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Conserved domains on  [gi|489212313|ref|WP_003121084|]
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fused MFS/spermidine synthase [Pseudomonas aeruginosa]

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

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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; ...
 44-316 1.08e-84

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 PLN02823:

Pssm-ID: 473071 [Multi-domain]  Cd Length: 336  Bit Score: 259.61  E-value: 1.08e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212313  44 YVYRLRRVLYQGRTRWQNVLIADTYNYDRVLMLDGAIQSAESDESLYHELLVQPAMLAHDEPRDVLIIGGGEGATLREVL 123
Cdd:PLN02823  43 WSYAVNSVLHTGTSEFQDIALVDTKPFGKVLIIDGKMQSAEADEFVYHESLVHPALLHHPNPKTVFIMGGGEGSTAREVL 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212313 124 SHASVRRAVMVDLDRELVELCREHLFQWHQgAFDDPRCELLAEDGRAYLERDPSLYDVVIIDVVDMLDNGPAQALYTRQF 203
Cdd:PLN02823 123 RHKTVEKVVMCDIDQEVVDFCRKHLTVNRE-AFCDKRLELIINDARAELEKRDEKFDVIIGDLADPVEGGPCYQLYTKSF 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212313 204 YE-LLHSRLRPGGVVAVQGLE---FSHSDdkPHAALARTLRSVFSQVHSYRATVPSFLSSWGFLLASD--WLDTNhwqAE 277
Cdd:PLN02823 202 YErIVKPKLNPGGIFVTQAGPagiLTHKE--VFSSIYNTLRQVFKYVVPYTAHVPSFADTWGWVMASDhpFADLS---AE 276

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 489212313 278 DIDRRI-ERKLGPlwLDHLDGDYLKACFVMDRETRFLLAQ 316
Cdd:PLN02823 277 ELDSRIkERIDGE--LKYLDGETFSSAFALNKTVRQALAN 314
 
Name Accession Description Interval E-value
PLN02823 PLN02823
spermine synthase
 44-316 1.08e-84

spermine synthase


Pssm-ID: 178418 [Multi-domain]  Cd Length: 336  Bit Score: 259.61  E-value: 1.08e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212313  44 YVYRLRRVLYQGRTRWQNVLIADTYNYDRVLMLDGAIQSAESDESLYHELLVQPAMLAHDEPRDVLIIGGGEGATLREVL 123
Cdd:PLN02823  43 WSYAVNSVLHTGTSEFQDIALVDTKPFGKVLIIDGKMQSAEADEFVYHESLVHPALLHHPNPKTVFIMGGGEGSTAREVL 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212313 124 SHASVRRAVMVDLDRELVELCREHLFQWHQgAFDDPRCELLAEDGRAYLERDPSLYDVVIIDVVDMLDNGPAQALYTRQF 203
Cdd:PLN02823 123 RHKTVEKVVMCDIDQEVVDFCRKHLTVNRE-AFCDKRLELIINDARAELEKRDEKFDVIIGDLADPVEGGPCYQLYTKSF 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212313 204 YE-LLHSRLRPGGVVAVQGLE---FSHSDdkPHAALARTLRSVFSQVHSYRATVPSFLSSWGFLLASD--WLDTNhwqAE 277
Cdd:PLN02823 202 YErIVKPKLNPGGIFVTQAGPagiLTHKE--VFSSIYNTLRQVFKYVVPYTAHVPSFADTWGWVMASDhpFADLS---AE 276

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 489212313 278 DIDRRI-ERKLGPlwLDHLDGDYLKACFVMDRETRFLLAQ 316
Cdd:PLN02823 277 ELDSRIkERIDGE--LKYLDGETFSSAFALNKTVRQALAN 314
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
71-265 2.25e-70

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


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 217.77  E-value: 2.25e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212313  71 DRVLMLDGAIQSA-ESDESLYHELLVQPAMLAHDEPRDVLIIGGGEGATLREVLSHASVRRAVMVDLDRELVELCREHlF 149
Cdd:COG0421    3 GRVLVLDGVVQSTmELDEFEYHEMMAHVPLLFHPNPKRVLIIGGGDGGLARELLKHPPVERVDVVEIDPEVVELAREY-F 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212313 150 QWHQGAFDDPRCELLAEDGRAYLERDPSLYDVVIIDVVDmlDNGPAQALYTRQFYELLHSRLRPGGVVAVQgLEFSHSDD 229
Cdd:COG0421   82 PLLAPAFDDPRLRVVIGDGRAFLREAEESYDVIIVDLTD--PVGPAEGLFTREFYEDCRRALKPGGVLVVN-LGSPFYGL 158

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 489212313 230 KPHAALARTLRSVFSQVHSYRATVPSFLSSWGFLLA 265
Cdd:COG0421  159 DLLRRVLATLREVFPHVVLYAAPVPTYGGGNVFLLA 194
speE TIGR00417
spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine ...
 47-306 2.69e-66

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: 210.36  E-value: 2.69e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212313   47 RLRRVLYQGRTRWQNVLIADTYNYDRVLMLDGAIQSAESDESLYHELLVQPAMLAHDEPRDVLIIGGGEGATLREVLSHA 126
Cdd:TIGR00417  15 KVDKVLYHEKSEFQDLEIFETEAFGNVLVLDGVVQTTERDEFIYHEMITHVPLFTHPNPKHVLVIGGGDGGVLREVLKHK 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212313  127 SVRRAVMVDLDRELVELCREHLFQwHQGAFDDPRCELLAEDGRAYLERDPSLYDVVIIDVVDMLdnGPAQALYTRQFYEL 206
Cdd:TIGR00417  95 SVESATLVDIDEKVIELSRKYLPN-LAGSYDDPRVKLVIDDGFKFLADTENTFDVIIVDSTDPV--GPAETLFTKEFYEL 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212313  207 LHSRLRPGGVVAVQG------LEFSHSddkphaaLARTLRSVFSQVHSYRATVPSFLSS-WGFLLASDWlDTNHWQAEdi 279
Cdd:TIGR00417 172 LKKALNPDGIFVAQSespwlqLELIID-------LKRKLKEAFPITEYYTAAIPTYPSGlWTFTIASKN-KYRPLEVE-- 241

                         250       260
                  ....*....|....*....|....*..
gi 489212313  280 DRRIERKLGPLWLDHLDGDYLKACFVM 306
Cdd:TIGR00417 242 IRRIKFEAEDGKTKYYNPDIHKAAFVL 268
Spermine_synth pfam01564
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ...
 87-267 1.17e-41

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: 143.61  E-value: 1.17e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212313   87 ESLYHELLVQPAMLAHDEPRDVLIIGGGEGATLREVLSHASVRRAVMVDLDRELVELCREHLFQWHqGAFDDPRCELLAE 166
Cdd:pfam01564   1 EFIYHEMIAHVPLCSHPNPKKVLIIGGGDGGVLREVVKHPSVEKITLVDIDEKVIDFSKKFLPSLA-IGFQDPRVKVVIG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212313  167 DGRAYLERDPSLYDVVIIDVVDMLdnGPAQALYTRQFYELLHSRLRPGGVVAVQGlefshsdDKPHAALA------RTLR 240
Cdd:pfam01564  80 DGFKFLKDYLNTFDVIIVDSTDPV--GPAENLFSKPFFDLLKKALKEDGVFITQA-------ESPWLHLEliinilKNGK 150

                         170       180
                  ....*....|....*....|....*...
gi 489212313  241 SVFSQVHSYRATVPSFLS-SWGFLLASD 267
Cdd:pfam01564 151 QVFPVVMPYVATIPTYPSgGWGFTVCSK 178
MFS_SpdSyn NF037959
fused MFS/spermidine synthase; Proteins of this family are fusion of a N-terminal MFS (Major ...
 97-254 2.69e-11

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: 64.48  E-value: 2.69e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212313  97 PAMLAHDEPRDVLIIGGGEGATLREVLSHASVRRAVMVDLDRELVELCREHLFqwhqgaFDDPRCELLAEDGRAYLERDP 176
Cdd:NF037959 268 ARLRMGRADFSAFFIGGGAYTLPRAWAARRPAGRITVAEIDPAVTRVAAEDFW------FDPASATVLHEDARRALRRRP 341

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212313 177 SL-YDVVIIDVVDmlDNGPAQALYTRQFYELLHSRLRPGGVVAVQGLEFShsdDKPHA--ALARTLRSVFSQVHSYRATV 253
Cdd:NF037959 342 EErFDVIVGDAFT--DIAVPAHLVTREFFELVRARLTPDGVYLMNVIDHA---DRLRAlaALVATLREVFPVVEVWTEAR 416


                 .
gi 489212313 254 P 254
Cdd:NF037959 417 P 417
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 107-224 3.50e-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: 48.20  E-value: 3.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212313 107 DVLIIGGGEGATLREVLSHaSVRRAVMVDLDRELVELCREHLFqwhqgAFDDPRCELLAEDGRAYLERDPSLYDVVIIDV 186
Cdd:cd02440    1 RVLDLGCGTGALALALASG-PGARVTGVDISPVALELARKAAA-----ALLADNVEVLKGDAEELPPEADESFDVIISDP 74

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 489212313 187 VdmldnGPAQALYTRQFYELLHSRLRPGGVVAVQGLEF 224
Cdd:cd02440   75 P-----LHHLVEDLARFLEEARRLLKPGGVLVLTLVLA 107
 
Name Accession Description Interval E-value
PLN02823 PLN02823
spermine synthase
 44-316 1.08e-84

spermine synthase


Pssm-ID: 178418 [Multi-domain]  Cd Length: 336  Bit Score: 259.61  E-value: 1.08e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212313  44 YVYRLRRVLYQGRTRWQNVLIADTYNYDRVLMLDGAIQSAESDESLYHELLVQPAMLAHDEPRDVLIIGGGEGATLREVL 123
Cdd:PLN02823  43 WSYAVNSVLHTGTSEFQDIALVDTKPFGKVLIIDGKMQSAEADEFVYHESLVHPALLHHPNPKTVFIMGGGEGSTAREVL 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212313 124 SHASVRRAVMVDLDRELVELCREHLFQWHQgAFDDPRCELLAEDGRAYLERDPSLYDVVIIDVVDMLDNGPAQALYTRQF 203
Cdd:PLN02823 123 RHKTVEKVVMCDIDQEVVDFCRKHLTVNRE-AFCDKRLELIINDARAELEKRDEKFDVIIGDLADPVEGGPCYQLYTKSF 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212313 204 YE-LLHSRLRPGGVVAVQGLE---FSHSDdkPHAALARTLRSVFSQVHSYRATVPSFLSSWGFLLASD--WLDTNhwqAE 277
Cdd:PLN02823 202 YErIVKPKLNPGGIFVTQAGPagiLTHKE--VFSSIYNTLRQVFKYVVPYTAHVPSFADTWGWVMASDhpFADLS---AE 276

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 489212313 278 DIDRRI-ERKLGPlwLDHLDGDYLKACFVMDRETRFLLAQ 316
Cdd:PLN02823 277 ELDSRIkERIDGE--LKYLDGETFSSAFALNKTVRQALAN 314
PRK00811 PRK00811
polyamine aminopropyltransferase;
46-306 4.50e-78

polyamine aminopropyltransferase;


Pssm-ID: 234843 [Multi-domain]  Cd Length: 283  Bit Score: 240.83  E-value: 4.50e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212313  46 YRLRRVLYQGRTRWQNVLIADTYNYDRVLMLDGAIQSAESDESLYHELLVQPAMLAHDEPRDVLIIGGGEGATLREVLSH 125
Cdd:PRK00811  18 FRVKKVLYEEKSPFQRIEIFETPEFGRLLALDGCVMTTERDEFIYHEMMTHVPLFAHPNPKRVLIIGGGDGGTLREVLKH 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212313 126 ASVRRAVMVDLDRELVELCREHLFQWHQGAFDDPRCELLAEDGRAYLERDPSLYDVVIIDVVDMLdnGPAQALYTRQFYE 205
Cdd:PRK00811  98 PSVEKITLVEIDERVVEVCRKYLPEIAGGAYDDPRVELVIGDGIKFVAETENSFDVIIVDSTDPV--GPAEGLFTKEFYE 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212313 206 LLHSRLRPGGVVAVQ-GLEFSHSDDkpHAALARTLRSVFSQVHSYRATVPSFLSS-WGFLLASDWLDTNHWQAEDIDRRI 283
Cdd:PRK00811 176 NCKRALKEDGIFVAQsGSPFYQADE--IKDMHRKLKEVFPIVRPYQAAIPTYPSGlWSFTFASKNDDLKFLPLDVIEARF 253

                        250       260
                 ....*....|....*....|...
gi 489212313 284 ERKLGPLWldHLDGDYLKACFVM 306
Cdd:PRK00811 254 AERGIKTR--YYNPELHKAAFAL 274
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
71-265 2.25e-70

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


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 217.77  E-value: 2.25e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212313  71 DRVLMLDGAIQSA-ESDESLYHELLVQPAMLAHDEPRDVLIIGGGEGATLREVLSHASVRRAVMVDLDRELVELCREHlF 149
Cdd:COG0421    3 GRVLVLDGVVQSTmELDEFEYHEMMAHVPLLFHPNPKRVLIIGGGDGGLARELLKHPPVERVDVVEIDPEVVELAREY-F 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212313 150 QWHQGAFDDPRCELLAEDGRAYLERDPSLYDVVIIDVVDmlDNGPAQALYTRQFYELLHSRLRPGGVVAVQgLEFSHSDD 229
Cdd:COG0421   82 PLLAPAFDDPRLRVVIGDGRAFLREAEESYDVIIVDLTD--PVGPAEGLFTREFYEDCRRALKPGGVLVVN-LGSPFYGL 158

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 489212313 230 KPHAALARTLRSVFSQVHSYRATVPSFLSSWGFLLA 265
Cdd:COG0421  159 DLLRRVLATLREVFPHVVLYAAPVPTYGGGNVFLLA 194
speE TIGR00417
spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine ...
 47-306 2.69e-66

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: 210.36  E-value: 2.69e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212313   47 RLRRVLYQGRTRWQNVLIADTYNYDRVLMLDGAIQSAESDESLYHELLVQPAMLAHDEPRDVLIIGGGEGATLREVLSHA 126
Cdd:TIGR00417  15 KVDKVLYHEKSEFQDLEIFETEAFGNVLVLDGVVQTTERDEFIYHEMITHVPLFTHPNPKHVLVIGGGDGGVLREVLKHK 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212313  127 SVRRAVMVDLDRELVELCREHLFQwHQGAFDDPRCELLAEDGRAYLERDPSLYDVVIIDVVDMLdnGPAQALYTRQFYEL 206
Cdd:TIGR00417  95 SVESATLVDIDEKVIELSRKYLPN-LAGSYDDPRVKLVIDDGFKFLADTENTFDVIIVDSTDPV--GPAETLFTKEFYEL 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212313  207 LHSRLRPGGVVAVQG------LEFSHSddkphaaLARTLRSVFSQVHSYRATVPSFLSS-WGFLLASDWlDTNHWQAEdi 279
Cdd:TIGR00417 172 LKKALNPDGIFVAQSespwlqLELIID-------LKRKLKEAFPITEYYTAAIPTYPSGlWTFTIASKN-KYRPLEVE-- 241

                         250       260
                  ....*....|....*....|....*..
gi 489212313  280 DRRIERKLGPLWLDHLDGDYLKACFVM 306
Cdd:TIGR00417 242 IRRIKFEAEDGKTKYYNPDIHKAAFVL 268
COG4262 COG4262
Predicted spermidine synthase with an N-terminal membrane domain [General function prediction ...
 30-243 2.58e-52

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


Pssm-ID: 443404 [Multi-domain]  Cd Length: 426  Bit Score: 178.52  E-value: 2.58e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212313  30 GAITAIEDSDPFDQYVYRlRRVLYQGRTRWQNVLIADTYNyDRVLMLDGAIQSAESDESLYHELLVQPAMLAHDEPRDVL 109
Cdd:COG4262  214 GLVFADPIESSAEQKLYG-DPVVYSEQTPYQRIVVTRDKD-DRRLYLNGNLQFSSLDEYRYHEALVHPPMAAHPRPRRVL 291

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212313 110 IIGGGEGATLREVLSHASVRRAVMVDLDRELVELCREHLF--QWHQGAFDDPRCELLAEDGRAYLERDPSLYDVVIIDVV 187
Cdd:COG4262  292 VLGGGDGLAAREVLKYPDVESVTLVDLDPEVTDLAKTNPFlrELNGGALNDPRVTVVNADAFQFLRETDEKYDVIIVDLP 371

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489212313 188 DMLDNGPAQaLYTRQFYELLHSRLRPGGVVAVQgLEFSHSDDKPHAALARTLRSVF 243
Cdd:COG4262  372 DPSNFSLGK-LYSVEFYRLVRRHLAPGGVLVVQ-ATSPYFAPKAFWCIAKTLEAAG 425
PRK03612 PRK03612
polyamine aminopropyltransferase;
41-317 8.03e-47

polyamine aminopropyltransferase;


Pssm-ID: 235139 [Multi-domain]  Cd Length: 521  Bit Score: 166.17  E-value: 8.03e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212313  41 FDQYVYRlRRVLYQGRTRWQNVLI---ADTYNYDRVLMLDGAIQSAESDESLYHELLVQPAMLAHDEPRDVLIIGGGEGA 117
Cdd:PRK03612 232 AEQLLYG-DPVVYAEQTPYQRIVVtrrGNGRGPDLRLYLNGRLQFSSRDEYRYHEALVHPAMAASARPRRVLVLGGGDGL 310

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212313 118 TLREVLSHASVRRAVMVDLDRELVELCREH--LFQWHQGAFDDPRCELLAEDGRAYLERDPSLYDVVIIDVVDmlDNGPA 195
Cdd:PRK03612 311 ALREVLKYPDVEQVTLVDLDPAMTELARTSpaLRALNGGALDDPRVTVVNDDAFNWLRKLAEKFDVIIVDLPD--PSNPA 388

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212313 196 QA-LYTRQFYELLHSRLRPGGVVAVQglefSHSddkPHAA------LARTLRSVFSQVHSYRATVPSFlSSWGFLLAsdw 268
Cdd:PRK03612 389 LGkLYSVEFYRLLKRRLAPDGLLVVQ----STS---PYFApkafwsIEATLEAAGLATTPYHVNVPSF-GEWGFVLA--- 457

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 489212313 269 ldtnhwqAEDIDRRIERKL-GPLWLDHLDGDYLKACFVMDRETRFLLAQP 317
Cdd:PRK03612 458 -------GAGARPPLAVPTeLPVPLRFLDPALLAAAFVFPKDMRRREVEP 500
PLN02366 PLN02366
spermidine synthase
 40-266 1.79e-45

spermidine synthase


Pssm-ID: 215208 [Multi-domain]  Cd Length: 308  Bit Score: 157.50  E-value: 1.79e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212313  40 PFDQYVYRLRRVLYQGRTRWQNVLIADTYNYDRVLMLDGAIQSAESDESLYHELLVQPAMLAHDEPRDVLIIGGGEGATL 119
Cdd:PLN02366  27 PGEAHSLKVEKVLFQGKSDFQDVLVFESATYGKVLVLDGVIQLTERDECAYQEMITHLPLCSIPNPKKVLVVGGGDGGVL 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212313 120 REVLSHASVRRAVMVDLDRELVELCREHLFQWHQGaFDDPRCELLAEDGRAYLERDP-SLYDVVIIDVVDmlDNGPAQAL 198
Cdd:PLN02366 107 REIARHSSVEQIDICEIDKMVIDVSKKFFPDLAVG-FDDPRVNLHIGDGVEFLKNAPeGTYDAIIVDSSD--PVGPAQEL 183

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489212313 199 YTRQFYELLHSRLRPGGVVAVQGlE--FSHSDD-KPHAALArtlRSVFS-QVHSYRATVPSFLSSW-GFLLAS 266
Cdd:PLN02366 184 FEKPFFESVARALRPGGVVCTQA-EsmWLHMDLiEDLIAIC---RETFKgSVNYAWTTVPTYPSGViGFVLCS 252
Spermine_synth pfam01564
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ...
 87-267 1.17e-41

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: 143.61  E-value: 1.17e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212313   87 ESLYHELLVQPAMLAHDEPRDVLIIGGGEGATLREVLSHASVRRAVMVDLDRELVELCREHLFQWHqGAFDDPRCELLAE 166
Cdd:pfam01564   1 EFIYHEMIAHVPLCSHPNPKKVLIIGGGDGGVLREVVKHPSVEKITLVDIDEKVIDFSKKFLPSLA-IGFQDPRVKVVIG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212313  167 DGRAYLERDPSLYDVVIIDVVDMLdnGPAQALYTRQFYELLHSRLRPGGVVAVQGlefshsdDKPHAALA------RTLR 240
Cdd:pfam01564  80 DGFKFLKDYLNTFDVIIVDSTDPV--GPAENLFSKPFFDLLKKALKEDGVFITQA-------ESPWLHLEliinilKNGK 150

                         170       180
                  ....*....|....*....|....*...
gi 489212313  241 SVFSQVHSYRATVPSFLS-SWGFLLASD 267
Cdd:pfam01564 151 QVFPVVMPYVATIPTYPSgGWGFTVCSK 178
speE PRK01581
polyamine aminopropyltransferase;
51-267 5.94e-35

polyamine aminopropyltransferase;


Pssm-ID: 234961 [Multi-domain]  Cd Length: 374  Bit Score: 131.24  E-value: 5.94e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212313  51 VLYQGRTRWQNVLIADTYnyDRVLMLDGAIQSAESDESLYHELLVQPAMLAHDEPRDVLIIGGGEGATLREVLSHASVRR 130
Cdd:PRK01581  99 NLFAEKSNYQNINLLQVS--DIRLYLDKQLQFSSVDEQIYHEALVHPIMSKVIDPKRVLILGGGDGLALREVLKYETVLH 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212313 131 AVMVDLDRELVELCR--EHLFQWHQGAFDDPRCELLAEDGRAYLERDPSLYDVVIIDVVDmldngPA----QALYTRQFY 204
Cdd:PRK01581 177 VDLVDLDGSMINMARnvPELVSLNKSAFFDNRVNVHVCDAKEFLSSPSSLYDVIIIDFPD-----PAtellSTLYTSELF 251

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489212313 205 ELLHSRLRPGGVVAVQglefSHSD-DKP--HAALARTLRSVFSQVHSYRATVPSFLSSWGFLLASD 267
Cdd:PRK01581 252 ARIATFLTEDGAFVCQ----SNSPaDAPlvYWSIGNTIEHAGLTVKSYHTIVPSFGTDWGFHIAAN 313
PRK04457 PRK04457
polyamine aminopropyltransferase;
99-245 2.25e-12

polyamine aminopropyltransferase;


Pssm-ID: 179854 [Multi-domain]  Cd Length: 262  Bit Score: 66.22  E-value: 2.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212313  99 MLAHDEPRDVLIIGGGEGATLREVLSHASVRRAVMVDLDRELVELCREHLFQwhqgAFDDPRCELLAEDGRAYLERDPSL 178
Cdd:PRK04457  61 LLFNPRPQHILQIGLGGGSLAKFIYTYLPDTRQTAVEINPQVIAVARNHFEL----PENGERFEVIEADGAEYIAVHRHS 136

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489212313 179 YDVVIIDVVDmlDNGPAQALYTRQFYELLHSRLRPGGVVAVQGLEfshSDDKPHAALARtLRSVFSQ 245
Cdd:PRK04457 137 TDVILVDGFD--GEGIIDALCTQPFFDDCRNALSSDGIFVVNLWS---RDKRYDRYLER-LESSFEG 197
MFS_SpdSyn NF037959
fused MFS/spermidine synthase; Proteins of this family are fusion of a N-terminal MFS (Major ...
 97-254 2.69e-11

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: 64.48  E-value: 2.69e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212313  97 PAMLAHDEPRDVLIIGGGEGATLREVLSHASVRRAVMVDLDRELVELCREHLFqwhqgaFDDPRCELLAEDGRAYLERDP 176
Cdd:NF037959 268 ARLRMGRADFSAFFIGGGAYTLPRAWAARRPAGRITVAEIDPAVTRVAAEDFW------FDPASATVLHEDARRALRRRP 341

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212313 177 SL-YDVVIIDVVDmlDNGPAQALYTRQFYELLHSRLRPGGVVAVQGLEFShsdDKPHA--ALARTLRSVFSQVHSYRATV 253
Cdd:NF037959 342 EErFDVIVGDAFT--DIAVPAHLVTREFFELVRARLTPDGVYLMNVIDHA---DRLRAlaALVATLREVFPVVEVWTEAR 416


                 .
gi 489212313 254 P 254
Cdd:NF037959 417 P 417
Spermine_synt_N pfam17284
Spermidine synthase tetramerization domain; This domain represents the N-terminal ...
 35-84 1.11e-08

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: 50.74  E-value: 1.11e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 489212313   35 IEDSDPFDQYVYRLRRVLYQGRTRWQNVLIADTYNYDRVLMLDGAIQSAE 84
Cdd:pfam17284   4 TEIHDLGQALEYKVEKVLYDEKSEYQDIEIFESKTFGNVLVLDGVVQLTE 53
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 107-224 3.50e-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: 48.20  E-value: 3.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212313 107 DVLIIGGGEGATLREVLSHaSVRRAVMVDLDRELVELCREHLFqwhqgAFDDPRCELLAEDGRAYLERDPSLYDVVIIDV 186
Cdd:cd02440    1 RVLDLGCGTGALALALASG-PGARVTGVDISPVALELARKAAA-----ALLADNVEVLKGDAEELPPEADESFDVIISDP 74

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 489212313 187 VdmldnGPAQALYTRQFYELLHSRLRPGGVVAVQGLEF 224
Cdd:cd02440   75 P-----LHHLVEDLARFLEEARRLLKPGGVLVLTLVLA 107
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
104-220 1.46e-06

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 45.97  E-value: 1.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212313 104 EPRDVLIIGGGEGATLREVLSHASVRRAVMVDLDRELVELCREHLfqwhqgafddPRCELLAEDGRAYLERDPslYDVVI 183
Cdd:COG4106    1 PPRRVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARARL----------PNVRFVVADLRDLDPPEP--FDLVV 68

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 489212313 184 IdvvdmldngpAQALY----TRQFYELLHSRLRPGGVVAVQ 220
Cdd:COG4106   69 S----------NAALHwlpdHAALLARLAAALAPGGVLAVQ 99
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 108-215 1.50e-06

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 46.02  E-value: 1.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212313  108 VLIIGGGEGATLREvLSHASVRRAVMVDLDRELVELCREHLfqwhqgAFDDPRCELLAEDGRAYLERDPSlYDVVIIdvV 187
Cdd:pfam13649   1 VLDLGCGTGRLTLA-LARRGGARVTGVDLSPEMLERARERA------AEAGLNVEFVQGDAEDLPFPDGS-FDLVVS--S 70

                          90       100
                  ....*....|....*....|....*...
gi 489212313  188 DMLDNGPAQALytRQFYELLHSRLRPGG 215
Cdd:pfam13649  71 GVLHHLPDPDL--EAALREIARVLKPGG 96
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 109-217 3.95e-05

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 41.97  E-value: 3.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212313  109 LIIGGGEGATLREVLSHASVRRAVMVDLDRELVELCREHLFQWHQGAFDdpRCELLAEDGrayLERDPSLYDVVI-IDVV 187
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERLAALGLLNAV--RVELFQLDL---GELDPGSFDVVVaSNVL 75

                          90       100       110
                  ....*....|....*....|....*....|
gi 489212313  188 DMLDNgPAQALytRQFYELlhsrLRPGGVV 217
Cdd:pfam08242  76 HHLAD-PRAVL--RNIRRL----LKPGGVL 98
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 103-219 7.05e-05

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: 41.93  E-value: 7.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212313 103 DEPRDVLIIGGGEGATLREVLSHASvrRAVMVDLDRELVELCREHL----FQWHQGAFDDprceLLAEDGRaylerdpsl 178
Cdd:COG2227   23 PAGGRVLDVGCGTGRLALALARRGA--DVTGVDISPEALEIARERAaelnVDFVQGDLED----LPLEDGS--------- 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 489212313 179 YDVVI-IDVVDMLDNgPAQALytrqfyELLHSRLRPGGVVAV 219
Cdd:COG2227   88 FDLVIcSEVLEHLPD-PAALL------RELARLLKPGGLLLL 122
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 108-221 2.44e-04

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 41.07  E-value: 2.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212313 108 VLIIGGGEGATLREVLSHASVRrAVMVDLDRELVELCREHLfqwhQGAFDDPRCELLAEDGRAYLERDPslYDVVIidVV 187
Cdd:COG2230   55 VLDIGCGWGGLALYLARRYGVR-VTGVTLSPEQLEYARERA----AEAGLADRVEVRLADYRDLPADGQ--FDAIV--SI 125

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489212313 188 DMLDN-GPAqalYTRQFYELLHSRLRPGGVVAVQG 221
Cdd:COG2230  126 GMFEHvGPE---NYPAYFAKVARLLKPGGRLLLHT 157
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 134-239 3.93e-04

tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; tRNA 5-hydroxyU34 O-methylase TrmR/YrrM is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443298  Cd Length: 173  Bit Score: 40.55  E-value: 3.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212313 134 VDLDRELVELCREHLfqwhQGAFDDPRCELLAEDGRAYLER-DPSLYDVVIIDVvdmldngpAQALYTRqFYELLHSRLR 212
Cdd:COG4122   47 IEIDPERAAIARENF----ARAGLADRIRLILGDALEVLPRlADGPFDLVFIDA--------DKSNYPD-YLELALPLLR 113

                         90       100       110
                 ....*....|....*....|....*....|..
gi 489212313 213 PGGVVAV-----QGLEFSHSDDKPHAALARTL 239
Cdd:COG4122  114 PGGLIVAdnvlwHGRVADPARRDPSTRAIREF 145
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 85-254 2.05e-03

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 38.74  E-value: 2.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212313  85 SDESLYHELLVQPAMLAHDEPRDVLIIGGGEGATLrEVLSHASVRRAVMVDLDRELVELCREHLfqwhqGAFDDPRCELL 164
Cdd:COG0500    7 SDELLPGLAALLALLERLPKGGRVLDLGCGTGRNL-LALAARFGGRVIGIDLSPEAIALARARA-----AKAGLGNVEFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212313 165 AEDGRAYLERDPSLYDVVI-IDVVDMLDngpaqALYTRQFYELLHSRLRPGGVVAVQGLEFSHSDDKPHAALARTLRSVF 243
Cdd:COG0500   81 VADLAELDPLPAESFDLVVaFGVLHHLP-----PEEREALLRELARALKPGGVLLLSASDAAAALSLARLLLLATASLLE 155

                        170
                 ....*....|.
gi 489212313 244 SQVHSYRATVP 254
Cdd:COG0500  156 LLLLLRLLALE 166
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 98-219 4.18e-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: 4.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212313  98 AMLAHDEPRDVLIIGGGEGATLREVLSHASvrRAVMVDLDRELVELCREHLfqwhqgAFDDPRCELLAEDGRAYLERDPS 177
Cdd:COG2226   16 AALGLRPGARVLDLGCGTGRLALALAERGA--RVTGVDISPEMLELARERA------AEAGLNVEFVVGDAEDLPFPDGS 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 489212313 178 lYDVVII-DVVDMLDNgPAQALytRQFYELlhsrLRPGGVVAV 219
Cdd:COG2226   88 -FDLVISsFVLHHLPD-PERAL--AEIARV----LKPGGRLVV 122
 
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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