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Conserved domains on  [gi|2745085176|ref|WP_349904590|]
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class I SAM-dependent methyltransferase [Bacillus safensis]

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 3.66e-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: 214.19  E-value: 3.66e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745085176  48 VFAFDVQQEALQQTSKRLG--GQYPYVHLIHDGHEKLADHLPkdvyGHISGAVFNLGYLPGGDKAVTTQAHTTIESIKQL 125
Cdd:pfam06962   1 VYAFDIQEEALENTRERLEeeGLEERVELILDGHENLDEYVP----GPVDAAMFNLGYLPGGDKSITTKPETTLKALEAA 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2745085176 126 LEWLKPGGLIVLVIYHGHPEGKREKEVLLDYCRSLPHEEVQVLSYQYMNIQNDPPFVVAIE 186
Cdd:pfam06962  77 LELLKPGGIISLVVYPGHPGGKEEKEAVLEYLSSLDQKKYNVLKYEFLNQPNNPPFLVLIE 137
PRK14901 super family cl36438
16S rRNA methyltransferase B; Provisional
 19-66 4.87e-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: 4.87e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2745085176  19 QKGDIVIDATMGNGHDTLYLADLVGTDGQVFAFDVQQ---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 3.66e-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: 214.19  E-value: 3.66e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745085176  48 VFAFDVQQEALQQTSKRLG--GQYPYVHLIHDGHEKLADHLPkdvyGHISGAVFNLGYLPGGDKAVTTQAHTTIESIKQL 125
Cdd:pfam06962   1 VYAFDIQEEALENTRERLEeeGLEERVELILDGHENLDEYVP----GPVDAAMFNLGYLPGGDKSITTKPETTLKALEAA 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2745085176 126 LEWLKPGGLIVLVIYHGHPEGKREKEVLLDYCRSLPHEEVQVLSYQYMNIQNDPPFVVAIE 186
Cdd:pfam06962  77 LELLKPGGIISLVVYPGHPGGKEEKEAVLEYLSSLDQKKYNVLKYEFLNQPNNPPFLVLIE 137
PRK08317 PRK08317
hypothetical protein; Provisional
 7-162 3.53e-08

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 51.48  E-value: 3.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745085176   7 LPFSKELLER-----ACQKGDIVIDATMGNGHDTLYLADLVGTDGQVFAFDVQQEALQQTSKRLGGQYPYVHLIHDGhek 81
Cdd:PRK08317    1 LPDFRRYRARtfellAVQPGDRVLDVGCGPGNDARELARRVGPEGRVVGIDRSEAMLALAKERAAGLGPNVEFVRGD--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745085176  82 lADHLPkdvyghisgavFNLGYLpggDKAVTTQAHTTIESIKQLL----EWLKPGGLIVL-------VIYHGHPEGkREK 150
Cdd:PRK08317   78 -ADGLP-----------FPDGSF---DAVRSDRVLQHLEDPARALaeiaRVLRPGGRVVVldtdwdtLVWHSGDRA-LMR 141

                         170
                  ....*....|..
gi 2745085176 151 EVLLDYCRSLPH 162
Cdd:PRK08317  142 KILNFWSDHFAD 153
RmsH COG0275
16S rRNA C1402 N4-methylase RsmH [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 13-102 4.00e-08

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: 51.60  E-value: 4.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745085176  13 LLER-----ACQKGDIVIDATMGN-GHdTLYLADLVGTDGQVFAFDVQQEALQQTSKRLGGQYPYVHLIHDGHEKLADHL 86
Cdd:COG0275    11 LLEEvlealAPKPGGVYVDGTLGGgGH-SRAILERLGPGGRLIGIDRDPDAIAAAKERLAEFGDRFTLVHGNFSELDEVL 89

                          90
                  ....*....|....*.
gi 2745085176  87 PKDVYGHISGAVFNLG 102
Cdd:COG0275    90 AELGIEKVDGILLDLG 105
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 24-142 6.85e-04

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: 6.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745085176  24 VIDATMGNGHDTLYLADLVGtdGQVFAFDVQQEALQQTSK-RLGGQYPYVHLIHDGHEKLADHLPKDVYGHISGAVFnlG 102
Cdd:cd02440     2 VLDLGCGTGALALALASGPG--ARVTGVDISPVALELARKaAAALLADNVEVLKGDAEELPPEADESFDVIISDPPL--H 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2745085176 103 YLPGGDKAVttqahttiesIKQLLEWLKPGGLIVLVIYHG 142
Cdd:cd02440    78 HLVEDLARF----------LEEARRLLKPGGVLVLTLVLA 107
B2-adapt-app_C smart01020
Beta2-adaptin appendage, C-terminal sub-domain; Members of this family adopt a structure ...
 144-191 2.91e-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: 36.13  E-value: 2.91e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2745085176  144 PEGKREKEVLLDYCRSLPHEEVQVLSYQYMNIQNDppfvvAIEKKLKS 191
Cdd:smart01020   3 EDGQMEREVFLKTWKSLPESNEQQFQLQPNNLNPD-----TIIKKLQS 45
PRK14901 PRK14901
16S rRNA methyltransferase B; Provisional
 19-66 4.87e-03

16S rRNA methyltransferase B; Provisional


Pssm-ID: 237856 [Multi-domain]  Cd Length: 434  Bit Score: 36.83  E-value: 4.87e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2745085176  19 QKGDIVIDATMGNGHDTLYLADLVGTDGQVFAFDVQQ---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 3.66e-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: 214.19  E-value: 3.66e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745085176  48 VFAFDVQQEALQQTSKRLG--GQYPYVHLIHDGHEKLADHLPkdvyGHISGAVFNLGYLPGGDKAVTTQAHTTIESIKQL 125
Cdd:pfam06962   1 VYAFDIQEEALENTRERLEeeGLEERVELILDGHENLDEYVP----GPVDAAMFNLGYLPGGDKSITTKPETTLKALEAA 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2745085176 126 LEWLKPGGLIVLVIYHGHPEGKREKEVLLDYCRSLPHEEVQVLSYQYMNIQNDPPFVVAIE 186
Cdd:pfam06962  77 LELLKPGGIISLVVYPGHPGGKEEKEAVLEYLSSLDQKKYNVLKYEFLNQPNNPPFLVLIE 137
PRK08317 PRK08317
hypothetical protein; Provisional
 7-162 3.53e-08

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 51.48  E-value: 3.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745085176   7 LPFSKELLER-----ACQKGDIVIDATMGNGHDTLYLADLVGTDGQVFAFDVQQEALQQTSKRLGGQYPYVHLIHDGhek 81
Cdd:PRK08317    1 LPDFRRYRARtfellAVQPGDRVLDVGCGPGNDARELARRVGPEGRVVGIDRSEAMLALAKERAAGLGPNVEFVRGD--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745085176  82 lADHLPkdvyghisgavFNLGYLpggDKAVTTQAHTTIESIKQLL----EWLKPGGLIVL-------VIYHGHPEGkREK 150
Cdd:PRK08317   78 -ADGLP-----------FPDGSF---DAVRSDRVLQHLEDPARALaeiaRVLRPGGRVVVldtdwdtLVWHSGDRA-LMR 141

                         170
                  ....*....|..
gi 2745085176 151 EVLLDYCRSLPH 162
Cdd:PRK08317  142 KILNFWSDHFAD 153
RmsH COG0275
16S rRNA C1402 N4-methylase RsmH [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 13-102 4.00e-08

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: 51.60  E-value: 4.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745085176  13 LLER-----ACQKGDIVIDATMGN-GHdTLYLADLVGTDGQVFAFDVQQEALQQTSKRLGGQYPYVHLIHDGHEKLADHL 86
Cdd:COG0275    11 LLEEvlealAPKPGGVYVDGTLGGgGH-SRAILERLGPGGRLIGIDRDPDAIAAAKERLAEFGDRFTLVHGNFSELDEVL 89

                          90
                  ....*....|....*.
gi 2745085176  87 PKDVYGHISGAVFNLG 102
Cdd:COG0275    90 AELGIEKVDGILLDLG 105
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 9-141 1.21e-06

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: 46.14  E-value: 1.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745085176   9 FSKELLER-ACQKGDIVIDATMGNGHDTLYLADLvgtDGQVFAFDVQQEALQQTSKRLGGQYPYVHLIH-DgheklADHL 86
Cdd:COG2226    10 GREALLAAlGLRPGARVLDLGCGTGRLALALAER---GARVTGVDISPEMLELARERAAEAGLNVEFVVgD-----AEDL 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2745085176  87 PkdvyghISGAVFnlgylpggDKAVTTQAHTTIESIKQLL-EW---LKPGGLIVLVIYH 141
Cdd:COG2226    82 P------FPDGSF--------DLVISSFVLHHLPDPERALaEIarvLKPGGRLVVVDFS 126
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 30-133 1.38e-06

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 44.86  E-value: 1.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745085176  30 GNGHDTLYLADLVGtdGQVFAFDVQQEALQQTSKRLGGQYPYVHLIHDGHEKLadHLPKDVYGHISgAVFNLGYLPGGDK 109
Cdd:pfam13649   7 GTGRLTLALARRGG--ARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDL--PFPDGSFDLVV-SSGVLHHLPDPDL 81

                          90       100
                  ....*....|....*....|....
gi 2745085176 110 AvttqahttiESIKQLLEWLKPGG 133
Cdd:pfam13649  82 E---------AALREIARVLKPGG 96
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 20-149 6.91e-05

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 41.25  E-value: 6.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745085176  20 KGDIVIDATMGNGHDTLYLADLVGTDGQVFAFDVQQEALQ---QTSKRLGgqYPYVHLIHDGHEKLADHLPKDVYGHI-S 95
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELAEELGPNAEVVGIDISEEAIEkarENAQKLG--FDNVEFEQGDIEELPELLEDDKFDVViS 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2745085176  96 GAVFNLGYLPGGdkavttqahtTIESIKQLlewLKPGGLIVLVIYHGHPEGKRE 149
Cdd:pfam13847  81 NCVLNHIPDPDK----------VLQEILRV---LKPGGRLIISDPDSLAELPAH 121
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 21-140 7.32e-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: 42.07  E-value: 7.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745085176  21 GDIVIDATMGNGHDTLYLADLVGTDGQVFAFDVQQEALQQTSKRLG--GQYPYVHLIHdghekladhlpKDVYGHISGAV 98
Cdd:COG2519    92 GARVLEAGTGSGALTLALARAVGPEGKVYSYERREDFAEIARKNLErfGLPDNVELKL-----------GDIREGIDEGD 160

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2745085176  99 FNLGYL----PggdkavttqahttIESIKQLLEWLKPGGliVLVIY 140
Cdd:COG2519   161 VDAVFLdmpdP-------------WEALEAVAKALKPGG--VLVAY 191
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 24-142 6.85e-04

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: 6.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745085176  24 VIDATMGNGHDTLYLADLVGtdGQVFAFDVQQEALQQTSK-RLGGQYPYVHLIHDGHEKLADHLPKDVYGHISGAVFnlG 102
Cdd:cd02440     2 VLDLGCGTGALALALASGPG--ARVTGVDISPVALELARKaAAALLADNVEVLKGDAEELPPEADESFDVIISDPPL--H 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2745085176 103 YLPGGDKAVttqahttiesIKQLLEWLKPGGLIVLVIYHG 142
Cdd:cd02440    78 HLVEDLARF----------LEEARRLLKPGGVLVLTLVLA 107
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 13-164 2.04e-03

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 37.59  E-value: 2.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2745085176  13 LLERACQKGDIVIDATMGNGHDTLYLADLVGtdGQVFAFDVQQEALQQTSKRLGGQ-YPYVHLIHDGHEKLADhLPKDVY 91
Cdd:COG0500    19 ALLERLPKGGRVLDLGCGTGRNLLALAARFG--GRVIGIDLSPEAIALARARAAKAgLGNVEFLVADLAELDP-LPAESF 95

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2745085176  92 GHISgAVFNLGYLPggdkavttqAHTTIESIKQLLEWLKPGGLIVLVIYHGHPEGKREKEVLLDYCRSLPHEE 164
Cdd:COG0500    96 DLVV-AFGVLHHLP---------PEEREALLRELARALKPGGVLLLSASDAAAALSLARLLLLATASLLELLL 158
B2-adapt-app_C smart01020
Beta2-adaptin appendage, C-terminal sub-domain; Members of this family adopt a structure ...
 144-191 2.91e-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: 36.13  E-value: 2.91e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2745085176  144 PEGKREKEVLLDYCRSLPHEEVQVLSYQYMNIQNDppfvvAIEKKLKS 191
Cdd:smart01020   3 EDGQMEREVFLKTWKSLPESNEQQFQLQPNNLNPD-----TIIKKLQS 45
PRK14901 PRK14901
16S rRNA methyltransferase B; Provisional
 19-66 4.87e-03

16S rRNA methyltransferase B; Provisional


Pssm-ID: 237856 [Multi-domain]  Cd Length: 434  Bit Score: 36.83  E-value: 4.87e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2745085176  19 QKGDIVIDATMGNGHDTLYLADLVGTDGQVFAFDVQQ---EALQQTSKRLG 66
Cdd:PRK14901  251 QPGEVILDACAAPGGKTTHIAELMGDQGEIWAVDRSAsrlKKLQENAQRLG 301
PLN02233 PLN02233
ubiquinone biosynthesis methyltransferase
 19-64 9.47e-03

ubiquinone biosynthesis methyltransferase


Pssm-ID: 177877 [Multi-domain]  Cd Length: 261  Bit Score: 36.02  E-value: 9.47e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2745085176  19 QKGDIVIDATMGNGHDTLYLADLVGTDGQVFAFDVQQEALQQTSKR 64
Cdd:PLN02233   72 KMGDRVLDLCCGSGDLAFLLSEKVGSDGKVMGLDFSSEQLAVAASR 117
 
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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