYDKFDIRLGNTLTEPHFGDEKPFDAIVSNPPYSVKWigSDDPTLINDERFVPAGV 326
Cdd:pfam02384  78 SIYGQEKNPTTYRLARMNMILHGIEYDDFHIRHGDTLTSPKFEDDKKFDVVVANPPFSDKW--DANDTLENDPRFRPAYG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573023248  327 LAPKSKADFAFVLHALNYLSAKGRAAIVCFPGIFYRGGAEQKIRKYLVDNNYVETVISLAPNLFFGTTIAVNILVLSKHK 406
Cdd:pfam02384 156 VAPKSNADLAFLQHIIYYLAPGGRAAVVLPNGVLFRGGAEGKIRKALVDKDLVETVIALPPNLFYNTSIPTCILFLTKNK 235

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 573023248  407 TDT--SVQFIDASGLFKKETNNNILTDAHIAQIMQVFCSKSDVDHLAKSVAFEEVAGNDYNLSVSSYVEAKDTRE 479
Cdd:pfam02384 236 AERkgKVLFIDASNEFKKEGKLNILTDEHIEKIIDTFGEFKDVDGFSKSATLEEIAANDYNLNVGRYVGTEEEEE 310
HsdM COG0286
Type I restriction-modification system, DNA methylase subunit [Defense mechanisms];
173-417 2.02e-96

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


Pssm-ID: 440055 [Multi-domain]  Cd Length: 243  Bit Score: 292.09  E-value: 2.02e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573023248 173 DLFGDAYEFLISNYAANAGKSGGEFFTPQHVSKLIAQLAMHGqtHVNKIYDPAAGSGSLLLQA----KKQFDDHIIEEGF 248
Cdd:COG0286    1 DVLGDAYEYLLRKFAEESGKKAGEFYTPREVVRLMVELLDPK--PGETVYDPACGSGGFLVEAaeylKEHGGDERKKLSL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573023248 249 FGQEINHTTFNLARMNMFLHNInyDKFDIRLGNTLTEpHFGDEKPFDAIVSNPPYSVKWigsDDPTLINDERFVPAGVLA 328
Cdd:COG0286   79 YGQEINPTTYRLAKMNLLLHGI--GDPNIELGDTLSN-DGDELEKFDVVLANPPFGGKW---KKEELKDDLLGRFGYGLP 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573023248 329 PKSKADFAFVLHALNYLSAKGRAAIVCFPGIFYRGgAEQKIRKYLVDNNYVETVISLAPNLFFGTTIAVNILVLSKHKTD 408
Cdd:COG0286  153 PKSNADLLFLQHILSLLKPGGRAAVVLPDGVLFRG-AEKEIRKKLLENDLLEAIIGLPSNLFYNTGIPTCILFLTKGKPE 231

                        250
                 ....*....|.
gi 573023248 409 T--SVQFIDAS 417
Cdd:COG0286  232 RtgKVLFIDAS 242
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 220-304 4.63e-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: 37.02  E-value: 4.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573023248 220 KIYDPAAGSGSLLLQAKKQFDDHIIeegffGQEINHTTFNLARMNMFlhNINYDKFDIRLGNtLTEPHFGDEKPFDAIVS 299
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGARVT-----GVDISPVALELARKAAA--ALLADNVEVLKGD-AEELPPEADESFDVIIS 72


                 ....*
gi 573023248 300 NPPYS 304
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 ...
 6-501 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: 613.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573023248    6 QRAELHRQIWAIANNVRGSVDGWDFKQYVLGALFYRFISENFSSYIEAG----DDSIHYAALDDSI-ITDDIKDDAIKTK 80
Cdd:TIGR00497   1 QRNELEKKIWEIANKLRGSVDGWDFKQYVLGGLFYRFISENLCKYINDSerrnDPSFSYANLTDDYeAIDALKDAAIASK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573023248   81 GYFIYPSQLFCNVAAKANTNDRLNADLNSIFVAIESSAYGYPSEADIKGLFADFDTTSNRLGNTVKDKNSRLAAVLKGVE 160
Cdd:TIGR00497  81 GFFIKPSQLFQNVVKSIRENEDLNTTLRDIFDDIEKSELGDGSKESFKGLFKDFNVSEVKLGSTLTIRTEKLKELLTSID 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573023248  161 GLNLGNFNDHQIDLFGDAYEFLISNYAANAGKSGGEFFTPQHVSKLIAQLAMHGQTHVNKIYDPAAGSGSLLLQAKKQFD 240
Cdd:TIGR00497 161 TMELDEFEKNSIDAFGDAYEFLISMYAQNAGKSGGEFFTPQDISELLARIAIGKKDTVDDVYDMACGSGSLLLQVIKVLG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573023248  241 DHIIEEGFFGQEINHTTFNLARMNMFLHNINYDKFDIRLGNTLTEPHFGDEKPFDAIVSNPPYSVKWIGSDDPTLINDER 320
Cdd:TIGR00497 241 EKTSLVSYYGQEINHTTYNLCRMNMILHNIDYANFNIINADTLTTKEWENENGFEVVVSNPPYSISWAGDKKSNLVSDVR 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573023248  321 FVPAGVLAPKSKADFAFVLHALNYLSAKGRAAIVCFPGIFYRGGAEQKIRKYLVDNNYVETVISLAPNLFFGTTIAVNIL 400
Cdd:TIGR00497 321 FKDAGTLAPNSKADLAFVLHALYVLGQEGTAAIVCFPGILYREGKEQTIRKYLVDQNFVDAVIQLPSNLFSTTSIATSIL 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573023248  401 VLSKHKTDTSVQFIDASGLFKKETNNNILTDAHIAQIMQVFCSKSDVDHLAKSVAFEEVAGNDYNLSVSSYVEAKDTREI 480
Cdd:TIGR00497 401 VLKKNRKKDPIFFIDGSNEFVREKKNNRLSPKNIEKIVDCFNSKKEEANFAKSVERDKIRESNYDLTVGKYVNSEAEKEE 480

                         490       500
                  ....*....|....*....|.
gi 573023248  481 VDITELNAELNTTVSKIDQLR 501
Cdd:TIGR00497 481 LDIKVLNHSIDEIVDKQKDLR 501
N6_Mtase pfam02384
N-6 DNA Methylase; Restriction-modification (R-M) systems protect a bacterial cell against ...
 171-479 1.33e-164

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: 468.34  E-value: 1.33e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573023248  171 QIDLFGDAYEFLISNYAANAGKSGGEFFTPQHVSKLIAQLAmhgQTHVNK-IYDPAAGSGSLLLQAKKQF---DDHIIEE 246
Cdd:pfam02384   1 SRDLFGDAYEYLLRKFAPNAGKSGGEFFTPREVSKLIVELL---DPKPGEsIYDPACGSGGFLIQAEKFVkehDGDTNDL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573023248  247 GFFGQEINHTTFNLARMNMFLHNINYDKFDIRLGNTLTEPHFGDEKPFDAIVSNPPYSVKWigSDDPTLINDERFVPAGV 326
Cdd:pfam02384  78 SIYGQEKNPTTYRLARMNMILHGIEYDDFHIRHGDTLTSPKFEDDKKFDVVVANPPFSDKW--DANDTLENDPRFRPAYG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573023248  327 LAPKSKADFAFVLHALNYLSAKGRAAIVCFPGIFYRGGAEQKIRKYLVDNNYVETVISLAPNLFFGTTIAVNILVLSKHK 406
Cdd:pfam02384 156 VAPKSNADLAFLQHIIYYLAPGGRAAVVLPNGVLFRGGAEGKIRKALVDKDLVETVIALPPNLFYNTSIPTCILFLTKNK 235

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 573023248  407 TDT--SVQFIDASGLFKKETNNNILTDAHIAQIMQVFCSKSDVDHLAKSVAFEEVAGNDYNLSVSSYVEAKDTRE 479
Cdd:pfam02384 236 AERkgKVLFIDASNEFKKEGKLNILTDEHIEKIIDTFGEFKDVDGFSKSATLEEIAANDYNLNVGRYVGTEEEEE 310
HsdM COG0286
Type I restriction-modification system, DNA methylase subunit [Defense mechanisms];
173-417 2.02e-96

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


Pssm-ID: 440055 [Multi-domain]  Cd Length: 243  Bit Score: 292.09  E-value: 2.02e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573023248 173 DLFGDAYEFLISNYAANAGKSGGEFFTPQHVSKLIAQLAMHGqtHVNKIYDPAAGSGSLLLQA----KKQFDDHIIEEGF 248
Cdd:COG0286    1 DVLGDAYEYLLRKFAEESGKKAGEFYTPREVVRLMVELLDPK--PGETVYDPACGSGGFLVEAaeylKEHGGDERKKLSL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573023248 249 FGQEINHTTFNLARMNMFLHNInyDKFDIRLGNTLTEpHFGDEKPFDAIVSNPPYSVKWigsDDPTLINDERFVPAGVLA 328
Cdd:COG0286   79 YGQEINPTTYRLAKMNLLLHGI--GDPNIELGDTLSN-DGDELEKFDVVLANPPFGGKW---KKEELKDDLLGRFGYGLP 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573023248 329 PKSKADFAFVLHALNYLSAKGRAAIVCFPGIFYRGgAEQKIRKYLVDNNYVETVISLAPNLFFGTTIAVNILVLSKHKTD 408
Cdd:COG0286  153 PKSNADLLFLQHILSLLKPGGRAAVVLPDGVLFRG-AEKEIRKKLLENDLLEAIIGLPSNLFYNTGIPTCILFLTKGKPE 231

                        250
                 ....*....|.
gi 573023248 409 T--SVQFIDAS 417
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 ...
 10-157 9.86e-13

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: 65.01  E-value: 9.86e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573023248   10 LHRQIWAIANNVRGSVDGWDFKQYVLGALFYRFISENFSSYIEAGDDSIHyaalddsiitddikddAIKTKGYFIYPSQL 89
Cdd:pfam12161   1 LESFLWNAADILRGDVDASEYKEYILPLLFLKRLDDVLEEREEEVLELIE----------------PLDSGFGFYIPSEL 64

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 573023248   90 FCNVAAKANTNDRLNADLNSIFVAIESsaygypSEADIKGLFAdfdttSNRLGNTVKDKNSRLAAVLK 157
Cdd:pfam12161  65 RWSKLANNLDNDELGENLNDAFPGLEE------LNPDLRGVFM-----KDARGIITLKSPDLLKKVIQ 121
YtxK COG0827
Adenine-specific DNA N6-methylase [Replication, recombination and repair];
198-409 3.46e-09

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


Pssm-ID: 440589 [Multi-domain]  Cd Length: 327  Bit Score: 58.42  E-value: 3.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573023248 198 FTPQHVSKLIAQLA--MHGQTHVnKIYDPAAGSGSLLLQAKKQFDDHIIEEGFfgqEINHTTFNLARMNMflhNINYDKF 275
Cdd:COG0827   95 MTPDAIGLLIGYLVekFTKKEGL-RILDPAVGTGNLLTTVLNQLKKKVNAYGV---EVDDLLIRLAAVLA---NLQGHPV 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573023248 276 DIRLGNTLTEPHfgdEKPFDAIVSNPPYSVKwigSDDptlINDERFvpagVLAPKSKADFA---FVLHALNYLSAKGRAA 352
Cdd:COG0827  168 ELFHQDALQPLL---IDPVDVVISDLPVGYY---PND---ERAKRF----KLKADEGHSYAhhlFIEQSLNYLKPGGYLF 234

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 573023248 353 IVCFPGIFyRGGAEQKIRKYLVDNNYVETVISLAPNLFFGTTIAVNILVLSKHKTDT 409
Cdd:COG0827  235 FLVPSNLF-ESDQAAQLREFLKEKAHIQGLIQLPESLFKNEAAAKSILILQKKGEGT 290
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 221-340 3.19e-06

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: 47.25  E-value: 3.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573023248 221 IYDPAAGSGSLLLQAKKQfddhiieeGF--FGQEINHTTFNLARMNM-FLhniNYDKFDIRLGNTlTEPHFGDEKpFDAI 297
Cdd:COG1041   30 VLDPFCGTGTILIEAGLL--------GRrvIGSDIDPKMVEGARENLeHY---GYEDADVIRGDA-RDLPLADES-VDAI 96

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 573023248 298 VSNPPY--SVKWIGSDDPTLIndERFVP--AGVLAPKSKAdfAFVLH 340
Cdd:COG1041   97 VTDPPYgrSSKISGEELLELY--EKALEeaARVLKPGGRV--VIVTP 139
RF_mod_PrmC TIGR03534
protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein ...
 219-353 1.78e-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: 46.31  E-value: 1.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573023248  219 NKIYDPAAGSGSLLLQAKKQFDDHIIeegfFGQEINHTTFNLARMNMFLHNInyDKFDIRLGNTLTepHFGDEKpFDAIV 298
Cdd:TIGR03534  88 PRVLDLGTGSGAIALALAKERPDARV----TAVDISPEALAVARKNARRLGL--ENVEFLQGDWFE--PLPSGK-FDLIV 158

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 573023248  299 SNPPYsvkwIGSDDPTLINDE--RFVPAGVL-APKSKADF--AFVLHALNYLSAKGRAAI 353
Cdd:TIGR03534 159 SNPPY----IPEADIHLLDPEvrDFEPRLALfGGEDGLDFyrRIIAQAPRLLKPGGWLLL 214
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
197-305 6.93e-04

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 41.04  E-value: 6.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573023248 197 FFTPqhvSKLIAQL----AMHGQTHVNKIYDPAAGSG-----SLLLQAKKqfddhiieegFFGQEINHTTFNLARMN--M 265
Cdd:COG2263   24 YPTP---AELAAELlhlaYLRGDIEGKTVLDLGCGTGmlaigAALLGAKK----------VVGVDIDPEALEIARENaeR 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 573023248 266 FLHNINYDKFDIRlgntltepHFGDEKPFDAIVSNPPYSV 305
Cdd:COG2263   91 LGVRVDFIRADVT--------RIPLGGSVDTVVMNPPFGA 122
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 220-303 1.07e-03

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: 40.90  E-value: 1.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573023248 220 KIYDPAAGSG--SLLLqAKKQFDDHIIeegffGQEINHTTFNLARMNMFLHNINyDKFDIRLGNtLTE--PHFGDEKpFD 295
Cdd:COG4123   40 RVLDLGTGTGviALML-AQRSPGARIT-----GVEIQPEAAELARRNVALNGLE-DRITVIHGD-LKEfaAELPPGS-FD 110


                 ....*...
gi 573023248 296 AIVSNPPY 303
Cdd:COG4123  111 LVVSNPPY 118
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 227-319 1.67e-03

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 40.52  E-value: 1.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573023248 227 GSGSLLLQAKKQFDDHIIeegfFGQEINHTTFNLARMNMFLHNINyDKFDIRLGNtLTEPhFGDEKPFDAIVSNPPYsvk 306
Cdd:COG2890  122 GSGAIALALAKERPDARV----TAVDISPDALAVARRNAERLGLE-DRVRFLQGD-LFEP-LPGDGRFDLIVSNPPY--- 191

                         90
                 ....*....|...
gi 573023248 307 wIGSDDPTLINDE 319
Cdd:COG2890  192 -IPEDEIALLPPE 203
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 220-304 4.63e-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: 37.02  E-value: 4.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573023248 220 KIYDPAAGSGSLLLQAKKQFDDHIIeegffGQEINHTTFNLARMNMFlhNINYDKFDIRLGNtLTEPHFGDEKPFDAIVS 299
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGARVT-----GVDISPVALELARKAAA--ALLADNVEVLKGD-AEELPPEADESFDVIIS 72


                 ....*
gi 573023248 300 NPPYS 304
Cdd:cd02440   73 DPPLH 77
UPF0020 pfam01170
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ...
 196-303 5.98e-03

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: 38.11  E-value: 5.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573023248  196 EFFTPQHVSKLIAQlAMH---GQTHVNKIYDPAAGSGSLLLQA-------KKQFDDHIIEEGFFGQEINHTTFNLARMNM 265
Cdd:pfam01170   5 PFNGPAPLKETLAA-AMVnlaGWKPGDPLLDPMCGSGTILIEAalmganiAPGKFDARVRAPLYGSDIDRRMVQGARLNA 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 573023248  266 ----FLHNINYDKFDIRlgnTLTEPhfgdEKPFDAIVSNPPY 303
Cdd:pfam01170  84 enagVGDLIEFVQADAA---DLPLL----EGSVDVIVTNPPY 118
 
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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