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Conserved domains on  [gi|157093019|gb|ABV22164|]
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conserved hypothetical protein [Perkinsus chesapeaki]

Protein Classification

SAM-dependent methyltransferase( domain architecture ID 1905023)

SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor

EC:  2.1.1.-
Gene Ontology:  GO:1904047|GO:0008168
PubMed:  12826405|12504684
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG4076 super family cl44002
Predicted RNA methylase [General function prediction only];
41-180 4.11e-30

Predicted RNA methylase [General function prediction only];


The actual alignment was detected with superfamily member COG4076:

Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 114.36  E-value: 4.11e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157093019  41 HDLMPKDKPRPEGYIRAFEANKDRlrGKAVLDVGCGTGVLSMLCAKICQpAQIIAAEATESTARIAETLIQQNELQGIIT 120
Cdd:COG4076   12 HHPMLNDVERNDAFKAAIERVVKP--GDVVLDIGTGSGLLSMLAARAGA-KKVYAVEVNPDIAAVARRIIAANGLSDRIT 88

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157093019 121 VVNRPIEMLDLSAPVDAIVSEWMGFYAFHESMLDSVLYARDHWLKPGGLLLPDSCRLWAA 180
Cdd:COG4076   89 VINADATDLDLPEKADVIISEMLDTALLDEGQVPILNHARKRLLKPGGRIIPERITNAAQ 148
 
Name Accession Description Interval E-value
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
41-180 4.11e-30

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 114.36  E-value: 4.11e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157093019  41 HDLMPKDKPRPEGYIRAFEANKDRlrGKAVLDVGCGTGVLSMLCAKICQpAQIIAAEATESTARIAETLIQQNELQGIIT 120
Cdd:COG4076   12 HHPMLNDVERNDAFKAAIERVVKP--GDVVLDIGTGSGLLSMLAARAGA-KKVYAVEVNPDIAAVARRIIAANGLSDRIT 88

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157093019 121 VVNRPIEMLDLSAPVDAIVSEWMGFYAFHESMLDSVLYARDHWLKPGGLLLPDSCRLWAA 180
Cdd:COG4076   89 VINADATDLDLPEKADVIISEMLDTALLDEGQVPILNHARKRLLKPGGRIIPERITNAAQ 148
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 70-168 4.36e-10

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 56.03  E-value: 4.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157093019   70 VLDVGCGTGVLSMLCAKICQpAQIIAAEATESTARIAETLIQQNELQgiITVVNRPIEMLDL-SAPVDAIVSeWMGFYAF 148
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGG-ARVTGVDLSPEMLERARERAAEAGLN--VEFVQGDAEDLPFpDGSFDLVVS-SGVLHHL 76

                          90       100
                  ....*....|....*....|..
gi 157093019  149 HESMLDSVL--YARdhWLKPGG 168
Cdd:pfam13649  77 PDPDLEAALreIAR--VLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 70-171 2.99e-08

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: 50.89  E-value: 2.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157093019  70 VLDVGCGTGVLSMLCAKICqPAQIIAAEATESTARIAETLIQQNELQGiITVVNRPIEMLDLSAP--VDAIVSeWMGFYA 147
Cdd:cd02440    2 VLDLGCGTGALALALASGP-GARVTGVDISPVALELARKAAAALLADN-VEVLKGDAEELPPEADesFDVIIS-DPPLHH 78

                         90       100
                 ....*....|....*....|....
gi 157093019 148 FHESMLDSVLYARDHwLKPGGLLL 171
Cdd:cd02440   79 LVEDLARFLEEARRL-LKPGGVLV 101
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
65-86 2.78e-04

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 41.68  E-value: 2.78e-04
                         10        20
                 ....*....|....*....|..
gi 157093019  65 LRGKAVLDVGCGTGVLSMLCAK 86
Cdd:PRK00517 118 LPGKTVLDVGCGSGILAIAAAK 139
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 68-171 2.80e-03

malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin biosynthetic gene clusters in proteobacteria, firmicutes, green-sulfur bacteria, fusobacterium and bacteroides, carries out an enzymatic step prior to the formation of pimeloyl-CoA, namely O-methylation of the malonyl group preferentially while on acyl carrier protein. The enzyme is recognizable as a methyltransferase by homology. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 38.81  E-value: 2.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157093019   68 KAVLDVGCGTGVLSMLCAKICQPAQIIAAEATESTARIAETLIQQNelqgIITVVNRpIEMLDLSAP-VDAIVSEwMGFY 146
Cdd:TIGR02072  36 ASVLDIGCGTGYLTRALLKRFPQAEFIALDISAGMLAQAKTKLSEN----VQFICGD-AEKLPLEDSsFDLIVSN-LALQ 109

                          90       100
                  ....*....|....*....|....*
gi 157093019  147 AFHEsmLDSVLYARDHWLKPGGLLL 171
Cdd:TIGR02072 110 WCDD--LSQALSELARVLKPGGLLA 132
 
Name Accession Description Interval E-value
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
41-180 4.11e-30

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 114.36  E-value: 4.11e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157093019  41 HDLMPKDKPRPEGYIRAFEANKDRlrGKAVLDVGCGTGVLSMLCAKICQpAQIIAAEATESTARIAETLIQQNELQGIIT 120
Cdd:COG4076   12 HHPMLNDVERNDAFKAAIERVVKP--GDVVLDIGTGSGLLSMLAARAGA-KKVYAVEVNPDIAAVARRIIAANGLSDRIT 88

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157093019 121 VVNRPIEMLDLSAPVDAIVSEWMGFYAFHESMLDSVLYARDHWLKPGGLLLPDSCRLWAA 180
Cdd:COG4076   89 VINADATDLDLPEKADVIISEMLDTALLDEGQVPILNHARKRLLKPGGRIIPERITNAAQ 148
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 67-171 3.19e-10

Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 58.02  E-value: 3.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157093019  67 GKAVLDVGCGTGVLSMLCAKICQpAQIIAAEATESTARIAETLIQQNELQGIITVVNRPIEMLDLSAPVDAIVS----EW 142
Cdd:COG2230   52 GMRVLDIGCGWGGLALYLARRYG-VRVTGVTLSPEQLEYARERAAEAGLADRVEVRLADYRDLPADGQFDAIVSigmfEH 130

                         90       100
                 ....*....|....*....|....*....
gi 157093019 143 MGfYAFHESMLDSVlyarDHWLKPGGLLL 171
Cdd:COG2230  131 VG-PENYPAYFAKV----ARLLKPGGRLL 154
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 70-168 4.36e-10

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 56.03  E-value: 4.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157093019   70 VLDVGCGTGVLSMLCAKICQpAQIIAAEATESTARIAETLIQQNELQgiITVVNRPIEMLDL-SAPVDAIVSeWMGFYAF 148
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGG-ARVTGVDLSPEMLERARERAAEAGLN--VEFVQGDAEDLPFpDGSFDLVVS-SGVLHHL 76

                          90       100
                  ....*....|....*....|..
gi 157093019  149 HESMLDSVL--YARdhWLKPGG 168
Cdd:pfam13649  77 PDPDLEAALreIAR--VLKPGG 96
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 66-170 8.49e-10

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: 58.23  E-value: 8.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157093019  66 RGKAVLDVGCGTGVLSMLCAKICQPAQIIAAEATESTARIAETLIQQNELQGIITVVNRPI-EMLDLSAP--VDAIVS-- 140
Cdd:COG4123   37 KGGRVLDLGTGTGVIALMLAQRSPGARITGVEIQPEAAELARRNVALNGLEDRITVIHGDLkEFAAELPPgsFDLVVSnp 116

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 157093019 141 ----EWMGF--------YAFHESM--LDSVLYARDHWLKPGGLL 170
Cdd:COG4123  117 pyfkAGSGRkspdearaIARHEDAltLEDLIRAAARLLKPGGRF 160
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
66-171 7.02e-09

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 52.52  E-value: 7.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157093019  66 RGKAVLDVGCGTGVLSMLCAKICQPAQIIAAEATESTARIAETLIQQnelqgiITVVNRPIEMLDLSAPVDAIVSewmgF 145
Cdd:COG4106    1 PPRRVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARARLPN------VRFVVADLRDLDPPEPFDLVVS----N 70

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 157093019 146 YAFHesmldsvlYARDH---------WLKPGGLLL 171
Cdd:COG4106   71 AALH--------WLPDHaallarlaaALAPGGVLA 97
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 70-171 2.99e-08

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: 50.89  E-value: 2.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157093019  70 VLDVGCGTGVLSMLCAKICqPAQIIAAEATESTARIAETLIQQNELQGiITVVNRPIEMLDLSAP--VDAIVSeWMGFYA 147
Cdd:cd02440    2 VLDLGCGTGALALALASGP-GARVTGVDISPVALELARKAAAALLADN-VEVLKGDAEELPPEADesFDVIIS-DPPLHH 78

                         90       100
                 ....*....|....*....|....
gi 157093019 148 FHESMLDSVLYARDHwLKPGGLLL 171
Cdd:cd02440   79 LVEDLARFLEEARRL-LKPGGVLV 101
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 65-171 1.31e-07

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 49.63  E-value: 1.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157093019  65 LRGKAVLDVGCGTGVLSMLCAKICqpAQIIAAEATESTARIAETLIQQNElqgiITVVNRPIEMLDLS-APVDAIVSewm 143
Cdd:COG2227   23 PAGGRVLDVGCGTGRLALALARRG--ADVTGVDISPEALEIARERAAELN----VDFVQGDLEDLPLEdGSFDLVIC--- 93

                         90       100       110
                 ....*....|....*....|....*....|...
gi 157093019 144 gFYAFH-----ESMLDSVLyardHWLKPGGLLL 171
Cdd:COG2227   94 -SEVLEhlpdpAALLRELA----RLLKPGGLLL 121
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 66-183 3.17e-07

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 48.84  E-value: 3.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157093019  66 RGKAVLDVGCGTGVLSMLCAKicQPAQIIAAEATESTARIAETLIQQNELQgiITVVNRPIEMLDLS-APVDAIVSewmg 144
Cdd:COG2226   22 PGARVLDLGCGTGRLALALAE--RGARVTGVDISPEMLELARERAAEAGLN--VEFVVGDAEDLPFPdGSFDLVIS---- 93

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 157093019 145 FYAFH-----ESMLDSVlyARdhWLKPGGLLL------PDSCRLWAAVAS 183
Cdd:COG2226   94 SFVLHhlpdpERALAEI--AR--VLKPGGRLVvvdfspPDLAELEELLAE 139
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
65-140 1.94e-06

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 47.59  E-value: 1.94e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157093019  65 LRGKAVLDVGCGTGVLSmLCAKICQPAQIIAAEATESTARIAETLIqqNELQGIITVVNRPIEMLDLSAPVDAIVS 140
Cdd:COG2263   44 IEGKTVLDLGCGTGMLA-IGAALLGAKKVVGVDIDPEALEIARENA--ERLGVRVDFIRADVTRIPLGGSVDTVVM 116
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 71-171 5.91e-06

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 44.19  E-value: 5.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157093019   71 LDVGCGTGVLSMLCAKICqpAQIIAAEATESTARIAETLIQQNELQGIITvvnrPIEMLDL-SAPVDAIVSEWMgfyAFH 149
Cdd:pfam08241   1 LDVGCGTGLLTELLARLG--ARVTGVDISPEMLELAREKAPREGLTFVVG----DAEDLPFpDNSFDLVLSSEV---LHH 71

                          90       100
                  ....*....|....*....|....
gi 157093019  150 ESMLDSVL--YARdhWLKPGGLLL 171
Cdd:pfam08241  72 VEDPERALreIAR--VLKPGGILI 93
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
29-171 6.03e-06

Predicted methyltransferase, contains TPR repeat [General function prediction only];


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 46.14  E-value: 6.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157093019  29 DGYFNSYDDLSVHDLmpkDKPRPEGYIRAFEANKDRLRGKAVLDVGCGTGVLSMLCAKICQpaQIIAAEATESTARIAET 108
Cdd:COG4976   12 DQYADSYDAALVEDL---GYEAPALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGY--RLTGVDLSEEMLAKARE 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157093019 109 LIQQNELqgiitVVNRPIEMLDLSAPVDAIVSeWMGFYAFHEsmLDSVLYARDHWLKPGGLLL 171
Cdd:COG4976   87 KGVYDRL-----LVADLADLAEPDGRFDLIVA-ADVLTYLGD--LAAVFAGVARALKPGGLFI 141
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 71-170 6.14e-06

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 44.28  E-value: 6.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157093019   71 LDVGCGTGVLSMLCAKICQPAQIIAAEATESTARIAETLIQQNELQGIITVVNRPIEMLDL-SAPVDAIVSewmgFYAFH 149
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERLAALGLLNAVRVELFQLDLGELdPGSFDVVVA----SNVLH 76

                          90       100
                  ....*....|....*....|..
gi 157093019  150 E-SMLDSVLYARDHWLKPGGLL 170
Cdd:pfam08242  77 HlADPRAVLRNIRRLLKPGGVL 98
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 49-171 1.34e-05

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 45.91  E-value: 1.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157093019  49 PRPEgyI-----RAFEANKDRlRGKAVLDVGCGTGVLSMLCAKICQPAQIIAAEATESTARIAETLIQQNELQGIITVVN 123
Cdd:COG2890   93 PRPE--TeelveLALALLPAG-APPRVLDLGTGSGAIALALAKERPDARVTAVDISPDALAVARRNAERLGLEDRVRFLQ 169

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157093019 124 RPI-EMLDLSAPVDAIVS--------EW---MGFYAFHE--SMLDS-----VLYAR-----DHWLKPGGLLL 171
Cdd:COG2890  170 GDLfEPLPGDGRFDLIVSnppyipedEIallPPEVRDHEprLALDGgedglDFYRRiiaqaPRLLKPGGWLL 241
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 67-194 1.73e-05

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 44.33  E-value: 1.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157093019   67 GKAVLDVGCGTGVLSMLCA-KICQPAQIIAAEATESTARIAETLIQQNELQGiITVVNRPIEMLDLS---APVDAIVSew 142
Cdd:pfam13847   4 GMRVLDLGCGTGHLSFELAeELGPNAEVVGIDISEEAIEKARENAQKLGFDN-VEFEQGDIEELPELledDKFDVVIS-- 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 157093019  143 mgFYAFH-----ESMLDSVLYArdhwLKPGGLLLPDSCRLWAAVAseDIWRRDNVEY 194
Cdd:pfam13847  81 --NCVLNhipdpDKVLQEILRV----LKPGGRLIISDPDSLAELP--AHVKEDSTYY 129
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
65-122 2.09e-05

Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 45.55  E-value: 2.09e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157093019  65 LRGKAVLDVGCGTGVLSMLCAKiCQPAQIIA----AEATESTariAETlIQQNELQGIITVV 122
Cdd:COG2264  147 KPGKTVLDVGCGSGILAIAAAK-LGAKRVLAvdidPVAVEAA---REN-AELNGVEDRIEVV 203
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 70-171 3.58e-05

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: 44.03  E-value: 3.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157093019  70 VLDVGCGTGVLSMLCAKICQPAQIIA----AEATESTARIAEtliqQNELQGIITVVN---RPIEmldlSAPVDAIVS-- 140
Cdd:COG2813   53 VLDLGCGYGVIGLALAKRNPEARVTLvdvnARAVELARANAA----ANGLENVEVLWSdglSGVP----DGSFDLILSnp 124

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 157093019 141 ----EWMGFYAFHESMLDSvlyARDHwLKPGGLLL 171
Cdd:COG2813  125 pfhaGRAVDKEVAHALIAD---AARH-LRPGGELW 155
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 57-171 3.93e-05

SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 43.75  E-value: 3.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157093019  57 AFEANKDRLRGKA-VLDVGCGTGVLSMLCAKICQpAQIIAAEATESTARIAETLIQQNELQGiITVVNRPIEMLD--LSA 133
Cdd:COG0500   16 ALLALLERLPKGGrVLDLGCGTGRNLLALAARFG-GRVIGIDLSPEAIALARARAAKAGLGN-VEFLVADLAELDplPAE 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 157093019 134 PVDAIVSewmgFYAFH-------ESMLDSVLYArdhwLKPGGLLL 171
Cdd:COG0500   94 SFDLVVA----FGVLHhlppeerEALLRELARA----LKPGGVLL 130
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
65-86 2.78e-04

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 41.68  E-value: 2.78e-04
                         10        20
                 ....*....|....*....|..
gi 157093019  65 LRGKAVLDVGCGTGVLSMLCAK 86
Cdd:PRK00517 118 LPGKTVLDVGCGSGILAIAAAK 139
rsmC PRK09489
16S rRNA (guanine(1207)-N(2))-methyltransferase RsmC;
62-117 9.63e-04

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


Pssm-ID: 181902 [Multi-domain]  Cd Length: 342  Bit Score: 40.69  E-value: 9.63e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157093019  62 KDRLRGKaVLDVGCGTGVLSMLCAKICQPAQI----IAAEATESTARiaeTLiQQNELQG 117
Cdd:PRK09489 193 TPHTKGK-VLDVGCGAGVLSAVLARHSPKIRLtlsdVSAAALESSRA---TL-AANGLEG 247
PRK14968 PRK14968
putative methyltransferase; Provisional
 67-168 1.21e-03

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 39.50  E-value: 1.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157093019  67 GKAVLDVGCGTGVLSMLCAKicQPAQIIAAEATESTARIAETLIQQNELQgiitvvNRPIEML--DLSAPV-----DAI- 138
Cdd:PRK14968  24 GDRVLEVGTGSGIVAIVAAK--NGKKVVGVDINPYAVECAKCNAKLNNIR------NNGVEVIrsDLFEPFrgdkfDVIl 95

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 157093019 139 -------------VSEWMGfYAFH--ES---MLDSVLYARDHWLKPGG 168
Cdd:PRK14968  96 fnppylpteeeeeWDDWLN-YALSggKDgreVIDRFLDEVGRYLKPGG 142
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 56-202 1.72e-03

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 38.56  E-value: 1.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157093019   56 RAFEANKDRLRgkaVLDVGCGTGVLSMLCAKicQPAQIIAAEATESTARIAetliqqneLQGIITVVNRPIEMLDLSAPV 135
Cdd:pfam13489  15 RLLPKLPSPGR---VLDFGCGTGIFLRLLRA--QGFSVTGVDPSPIAIERA--------LLNVRFDQFDEQEAAVPAGKF 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157093019  136 DAIVSeWMGFYAFH--ESMLDSvLYArdhWLKPGGLLLpdsCRLWAAVASEDIWRRDN---VEYYQ--NYYSLD 202
Cdd:pfam13489  82 DVIVA-REVLEHVPdpPALLRQ-IAA---LLKPGGLLL---LSTPLASDEADRLLLEWpylRPRNGhiSLFSAR 147
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 68-171 2.80e-03

malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin biosynthetic gene clusters in proteobacteria, firmicutes, green-sulfur bacteria, fusobacterium and bacteroides, carries out an enzymatic step prior to the formation of pimeloyl-CoA, namely O-methylation of the malonyl group preferentially while on acyl carrier protein. The enzyme is recognizable as a methyltransferase by homology. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 38.81  E-value: 2.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157093019   68 KAVLDVGCGTGVLSMLCAKICQPAQIIAAEATESTARIAETLIQQNelqgIITVVNRpIEMLDLSAP-VDAIVSEwMGFY 146
Cdd:TIGR02072  36 ASVLDIGCGTGYLTRALLKRFPQAEFIALDISAGMLAQAKTKLSEN----VQFICGD-AEKLPLEDSsFDLIVSN-LALQ 109

                          90       100
                  ....*....|....*....|....*
gi 157093019  147 AFHEsmLDSVLYARDHWLKPGGLLL 171
Cdd:TIGR02072 110 WCDD--LSQALSELARVLKPGGLLA 132
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
 55-113 4.21e-03

Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441843 [Multi-domain]  Cd Length: 403  Bit Score: 38.61  E-value: 4.21e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157093019  55 IRAFEANKDRLRGKAVL-DVGCGTGVLSMLCAKICQPAQIIAAEATEstARIAetLIQQN 113
Cdd:COG2242  235 VRALTLAKLALRPGDVLwDIGAGSGSVSIEAARLAPGGRVYAIERDP--ERAA--LIRAN 290
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 49-140 4.48e-03

HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. Both E. coli and H. influenzae have two members rather than one. The members from the Mycoplasmas have an additional C-terminal domain. [Protein fate, Protein modification and repair]


Pssm-ID: 273125 [Multi-domain]  Cd Length: 284  Bit Score: 38.10  E-value: 4.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157093019   49 PRPEGYIRAFEANKD---RLRGKAVLDVGCGTGVLSMLCAKICQPAQIIAAEATESTARIAETLIQQNELQGIITVVN-- 123
Cdd:TIGR00536  94 PRPETEELVEKALASlisQPPILHILDLGTGSGCIALALAYEFPNAEVIAVDISPDALAVAEENAEKNQLEHRVEFIQsn 173

                          90
                  ....*....|....*....
gi 157093019  124 --RPIEMLDlsapVDAIVS 140
Cdd:TIGR00536 174 lfEPLAGQK----IDIIVS 188
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 66-171 7.03e-03

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: 36.80  E-value: 7.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157093019   66 RGKAVLDVGCGTGVLSMLCAKICQPAQI----IAAEATEStariAETLIQQNELQGIITVVNrpiemlDLSAPV-----D 136
Cdd:pfam05175  31 LSGKVLDLGCGAGVLGAALAKESPDAELtmvdINARALES----ARENLAANGLENGEVVAS------DVYSGVedgkfD 100

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 157093019  137 AIVSEwmgfYAFHESMLDS-------VLYARDHwLKPGGLLL 171
Cdd:pfam05175 101 LIISN----PPFHAGLATTynvaqrfIADAKRH-LRPGGELW 137
CbiT TIGR02469
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ...
 55-171 7.30e-03

precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes the CbiT methylase which is responsible, in part (along with CbiE), for methylating precorrin-6y (or cobalt-precorrin-6y) at both the 5 and 15 positions as well as the concomitant decarbozylation at C-12. In many organisms, this protein is fused to the CbiE subunit. The fused protein, when found in organisms catalyzing the oxidative version of the cobalamin biosynthesis pathway, is called CobL. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 274148 [Multi-domain]  Cd Length: 124  Bit Score: 36.15  E-value: 7.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157093019   55 IRAFEANKDRLR-GKAVLDVGCGTGVLSMLCAKICQPAQIIAAEATESTARIAETLIQQNELQGIITVVNRPIEMLDLSA 133
Cdd:TIGR02469   7 VRALTLAKLRLRpGDVLWDIGAGTGSVTIEAARLVPNGRVYAIERNPEALDLIERNLRRFGVSNIVIVEGDAPEAPEALL 86

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 157093019  134 P-VDAIVSEWMGfyafheSMLDSVLYARDHWLKPGGLLL 171
Cdd:TIGR02469  87 PdPDAVFVGGSG------GLLQEILEAVERRLRPGGRIV 119
PRK07402 PRK07402
precorrin-6Y C5,15-methyltransferase subunit CbiT;
64-113 8.36e-03

precorrin-6Y C5,15-methyltransferase subunit CbiT;


Pssm-ID: 180961  Cd Length: 196  Bit Score: 36.90  E-value: 8.36e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 157093019  64 RLRGKAVL-DVGCGTGVLSMLCAKICQPAQIIAAEATESTAriaeTLIQQN 113
Cdd:PRK07402  37 RLEPDSVLwDIGAGTGTIPVEAGLLCPKGRVIAIERDEEVV----NLIRRN 83
RsmG COG0357
16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) [Translation, ...
 64-171 9.35e-03

16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) [Translation, ribosomal structure and biogenesis]; 16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 440126  Cd Length: 211  Bit Score: 37.05  E-value: 9.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157093019  64 RLRGKAVLDVGCGTG----VLsmlcaKICQP-AQIIAAEATEstARIA--ETLIQQNELQGiITVVNRPIEMLDLSAPVD 136
Cdd:COG0357   65 PKEGARVLDVGSGAGfpgiPL-----AIARPdLQVTLVDSLG--KKIAflREVVRELGLKN-VTVVHGRAEELAPREKFD 136

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 157093019 137 AIVSEwmgfyAFhESMLDSVLYARdHWLKPGGLLL 171
Cdd:COG0357  137 VVTAR-----AV-APLPDLLELAL-PLLKPGGRLL 164
 
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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