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Conserved domains on  [gi|145334519|ref|NP_001078605|]
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S-adenosyl-L-methionine-dependent methyltransferases superfamily protein [Arabidopsis thaliana]

Protein Classification

spermidine/spermine synthase family protein( domain architecture ID 10010914)

spermidine/spermine synthase family protein similar to Arabidopsis thaliana thermospermine synthase ACAULIS5 that is required for correct xylem specification through regulation of the lifetime of the xylem elements

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02823 PLN02823
spermine synthase
1-331 0e+00

spermine synthase


:

Pssm-ID: 178418 [Multi-domain]  Cd Length: 336  Bit Score: 637.88  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519   1 MFGNGFPEIHKATSPTQTLHSNQQDCHWYEETIDDDLKWSFALNSVLHQGTSEYQDIALLDTKRFGKVLVIDGKMQSAER 80
Cdd:PLN02823   5 VHGNGTSHITAVATPTAALASNYAKSLWYEEEIEDDLRWSYAVNSVLHTGTSEFQDIALVDTKPFGKVLIIDGKMQSAEA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519  81 DEFIYHECLIHPALLFHPNPKTVFIMGGGEGSAAREILKHTTIEKVVMCDIDQEVVDFCRRFLTVNSDAFCNKKLELVIK 160
Cdd:PLN02823  85 DEFVYHESLVHPALLHHPNPKTVFIMGGGEGSTAREVLRHKTVEKVVMCDIDQEVVDFCRKHLTVNREAFCDKRLELIIN 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 161 DAKAELEKREEKFDIIVGDLADPVEGGPCYQLYTKSFYQNILKPKLSPNGIFVTQAGPAGIFTHKEVFTSIYNTMKQVFK 240
Cdd:PLN02823 165 DARAELEKRDEKFDVIIGDLADPVEGGPCYQLYTKSFYERIVKPKLNPGGIFVTQAGPAGILTHKEVFSSIYNTLRQVFK 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 241 YVKAYTAHVPSFADTWGWVMASDHEF-DVEVDEMDRRIEERVNGELMYLNAPSFVSAATLNKTISLALEKETEVYSEENA 319
Cdd:PLN02823 245 YVVPYTAHVPSFADTWGWVMASDHPFaDLSAEELDSRIKERIDGELKYLDGETFSSAFALNKTVRQALANETHVYTEENA 324
                        330
                 ....*....|..
gi 145334519 320 RFIHGHGVAYRH 331
Cdd:PLN02823 325 RFIHGHGTAAKA 336
 
Name Accession Description Interval E-value
PLN02823 PLN02823
spermine synthase
1-331 0e+00

spermine synthase


Pssm-ID: 178418 [Multi-domain]  Cd Length: 336  Bit Score: 637.88  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519   1 MFGNGFPEIHKATSPTQTLHSNQQDCHWYEETIDDDLKWSFALNSVLHQGTSEYQDIALLDTKRFGKVLVIDGKMQSAER 80
Cdd:PLN02823   5 VHGNGTSHITAVATPTAALASNYAKSLWYEEEIEDDLRWSYAVNSVLHTGTSEFQDIALVDTKPFGKVLIIDGKMQSAEA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519  81 DEFIYHECLIHPALLFHPNPKTVFIMGGGEGSAAREILKHTTIEKVVMCDIDQEVVDFCRRFLTVNSDAFCNKKLELVIK 160
Cdd:PLN02823  85 DEFVYHESLVHPALLHHPNPKTVFIMGGGEGSTAREVLRHKTVEKVVMCDIDQEVVDFCRKHLTVNREAFCDKRLELIIN 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 161 DAKAELEKREEKFDIIVGDLADPVEGGPCYQLYTKSFYQNILKPKLSPNGIFVTQAGPAGIFTHKEVFTSIYNTMKQVFK 240
Cdd:PLN02823 165 DARAELEKRDEKFDVIIGDLADPVEGGPCYQLYTKSFYERIVKPKLNPGGIFVTQAGPAGILTHKEVFSSIYNTLRQVFK 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 241 YVKAYTAHVPSFADTWGWVMASDHEF-DVEVDEMDRRIEERVNGELMYLNAPSFVSAATLNKTISLALEKETEVYSEENA 319
Cdd:PLN02823 245 YVVPYTAHVPSFADTWGWVMASDHPFaDLSAEELDSRIKERIDGELKYLDGETFSSAFALNKTVRQALANETHVYTEENA 324
                        330
                 ....*....|..
gi 145334519 320 RFIHGHGVAYRH 331
Cdd:PLN02823 325 RFIHGHGTAAKA 336
speE TIGR00417
spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine ...
28-289 1.34e-76

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: 236.17  E-value: 1.34e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519   28 WYEETIDDDLKWSFALNSVLHQGTSEYQDIALLDTKRFGKVLVIDGKMQSAERDEFIYHECLIHPALLFHPNPKTVFIMG 107
Cdd:TIGR00417   1 WFTEYHDKNFGLTMKVDKVLYHEKSEFQDLEIFETEAFGNVLVLDGVVQTTERDEFIYHEMITHVPLFTHPNPKHVLVIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519  108 GGEGSAAREILKHTTIEKVVMCDIDQEVVDFCRRFLTVNSDAFCNKKLELVIKDAKAELEKREEKFDIIVGDLADPVegG 187
Cdd:TIGR00417  81 GGDGGVLREVLKHKSVESATLVDIDEKVIELSRKYLPNLAGSYDDPRVKLVIDDGFKFLADTENTFDVIIVDSTDPV--G 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519  188 PCYQLYTKSFYQNiLKPKLSPNGIFVTQAGpaGIFTHKEVFTSIYNTMKQVFKYVKAYTAHVPSF-ADTWGWVMASDHEF 266
Cdd:TIGR00417 159 PAETLFTKEFYEL-LKKALNPDGIFVAQSE--SPWLQLELIIDLKRKLKEAFPITEYYTAAIPTYpSGLWTFTIASKNKY 235
                         250       260
                  ....*....|....*....|....*
gi 145334519  267 D-VEVDemDRRI-EERVNGELMYLN 289
Cdd:TIGR00417 236 RpLEVE--IRRIkFEAEDGKTKYYN 258
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
66-261 1.26e-73

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


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 225.48  E-value: 1.26e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519  66 GKVLVIDGKMQSA-ERDEFIYHECLIHPALLFHPNPKTVFIMGGGEGSAAREILKHTTIEKVVMCDIDQEVVDFCRRFLT 144
Cdd:COG0421    3 GRVLVLDGVVQSTmELDEFEYHEMMAHVPLLFHPNPKRVLIIGGGDGGLARELLKHPPVERVDVVEIDPEVVELAREYFP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 145 VNSDAFCNKKLELVIKDAKAELEKREEKFDIIVGDLADPVegGPCYQLYTKSFYQNIlKPKLSPNGIFVTQAGpaGIFTH 224
Cdd:COG0421   83 LLAPAFDDPRLRVVIGDGRAFLREAEESYDVIIVDLTDPV--GPAEGLFTREFYEDC-RRALKPGGVLVVNLG--SPFYG 157
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 145334519 225 KEVFTSIYNTMKQVFKYVKAYTAHVPSFADTWGWVMA 261
Cdd:COG0421  158 LDLLRRVLATLREVFPHVVLYAAPVPTYGGGNVFLLA 194
Spermine_synth pfam01564
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ...
82-267 1.14e-50

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: 166.34  E-value: 1.14e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519   82 EFIYHECLIHPALLFHPNPKTVFIMGGGEGSAAREILKHTTIEKVVMCDIDQEVVDFCRRFLTVNSDAFCNKKLELVIKD 161
Cdd:pfam01564   1 EFIYHEMIAHVPLCSHPNPKKVLIIGGGDGGVLREVVKHPSVEKITLVDIDEKVIDFSKKFLPSLAIGFQDPRVKVVIGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519  162 AKAELEKREEKFDIIVGDLADPVegGPCYQLYTKSFYQNiLKPKLSPNGIFVTQAGpaGIFTHKEVFTSIYNTMKQVFKY 241
Cdd:pfam01564  81 GFKFLKDYLNTFDVIIVDSTDPV--GPAENLFSKPFFDL-LKKALKEDGVFITQAE--SPWLHLELIINILKNGKQVFPV 155
                         170       180
                  ....*....|....*....|....*..
gi 145334519  242 VKAYTAHVPSFAD-TWGWVMASDHEFD 267
Cdd:pfam01564 156 VMPYVATIPTYPSgGWGFTVCSKNPLK 182
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
107-215 7.57e-06

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: 44.34  E-value: 7.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 107 GGGEGSAAREILKHTtIEKVVMCDIDQEVVDFCRRfltvNSDAFCNKKLELVIKDAKAELEKREEKFDIIVGDLAdpveg 186
Cdd:cd02440    6 GCGTGALALALASGP-GARVTGVDISPVALELARK----AAAALLADNVEVLKGDAEELPPEADESFDVIISDPP----- 75
                         90       100
                 ....*....|....*....|....*....
gi 145334519 187 GPCYQLYTKSFYQNILKpKLSPNGIFVTQ 215
Cdd:cd02440   76 LHHLVEDLARFLEEARR-LLKPGGVLVLT 103
MFS_SpdSyn NF037959
fused MFS/spermidine synthase; Proteins of this family are fusion of a N-terminal MFS (Major ...
92-250 8.48e-04

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: 40.98  E-value: 8.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519  92 PALLFHPNPKTVFIMGGGEGSAAREILKHTTIEKVVMCDIDQEVVDFCRRFLTVNSDAFcnkklELVIKDAKAELEKR-E 170
Cdd:NF037959 268 ARLRMGRADFSAFFIGGGAYTLPRAWAARRPAGRITVAEIDPAVTRVAAEDFWFDPASA-----TVLHEDARRALRRRpE 342
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 171 EKFDIIVGD----LADPveggpcYQLYTKSFYQnILKPKLSPNGIFVTQAgpagI--FTHKEVFTSIYNTMKQVFKYVKA 244
Cdd:NF037959 343 ERFDVIVGDaftdIAVP------AHLVTREFFE-LVRARLTPDGVYLMNV----IdhADRLRALAALVATLREVFPVVEV 411

                 ....*.
gi 145334519 245 YTAHVP 250
Cdd:NF037959 412 WTEARP 417
 
Name Accession Description Interval E-value
PLN02823 PLN02823
spermine synthase
1-331 0e+00

spermine synthase


Pssm-ID: 178418 [Multi-domain]  Cd Length: 336  Bit Score: 637.88  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519   1 MFGNGFPEIHKATSPTQTLHSNQQDCHWYEETIDDDLKWSFALNSVLHQGTSEYQDIALLDTKRFGKVLVIDGKMQSAER 80
Cdd:PLN02823   5 VHGNGTSHITAVATPTAALASNYAKSLWYEEEIEDDLRWSYAVNSVLHTGTSEFQDIALVDTKPFGKVLIIDGKMQSAEA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519  81 DEFIYHECLIHPALLFHPNPKTVFIMGGGEGSAAREILKHTTIEKVVMCDIDQEVVDFCRRFLTVNSDAFCNKKLELVIK 160
Cdd:PLN02823  85 DEFVYHESLVHPALLHHPNPKTVFIMGGGEGSTAREVLRHKTVEKVVMCDIDQEVVDFCRKHLTVNREAFCDKRLELIIN 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 161 DAKAELEKREEKFDIIVGDLADPVEGGPCYQLYTKSFYQNILKPKLSPNGIFVTQAGPAGIFTHKEVFTSIYNTMKQVFK 240
Cdd:PLN02823 165 DARAELEKRDEKFDVIIGDLADPVEGGPCYQLYTKSFYERIVKPKLNPGGIFVTQAGPAGILTHKEVFSSIYNTLRQVFK 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 241 YVKAYTAHVPSFADTWGWVMASDHEF-DVEVDEMDRRIEERVNGELMYLNAPSFVSAATLNKTISLALEKETEVYSEENA 319
Cdd:PLN02823 245 YVVPYTAHVPSFADTWGWVMASDHPFaDLSAEELDSRIKERIDGELKYLDGETFSSAFALNKTVRQALANETHVYTEENA 324
                        330
                 ....*....|..
gi 145334519 320 RFIHGHGVAYRH 331
Cdd:PLN02823 325 RFIHGHGTAAKA 336
PRK00811 PRK00811
polyamine aminopropyltransferase;
28-290 1.15e-90

polyamine aminopropyltransferase;


Pssm-ID: 234843 [Multi-domain]  Cd Length: 283  Bit Score: 272.41  E-value: 1.15e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519  28 WYEETIDDDLKWSFALNSVLHQGTSEYQDIALLDTKRFGKVLVIDGKMQSAERDEFIYHECLIHPALLFHPNPKTVFIMG 107
Cdd:PRK00811   5 WFTETLTDNYGQSFRVKKVLYEEKSPFQRIEIFETPEFGRLLALDGCVMTTERDEFIYHEMMTHVPLFAHPNPKRVLIIG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 108 GGEGSAAREILKHTTIEKVVMCDIDQEVVDFCRRFL-TVNSDAFCNKKLELVIKDAKAELEKREEKFDIIVGDLADPVeg 186
Cdd:PRK00811  85 GGDGGTLREVLKHPSVEKITLVEIDERVVEVCRKYLpEIAGGAYDDPRVELVIGDGIKFVAETENSFDVIIVDSTDPV-- 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 187 GPCYQLYTKSFYQNILKpKLSPNGIFVTQAG-PagiFTHKEVFTSIYNTMKQVFKYVKAYTAHVPSF-ADTWGWVMASD- 263
Cdd:PRK00811 163 GPAEGLFTKEFYENCKR-ALKEDGIFVAQSGsP---FYQADEIKDMHRKLKEVFPIVRPYQAAIPTYpSGLWSFTFASKn 238
                        250       260
                 ....*....|....*....|....*...
gi 145334519 264 HEFD-VEVDEMDRRIEERvNGELMYLNA 290
Cdd:PRK00811 239 DDLKfLPLDVIEARFAER-GIKTRYYNP 265
speE TIGR00417
spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine ...
28-289 1.34e-76

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: 236.17  E-value: 1.34e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519   28 WYEETIDDDLKWSFALNSVLHQGTSEYQDIALLDTKRFGKVLVIDGKMQSAERDEFIYHECLIHPALLFHPNPKTVFIMG 107
Cdd:TIGR00417   1 WFTEYHDKNFGLTMKVDKVLYHEKSEFQDLEIFETEAFGNVLVLDGVVQTTERDEFIYHEMITHVPLFTHPNPKHVLVIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519  108 GGEGSAAREILKHTTIEKVVMCDIDQEVVDFCRRFLTVNSDAFCNKKLELVIKDAKAELEKREEKFDIIVGDLADPVegG 187
Cdd:TIGR00417  81 GGDGGVLREVLKHKSVESATLVDIDEKVIELSRKYLPNLAGSYDDPRVKLVIDDGFKFLADTENTFDVIIVDSTDPV--G 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519  188 PCYQLYTKSFYQNiLKPKLSPNGIFVTQAGpaGIFTHKEVFTSIYNTMKQVFKYVKAYTAHVPSF-ADTWGWVMASDHEF 266
Cdd:TIGR00417 159 PAETLFTKEFYEL-LKKALNPDGIFVAQSE--SPWLQLELIIDLKRKLKEAFPITEYYTAAIPTYpSGLWTFTIASKNKY 235
                         250       260
                  ....*....|....*....|....*
gi 145334519  267 D-VEVDemDRRI-EERVNGELMYLN 289
Cdd:TIGR00417 236 RpLEVE--IRRIkFEAEDGKTKYYN 258
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
66-261 1.26e-73

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


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 225.48  E-value: 1.26e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519  66 GKVLVIDGKMQSA-ERDEFIYHECLIHPALLFHPNPKTVFIMGGGEGSAAREILKHTTIEKVVMCDIDQEVVDFCRRFLT 144
Cdd:COG0421    3 GRVLVLDGVVQSTmELDEFEYHEMMAHVPLLFHPNPKRVLIIGGGDGGLARELLKHPPVERVDVVEIDPEVVELAREYFP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 145 VNSDAFCNKKLELVIKDAKAELEKREEKFDIIVGDLADPVegGPCYQLYTKSFYQNIlKPKLSPNGIFVTQAGpaGIFTH 224
Cdd:COG0421   83 LLAPAFDDPRLRVVIGDGRAFLREAEESYDVIIVDLTDPV--GPAEGLFTREFYEDC-RRALKPGGVLVVNLG--SPFYG 157
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 145334519 225 KEVFTSIYNTMKQVFKYVKAYTAHVPSFADTWGWVMA 261
Cdd:COG0421  158 LDLLRRVLATLREVFPHVVLYAAPVPTYGGGNVFLLA 194
PRK03612 PRK03612
polyamine aminopropyltransferase;
46-261 2.09e-56

polyamine aminopropyltransferase;


Pssm-ID: 235139 [Multi-domain]  Cd Length: 521  Bit Score: 190.82  E-value: 2.09e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519  46 VLHQGTSEYQDIALLDTKR-FGKV--LVIDGKMQSAERDEFIYHECLIHPALLFHPNPKTVFIMGGGEGSAAREILKHTT 122
Cdd:PRK03612 241 VVYAEQTPYQRIVVTRRGNgRGPDlrLYLNGRLQFSSRDEYRYHEALVHPAMAASARPRRVLVLGGGDGLALREVLKYPD 320
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 123 IEKVVMCDIDQEVVDFCR---RFLTVNSDAFCNKKLELVIKDAKAELEKREEKFDIIVGDLADP--VEGGpcyQLYTKSF 197
Cdd:PRK03612 321 VEQVTLVDLDPAMTELARtspALRALNGGALDDPRVTVVNDDAFNWLRKLAEKFDVIIVDLPDPsnPALG---KLYSVEF 397
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145334519 198 YqNILKPKLSPNGIFVTQAGPAgiFTHKEVFTSIYNTMKQVFKYVKAYTAHVPSFADtWGWVMA 261
Cdd:PRK03612 398 Y-RLLKRRLAPDGLLVVQSTSP--YFAPKAFWSIEATLEAAGLATTPYHVNVPSFGE-WGFVLA 457
COG4262 COG4262
Predicted spermidine synthase with an N-terminal membrane domain [General function prediction ...
46-239 6.37e-53

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


Pssm-ID: 443404 [Multi-domain]  Cd Length: 426  Bit Score: 179.68  E-value: 6.37e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519  46 VLHQGTSEYQDIALLDTKRFgKVLVIDGKMQSAERDEFIYHECLIHPALLFHPNPKTVFIMGGGEGSAAREILKHTTIEK 125
Cdd:COG4262  234 VVYSEQTPYQRIVVTRDKDD-RRLYLNGNLQFSSLDEYRYHEALVHPPMAAHPRPRRVLVLGGGDGLAAREVLKYPDVES 312
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 126 VVMCDIDQEVVDFCRR---FLTVNSDAFCNKKLELVIKDAKAELEKREEKFDIIVGDLADPVEGGPcYQLYTKSFYQnIL 202
Cdd:COG4262  313 VTLVDLDPEVTDLAKTnpfLRELNGGALNDPRVTVVNADAFQFLRETDEKYDVIIVDLPDPSNFSL-GKLYSVEFYR-LV 390
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 145334519 203 KPKLSPNGIFVTQAGPAgiFTHKEVFTSIYNTMKQVF 239
Cdd:COG4262  391 RRHLAPGGVLVVQATSP--YFAPKAFWCIAKTLEAAG 425
Spermine_synth pfam01564
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ...
82-267 1.14e-50

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: 166.34  E-value: 1.14e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519   82 EFIYHECLIHPALLFHPNPKTVFIMGGGEGSAAREILKHTTIEKVVMCDIDQEVVDFCRRFLTVNSDAFCNKKLELVIKD 161
Cdd:pfam01564   1 EFIYHEMIAHVPLCSHPNPKKVLIIGGGDGGVLREVVKHPSVEKITLVDIDEKVIDFSKKFLPSLAIGFQDPRVKVVIGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519  162 AKAELEKREEKFDIIVGDLADPVegGPCYQLYTKSFYQNiLKPKLSPNGIFVTQAGpaGIFTHKEVFTSIYNTMKQVFKY 241
Cdd:pfam01564  81 GFKFLKDYLNTFDVIIVDSTDPV--GPAENLFSKPFFDL-LKKALKEDGVFITQAE--SPWLHLELIINILKNGKQVFPV 155
                         170       180
                  ....*....|....*....|....*..
gi 145334519  242 VKAYTAHVPSFAD-TWGWVMASDHEFD 267
Cdd:pfam01564 156 VMPYVATIPTYPSgGWGFTVCSKNPLK 182
PLN02366 PLN02366
spermidine synthase
21-297 1.13e-48

spermidine synthase


Pssm-ID: 215208 [Multi-domain]  Cd Length: 308  Bit Score: 165.20  E-value: 1.13e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519  21 SNQQDCH------WYEETiddDLKW-----SFALNSVLHQGTSEYQDIALLDTKRFGKVLVIDGKMQSAERDEFIYHECL 89
Cdd:PLN02366   5 ESEAKCHstvipgWFSEI---SPMWpgeahSLKVEKVLFQGKSDFQDVLVFESATYGKVLVLDGVIQLTERDECAYQEMI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519  90 IHPALLFHPNPKTVFIMGGGEGSAAREILKHTTIEKVVMCDIDQEVVDFCRRFLTVNSDAFCNKKLELVIKDAKAELEK- 168
Cdd:PLN02366  82 THLPLCSIPNPKKVLVVGGGDGGVLREIARHSSVEQIDICEIDKMVIDVSKKFFPDLAVGFDDPRVNLHIGDGVEFLKNa 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 169 REEKFDIIVGDLADPVegGPCYQLYTKSFYQNILKpKLSPNGIFVTQAgpAGIFTHKEVFTSIYNTMKQVFK----YvkA 244
Cdd:PLN02366 162 PEGTYDAIIVDSSDPV--GPAQELFEKPFFESVAR-ALRPGGVVCTQA--ESMWLHMDLIEDLIAICRETFKgsvnY--A 234
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145334519 245 YTAhVPSF-ADTWGWVMASDHEFDVEVDEMDRRIEE-----RVNGELMYLNA---------PSFVSAA 297
Cdd:PLN02366 235 WTT-VPTYpSGVIGFVLCSKEGPAVDFKHPVNPIDKlegagKAKRPLKFYNSevhraafclPSFAKRE 301
speE PRK01581
polyamine aminopropyltransferase;
44-263 3.09e-34

polyamine aminopropyltransferase;


Pssm-ID: 234961 [Multi-domain]  Cd Length: 374  Bit Score: 128.93  E-value: 3.09e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519  44 NSVLHQgTSEYQDIALLDTKRFGkvLVIDGKMQSAERDEFIYHECLIHPALLFHPNPKTVFIMGGGEGSAAREILKHTTI 123
Cdd:PRK01581  98 TNLFAE-KSNYQNINLLQVSDIR--LYLDKQLQFSSVDEQIYHEALVHPIMSKVIDPKRVLILGGGDGLALREVLKYETV 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 124 EKVVMCDIDQEVVDFCR---RFLTVNSDAFCNKKLELVIKDAKAELEKREEKFDIIVGDLADPVEgGPCYQLYTKSFYQN 200
Cdd:PRK01581 175 LHVDLVDLDGSMINMARnvpELVSLNKSAFFDNRVNVHVCDAKEFLSSPSSLYDVIIIDFPDPAT-ELLSTLYTSELFAR 253
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145334519 201 ILKpKLSPNGIFVTQA-GPAGIfthKEVFTSIYNTMKQVFKYVKAYTAHVPSFADTWGWVMASD 263
Cdd:PRK01581 254 IAT-FLTEDGAFVCQSnSPADA---PLVYWSIGNTIEHAGLTVKSYHTIVPSFGTDWGFHIAAN 313
Spermine_synt_N pfam17284
Spermidine synthase tetramerization domain; This domain represents the N-terminal ...
28-79 4.57e-11

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: 57.29  E-value: 4.57e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 145334519   28 WYEETIDDDLKWSFALNSVLHQGTSEYQDIALLDTKRFGKVLVIDGKMQSAE 79
Cdd:pfam17284   2 WFTEIHDLGQALEYKVEKVLYDEKSEYQDIEIFESKTFGNVLVLDGVVQLTE 53
PRK04457 PRK04457
polyamine aminopropyltransferase;
94-214 1.30e-08

polyamine aminopropyltransferase;


Pssm-ID: 179854 [Multi-domain]  Cd Length: 262  Bit Score: 55.05  E-value: 1.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519  94 LLFHPNPKTVFIMGGGEGSAAREILKHTTIEKVVMCDIDQEVVDFCRRFLTVNSDafcNKKLELVIKDAKAELEKREEKF 173
Cdd:PRK04457  61 LLFNPRPQHILQIGLGGGSLAKFIYTYLPDTRQTAVEINPQVIAVARNHFELPEN---GERFEVIEADGAEYIAVHRHST 137
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 145334519 174 DIIVGDLADpvEGGPCYQLYTKSFYQNIlKPKLSPNGIFVT 214
Cdd:PRK04457 138 DVILVDGFD--GEGIIDALCTQPFFDDC-RNALSSDGIFVV 175
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
107-215 7.57e-06

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: 44.34  E-value: 7.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 107 GGGEGSAAREILKHTtIEKVVMCDIDQEVVDFCRRfltvNSDAFCNKKLELVIKDAKAELEKREEKFDIIVGDLAdpveg 186
Cdd:cd02440    6 GCGTGALALALASGP-GARVTGVDISPVALELARK----AAAALLADNVEVLKGDAEELPPEADESFDVIISDPP----- 75
                         90       100
                 ....*....|....*....|....*....
gi 145334519 187 GPCYQLYTKSFYQNILKpKLSPNGIFVTQ 215
Cdd:cd02440   76 LHHLVEDLARFLEEARR-LLKPGGVLVLT 103
TRM1 COG1867
tRNA G26 N,N-dimethylase Trm1 [Translation, ribosomal structure and biogenesis]; tRNA G26 N, ...
125-183 2.15e-04

tRNA G26 N,N-dimethylase Trm1 [Translation, ribosomal structure and biogenesis]; tRNA G26 N,N-dimethylase Trm1 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441472  Cd Length: 383  Bit Score: 42.55  E-value: 2.15e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 145334519 125 KVVMCDIDQEVVDFCRRFLTVNSDAFCnkklELVIKDAKAELEKREEKFDIIvgDLaDP 183
Cdd:COG1867   82 KVTLNDIDPEAVELIRENLELNGLEDV----EVYNRDANALLHELGRRFDVV--DL-DP 133
MFS_SpdSyn NF037959
fused MFS/spermidine synthase; Proteins of this family are fusion of a N-terminal MFS (Major ...
92-250 8.48e-04

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: 40.98  E-value: 8.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519  92 PALLFHPNPKTVFIMGGGEGSAAREILKHTTIEKVVMCDIDQEVVDFCRRFLTVNSDAFcnkklELVIKDAKAELEKR-E 170
Cdd:NF037959 268 ARLRMGRADFSAFFIGGGAYTLPRAWAARRPAGRITVAEIDPAVTRVAAEDFWFDPASA-----TVLHEDARRALRRRpE 342
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 171 EKFDIIVGD----LADPveggpcYQLYTKSFYQnILKPKLSPNGIFVTQAgpagI--FTHKEVFTSIYNTMKQVFKYVKA 244
Cdd:NF037959 343 ERFDVIVGDaftdIAVP------AHLVTREFFE-LVRARLTPDGVYLMNV----IdhADRLRALAALVATLREVFPVVEV 411

                 ....*.
gi 145334519 245 YTAHVP 250
Cdd:NF037959 412 WTEARP 417
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
107-177 4.71e-03

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 36.00  E-value: 4.71e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145334519  107 GGGEGSAAREILKHTTIEkVVMCDIDQEVVDFCRRFLtvnsdAFCNKKLELVIKDAkAELEKREEKFDIIV 177
Cdd:pfam13649   5 GCGTGRLTLALARRGGAR-VTGVDLSPEMLERARERA-----AEAGLNVEFVQGDA-EDLPFPDGSFDLVV 68
PIN_FAM120B-like cd18672
FEN-like PIN domains of FAM120B (family with sequence similarity 120B) and related proteins; ...
68-141 4.72e-03

FEN-like PIN domains of FAM120B (family with sequence similarity 120B) and related proteins; FAM120B (also known as CCPG, "constitutive coactivator of PPAR-gamma", PGCC1, "PPARgamma constitutive coactivator 1") is a constitutive coactivator of peroxisome proliferator-activated receptor (PPARgamma) that promotes adipogenesis in a PPARgamma-dependent manner. This subfamily belongs to the structure-specific, 5' nuclease family (FEN-like) that catalyzes hydrolysis of DNA duplex-containing nucleic acid structures during DNA replication, repair, and recombination. Canonical members of the FEN-like family possess a PIN domain with a two-helical structure insert (also known as the helical arch, helical clamp or I domain) of variable length (approximately 16 to 800 residues), the helical arch/clamp region is involved in DNA binding. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its putative active center, consisting of invariant acidic amino acid residues (putative metal-binding residues), is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons.


Pssm-ID: 350239 [Multi-domain]  Cd Length: 210  Bit Score: 37.66  E-value: 4.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519  68 VLVIDGKMQSAERDEFI---------YHECLIHPALLFHPNPKTVFIMGGGEGSAAREILKHTTIEkvVMC---DIDQEV 135
Cdd:cd18672   83 VFFFDGVVESQKRDEWVkrrlknnkkVSKVFNHIKKKGTQPPKNLFFLPSGLATFTRFALRSLGVE--VICsmdEADQEV 160

                 ....*.
gi 145334519 136 VDFCRR 141
Cdd:cd18672  161 ASYCRQ 166
 
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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