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Conserved domains on  [gi|55956895|ref|NP_001007240|]
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eEF1A lysine and N-terminal methyltransferase isoform 3 [Homo sapiens]

Protein Classification

eEF1A lysine and N-terminal methyltransferase( domain architecture ID 20705015)

eEF1A lysine and N-terminal methyltransferase is a dual methyltransferase that catalyzes methylation of elongation factor 1-alpha (EEF1A1 and EEF1A2) at two different positions, and is therefore involved in the regulation of mRNA translation

CATH:  2.20.25.110
EC:  2.1.1.-
Gene Ontology:  GO:0032259|GO:0008757|GO:0016279|GO:1904047
PubMed:  12504684|12826405
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
343-483 1.15e-28

Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];


:

Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 112.61  E-value: 1.15e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956895 343 VVGLGGGSLPLFVHDHFPKSCIDAVEIDPSMLEVATQWFGFSQS----DRMKVHIADGLDYIAslagggEARPCYDVIMf 418
Cdd:COG0421  43 IIGGGDGGLARELLKHPPVERVDVVEIDPEVVELAREYFPLLAPafddPRLRVVIGDGRAFLR------EAEESYDVII- 115

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55956895 419 dVDSKDPTlgmsCPPPAFVEQSFLQKVKSILTPEGVFILNLVCRDLGLK--DSVLAGLKAVFPLLYV 483
Cdd:COG0421 116 -VDLTDPV----GPAEGLFTREFYEDCRRALKPGGVLVVNLGSPFYGLDllRRVLATLREVFPHVVL 177
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 52-150 1.07e-13

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


:

Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 66.82  E-value: 1.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956895    52 VLVIGCGNSELSEQLYDVGYRDIVNIDISEVVIKQMKECNATRRPQMSFLKMDMTQMEFPDASFQVVLDKGTLDAVltde 131
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLPFPDGSFDLVVSSGVLHHL---- 76

                          90
                  ....*....|....*....
gi 55956895   132 eekTLQQVDRMLAEVGRVL 150
Cdd:pfam13649  77 ---PDPDLEAALREIARVL 92
 
Name Accession Description Interval E-value
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
343-483 1.15e-28

Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 112.61  E-value: 1.15e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956895 343 VVGLGGGSLPLFVHDHFPKSCIDAVEIDPSMLEVATQWFGFSQS----DRMKVHIADGLDYIAslagggEARPCYDVIMf 418
Cdd:COG0421  43 IIGGGDGGLARELLKHPPVERVDVVEIDPEVVELAREYFPLLAPafddPRLRVVIGDGRAFLR------EAEESYDVII- 115

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55956895 419 dVDSKDPTlgmsCPPPAFVEQSFLQKVKSILTPEGVFILNLVCRDLGLK--DSVLAGLKAVFPLLYV 483
Cdd:COG0421 116 -VDLTDPV----GPAEGLFTREFYEDCRRALKPGGVLVVNLGSPFYGLDllRRVLATLREVFPHVVL 177
PRK04457 PRK04457
polyamine aminopropyltransferase;
343-517 1.06e-20

polyamine aminopropyltransferase;


Pssm-ID: 179854 [Multi-domain]  Cd Length: 262  Bit Score: 91.64  E-value: 1.06e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956895  343 VVGLGGGSLPLFVHDHFPKSCIDAVEIDPSMLEVA-TQWFGFSQSDRMKVHIADGLDYIAslagggEARPCYDVIMFD-V 420
Cdd:PRK04457  72 QIGLGGGSLAKFIYTYLPDTRQTAVEINPQVIAVArNHFELPENGERFEVIEADGAEYIA------VHRHSTDVILVDgF 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956895  421 DSKDptlgmscPPPAFVEQSFLQKVKSILTPEGVFILNLVCRDlGLKDSVLAGLKAVFP-LLYVRRIEGEVNEILFCQLH 499
Cdd:PRK04457 146 DGEG-------IIDALCTQPFFDDCRNALSSDGIFVVNLWSRD-KRYDRYLERLESSFEgRVLELPAESHGNVAVFAFKS 217

                        170
                 ....*....|....*...
gi 55956895  500 PEQKLATPELLETAQALE 517
Cdd:PRK04457 218 APKELRWDKLRKRAKKLE 235
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 52-150 1.07e-13

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 66.82  E-value: 1.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956895    52 VLVIGCGNSELSEQLYDVGYRDIVNIDISEVVIKQMKECNATRRPQMSFLKMDMTQMEFPDASFQVVLDKGTLDAVltde 131
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLPFPDGSFDLVVSSGVLHHL---- 76

                          90
                  ....*....|....*....
gi 55956895   132 eekTLQQVDRMLAEVGRVL 150
Cdd:pfam13649  77 ---PDPDLEAALREIARVL 92
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 30-175 1.75e-12

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: 65.02  E-value: 1.75e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956895  30 EWYGTYLELCGVLHkyIKPREKVLVIGCGNSELSEQLYDVGYRdIVNIDISEVVIKQMKECNATRRPQMSFLKMDMTQME 109
Cdd:COG2226   6 ARYDGREALLAALG--LRPGARVLDLGCGTGRLALALAERGAR-VTGVDISPEMLELARERAAEAGLNVEFVVGDAEDLP 82

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 55956895 110 FPDASFQVVLDKGTLDAVltDEEEKTLQQVDRMLAEVGRVLqgrETEWLFGMDEGRKQLAASAGFR 175
Cdd:COG2226  83 FPDGSFDLVISSFVLHHL--PDPERALAEIARVLKPGGRLV---VVDFSPPDLAELEELLAEAGFE 143
MFS_SpdSyn NF037959
fused MFS/spermidine synthase; Proteins of this family are fusion of a N-terminal MFS (Major ...
 318-479 6.14e-10

fused MFS/spermidine synthase; Proteins of this family are fusion of a N-terminal MFS (Major Facilitator Superfamily) transporter domain and a C-terminal spermidine synthase (SpdSyn)-like domain. The encoding genes usually near the genes encoding S-adenosylmethionine decarboxylase (AdoMetDC) on many bacterial genomes. It has been shown in Shewanella oneidensis that the fused protein aminopropylates a substrate other than putrescine, and has a role outside of polyamine biosynthesis.


Pssm-ID: 468290 [Multi-domain]  Cd Length: 480  Bit Score: 61.40  E-value: 6.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956895  318 HKAMIAGLALLRNPELLLEIPLallvvgLGGG--SLPLFVHDHFPKSCIDAVEIDPSMLEVATQWFGFsQSDRMKVHIAD 395
Cdd:NF037959 260 YAAMLDELARLRMGRADFSAFF------IGGGayTLPRAWAARRPAGRITVAEIDPAVTRVAAEDFWF-DPASATVLHED 332

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956895  396 gldyiASLAGGGEARPCYDVIMFDVdSKDPTLgmscpPPAFVEQSFLQKVKSILTPEGVFILNLV--CRDLGLKDSVLAG 473
Cdd:NF037959 333 -----ARRALRRRPEERFDVIVGDA-FTDIAV-----PAHLVTREFFELVRARLTPDGVYLMNVIdhADRLRALAALVAT 401


                 ....*.
gi 55956895  474 LKAVFP 479
Cdd:NF037959 402 LREVFP 407
Spermine_synth pfam01564
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ...
 321-479 6.87e-09

Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family includes spermidine synthase that catalyzes the fifth (last) step in the biosynthesis of spermidine from arginine, and spermine synthase.


Pssm-ID: 396237 [Multi-domain]  Cd Length: 183  Bit Score: 55.40  E-value: 6.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956895   321 MIAGLALLRNPELLLeiplallVVGLGGGSL----PLFVHDhfPKSCIDAVEIDPSMLEVATQWF----GFSQSDRMKVH 392
Cdd:pfam01564   7 MIAHVPLCSHPNPKK-------VLIIGGGDGgvlrEVVKHP--SVEKITLVDIDEKVIDFSKKFLpslaIGFQDPRVKVV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956895   393 IADGLDYIASLAGGgearpcYDVIMfdVDSKDPTlgmsCPPPAFVEQSFLQKVKSILTPEGVFILNLVCRDLGLKD--SV 470
Cdd:pfam01564  78 IGDGFKFLKDYLNT------FDVII--VDSTDPV----GPAENLFSKPFFDLLKKALKEDGVFITQAESPWLHLELiiNI 145


                  ....*....
gi 55956895   471 LAGLKAVFP 479
Cdd:pfam01564 146 LKNGKQVFP 154
PRK08317 PRK08317
hypothetical protein; Provisional
 46-157 3.32e-07

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 51.48  E-value: 3.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956895   46 IKPREKVLVIGCGNS----ELSEQLYDVGyrDIVNIDISEVVIKQMKECNATRRPQMSFLKMDMTQMEFPDASFqvvldk 121
Cdd:PRK08317  17 VQPGDRVLDVGCGPGndarELARRVGPEG--RVVGIDRSEAMLALAKERAAGLGPNVEFVRGDADGLPFPDGSF------ 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 55956895  122 gtlDAVLTDEEEKTLQQVDRMLAEVGRVLQ--GR----ETEW 157
Cdd:PRK08317  89 ---DAVRSDRVLQHLEDPARALAEIARVLRpgGRvvvlDTDW 127
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 51-150 8.00e-07

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: 47.81  E-value: 8.00e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956895  51 KVLVIGCGNSELSEQLYDVGYRDIVNIDISEVVIKQMKECNATRRPQ-MSFLKMDMTQ-MEFPDASFQVVLDKGTLDAVL 128
Cdd:cd02440   1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADnVEVLKGDAEElPPEADESFDVIISDPPLHHLV 80

                        90       100
                ....*....|....*....|..
gi 55956895 129 TDEEEkTLQQVDRMLAEVGRVL 150
Cdd:cd02440  81 EDLAR-FLEEARRLLKPGGVLV 101
 
Name Accession Description Interval E-value
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
343-483 1.15e-28

Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 112.61  E-value: 1.15e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956895 343 VVGLGGGSLPLFVHDHFPKSCIDAVEIDPSMLEVATQWFGFSQS----DRMKVHIADGLDYIAslagggEARPCYDVIMf 418
Cdd:COG0421  43 IIGGGDGGLARELLKHPPVERVDVVEIDPEVVELAREYFPLLAPafddPRLRVVIGDGRAFLR------EAEESYDVII- 115

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55956895 419 dVDSKDPTlgmsCPPPAFVEQSFLQKVKSILTPEGVFILNLVCRDLGLK--DSVLAGLKAVFPLLYV 483
Cdd:COG0421 116 -VDLTDPV----GPAEGLFTREFYEDCRRALKPGGVLVVNLGSPFYGLDllRRVLATLREVFPHVVL 177
PRK04457 PRK04457
polyamine aminopropyltransferase;
343-517 1.06e-20

polyamine aminopropyltransferase;


Pssm-ID: 179854 [Multi-domain]  Cd Length: 262  Bit Score: 91.64  E-value: 1.06e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956895  343 VVGLGGGSLPLFVHDHFPKSCIDAVEIDPSMLEVA-TQWFGFSQSDRMKVHIADGLDYIAslagggEARPCYDVIMFD-V 420
Cdd:PRK04457  72 QIGLGGGSLAKFIYTYLPDTRQTAVEINPQVIAVArNHFELPENGERFEVIEADGAEYIA------VHRHSTDVILVDgF 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956895  421 DSKDptlgmscPPPAFVEQSFLQKVKSILTPEGVFILNLVCRDlGLKDSVLAGLKAVFP-LLYVRRIEGEVNEILFCQLH 499
Cdd:PRK04457 146 DGEG-------IIDALCTQPFFDDCRNALSSDGIFVVNLWSRD-KRYDRYLERLESSFEgRVLELPAESHGNVAVFAFKS 217

                        170
                 ....*....|....*...
gi 55956895  500 PEQKLATPELLETAQALE 517
Cdd:PRK04457 218 APKELRWDKLRKRAKKLE 235
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 52-150 1.07e-13

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 66.82  E-value: 1.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956895    52 VLVIGCGNSELSEQLYDVGYRDIVNIDISEVVIKQMKECNATRRPQMSFLKMDMTQMEFPDASFQVVLDKGTLDAVltde 131
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLPFPDGSFDLVVSSGVLHHL---- 76

                          90
                  ....*....|....*....
gi 55956895   132 eekTLQQVDRMLAEVGRVL 150
Cdd:pfam13649  77 ---PDPDLEAALREIARVL 92
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 30-175 1.75e-12

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: 65.02  E-value: 1.75e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956895  30 EWYGTYLELCGVLHkyIKPREKVLVIGCGNSELSEQLYDVGYRdIVNIDISEVVIKQMKECNATRRPQMSFLKMDMTQME 109
Cdd:COG2226   6 ARYDGREALLAALG--LRPGARVLDLGCGTGRLALALAERGAR-VTGVDISPEMLELARERAAEAGLNVEFVVGDAEDLP 82

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 55956895 110 FPDASFQVVLDKGTLDAVltDEEEKTLQQVDRMLAEVGRVLqgrETEWLFGMDEGRKQLAASAGFR 175
Cdd:COG2226  83 FPDGSFDLVISSFVLHHL--PDPERALAEIARVLKPGGRLV---VVDFSPPDLAELEELLAEAGFE 143
MFS_SpdSyn NF037959
fused MFS/spermidine synthase; Proteins of this family are fusion of a N-terminal MFS (Major ...
 318-479 6.14e-10

fused MFS/spermidine synthase; Proteins of this family are fusion of a N-terminal MFS (Major Facilitator Superfamily) transporter domain and a C-terminal spermidine synthase (SpdSyn)-like domain. The encoding genes usually near the genes encoding S-adenosylmethionine decarboxylase (AdoMetDC) on many bacterial genomes. It has been shown in Shewanella oneidensis that the fused protein aminopropylates a substrate other than putrescine, and has a role outside of polyamine biosynthesis.


Pssm-ID: 468290 [Multi-domain]  Cd Length: 480  Bit Score: 61.40  E-value: 6.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956895  318 HKAMIAGLALLRNPELLLEIPLallvvgLGGG--SLPLFVHDHFPKSCIDAVEIDPSMLEVATQWFGFsQSDRMKVHIAD 395
Cdd:NF037959 260 YAAMLDELARLRMGRADFSAFF------IGGGayTLPRAWAARRPAGRITVAEIDPAVTRVAAEDFWF-DPASATVLHED 332

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956895  396 gldyiASLAGGGEARPCYDVIMFDVdSKDPTLgmscpPPAFVEQSFLQKVKSILTPEGVFILNLV--CRDLGLKDSVLAG 473
Cdd:NF037959 333 -----ARRALRRRPEERFDVIVGDA-FTDIAV-----PAHLVTREFFELVRARLTPDGVYLMNVIdhADRLRALAALVAT 401


                 ....*.
gi 55956895  474 LKAVFP 479
Cdd:NF037959 402 LREVFP 407
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 37-150 6.98e-10

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: 56.95  E-value: 6.98e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956895  37 ELCGVLHKYIKPREKVLVIGCGNSELSEQLYDVGYrDIVNIDISEVVIKQMKEcnATRRPQMSFLKMDMTQMEFPDASFQ 116
Cdd:COG2227  13 RLAALLARLLPAGGRVLDVGCGTGRLALALARRGA-DVTGVDISPEALEIARE--RAAELNVDFVQGDLEDLPLEDGSFD 89

                        90       100       110
                ....*....|....*....|....*....|....
gi 55956895 117 VVLDKGTLDAVltDEEEKTLQQVDRMLAEVGRVL 150
Cdd:COG2227  90 LVICSEVLEHL--PDPAALLRELARLLKPGGLLL 121
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 53-143 5.12e-09

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 53.44  E-value: 5.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956895    53 LVIGCGNSELSEQLYDVGYRdIVNIDISEVVIKQMKECNatRRPQMSFLKMDMTQMEFPDASFQVVLDKGTLDAVltDEE 132
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGAR-VTGVDISPEMLELAREKA--PREGLTFVVGDAEDLPFPDNSFDLVLSSEVLHHV--EDP 75

                          90
                  ....*....|.
gi 55956895   133 EKTLQQVDRML 143
Cdd:pfam08241  76 ERALREIARVL 86
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 46-150 6.85e-09

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 54.73  E-value: 6.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956895    46 IKPREKVLVIGCGNSELSEQLYDVGYRD--IVNIDISEVVIKQMKEcNATRRP--QMSFLKMDMTQME--FPDASFQVVL 119
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSFELAEELGPNaeVVGIDISEEAIEKARE-NAQKLGfdNVEFEQGDIEELPelLEDDKFDVVI 79

                          90       100       110
                  ....*....|....*....|....*....|.
gi 55956895   120 DKGTLDAVltDEEEKTLQQVDRMLAEVGRVL 150
Cdd:pfam13847  80 SNCVLNHI--PDPDKVLQEILRVLKPGGRLI 108
Spermine_synth pfam01564
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ...
 321-479 6.87e-09

Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family includes spermidine synthase that catalyzes the fifth (last) step in the biosynthesis of spermidine from arginine, and spermine synthase.


Pssm-ID: 396237 [Multi-domain]  Cd Length: 183  Bit Score: 55.40  E-value: 6.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956895   321 MIAGLALLRNPELLLeiplallVVGLGGGSL----PLFVHDhfPKSCIDAVEIDPSMLEVATQWF----GFSQSDRMKVH 392
Cdd:pfam01564   7 MIAHVPLCSHPNPKK-------VLIIGGGDGgvlrEVVKHP--SVEKITLVDIDEKVIDFSKKFLpslaIGFQDPRVKVV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956895   393 IADGLDYIASLAGGgearpcYDVIMfdVDSKDPTlgmsCPPPAFVEQSFLQKVKSILTPEGVFILNLVCRDLGLKD--SV 470
Cdd:pfam01564  78 IGDGFKFLKDYLNT------FDVII--VDSTDPV----GPAENLFSKPFFDLLKKALKEDGVFITQAESPWLHLELiiNI 145


                  ....*....
gi 55956895   471 LAGLKAVFP 479
Cdd:pfam01564 146 LKNGKQVFP 154
PRK00811 PRK00811
polyamine aminopropyltransferase;
364-456 2.89e-08

polyamine aminopropyltransferase;


Pssm-ID: 234843 [Multi-domain]  Cd Length: 283  Bit Score: 55.16  E-value: 2.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956895  364 IDAVEIDPSMLEVATQWF-----GFSQSDRMKVHIADGLDYIAslagggEARPCYDVIMfdVDSKDPTlGmscppPA--- 435
Cdd:PRK00811 103 ITLVEIDERVVEVCRKYLpeiagGAYDDPRVELVIGDGIKFVA------ETENSFDVII--VDSTDPV-G-----PAegl 168

                         90       100
                 ....*....|....*....|.
gi 55956895  436 FvEQSFLQKVKSILTPEGVFI 456
Cdd:PRK00811 169 F-TKEFYENCKRALKEDGIFV 188
PRK08317 PRK08317
hypothetical protein; Provisional
 46-157 3.32e-07

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 51.48  E-value: 3.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956895   46 IKPREKVLVIGCGNS----ELSEQLYDVGyrDIVNIDISEVVIKQMKECNATRRPQMSFLKMDMTQMEFPDASFqvvldk 121
Cdd:PRK08317  17 VQPGDRVLDVGCGPGndarELARRVGPEG--RVVGIDRSEAMLALAKERAAGLGPNVEFVRGDADGLPFPDGSF------ 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 55956895  122 gtlDAVLTDEEEKTLQQVDRMLAEVGRVLQ--GR----ETEW 157
Cdd:PRK08317  89 ---DAVRSDRVLQHLEDPARALAEIARVLRpgGRvvvlDTDW 127
PLN02366 PLN02366
spermidine synthase
 364-454 4.58e-07

spermidine synthase


Pssm-ID: 215208 [Multi-domain]  Cd Length: 308  Bit Score: 51.57  E-value: 4.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956895  364 IDAVEIDPSMLEVATQWF-----GFSQSdRMKVHIADGLDYIASLAGGGearpcYDVIMfdVDSKDPtLGmscPPPAFVE 438
Cdd:PLN02366 118 IDICEIDKMVIDVSKKFFpdlavGFDDP-RVNLHIGDGVEFLKNAPEGT-----YDAII--VDSSDP-VG---PAQELFE 185

                         90
                 ....*....|....*.
gi 55956895  439 QSFLQKVKSILTPEGV 454
Cdd:PLN02366 186 KPFFESVARALRPGGV 201
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 51-150 8.00e-07

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: 47.81  E-value: 8.00e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956895  51 KVLVIGCGNSELSEQLYDVGYRDIVNIDISEVVIKQMKECNATRRPQ-MSFLKMDMTQ-MEFPDASFQVVLDKGTLDAVL 128
Cdd:cd02440   1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADnVEVLKGDAEElPPEADESFDVIISDPPLHHLV 80

                        90       100
                ....*....|....*....|..
gi 55956895 129 TDEEEkTLQQVDRMLAEVGRVL 150
Cdd:cd02440  81 EDLAR-FLEEARRLLKPGGVLV 101
COG4262 COG4262
Predicted spermidine synthase with an N-terminal membrane domain [General function prediction ...
 364-459 1.48e-06

Predicted spermidine synthase with an N-terminal membrane domain [General function prediction only];


Pssm-ID: 443404 [Multi-domain]  Cd Length: 426  Bit Score: 50.63  E-value: 1.48e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956895 364 IDAVEIDPSMLEVATQWFGFSQ-------SDRMKVHIADGLDYIAslagggEARPCYDVIMFD-VDSKDPTLGmscpppA 435
Cdd:COG4262 313 VTLVDLDPEVTDLAKTNPFLRElnggalnDPRVTVVNADAFQFLR------ETDEKYDVIIVDlPDPSNFSLG------K 380

                        90       100
                ....*....|....*....|....
gi 55956895 436 FVEQSFLQKVKSILTPEGVFILNL 459
Cdd:COG4262 381 LYSVEFYRLVRRHLAPGGVLVVQA 404
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
46-174 3.37e-05

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 44.60  E-value: 3.37e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956895  46 IKPREKVLVIGCGNSELSEQLYDVGYRdIVNIDISEVVIKQMKEcnatRRPQMSFLKMDMTQMEFPDASFQVVLDKGTLD 125
Cdd:COG4976  44 PGPFGRVLDLGCGTGLLGEALRPRGYR-LTGVDLSEEMLAKARE----KGVYDRLLVADLADLAEPDGRFDLIVAADVLT 118

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 55956895 126 AVltDEEEKTLQQVDRMLAEVGRV---LQGRETEWLFGMDEGR-KQLAASAGF 174
Cdd:COG4976 119 YL--GDLAAVFAGVARALKPGGLFifsVEDADGSGRYAHSLDYvRDLLAAAGF 169
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 344-457 4.21e-05

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: 45.14  E-value: 4.21e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956895 344 VGLGGGSLPLFVHDHFPKSCIDAVEIDPSMLEVATQWFGFSQ-SDRMKVHIADGLDYIASLAGGgearpCYDVIM----- 417
Cdd:COG4123  44 LGTGTGVIALMLAQRSPGARITGVEIQPEAAELARRNVALNGlEDRITVIHGDLKEFAAELPPG-----SFDLVVsnppy 118

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 55956895 418 FDVDSkdptlGMSCPPP----AFVE-----QSFLQKVKSILTPEGVFIL 457
Cdd:COG4123 119 FKAGS-----GRKSPDEaraiARHEdaltlEDLIRAAARLLKPGGRFAL 162
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 46-150 9.14e-05

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 42.99  E-value: 9.14e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956895  46 IKPREKVLVIGCGNSELSEQL---YDVgyrDIVNIDISEVVIKQMKECNATR--RPQMSFLKMDMTQMEfPDASFQVVLD 120
Cdd:COG2230  49 LKPGMRVLDIGCGWGGLALYLarrYGV---RVTGVTLSPEQLEYARERAAEAglADRVEVRLADYRDLP-ADGQFDAIVS 124

                        90       100       110
                ....*....|....*....|....*....|
gi 55956895 121 KGTLDAVLTDEEEKTLQQVDRMLAEVGRVL 150
Cdd:COG2230 125 IGMFEHVGPENYPAYFAKVARLLKPGGRLL 154
PLN03075 PLN03075
nicotianamine synthase; Provisional
 346-416 3.07e-03

nicotianamine synthase; Provisional


Pssm-ID: 178624  Cd Length: 296  Bit Score: 39.65  E-value: 3.07e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55956895  346 LGGGSLPL----FVHDHFPKSCIDAVEIDPSMLEVATQWFGF--SQSDRMKVHIADGLDYIASLAGggearpcYDVI 416
Cdd:PLN03075 130 VGSGPLPLtsivLAKHHLPTTSFHNFDIDPSANDVARRLVSSdpDLSKRMFFHTADVMDVTESLKE-------YDVV 199
 
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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