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Conserved domains on  [gi|145334807|ref|NP_001078749|]
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spermidine synthase 3 [Arabidopsis thaliana]

Protein Classification

spermidine/spermine synthase family protein( domain architecture ID 10010775)

spermidine/spermine synthase family protein similar to spermidine synthase, an aminopropyltransferase that transfers aminopropyl groups from decarboxylated S-adenosylmethionine to putrescine forming sperrmidine

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02366 PLN02366
spermidine synthase
 38-359 0e+00

spermidine synthase


:

Pssm-ID: 215208 [Multi-domain]  Cd Length: 308  Bit Score: 572.36  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334807  38 ACVPEDDAKCHSTVVSGWFSEPhprsgkkggkavyfnNPMWPGEAHSLKVEKVLFKDKSDFQEVLVFESATYGKVLVLDG 117
Cdd:PLN02366   1 AAAPESEAKCHSTVIPGWFSEI---------------SPMWPGEAHSLKVEKVLFQGKSDFQDVLVFESATYGKVLVLDG 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334807 118 IVQLTEKDECAYQEMIAHLPLCSISSPKNVLVVGGGDGGVLREISRHSSVEVIDICEIDKMVIDVSKKFFPELAVGFDDP 197
Cdd:PLN02366  66 VIQLTERDECAYQEMITHLPLCSIPNPKKVLVVGGGDGGVLREIARHSSVEQIDICEIDKMVIDVSKKFFPDLAVGFDDP 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334807 198 RVQLHIGDAAEFLRKSPEGKYDAIIVDSSDPVGPALALVEKPFFETLARALKPGGVLCNMAESMWLHTHLIEDMISICRQ 277
Cdd:PLN02366 146 RVNLHIGDGVEFLKNAPEGTYDAIIVDSSDPVGPAQELFEKPFFESVARALRPGGVVCTQAESMWLHMDLIEDLIAICRE 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334807 278 TFK-SVHYAWSSVPTYPSGVIGFVLCSTEGPAVDFKNPINPIEKLDGAMTHKRELKFYNSDMHRAAFALPTFLRREVASL 356
Cdd:PLN02366 226 TFKgSVNYAWTTVPTYPSGVIGFVLCSKEGPAVDFKHPVNPIDKLEGAGKAKRPLKFYNSEVHRAAFCLPSFAKRELESL 305


                 ...
gi 145334807 357 LAS 359
Cdd:PLN02366 306 LTS 308
 
Name Accession Description Interval E-value
PLN02366 PLN02366
spermidine synthase
 38-359 0e+00

spermidine synthase


Pssm-ID: 215208 [Multi-domain]  Cd Length: 308  Bit Score: 572.36  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334807  38 ACVPEDDAKCHSTVVSGWFSEPhprsgkkggkavyfnNPMWPGEAHSLKVEKVLFKDKSDFQEVLVFESATYGKVLVLDG 117
Cdd:PLN02366   1 AAAPESEAKCHSTVIPGWFSEI---------------SPMWPGEAHSLKVEKVLFQGKSDFQDVLVFESATYGKVLVLDG 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334807 118 IVQLTEKDECAYQEMIAHLPLCSISSPKNVLVVGGGDGGVLREISRHSSVEVIDICEIDKMVIDVSKKFFPELAVGFDDP 197
Cdd:PLN02366  66 VIQLTERDECAYQEMITHLPLCSIPNPKKVLVVGGGDGGVLREIARHSSVEQIDICEIDKMVIDVSKKFFPDLAVGFDDP 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334807 198 RVQLHIGDAAEFLRKSPEGKYDAIIVDSSDPVGPALALVEKPFFETLARALKPGGVLCNMAESMWLHTHLIEDMISICRQ 277
Cdd:PLN02366 146 RVNLHIGDGVEFLKNAPEGTYDAIIVDSSDPVGPAQELFEKPFFESVARALRPGGVVCTQAESMWLHMDLIEDLIAICRE 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334807 278 TFK-SVHYAWSSVPTYPSGVIGFVLCSTEGPAVDFKNPINPIEKLDGAMTHKRELKFYNSDMHRAAFALPTFLRREVASL 356
Cdd:PLN02366 226 TFKgSVNYAWTTVPTYPSGVIGFVLCSKEGPAVDFKHPVNPIDKLEGAGKAKRPLKFYNSEVHRAAFCLPSFAKRELESL 305


                 ...
gi 145334807 357 LAS 359
Cdd:PLN02366 306 LTS 308
speE TIGR00417
spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine ...
 82-348 7.89e-97

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: 288.56  E-value: 7.89e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334807   82 AHSLKVEKVLFKDKSDFQEVLVFESATYGKVLVLDGIVQLTEKDECAYQEMIAHLPLCSISSPKNVLVVGGGDGGVLREI 161
Cdd:TIGR00417  11 GLTMKVDKVLYHEKSEFQDLEIFETEAFGNVLVLDGVVQTTERDEFIYHEMITHVPLFTHPNPKHVLVIGGGDGGVLREV 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334807  162 SRHSSVEVIDICEIDKMVIDVSKKFFPELAVGFDDPRVQLHIGDAAEFLRKSpEGKYDAIIVDSSDPVGPALALVEKPFF 241
Cdd:TIGR00417  91 LKHKSVESATLVDIDEKVIELSRKYLPNLAGSYDDPRVKLVIDDGFKFLADT-ENTFDVIIVDSTDPVGPAETLFTKEFY 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334807  242 ETLARALKPGGVLCNMAESMWLHTHLIEDMISICRQTFKSVHYAWSSVPTYPSGVIGFVLCStegpavdfKNPINPIEKL 321
Cdd:TIGR00417 170 ELLKKALNPDGIFVAQSESPWLQLELIIDLKRKLKEAFPITEYYTAAIPTYPSGLWTFTIAS--------KNKYRPLEVE 241

                         250       260       270
                  ....*....|....*....|....*....|
gi 145334807  322 DGAMTHKR---ELKFYNSDMHRAAFALPTF 348
Cdd:TIGR00417 242 IRRIKFEAedgKTKYYNPDIHKAAFVLPKW 271
Spermine_synth pfam01564
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ...
 126-306 2.49e-70

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: 217.57  E-value: 2.49e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334807  126 ECAYQEMIAHLPLCSISSPKNVLVVGGGDGGVLREISRHSSVEVIDICEIDKMVIDVSKKFFPELAVGFDDPRVQLHIGD 205
Cdd:pfam01564   1 EFIYHEMIAHVPLCSHPNPKKVLIIGGGDGGVLREVVKHPSVEKITLVDIDEKVIDFSKKFLPSLAIGFQDPRVKVVIGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334807  206 AAEFLRKSPEgKYDAIIVDSSDPVGPALALVEKPFFETLARALKPGGVLCNMAESMWLHTHLIEDMISICRQTFKSVHYA 285
Cdd:pfam01564  81 GFKFLKDYLN-TFDVIIVDSTDPVGPAENLFSKPFFDLLKKALKEDGVFITQAESPWLHLELIINILKNGKQVFPVVMPY 159

                         170       180
                  ....*....|....*....|.
gi 145334807  286 WSSVPTYPSGVIGFVLCSTEG 306
Cdd:pfam01564 160 VATIPTYPSGGWGFTVCSKNP 180
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
110-301 8.24e-58

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


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 186.19  E-value: 8.24e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334807 110 GKVLVLDGIVQLT-EKDECAYQEMIAHLPLCSISSPKNVLVVGGGDGGVLREISRHSSVEVIDICEIDKMVIDVSKKFFP 188
Cdd:COG0421    3 GRVLVLDGVVQSTmELDEFEYHEMMAHVPLLFHPNPKRVLIIGGGDGGLARELLKHPPVERVDVVEIDPEVVELAREYFP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334807 189 ELAVGFDDPRVQLHIGDAAEFLRKSPEgKYDAIIVDSSDPVGPALALVEKPFFETLARALKPGGVLCNMAESMWLHTHLI 268
Cdd:COG0421   83 LLAPAFDDPRLRVVIGDGRAFLREAEE-SYDVIIVDLTDPVGPAEGLFTREFYEDCRRALKPGGVLVVNLGSPFYGLDLL 161

                        170       180       190
                 ....*....|....*....|....*....|....
gi 145334807 269 EDMISICRQTFKSVHYAWSSVPTYPSG-VIGFVL 301
Cdd:COG0421  162 RRVLATLREVFPHVVLYAAPVPTYGGGnVFLLAL 195
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 159-254 1.09e-08

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: 52.43  E-value: 1.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334807 159 REISRHSSVEVIdICEIDKMVIDVSKKFfpelAVGFDDPRVQLHIGDAAEFLrKSPEGKYDAIIvdsSDPVGPALALVEK 238
Cdd:cd02440   14 LALASGPGARVT-GVDISPVALELARKA----AAALLADNVEVLKGDAEELP-PEADESFDVII---SDPPLHHLVEDLA 84

                         90
                 ....*....|....*.
gi 145334807 239 PFFETLARALKPGGVL 254
Cdd:cd02440   85 RFLEEARRLLKPGGVL 100
MFS_SpdSyn NF037959
fused MFS/spermidine synthase; Proteins of this family are fusion of a N-terminal MFS (Major ...
 174-253 1.42e-05

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: 46.76  E-value: 1.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334807 174 EIDKMVIDVSKKFFpelavGFDDPRVQLHIGDAAEFLRKSPEGKYDAIIVDS-SDPVGPAlALVEKPFFETLARALKPGG 252
Cdd:NF037959 306 EIDPAVTRVAAEDF-----WFDPASATVLHEDARRALRRRPEERFDVIVGDAfTDIAVPA-HLVTREFFELVRARLTPDG 379


                 .
gi 145334807 253 V 253
Cdd:NF037959 380 V 380
 
Name Accession Description Interval E-value
PLN02366 PLN02366
spermidine synthase
 38-359 0e+00

spermidine synthase


Pssm-ID: 215208 [Multi-domain]  Cd Length: 308  Bit Score: 572.36  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334807  38 ACVPEDDAKCHSTVVSGWFSEPhprsgkkggkavyfnNPMWPGEAHSLKVEKVLFKDKSDFQEVLVFESATYGKVLVLDG 117
Cdd:PLN02366   1 AAAPESEAKCHSTVIPGWFSEI---------------SPMWPGEAHSLKVEKVLFQGKSDFQDVLVFESATYGKVLVLDG 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334807 118 IVQLTEKDECAYQEMIAHLPLCSISSPKNVLVVGGGDGGVLREISRHSSVEVIDICEIDKMVIDVSKKFFPELAVGFDDP 197
Cdd:PLN02366  66 VIQLTERDECAYQEMITHLPLCSIPNPKKVLVVGGGDGGVLREIARHSSVEQIDICEIDKMVIDVSKKFFPDLAVGFDDP 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334807 198 RVQLHIGDAAEFLRKSPEGKYDAIIVDSSDPVGPALALVEKPFFETLARALKPGGVLCNMAESMWLHTHLIEDMISICRQ 277
Cdd:PLN02366 146 RVNLHIGDGVEFLKNAPEGTYDAIIVDSSDPVGPAQELFEKPFFESVARALRPGGVVCTQAESMWLHMDLIEDLIAICRE 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334807 278 TFK-SVHYAWSSVPTYPSGVIGFVLCSTEGPAVDFKNPINPIEKLDGAMTHKRELKFYNSDMHRAAFALPTFLRREVASL 356
Cdd:PLN02366 226 TFKgSVNYAWTTVPTYPSGVIGFVLCSKEGPAVDFKHPVNPIDKLEGAGKAKRPLKFYNSEVHRAAFCLPSFAKRELESL 305


                 ...
gi 145334807 357 LAS 359
Cdd:PLN02366 306 LTS 308
PRK00811 PRK00811
polyamine aminopropyltransferase;
53-354 6.84e-97

polyamine aminopropyltransferase;


Pssm-ID: 234843 [Multi-domain]  Cd Length: 283  Bit Score: 288.98  E-value: 6.84e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334807  53 SGWFSEPHPrsgkkggkavyfnnpmwPGEAHSLKVEKVLFKDKSDFQEVLVFESATYGKVLVLDGIVQLTEKDECAYQEM 132
Cdd:PRK00811   3 ELWFTETLT-----------------DNYGQSFRVKKVLYEEKSPFQRIEIFETPEFGRLLALDGCVMTTERDEFIYHEM 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334807 133 IAHLPLCSISSPKNVLVVGGGDGGVLREISRHSSVEVIDICEIDKMVIDVSKKFFPELAVG-FDDPRVQLHIGDAAEFLR 211
Cdd:PRK00811  66 MTHVPLFAHPNPKRVLIIGGGDGGTLREVLKHPSVEKITLVEIDERVVEVCRKYLPEIAGGaYDDPRVELVIGDGIKFVA 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334807 212 KsPEGKYDAIIVDSSDPVGPALALVEKPFFETLARALKPGGVLCNMAESMWLHTHLIEDMISICRQTFKSVHYAWSSVPT 291
Cdd:PRK00811 146 E-TENSFDVIIVDSTDPVGPAEGLFTKEFYENCKRALKEDGIFVAQSGSPFYQADEIKDMHRKLKEVFPIVRPYQAAIPT 224

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145334807 292 YPSGVIGFVLCSTEGPAVDFKNPINPIEKLDGAMthkrELKFYNSDMHRAAFALPTFLRREVA 354
Cdd:PRK00811 225 YPSGLWSFTFASKNDDLKFLPLDVIEARFAERGI----KTRYYNPELHKAAFALPQFVKDALK 283
speE TIGR00417
spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine ...
 82-348 7.89e-97

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: 288.56  E-value: 7.89e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334807   82 AHSLKVEKVLFKDKSDFQEVLVFESATYGKVLVLDGIVQLTEKDECAYQEMIAHLPLCSISSPKNVLVVGGGDGGVLREI 161
Cdd:TIGR00417  11 GLTMKVDKVLYHEKSEFQDLEIFETEAFGNVLVLDGVVQTTERDEFIYHEMITHVPLFTHPNPKHVLVIGGGDGGVLREV 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334807  162 SRHSSVEVIDICEIDKMVIDVSKKFFPELAVGFDDPRVQLHIGDAAEFLRKSpEGKYDAIIVDSSDPVGPALALVEKPFF 241
Cdd:TIGR00417  91 LKHKSVESATLVDIDEKVIELSRKYLPNLAGSYDDPRVKLVIDDGFKFLADT-ENTFDVIIVDSTDPVGPAETLFTKEFY 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334807  242 ETLARALKPGGVLCNMAESMWLHTHLIEDMISICRQTFKSVHYAWSSVPTYPSGVIGFVLCStegpavdfKNPINPIEKL 321
Cdd:TIGR00417 170 ELLKKALNPDGIFVAQSESPWLQLELIIDLKRKLKEAFPITEYYTAAIPTYPSGLWTFTIAS--------KNKYRPLEVE 241

                         250       260       270
                  ....*....|....*....|....*....|
gi 145334807  322 DGAMTHKR---ELKFYNSDMHRAAFALPTF 348
Cdd:TIGR00417 242 IRRIKFEAedgKTKYYNPDIHKAAFVLPKW 271
Spermine_synth pfam01564
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ...
 126-306 2.49e-70

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: 217.57  E-value: 2.49e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334807  126 ECAYQEMIAHLPLCSISSPKNVLVVGGGDGGVLREISRHSSVEVIDICEIDKMVIDVSKKFFPELAVGFDDPRVQLHIGD 205
Cdd:pfam01564   1 EFIYHEMIAHVPLCSHPNPKKVLIIGGGDGGVLREVVKHPSVEKITLVDIDEKVIDFSKKFLPSLAIGFQDPRVKVVIGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334807  206 AAEFLRKSPEgKYDAIIVDSSDPVGPALALVEKPFFETLARALKPGGVLCNMAESMWLHTHLIEDMISICRQTFKSVHYA 285
Cdd:pfam01564  81 GFKFLKDYLN-TFDVIIVDSTDPVGPAENLFSKPFFDLLKKALKEDGVFITQAESPWLHLELIINILKNGKQVFPVVMPY 159

                         170       180
                  ....*....|....*....|.
gi 145334807  286 WSSVPTYPSGVIGFVLCSTEG 306
Cdd:pfam01564 160 VATIPTYPSGGWGFTVCSKNP 180
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
110-301 8.24e-58

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


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 186.19  E-value: 8.24e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334807 110 GKVLVLDGIVQLT-EKDECAYQEMIAHLPLCSISSPKNVLVVGGGDGGVLREISRHSSVEVIDICEIDKMVIDVSKKFFP 188
Cdd:COG0421    3 GRVLVLDGVVQSTmELDEFEYHEMMAHVPLLFHPNPKRVLIIGGGDGGLARELLKHPPVERVDVVEIDPEVVELAREYFP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334807 189 ELAVGFDDPRVQLHIGDAAEFLRKSPEgKYDAIIVDSSDPVGPALALVEKPFFETLARALKPGGVLCNMAESMWLHTHLI 268
Cdd:COG0421   83 LLAPAFDDPRLRVVIGDGRAFLREAEE-SYDVIIVDLTDPVGPAEGLFTREFYEDCRRALKPGGVLVVNLGSPFYGLDLL 161

                        170       180       190
                 ....*....|....*....|....*....|....
gi 145334807 269 EDMISICRQTFKSVHYAWSSVPTYPSG-VIGFVL 301
Cdd:COG0421  162 RRVLATLREVFPHVVLYAAPVPTYGGGnVFLLAL 195
PLN02823 PLN02823
spermine synthase
 84-355 5.88e-47

spermine synthase


Pssm-ID: 178418 [Multi-domain]  Cd Length: 336  Bit Score: 162.54  E-value: 5.88e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334807  84 SLKVEKVLFKDKSDFQEVLVFESATYGKVLVLDGIVQLTEKDECAYQEMIAHLPLCSISSPKNVLVVGGGDGGVLREISR 163
Cdd:PLN02823  44 SYAVNSVLHTGTSEFQDIALVDTKPFGKVLIIDGKMQSAEADEFVYHESLVHPALLHHPNPKTVFIMGGGEGSTAREVLR 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334807 164 HSSVEVIDICEIDKMVIDVSKKFFPELAVGFDDPRVQLHIGDAAEFLRKsPEGKYDAIIVDSSDPV--GPALALVEKPFF 241
Cdd:PLN02823 124 HKTVEKVVMCDIDQEVVDFCRKHLTVNREAFCDKRLELIINDARAELEK-RDEKFDVIIGDLADPVegGPCYQLYTKSFY 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334807 242 E-TLARALKPGGVLCNMAESMWLHTHLiEDMISIC---RQTFKSVhYAWSS-VPTYPSgVIGFVLcstegpAVDFKNPIN 316
Cdd:PLN02823 203 ErIVKPKLNPGGIFVTQAGPAGILTHK-EVFSSIYntlRQVFKYV-VPYTAhVPSFAD-TWGWVM------ASDHPFADL 273

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 145334807 317 PIEKLDGAMTHK--RELKFYNSDMHRAAFALPTFLRREVAS 355
Cdd:PLN02823 274 SAEELDSRIKERidGELKYLDGETFSSAFALNKTVRQALAN 314
COG4262 COG4262
Predicted spermidine synthase with an N-terminal membrane domain [General function prediction ...
 70-254 6.30e-29

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


Pssm-ID: 443404 [Multi-domain]  Cd Length: 426  Bit Score: 115.73  E-value: 6.30e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334807  70 AVYFNNPMWPGEAHSLKVEKVLFKDKSDFQEVLVFESATYgKVLVLDGIVQLTEKDECAYQEMIAHLPLCSISSPKNVLV 149
Cdd:COG4262  214 GLVFADPIESSAEQKLYGDPVVYSEQTPYQRIVVTRDKDD-RRLYLNGNLQFSSLDEYRYHEALVHPPMAAHPRPRRVLV 292

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334807 150 VGGGDGGVLREISRHSSVEVIDICEIDKMVIDVSKK--FFPELAVG-FDDPRVQLHIGDAAEFLRKSPEgKYDAIIVDSS 226
Cdd:COG4262  293 LGGGDGLAAREVLKYPDVESVTLVDLDPEVTDLAKTnpFLRELNGGaLNDPRVTVVNADAFQFLRETDE-KYDVIIVDLP 371

                        170       180
                 ....*....|....*....|....*....
gi 145334807 227 DPVGPALA-LVEKPFFETLARALKPGGVL 254
Cdd:COG4262  372 DPSNFSLGkLYSVEFYRLVRRHLAPGGVL 400
PRK03612 PRK03612
polyamine aminopropyltransferase;
88-353 4.31e-20

polyamine aminopropyltransferase;


Pssm-ID: 235139 [Multi-domain]  Cd Length: 521  Bit Score: 91.44  E-value: 4.31e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334807  88 EKVLFKDK------SDFQEVLVFESATYGKV---LVLDGIVQLTEKDECAYQEMIAHLPLCSISSPKNVLVVGGGDGGVL 158
Cdd:PRK03612 233 EQLLYGDPvvyaeqTPYQRIVVTRRGNGRGPdlrLYLNGRLQFSSRDEYRYHEALVHPAMAASARPRRVLVLGGGDGLAL 312

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334807 159 REISRHSSVEVIDICEIDKMVIDVSKKfFPELAV----GFDDPRVQLHIGDAAEFLRKSPEgKYDAIIVDSSDPVGPALA 234
Cdd:PRK03612 313 REVLKYPDVEQVTLVDLDPAMTELART-SPALRAlnggALDDPRVTVVNDDAFNWLRKLAE-KFDVIIVDLPDPSNPALG 390

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334807 235 -LVEKPFFETLARALKPGGVLCNMAESMWlhtHLIEDMISIcRQTFKSVHYAWSS----VPTYpsGVIGFVLCSTEGPAV 309
Cdd:PRK03612 391 kLYSVEFYRLLKRRLAPDGLLVVQSTSPY---FAPKAFWSI-EATLEAAGLATTPyhvnVPSF--GEWGFVLAGAGARPP 464

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 145334807 310 DFKNPINPIekldgamthkrELKFYNSDMHRAAFALP-TFLRREV 353
Cdd:PRK03612 465 LAVPTELPV-----------PLRFLDPALLAAAFVFPkDMRRREV 498
Spermine_synt_N pfam17284
Spermidine synthase tetramerization domain; This domain represents the N-terminal ...
 54-123 4.41e-19

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: 79.63  E-value: 4.41e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334807   54 GWFSEPHPrsgkkggkavyfnnpmwPGEAHSLKVEKVLFKDKSDFQEVLVFESATYGKVLVLDGIVQLTE 123
Cdd:pfam17284   1 GWFTEIHD-----------------LGQALEYKVEKVLYDEKSEYQDIEIFESKTFGNVLVLDGVVQLTE 53
speE PRK01581
polyamine aminopropyltransferase;
90-255 2.86e-17

polyamine aminopropyltransferase;


Pssm-ID: 234961 [Multi-domain]  Cd Length: 374  Bit Score: 81.93  E-value: 2.86e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334807  90 VLFKDKSDFQEVLVFESATYGkvLVLDGIVQLTEKDECAYQEMIAHLPLCSISSPKNVLVVGGGDGGVLREISRHSSVEV 169
Cdd:PRK01581  99 NLFAEKSNYQNINLLQVSDIR--LYLDKQLQFSSVDEQIYHEALVHPIMSKVIDPKRVLILGGGDGLALREVLKYETVLH 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334807 170 IDICEIDKMVIDVSKKfFPELAV----GFDDPRVQLHIGDAAEFLrKSPEGKYDAIIVDSSDPVGPAL-ALVEKPFFETL 244
Cdd:PRK01581 177 VDLVDLDGSMINMARN-VPELVSlnksAFFDNRVNVHVCDAKEFL-SSPSSLYDVIIIDFPDPATELLsTLYTSELFARI 254

                        170
                 ....*....|..
gi 145334807 245 ARALKPGG-VLC 255
Cdd:PRK01581 255 ATFLTEDGaFVC 266
speE PRK00536
spermidine synthase; Provisional
 87-349 1.26e-11

spermidine synthase; Provisional


Pssm-ID: 134311 [Multi-domain]  Cd Length: 262  Bit Score: 64.11  E-value: 1.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334807  87 VEKVLFKDKSDFQEVLVFESATYGKVLVLDGivQLTEKDECAYQ-EMIAHLPLCSISSPKNVLVVGGGDGGVLREISRHS 165
Cdd:PRK00536  17 IEAKLLDVRSEHNILEIFKSKDFGEIAMLNK--QLLFKNFLHIEsELLAHMGGCTKKELKEVLIVDGFDLELAHQLFKYD 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334807 166 SVevIDICEIDKMVIDVSKKFFPELAVGFDDPRVQlHIGDAAEFLRKspegKYDAIIVDSsdpvgpalaLVEKPFFETLA 245
Cdd:PRK00536  95 TH--VDFVQADEKILDSFISFFPHFHEVKNNKNFT-HAKQLLDLDIK----KYDLIICLQ---------EPDIHKIDGLK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334807 246 RALKPGGVLCNMAESMWLHTHLIEDMISICRQTFKSVhyawssVPTYPSGVI----GFVLCSTE-GPAVDFKNPinPIEK 320
Cdd:PRK00536 159 RMLKEDGVFISVAKHPLLEHVSMQNALKNMGDFFSIA------MPFVAPLRIlsnkGYIYASFKtHPLKDLMLQ--KIEA 230

                        250       260
                 ....*....|....*....|....*....
gi 145334807 321 LDGamthkreLKFYNSDMHRAAFALPTFL 349
Cdd:PRK00536 231 LKS-------VRYYNEDIHRAAFALPKNL 252
PRK04457 PRK04457
polyamine aminopropyltransferase;
174-254 1.67e-09

polyamine aminopropyltransferase;


Pssm-ID: 179854 [Multi-domain]  Cd Length: 262  Bit Score: 57.74  E-value: 1.67e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334807 174 EIDKMVIDVSKKFFpelAVGFDDPRVQLHIGDAAEFLRKSPEgKYDAIIVDSSDPVGPALALVEKPFFETLARALKPGGV 253
Cdd:PRK04457  97 EINPQVIAVARNHF---ELPENGERFEVIEADGAEYIAVHRH-STDVILVDGFDGEGIIDALCTQPFFDDCRNALSSDGI 172


                 .
gi 145334807 254 L 254
Cdd:PRK04457 173 F 173
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 159-254 1.09e-08

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: 52.43  E-value: 1.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334807 159 REISRHSSVEVIdICEIDKMVIDVSKKFfpelAVGFDDPRVQLHIGDAAEFLrKSPEGKYDAIIvdsSDPVGPALALVEK 238
Cdd:cd02440   14 LALASGPGARVT-GVDISPVALELARKA----AAALLADNVEVLKGDAEELP-PEADESFDVII---SDPPLHHLVEDLA 84

                         90
                 ....*....|....*.
gi 145334807 239 PFFETLARALKPGGVL 254
Cdd:cd02440   85 RFLEEARRLLKPGGVL 100
COG2521 COG2521
Predicted archaeal methyltransferase [General function prediction only];
168-254 2.35e-08

Predicted archaeal methyltransferase [General function prediction only];


Pssm-ID: 442011 [Multi-domain]  Cd Length: 285  Bit Score: 54.53  E-value: 2.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334807 168 EVIDIcEIDKMVIDVSKK--FFPELAvgfdDPRVQLHIGDAAEFLRKSPEGKYDAIIvdsSDP--VGPALALVEKPFFET 243
Cdd:COG2521  157 EVITV-EKDPNVLELAELnpWSRELA----NERIKIILGDASEVIKTFPDESFDAII---HDPprFSLAGELYSLEFYRE 228

                         90
                 ....*....|.
gi 145334807 244 LARALKPGGVL 254
Cdd:COG2521  229 LYRVLKPGGRL 239
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 173-254 3.17e-08

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: 52.49  E-value: 3.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334807 173 CEIDKMVIDVSKKFFPELavGFDDpRVQLHIGDAAEFLRKSPEGKYDAIIVDSsdpvGPALALvekPFFETLARALKPGG 252
Cdd:COG4122   47 IEIDPERAAIARENFARA--GLAD-RIRLILGDALEVLPRLADGPFDLVFIDA----DKSNYP---DYLELALPLLRPGG 116


                 ..
gi 145334807 253 VL 254
Cdd:COG4122  117 LI 118
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 194-255 2.83e-07

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: 50.93  E-value: 2.83e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145334807 194 FDDPRVQLHIGDAAEFLrksPEGKYDAIIVDSSDPVgpaLALvekpffETLARALKPGGVLC 255
Cdd:COG2519  140 GLPDNVELKLGDIREGI---DEGDVDAVFLDMPDPW---EAL------EAVAKALKPGGVLV 189
MFS_SpdSyn NF037959
fused MFS/spermidine synthase; Proteins of this family are fusion of a N-terminal MFS (Major ...
 174-253 1.42e-05

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: 46.76  E-value: 1.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334807 174 EIDKMVIDVSKKFFpelavGFDDPRVQLHIGDAAEFLRKSPEGKYDAIIVDS-SDPVGPAlALVEKPFFETLARALKPGG 252
Cdd:NF037959 306 EIDPAVTRVAAEDF-----WFDPASATVLHEDARRALRRRPEERFDVIVGDAfTDIAVPA-HLVTREFFELVRARLTPDG 379


                 .
gi 145334807 253 V 253
Cdd:NF037959 380 V 380
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
197-254 1.49e-05

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 43.27  E-value: 1.49e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334807 197 PRVQLHIGDAAEFlrkSPEGKYDAIIvdSSDpvgpALALVEKP--FFETLARALKPGGVL 254
Cdd:COG4106   46 PNVRFVVADLRDL---DPPEPFDLVV--SNA----ALHWLPDHaaLLARLAAALAPGGVL 96
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
199-255 1.51e-04

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 41.91  E-value: 1.51e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 145334807 199 VQLHIGDAAEFlrKSPEGKYDAIIvdSSD--PVGPALAlvekPFFETLARALKPGGVLC 255
Cdd:COG4976   91 DRLLVADLADL--AEPDGRFDLIV--AADvlTYLGDLA----AVFAGVARALKPGGLFI 141
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 164-261 1.51e-04

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 42.21  E-value: 1.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334807 164 HSSVEVIDICEIdkmVIDVSKKFFPELAVGfddpRVQLHIGDAAEFLrKSPEGKYDAIIVDSS----DPVgpalalVEKP 239
Cdd:COG0500   49 GGRVIGIDLSPE---AIALARARAAKAGLG----NVEFLVADLAELD-PLPAESFDLVVAFGVlhhlPPE------EREA 114

                         90       100
                 ....*....|....*....|..
gi 145334807 240 FFETLARALKPGGVLCNMAESM 261
Cdd:COG0500  115 LLRELARALKPGGVLLLSASDA 136
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 159-252 1.71e-04

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 40.24  E-value: 1.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334807  159 REISRHSSVEV--IDICEidKMvIDVSKKFFPElavgfDDPRVQLHIGDAAEFlrKSPEGKYDAIIvdSSDpvgpALALV 236
Cdd:pfam13649  13 LALARRGGARVtgVDLSP--EM-LERARERAAE-----AGLNVEFVQGDAEDL--PFPDGSFDLVV--SSG----VLHHL 76

                          90       100
                  ....*....|....*....|
gi 145334807  237 EKP----FFETLARALKPGG 252
Cdd:pfam13649  77 PDPdleaALREIARVLKPGG 96
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 198-254 2.18e-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: 2.18e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 145334807 198 RVQLHIGDAAEFlrkSPEGKYDAII-VDSSDPVGPALAlveKPFFETLARALKPGGVL 254
Cdd:COG2230  102 RVEVRLADYRDL---PADGQFDAIVsIGMFEHVGPENY---PAYFAKVARLLKPGGRL 153
Methyltransf_24 pfam13578
Methyltransferase domain; This family appears to be a methyltransferase domain.
 196-254 4.54e-04

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


Pssm-ID: 433324 [Multi-domain]  Cd Length: 106  Bit Score: 39.21  E-value: 4.54e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 145334807  196 DPRVQLHIGDAAEFLRKSPEGKYDAIIVDSsDPVGPAlalvEKPFFETLARALKPGGVL 254
Cdd:pfam13578  48 DDRVRLIVGDSREALPSLADGPIDLLFIDG-DHTYEA----VLNDLELWLPRLAPGGVI 101
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 173-254 5.62e-04

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: 39.23  E-value: 5.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334807 173 CEIDKMVIDVSKKFFPELavgfddpRVQLHIGDAAEFlrKSPEGKYDAIIvdSSDpvgpALALVEKP--FFETLARALKP 250
Cdd:COG2227   52 VDISPEALEIARERAAEL-------NVDFVQGDLEDL--PLEDGSFDLVI--CSE----VLEHLPDPaaLLRELARLLKP 116


                 ....
gi 145334807 251 GGVL 254
Cdd:COG2227  117 GGLL 120
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 170-277 1.26e-03

tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443299 [Multi-domain]  Cd Length: 238  Bit Score: 39.74  E-value: 1.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334807 170 IDICEIDK-MVidvskkffpELAV------GFDDpRVQLHIGDAAEFLRKSPEGKYDAII-----------VDSSDPvGP 231
Cdd:COG4123   64 ITGVEIQPeAA---------ELARrnvalnGLED-RITVIHGDLKEFAAELPPGSFDLVVsnppyfkagsgRKSPDE-AR 132

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 145334807 232 ALALVE-----KPFFETLARALKPGGVLCnmaesMWLHTHLIEDMISICRQ 277
Cdd:COG4123  133 AIARHEdaltlEDLIRAAARLLKPGGRFA-----LIHPAERLAEILAALRK 178
YhdJ COG0863
DNA modification methylase [Replication, recombination and repair];
200-277 4.01e-03

DNA modification methylase [Replication, recombination and repair];


Pssm-ID: 440623  Cd Length: 236  Bit Score: 38.37  E-value: 4.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334807 200 QLHIGDAAEFLRKSPEGKYDAIIVD-----------SSDPVGPALALVE-----KPFFETLARALKPGGvlcnmaeSMWL 263
Cdd:COG0863    1 RLICGDCLEVLKELPDESVDLIVTDppynlgkkyglGRREIGNELSFEEyleflREWLAECYRVLKPGG-------SLYV 73

                         90
                 ....*....|....*.
gi 145334807 264 HT--HLIEDMISICRQ 277
Cdd:COG0863   74 NIgdRYISRLIAALRD 89
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
 174-254 9.62e-03

Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 36.99  E-value: 9.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334807 174 EIDKMVIDVSKKFFPELavGFDdpRVQLHIGDAAEFLrkSPEGKYDAIIVDSSDPVGPAlALVEkpffetlarALKPGGV 253
Cdd:COG2518   95 ERDPELAERARERLAAL--GYD--NVTVRVGDGALGW--PEHAPFDRIIVTAAAPEVPE-ALLE---------QLAPGGR 158


                 .
gi 145334807 254 L 254
Cdd:COG2518  159 L 159
 
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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