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Conserved domains on  [gi|637162366|ref|WP_024424904|]
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MULTISPECIES: class I SAM-dependent methyltransferase [Bacillus]

Protein Classification

tRNA (mnm(5)s(2)U34)-methyltransferase( domain architecture ID 10536603)

tRNA (mnm(5)s(2)U34)-methyltransferase catalyzes the transfer of a methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34 to form mnm(5)s(2)U34

CATH:  2.20.25.110
EC:  2.1.1.61
Gene Ontology:  GO:0004808|GO:1904047|GO:0008033|GO:0032259|GO:0008757
PubMed:  12826405|12504684
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
rRNA_methylase pfam06962
Putative rRNA methylase; This family contains a number of putative rRNA methylases. Note that ...
 48-186 1.15e-72

Putative rRNA methylase; This family contains a number of putative rRNA methylases. Note that many family members are hypothetical proteins.


:

Pssm-ID: 429214  Cd Length: 137  Bit Score: 215.35  E-value: 1.15e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637162366   48 VFAFDVQEEALQQTSKRLGDQY--PYVHLIHDGHEKLADHLPkdayGQIAGAVFNLGYLPGGDKAVTTQAHTTIEAIKQL 125
Cdd:pfam06962   1 VYAFDIQEEALENTRERLEEEGleERVELILDGHENLDEYVP----GPVDAAMFNLGYLPGGDKSITTKPETTLKALEAA 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 637162366  126 LEWLKPGGLIVLVIYHGHPEGKREKEVLLDYCRSLPHEEVQVLSYQYMNIQNDPPFVVAIE 186
Cdd:pfam06962  77 LELLKPGGIISLVVYPGHPGGKEEKEAVLEYLSSLDQKKYNVLKYEFLNQPNNPPFLVLIE 137
PRK14901 super family cl36438
16S rRNA methyltransferase B; Provisional
 19-66 4.94e-03

16S rRNA methyltransferase B; Provisional


The actual alignment was detected with superfamily member PRK14901:

Pssm-ID: 237856 [Multi-domain]  Cd Length: 434  Bit Score: 36.83  E-value: 4.94e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 637162366  19 QKGDIVIDATMGNGHDTLYLADLVGTDGQVFAFDVQE---EALQQTSKRLG 66
Cdd:PRK14901 251 QPGEVILDACAAPGGKTTHIAELMGDQGEIWAVDRSAsrlKKLQENAQRLG 301
 
Name Accession Description Interval E-value
rRNA_methylase pfam06962
Putative rRNA methylase; This family contains a number of putative rRNA methylases. Note that ...
 48-186 1.15e-72

Putative rRNA methylase; This family contains a number of putative rRNA methylases. Note that many family members are hypothetical proteins.


Pssm-ID: 429214  Cd Length: 137  Bit Score: 215.35  E-value: 1.15e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637162366   48 VFAFDVQEEALQQTSKRLGDQY--PYVHLIHDGHEKLADHLPkdayGQIAGAVFNLGYLPGGDKAVTTQAHTTIEAIKQL 125
Cdd:pfam06962   1 VYAFDIQEEALENTRERLEEEGleERVELILDGHENLDEYVP----GPVDAAMFNLGYLPGGDKSITTKPETTLKALEAA 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 637162366  126 LEWLKPGGLIVLVIYHGHPEGKREKEVLLDYCRSLPHEEVQVLSYQYMNIQNDPPFVVAIE 186
Cdd:pfam06962  77 LELLKPGGIISLVVYPGHPGGKEEKEAVLEYLSSLDQKKYNVLKYEFLNQPNNPPFLVLIE 137
RmsH COG0275
16S rRNA C1402 N4-methylase RsmH [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 13-102 6.34e-09

16S rRNA C1402 N4-methylase RsmH [Translation, ribosomal structure and biogenesis]; 16S rRNA C1402 N4-methylase RsmH is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 440044  Cd Length: 312  Bit Score: 53.91  E-value: 6.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637162366  13 LLER-----ACQKGDIVIDATMGN-GHdTLYLADLVGTDGQVFAFDVQEEALQQTSKRLGDQYPYVHLIHDGHEKLADHL 86
Cdd:COG0275   11 LLEEvlealAPKPGGVYVDGTLGGgGH-SRAILERLGPGGRLIGIDRDPDAIAAAKERLAEFGDRFTLVHGNFSELDEVL 89

                         90
                 ....*....|....*.
gi 637162366  87 PKDAYGQIAGAVFNLG 102
Cdd:COG0275   90 AELGIEKVDGILLDLG 105
PRK08317 PRK08317
hypothetical protein; Provisional
 7-162 2.03e-08

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 52.25  E-value: 2.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637162366   7 LPFSKELLER-----ACQKGDIVIDATMGNGHDTLYLADLVGTDGQVFAFDVQEEALQQTSKRLGDQYPYVHLIHDGhek 81
Cdd:PRK08317   1 LPDFRRYRARtfellAVQPGDRVLDVGCGPGNDARELARRVGPEGRVVGIDRSEAMLALAKERAAGLGPNVEFVRGD--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637162366  82 lADHLP-KDAYGQIAGAVFNLGYLPGGDKAVTtqahttieaikQLLEWLKPGGLIVL-------VIYHGHPEGkREKEVL 153
Cdd:PRK08317  78 -ADGLPfPDGSFDAVRSDRVLQHLEDPARALA-----------EIARVLRPGGRVVVldtdwdtLVWHSGDRA-LMRKIL 144


                 ....*....
gi 637162366 154 LDYCRSLPH 162
Cdd:PRK08317 145 NFWSDHFAD 153
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 24-142 9.52e-05

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: 40.11  E-value: 9.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637162366  24 VIDATMGNGHDTLYLADLVGtdGQVFAFDVQEEALQQTSK-RLGDQYPYVHLIHDGheklADHLPKDAYGQIAGAVFNLG 102
Cdd:cd02440    2 VLDLGCGTGALALALASGPG--ARVTGVDISPVALELARKaAAALLADNVEVLKGD----AEELPPEADESFDVIISDPP 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 637162366 103 YLPGGDKAVttqahttiEAIKQLLEWLKPGGLIVLVIYHG 142
Cdd:cd02440   76 LHHLVEDLA--------RFLEEARRLLKPGGVLVLTLVLA 107
PRK14901 PRK14901
16S rRNA methyltransferase B; Provisional
 19-66 4.94e-03

16S rRNA methyltransferase B; Provisional


Pssm-ID: 237856 [Multi-domain]  Cd Length: 434  Bit Score: 36.83  E-value: 4.94e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 637162366  19 QKGDIVIDATMGNGHDTLYLADLVGTDGQVFAFDVQE---EALQQTSKRLG 66
Cdd:PRK14901 251 QPGEVILDACAAPGGKTTHIAELMGDQGEIWAVDRSAsrlKKLQENAQRLG 301
B2-adapt-app_C smart01020
Beta2-adaptin appendage, C-terminal sub-domain; Members of this family adopt a structure ...
 144-190 8.51e-03

Beta2-adaptin appendage, C-terminal sub-domain; Members of this family adopt a structure consisting of a 5 stranded beta-sheet, flanked by one alpha helix on the outer side, and by two alpha helices on the inner side. This domain is required for binding to clathrin, and its subsequent polymerisation. Furthermore, a hydrophobic patch present in the domain also binds to a subset of D-phi-F/W motif-containing proteins that are bound by the alpha-adaptin appendage domain (epsin, AP180, eps15).


Pssm-ID: 198088  Cd Length: 111  Bit Score: 34.59  E-value: 8.51e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 637162366   144 PEGKREKEVLLDYCRSLPHEEVQVLSYQYMNIQNDppfvvAIEKKLK 190
Cdd:smart01020   3 EDGQMEREVFLKTWKSLPESNEQQFQLQPNNLNPD-----TIIKKLQ 44
 
Name Accession Description Interval E-value
rRNA_methylase pfam06962
Putative rRNA methylase; This family contains a number of putative rRNA methylases. Note that ...
 48-186 1.15e-72

Putative rRNA methylase; This family contains a number of putative rRNA methylases. Note that many family members are hypothetical proteins.


Pssm-ID: 429214  Cd Length: 137  Bit Score: 215.35  E-value: 1.15e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637162366   48 VFAFDVQEEALQQTSKRLGDQY--PYVHLIHDGHEKLADHLPkdayGQIAGAVFNLGYLPGGDKAVTTQAHTTIEAIKQL 125
Cdd:pfam06962   1 VYAFDIQEEALENTRERLEEEGleERVELILDGHENLDEYVP----GPVDAAMFNLGYLPGGDKSITTKPETTLKALEAA 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 637162366  126 LEWLKPGGLIVLVIYHGHPEGKREKEVLLDYCRSLPHEEVQVLSYQYMNIQNDPPFVVAIE 186
Cdd:pfam06962  77 LELLKPGGIISLVVYPGHPGGKEEKEAVLEYLSSLDQKKYNVLKYEFLNQPNNPPFLVLIE 137
RmsH COG0275
16S rRNA C1402 N4-methylase RsmH [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 13-102 6.34e-09

16S rRNA C1402 N4-methylase RsmH [Translation, ribosomal structure and biogenesis]; 16S rRNA C1402 N4-methylase RsmH is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 440044  Cd Length: 312  Bit Score: 53.91  E-value: 6.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637162366  13 LLER-----ACQKGDIVIDATMGN-GHdTLYLADLVGTDGQVFAFDVQEEALQQTSKRLGDQYPYVHLIHDGHEKLADHL 86
Cdd:COG0275   11 LLEEvlealAPKPGGVYVDGTLGGgGH-SRAILERLGPGGRLIGIDRDPDAIAAAKERLAEFGDRFTLVHGNFSELDEVL 89

                         90
                 ....*....|....*.
gi 637162366  87 PKDAYGQIAGAVFNLG 102
Cdd:COG0275   90 AELGIEKVDGILLDLG 105
PRK08317 PRK08317
hypothetical protein; Provisional
 7-162 2.03e-08

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 52.25  E-value: 2.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637162366   7 LPFSKELLER-----ACQKGDIVIDATMGNGHDTLYLADLVGTDGQVFAFDVQEEALQQTSKRLGDQYPYVHLIHDGhek 81
Cdd:PRK08317   1 LPDFRRYRARtfellAVQPGDRVLDVGCGPGNDARELARRVGPEGRVVGIDRSEAMLALAKERAAGLGPNVEFVRGD--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637162366  82 lADHLP-KDAYGQIAGAVFNLGYLPGGDKAVTtqahttieaikQLLEWLKPGGLIVL-------VIYHGHPEGkREKEVL 153
Cdd:PRK08317  78 -ADGLPfPDGSFDAVRSDRVLQHLEDPARALA-----------EIARVLRPGGRVVVldtdwdtLVWHSGDRA-LMRKIL 144


                 ....*....
gi 637162366 154 LDYCRSLPH 162
Cdd:PRK08317 145 NFWSDHFAD 153
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 9-141 1.29e-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: 1.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637162366   9 FSKELLER-ACQKGDIVIDATMGNGHDTLYLADLvgtDGQVFAFDVQEEALQQTSKRLGDQYPYVHLIH-DgheklADHL 86
Cdd:COG2226   10 GREALLAAlGLRPGARVLDLGCGTGRLALALAER---GARVTGVDISPEMLELARERAAEAGLNVEFVVgD-----AEDL 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 637162366  87 PkdaygqIAGAVFnlgylpggDKAVTTQAHTTIE----AIKQLLEWLKPGGLIVLVIYH 141
Cdd:COG2226   82 P------FPDGSF--------DLVISSFVLHHLPdperALAEIARVLKPGGRLVVVDFS 126
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 30-133 3.17e-07

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 46.40  E-value: 3.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637162366   30 GNGHDTLYLADLVGtdGQVFAFDVQEEALQQTSKRLGDQYPYVHLIHDGHEKLadHLPKDAYGQIAgAVFNLGYLPGGDK 109
Cdd:pfam13649   7 GTGRLTLALARRGG--ARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDL--PFPDGSFDLVV-SSGVLHHLPDPDL 81

                          90       100
                  ....*....|....*....|....
gi 637162366  110 AvttqahttiEAIKQLLEWLKPGG 133
Cdd:pfam13649  82 E---------AALREIARVLKPGG 96
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 21-140 1.21e-05

tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 N-methylase Trm61 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442009 [Multi-domain]  Cd Length: 249  Bit Score: 44.38  E-value: 1.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637162366  21 GDIVIDATMGNGHDTLYLADLVGTDGQVFAFDVQEEALQQTSK---RLGDQyPYVHLIHdghekladhlpKDAYGQIAGA 97
Cdd:COG2519   92 GARVLEAGTGSGALTLALARAVGPEGKVYSYERREDFAEIARKnleRFGLP-DNVELKL-----------GDIREGIDEG 159

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 637162366  98 VFNLGYL----PggdkavttqahttIEAIKQLLEWLKPGGliVLVIY 140
Cdd:COG2519  160 DVDAVFLdmpdP-------------WEALEAVAKALKPGG--VLVAY 191
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 20-149 2.20e-05

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 42.79  E-value: 2.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637162366   20 KGDIVIDATMGNGHDTLYLADLVGTDGQVFAFDVQEEALQQtSKRLGDQYPY--VHLIHDGHEKLADHLPKDAYGQI-AG 96
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELAEELGPNAEVVGIDISEEAIEK-ARENAQKLGFdnVEFEQGDIEELPELLEDDKFDVViSN 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 637162366   97 AVFNLGYLPggdkavttqahttIEAIKQLLEWLKPGGLIVLVIYHGHPEGKRE 149
Cdd:pfam13847  82 CVLNHIPDP-------------DKVLQEILRVLKPGGRLIISDPDSLAELPAH 121
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 24-142 9.52e-05

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: 40.11  E-value: 9.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637162366  24 VIDATMGNGHDTLYLADLVGtdGQVFAFDVQEEALQQTSK-RLGDQYPYVHLIHDGheklADHLPKDAYGQIAGAVFNLG 102
Cdd:cd02440    2 VLDLGCGTGALALALASGPG--ARVTGVDISPVALELARKaAAALLADNVEVLKGD----AEELPPEADESFDVIISDPP 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 637162366 103 YLPGGDKAVttqahttiEAIKQLLEWLKPGGLIVLVIYHG 142
Cdd:cd02440   76 LHHLVEDLA--------RFLEEARRLLKPGGVLVLTLVLA 107
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 12-141 4.38e-04

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: 38.46  E-value: 4.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637162366  12 ELLERACQKGDIVIDATMGNGHDTLYLADLvgtdG-QVFAFDVQEEALQQTSKRLGDQYpyVHLIHDGHEKLAdhLPKDA 90
Cdd:COG2227   16 ALLARLLPAGGRVLDVGCGTGRLALALARR----GaDVTGVDISPEALEIARERAAELN--VDFVQGDLEDLP--LEDGS 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 637162366  91 YGQIAgAVFNLGYLPggdkavttqahTTIEAIKQLLEWLKPGGLIVLVIYH 141
Cdd:COG2227   88 FDLVI-CSEVLEHLP-----------DPAALLRELARLLKPGGLLLLSTPN 126
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 13-164 2.30e-03

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 37.20  E-value: 2.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637162366  13 LLERACQKGDIVIDATMGNGHDTLYLADLVGtdGQVFAFDVQEEALQQTSKRLGDQ-YPYVHLIHDGHEKLADhLPKDAY 91
Cdd:COG0500   19 ALLERLPKGGRVLDLGCGTGRNLLALAARFG--GRVIGIDLSPEAIALARARAAKAgLGNVEFLVADLAELDP-LPAESF 95

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 637162366  92 GQIAgAVFNLGYLPggdkavttqAHTTIEAIKQLLEWLKPGGLIVLVIYHGHPEGKREKEVLLDYCRSLPHEE 164
Cdd:COG0500   96 DLVV-AFGVLHHLP---------PEEREALLRELARALKPGGVLLLSASDAAAALSLARLLLLATASLLELLL 158
PRK14901 PRK14901
16S rRNA methyltransferase B; Provisional
 19-66 4.94e-03

16S rRNA methyltransferase B; Provisional


Pssm-ID: 237856 [Multi-domain]  Cd Length: 434  Bit Score: 36.83  E-value: 4.94e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 637162366  19 QKGDIVIDATMGNGHDTLYLADLVGTDGQVFAFDVQE---EALQQTSKRLG 66
Cdd:PRK14901 251 QPGEVILDACAAPGGKTTHIAELMGDQGEIWAVDRSAsrlKKLQENAQRLG 301
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 30-135 5.93e-03

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 34.65  E-value: 5.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637162366   30 GNGHDTLYLADLVGtDGQVFAFDVQEEALQQTSKRLGDQYPYVHLIHDGHEKLADHLPKDAYGQIAgAVFNLGYLPggdk 109
Cdd:pfam08242   6 GTGTLLRALLEALP-GLEYTGLDISPAALEAARERLAALGLLNAVRVELFQLDLGELDPGSFDVVV-ASNVLHHLA---- 79

                          90       100
                  ....*....|....*....|....*.
gi 637162366  110 avttqahTTIEAIKQLLEWLKPGGLI 135
Cdd:pfam08242  80 -------DPRAVLRNIRRLLKPGGVL 98
B2-adapt-app_C smart01020
Beta2-adaptin appendage, C-terminal sub-domain; Members of this family adopt a structure ...
 144-190 8.51e-03

Beta2-adaptin appendage, C-terminal sub-domain; Members of this family adopt a structure consisting of a 5 stranded beta-sheet, flanked by one alpha helix on the outer side, and by two alpha helices on the inner side. This domain is required for binding to clathrin, and its subsequent polymerisation. Furthermore, a hydrophobic patch present in the domain also binds to a subset of D-phi-F/W motif-containing proteins that are bound by the alpha-adaptin appendage domain (epsin, AP180, eps15).


Pssm-ID: 198088  Cd Length: 111  Bit Score: 34.59  E-value: 8.51e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 637162366   144 PEGKREKEVLLDYCRSLPHEEVQVLSYQYMNIQNDppfvvAIEKKLK 190
Cdd:smart01020   3 EDGQMEREVFLKTWKSLPESNEQQFQLQPNNLNPD-----TIIKKLQ 44
 
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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