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Conserved domains on  [gi|6323175|ref|NP_013247|]
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spermine synthase [Saccharomyces cerevisiae S288C]

Protein Classification

spermidine/spermine synthase( domain architecture ID 10015647)

spermidine/spermine synthase catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) or spermidine to yield spermidine or spermine, respectively

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
speE TIGR00417
spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine ...
 14-293 2.33e-167

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: 464.98  E-value: 2.33e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175     14 WFREINDKSFpgqAFTMTVDSILYEARSEFQDILIFRNKVYGTVLVLDGIVQCTEFDEFAYQEMITHIAMFAHSNPKRVL 93
Cdd:TIGR00417   1 WFTEYHDKNF---GLTMKVDKVLYHEKSEFQDLEIFETEAFGNVLVLDGVVQTTERDEFIYHEMITHVPLFTHPNPKHVL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175     94 IIGGGDGGVLREVAKHSCVEDITMVEIDSSVIELSRKFLPTLSnGAFDDERLDLKLCDGFKFLQDIgasdvHKKFDVIIT 173
Cdd:TIGR00417  78 VIGGGDGGVLREVLKHKSVESATLVDIDEKVIELSRKYLPNLA-GSYDDPRVKLVIDDGFKFLADT-----ENTFDVIIV 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175    174 DSSDPEGPAEAFFQERYFELLKDALNPNGVVIMQsSENFWLNLKYLHDLKNTAKKVFPNTEYCYTMVPTYTSGQLGLIVC 253
Cdd:TIGR00417 152 DSTDPVGPAETLFTKEFYELLKKALNPDGIFVAQ-SESPWLQLELIIDLKRKLKEAFPITEYYTAAIPTYPSGLWTFTIA 230

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 6323175    254 SNNANIPLNIPQRKIS-EQEQGKLKYYNPQIHSSAFVLPTW 293
Cdd:TIGR00417 231 SKNKYRPLEVEIRRIKfEAEDGKTKYYNPDIHKAAFVLPKW 271
 
Name Accession Description Interval E-value
speE TIGR00417
spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine ...
 14-293 2.33e-167

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: 464.98  E-value: 2.33e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175     14 WFREINDKSFpgqAFTMTVDSILYEARSEFQDILIFRNKVYGTVLVLDGIVQCTEFDEFAYQEMITHIAMFAHSNPKRVL 93
Cdd:TIGR00417   1 WFTEYHDKNF---GLTMKVDKVLYHEKSEFQDLEIFETEAFGNVLVLDGVVQTTERDEFIYHEMITHVPLFTHPNPKHVL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175     94 IIGGGDGGVLREVAKHSCVEDITMVEIDSSVIELSRKFLPTLSnGAFDDERLDLKLCDGFKFLQDIgasdvHKKFDVIIT 173
Cdd:TIGR00417  78 VIGGGDGGVLREVLKHKSVESATLVDIDEKVIELSRKYLPNLA-GSYDDPRVKLVIDDGFKFLADT-----ENTFDVIIV 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175    174 DSSDPEGPAEAFFQERYFELLKDALNPNGVVIMQsSENFWLNLKYLHDLKNTAKKVFPNTEYCYTMVPTYTSGQLGLIVC 253
Cdd:TIGR00417 152 DSTDPVGPAETLFTKEFYELLKKALNPDGIFVAQ-SESPWLQLELIIDLKRKLKEAFPITEYYTAAIPTYPSGLWTFTIA 230

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 6323175    254 SNNANIPLNIPQRKIS-EQEQGKLKYYNPQIHSSAFVLPTW 293
Cdd:TIGR00417 231 SKNKYRPLEVEIRRIKfEAEDGKTKYYNPDIHKAAFVLPKW 271
PLN02366 PLN02366
spermidine synthase
 10-298 3.43e-119

spermidine synthase


Pssm-ID: 215208 [Multi-domain]  Cd Length: 308  Bit Score: 344.32  E-value: 3.43e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175    10 IKDGWFREINdKSFPGQAFTMTVDSILYEARSEFQDILIFRNKVYGTVLVLDGIVQCTEFDEFAYQEMITHIAMFAHSNP 89
Cdd:PLN02366  14 VIPGWFSEIS-PMWPGEAHSLKVEKVLFQGKSDFQDVLVFESATYGKVLVLDGVIQLTERDECAYQEMITHLPLCSIPNP 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175    90 KRVLIIGGGDGGVLREVAKHSCVEDITMVEIDSSVIELSRKFLPTLSNGaFDDERLDLKLCDGFKFLQDIGASdvhkKFD 169
Cdd:PLN02366  93 KKVLVVGGGDGGVLREIARHSSVEQIDICEIDKMVIDVSKKFFPDLAVG-FDDPRVNLHIGDGVEFLKNAPEG----TYD 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175   170 VIITDSSDPEGPAEAFFQERYFELLKDALNPNGVVIMQsSENFWLNLKYLHDLKNTAKKVFPNT-EYCYTMVPTYTSGQL 248
Cdd:PLN02366 168 AIIVDSSDPVGPAQELFEKPFFESVARALRPGGVVCTQ-AESMWLHMDLIEDLIAICRETFKGSvNYAWTTVPTYPSGVI 246

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 6323175   249 GLIVCSN-----NANIPLNIPQRKISEQE-QGKLKYYNPQIHSSAFVLPTWADKVI 298
Cdd:PLN02366 247 GFVLCSKegpavDFKHPVNPIDKLEGAGKaKRPLKFYNSEVHRAAFCLPSFAKREL 302
Spermine_synth pfam01564
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ...
 71-257 1.59e-87

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: 259.56  E-value: 1.59e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175     71 EFAYQEMITHIAMFAHSNPKRVLIIGGGDGGVLREVAKHSCVEDITMVEIDSSVIELSRKFLPTLSNGaFDDERLDLKLC 150
Cdd:pfam01564   1 EFIYHEMIAHVPLCSHPNPKKVLIIGGGDGGVLREVVKHPSVEKITLVDIDEKVIDFSKKFLPSLAIG-FQDPRVKVVIG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175    151 DGFKFLQDIGasdvhKKFDVIITDSSDPEGPAEAFFQERYFELLKDALNPNGVVIMQsSENFWLNLKYLHDLKNTAKKVF 230
Cdd:pfam01564  80 DGFKFLKDYL-----NTFDVIIVDSTDPVGPAENLFSKPFFDLLKKALKEDGVFITQ-AESPWLHLELIINILKNGKQVF 153

                         170       180
                  ....*....|....*....|....*..
gi 6323175    231 PNTEYCYTMVPTYTSGQLGLIVCSNNA 257
Cdd:pfam01564 154 PVVMPYVATIPTYPSGGWGFTVCSKNP 180
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
55-246 4.34e-75

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


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 228.17  E-value: 4.34e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175   55 GTVLVLDGIVQCT-EFDEFAYQEMITHIAMFAHSNPKRVLIIGGGDGGVLREVAKHSCVEDITMVEIDSSVIELSRKFLP 133
Cdd:COG0421   3 GRVLVLDGVVQSTmELDEFEYHEMMAHVPLLFHPNPKRVLIIGGGDGGLARELLKHPPVERVDVVEIDPEVVELAREYFP 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175  134 tLSNGAFDDERLDLKLCDGFKFLQdigasDVHKKFDVIITDSSDPEGPAEAFFQERYFELLKDALNPNGVVIMQsSENFW 213
Cdd:COG0421  83 -LLAPAFDDPRLRVVIGDGRAFLR-----EAEESYDVIIVDLTDPVGPAEGLFTREFYEDCRRALKPGGVLVVN-LGSPF 155

                       170       180       190
                ....*....|....*....|....*....|...
gi 6323175  214 LNLKYLHDLKNTAKKVFPNTEYCYTMVPTYTSG 246
Cdd:COG0421 156 YGLDLLRRVLATLREVFPHVVLYAAPVPTYGGG 188
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 91-207 5.89e-12

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: 61.29  E-value: 5.89e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175   91 RVLIIGGGDGGVLREVAKHSCVEdITMVEIDSSVIELSRKFlptlsNGAFDDERLDLKLCDGFKFLQDIGasdvhKKFDV 170
Cdd:cd02440   1 RVLDLGCGTGALALALASGPGAR-VTGVDISPVALELARKA-----AAALLADNVEVLKGDAEELPPEAD-----ESFDV 69

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 6323175  171 IItdsSDPEGPAEAFFQERYFELLKDALNPNGVVIMQ 207
Cdd:cd02440  70 II---SDPPLHHLVEDLARFLEEARRLLKPGGVLVLT 103
MFS_SpdSyn NF037959
fused MFS/spermidine synthase; Proteins of this family are fusion of a N-terminal MFS (Major ...
 57-234 1.57e-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: 45.99  E-value: 1.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175    57 VLVLDGIVQCTEfDEFAYQEMIT-HIAMF-------AHSNPKRVLIIGGGDGGVLREVAKHSCVEDITMVEIDSSVIELS 128
Cdd:NF037959 237 LMVLDHLAHGIN-ARDDPTVLFTpYAAMLdelarlrMGRADFSAFFIGGGAYTLPRAWAARRPAGRITVAEIDPAVTRVA 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175   129 RKFLptlsngAFDDERLDLKLCDGFKFLQDIGASdvhkKFDVIITDS-SDPEGPAEAFFQErYFELLKDALNPNGVVIMQ 207
Cdd:NF037959 316 AEDF------WFDPASATVLHEDARRALRRRPEE----RFDVIVGDAfTDIAVPAHLVTRE-FFELVRARLTPDGVYLMN 384

                        170       180
                 ....*....|....*....|....*..
gi 6323175   208 SSENFwLNLKYLHDLKNTAKKVFPNTE 234
Cdd:NF037959 385 VIDHA-DRLRALAALVATLREVFPVVE 410
 
Name Accession Description Interval E-value
speE TIGR00417
spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine ...
 14-293 2.33e-167

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: 464.98  E-value: 2.33e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175     14 WFREINDKSFpgqAFTMTVDSILYEARSEFQDILIFRNKVYGTVLVLDGIVQCTEFDEFAYQEMITHIAMFAHSNPKRVL 93
Cdd:TIGR00417   1 WFTEYHDKNF---GLTMKVDKVLYHEKSEFQDLEIFETEAFGNVLVLDGVVQTTERDEFIYHEMITHVPLFTHPNPKHVL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175     94 IIGGGDGGVLREVAKHSCVEDITMVEIDSSVIELSRKFLPTLSnGAFDDERLDLKLCDGFKFLQDIgasdvHKKFDVIIT 173
Cdd:TIGR00417  78 VIGGGDGGVLREVLKHKSVESATLVDIDEKVIELSRKYLPNLA-GSYDDPRVKLVIDDGFKFLADT-----ENTFDVIIV 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175    174 DSSDPEGPAEAFFQERYFELLKDALNPNGVVIMQsSENFWLNLKYLHDLKNTAKKVFPNTEYCYTMVPTYTSGQLGLIVC 253
Cdd:TIGR00417 152 DSTDPVGPAETLFTKEFYELLKKALNPDGIFVAQ-SESPWLQLELIIDLKRKLKEAFPITEYYTAAIPTYPSGLWTFTIA 230

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 6323175    254 SNNANIPLNIPQRKIS-EQEQGKLKYYNPQIHSSAFVLPTW 293
Cdd:TIGR00417 231 SKNKYRPLEVEIRRIKfEAEDGKTKYYNPDIHKAAFVLPKW 271
PLN02366 PLN02366
spermidine synthase
 10-298 3.43e-119

spermidine synthase


Pssm-ID: 215208 [Multi-domain]  Cd Length: 308  Bit Score: 344.32  E-value: 3.43e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175    10 IKDGWFREINdKSFPGQAFTMTVDSILYEARSEFQDILIFRNKVYGTVLVLDGIVQCTEFDEFAYQEMITHIAMFAHSNP 89
Cdd:PLN02366  14 VIPGWFSEIS-PMWPGEAHSLKVEKVLFQGKSDFQDVLVFESATYGKVLVLDGVIQLTERDECAYQEMITHLPLCSIPNP 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175    90 KRVLIIGGGDGGVLREVAKHSCVEDITMVEIDSSVIELSRKFLPTLSNGaFDDERLDLKLCDGFKFLQDIGASdvhkKFD 169
Cdd:PLN02366  93 KKVLVVGGGDGGVLREIARHSSVEQIDICEIDKMVIDVSKKFFPDLAVG-FDDPRVNLHIGDGVEFLKNAPEG----TYD 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175   170 VIITDSSDPEGPAEAFFQERYFELLKDALNPNGVVIMQsSENFWLNLKYLHDLKNTAKKVFPNT-EYCYTMVPTYTSGQL 248
Cdd:PLN02366 168 AIIVDSSDPVGPAQELFEKPFFESVARALRPGGVVCTQ-AESMWLHMDLIEDLIAICRETFKGSvNYAWTTVPTYPSGVI 246

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 6323175   249 GLIVCSN-----NANIPLNIPQRKISEQE-QGKLKYYNPQIHSSAFVLPTWADKVI 298
Cdd:PLN02366 247 GFVLCSKegpavDFKHPVNPIDKLEGAGKaKRPLKFYNSEVHRAAFCLPSFAKREL 302
PRK00811 PRK00811
polyamine aminopropyltransferase;
11-291 6.49e-107

polyamine aminopropyltransferase;


Pssm-ID: 234843 [Multi-domain]  Cd Length: 283  Bit Score: 312.48  E-value: 6.49e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175    11 KDGWFREINDKSFpgqAFTMTVDSILYEARSEFQDILIFRNKVYGTVLVLDGIVQCTEFDEFAYQEMITHIAMFAHSNPK 90
Cdd:PRK00811   2 MELWFTETLTDNY---GQSFRVKKVLYEEKSPFQRIEIFETPEFGRLLALDGCVMTTERDEFIYHEMMTHVPLFAHPNPK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175    91 RVLIIGGGDGGVLREVAKHSCVEDITMVEIDSSVIELSRKFLPTLSNGAFDDERLDLKLCDGFKFLQdigasDVHKKFDV 170
Cdd:PRK00811  79 RVLIIGGGDGGTLREVLKHPSVEKITLVEIDERVVEVCRKYLPEIAGGAYDDPRVELVIGDGIKFVA-----ETENSFDV 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175   171 IITDSSDPEGPAEAFFQERYFELLKDALNPNGVVIMQsSENFWLNLKYLHDLKNTAKKVFPNTEYCYTMVPTYTSGQLGL 250
Cdd:PRK00811 154 IIVDSTDPVGPAEGLFTKEFYENCKRALKEDGIFVAQ-SGSPFYQADEIKDMHRKLKEVFPIVRPYQAAIPTYPSGLWSF 232

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 6323175   251 IVCSNNANI---PLNIPQRKISEQEQgKLKYYNPQIHSSAFVLP 291
Cdd:PRK00811 233 TFASKNDDLkflPLDVIEARFAERGI-KTRYYNPELHKAAFALP 275
Spermine_synth pfam01564
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ...
 71-257 1.59e-87

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: 259.56  E-value: 1.59e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175     71 EFAYQEMITHIAMFAHSNPKRVLIIGGGDGGVLREVAKHSCVEDITMVEIDSSVIELSRKFLPTLSNGaFDDERLDLKLC 150
Cdd:pfam01564   1 EFIYHEMIAHVPLCSHPNPKKVLIIGGGDGGVLREVVKHPSVEKITLVDIDEKVIDFSKKFLPSLAIG-FQDPRVKVVIG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175    151 DGFKFLQDIGasdvhKKFDVIITDSSDPEGPAEAFFQERYFELLKDALNPNGVVIMQsSENFWLNLKYLHDLKNTAKKVF 230
Cdd:pfam01564  80 DGFKFLKDYL-----NTFDVIIVDSTDPVGPAENLFSKPFFDLLKKALKEDGVFITQ-AESPWLHLELIINILKNGKQVF 153

                         170       180
                  ....*....|....*....|....*..
gi 6323175    231 PNTEYCYTMVPTYTSGQLGLIVCSNNA 257
Cdd:pfam01564 154 PVVMPYVATIPTYPSGGWGFTVCSKNP 180
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
55-246 4.34e-75

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


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 228.17  E-value: 4.34e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175   55 GTVLVLDGIVQCT-EFDEFAYQEMITHIAMFAHSNPKRVLIIGGGDGGVLREVAKHSCVEDITMVEIDSSVIELSRKFLP 133
Cdd:COG0421   3 GRVLVLDGVVQSTmELDEFEYHEMMAHVPLLFHPNPKRVLIIGGGDGGLARELLKHPPVERVDVVEIDPEVVELAREYFP 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175  134 tLSNGAFDDERLDLKLCDGFKFLQdigasDVHKKFDVIITDSSDPEGPAEAFFQERYFELLKDALNPNGVVIMQsSENFW 213
Cdd:COG0421  83 -LLAPAFDDPRLRVVIGDGRAFLR-----EAEESYDVIIVDLTDPVGPAEGLFTREFYEDCRRALKPGGVLVVN-LGSPF 155

                       170       180       190
                ....*....|....*....|....*....|...
gi 6323175  214 LNLKYLHDLKNTAKKVFPNTEYCYTMVPTYTSG 246
Cdd:COG0421 156 YGLDLLRRVLATLREVFPHVVLYAAPVPTYGGG 188
PLN02823 PLN02823
spermine synthase
 4-291 7.93e-62

spermine synthase


Pssm-ID: 178418 [Multi-domain]  Cd Length: 336  Bit Score: 199.14  E-value: 7.93e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175     4 NSQHPYIKDGWFRE-INDksfpGQAFTMTVDSILYEARSEFQDILIFRNKVYGTVLVLDGIVQCTEFDEFAYQEMITHIA 82
Cdd:PLN02823  22 ALASNYAKSLWYEEeIED----DLRWSYAVNSVLHTGTSEFQDIALVDTKPFGKVLIIDGKMQSAEADEFVYHESLVHPA 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175    83 MFAHSNPKRVLIIGGGDGGVLREVAKHSCVEDITMVEIDSSVIELSRKFLPtLSNGAFDDERLDLKLCDGFKFLQdigas 162
Cdd:PLN02823  98 LLHHPNPKTVFIMGGGEGSTAREVLRHKTVEKVVMCDIDQEVVDFCRKHLT-VNREAFCDKRLELIINDARAELE----- 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175   163 DVHKKFDVIITDSSDP--EGPAEAFF-QERYFELLKDALNPNGVVIMQS-SENFWLNLKYLHDLKNTAKKVFPnteYC-- 236
Cdd:PLN02823 172 KRDEKFDVIIGDLADPveGGPCYQLYtKSFYERIVKPKLNPGGIFVTQAgPAGILTHKEVFSSIYNTLRQVFK---YVvp 248

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 6323175   237 YTM-VPTYTSgQLGLIVCSNNANIPLNIPQ--RKISEQEQGKLKYYNPQIHSSAFVLP 291
Cdd:PLN02823 249 YTAhVPSFAD-TWGWVMASDHPFADLSAEEldSRIKERIDGELKYLDGETFSSAFALN 305
COG4262 COG4262
Predicted spermidine synthase with an N-terminal membrane domain [General function prediction ...
 33-209 6.74e-47

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


Pssm-ID: 443404 [Multi-domain]  Cd Length: 426  Bit Score: 162.73  E-value: 6.74e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175   33 DSILYEARSEFQDILIFRNKVYgTVLVLDGIVQCTEFDEFAYQEMITHIAMFAHSNPKRVLIIGGGDGGVLREVAKHSCV 112
Cdd:COG4262 232 DPVVYSEQTPYQRIVVTRDKDD-RRLYLNGNLQFSSLDEYRYHEALVHPPMAAHPRPRRVLVLGGGDGLAAREVLKYPDV 310

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175  113 EDITMVEIDSSVIELSRK--FLPTLSNGAFDDERLDLKLCDGFKFLQDIGasdvhKKFDVIITDSSDPEGPAEA-FFQER 189
Cdd:COG4262 311 ESVTLVDLDPEVTDLAKTnpFLRELNGGALNDPRVTVVNADAFQFLRETD-----EKYDVIIVDLPDPSNFSLGkLYSVE 385

                       170       180
                ....*....|....*....|
gi 6323175  190 YFELLKDALNPNGVVIMQSS 209
Cdd:COG4262 386 FYRLVRRHLAPGGVLVVQAT 405
PRK03612 PRK03612
polyamine aminopropyltransferase;
33-291 1.79e-36

polyamine aminopropyltransferase;


Pssm-ID: 235139 [Multi-domain]  Cd Length: 521  Bit Score: 136.51  E-value: 1.79e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175    33 DSILYEARSEFQDILIFRNKVYGTV---LVLDGIVQCTEFDEFAYQEMITHIAMFAHSNPKRVLIIGGGDGGVLREVAKH 109
Cdd:PRK03612 239 DPVVYAEQTPYQRIVVTRRGNGRGPdlrLYLNGRLQFSSRDEYRYHEALVHPAMAASARPRRVLVLGGGDGLALREVLKY 318

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175   110 SCVEDITMVEIDSSVIELSRKF--LPTLSNGAFDDERLDLKLCDGFKFLQDIGAsdvhkKFDVIITDSSDPEGPAEAFFQ 187
Cdd:PRK03612 319 PDVEQVTLVDLDPAMTELARTSpaLRALNGGALDDPRVTVVNDDAFNWLRKLAE-----KFDVIIVDLPDPSNPALGKLY 393

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175   188 ERYF-ELLKDALNPNGVVIMQSS------ENFWlnlkylhDLKNTAKKV-FPNTEYcYTMVPTYtsGQLGLIVCSNNANI 259
Cdd:PRK03612 394 SVEFyRLLKRRLAPDGLLVVQSTspyfapKAFW-------SIEATLEAAgLATTPY-HVNVPSF--GEWGFVLAGAGARP 463

                        250       260       270
                 ....*....|....*....|....*....|..
gi 6323175   260 PLNIPqrkisEQEQGKLKYYNPQIHSSAFVLP 291
Cdd:PRK03612 464 PLAVP-----TELPVPLRFLDPALLAAAFVFP 490
speE PRK01581
polyamine aminopropyltransferase;
34-265 3.71e-28

polyamine aminopropyltransferase;


Pssm-ID: 234961 [Multi-domain]  Cd Length: 374  Bit Score: 111.60  E-value: 3.71e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175    34 SILYEARSEFQDILIFrnKVYGTVLVLDGIVQCTEFDEFAYQEMITHIAMFAHSNPKRVLIIGGGDGGVLREVAKHSCVE 113
Cdd:PRK01581  98 TNLFAEKSNYQNINLL--QVSDIRLYLDKQLQFSSVDEQIYHEALVHPIMSKVIDPKRVLILGGGDGLALREVLKYETVL 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175   114 DITMVEIDSSVIELSRKF--LPTLSNGAFDDERLDLKLCDGFKFLQDIGASdvhkkFDVIITDSSDPEGPA-EAFFQERY 190
Cdd:PRK01581 176 HVDLVDLDGSMINMARNVpeLVSLNKSAFFDNRVNVHVCDAKEFLSSPSSL-----YDVIIIDFPDPATELlSTLYTSEL 250

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175   191 FELLKDALNPNGVVIMQSSEN------FWlnlkylhDLKNTAKKVFPNTEYCYTMVPTYTSgQLGLIVCSNNANIPLNIP 264
Cdd:PRK01581 251 FARIATFLTEDGAFVCQSNSPadaplvYW-------SIGNTIEHAGLTVKSYHTIVPSFGT-DWGFHIAANSAYVLDQIE 322


                 .
gi 6323175   265 Q 265
Cdd:PRK01581 323 Q 323
Spermine_synt_N pfam17284
Spermidine synthase tetramerization domain; This domain represents the N-terminal ...
 13-68 1.23e-21

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: 85.79  E-value: 1.23e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 6323175     13 GWFREINDksfPGQAFTMTVDSILYEARSEFQDILIFRNKVYGTVLVLDGIVQCTE 68
Cdd:pfam17284   1 GWFTEIHD---LGQALEYKVEKVLYDEKSEYQDIEIFESKTFGNVLVLDGVVQLTE 53
PRK04457 PRK04457
polyamine aminopropyltransferase;
71-213 1.96e-12

polyamine aminopropyltransferase;


Pssm-ID: 179854 [Multi-domain]  Cd Length: 262  Bit Score: 65.83  E-value: 1.96e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175    71 EFAYQEMITHIAMFaHSNPKRVLIIGGGDGGVLREVAKHSCVEDITMVEIDSSVIELSRK--FLPtlsngaFDDERLDLK 148
Cdd:PRK04457  50 ELAYTRAMMGFLLF-NPRPQHILQIGLGGGSLAKFIYTYLPDTRQTAVEINPQVIAVARNhfELP------ENGERFEVI 122

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6323175   149 LCDGFKFLQDIGASdvhkkFDVIITDSSDPEGPAEAFFQERYFELLKDALNPNGVVIMqsseNFW 213
Cdd:PRK04457 123 EADGAEYIAVHRHS-----TDVILVDGFDGEGIIDALCTQPFFDDCRNALSSDGIFVV----NLW 178
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 91-207 5.89e-12

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: 61.29  E-value: 5.89e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175   91 RVLIIGGGDGGVLREVAKHSCVEdITMVEIDSSVIELSRKFlptlsNGAFDDERLDLKLCDGFKFLQDIGasdvhKKFDV 170
Cdd:cd02440   1 RVLDLGCGTGALALALASGPGAR-VTGVDISPVALELARKA-----AAALLADNVEVLKGDAEELPPEAD-----ESFDV 69

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 6323175  171 IItdsSDPEGPAEAFFQERYFELLKDALNPNGVVIMQ 207
Cdd:cd02440  70 II---SDPPLHHLVEDLARFLEEARRLLKPGGVLVLT 103
speE PRK00536
spermidine synthase; Provisional
 31-300 2.44e-07

spermidine synthase; Provisional


Pssm-ID: 134311 [Multi-domain]  Cd Length: 262  Bit Score: 51.01  E-value: 2.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175    31 TVDSILYEARSEFQDILIFRNKVYGTVLVLDGIVQCTEFdEFAYQEMITHIAMFAHSNPKRVLIIGGGDGGVLREVAKHS 110
Cdd:PRK00536  16 TIEAKLLDVRSEHNILEIFKSKDFGEIAMLNKQLLFKNF-LHIESELLAHMGGCTKKELKEVLIVDGFDLELAHQLFKYD 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175   111 CveDITMVEIDSSVIELSRKFLP----TLSNGAFD--DERLDLKLcdgfkflqdigasdvhKKFDVIITDSsdpegpaea 184
Cdd:PRK00536  95 T--HVDFVQADEKILDSFISFFPhfheVKNNKNFThaKQLLDLDI----------------KKYDLIICLQ--------- 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175   185 FFQERYFELLKDALNPNGVVIMQSSENFWLNLKYLHDLKNTA---KKVFPnteycyTMVPTYTSGQLGLIVCSNNANIPL 261
Cdd:PRK00536 148 EPDIHKIDGLKRMLKEDGVFISVAKHPLLEHVSMQNALKNMGdffSIAMP------FVAPLRILSNKGYIYASFKTHPLK 221

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 6323175   262 NIPQRKISEQEQgkLKYYNPQIHSSAFVLPTWADKVINE 300
Cdd:PRK00536 222 DLMLQKIEALKS--VRYYNEDIHRAAFALPKNLQEVFKD 258
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 88-206 9.21e-07

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: 46.93  E-value: 9.21e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175   88 NPKRVLIIGGGDGGVLREVAKHSCveDITMVEIDSSVIELSRKFLPTLsngafddeRLDLKLCDgfkfLQDIGASDvhKK 167
Cdd:COG2227  24 AGGRVLDVGCGTGRLALALARRGA--DVTGVDISPEALEIARERAAEL--------NVDFVQGD----LEDLPLED--GS 87

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 6323175  168 FDVIITDSS-----DPegpaEAFFQEryfelLKDALNPNGVVIM 206
Cdd:COG2227  88 FDLVICSEVlehlpDP----AALLRE-----LARLLKPGGLLLL 122
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
89-207 7.43e-06

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 43.66  E-value: 7.43e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175   89 PKRVLIIGGGDGGVLREVAKHSCVEDITMVEIDSSVIELSRKFLPTLSngafdderldlklcdgfkFLQ-DIGASDVHKK 167
Cdd:COG4106   2 PRRVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARARLPNVR------------------FVVaDLRDLDPPEP 63

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 6323175  168 FDVIITdssdpegpAEAFF----QERYFELLKDALNPNGVVIMQ 207
Cdd:COG4106  64 FDLVVS--------NAALHwlpdHAALLARLAAALAPGGVLAVQ 99
MFS_SpdSyn NF037959
fused MFS/spermidine synthase; Proteins of this family are fusion of a N-terminal MFS (Major ...
 57-234 1.57e-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: 45.99  E-value: 1.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175    57 VLVLDGIVQCTEfDEFAYQEMIT-HIAMF-------AHSNPKRVLIIGGGDGGVLREVAKHSCVEDITMVEIDSSVIELS 128
Cdd:NF037959 237 LMVLDHLAHGIN-ARDDPTVLFTpYAAMLdelarlrMGRADFSAFFIGGGAYTLPRAWAARRPAGRITVAEIDPAVTRVA 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175   129 RKFLptlsngAFDDERLDLKLCDGFKFLQDIGASdvhkKFDVIITDS-SDPEGPAEAFFQErYFELLKDALNPNGVVIMQ 207
Cdd:NF037959 316 AEDF------WFDPASATVLHEDARRALRRRPEE----RFDVIVGDAfTDIAVPAHLVTRE-FFELVRARLTPDGVYLMN 384

                        170       180
                 ....*....|....*....|....*..
gi 6323175   208 SSENFwLNLKYLHDLKNTAKKVFPNTE 234
Cdd:NF037959 385 VIDHA-DRLRALAALVATLREVFPVVE 410
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 70-209 1.20e-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: 1.20e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175   70 DEFAYQEMITHIAMFAHSNPKRVLIIGGGDGGVLREVAKHSCvEDITMVEIDSSVIELSRKFLPtlsngAFDDERLDLKL 149
Cdd:COG0500   8 DELLPGLAALLALLERLPKGGRVLDLGCGTGRNLLALAARFG-GRVIGIDLSPEAIALARARAA-----KAGLGNVEFLV 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6323175  150 CDGFKFLQDIGAsdvhkKFDVIITDSS----DPEGpaeaffQERYFELLKDALNPNGVVIMQSS 209
Cdd:COG0500  82 ADLAELDPLPAE-----SFDLVVAFGVlhhlPPEE------REALLRELARALKPGGVLLLSAS 134
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 71-208 2.67e-04

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 40.68  E-value: 2.67e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175   71 EFAYQEMITHIAMFAHSNP-KRVLIIGGGDGGVLREVAKHSCVeDITMVEIDSSVIELSRKFLptlsNGAFDDERLDLKL 149
Cdd:COG2230  33 EEAQEAKLDLILRKLGLKPgMRVLDIGCGWGGLALYLARRYGV-RVTGVTLSPEQLEYARERA----AEAGLADRVEVRL 107

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6323175  150 CDgfkfLQDIGASDvhkKFDVIITdssdpEGPAEAF---FQERYFELLKDALNPNGVVIMQS 208
Cdd:COG2230 108 AD----YRDLPADG---QFDAIVS-----IGMFEHVgpeNYPAYFAKVARLLKPGGRLLLHT 157
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 76-234 3.68e-04

16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA G1207 methylase RsmC is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 442062 [Multi-domain]  Cd Length: 191  Bit Score: 40.56  E-value: 3.68e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175   76 EMITHIAMFAHS----------------NPKRVLIIGGGDGGVLREVAKHSCVEDITMVEIDSSVIELSRKflpTLsnga 139
Cdd:COG2813  21 TFVTLPGVFSRDrldigtrlllehlpepLGGRVLDLGCGYGVIGLALAKRNPEARVTLVDVNARAVELARA---NA---- 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175  140 fddERLDLklcDGFKFLQDIGASDV-HKKFDVIIT-------DSSDPEgPAEAFFQEryfelLKDALNPNGVvimqssen 211
Cdd:COG2813  94 ---AANGL---ENVEVLWSDGLSGVpDGSFDLILSnppfhagRAVDKE-VAHALIAD-----AARHLRPGGE-------- 153

                       170       180
                ....*....|....*....|....*..
gi 6323175  212 FWL----NLKYLHDLkntaKKVFPNTE 234
Cdd:COG2813 154 LWLvanrHLPYERKL----EELFGNVE 176
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 93-204 4.52e-04

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 38.89  E-value: 4.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175     93 LIIGGGDGGVLREVAKHSCVEDITMVEIDSSVIELSRKFLPTLSNGAFDdeRLDLKLCDGFKFLQdigasdvhKKFDVII 172
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERLAALGLLNAV--RVELFQLDLGELDP--------GSFDVVV 70

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 6323175    173 tdssdpegpaeAFF-------QERYFELLKDALNPNGVV 204
Cdd:pfam08242  71 -----------ASNvlhhladPRAVLRNIRRLLKPGGVL 98
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 81-205 1.10e-03

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: 39.01  E-value: 1.10e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175   81 IAMFAH-SNPKRVLIIGGGdGGV--------LREVAKhscvedITMVEIDSSVIELSRKFLptlsNGAFDDERLDLKLCD 151
Cdd:COG4122   8 LYLLARlLGAKRILEIGTG-TGYstlwlaraLPDDGR------LTTIEIDPERAAIARENF----ARAGLADRIRLILGD 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 6323175  152 GFKFLQDIgasdVHKKFDVIITDSsDPEGpaeaffQERYFELLKDALNPNGVVI 205
Cdd:COG4122  77 ALEVLPRL----ADGPFDLVFIDA-DKSN------YPDYLELALPLLRPGGLIV 119
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 69-206 1.50e-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: 38.05  E-value: 1.50e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175   69 FDEFA--YQEMITHIAMFAHSNPKRVLIIGGGDGGVLREVAKHSCveDITMVEIDSSVIELSRKFLPTLsngafdDERLD 146
Cdd:COG2226   1 FDRVAarYDGREALLAALGLRPGARVLDLGCGTGRLALALAERGA--RVTGVDISPEMLELARERAAEA------GLNVE 72

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6323175  147 LKLCDGfkflQDIGASDvhKKFDVIIT-----DSSDPegpaEAFFQEryfelLKDALNPNGVVIM 206
Cdd:COG2226  73 FVVGDA----EDLPFPD--GSFDLVISsfvlhHLPDP----ERALAE-----IARVLKPGGRLVV 122
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 69-221 1.99e-03

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 38.18  E-value: 1.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175     69 FDEFAYQEM--ITHIAMFAHSNPKRVLIIGGGDGGVLREVAKHSCveDITMVEIDSSVIELSRKFLPTLSngafDDERLD 146
Cdd:pfam13489   1 YAHQRERLLadLLLRLLPKLPSPGRVLDFGCGTGIFLRLLRAQGF--SVTGVDPSPIAIERALLNVRFDQ----FDEQEA 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6323175    147 LKLCDGFKFlqdIGASDV--HKKfdviitdssDPegpaeaffqERYFELLKDALNPNGVVIMQSSENFWLNLKYLHD 221
Cdd:pfam13489  75 AVPAGKFDV---IVAREVleHVP---------DP---------PALLRQIAALLKPGGLLLLSTPLASDEADRLLLE 130
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
81-222 9.81e-03

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 36.51  E-value: 9.81e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175   81 IAMFAHSNPKRVLIIGGGDGGVLREVAKHscVEDITMVEIDSSVIELSRKflptlsNGAFDdeRLdlklcdgfkFLQDIG 160
Cdd:COG4976  39 LARLPPGPFGRVLDLGCGTGLLGEALRPR--GYRLTGVDLSEEMLAKARE------KGVYD--RL---------LVADLA 99

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323175  161 A-SDVHKKFDVIItdSSD--PEGPAeaffQERYFELLKDALNPNGVVI--MQSSEN---FWLNLKYLHDL 222
Cdd:COG4976 100 DlAEPDGRFDLIV--AADvlTYLGD----LAAVFAGVARALKPGGLFIfsVEDADGsgrYAHSLDYVRDL 163
 
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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