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Conserved domains on  [gi|1108555412|gb|APE47022|]
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spermidine synthase [Delftia sp. HK171]

Protein Classification

bifunctional adenosylmethionine decarboxylase/class I SAM-dependent methyltransferase( domain architecture ID 11133641)

bifunctional adenosylmethionine decarboxylase/class I SAM-dependent methyltransferase catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet) and/or the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK00811 PRK00811
polyamine aminopropyltransferase;
139-416 6.24e-107

polyamine aminopropyltransferase;


:

Pssm-ID: 234843 [Multi-domain]  Cd Length: 283  Bit Score: 317.48  E-value: 6.24e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 139 WALEALTPHARFGWRAMRR-ETVQTPHQELELLHTPQFGKVLRLDGRFMTSEGEEFFYHEALVHPAALAHPAPRKALILG 217
Cdd:PRK00811    5 WFTETLTDNYGQSFRVKKVlYEEKSPFQRIEIFETPEFGRLLALDGCVMTTERDEFIYHEMMTHVPLFAHPNPKRVLIIG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 218 GGDGGAAEELLKHPSMEQVVVAELDEAVVQAARTHLQQVHRGVFDDPRLQLRIGDGMAMVEHTEERFDLALMDLTDPDTP 297
Cdd:PRK00811   85 GGDGGTLREVLKHPSVEKITLVEIDERVVEVCRKYLPEIAGGAYDDPRVELVIGDGIKFVAETENSFDVIIVDSTDPVGP 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 298 ASALYSDQALARMKRVLAPGGALVLHLGSPVFHGEQVARLVASLRERFAIVRCYGLYIPLY-GAYWGLAVASDTLDAAAL 376
Cdd:PRK00811  165 AEGLFTKEFYENCKRALKEDGIFVAQSGSPFYQADEIKDMHRKLKEVFPIVRPYQAAIPTYpSGLWSFTFASKNDDLKFL 244

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1108555412 377 PPAQLRQRLAERRLpDLRYYNAEVHPALFALPNYYRDLVQ 416
Cdd:PRK00811  245 PLDVIEARFAERGI-KTRYYNPELHKAAFALPQFVKDALK 283
SpeD COG1586
S-adenosylmethionine decarboxylase [Amino acid transport and metabolism];
1-126 7.04e-37

S-adenosylmethionine decarboxylase [Amino acid transport and metabolism];


:

Pssm-ID: 441194  Cd Length: 118  Bit Score: 130.71  E-value: 7.04e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412   1 MHGLHLTADLYQCqgDARHMLDADAIAALCRAQTAQAGLTLVEDRWVKFPdyqgqPGGVTGTVLLAESHLAIHTWPETGC 80
Cdd:COG1586     2 FLGKHLIADLYGC--DPELLNDAERLEEILVEAAEAAGATVLGVAFHKFE-----PQGVSGVVLLAESHISIHTWPEYGY 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1108555412  81 VTVDVYVCNFSADnsgkARALMEGVIAAYAPGRVVRQQLMRGDIGP 126
Cdd:COG1586    75 AAVDVFTCGDDID----PEKALEYLKEAFGADKVEVTELKRGFTRD 116
 
Name Accession Description Interval E-value
PRK00811 PRK00811
polyamine aminopropyltransferase;
139-416 6.24e-107

polyamine aminopropyltransferase;


Pssm-ID: 234843 [Multi-domain]  Cd Length: 283  Bit Score: 317.48  E-value: 6.24e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 139 WALEALTPHARFGWRAMRR-ETVQTPHQELELLHTPQFGKVLRLDGRFMTSEGEEFFYHEALVHPAALAHPAPRKALILG 217
Cdd:PRK00811    5 WFTETLTDNYGQSFRVKKVlYEEKSPFQRIEIFETPEFGRLLALDGCVMTTERDEFIYHEMMTHVPLFAHPNPKRVLIIG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 218 GGDGGAAEELLKHPSMEQVVVAELDEAVVQAARTHLQQVHRGVFDDPRLQLRIGDGMAMVEHTEERFDLALMDLTDPDTP 297
Cdd:PRK00811   85 GGDGGTLREVLKHPSVEKITLVEIDERVVEVCRKYLPEIAGGAYDDPRVELVIGDGIKFVAETENSFDVIIVDSTDPVGP 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 298 ASALYSDQALARMKRVLAPGGALVLHLGSPVFHGEQVARLVASLRERFAIVRCYGLYIPLY-GAYWGLAVASDTLDAAAL 376
Cdd:PRK00811  165 AEGLFTKEFYENCKRALKEDGIFVAQSGSPFYQADEIKDMHRKLKEVFPIVRPYQAAIPTYpSGLWSFTFASKNDDLKFL 244

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1108555412 377 PPAQLRQRLAERRLpDLRYYNAEVHPALFALPNYYRDLVQ 416
Cdd:PRK00811  245 PLDVIEARFAERGI-KTRYYNPELHKAAFALPQFVKDALK 283
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
176-367 3.88e-63

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


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 201.98  E-value: 3.88e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 176 GKVLRLDGRFMTS-EGEEFFYHEALVHPAALAHPAPRKALILGGGDGGAAEELLKHPSMEQVVVAELDEAVVQAARTHLQ 254
Cdd:COG0421     3 GRVLVLDGVVQSTmELDEFEYHEMMAHVPLLFHPNPKRVLIIGGGDGGLARELLKHPPVERVDVVEIDPEVVELAREYFP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 255 QVhRGVFDDPRLQLRIGDGMAMVEHTEERFDLALMDLTDPDTPASALYSDQALARMKRVLAPGGALVLHLGSPVFHGEQV 334
Cdd:COG0421    83 LL-APAFDDPRLRVVIGDGRAFLREAEESYDVIIVDLTDPVGPAEGLFTREFYEDCRRALKPGGVLVVNLGSPFYGLDLL 161

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1108555412 335 ARLVASLRERFAIVRCYGLYIPLYGAYWGLAVA 367
Cdd:COG0421   162 RRVLATLREVFPHVVLYAAPVPTYGGGNVFLLA 194
speE TIGR00417
spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine ...
 161-410 2.62e-58

spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine + S-adenosylmethioninamine = spermidine + 5'-methylthioadenosine) and is involved in polyamine biosynthesis and in the biosynthesis of spermidine from arganine. The region between residues 77 and 120 of the seed alignment is thought to be involved in binding to decarboxylated SAM. [Central intermediary metabolism, Polyamine biosynthesis]


Pssm-ID: 188048 [Multi-domain]  Cd Length: 271  Bit Score: 192.26  E-value: 2.62e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 161 QTPHQELELLHTPQFGKVLRLDGRFMTSEGEEFFYHEALVHPAALAHPAPRKALILGGGDGGAAEELLKHPSMEQVVVAE 240
Cdd:TIGR00417  24 KSEFQDLEIFETEAFGNVLVLDGVVQTTERDEFIYHEMITHVPLFTHPNPKHVLVIGGGDGGVLREVLKHKSVESATLVD 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 241 LDEAVVQAARTHLQQVHrGVFDDPRLQLRIGDGMAMVEHTEERFDLALMDLTDPDTPASALYSDQALARMKRVLAPGGAL 320
Cdd:TIGR00417 104 IDEKVIELSRKYLPNLA-GSYDDPRVKLVIDDGFKFLADTENTFDVIIVDSTDPVGPAETLFTKEFYELLKKALNPDGIF 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 321 VLHLGSPVFHGEQVARLVASLRERFAIVRCYGLYIPLY-GAYWGLAVASDTldaaALPPAQLRQRLAERRLPDL--RYYN 397
Cdd:TIGR00417 183 VAQSESPWLQLELIIDLKRKLKEAFPITEYYTAAIPTYpSGLWTFTIASKN----KYRPLEVEIRRIKFEAEDGktKYYN 258

                         250
                  ....*....|...
gi 1108555412 398 AEVHPALFALPNY 410
Cdd:TIGR00417 259 PDIHKAAFVLPKW 271
SpeD COG1586
S-adenosylmethionine decarboxylase [Amino acid transport and metabolism];
1-126 7.04e-37

S-adenosylmethionine decarboxylase [Amino acid transport and metabolism];


Pssm-ID: 441194  Cd Length: 118  Bit Score: 130.71  E-value: 7.04e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412   1 MHGLHLTADLYQCqgDARHMLDADAIAALCRAQTAQAGLTLVEDRWVKFPdyqgqPGGVTGTVLLAESHLAIHTWPETGC 80
Cdd:COG1586     2 FLGKHLIADLYGC--DPELLNDAERLEEILVEAAEAAGATVLGVAFHKFE-----PQGVSGVVLLAESHISIHTWPEYGY 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1108555412  81 VTVDVYVCNFSADnsgkARALMEGVIAAYAPGRVVRQQLMRGDIGP 126
Cdd:COG1586    75 AAVDVFTCGDDID----PEKALEYLKEAFGADKVEVTELKRGFTRD 116
Spermine_synth pfam01564
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ...
 192-369 1.01e-36

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: 132.44  E-value: 1.01e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 192 EFFYHEALVHPAALAHPAPRKALILGGGDGGAAEELLKHPSMEQVVVAELDEAVVQAARTHLQQVHrGVFDDPRLQLRIG 271
Cdd:pfam01564   1 EFIYHEMIAHVPLCSHPNPKKVLIIGGGDGGVLREVVKHPSVEKITLVDIDEKVIDFSKKFLPSLA-IGFQDPRVKVVIG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 272 DGMAMVEHTEERFDLALMDLTDPDTPASALYSDQALARMKRVLAPGGALVLHLGSPVFHGEQVARLVASLRERFAIVRCY 351
Cdd:pfam01564  80 DGFKFLKDYLNTFDVIIVDSTDPVGPAENLFSKPFFDLLKKALKEDGVFITQAESPWLHLELIINILKNGKQVFPVVMPY 159

                         170
                  ....*....|....*....
gi 1108555412 352 GLYIPLY-GAYWGLAVASD 369
Cdd:pfam01564 160 VATIPTYpSGGWGFTVCSK 178
AdoMet_dc pfam02675
S-adenosylmethionine decarboxylase; This family contains several S-adenosylmethionine ...
 5-122 1.33e-30

S-adenosylmethionine decarboxylase; This family contains several S-adenosylmethionine decarboxylase proteins from bacterial and archaebacterial species. S-adenosylmethionine decarboxylase (AdoMetDC), a key enzyme in the biosynthesis of spermidine and spermine, is first synthesized as a proenzyme, which is cleaved post translationally to form alpha and beta subunits. The alpha subunit contains a covalently bound pyruvoyl group derived from serine that is essential for activity.


Pssm-ID: 460648  Cd Length: 107  Bit Score: 113.76  E-value: 1.33e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412   5 HLTADLYQCQGDArhMLDADAIAALCRAQTAQAGLTLVEDRWVKFPdyqgqPGGVTGTVLLAESHLAIHTWPETGCVTVD 84
Cdd:pfam02675   1 HLIVDLYGCDPEL--LDDAELIEQALREAAEAAGATVVEVVFHKFE-----PQGVSGVVLLAESHISIHTWPEYGYAAVD 73

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1108555412  85 VYVCNFSADnsgkARALMEGVIAAYAPGRVVRQQLMRG 122
Cdd:pfam02675  74 VFTCGDHVD----PEKAFEYLKEALGAKRVSVRELDRG 107
SAM_DCase_Bsu TIGR03330
S-adenosylmethionine decarboxylase proenzyme, Bacillus form; Members of this protein family ...
 3-122 1.62e-21

S-adenosylmethionine decarboxylase proenzyme, Bacillus form; Members of this protein family are the single chain precursor of the two chains of the mature S-adenosylmethionine decarboxylase as found in Methanocaldococcus jannaschii, Bacillus subtilis, and a wide range of other species. It differs substantially in architecture from the form as found in Escherichia coli, and lacks any extended homology to the eukaryotic form (TIGR00535). [Central intermediary metabolism, Polyamine biosynthesis]


Pssm-ID: 274523  Cd Length: 112  Bit Score: 89.20  E-value: 1.62e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412   3 GLHLTADLYQCqgDARHMLDADAI-AALCRAqTAQAGLTLVEDRWVKFPdyqgqPGGVTGTVLLAESHLAIHTWPETGCV 81
Cdd:TIGR03330   4 GRHLIVDLYGC--DPEKLDDVEFIeEILLEA-AKVAGATLVASHFHKFS-----PGGVSGVVLLAESHISIHTWPEYGYA 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1108555412  82 TVDVYVCnfsADNSGKARALmEGVIAAYAPGRVVRQQLMRG 122
Cdd:TIGR03330  76 AVDVFTC---GDHSDPEKAF-EYLVEALKPKRVEVRELDRG 112
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 224-324 2.46e-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: 40.11  E-value: 2.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 224 AEELLKHPSmEQVVVAELDEAVVQAARTHLQQVHRgvfddPRLQLRIGDGMAMVEHTEERFDLALMDLTDPDTPASAlys 303
Cdd:cd02440    13 ALALASGPG-ARVTGVDISPVALELARKAAAALLA-----DNVEVLKGDAEELPPEADESFDVIISDPPLHHLVEDL--- 83

                          90       100
                  ....*....|....*....|.
gi 1108555412 304 DQALARMKRVLAPGGALVLHL 324
Cdd:cd02440    84 ARFLEEARRLLKPGGVLVLTL 104
 
Name Accession Description Interval E-value
PRK00811 PRK00811
polyamine aminopropyltransferase;
139-416 6.24e-107

polyamine aminopropyltransferase;


Pssm-ID: 234843 [Multi-domain]  Cd Length: 283  Bit Score: 317.48  E-value: 6.24e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 139 WALEALTPHARFGWRAMRR-ETVQTPHQELELLHTPQFGKVLRLDGRFMTSEGEEFFYHEALVHPAALAHPAPRKALILG 217
Cdd:PRK00811    5 WFTETLTDNYGQSFRVKKVlYEEKSPFQRIEIFETPEFGRLLALDGCVMTTERDEFIYHEMMTHVPLFAHPNPKRVLIIG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 218 GGDGGAAEELLKHPSMEQVVVAELDEAVVQAARTHLQQVHRGVFDDPRLQLRIGDGMAMVEHTEERFDLALMDLTDPDTP 297
Cdd:PRK00811   85 GGDGGTLREVLKHPSVEKITLVEIDERVVEVCRKYLPEIAGGAYDDPRVELVIGDGIKFVAETENSFDVIIVDSTDPVGP 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 298 ASALYSDQALARMKRVLAPGGALVLHLGSPVFHGEQVARLVASLRERFAIVRCYGLYIPLY-GAYWGLAVASDTLDAAAL 376
Cdd:PRK00811  165 AEGLFTKEFYENCKRALKEDGIFVAQSGSPFYQADEIKDMHRKLKEVFPIVRPYQAAIPTYpSGLWSFTFASKNDDLKFL 244

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1108555412 377 PPAQLRQRLAERRLpDLRYYNAEVHPALFALPNYYRDLVQ 416
Cdd:PRK00811  245 PLDVIEARFAERGI-KTRYYNPELHKAAFALPQFVKDALK 283
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
176-367 3.88e-63

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


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 201.98  E-value: 3.88e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 176 GKVLRLDGRFMTS-EGEEFFYHEALVHPAALAHPAPRKALILGGGDGGAAEELLKHPSMEQVVVAELDEAVVQAARTHLQ 254
Cdd:COG0421     3 GRVLVLDGVVQSTmELDEFEYHEMMAHVPLLFHPNPKRVLIIGGGDGGLARELLKHPPVERVDVVEIDPEVVELAREYFP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 255 QVhRGVFDDPRLQLRIGDGMAMVEHTEERFDLALMDLTDPDTPASALYSDQALARMKRVLAPGGALVLHLGSPVFHGEQV 334
Cdd:COG0421    83 LL-APAFDDPRLRVVIGDGRAFLREAEESYDVIIVDLTDPVGPAEGLFTREFYEDCRRALKPGGVLVVNLGSPFYGLDLL 161

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1108555412 335 ARLVASLRERFAIVRCYGLYIPLYGAYWGLAVA 367
Cdd:COG0421   162 RRVLATLREVFPHVVLYAAPVPTYGGGNVFLLA 194
speE TIGR00417
spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine ...
 161-410 2.62e-58

spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine + S-adenosylmethioninamine = spermidine + 5'-methylthioadenosine) and is involved in polyamine biosynthesis and in the biosynthesis of spermidine from arganine. The region between residues 77 and 120 of the seed alignment is thought to be involved in binding to decarboxylated SAM. [Central intermediary metabolism, Polyamine biosynthesis]


Pssm-ID: 188048 [Multi-domain]  Cd Length: 271  Bit Score: 192.26  E-value: 2.62e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 161 QTPHQELELLHTPQFGKVLRLDGRFMTSEGEEFFYHEALVHPAALAHPAPRKALILGGGDGGAAEELLKHPSMEQVVVAE 240
Cdd:TIGR00417  24 KSEFQDLEIFETEAFGNVLVLDGVVQTTERDEFIYHEMITHVPLFTHPNPKHVLVIGGGDGGVLREVLKHKSVESATLVD 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 241 LDEAVVQAARTHLQQVHrGVFDDPRLQLRIGDGMAMVEHTEERFDLALMDLTDPDTPASALYSDQALARMKRVLAPGGAL 320
Cdd:TIGR00417 104 IDEKVIELSRKYLPNLA-GSYDDPRVKLVIDDGFKFLADTENTFDVIIVDSTDPVGPAETLFTKEFYELLKKALNPDGIF 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 321 VLHLGSPVFHGEQVARLVASLRERFAIVRCYGLYIPLY-GAYWGLAVASDTldaaALPPAQLRQRLAERRLPDL--RYYN 397
Cdd:TIGR00417 183 VAQSESPWLQLELIIDLKRKLKEAFPITEYYTAAIPTYpSGLWTFTIASKN----KYRPLEVEIRRIKFEAEDGktKYYN 258

                         250
                  ....*....|...
gi 1108555412 398 AEVHPALFALPNY 410
Cdd:TIGR00417 259 PDIHKAAFVLPKW 271
PLN02823 PLN02823
spermine synthase
 159-412 8.16e-57

spermine synthase


Pssm-ID: 178418 [Multi-domain]  Cd Length: 336  Bit Score: 190.28  E-value: 8.16e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 159 TVQTPHQELELLHTPQFGKVLRLDGRFMTSEGEEFFYHEALVHPAALAHPAPRKALILGGGDGGAAEELLKHPSMEQVVV 238
Cdd:PLN02823   53 TGTSEFQDIALVDTKPFGKVLIIDGKMQSAEADEFVYHESLVHPALLHHPNPKTVFIMGGGEGSTAREVLRHKTVEKVVM 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 239 AELDEAVVQAARTHLqQVHRGVFDDPRLQLRIGDGMAMVEHTEERFDLALMDLTDP--DTPASALYSDQALARM-KRVLA 315
Cdd:PLN02823  133 CDIDQEVVDFCRKHL-TVNREAFCDKRLELIINDARAELEKRDEKFDVIIGDLADPveGGPCYQLYTKSFYERIvKPKLN 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 316 PGGALVLHLGSPVF--HGEQVARLVASLRERFAIVRCYGLYIPLYGAYWGLAVASDTlDAAALPPAQLRQRLAERRLPDL 393
Cdd:PLN02823  212 PGGIFVTQAGPAGIltHKEVFSSIYNTLRQVFKYVVPYTAHVPSFADTWGWVMASDH-PFADLSAEELDSRIKERIDGEL 290

                         250
                  ....*....|....*....
gi 1108555412 394 RYYNAEVHPALFALPNYYR 412
Cdd:PLN02823  291 KYLDGETFSSAFALNKTVR 309
PRK03612 PRK03612
polyamine aminopropyltransferase;
161-417 3.43e-43

polyamine aminopropyltransferase;


Pssm-ID: 235139 [Multi-domain]  Cd Length: 521  Bit Score: 158.46  E-value: 3.43e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 161 QTPHQELELLHTPQ-FGKVLRL--DGRFMTSEGEEFFYHEALVHPAALAHPAPRKALILGGGDGGAAEELLKHPSMEQVV 237
Cdd:PRK03612  246 QTPYQRIVVTRRGNgRGPDLRLylNGRLQFSSRDEYRYHEALVHPAMAASARPRRVLVLGGGDGLALREVLKYPDVEQVT 325

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 238 VAELDEAVVQAARTH--LQQVHRGVFDDPRLQLRIGDGMAMVEHTEERFDLALMDLTDPDTPASA-LYSDQALARMKRVL 314
Cdd:PRK03612  326 LVDLDPAMTELARTSpaLRALNGGALDDPRVTVVNDDAFNWLRKLAEKFDVIIVDLPDPSNPALGkLYSVEFYRLLKRRL 405

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 315 APGGALVLHLGSPVFHGEQVARLVASLRERFAIVRCYGLYIPLYGAyWGLAVASDTLDAAALPPAQLRqrlaerrlPDLR 394
Cdd:PRK03612  406 APDGLLVVQSTSPYFAPKAFWSIEATLEAAGLATTPYHVNVPSFGE-WGFVLAGAGARPPLAVPTELP--------VPLR 476

                         250       260
                  ....*....|....*....|....
gi 1108555412 395 YYNAEVHPALFALP-NYYRDLVQP 417
Cdd:PRK03612  477 FLDPALLAAAFVFPkDMRRREVEP 500
COG4262 COG4262
Predicted spermidine synthase with an N-terminal membrane domain [General function prediction ...
 161-343 1.22e-39

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


Pssm-ID: 443404 [Multi-domain]  Cd Length: 426  Bit Score: 146.93  E-value: 1.22e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 161 QTPHQELELLHTPQFgKVLRLDGRFMTSEGEEFFYHEALVHPAALAHPAPRKALILGGGDGGAAEELLKHPSMEQVVVAE 240
Cdd:COG4262   239 QTPYQRIVVTRDKDD-RRLYLNGNLQFSSLDEYRYHEALVHPPMAAHPRPRRVLVLGGGDGLAAREVLKYPDVESVTLVD 317

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 241 LDEAVVQAARTH--LQQVHRGVFDDPRLQLRIGDGMAMVEHTEERFDLALMDLTDPDTPASA-LYSDQALARMKRVLAPG 317
Cdd:COG4262   318 LDPEVTDLAKTNpfLRELNGGALNDPRVTVVNADAFQFLRETDEKYDVIIVDLPDPSNFSLGkLYSVEFYRLVRRHLAPG 397

                         170       180
                  ....*....|....*....|....*.
gi 1108555412 318 GALVLHLGSPVFHGEQVARLVASLRE 343
Cdd:COG4262   398 GVLVVQATSPYFAPKAFWCIAKTLEA 423
SpeD COG1586
S-adenosylmethionine decarboxylase [Amino acid transport and metabolism];
1-126 7.04e-37

S-adenosylmethionine decarboxylase [Amino acid transport and metabolism];


Pssm-ID: 441194  Cd Length: 118  Bit Score: 130.71  E-value: 7.04e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412   1 MHGLHLTADLYQCqgDARHMLDADAIAALCRAQTAQAGLTLVEDRWVKFPdyqgqPGGVTGTVLLAESHLAIHTWPETGC 80
Cdd:COG1586     2 FLGKHLIADLYGC--DPELLNDAERLEEILVEAAEAAGATVLGVAFHKFE-----PQGVSGVVLLAESHISIHTWPEYGY 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1108555412  81 VTVDVYVCNFSADnsgkARALMEGVIAAYAPGRVVRQQLMRGDIGP 126
Cdd:COG1586    75 AAVDVFTCGDDID----PEKALEYLKEAFGADKVEVTELKRGFTRD 116
Spermine_synth pfam01564
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ...
 192-369 1.01e-36

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: 132.44  E-value: 1.01e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 192 EFFYHEALVHPAALAHPAPRKALILGGGDGGAAEELLKHPSMEQVVVAELDEAVVQAARTHLQQVHrGVFDDPRLQLRIG 271
Cdd:pfam01564   1 EFIYHEMIAHVPLCSHPNPKKVLIIGGGDGGVLREVVKHPSVEKITLVDIDEKVIDFSKKFLPSLA-IGFQDPRVKVVIG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 272 DGMAMVEHTEERFDLALMDLTDPDTPASALYSDQALARMKRVLAPGGALVLHLGSPVFHGEQVARLVASLRERFAIVRCY 351
Cdd:pfam01564  80 DGFKFLKDYLNTFDVIIVDSTDPVGPAENLFSKPFFDLLKKALKEDGVFITQAESPWLHLELIINILKNGKQVFPVVMPY 159

                         170
                  ....*....|....*....
gi 1108555412 352 GLYIPLY-GAYWGLAVASD 369
Cdd:pfam01564 160 VATIPTYpSGGWGFTVCSK 178
PLN02366 PLN02366
spermidine synthase
 162-412 5.38e-34

spermidine synthase


Pssm-ID: 215208 [Multi-domain]  Cd Length: 308  Bit Score: 128.99  E-value: 5.38e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 162 TPHQELELLHTPQFGKVLRLDGRFMTSEGEEFFYHEALVHPAALAHPAPRKALILGGGDGGAAEELLKHPSMEQVVVAEL 241
Cdd:PLN02366   44 SDFQDVLVFESATYGKVLVLDGVIQLTERDECAYQEMITHLPLCSIPNPKKVLVVGGGDGGVLREIARHSSVEQIDICEI 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 242 DEAVVQAARTHLQQVHRGvFDDPRLQLRIGDGMAMVEH-TEERFDLALMDLTDPDTPASALYSDQALARMKRVLAPGGAL 320
Cdd:PLN02366  124 DKMVIDVSKKFFPDLAVG-FDDPRVNLHIGDGVEFLKNaPEGTYDAIIVDSSDPVGPAQELFEKPFFESVARALRPGGVV 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 321 VLHLGSPVFHGEQVARLVASLRERFAIVRCYG-LYIPLY-GAYWGLAVAS------DTLDAAALPPAQLRQRLAERrlpD 392
Cdd:PLN02366  203 CTQAESMWLHMDLIEDLIAICRETFKGSVNYAwTTVPTYpSGVIGFVLCSkegpavDFKHPVNPIDKLEGAGKAKR---P 279

                         250       260
                  ....*....|....*....|
gi 1108555412 393 LRYYNAEVHPALFALPNYYR 412
Cdd:PLN02366  280 LKFYNSEVHRAAFCLPSFAK 299
AdoMet_dc pfam02675
S-adenosylmethionine decarboxylase; This family contains several S-adenosylmethionine ...
 5-122 1.33e-30

S-adenosylmethionine decarboxylase; This family contains several S-adenosylmethionine decarboxylase proteins from bacterial and archaebacterial species. S-adenosylmethionine decarboxylase (AdoMetDC), a key enzyme in the biosynthesis of spermidine and spermine, is first synthesized as a proenzyme, which is cleaved post translationally to form alpha and beta subunits. The alpha subunit contains a covalently bound pyruvoyl group derived from serine that is essential for activity.


Pssm-ID: 460648  Cd Length: 107  Bit Score: 113.76  E-value: 1.33e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412   5 HLTADLYQCQGDArhMLDADAIAALCRAQTAQAGLTLVEDRWVKFPdyqgqPGGVTGTVLLAESHLAIHTWPETGCVTVD 84
Cdd:pfam02675   1 HLIVDLYGCDPEL--LDDAELIEQALREAAEAAGATVVEVVFHKFE-----PQGVSGVVLLAESHISIHTWPEYGYAAVD 73

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1108555412  85 VYVCNFSADnsgkARALMEGVIAAYAPGRVVRQQLMRG 122
Cdd:pfam02675  74 VFTCGDHVD----PEKAFEYLKEALGAKRVSVRELDRG 107
SAM_DCase_Bsu TIGR03330
S-adenosylmethionine decarboxylase proenzyme, Bacillus form; Members of this protein family ...
 3-122 1.62e-21

S-adenosylmethionine decarboxylase proenzyme, Bacillus form; Members of this protein family are the single chain precursor of the two chains of the mature S-adenosylmethionine decarboxylase as found in Methanocaldococcus jannaschii, Bacillus subtilis, and a wide range of other species. It differs substantially in architecture from the form as found in Escherichia coli, and lacks any extended homology to the eukaryotic form (TIGR00535). [Central intermediary metabolism, Polyamine biosynthesis]


Pssm-ID: 274523  Cd Length: 112  Bit Score: 89.20  E-value: 1.62e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412   3 GLHLTADLYQCqgDARHMLDADAI-AALCRAqTAQAGLTLVEDRWVKFPdyqgqPGGVTGTVLLAESHLAIHTWPETGCV 81
Cdd:TIGR03330   4 GRHLIVDLYGC--DPEKLDDVEFIeEILLEA-AKVAGATLVASHFHKFS-----PGGVSGVVLLAESHISIHTWPEYGYA 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1108555412  82 TVDVYVCnfsADNSGKARALmEGVIAAYAPGRVVRQQLMRG 122
Cdd:TIGR03330  76 AVDVFTC---GDHSDPEKAF-EYLVEALKPKRVEVRELDRG 112
speE PRK01581
polyamine aminopropyltransferase;
179-393 3.65e-21

polyamine aminopropyltransferase;


Pssm-ID: 234961 [Multi-domain]  Cd Length: 374  Bit Score: 94.26  E-value: 3.65e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 179 LRLDGRFMTSEGEEFFYHEALVHPAALAHPAPRKALILGGGDGGAAEELLKHPSMEQVVVAELDEAVVQAART--HLQQV 256
Cdd:PRK01581  120 LYLDKQLQFSSVDEQIYHEALVHPIMSKVIDPKRVLILGGGDGLALREVLKYETVLHVDLVDLDGSMINMARNvpELVSL 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 257 HRGVFDDPRLQLRIGDGMAMVEHTEERFDLALMDLTDPDTPA-SALYSDQALARMKRVLAPGGALVLHLGSPVFHGEQVA 335
Cdd:PRK01581  200 NKSAFFDNRVNVHVCDAKEFLSSPSSLYDVIIIDFPDPATELlSTLYTSELFARIATFLTEDGAFVCQSNSPADAPLVYW 279

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1108555412 336 RLVASLRERFAIVRCYGLYIPLYGAYWGLAVASDTLDAAALPPaQLRQRLAERRLPDL 393
Cdd:PRK01581  280 SIGNTIEHAGLTVKSYHTIVPSFGTDWGFHIAANSAYVLDQIE-QLYVVPTPRTLPSL 336
speE PRK00536
spermidine synthase; Provisional
 160-416 2.00e-10

spermidine synthase; Provisional


Pssm-ID: 134311 [Multi-domain]  Cd Length: 262  Bit Score: 61.03  E-value: 2.00e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 160 VQTPHQELELLHTPQFGKVLRLDGRFMTSEgeefFYH---EALVHPAALAHPAPRKALILGGGDGGAAEELLKHPSmeQV 236
Cdd:PRK00536   24 VRSEHNILEIFKSKDFGEIAMLNKQLLFKN----FLHiesELLAHMGGCTKKELKEVLIVDGFDLELAHQLFKYDT--HV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 237 VVAELDEAVVQAARTHLQQVHrGVFDDPRLQlrigdgmamveHTEERFDLalmDLTDPDTP-ASALYSDQALARMKRVLA 315
Cdd:PRK00536   98 DFVQADEKILDSFISFFPHFH-EVKNNKNFT-----------HAKQLLDL---DIKKYDLIiCLQEPDIHKIDGLKRMLK 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 316 PGGALVLHLGSPVFHGEQVARLVASLRERFAIVRCYGLYIPLYGAYwGLAVASDTLDaaalPPAQLRQRLAERrLPDLRY 395
Cdd:PRK00536  163 EDGVFISVAKHPLLEHVSMQNALKNMGDFFSIAMPFVAPLRILSNK-GYIYASFKTH----PLKDLMLQKIEA-LKSVRY 236

                         250       260
                  ....*....|....*....|.
gi 1108555412 396 YNAEVHPALFALPNYYRDLVQ 416
Cdd:PRK00536  237 YNEDIHRAAFALPKNLQEVFK 257
Spermine_synt_N pfam17284
Spermidine synthase tetramerization domain; This domain represents the N-terminal ...
 159-189 2.93e-06

Spermidine synthase tetramerization domain; This domain represents the N-terminal tetramerization domain from spermidine synthase.


Pssm-ID: 407397 [Multi-domain]  Cd Length: 53  Bit Score: 44.19  E-value: 2.93e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1108555412 159 TVQTPHQELELLHTPQFGKVLRLDGRFMTSE 189
Cdd:pfam17284  23 DEKSEYQDIEIFESKTFGNVLVLDGVVQLTE 53
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 235-318 3.39e-05

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 42.55  E-value: 3.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 235 QVVVAELDEAVVQAARTHLQQvhrgvfDDPRLQLRIGDGMAMvEHTEERFDL-----ALMDLTDPDTPAsalysdqALAR 309
Cdd:pfam13649  22 RVTGVDLSPEMLERARERAAE------AGLNVEFVQGDAEDL-PFPDGSFDLvvssgVLHHLPDPDLEA-------ALRE 87


                  ....*....
gi 1108555412 310 MKRVLAPGG 318
Cdd:pfam13649  88 IARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 224-324 2.46e-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: 40.11  E-value: 2.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 224 AEELLKHPSmEQVVVAELDEAVVQAARTHLQQVHRgvfddPRLQLRIGDGMAMVEHTEERFDLALMDLTDPDTPASAlys 303
Cdd:cd02440    13 ALALASGPG-ARVTGVDISPVALELARKAAAALLA-----DNVEVLKGDAEELPPEADESFDVIISDPPLHHLVEDL--- 83

                          90       100
                  ....*....|....*....|.
gi 1108555412 304 DQALARMKRVLAPGGALVLHL 324
Cdd:cd02440    84 ARFLEEARRLLKPGGVLVLTL 104
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 258-351 6.55e-04

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: 41.30  E-value: 6.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 258 RGVFDDPRLQLRIGDgmaMVEHTEER-FDLALMDLTDPDtpasalysdQALARMKRVLAPGGALVLHLgsPVFhgEQVAR 336
Cdd:COG2519   137 ERFGLPDNVELKLGD---IREGIDEGdVDAVFLDMPDPW---------EALEAVAKALKPGGVLVAYV--PTV--NQVSK 200

                          90
                  ....*....|....*.
gi 1108555412 337 LVASLRER-FAIVRCY 351
Cdd:COG2519   201 LVEALRESgFTDIEAV 216
PRK04457 PRK04457
polyamine aminopropyltransferase;
231-349 1.04e-03

polyamine aminopropyltransferase;


Pssm-ID: 179854 [Multi-domain]  Cd Length: 262  Bit Score: 40.79  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 231 PSMEQVVVaELDEAVVQAARTHLQQVHrgvfDDPRLQLRIGDGMAMVEHTEERFDLALMDLTDPDTPASALYSDQALARM 310
Cdd:PRK04457   89 PDTRQTAV-EINPQVIAVARNHFELPE----NGERFEVIEADGAEYIAVHRHSTDVILVDGFDGEGIIDALCTQPFFDDC 163

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1108555412 311 KRVLAPGGALVLHL--GSPVFHgEQVARLVASLRERFAIVR 349
Cdd:PRK04457  164 RNALSSDGIFVVNLwsRDKRYD-RYLERLESSFEGRVLELP 203
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 223-348 3.18e-03

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 38.17  E-value: 3.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 223 AAEELlkhPSMEQVVVAELDEAVVQAARTHLQQvhRGvFDdpRLQLRIGDGMAMVEH-TEERFDL-----ALMDLTDPDt 296
Cdd:pfam13847  21 LAEEL---GPNAEVVGIDISEEAIEKARENAQK--LG-FD--NVEFEQGDIEELPELlEDDKFDVvisncVLNHIPDPD- 91

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1108555412 297 pasalysdQALARMKRVLAPGGALVlhLGSPVFHGEQVARLVASLRERFAIV 348
Cdd:pfam13847  92 --------KVLQEILRVLKPGGRLI--ISDPDSLAELPAHVKEDSTYYAGCV 133
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 235-322 4.24e-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: 37.67  E-value: 4.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 235 QVVVAELDEAVVQAARTHLQQvhrgvfDDPRLQLRIGDGMAMvEHTEERFDL-----ALMDLTDPDtpasalysdQALAR 309
Cdd:COG2226    46 RVTGVDISPEMLELARERAAE------AGLNVEFVVGDAEDL-PFPDGSFDLvissfVLHHLPDPE---------RALAE 109

                          90
                  ....*....|...
gi 1108555412 310 MKRVLAPGGALVL 322
Cdd:COG2226   110 IARVLKPGGRLVV 122
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 235-322 5.60e-03

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 36.10  E-value: 5.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 235 QVVVAELDEAVVQAARTHLQqvhrgvfdDPRLQLRIGDGMAMvEHTEERFDL-----ALMDLTDPDtpasalysdQALAR 309
Cdd:pfam08241  20 RVTGVDISPEMLELAREKAP--------REGLTFVVGDAEDL-PFPDNSFDLvlsseVLHHVEDPE---------RALRE 81

                          90
                  ....*....|...
gi 1108555412 310 MKRVLAPGGALVL 322
Cdd:pfam08241  82 IARVLKPGGILII 94
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
223-322 8.21e-03

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 35.57  E-value: 8.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 223 AAEELLKHPSMEQVVVAELDEAVVQAARTHLqqvhrgvfddPRLQLRIGDgMAMVEhTEERFDL-----ALMDLTDPdtp 297
Cdd:COG4106    15 LTALLAERFPGARVTGVDLSPEMLARARARL----------PNVRFVVAD-LRDLD-PPEPFDLvvsnaALHWLPDH--- 79

                          90       100
                  ....*....|....*....|....*
gi 1108555412 298 asalysDQALARMKRVLAPGGALVL 322
Cdd:COG4106    80 ------AALLARLAAALAPGGVLAV 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.
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