NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|255003839|ref|NP_001019633|]
View 

glutathione S-transferase C-terminal domain-containing protein [Danio rerio]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 106779)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
AdoMet_MTases super family cl17173
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 403-521 9.60e-15

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.).


The actual alignment was detected with superfamily member pfam13679:

Pssm-ID: 473071 [Multi-domain]  Cd Length: 138  Bit Score: 71.45  E-value: 9.60e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003839  403 RKQQQLDNLLAMV------LNQAQPGHTVVDFCSGGGHVGIVLAYMLPKCQVILVENKEESLIRARERSAQLTL-TNIGF 475
Cdd:pfam13679   1 KKLHQVEHLAEFIapllkeLLDENGPITIVDHGAGKGYLGFILYYLKYGVRVYGIDTRAELVEKANALAQKLGFnKRMSF 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 255003839  476 IQTNLDYFT----GNFNIGV-ALHACGVATDMVLDRCLQARAGFVIS-PCCY 521
Cdd:pfam13679  81 LEGTIAGSTpvelPDRVDVVtALHACDTATDDALRFALAKQARAIVLvPCCY 132
 
Name Accession Description Interval E-value
Methyltransf_32 pfam13679
Methyltransferase domain; This family appears to be a methyltransferase domain.
 403-521 9.60e-15

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


Pssm-ID: 379330 [Multi-domain]  Cd Length: 138  Bit Score: 71.45  E-value: 9.60e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003839  403 RKQQQLDNLLAMV------LNQAQPGHTVVDFCSGGGHVGIVLAYMLPKCQVILVENKEESLIRARERSAQLTL-TNIGF 475
Cdd:pfam13679   1 KKLHQVEHLAEFIapllkeLLDENGPITIVDHGAGKGYLGFILYYLKYGVRVYGIDTRAELVEKANALAQKLGFnKRMSF 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 255003839  476 IQTNLDYFT----GNFNIGV-ALHACGVATDMVLDRCLQARAGFVIS-PCCY 521
Cdd:pfam13679  81 LEGTIAGSTpvelPDRVDVVtALHACDTATDDALRFALAKQARAIVLvPCCY 132
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 411-480 4.35e-03

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 39.36  E-value: 4.35e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255003839 411 LLAMVLN--QAQPGHTVVDFCSGGGHVGIVLAYMLPKCQVILVENKEESLIRARERSAQLTLTN-IGFIQTNL 480
Cdd:COG2890  100 LVELALAllPAGAPPRVLDLGTGSGAIALALAKERPDARVTAVDISPDALAVARRNAERLGLEDrVRFLQGDL 172
 
Name Accession Description Interval E-value
Methyltransf_32 pfam13679
Methyltransferase domain; This family appears to be a methyltransferase domain.
 403-521 9.60e-15

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


Pssm-ID: 379330 [Multi-domain]  Cd Length: 138  Bit Score: 71.45  E-value: 9.60e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003839  403 RKQQQLDNLLAMV------LNQAQPGHTVVDFCSGGGHVGIVLAYMLPKCQVILVENKEESLIRARERSAQLTL-TNIGF 475
Cdd:pfam13679   1 KKLHQVEHLAEFIapllkeLLDENGPITIVDHGAGKGYLGFILYYLKYGVRVYGIDTRAELVEKANALAQKLGFnKRMSF 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 255003839  476 IQTNLDYFT----GNFNIGV-ALHACGVATDMVLDRCLQARAGFVIS-PCCY 521
Cdd:pfam13679  81 LEGTIAGSTpvelPDRVDVVtALHACDTATDDALRFALAKQARAIVLvPCCY 132
TRM13 pfam05206
Methyltransferase TRM13; This is a family of eukaryotic proteins which are responsible for 2 ...
 416-609 2.57e-07

Methyltransferase TRM13; This is a family of eukaryotic proteins which are responsible for 2'-O-methylation of tRNA at position 4. TRM13 shows no sequence similarity to other known methyltransferases.


Pssm-ID: 398743  Cd Length: 256  Bit Score: 52.30  E-value: 2.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003839  416 LNQAQPGHTVVDFCSGGGHvgivLAYMLPKC---------QVILVE-----NKEESLIRARERSAQLTLTNIGFIQTNLD 481
Cdd:pfam05206  13 LGLLNPDSAYVEFGAGRGE----LSRYVNQCiqedklgnsGYVLIDrasnrMKFDRKIRKDESEPIIKRLRIDIKDLNLD 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003839  482 YFT----GNFNIGVALHACGVATDMVLdRCLQAR--------AGFVISPCCYGFIQ-NTLkfnFPKSARFAETLSYKEHM 548
Cdd:pfam05206  89 AVLsledGSPVVAVSKHLCGAATDLTL-RCLLNSlnnstdkfRGLLIAMCCHHVCNwRTY---VNREFLLELGITYDEFQ 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003839  549 ILCRF-------------------ADQTAVS---------LPPERRS-IGKRCMGLVDLDRSWAAEAHGYSVRVMTMIPK 599
Cdd:pfam05206 165 ILTKMvswavcgkrdenskeekekEEDDVVEgsvenhisgLSSEEREeIGLKCKRLIDEGRLLWLKEKGFEAELVKYVEP 244

                         250
                  ....*....|
gi 255003839  600 GCSPKNNMLV 609
Cdd:pfam05206 245 DVSLENVCLL 254
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 421-531 3.98e-06

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 47.03  E-value: 3.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003839  421 PGHTVVDFCSGGGHVGIVLAY-MLPKCQVILVENKEESLIRARERSAQLTLTNIGFIQTNLDYFTGNFNIGVAlhacgva 499
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELAEeLGPNAEVVGIDISEEAIEKARENAQKLGFDNVEFEQGDIEELPELLEDDKF------- 75

                          90       100       110
                  ....*....|....*....|....*....|..
gi 255003839  500 tDMVLDRCLQARAGFviSPCCYGFIQNTLKFN 531
Cdd:pfam13847  76 -DVVISNCVLNHIPD--PDKVLQEILRVLKPG 104
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 425-509 3.76e-03

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 37.16  E-value: 3.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003839  425 VVDFCSGGGHVGIVLAYMLpKCQVILVENKEESLIRARERSAQLTLtNIGFIQ---TNLDYFTGNFNIGVALHACGVATD 501
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRG-GARVTGVDLSPEMLERARERAAEAGL-NVEFVQgdaEDLPFPDGSFDLVVSSGVLHHLPD 78


                  ....*...
gi 255003839  502 MVLDRCLQ 509
Cdd:pfam13649  79 PDLEAALR 86
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 411-480 4.35e-03

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 39.36  E-value: 4.35e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255003839 411 LLAMVLN--QAQPGHTVVDFCSGGGHVGIVLAYMLPKCQVILVENKEESLIRARERSAQLTLTN-IGFIQTNL 480
Cdd:COG2890  100 LVELALAllPAGAPPRVLDLGTGSGAIALALAKERPDARVTAVDISPDALAVARRNAERLGLEDrVRFLQGDL 172
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 419-463 6.35e-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: 38.59  E-value: 6.35e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 255003839 419 AQPGHTVVDFCSGGGHVGIVLAYMLPKCQVILVENKEESLIRARE 463
Cdd:COG4123   35 VKKGGRVLDLGTGTGVIALMLAQRSPGARITGVEIQPEAAELARR 79
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 419-495 6.78e-03

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: 37.28  E-value: 6.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255003839 419 AQPGHTVVDFCSGGGHVGIVLAYMlpKCQVILVENKEESLIRARERSAQLTLtNIGFIQ---TNLDYFTGNFNIGVALHA 495
Cdd:COG2226   20 LRPGARVLDLGCGTGRLALALAER--GARVTGVDISPEMLELARERAAEAGL-NVEFVVgdaEDLPFPDGSFDLVISSFV 96
RsmB COG0144
16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and ...
 411-473 7.79e-03

16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and biogenesis]; 16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 439914 [Multi-domain]  Cd Length: 441  Bit Score: 39.22  E-value: 7.79e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255003839 411 LLAMVLNqAQPGHTVVDFCSGGG----HvgiVLAYMLPKCQVILVENKEESLIRARERSAQLTLTNI 473
Cdd:COG0144  240 LVALLLD-PKPGERVLDLCAAPGgktlH---LAELMGNKGRVVAVDISEHRLKRLRENLARLGLSNV 302
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
421-469 8.87e-03

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 35.95  E-value: 8.87e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 255003839 421 PGHTVVDFCSGGGHVGIVLAYMLPKCQVILVENKEESLIRARERSAQLT 469
Cdd:COG4106    1 PPRRVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARARLPNVR 49
RsmG COG0357
16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) [Translation, ...
 420-452 8.91e-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: 37.82  E-value: 8.91e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 255003839 420 QPGHTVVDFCSGGGHVGIVLAYMLPKCQVILVE 452
Cdd:COG0357   66 KEGARVLDVGSGAGFPGIPLAIARPDLQVTLVD 98
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH