|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00811 |
PRK00811 |
polyamine aminopropyltransferase; |
139-416 |
6.24e-107 |
|
polyamine aminopropyltransferase;
Pssm-ID: 234843 [Multi-domain] Cd Length: 283 Bit Score: 317.48 E-value: 6.24e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 139 WALEALTPHARFGWRAMRR-ETVQTPHQELELLHTPQFGKVLRLDGRFMTSEGEEFFYHEALVHPAALAHPAPRKALILG 217
Cdd:PRK00811 5 WFTETLTDNYGQSFRVKKVlYEEKSPFQRIEIFETPEFGRLLALDGCVMTTERDEFIYHEMMTHVPLFAHPNPKRVLIIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 218 GGDGGAAEELLKHPSMEQVVVAELDEAVVQAARTHLQQVHRGVFDDPRLQLRIGDGMAMVEHTEERFDLALMDLTDPDTP 297
Cdd:PRK00811 85 GGDGGTLREVLKHPSVEKITLVEIDERVVEVCRKYLPEIAGGAYDDPRVELVIGDGIKFVAETENSFDVIIVDSTDPVGP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 298 ASALYSDQALARMKRVLAPGGALVLHLGSPVFHGEQVARLVASLRERFAIVRCYGLYIPLY-GAYWGLAVASDTLDAAAL 376
Cdd:PRK00811 165 AEGLFTKEFYENCKRALKEDGIFVAQSGSPFYQADEIKDMHRKLKEVFPIVRPYQAAIPTYpSGLWSFTFASKNDDLKFL 244
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1108555412 377 PPAQLRQRLAERRLpDLRYYNAEVHPALFALPNYYRDLVQ 416
Cdd:PRK00811 245 PLDVIEARFAERGI-KTRYYNPELHKAAFALPQFVKDALK 283
|
|
| SpeE |
COG0421 |
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism]; |
176-367 |
3.88e-63 |
|
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
Pssm-ID: 440190 [Multi-domain] Cd Length: 195 Bit Score: 201.98 E-value: 3.88e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 176 GKVLRLDGRFMTS-EGEEFFYHEALVHPAALAHPAPRKALILGGGDGGAAEELLKHPSMEQVVVAELDEAVVQAARTHLQ 254
Cdd:COG0421 3 GRVLVLDGVVQSTmELDEFEYHEMMAHVPLLFHPNPKRVLIIGGGDGGLARELLKHPPVERVDVVEIDPEVVELAREYFP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 255 QVhRGVFDDPRLQLRIGDGMAMVEHTEERFDLALMDLTDPDTPASALYSDQALARMKRVLAPGGALVLHLGSPVFHGEQV 334
Cdd:COG0421 83 LL-APAFDDPRLRVVIGDGRAFLREAEESYDVIIVDLTDPVGPAEGLFTREFYEDCRRALKPGGVLVVNLGSPFYGLDLL 161
|
170 180 190
....*....|....*....|....*....|...
gi 1108555412 335 ARLVASLRERFAIVRCYGLYIPLYGAYWGLAVA 367
Cdd:COG0421 162 RRVLATLREVFPHVVLYAAPVPTYGGGNVFLLA 194
|
|
| speE |
TIGR00417 |
spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine ... |
161-410 |
2.62e-58 |
|
spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine + S-adenosylmethioninamine = spermidine + 5'-methylthioadenosine) and is involved in polyamine biosynthesis and in the biosynthesis of spermidine from arganine. The region between residues 77 and 120 of the seed alignment is thought to be involved in binding to decarboxylated SAM. [Central intermediary metabolism, Polyamine biosynthesis]
Pssm-ID: 188048 [Multi-domain] Cd Length: 271 Bit Score: 192.26 E-value: 2.62e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 161 QTPHQELELLHTPQFGKVLRLDGRFMTSEGEEFFYHEALVHPAALAHPAPRKALILGGGDGGAAEELLKHPSMEQVVVAE 240
Cdd:TIGR00417 24 KSEFQDLEIFETEAFGNVLVLDGVVQTTERDEFIYHEMITHVPLFTHPNPKHVLVIGGGDGGVLREVLKHKSVESATLVD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 241 LDEAVVQAARTHLQQVHrGVFDDPRLQLRIGDGMAMVEHTEERFDLALMDLTDPDTPASALYSDQALARMKRVLAPGGAL 320
Cdd:TIGR00417 104 IDEKVIELSRKYLPNLA-GSYDDPRVKLVIDDGFKFLADTENTFDVIIVDSTDPVGPAETLFTKEFYELLKKALNPDGIF 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 321 VLHLGSPVFHGEQVARLVASLRERFAIVRCYGLYIPLY-GAYWGLAVASDTldaaALPPAQLRQRLAERRLPDL--RYYN 397
Cdd:TIGR00417 183 VAQSESPWLQLELIIDLKRKLKEAFPITEYYTAAIPTYpSGLWTFTIASKN----KYRPLEVEIRRIKFEAEDGktKYYN 258
|
250
....*....|...
gi 1108555412 398 AEVHPALFALPNY 410
Cdd:TIGR00417 259 PDIHKAAFVLPKW 271
|
|
| SpeD |
COG1586 |
S-adenosylmethionine decarboxylase [Amino acid transport and metabolism]; |
1-126 |
7.04e-37 |
|
S-adenosylmethionine decarboxylase [Amino acid transport and metabolism];
Pssm-ID: 441194 Cd Length: 118 Bit Score: 130.71 E-value: 7.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 1 MHGLHLTADLYQCqgDARHMLDADAIAALCRAQTAQAGLTLVEDRWVKFPdyqgqPGGVTGTVLLAESHLAIHTWPETGC 80
Cdd:COG1586 2 FLGKHLIADLYGC--DPELLNDAERLEEILVEAAEAAGATVLGVAFHKFE-----PQGVSGVVLLAESHISIHTWPEYGY 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1108555412 81 VTVDVYVCNFSADnsgkARALMEGVIAAYAPGRVVRQQLMRGDIGP 126
Cdd:COG1586 75 AAVDVFTCGDDID----PEKALEYLKEAFGADKVEVTELKRGFTRD 116
|
|
| Spermine_synth |
pfam01564 |
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ... |
192-369 |
1.01e-36 |
|
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family includes spermidine synthase that catalyzes the fifth (last) step in the biosynthesis of spermidine from arginine, and spermine synthase.
Pssm-ID: 396237 [Multi-domain] Cd Length: 183 Bit Score: 132.44 E-value: 1.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 192 EFFYHEALVHPAALAHPAPRKALILGGGDGGAAEELLKHPSMEQVVVAELDEAVVQAARTHLQQVHrGVFDDPRLQLRIG 271
Cdd:pfam01564 1 EFIYHEMIAHVPLCSHPNPKKVLIIGGGDGGVLREVVKHPSVEKITLVDIDEKVIDFSKKFLPSLA-IGFQDPRVKVVIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 272 DGMAMVEHTEERFDLALMDLTDPDTPASALYSDQALARMKRVLAPGGALVLHLGSPVFHGEQVARLVASLRERFAIVRCY 351
Cdd:pfam01564 80 DGFKFLKDYLNTFDVIIVDSTDPVGPAENLFSKPFFDLLKKALKEDGVFITQAESPWLHLELIINILKNGKQVFPVVMPY 159
|
170
....*....|....*....
gi 1108555412 352 GLYIPLY-GAYWGLAVASD 369
Cdd:pfam01564 160 VATIPTYpSGGWGFTVCSK 178
|
|
| AdoMet_dc |
pfam02675 |
S-adenosylmethionine decarboxylase; This family contains several S-adenosylmethionine ... |
5-122 |
1.33e-30 |
|
S-adenosylmethionine decarboxylase; This family contains several S-adenosylmethionine decarboxylase proteins from bacterial and archaebacterial species. S-adenosylmethionine decarboxylase (AdoMetDC), a key enzyme in the biosynthesis of spermidine and spermine, is first synthesized as a proenzyme, which is cleaved post translationally to form alpha and beta subunits. The alpha subunit contains a covalently bound pyruvoyl group derived from serine that is essential for activity.
Pssm-ID: 460648 Cd Length: 107 Bit Score: 113.76 E-value: 1.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 5 HLTADLYQCQGDArhMLDADAIAALCRAQTAQAGLTLVEDRWVKFPdyqgqPGGVTGTVLLAESHLAIHTWPETGCVTVD 84
Cdd:pfam02675 1 HLIVDLYGCDPEL--LDDAELIEQALREAAEAAGATVVEVVFHKFE-----PQGVSGVVLLAESHISIHTWPEYGYAAVD 73
|
90 100 110
....*....|....*....|....*....|....*...
gi 1108555412 85 VYVCNFSADnsgkARALMEGVIAAYAPGRVVRQQLMRG 122
Cdd:pfam02675 74 VFTCGDHVD----PEKAFEYLKEALGAKRVSVRELDRG 107
|
|
| SAM_DCase_Bsu |
TIGR03330 |
S-adenosylmethionine decarboxylase proenzyme, Bacillus form; Members of this protein family ... |
3-122 |
1.62e-21 |
|
S-adenosylmethionine decarboxylase proenzyme, Bacillus form; Members of this protein family are the single chain precursor of the two chains of the mature S-adenosylmethionine decarboxylase as found in Methanocaldococcus jannaschii, Bacillus subtilis, and a wide range of other species. It differs substantially in architecture from the form as found in Escherichia coli, and lacks any extended homology to the eukaryotic form (TIGR00535). [Central intermediary metabolism, Polyamine biosynthesis]
Pssm-ID: 274523 Cd Length: 112 Bit Score: 89.20 E-value: 1.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 3 GLHLTADLYQCqgDARHMLDADAI-AALCRAqTAQAGLTLVEDRWVKFPdyqgqPGGVTGTVLLAESHLAIHTWPETGCV 81
Cdd:TIGR03330 4 GRHLIVDLYGC--DPEKLDDVEFIeEILLEA-AKVAGATLVASHFHKFS-----PGGVSGVVLLAESHISIHTWPEYGYA 75
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1108555412 82 TVDVYVCnfsADNSGKARALmEGVIAAYAPGRVVRQQLMRG 122
Cdd:TIGR03330 76 AVDVFTC---GDHSDPEKAF-EYLVEALKPKRVEVRELDRG 112
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
224-324 |
2.46e-04 |
|
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).
Pssm-ID: 100107 [Multi-domain] Cd Length: 107 Bit Score: 40.11 E-value: 2.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 224 AEELLKHPSmEQVVVAELDEAVVQAARTHLQQVHRgvfddPRLQLRIGDGMAMVEHTEERFDLALMDLTDPDTPASAlys 303
Cdd:cd02440 13 ALALASGPG-ARVTGVDISPVALELARKAAAALLA-----DNVEVLKGDAEELPPEADESFDVIISDPPLHHLVEDL--- 83
|
90 100
....*....|....*....|.
gi 1108555412 304 DQALARMKRVLAPGGALVLHL 324
Cdd:cd02440 84 ARFLEEARRLLKPGGVLVLTL 104
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00811 |
PRK00811 |
polyamine aminopropyltransferase; |
139-416 |
6.24e-107 |
|
polyamine aminopropyltransferase;
Pssm-ID: 234843 [Multi-domain] Cd Length: 283 Bit Score: 317.48 E-value: 6.24e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 139 WALEALTPHARFGWRAMRR-ETVQTPHQELELLHTPQFGKVLRLDGRFMTSEGEEFFYHEALVHPAALAHPAPRKALILG 217
Cdd:PRK00811 5 WFTETLTDNYGQSFRVKKVlYEEKSPFQRIEIFETPEFGRLLALDGCVMTTERDEFIYHEMMTHVPLFAHPNPKRVLIIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 218 GGDGGAAEELLKHPSMEQVVVAELDEAVVQAARTHLQQVHRGVFDDPRLQLRIGDGMAMVEHTEERFDLALMDLTDPDTP 297
Cdd:PRK00811 85 GGDGGTLREVLKHPSVEKITLVEIDERVVEVCRKYLPEIAGGAYDDPRVELVIGDGIKFVAETENSFDVIIVDSTDPVGP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 298 ASALYSDQALARMKRVLAPGGALVLHLGSPVFHGEQVARLVASLRERFAIVRCYGLYIPLY-GAYWGLAVASDTLDAAAL 376
Cdd:PRK00811 165 AEGLFTKEFYENCKRALKEDGIFVAQSGSPFYQADEIKDMHRKLKEVFPIVRPYQAAIPTYpSGLWSFTFASKNDDLKFL 244
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1108555412 377 PPAQLRQRLAERRLpDLRYYNAEVHPALFALPNYYRDLVQ 416
Cdd:PRK00811 245 PLDVIEARFAERGI-KTRYYNPELHKAAFALPQFVKDALK 283
|
|
| SpeE |
COG0421 |
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism]; |
176-367 |
3.88e-63 |
|
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
Pssm-ID: 440190 [Multi-domain] Cd Length: 195 Bit Score: 201.98 E-value: 3.88e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 176 GKVLRLDGRFMTS-EGEEFFYHEALVHPAALAHPAPRKALILGGGDGGAAEELLKHPSMEQVVVAELDEAVVQAARTHLQ 254
Cdd:COG0421 3 GRVLVLDGVVQSTmELDEFEYHEMMAHVPLLFHPNPKRVLIIGGGDGGLARELLKHPPVERVDVVEIDPEVVELAREYFP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 255 QVhRGVFDDPRLQLRIGDGMAMVEHTEERFDLALMDLTDPDTPASALYSDQALARMKRVLAPGGALVLHLGSPVFHGEQV 334
Cdd:COG0421 83 LL-APAFDDPRLRVVIGDGRAFLREAEESYDVIIVDLTDPVGPAEGLFTREFYEDCRRALKPGGVLVVNLGSPFYGLDLL 161
|
170 180 190
....*....|....*....|....*....|...
gi 1108555412 335 ARLVASLRERFAIVRCYGLYIPLYGAYWGLAVA 367
Cdd:COG0421 162 RRVLATLREVFPHVVLYAAPVPTYGGGNVFLLA 194
|
|
| speE |
TIGR00417 |
spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine ... |
161-410 |
2.62e-58 |
|
spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine + S-adenosylmethioninamine = spermidine + 5'-methylthioadenosine) and is involved in polyamine biosynthesis and in the biosynthesis of spermidine from arganine. The region between residues 77 and 120 of the seed alignment is thought to be involved in binding to decarboxylated SAM. [Central intermediary metabolism, Polyamine biosynthesis]
Pssm-ID: 188048 [Multi-domain] Cd Length: 271 Bit Score: 192.26 E-value: 2.62e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 161 QTPHQELELLHTPQFGKVLRLDGRFMTSEGEEFFYHEALVHPAALAHPAPRKALILGGGDGGAAEELLKHPSMEQVVVAE 240
Cdd:TIGR00417 24 KSEFQDLEIFETEAFGNVLVLDGVVQTTERDEFIYHEMITHVPLFTHPNPKHVLVIGGGDGGVLREVLKHKSVESATLVD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 241 LDEAVVQAARTHLQQVHrGVFDDPRLQLRIGDGMAMVEHTEERFDLALMDLTDPDTPASALYSDQALARMKRVLAPGGAL 320
Cdd:TIGR00417 104 IDEKVIELSRKYLPNLA-GSYDDPRVKLVIDDGFKFLADTENTFDVIIVDSTDPVGPAETLFTKEFYELLKKALNPDGIF 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 321 VLHLGSPVFHGEQVARLVASLRERFAIVRCYGLYIPLY-GAYWGLAVASDTldaaALPPAQLRQRLAERRLPDL--RYYN 397
Cdd:TIGR00417 183 VAQSESPWLQLELIIDLKRKLKEAFPITEYYTAAIPTYpSGLWTFTIASKN----KYRPLEVEIRRIKFEAEDGktKYYN 258
|
250
....*....|...
gi 1108555412 398 AEVHPALFALPNY 410
Cdd:TIGR00417 259 PDIHKAAFVLPKW 271
|
|
| PLN02823 |
PLN02823 |
spermine synthase |
159-412 |
8.16e-57 |
|
spermine synthase
Pssm-ID: 178418 [Multi-domain] Cd Length: 336 Bit Score: 190.28 E-value: 8.16e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 159 TVQTPHQELELLHTPQFGKVLRLDGRFMTSEGEEFFYHEALVHPAALAHPAPRKALILGGGDGGAAEELLKHPSMEQVVV 238
Cdd:PLN02823 53 TGTSEFQDIALVDTKPFGKVLIIDGKMQSAEADEFVYHESLVHPALLHHPNPKTVFIMGGGEGSTAREVLRHKTVEKVVM 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 239 AELDEAVVQAARTHLqQVHRGVFDDPRLQLRIGDGMAMVEHTEERFDLALMDLTDP--DTPASALYSDQALARM-KRVLA 315
Cdd:PLN02823 133 CDIDQEVVDFCRKHL-TVNREAFCDKRLELIINDARAELEKRDEKFDVIIGDLADPveGGPCYQLYTKSFYERIvKPKLN 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 316 PGGALVLHLGSPVF--HGEQVARLVASLRERFAIVRCYGLYIPLYGAYWGLAVASDTlDAAALPPAQLRQRLAERRLPDL 393
Cdd:PLN02823 212 PGGIFVTQAGPAGIltHKEVFSSIYNTLRQVFKYVVPYTAHVPSFADTWGWVMASDH-PFADLSAEELDSRIKERIDGEL 290
|
250
....*....|....*....
gi 1108555412 394 RYYNAEVHPALFALPNYYR 412
Cdd:PLN02823 291 KYLDGETFSSAFALNKTVR 309
|
|
| PRK03612 |
PRK03612 |
polyamine aminopropyltransferase; |
161-417 |
3.43e-43 |
|
polyamine aminopropyltransferase;
Pssm-ID: 235139 [Multi-domain] Cd Length: 521 Bit Score: 158.46 E-value: 3.43e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 161 QTPHQELELLHTPQ-FGKVLRL--DGRFMTSEGEEFFYHEALVHPAALAHPAPRKALILGGGDGGAAEELLKHPSMEQVV 237
Cdd:PRK03612 246 QTPYQRIVVTRRGNgRGPDLRLylNGRLQFSSRDEYRYHEALVHPAMAASARPRRVLVLGGGDGLALREVLKYPDVEQVT 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 238 VAELDEAVVQAARTH--LQQVHRGVFDDPRLQLRIGDGMAMVEHTEERFDLALMDLTDPDTPASA-LYSDQALARMKRVL 314
Cdd:PRK03612 326 LVDLDPAMTELARTSpaLRALNGGALDDPRVTVVNDDAFNWLRKLAEKFDVIIVDLPDPSNPALGkLYSVEFYRLLKRRL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 315 APGGALVLHLGSPVFHGEQVARLVASLRERFAIVRCYGLYIPLYGAyWGLAVASDTLDAAALPPAQLRqrlaerrlPDLR 394
Cdd:PRK03612 406 APDGLLVVQSTSPYFAPKAFWSIEATLEAAGLATTPYHVNVPSFGE-WGFVLAGAGARPPLAVPTELP--------VPLR 476
|
250 260
....*....|....*....|....
gi 1108555412 395 YYNAEVHPALFALP-NYYRDLVQP 417
Cdd:PRK03612 477 FLDPALLAAAFVFPkDMRRREVEP 500
|
|
| COG4262 |
COG4262 |
Predicted spermidine synthase with an N-terminal membrane domain [General function prediction ... |
161-343 |
1.22e-39 |
|
Predicted spermidine synthase with an N-terminal membrane domain [General function prediction only];
Pssm-ID: 443404 [Multi-domain] Cd Length: 426 Bit Score: 146.93 E-value: 1.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 161 QTPHQELELLHTPQFgKVLRLDGRFMTSEGEEFFYHEALVHPAALAHPAPRKALILGGGDGGAAEELLKHPSMEQVVVAE 240
Cdd:COG4262 239 QTPYQRIVVTRDKDD-RRLYLNGNLQFSSLDEYRYHEALVHPPMAAHPRPRRVLVLGGGDGLAAREVLKYPDVESVTLVD 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 241 LDEAVVQAARTH--LQQVHRGVFDDPRLQLRIGDGMAMVEHTEERFDLALMDLTDPDTPASA-LYSDQALARMKRVLAPG 317
Cdd:COG4262 318 LDPEVTDLAKTNpfLRELNGGALNDPRVTVVNADAFQFLRETDEKYDVIIVDLPDPSNFSLGkLYSVEFYRLVRRHLAPG 397
|
170 180
....*....|....*....|....*.
gi 1108555412 318 GALVLHLGSPVFHGEQVARLVASLRE 343
Cdd:COG4262 398 GVLVVQATSPYFAPKAFWCIAKTLEA 423
|
|
| SpeD |
COG1586 |
S-adenosylmethionine decarboxylase [Amino acid transport and metabolism]; |
1-126 |
7.04e-37 |
|
S-adenosylmethionine decarboxylase [Amino acid transport and metabolism];
Pssm-ID: 441194 Cd Length: 118 Bit Score: 130.71 E-value: 7.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 1 MHGLHLTADLYQCqgDARHMLDADAIAALCRAQTAQAGLTLVEDRWVKFPdyqgqPGGVTGTVLLAESHLAIHTWPETGC 80
Cdd:COG1586 2 FLGKHLIADLYGC--DPELLNDAERLEEILVEAAEAAGATVLGVAFHKFE-----PQGVSGVVLLAESHISIHTWPEYGY 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1108555412 81 VTVDVYVCNFSADnsgkARALMEGVIAAYAPGRVVRQQLMRGDIGP 126
Cdd:COG1586 75 AAVDVFTCGDDID----PEKALEYLKEAFGADKVEVTELKRGFTRD 116
|
|
| Spermine_synth |
pfam01564 |
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ... |
192-369 |
1.01e-36 |
|
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family includes spermidine synthase that catalyzes the fifth (last) step in the biosynthesis of spermidine from arginine, and spermine synthase.
Pssm-ID: 396237 [Multi-domain] Cd Length: 183 Bit Score: 132.44 E-value: 1.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 192 EFFYHEALVHPAALAHPAPRKALILGGGDGGAAEELLKHPSMEQVVVAELDEAVVQAARTHLQQVHrGVFDDPRLQLRIG 271
Cdd:pfam01564 1 EFIYHEMIAHVPLCSHPNPKKVLIIGGGDGGVLREVVKHPSVEKITLVDIDEKVIDFSKKFLPSLA-IGFQDPRVKVVIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 272 DGMAMVEHTEERFDLALMDLTDPDTPASALYSDQALARMKRVLAPGGALVLHLGSPVFHGEQVARLVASLRERFAIVRCY 351
Cdd:pfam01564 80 DGFKFLKDYLNTFDVIIVDSTDPVGPAENLFSKPFFDLLKKALKEDGVFITQAESPWLHLELIINILKNGKQVFPVVMPY 159
|
170
....*....|....*....
gi 1108555412 352 GLYIPLY-GAYWGLAVASD 369
Cdd:pfam01564 160 VATIPTYpSGGWGFTVCSK 178
|
|
| PLN02366 |
PLN02366 |
spermidine synthase |
162-412 |
5.38e-34 |
|
spermidine synthase
Pssm-ID: 215208 [Multi-domain] Cd Length: 308 Bit Score: 128.99 E-value: 5.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 162 TPHQELELLHTPQFGKVLRLDGRFMTSEGEEFFYHEALVHPAALAHPAPRKALILGGGDGGAAEELLKHPSMEQVVVAEL 241
Cdd:PLN02366 44 SDFQDVLVFESATYGKVLVLDGVIQLTERDECAYQEMITHLPLCSIPNPKKVLVVGGGDGGVLREIARHSSVEQIDICEI 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 242 DEAVVQAARTHLQQVHRGvFDDPRLQLRIGDGMAMVEH-TEERFDLALMDLTDPDTPASALYSDQALARMKRVLAPGGAL 320
Cdd:PLN02366 124 DKMVIDVSKKFFPDLAVG-FDDPRVNLHIGDGVEFLKNaPEGTYDAIIVDSSDPVGPAQELFEKPFFESVARALRPGGVV 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 321 VLHLGSPVFHGEQVARLVASLRERFAIVRCYG-LYIPLY-GAYWGLAVAS------DTLDAAALPPAQLRQRLAERrlpD 392
Cdd:PLN02366 203 CTQAESMWLHMDLIEDLIAICRETFKGSVNYAwTTVPTYpSGVIGFVLCSkegpavDFKHPVNPIDKLEGAGKAKR---P 279
|
250 260
....*....|....*....|
gi 1108555412 393 LRYYNAEVHPALFALPNYYR 412
Cdd:PLN02366 280 LKFYNSEVHRAAFCLPSFAK 299
|
|
| AdoMet_dc |
pfam02675 |
S-adenosylmethionine decarboxylase; This family contains several S-adenosylmethionine ... |
5-122 |
1.33e-30 |
|
S-adenosylmethionine decarboxylase; This family contains several S-adenosylmethionine decarboxylase proteins from bacterial and archaebacterial species. S-adenosylmethionine decarboxylase (AdoMetDC), a key enzyme in the biosynthesis of spermidine and spermine, is first synthesized as a proenzyme, which is cleaved post translationally to form alpha and beta subunits. The alpha subunit contains a covalently bound pyruvoyl group derived from serine that is essential for activity.
Pssm-ID: 460648 Cd Length: 107 Bit Score: 113.76 E-value: 1.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 5 HLTADLYQCQGDArhMLDADAIAALCRAQTAQAGLTLVEDRWVKFPdyqgqPGGVTGTVLLAESHLAIHTWPETGCVTVD 84
Cdd:pfam02675 1 HLIVDLYGCDPEL--LDDAELIEQALREAAEAAGATVVEVVFHKFE-----PQGVSGVVLLAESHISIHTWPEYGYAAVD 73
|
90 100 110
....*....|....*....|....*....|....*...
gi 1108555412 85 VYVCNFSADnsgkARALMEGVIAAYAPGRVVRQQLMRG 122
Cdd:pfam02675 74 VFTCGDHVD----PEKAFEYLKEALGAKRVSVRELDRG 107
|
|
| SAM_DCase_Bsu |
TIGR03330 |
S-adenosylmethionine decarboxylase proenzyme, Bacillus form; Members of this protein family ... |
3-122 |
1.62e-21 |
|
S-adenosylmethionine decarboxylase proenzyme, Bacillus form; Members of this protein family are the single chain precursor of the two chains of the mature S-adenosylmethionine decarboxylase as found in Methanocaldococcus jannaschii, Bacillus subtilis, and a wide range of other species. It differs substantially in architecture from the form as found in Escherichia coli, and lacks any extended homology to the eukaryotic form (TIGR00535). [Central intermediary metabolism, Polyamine biosynthesis]
Pssm-ID: 274523 Cd Length: 112 Bit Score: 89.20 E-value: 1.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 3 GLHLTADLYQCqgDARHMLDADAI-AALCRAqTAQAGLTLVEDRWVKFPdyqgqPGGVTGTVLLAESHLAIHTWPETGCV 81
Cdd:TIGR03330 4 GRHLIVDLYGC--DPEKLDDVEFIeEILLEA-AKVAGATLVASHFHKFS-----PGGVSGVVLLAESHISIHTWPEYGYA 75
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1108555412 82 TVDVYVCnfsADNSGKARALmEGVIAAYAPGRVVRQQLMRG 122
Cdd:TIGR03330 76 AVDVFTC---GDHSDPEKAF-EYLVEALKPKRVEVRELDRG 112
|
|
| speE |
PRK01581 |
polyamine aminopropyltransferase; |
179-393 |
3.65e-21 |
|
polyamine aminopropyltransferase;
Pssm-ID: 234961 [Multi-domain] Cd Length: 374 Bit Score: 94.26 E-value: 3.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 179 LRLDGRFMTSEGEEFFYHEALVHPAALAHPAPRKALILGGGDGGAAEELLKHPSMEQVVVAELDEAVVQAART--HLQQV 256
Cdd:PRK01581 120 LYLDKQLQFSSVDEQIYHEALVHPIMSKVIDPKRVLILGGGDGLALREVLKYETVLHVDLVDLDGSMINMARNvpELVSL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 257 HRGVFDDPRLQLRIGDGMAMVEHTEERFDLALMDLTDPDTPA-SALYSDQALARMKRVLAPGGALVLHLGSPVFHGEQVA 335
Cdd:PRK01581 200 NKSAFFDNRVNVHVCDAKEFLSSPSSLYDVIIIDFPDPATELlSTLYTSELFARIATFLTEDGAFVCQSNSPADAPLVYW 279
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1108555412 336 RLVASLRERFAIVRCYGLYIPLYGAYWGLAVASDTLDAAALPPaQLRQRLAERRLPDL 393
Cdd:PRK01581 280 SIGNTIEHAGLTVKSYHTIVPSFGTDWGFHIAANSAYVLDQIE-QLYVVPTPRTLPSL 336
|
|
| speE |
PRK00536 |
spermidine synthase; Provisional |
160-416 |
2.00e-10 |
|
spermidine synthase; Provisional
Pssm-ID: 134311 [Multi-domain] Cd Length: 262 Bit Score: 61.03 E-value: 2.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 160 VQTPHQELELLHTPQFGKVLRLDGRFMTSEgeefFYH---EALVHPAALAHPAPRKALILGGGDGGAAEELLKHPSmeQV 236
Cdd:PRK00536 24 VRSEHNILEIFKSKDFGEIAMLNKQLLFKN----FLHiesELLAHMGGCTKKELKEVLIVDGFDLELAHQLFKYDT--HV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 237 VVAELDEAVVQAARTHLQQVHrGVFDDPRLQlrigdgmamveHTEERFDLalmDLTDPDTP-ASALYSDQALARMKRVLA 315
Cdd:PRK00536 98 DFVQADEKILDSFISFFPHFH-EVKNNKNFT-----------HAKQLLDL---DIKKYDLIiCLQEPDIHKIDGLKRMLK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 316 PGGALVLHLGSPVFHGEQVARLVASLRERFAIVRCYGLYIPLYGAYwGLAVASDTLDaaalPPAQLRQRLAERrLPDLRY 395
Cdd:PRK00536 163 EDGVFISVAKHPLLEHVSMQNALKNMGDFFSIAMPFVAPLRILSNK-GYIYASFKTH----PLKDLMLQKIEA-LKSVRY 236
|
250 260
....*....|....*....|.
gi 1108555412 396 YNAEVHPALFALPNYYRDLVQ 416
Cdd:PRK00536 237 YNEDIHRAAFALPKNLQEVFK 257
|
|
| Spermine_synt_N |
pfam17284 |
Spermidine synthase tetramerization domain; This domain represents the N-terminal ... |
159-189 |
2.93e-06 |
|
Spermidine synthase tetramerization domain; This domain represents the N-terminal tetramerization domain from spermidine synthase.
Pssm-ID: 407397 [Multi-domain] Cd Length: 53 Bit Score: 44.19 E-value: 2.93e-06
10 20 30
....*....|....*....|....*....|.
gi 1108555412 159 TVQTPHQELELLHTPQFGKVLRLDGRFMTSE 189
Cdd:pfam17284 23 DEKSEYQDIEIFESKTFGNVLVLDGVVQLTE 53
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
235-318 |
3.39e-05 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 42.55 E-value: 3.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 235 QVVVAELDEAVVQAARTHLQQvhrgvfDDPRLQLRIGDGMAMvEHTEERFDL-----ALMDLTDPDTPAsalysdqALAR 309
Cdd:pfam13649 22 RVTGVDLSPEMLERARERAAE------AGLNVEFVQGDAEDL-PFPDGSFDLvvssgVLHHLPDPDLEA-------ALRE 87
|
....*....
gi 1108555412 310 MKRVLAPGG 318
Cdd:pfam13649 88 IARVLKPGG 96
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
224-324 |
2.46e-04 |
|
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).
Pssm-ID: 100107 [Multi-domain] Cd Length: 107 Bit Score: 40.11 E-value: 2.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 224 AEELLKHPSmEQVVVAELDEAVVQAARTHLQQVHRgvfddPRLQLRIGDGMAMVEHTEERFDLALMDLTDPDTPASAlys 303
Cdd:cd02440 13 ALALASGPG-ARVTGVDISPVALELARKAAAALLA-----DNVEVLKGDAEELPPEADESFDVIISDPPLHHLVEDL--- 83
|
90 100
....*....|....*....|.
gi 1108555412 304 DQALARMKRVLAPGGALVLHL 324
Cdd:cd02440 84 ARFLEEARRLLKPGGVLVLTL 104
|
|
| Gcd14 |
COG2519 |
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ... |
258-351 |
6.55e-04 |
|
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 N-methylase Trm61 is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 442009 [Multi-domain] Cd Length: 249 Bit Score: 41.30 E-value: 6.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 258 RGVFDDPRLQLRIGDgmaMVEHTEER-FDLALMDLTDPDtpasalysdQALARMKRVLAPGGALVLHLgsPVFhgEQVAR 336
Cdd:COG2519 137 ERFGLPDNVELKLGD---IREGIDEGdVDAVFLDMPDPW---------EALEAVAKALKPGGVLVAYV--PTV--NQVSK 200
|
90
....*....|....*.
gi 1108555412 337 LVASLRER-FAIVRCY 351
Cdd:COG2519 201 LVEALRESgFTDIEAV 216
|
|
| PRK04457 |
PRK04457 |
polyamine aminopropyltransferase; |
231-349 |
1.04e-03 |
|
polyamine aminopropyltransferase;
Pssm-ID: 179854 [Multi-domain] Cd Length: 262 Bit Score: 40.79 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 231 PSMEQVVVaELDEAVVQAARTHLQQVHrgvfDDPRLQLRIGDGMAMVEHTEERFDLALMDLTDPDTPASALYSDQALARM 310
Cdd:PRK04457 89 PDTRQTAV-EINPQVIAVARNHFELPE----NGERFEVIEADGAEYIAVHRHSTDVILVDGFDGEGIIDALCTQPFFDDC 163
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1108555412 311 KRVLAPGGALVLHL--GSPVFHgEQVARLVASLRERFAIVR 349
Cdd:PRK04457 164 RNALSSDGIFVVNLwsRDKRYD-RYLERLESSFEGRVLELP 203
|
|
| Methyltransf_31 |
pfam13847 |
Methyltransferase domain; This family appears to have methyltransferase activity. |
223-348 |
3.18e-03 |
|
Methyltransferase domain; This family appears to have methyltransferase activity.
Pssm-ID: 463998 [Multi-domain] Cd Length: 150 Bit Score: 38.17 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 223 AAEELlkhPSMEQVVVAELDEAVVQAARTHLQQvhRGvFDdpRLQLRIGDGMAMVEH-TEERFDL-----ALMDLTDPDt 296
Cdd:pfam13847 21 LAEEL---GPNAEVVGIDISEEAIEKARENAQK--LG-FD--NVEFEQGDIEELPELlEDDKFDVvisncVLNHIPDPD- 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1108555412 297 pasalysdQALARMKRVLAPGGALVlhLGSPVFHGEQVARLVASLRERFAIV 348
Cdd:pfam13847 92 --------KVLQEILRVLKPGGRLI--ISDPDSLAELPAHVKEDSTYYAGCV 133
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
235-322 |
4.24e-03 |
|
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis
Pssm-ID: 441828 [Multi-domain] Cd Length: 143 Bit Score: 37.67 E-value: 4.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 235 QVVVAELDEAVVQAARTHLQQvhrgvfDDPRLQLRIGDGMAMvEHTEERFDL-----ALMDLTDPDtpasalysdQALAR 309
Cdd:COG2226 46 RVTGVDISPEMLELARERAAE------AGLNVEFVVGDAEDL-PFPDGSFDLvissfVLHHLPDPE---------RALAE 109
|
90
....*....|...
gi 1108555412 310 MKRVLAPGGALVL 322
Cdd:COG2226 110 IARVLKPGGRLVV 122
|
|
| Methyltransf_11 |
pfam08241 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
235-322 |
5.60e-03 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 462406 [Multi-domain] Cd Length: 94 Bit Score: 36.10 E-value: 5.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 235 QVVVAELDEAVVQAARTHLQqvhrgvfdDPRLQLRIGDGMAMvEHTEERFDL-----ALMDLTDPDtpasalysdQALAR 309
Cdd:pfam08241 20 RVTGVDISPEMLELAREKAP--------REGLTFVVGDAEDL-PFPDNSFDLvlsseVLHHVEDPE---------RALRE 81
|
90
....*....|...
gi 1108555412 310 MKRVLAPGGALVL 322
Cdd:pfam08241 82 IARVLKPGGILII 94
|
|
| Tam |
COG4106 |
Trans-aconitate methyltransferase [Energy production and conversion]; |
223-322 |
8.21e-03 |
|
Trans-aconitate methyltransferase [Energy production and conversion];
Pssm-ID: 443282 [Multi-domain] Cd Length: 100 Bit Score: 35.57 E-value: 8.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108555412 223 AAEELLKHPSMEQVVVAELDEAVVQAARTHLqqvhrgvfddPRLQLRIGDgMAMVEhTEERFDL-----ALMDLTDPdtp 297
Cdd:COG4106 15 LTALLAERFPGARVTGVDLSPEMLARARARL----------PNVRFVVAD-LRDLD-PPEPFDLvvsnaALHWLPDH--- 79
|
90 100
....*....|....*....|....*
gi 1108555412 298 asalysDQALARMKRVLAPGGALVL 322
Cdd:COG4106 80 ------AALLARLAAALAPGGVLAV 98
|
|
| |
