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Conserved domains on  [gi|15596884|ref|NP_250378|]
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polyamine aminopropyltransferase [Pseudomonas aeruginosa PAO1]

Protein Classification

spermidine synthase( domain architecture ID 10011535)

spermidine synthase catalyzes the irreversible transfer of a propylamine group from S-adenosylmethioninamine to putrescine to form spermidine

CATH:  2.30.140.10
EC:  2.5.1.16
Gene Symbol:  speE
Gene Ontology:  GO:0004766|GO:0008295
SCOP:  4003319

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
PRK00811 PRK00811
polyamine aminopropyltransferase;
4-281 9.15e-176

polyamine aminopropyltransferase;


:

Pssm-ID: 234843 [Multi-domain]  Cd Length: 283  Bit Score: 486.20  E-value: 9.15e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596884    4 YQETLYQGYGQRFSIDNMLHEVRTEHQHLVIFENARMGRVMALDGVIQTTEADEFIYHEMLTHVPILAHGAARRVLIIGG 83
Cdd:PRK00811   6 FTETLTDNYGQSFRVKKVLYEEKSPFQRIEIFETPEFGRLLALDGCVMTTERDEFIYHEMMTHVPLFAHPNPKRVLIIGG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596884   84 GDGGMLREVAKHKSVERITMVEIDGTVVDMCKEFLPNHSQGAFDDPRLNLVIDDGMRFVATTEERFDVIISDSTDPIGPG 163
Cdd:PRK00811  86 GDGGTLREVLKHPSVEKITLVEIDERVVEVCRKYLPEIAGGAYDDPRVELVIGDGIKFVAETENSFDVIIVDSTDPVGPA 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596884  164 EVLFSENFYQACRRCLNEGGILVTQNGTPFMQLEEVRTTAARTDGLFADWHFYQAAVPTYIGGAMTFAWGSTHEGLRRLP 243
Cdd:PRK00811 166 EGLFTKEFYENCKRALKEDGIFVAQSGSPFYQADEIKDMHRKLKEVFPIVRPYQAAIPTYPSGLWSFTFASKNDDLKFLP 245
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 15596884  244 LETLRQRFRDSGIATRYYNADIHLGAFALPQYVLQAIG 281
Cdd:PRK00811 246 LDVIEARFAERGIKTRYYNPELHKAAFALPQFVKDALK 283
 
Name Accession Description Interval E-value
PRK00811 PRK00811
polyamine aminopropyltransferase;
4-281 9.15e-176

polyamine aminopropyltransferase;


Pssm-ID: 234843 [Multi-domain]  Cd Length: 283  Bit Score: 486.20  E-value: 9.15e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596884    4 YQETLYQGYGQRFSIDNMLHEVRTEHQHLVIFENARMGRVMALDGVIQTTEADEFIYHEMLTHVPILAHGAARRVLIIGG 83
Cdd:PRK00811   6 FTETLTDNYGQSFRVKKVLYEEKSPFQRIEIFETPEFGRLLALDGCVMTTERDEFIYHEMMTHVPLFAHPNPKRVLIIGG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596884   84 GDGGMLREVAKHKSVERITMVEIDGTVVDMCKEFLPNHSQGAFDDPRLNLVIDDGMRFVATTEERFDVIISDSTDPIGPG 163
Cdd:PRK00811  86 GDGGTLREVLKHPSVEKITLVEIDERVVEVCRKYLPEIAGGAYDDPRVELVIGDGIKFVAETENSFDVIIVDSTDPVGPA 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596884  164 EVLFSENFYQACRRCLNEGGILVTQNGTPFMQLEEVRTTAARTDGLFADWHFYQAAVPTYIGGAMTFAWGSTHEGLRRLP 243
Cdd:PRK00811 166 EGLFTKEFYENCKRALKEDGIFVAQSGSPFYQADEIKDMHRKLKEVFPIVRPYQAAIPTYPSGLWSFTFASKNDDLKFLP 245
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 15596884  244 LETLRQRFRDSGIATRYYNADIHLGAFALPQYVLQAIG 281
Cdd:PRK00811 246 LDVIEARFAERGIKTRYYNPELHKAAFALPQFVKDALK 283
speE TIGR00417
spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine ...
4-275 1.70e-130

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: 370.99  E-value: 1.70e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596884     4 YQETLYQGYGQRFSIDNMLHEVRTEHQHLVIFENARMGRVMALDGVIQTTEADEFIYHEMLTHVPILAHGAARRVLIIGG 83
Cdd:TIGR00417   2 FTEYHDKNFGLTMKVDKVLYHEKSEFQDLEIFETEAFGNVLVLDGVVQTTERDEFIYHEMITHVPLFTHPNPKHVLVIGG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596884    84 GDGGMLREVAKHKSVERITMVEIDGTVVDMCKEFLPNHSqGAFDDPRLNLVIDDGMRFVATTEERFDVIISDSTDPIGPG 163
Cdd:TIGR00417  82 GDGGVLREVLKHKSVESATLVDIDEKVIELSRKYLPNLA-GSYDDPRVKLVIDDGFKFLADTENTFDVIIVDSTDPVGPA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596884   164 EVLFSENFYQACRRCLNEGGILVTQNGTPFMQLEEVRTTAARTDGLFADWHFYQAAVPTYIGGAMTFAWGSTHEgLRRLP 243
Cdd:TIGR00417 161 ETLFTKEFYELLKKALNPDGIFVAQSESPWLQLELIIDLKRKLKEAFPITEYYTAAIPTYPSGLWTFTIASKNK-YRPLE 239
                         250       260       270
                  ....*....|....*....|....*....|..
gi 15596884   244 LETLRQRFRDSGIATRYYNADIHLGAFALPQY 275
Cdd:TIGR00417 240 VEIRRIKFEAEDGKTKYYNPDIHKAAFVLPKW 271
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
41-233 6.71e-92

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


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 270.16  E-value: 6.71e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596884  41 GRVMALDGVIQTT-EADEFIYHEMLTHVPILAHGAARRVLIIGGGDGGMLREVAKHKSVERITMVEIDGTVVDMCKEFLP 119
Cdd:COG0421   3 GRVLVLDGVVQSTmELDEFEYHEMMAHVPLLFHPNPKRVLIIGGGDGGLARELLKHPPVERVDVVEIDPEVVELAREYFP 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596884 120 NHSqGAFDDPRLNLVIDDGMRFVATTEERFDVIISDSTDPIGPGEVLFSENFYQACRRCLNEGGILVTQNGTPFMQLEEV 199
Cdd:COG0421  83 LLA-PAFDDPRLRVVIGDGRAFLREAEESYDVIIVDLTDPVGPAEGLFTREFYEDCRRALKPGGVLVVNLGSPFYGLDLL 161
                       170       180       190
                ....*....|....*....|....*....|....
gi 15596884 200 RTTAARTDGLFADWHFYQAAVPTYiGGAMTFAWG 233
Cdd:COG0421 162 RRVLATLREVFPHVVLYAAPVPTY-GGGNVFLLA 194
Spermine_synth pfam01564
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ...
57-236 3.16e-80

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: 240.30  E-value: 3.16e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596884    57 EFIYHEMLTHVPILAHGAARRVLIIGGGDGGMLREVAKHKSVERITMVEIDGTVVDMCKEFLPNHSqGAFDDPRLNLVID 136
Cdd:pfam01564   1 EFIYHEMIAHVPLCSHPNPKKVLIIGGGDGGVLREVVKHPSVEKITLVDIDEKVIDFSKKFLPSLA-IGFQDPRVKVVIG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596884   137 DGMRFVATTEERFDVIISDSTDPIGPGEVLFSENFYQACRRCLNEGGILVTQNGTPFMQLEEVRTTAARTDGLFADWHFY 216
Cdd:pfam01564  80 DGFKFLKDYLNTFDVIIVDSTDPVGPAENLFSKPFFDLLKKALKEDGVFITQAESPWLHLELIINILKNGKQVFPVVMPY 159
                         170       180
                  ....*....|....*....|
gi 15596884   217 QAAVPTYIGGAMTFAWGSTH 236
Cdd:pfam01564 160 VATIPTYPSGGWGFTVCSKN 179
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
77-188 7.98e-10

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: 55.13  E-value: 7.98e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596884  77 RVLIIGGGDGGMLREVAKHKsVERITMVEIDGTVVDMCKEFlpnhsQGAFDDPRLNLVIDDGMRFVATTEERFDVIISDS 156
Cdd:cd02440   1 RVLDLGCGTGALALALASGP-GARVTGVDISPVALELARKA-----AAALLADNVEVLKGDAEELPPEADESFDVIISDP 74
                        90       100       110
                ....*....|....*....|....*....|..
gi 15596884 157 TDPIGPGEVlfsENFYQACRRCLNEGGILVTQ 188
Cdd:cd02440  75 PLHHLVEDL---ARFLEEARRLLKPGGVLVLT 103
MFS_SpdSyn NF037959
fused MFS/spermidine synthase; Proteins of this family are fusion of a N-terminal MFS (Major ...
42-184 3.37e-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: 44.83  E-value: 3.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596884   42 RVMALDGVIQTTEADE-----FI-YHEMLTHVPILAHGAAR-RVLIIGGGDGGMLREVAKHKSVERITMVEIDGTVVDMC 114
Cdd:NF037959 236 RLMVLDHLAHGINARDdptvlFTpYAAMLDELARLRMGRADfSAFFIGGGAYTLPRAWAARRPAGRITVAEIDPAVTRVA 315
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15596884  115 KEFLpnhsqgAFDDPRLNLVIDDGMRFVAT-TEERFDVIISDS-TDpIGPGEVLFSENFYQACRRCLNEGGI 184
Cdd:NF037959 316 AEDF------WFDPASATVLHEDARRALRRrPEERFDVIVGDAfTD-IAVPAHLVTREFFELVRARLTPDGV 380
 
Name Accession Description Interval E-value
PRK00811 PRK00811
polyamine aminopropyltransferase;
4-281 9.15e-176

polyamine aminopropyltransferase;


Pssm-ID: 234843 [Multi-domain]  Cd Length: 283  Bit Score: 486.20  E-value: 9.15e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596884    4 YQETLYQGYGQRFSIDNMLHEVRTEHQHLVIFENARMGRVMALDGVIQTTEADEFIYHEMLTHVPILAHGAARRVLIIGG 83
Cdd:PRK00811   6 FTETLTDNYGQSFRVKKVLYEEKSPFQRIEIFETPEFGRLLALDGCVMTTERDEFIYHEMMTHVPLFAHPNPKRVLIIGG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596884   84 GDGGMLREVAKHKSVERITMVEIDGTVVDMCKEFLPNHSQGAFDDPRLNLVIDDGMRFVATTEERFDVIISDSTDPIGPG 163
Cdd:PRK00811  86 GDGGTLREVLKHPSVEKITLVEIDERVVEVCRKYLPEIAGGAYDDPRVELVIGDGIKFVAETENSFDVIIVDSTDPVGPA 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596884  164 EVLFSENFYQACRRCLNEGGILVTQNGTPFMQLEEVRTTAARTDGLFADWHFYQAAVPTYIGGAMTFAWGSTHEGLRRLP 243
Cdd:PRK00811 166 EGLFTKEFYENCKRALKEDGIFVAQSGSPFYQADEIKDMHRKLKEVFPIVRPYQAAIPTYPSGLWSFTFASKNDDLKFLP 245
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 15596884  244 LETLRQRFRDSGIATRYYNADIHLGAFALPQYVLQAIG 281
Cdd:PRK00811 246 LDVIEARFAERGIKTRYYNPELHKAAFALPQFVKDALK 283
speE TIGR00417
spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine ...
4-275 1.70e-130

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: 370.99  E-value: 1.70e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596884     4 YQETLYQGYGQRFSIDNMLHEVRTEHQHLVIFENARMGRVMALDGVIQTTEADEFIYHEMLTHVPILAHGAARRVLIIGG 83
Cdd:TIGR00417   2 FTEYHDKNFGLTMKVDKVLYHEKSEFQDLEIFETEAFGNVLVLDGVVQTTERDEFIYHEMITHVPLFTHPNPKHVLVIGG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596884    84 GDGGMLREVAKHKSVERITMVEIDGTVVDMCKEFLPNHSqGAFDDPRLNLVIDDGMRFVATTEERFDVIISDSTDPIGPG 163
Cdd:TIGR00417  82 GDGGVLREVLKHKSVESATLVDIDEKVIELSRKYLPNLA-GSYDDPRVKLVIDDGFKFLADTENTFDVIIVDSTDPVGPA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596884   164 EVLFSENFYQACRRCLNEGGILVTQNGTPFMQLEEVRTTAARTDGLFADWHFYQAAVPTYIGGAMTFAWGSTHEgLRRLP 243
Cdd:TIGR00417 161 ETLFTKEFYELLKKALNPDGIFVAQSESPWLQLELIIDLKRKLKEAFPITEYYTAAIPTYPSGLWTFTIASKNK-YRPLE 239
                         250       260       270
                  ....*....|....*....|....*....|..
gi 15596884   244 LETLRQRFRDSGIATRYYNADIHLGAFALPQY 275
Cdd:TIGR00417 240 VEIRRIKFEAEDGKTKYYNPDIHKAAFVLPKW 271
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
41-233 6.71e-92

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


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 270.16  E-value: 6.71e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596884  41 GRVMALDGVIQTT-EADEFIYHEMLTHVPILAHGAARRVLIIGGGDGGMLREVAKHKSVERITMVEIDGTVVDMCKEFLP 119
Cdd:COG0421   3 GRVLVLDGVVQSTmELDEFEYHEMMAHVPLLFHPNPKRVLIIGGGDGGLARELLKHPPVERVDVVEIDPEVVELAREYFP 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596884 120 NHSqGAFDDPRLNLVIDDGMRFVATTEERFDVIISDSTDPIGPGEVLFSENFYQACRRCLNEGGILVTQNGTPFMQLEEV 199
Cdd:COG0421  83 LLA-PAFDDPRLRVVIGDGRAFLREAEESYDVIIVDLTDPVGPAEGLFTREFYEDCRRALKPGGVLVVNLGSPFYGLDLL 161
                       170       180       190
                ....*....|....*....|....*....|....
gi 15596884 200 RTTAARTDGLFADWHFYQAAVPTYiGGAMTFAWG 233
Cdd:COG0421 162 RRVLATLREVFPHVVLYAAPVPTY-GGGNVFLLA 194
PLN02366 PLN02366
spermidine synthase
13-281 1.03e-84

spermidine synthase


Pssm-ID: 215208 [Multi-domain]  Cd Length: 308  Bit Score: 256.11  E-value: 1.03e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596884   13 GQRFS--IDNMLHEVRTEHQHLVIFENARMGRVMALDGVIQTTEADEFIYHEMLTHVPILAHGAARRVLIIGGGDGGMLR 90
Cdd:PLN02366  28 GEAHSlkVEKVLFQGKSDFQDVLVFESATYGKVLVLDGVIQLTERDECAYQEMITHLPLCSIPNPKKVLVVGGGDGGVLR 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596884   91 EVAKHKSVERITMVEIDGTVVDMCKEFLPNHSQGaFDDPRLNLVIDDGMRFV-ATTEERFDVIISDSTDPIGPGEVLFSE 169
Cdd:PLN02366 108 EIARHSSVEQIDICEIDKMVIDVSKKFFPDLAVG-FDDPRVNLHIGDGVEFLkNAPEGTYDAIIVDSSDPVGPAQELFEK 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596884  170 NFYQACRRCLNEGGILVTQNGTPFMQLEEVRTTAARTDGLFADW-HFYQAAVPTYIGGAMTFAWGSThEGLRRLPLETLR 248
Cdd:PLN02366 187 PFFESVARALRPGGVVCTQAESMWLHMDLIEDLIAICRETFKGSvNYAWTTVPTYPSGVIGFVLCSK-EGPAVDFKHPVN 265
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 15596884  249 QRFRDSGIAT-----RYYNADIHLGAFALPQYVLQAIG 281
Cdd:PLN02366 266 PIDKLEGAGKakrplKFYNSEVHRAAFCLPSFAKRELE 303
Spermine_synth pfam01564
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ...
57-236 3.16e-80

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: 240.30  E-value: 3.16e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596884    57 EFIYHEMLTHVPILAHGAARRVLIIGGGDGGMLREVAKHKSVERITMVEIDGTVVDMCKEFLPNHSqGAFDDPRLNLVID 136
Cdd:pfam01564   1 EFIYHEMIAHVPLCSHPNPKKVLIIGGGDGGVLREVVKHPSVEKITLVDIDEKVIDFSKKFLPSLA-IGFQDPRVKVVIG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596884   137 DGMRFVATTEERFDVIISDSTDPIGPGEVLFSENFYQACRRCLNEGGILVTQNGTPFMQLEEVRTTAARTDGLFADWHFY 216
Cdd:pfam01564  80 DGFKFLKDYLNTFDVIIVDSTDPVGPAENLFSKPFFDLLKKALKEDGVFITQAESPWLHLELIINILKNGKQVFPVVMPY 159
                         170       180
                  ....*....|....*....|
gi 15596884   217 QAAVPTYIGGAMTFAWGSTH 236
Cdd:pfam01564 160 VATIPTYPSGGWGFTVCSKN 179
PLN02823 PLN02823
spermine synthase
4-280 3.42e-66

spermine synthase


Pssm-ID: 178418 [Multi-domain]  Cd Length: 336  Bit Score: 209.92  E-value: 3.42e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596884    4 YQETLYQGYGQRFSIDNMLHEVRTEHQHLVIFENARMGRVMALDGVIQTTEADEFIYHEMLTHVPILAHGAARRVLIIGG 83
Cdd:PLN02823  33 YEEEIEDDLRWSYAVNSVLHTGTSEFQDIALVDTKPFGKVLIIDGKMQSAEADEFVYHESLVHPALLHHPNPKTVFIMGG 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596884   84 GDGGMLREVAKHKSVERITMVEIDGTVVDMCKEFLPNHSQgAFDDPRLNLVIDDGMRFVATTEERFDVIISDSTDPI--G 161
Cdd:PLN02823 113 GEGSTAREVLRHKTVEKVVMCDIDQEVVDFCRKHLTVNRE-AFCDKRLELIINDARAELEKRDEKFDVIIGDLADPVegG 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596884  162 PGEVLFSENFYQ-ACRRCLNEGGILVTQNGTP-FMQLEEVRTTAARTDG-LFADWHFYQAAVPTYiggAMTFAW----GS 234
Cdd:PLN02823 192 PCYQLYTKSFYErIVKPKLNPGGIFVTQAGPAgILTHKEVFSSIYNTLRqVFKYVVPYTAHVPSF---ADTWGWvmasDH 268
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 15596884  235 THEGLRRLPL-ETLRQRFRDSgiaTRYYNADIHLGAFALPQYVLQAI 280
Cdd:PLN02823 269 PFADLSAEELdSRIKERIDGE---LKYLDGETFSSAFALNKTVRQAL 312
COG4262 COG4262
Predicted spermidine synthase with an N-terminal membrane domain [General function prediction ...
14-204 7.39e-58

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


Pssm-ID: 443404 [Multi-domain]  Cd Length: 426  Bit Score: 190.85  E-value: 7.39e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596884  14 QRFSIDNMLHEVRTEHQHLVIFENARmGRVMALDGVIQTTEADEFIYHEMLTHVPILAHGAARRVLIIGGGDGGMLREVA 93
Cdd:COG4262 227 QKLYGDPVVYSEQTPYQRIVVTRDKD-DRRLYLNGNLQFSSLDEYRYHEALVHPPMAAHPRPRRVLVLGGGDGLAAREVL 305
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596884  94 KHKSVERITMVEIDGTVVDMCKE--FLPNHSQGAFDDPRLNLVIDDGMRFVATTEERFDVIISDSTDPIGPGEV-LFSEN 170
Cdd:COG4262 306 KYPDVESVTLVDLDPEVTDLAKTnpFLRELNGGALNDPRVTVVNADAFQFLRETDEKYDVIIVDLPDPSNFSLGkLYSVE 385
                       170       180       190
                ....*....|....*....|....*....|....
gi 15596884 171 FYQACRRCLNEGGILVTQNGTPFMQLEEVRTTAA 204
Cdd:COG4262 386 FYRLVRRHLAPGGVLVVQATSPYFAPKAFWCIAK 419
PRK03612 PRK03612
polyamine aminopropyltransferase;
14-273 4.77e-46

polyamine aminopropyltransferase;


Pssm-ID: 235139 [Multi-domain]  Cd Length: 521  Bit Score: 161.93  E-value: 4.77e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596884   14 QRFSIDNMLHEVRTEHQHLVIFENAR-MGRVMAL--DGVIQTTEADEFIYHEMLTHVPILAHGAARRVLIIGGGDGGMLR 90
Cdd:PRK03612 234 QLLYGDPVVYAEQTPYQRIVVTRRGNgRGPDLRLylNGRLQFSSRDEYRYHEALVHPAMAASARPRRVLVLGGGDGLALR 313
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596884   91 EVAKHKSVERITMVEIDGTVVDMCKEFLP----NhsQGAFDDPRLNLVIDDGMRFVATTEERFDVIISDSTDPIGPGEV- 165
Cdd:PRK03612 314 EVLKYPDVEQVTLVDLDPAMTELARTSPAlralN--GGALDDPRVTVVNDDAFNWLRKLAEKFDVIIVDLPDPSNPALGk 391
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596884  166 LFSENFYQACRRCLNEGGILVTQNGTPFMQLEE----VRTTAArtdglfADWHF--YQAAVPtyiggamTFA-WGSTheg 238
Cdd:PRK03612 392 LYSVEFYRLLKRRLAPDGLLVVQSTSPYFAPKAfwsiEATLEA------AGLATtpYHVNVP-------SFGeWGFV--- 455
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 15596884  239 LRRLPLETLRQRFRDSGIATRYYNADIHLGAFALP 273
Cdd:PRK03612 456 LAGAGARPPLAVPTELPVPLRFLDPALLAAAFVFP 490
speE PRK01581
polyamine aminopropyltransferase;
19-192 9.57e-28

polyamine aminopropyltransferase;


Pssm-ID: 234961 [Multi-domain]  Cd Length: 374  Bit Score: 110.05  E-value: 9.57e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596884   19 DNMLHE-VRTEHQHLVIFENARMgrvmALDGVIQTTEADEFIYHEMLTHvPILAHGA-ARRVLIIGGGDGGMLREVAKHK 96
Cdd:PRK01581  98 TNLFAEkSNYQNINLLQVSDIRL----YLDKQLQFSSVDEQIYHEALVH-PIMSKVIdPKRVLILGGGDGLALREVLKYE 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596884   97 SVERITMVEIDGTVVDMCK--EFLPNHSQGAFDDPRLNLVIDDGMRFVATTEERFDVIISDSTDPIGPG-EVLFSENFYQ 173
Cdd:PRK01581 173 TVLHVDLVDLDGSMINMARnvPELVSLNKSAFFDNRVNVHVCDAKEFLSSPSSLYDVIIIDFPDPATELlSTLYTSELFA 252
                        170
                 ....*....|....*....
gi 15596884  174 ACRRCLNEGGILVTQNGTP 192
Cdd:PRK01581 253 RIATFLTEDGAFVCQSNSP 271
speE PRK00536
spermidine synthase; Provisional
14-285 4.43e-17

spermidine synthase; Provisional


Pssm-ID: 134311 [Multi-domain]  Cd Length: 262  Bit Score: 78.75  E-value: 4.43e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596884   14 QRFSIDNMLHEVRTEHQHLVIFENARMGRVMALDGVIqTTEADEFIYHEMLTHVPILAHGAARRVLIIGGGDGGMLREVA 93
Cdd:PRK00536  13 KEYTIEAKLLDVRSEHNILEIFKSKDFGEIAMLNKQL-LFKNFLHIESELLAHMGGCTKKELKEVLIVDGFDLELAHQLF 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596884   94 KHKSveRITMVEIDGTVVDMCKEFLPnHSQGAFDDPRLNLViddgMRFVATTEERFDVIISDStdpigpgevLFSENFYQ 173
Cdd:PRK00536  92 KYDT--HVDFVQADEKILDSFISFFP-HFHEVKNNKNFTHA----KQLLDLDIKKYDLIICLQ---------EPDIHKID 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596884  174 ACRRCLNEGGILVTQNGTPFMQlEEVRTTAARTDGlfadwHFYQAAVPTY----IGGAMTFAWGSthegLRRLPLETLRQ 249
Cdd:PRK00536 156 GLKRMLKEDGVFISVAKHPLLE-HVSMQNALKNMG-----DFFSIAMPFVaplrILSNKGYIYAS----FKTHPLKDLML 225
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 15596884  250 RFRDSGIATRYYNADIHLGAFALPQYVLQAIgkQDN 285
Cdd:PRK00536 226 QKIEALKSVRYYNEDIHRAAFALPKNLQEVF--KDN 259
PRK04457 PRK04457
polyamine aminopropyltransferase;
76-187 6.87e-14

polyamine aminopropyltransferase;


Pssm-ID: 179854 [Multi-domain]  Cd Length: 262  Bit Score: 69.68  E-value: 6.87e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596884   76 RRVLIIGGGDGGMLREVAKHKSVERITMVEIDGTVVDMCKeflpNHSQGAFDDPRLNLVIDDGMRFVATTEERFDVIISD 155
Cdd:PRK04457  68 QHILQIGLGGGSLAKFIYTYLPDTRQTAVEINPQVIAVAR----NHFELPENGERFEVIEADGAEYIAVHRHSTDVILVD 143
                         90       100       110
                 ....*....|....*....|....*....|..
gi 15596884  156 STDPIGPGEVLFSENFYQACRRCLNEGGILVT 187
Cdd:PRK04457 144 GFDGEGIIDALCTQPFFDDCRNALSSDGIFVV 175
Spermine_synt_N pfam17284
Spermidine synthase tetramerization domain; This domain represents the N-terminal ...
7-54 9.33e-13

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: 61.52  E-value: 9.33e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 15596884     7 TLYQGYGQRFS--IDNMLHEVRTEHQHLVIFENARMGRVMALDGVIQTTE 54
Cdd:pfam17284   4 TEIHDLGQALEykVEKVLYDEKSEYQDIEIFESKTFGNVLVLDGVVQLTE 53
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
77-188 7.98e-10

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: 55.13  E-value: 7.98e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596884  77 RVLIIGGGDGGMLREVAKHKsVERITMVEIDGTVVDMCKEFlpnhsQGAFDDPRLNLVIDDGMRFVATTEERFDVIISDS 156
Cdd:cd02440   1 RVLDLGCGTGALALALASGP-GARVTGVDISPVALELARKA-----AAALLADNVEVLKGDAEELPPEADESFDVIISDP 74
                        90       100       110
                ....*....|....*....|....*....|..
gi 15596884 157 TDPIGPGEVlfsENFYQACRRCLNEGGILVTQ 188
Cdd:cd02440  75 PLHHLVEDL---ARFLEEARRLLKPGGVLVLT 103
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
73-186 1.05e-06

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: 1.05e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596884  73 GAARRVLIIGGGDGGMLREVAKHksVERITMVEIDGTVVDMCKEFLPnhsqgafdDPRLNLVIDDgMRFVATTEERFDVI 152
Cdd:COG2227  23 PAGGRVLDVGCGTGRLALALARR--GADVTGVDISPEALEIARERAA--------ELNVDFVQGD-LEDLPLEDGSFDLV 91
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 15596884 153 ISDST-----DPigpgevlfsENFYQACRRCLNEGGILV 186
Cdd:COG2227  92 ICSEVlehlpDP---------AALLRELARLLKPGGLLL 121
MFS_SpdSyn NF037959
fused MFS/spermidine synthase; Proteins of this family are fusion of a N-terminal MFS (Major ...
42-184 3.37e-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: 44.83  E-value: 3.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596884   42 RVMALDGVIQTTEADE-----FI-YHEMLTHVPILAHGAAR-RVLIIGGGDGGMLREVAKHKSVERITMVEIDGTVVDMC 114
Cdd:NF037959 236 RLMVLDHLAHGINARDdptvlFTpYAAMLDELARLRMGRADfSAFFIGGGAYTLPRAWAARRPAGRITVAEIDPAVTRVA 315
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15596884  115 KEFLpnhsqgAFDDPRLNLVIDDGMRFVAT-TEERFDVIISDS-TDpIGPGEVLFSENFYQACRRCLNEGGI 184
Cdd:NF037959 316 AEDF------WFDPASATVLHEDARRALRRrPEERFDVIVGDAfTD-IAVPAHLVTREFFELVRARLTPDGV 380
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
74-252 1.03e-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: 1.03e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596884  74 AARRVLIIGGGDGGMLREVAKHKsVERITMVEIDGTVVDMCKEFLPnhsqgAFDDPRLNLVIDDGMRFVATTEERFDVII 153
Cdd:COG0500  26 KGGRVLDLGCGTGRNLLALAARF-GGRVIGIDLSPEAIALARARAA-----KAGLGNVEFLVADLAELDPLPAESFDLVV 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596884 154 SDST----DPIGPGEVLfsenfyQACRRCLNEGGIL-VTQNGTPFMQLEEvRTTAARTDGLFADWHFYQAAVPTyIGGAM 228
Cdd:COG0500 100 AFGVlhhlPPEEREALL------RELARALKPGGVLlLSASDAAAALSLA-RLLLLATASLLELLLLLRLLALE-LYLRA 171
                       170       180
                ....*....|....*....|....
gi 15596884 229 TFAWGSTHEGLRRLPLETLRQRFR 252
Cdd:COG0500 172 LLAAAATEDLRSDALLESANALEY 195
COG2521 COG2521
Predicted archaeal methyltransferase [General function prediction only];
77-192 1.61e-04

Predicted archaeal methyltransferase [General function prediction only];


Pssm-ID: 442011 [Multi-domain]  Cd Length: 285  Bit Score: 42.20  E-value: 1.61e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596884  77 RVLIIGGGDGGMLREVAKhKSVERITMVEIDGTVVDMCKefLPNHSQGAFDdPRLNLVIDDGMRFVAT-TEERFDVIISD 155
Cdd:COG2521 135 RVLDTCTGLGYTAIEALK-RGAREVITVEKDPNVLELAE--LNPWSRELAN-ERIKIILGDASEVIKTfPDESFDAIIHD 210
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 15596884 156 stdpigP------GEvLFSENFYQACRRCLNEGGILVTQNGTP 192
Cdd:COG2521 211 ------PprfslaGE-LYSLEFYRELYRVLKPGGRLFHYTGNP 246
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
63-186 4.61e-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: 40.17  E-value: 4.61e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596884  63 MLTHVPILAHGaarRVLIIGGGDGGMLREVAKHKSVERITMVEIDGTVVDMCKE-FLPNHSQGAfddprlNLVIDDGMRF 141
Cdd:COG2813  41 LLEHLPEPLGG---RVLDLGCGYGVIGLALAKRNPEARVTLVDVNARAVELARAnAAANGLENV------EVLWSDGLSG 111
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 15596884 142 VAttEERFDVIIS--------DSTDPIGpgevlfsENFYQACRRCLNEGGILV 186
Cdd:COG2813 112 VP--DGSFDLILSnppfhagrAVDKEVA-------HALIADAARHLRPGGELW 155
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
74-186 7.08e-04

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 38.27  E-value: 7.08e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596884  74 AARRVLIIGGGDGGMLREVAKHKSVERITMVEIDGTVVDMCKEFLPNhsqgafddprLNLVIDDGMRFvaTTEERFDVII 153
Cdd:COG4106   1 PPRRVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARARLPN----------VRFVVADLRDL--DPPEPFDLVV 68
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 15596884 154 SDST-----DPigpgevlfsENFYQACRRCLNEGGILV 186
Cdd:COG4106  69 SNAAlhwlpDH---------AALLARLAAALAPGGVLA 97
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
77-188 1.04e-03

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 38.76  E-value: 1.04e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596884  77 RVLIIGGGDGGMLREVAKHKSVeRITMVEIDGTVVDMCKEFLpnhsQGAFDDPRLNLVIDDGMRFVAttEERFDVIIS-D 155
Cdd:COG2230  54 RVLDIGCGWGGLALYLARRYGV-RVTGVTLSPEQLEYARERA----AEAGLADRVEVRLADYRDLPA--DGQFDAIVSiG 126
                        90       100       110
                ....*....|....*....|....*....|...
gi 15596884 156 STDPIGPGEVlfsENFYQACRRCLNEGGILVTQ 188
Cdd:COG2230 127 MFEHVGPENY---PAYFAKVARLLKPGGRLLLH 156
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
70-186 4.22e-03

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 37.29  E-value: 4.22e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596884  70 LAHGAARRVLIIGGGDGGMLREVAKHksVERITMVEIDGTVVDMCKEflpnhsQGAFDdprlNLVIDDgMRFVATTEERF 149
Cdd:COG4976  42 LPPGPFGRVLDLGCGTGLLGEALRPR--GYRLTGVDLSEEMLAKARE------KGVYD----RLLVAD-LADLAEPDGRF 108
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 15596884 150 DVIIS-DSTDPIGPGEVLFsenfyQACRRCLNEGGILV 186
Cdd:COG4976 109 DLIVAaDVLTYLGDLAAVF-----AGVARALKPGGLFI 141
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
76-215 9.88e-03

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 36.55  E-value: 9.88e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596884  76 RRVLIIGGGDG--GMLrevAKHKSVERITMVEIDGTVVDMCKEFLPNHsqgAFDDpRLNLVIDDgmrfvATT---EERFD 150
Cdd:COG4076  37 DVVLDIGTGSGllSML---AARAGAKKVYAVEVNPDIAAVARRIIAAN---GLSD-RITVINAD-----ATDldlPEKAD 104
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15596884 151 VIISD--STDPIGPGEVlfsENFYQACRRCLNEGGILVTQNGTPFMQLEEVRtTAARTDGLFADWHF 215
Cdd:COG4076 105 VIISEmlDTALLDEGQV---PILNHARKRLLKPGGRIIPERITNAAQPVESP-VDAEGFEDWQFDGF 167
 
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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