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Conserved domains on  [gi|2111842747|gb|KAH0994262|]
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hypothetical protein GBA52_005745 [Prunus armeniaca]

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
 25-329 0e+00

spermine synthase


:

Pssm-ID: 178418 [Multi-domain]  Cd Length: 336  Bit Score: 609.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111842747  25 KAHSVLNGYRKSCWYEEEIEENLRWSFALNSILHTGATPYQDIALLDTKPFGKALVIDGKLQSAETDEFIYHECLVHPPL 104
Cdd:PLN02823   19 PTAALASNYAKSLWYEEEIEDDLRWSYAVNSVLHTGTSEFQDIALVDTKPFGKVLIIDGKMQSAEADEFVYHESLVHPAL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111842747 105 LHHPNPKNIFIMGGGEGSTARELLRHRTVEKVVMCDIDEEVVEFCKSYLIVNSEAFCDPRLELIINDARAELEHREEQYD 184
Cdd:PLN02823   99 LHHPNPKTVFIMGGGEGSTAREVLRHKTVEKVVMCDIDQEVVDFCRKHLTVNREAFCDKRLELIINDARAELEKRDEKFD 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111842747 185 VIIGDLADPIEGGPCYKLYTKSFYELIVKPRLSKEGIFVTQAGPAGIFSHTEVFSCIYNTLRQVFKYVVPYSAHVPSYAD 264
Cdd:PLN02823  179 VIIGDLADPVEGGPCYQLYTKSFYERIVKPKLNPGGIFVTQAGPAGILTHKEVFSSIYNTLRQVFKYVVPYTAHVPSFAD 258

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2111842747 265 IWGWIMASDTPF-ELSTDELDLRIKQRIKGENRYLDGKTLSSASTLSKAVRQSMDNETHVYTEGTA 329
Cdd:PLN02823  259 TWGWVMASDHPFaDLSAEELDSRIKERIDGELKYLDGETFSSAFALNKTVRQALANETHVYTEENA 324
HNHc super family cl00083
HNH nucleases; HNH endonuclease signature which is found in viral, prokaryotic, and eukaryotic ...
 355-388 3.40e-03

HNH nucleases; HNH endonuclease signature which is found in viral, prokaryotic, and eukaryotic proteins. The alignment includes members of the large group of homing endonucleases, yeast intron 1 protein, MutS, as well as bacterial colicins, pyocins, and anaredoxins.


The actual alignment was detected with superfamily member TIGR02646:

Pssm-ID: 469607 [Multi-domain]  Cd Length: 144  Bit Score: 37.88  E-value: 3.40e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2111842747 355 CCMCKGVMDLEDEHVERF--QSHYPILEFEQHNPFA 388
Cdd:TIGR02646  27 CAYCEREIELLGSHIEHFrpKGAYPPLTLDWSNLFG 62
 
Name Accession Description Interval E-value
PLN02823 PLN02823
spermine synthase
 25-329 0e+00

spermine synthase


Pssm-ID: 178418 [Multi-domain]  Cd Length: 336  Bit Score: 609.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111842747  25 KAHSVLNGYRKSCWYEEEIEENLRWSFALNSILHTGATPYQDIALLDTKPFGKALVIDGKLQSAETDEFIYHECLVHPPL 104
Cdd:PLN02823   19 PTAALASNYAKSLWYEEEIEDDLRWSYAVNSVLHTGTSEFQDIALVDTKPFGKVLIIDGKMQSAEADEFVYHESLVHPAL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111842747 105 LHHPNPKNIFIMGGGEGSTARELLRHRTVEKVVMCDIDEEVVEFCKSYLIVNSEAFCDPRLELIINDARAELEHREEQYD 184
Cdd:PLN02823   99 LHHPNPKTVFIMGGGEGSTAREVLRHKTVEKVVMCDIDQEVVDFCRKHLTVNREAFCDKRLELIINDARAELEKRDEKFD 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111842747 185 VIIGDLADPIEGGPCYKLYTKSFYELIVKPRLSKEGIFVTQAGPAGIFSHTEVFSCIYNTLRQVFKYVVPYSAHVPSYAD 264
Cdd:PLN02823  179 VIIGDLADPVEGGPCYQLYTKSFYERIVKPKLNPGGIFVTQAGPAGILTHKEVFSSIYNTLRQVFKYVVPYTAHVPSFAD 258

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2111842747 265 IWGWIMASDTPF-ELSTDELDLRIKQRIKGENRYLDGKTLSSASTLSKAVRQSMDNETHVYTEGTA 329
Cdd:PLN02823  259 TWGWVMASDHPFaDLSAEELDSRIKERIDGELKYLDGETFSSAFALNKTVRQALANETHVYTEENA 324
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
76-271 2.42e-77

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


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 237.80  E-value: 2.42e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111842747  76 GKALVIDGKLQSA-ETDEFIYHECLVHPPLLHHPNPKNIFIMGGGEGSTARELLRHRTVEKVVMCDIDEEVVEFCKSYLI 154
Cdd:COG0421     3 GRVLVLDGVVQSTmELDEFEYHEMMAHVPLLFHPNPKRVLIIGGGDGGLARELLKHPPVERVDVVEIDPEVVELAREYFP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111842747 155 VNSEAFCDPRLELIINDARAELEHREEQYDVIIGDLADPIegGPCYKLYTKSFYELiVKPRLSKEGIFVTQAGpaGIFSH 234
Cdd:COG0421    83 LLAPAFDDPRLRVVIGDGRAFLREAEESYDVIIVDLTDPV--GPAEGLFTREFYED-CRRALKPGGVLVVNLG--SPFYG 157

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2111842747 235 TEVFSCIYNTLRQVFKYVVPYSAHVPSYADIWGWIMA 271
Cdd:COG0421   158 LDLLRRVLATLREVFPHVVLYAAPVPTYGGGNVFLLA 194
speE TIGR00417
spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine ...
 38-311 7.10e-74

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: 231.55  E-value: 7.10e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111842747  38 WYEEEIEENLRWSFALNSILHTGATPYQDIALLDTKPFGKALVIDGKLQSAETDEFIYHECLVHPPLLHHPNPKNIFIMG 117
Cdd:TIGR00417   1 WFTEYHDKNFGLTMKVDKVLYHEKSEFQDLEIFETEAFGNVLVLDGVVQTTERDEFIYHEMITHVPLFTHPNPKHVLVIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111842747 118 GGEGSTARELLRHRTVEKVVMCDIDEEVVEFCKSYLIVNSEAFCDPRLELIINDARAELEHREEQYDVIIGDLADPIegG 197
Cdd:TIGR00417  81 GGDGGVLREVLKHKSVESATLVDIDEKVIELSRKYLPNLAGSYDDPRVKLVIDDGFKFLADTENTFDVIIVDSTDPV--G 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111842747 198 PCYKLYTKSFYELIvKPRLSKEGIFVTQAGpaGIFSHTEVFSCIYNTLRQVFKYVVPYSAHVPSY-ADIWGWIMASDTPF 276
Cdd:TIGR00417 159 PAETLFTKEFYELL-KKALNPDGIFVAQSE--SPWLQLELIIDLKRKLKEAFPITEYYTAAIPTYpSGLWTFTIASKNKY 235

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2111842747 277 E-LSTDelDLRIKQRIK-GENRYLDGKTLSSASTLSK 311
Cdd:TIGR00417 236 RpLEVE--IRRIKFEAEdGKTKYYNPDIHKAAFVLPK 270
Spermine_synth pfam01564
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ...
 92-276 2.21e-51

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: 170.58  E-value: 2.21e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111842747  92 EFIYHECLVHPPLLHHPNPKNIFIMGGGEGSTARELLRHRTVEKVVMCDIDEEVVEFCKSYLIVNSEAFCDPRLELIIND 171
Cdd:pfam01564   1 EFIYHEMIAHVPLCSHPNPKKVLIIGGGDGGVLREVVKHPSVEKITLVDIDEKVIDFSKKFLPSLAIGFQDPRVKVVIGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111842747 172 ARAELEHREEQYDVIIGDLADPIegGPCYKLYTKSFYELIVKpRLSKEGIFVTQAGpaGIFSHTEVFSCIYNTLRQVFKY 251
Cdd:pfam01564  81 GFKFLKDYLNTFDVIIVDSTDPV--GPAENLFSKPFFDLLKK-ALKEDGVFITQAE--SPWLHLELIINILKNGKQVFPV 155

                         170       180
                  ....*....|....*....|....*.
gi 2111842747 252 VVPYSAHVPSYAD-IWGWIMASDTPF 276
Cdd:pfam01564 156 VMPYVATIPTYPSgGWGFTVCSKNPL 181
MFS_SpdSyn NF037959
fused MFS/spermidine synthase; Proteins of this family are fusion of a N-terminal MFS (Major ...
 103-252 8.13e-07

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: 51.00  E-value: 8.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111842747 103 PLLHHPNPK-NIFIMGGGEGSTARELLRHRTVEKVVMCDIDEEVVEFCKSYLivnseaFCDP-RLELIINDARAELEHR- 179
Cdd:NF037959  268 ARLRMGRADfSAFFIGGGAYTLPRAWAARRPAGRITVAEIDPAVTRVAAEDF------WFDPaSATVLHEDARRALRRRp 341

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2111842747 180 EEQYDVIIGD----LADPieggpcYKLYTKSFYELiVKPRLSKEGIFVTQAgpagI--FSHTEVFSCIYNTLRQVFKYV 252
Cdd:NF037959  342 EERFDVIVGDaftdIAVP------AHLVTREFFEL-VRARLTPDGVYLMNV----IdhADRLRALAALVATLREVFPVV 409
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 117-225 1.07e-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: 47.04  E-value: 1.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111842747 117 GGGEGSTARELLRHRtVEKVVMCDIDEEVVEFCKSylivNSEAFCDPRLELIINDARAELEHREEQYDVIIGDLAdpieg 196
Cdd:cd02440     6 GCGTGALALALASGP-GARVTGVDISPVALELARK----AAAALLADNVEVLKGDAEELPPEADESFDVIISDPP----- 75

                          90       100
                  ....*....|....*....|....*....
gi 2111842747 197 GPCYKLYTKSFYELIVKpRLSKEGIFVTQ 225
Cdd:cd02440    76 LHHLVEDLARFLEEARR-LLKPGGVLVLT 103
TIGR02646 TIGR02646
TIGR02646 family protein; Members of this uncharacterized protein family are found exclusively ...
 355-388 3.40e-03

TIGR02646 family protein; Members of this uncharacterized protein family are found exclusively in bacteria. Neighboring genes in various genomes are also uncharacterized or may annotated as similar to restriction system proteins. [Hypothetical proteins, Conserved]


Pssm-ID: 131694 [Multi-domain]  Cd Length: 144  Bit Score: 37.88  E-value: 3.40e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2111842747 355 CCMCKGVMDLEDEHVERF--QSHYPILEFEQHNPFA 388
Cdd:TIGR02646  27 CAYCEREIELLGSHIEHFrpKGAYPPLTLDWSNLFG 62
 
Name Accession Description Interval E-value
PLN02823 PLN02823
spermine synthase
 25-329 0e+00

spermine synthase


Pssm-ID: 178418 [Multi-domain]  Cd Length: 336  Bit Score: 609.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111842747  25 KAHSVLNGYRKSCWYEEEIEENLRWSFALNSILHTGATPYQDIALLDTKPFGKALVIDGKLQSAETDEFIYHECLVHPPL 104
Cdd:PLN02823   19 PTAALASNYAKSLWYEEEIEDDLRWSYAVNSVLHTGTSEFQDIALVDTKPFGKVLIIDGKMQSAEADEFVYHESLVHPAL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111842747 105 LHHPNPKNIFIMGGGEGSTARELLRHRTVEKVVMCDIDEEVVEFCKSYLIVNSEAFCDPRLELIINDARAELEHREEQYD 184
Cdd:PLN02823   99 LHHPNPKTVFIMGGGEGSTAREVLRHKTVEKVVMCDIDQEVVDFCRKHLTVNREAFCDKRLELIINDARAELEKRDEKFD 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111842747 185 VIIGDLADPIEGGPCYKLYTKSFYELIVKPRLSKEGIFVTQAGPAGIFSHTEVFSCIYNTLRQVFKYVVPYSAHVPSYAD 264
Cdd:PLN02823  179 VIIGDLADPVEGGPCYQLYTKSFYERIVKPKLNPGGIFVTQAGPAGILTHKEVFSSIYNTLRQVFKYVVPYTAHVPSFAD 258

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2111842747 265 IWGWIMASDTPF-ELSTDELDLRIKQRIKGENRYLDGKTLSSASTLSKAVRQSMDNETHVYTEGTA 329
Cdd:PLN02823  259 TWGWVMASDHPFaDLSAEELDSRIKERIDGELKYLDGETFSSAFALNKTVRQALANETHVYTEENA 324
PRK00811 PRK00811
polyamine aminopropyltransferase;
38-315 6.95e-92

polyamine aminopropyltransferase;


Pssm-ID: 234843 [Multi-domain]  Cd Length: 283  Bit Score: 278.19  E-value: 6.95e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111842747  38 WYEEEIEENLRWSFALNSILHTGATPYQDIALLDTKPFGKALVIDGKLQSAETDEFIYHECLVHPPLLHHPNPKNIFIMG 117
Cdd:PRK00811    5 WFTETLTDNYGQSFRVKKVLYEEKSPFQRIEIFETPEFGRLLALDGCVMTTERDEFIYHEMMTHVPLFAHPNPKRVLIIG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111842747 118 GGEGSTARELLRHRTVEKVVMCDIDEEVVEFCKSYL-IVNSEAFCDPRLELIINDARAELEHREEQYDVIIGDLADPIeg 196
Cdd:PRK00811   85 GGDGGTLREVLKHPSVEKITLVEIDERVVEVCRKYLpEIAGGAYDDPRVELVIGDGIKFVAETENSFDVIIVDSTDPV-- 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111842747 197 GPCYKLYTKSFYELIVKpRLSKEGIFVTQAG-PagiFSHTEVFSCIYNTLRQVFKYVVPYSAHVPSY-ADIWGWIMASDT 274
Cdd:PRK00811  163 GPAEGLFTKEFYENCKR-ALKEDGIFVAQSGsP---FYQADEIKDMHRKLKEVFPIVRPYQAAIPTYpSGLWSFTFASKN 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 2111842747 275 PF--ELSTDELDLRIKQRiKGENRYLDGKTLSSASTLSKAVRQ 315
Cdd:PRK00811  239 DDlkFLPLDVIEARFAER-GIKTRYYNPELHKAAFALPQFVKD 280
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
76-271 2.42e-77

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


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 237.80  E-value: 2.42e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111842747  76 GKALVIDGKLQSA-ETDEFIYHECLVHPPLLHHPNPKNIFIMGGGEGSTARELLRHRTVEKVVMCDIDEEVVEFCKSYLI 154
Cdd:COG0421     3 GRVLVLDGVVQSTmELDEFEYHEMMAHVPLLFHPNPKRVLIIGGGDGGLARELLKHPPVERVDVVEIDPEVVELAREYFP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111842747 155 VNSEAFCDPRLELIINDARAELEHREEQYDVIIGDLADPIegGPCYKLYTKSFYELiVKPRLSKEGIFVTQAGpaGIFSH 234
Cdd:COG0421    83 LLAPAFDDPRLRVVIGDGRAFLREAEESYDVIIVDLTDPV--GPAEGLFTREFYED-CRRALKPGGVLVVNLG--SPFYG 157

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2111842747 235 TEVFSCIYNTLRQVFKYVVPYSAHVPSYADIWGWIMA 271
Cdd:COG0421   158 LDLLRRVLATLREVFPHVVLYAAPVPTYGGGNVFLLA 194
speE TIGR00417
spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine ...
 38-311 7.10e-74

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: 231.55  E-value: 7.10e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111842747  38 WYEEEIEENLRWSFALNSILHTGATPYQDIALLDTKPFGKALVIDGKLQSAETDEFIYHECLVHPPLLHHPNPKNIFIMG 117
Cdd:TIGR00417   1 WFTEYHDKNFGLTMKVDKVLYHEKSEFQDLEIFETEAFGNVLVLDGVVQTTERDEFIYHEMITHVPLFTHPNPKHVLVIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111842747 118 GGEGSTARELLRHRTVEKVVMCDIDEEVVEFCKSYLIVNSEAFCDPRLELIINDARAELEHREEQYDVIIGDLADPIegG 197
Cdd:TIGR00417  81 GGDGGVLREVLKHKSVESATLVDIDEKVIELSRKYLPNLAGSYDDPRVKLVIDDGFKFLADTENTFDVIIVDSTDPV--G 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111842747 198 PCYKLYTKSFYELIvKPRLSKEGIFVTQAGpaGIFSHTEVFSCIYNTLRQVFKYVVPYSAHVPSY-ADIWGWIMASDTPF 276
Cdd:TIGR00417 159 PAETLFTKEFYELL-KKALNPDGIFVAQSE--SPWLQLELIIDLKRKLKEAFPITEYYTAAIPTYpSGLWTFTIASKNKY 235

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2111842747 277 E-LSTDelDLRIKQRIK-GENRYLDGKTLSSASTLSK 311
Cdd:TIGR00417 236 RpLEVE--IRRIKFEAEdGKTKYYNPDIHKAAFVLPK 270
PRK03612 PRK03612
polyamine aminopropyltransferase;
38-314 4.54e-62

polyamine aminopropyltransferase;


Pssm-ID: 235139 [Multi-domain]  Cd Length: 521  Bit Score: 208.54  E-value: 4.54e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111842747  38 WYEEEIEENLRWSFALNSILHTGATPYQDIAL---LDTKPFGKALVIDGKLQSAETDEFIYHECLVHPPLLHHPNPKNIF 114
Cdd:PRK03612  223 VLADRIETTAEQLLYGDPVVYAEQTPYQRIVVtrrGNGRGPDLRLYLNGRLQFSSRDEYRYHEALVHPAMAASARPRRVL 302

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111842747 115 IMGGGEGSTARELLRHRTVEKVVMCDIDEEVVEFCKSYLIV---NSEAFCDPRLELIINDARAELEHREEQYDVIIGDLA 191
Cdd:PRK03612  303 VLGGGDGLALREVLKYPDVEQVTLVDLDPAMTELARTSPALralNGGALDDPRVTVVNDDAFNWLRKLAEKFDVIIVDLP 382

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111842747 192 DP--IEGGpcyKLYTKSFYELiVKPRLSKEGIFVTQAGPAgiFSHTEVFSCIYNTLRQVFKYVVPYSAHVPSYADiWGWI 269
Cdd:PRK03612  383 DPsnPALG---KLYSVEFYRL-LKRRLAPDGLLVVQSTSP--YFAPKAFWSIEATLEAAGLATTPYHVNVPSFGE-WGFV 455

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2111842747 270 MASDTPfelstdELDLRIKQRIKGENRYLDGKTLSSASTLSKAVR 314
Cdd:PRK03612  456 LAGAGA------RPPLAVPTELPVPLRFLDPALLAAAFVFPKDMR 494
COG4262 COG4262
Predicted spermidine synthase with an N-terminal membrane domain [General function prediction ...
 56-249 3.98e-58

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


Pssm-ID: 443404 [Multi-domain]  Cd Length: 426  Bit Score: 195.47  E-value: 3.98e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111842747  56 ILHTGATPYQDIALLDTKPFgKALVIDGKLQSAETDEFIYHECLVHPPLLHHPNPKNIFIMGGGEGSTARELLRHRTVEK 135
Cdd:COG4262   234 VVYSEQTPYQRIVVTRDKDD-RRLYLNGNLQFSSLDEYRYHEALVHPPMAAHPRPRRVLVLGGGDGLAAREVLKYPDVES 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111842747 136 VVMCDIDEEVVEFCKSYLI---VNSEAFCDPRLELIINDARAELEHREEQYDVIIGDLADPIEGGPcYKLYTKSFYELiV 212
Cdd:COG4262   313 VTLVDLDPEVTDLAKTNPFlreLNGGALNDPRVTVVNADAFQFLRETDEKYDVIIVDLPDPSNFSL-GKLYSVEFYRL-V 390

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2111842747 213 KPRLSKEGIFVTQAGPAGIFShtEVFSCIYNTLRQVF 249
Cdd:COG4262   391 RRHLAPGGVLVVQATSPYFAP--KAFWCIAKTLEAAG 425
Spermine_synth pfam01564
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ...
 92-276 2.21e-51

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: 170.58  E-value: 2.21e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111842747  92 EFIYHECLVHPPLLHHPNPKNIFIMGGGEGSTARELLRHRTVEKVVMCDIDEEVVEFCKSYLIVNSEAFCDPRLELIIND 171
Cdd:pfam01564   1 EFIYHEMIAHVPLCSHPNPKKVLIIGGGDGGVLREVVKHPSVEKITLVDIDEKVIDFSKKFLPSLAIGFQDPRVKVVIGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111842747 172 ARAELEHREEQYDVIIGDLADPIegGPCYKLYTKSFYELIVKpRLSKEGIFVTQAGpaGIFSHTEVFSCIYNTLRQVFKY 251
Cdd:pfam01564  81 GFKFLKDYLNTFDVIIVDSTDPV--GPAENLFSKPFFDLLKK-ALKEDGVFITQAE--SPWLHLELIINILKNGKQVFPV 155

                         170       180
                  ....*....|....*....|....*.
gi 2111842747 252 VVPYSAHVPSYAD-IWGWIMASDTPF 276
Cdd:pfam01564 156 VMPYVATIPTYPSgGWGFTVCSKNPL 181
PLN02366 PLN02366
spermidine synthase
 50-262 5.40e-48

spermidine synthase


Pssm-ID: 215208 [Multi-domain]  Cd Length: 308  Bit Score: 165.59  E-value: 5.40e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111842747  50 SFALNSILHTGATPYQDIALLDTKPFGKALVIDGKLQSAETDEFIYHECLVHPPLLHHPNPKNIFIMGGGEGSTARELLR 129
Cdd:PLN02366   32 SLKVEKVLFQGKSDFQDVLVFESATYGKVLVLDGVIQLTERDECAYQEMITHLPLCSIPNPKKVLVVGGGDGGVLREIAR 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111842747 130 HRTVEKVVMCDIDEEVVEFCKSYLIVNSEAFCDPRLELIINDARAELEH-REEQYDVIIGDLADPIegGPCYKLYTKSFY 208
Cdd:PLN02366  112 HSSVEQIDICEIDKMVIDVSKKFFPDLAVGFDDPRVNLHIGDGVEFLKNaPEGTYDAIIVDSSDPV--GPAQELFEKPFF 189

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2111842747 209 ELIVKPrLSKEGIFVTQAgpAGIFSHTEVFSCIYNTLRQVFKYVVPY-SAHVPSY 262
Cdd:PLN02366  190 ESVARA-LRPGGVVCTQA--ESMWLHMDLIEDLIAICRETFKGSVNYaWTTVPTY 241
speE PRK01581
polyamine aminopropyltransferase;
64-282 1.23e-32

polyamine aminopropyltransferase;


Pssm-ID: 234961 [Multi-domain]  Cd Length: 374  Bit Score: 126.23  E-value: 1.23e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111842747  64 YQDIALLDTKPFgkALVIDGKLQSAETDEFIYHECLVHPPLLHHPNPKNIFIMGGGEGSTARELLRHRTVEKVVMCDIDE 143
Cdd:PRK01581  107 YQNINLLQVSDI--RLYLDKQLQFSSVDEQIYHEALVHPIMSKVIDPKRVLILGGGDGLALREVLKYETVLHVDLVDLDG 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111842747 144 EVVEFCKS---YLIVNSEAFCDPRLELIINDARAELEHREEQYDVIIGDLADPIEgGPCYKLYTKSFYELIVKpRLSKEG 220
Cdd:PRK01581  185 SMINMARNvpeLVSLNKSAFFDNRVNVHVCDAKEFLSSPSSLYDVIIIDFPDPAT-ELLSTLYTSELFARIAT-FLTEDG 262

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2111842747 221 IFVTQA-GPAgifSHTEVFSCIYNTLRQVFKYVVPYSAHVPSYADIWGWIMASDTPFELSTDE 282
Cdd:PRK01581  263 AFVCQSnSPA---DAPLVYWSIGNTIEHAGLTVKSYHTIVPSFGTDWGFHIAANSAYVLDQIE 322
Spermine_synt_N pfam17284
Spermidine synthase tetramerization domain; This domain represents the N-terminal ...
 38-89 3.23e-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: 58.06  E-value: 3.23e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2111842747  38 WYEEEIEENLRWSFALNSILHTGATPYQDIALLDTKPFGKALVIDGKLQSAE 89
Cdd:pfam17284   2 WFTEIHDLGQALEYKVEKVLYDEKSEYQDIEIFESKTFGNVLVLDGVVQLTE 53
PRK04457 PRK04457
polyamine aminopropyltransferase;
104-224 4.44e-07

polyamine aminopropyltransferase;


Pssm-ID: 179854 [Multi-domain]  Cd Length: 262  Bit Score: 50.81  E-value: 4.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111842747 104 LLHHPNPKNIFIMGGGEGSTARELLRHRTVEKVVMCDIDEEVVEFCKSYLIVNSEafcDPRLELIINDARAELEHREEQY 183
Cdd:PRK04457   61 LLFNPRPQHILQIGLGGGSLAKFIYTYLPDTRQTAVEINPQVIAVARNHFELPEN---GERFEVIEADGAEYIAVHRHST 137

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2111842747 184 DVIIGDLADpiEGGPCYKLYTKSFYElIVKPRLSKEGIFVT 224
Cdd:PRK04457  138 DVILVDGFD--GEGIIDALCTQPFFD-DCRNALSSDGIFVV 175
MFS_SpdSyn NF037959
fused MFS/spermidine synthase; Proteins of this family are fusion of a N-terminal MFS (Major ...
 103-252 8.13e-07

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: 51.00  E-value: 8.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111842747 103 PLLHHPNPK-NIFIMGGGEGSTARELLRHRTVEKVVMCDIDEEVVEFCKSYLivnseaFCDP-RLELIINDARAELEHR- 179
Cdd:NF037959  268 ARLRMGRADfSAFFIGGGAYTLPRAWAARRPAGRITVAEIDPAVTRVAAEDF------WFDPaSATVLHEDARRALRRRp 341

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2111842747 180 EEQYDVIIGD----LADPieggpcYKLYTKSFYELiVKPRLSKEGIFVTQAgpagI--FSHTEVFSCIYNTLRQVFKYV 252
Cdd:NF037959  342 EERFDVIVGDaftdIAVP------AHLVTREFFEL-VRARLTPDGVYLMNV----IdhADRLRALAALVATLREVFPVV 409
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 117-225 1.07e-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: 47.04  E-value: 1.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111842747 117 GGGEGSTARELLRHRtVEKVVMCDIDEEVVEFCKSylivNSEAFCDPRLELIINDARAELEHREEQYDVIIGDLAdpieg 196
Cdd:cd02440     6 GCGTGALALALASGP-GARVTGVDISPVALELARK----AAAALLADNVEVLKGDAEELPPEADESFDVIISDPP----- 75

                          90       100
                  ....*....|....*....|....*....
gi 2111842747 197 GPCYKLYTKSFYELIVKpRLSKEGIFVTQ 225
Cdd:cd02440    76 LHHLVEDLARFLEEARR-LLKPGGVLVLT 103
speE PRK00536
spermidine synthase; Provisional
 38-272 4.43e-06

spermidine synthase; Provisional


Pssm-ID: 134311 [Multi-domain]  Cd Length: 262  Bit Score: 47.93  E-value: 4.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111842747  38 WYEEEIEENLRWSFALNSILHTGATPYQDIALLDTKPFGKALVIDGKLQsAETDEFIYHECLVHPPLLHHPNPKNIFIMG 117
Cdd:PRK00536    2 WITQEITPYLRKEYTIEAKLLDVRSEHNILEIFKSKDFGEIAMLNKQLL-FKNFLHIESELLAHMGGCTKKELKEVLIVD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111842747 118 GGEGSTARELLRHRTveKVVMCDIDEEVVEFCKSYLIVNSEAFCDPRLELiindARAELEHREEQYDVIIGD-LADPIEG 196
Cdd:PRK00536   81 GFDLELAHQLFKYDT--HVDFVQADEKILDSFISFFPHFHEVKNNKNFTH----AKQLLDLDIKKYDLIICLqEPDIHKI 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2111842747 197 GPcyklytksfyeliVKPRLSKEGIFVTQAgpAGIFSHTEVFSCIYNTLRQVFKYVVPYSAHVPSYADIwGWIMAS 272
Cdd:PRK00536  155 DG-------------LKRMLKEDGVFISVA--KHPLLEHVSMQNALKNMGDFFSIAMPFVAPLRILSNK-GYIYAS 214
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 117-187 2.70e-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: 2.70e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2111842747 117 GGGEGSTARELLRhRTVEKVVMCDIDEEVVEFCKSYLivnseAFCDPRLELIINDARaELEHREEQYDVII 187
Cdd:pfam13649   5 GCGTGRLTLALAR-RGGARVTGVDLSPEMLERARERA-----AEAGLNVEFVQGDAE-DLPFPDGSFDLVV 68
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 106-187 4.90e-05

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: 42.70  E-value: 4.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111842747 106 HHPNPKNIFIMGGGEGSTARELLRHrtVEKVVMCDIDEEVVEFCKsylivnsEAFCDPRLELIINDARaELEHREEQYDV 185
Cdd:COG2227    21 LLPAGGRVLDVGCGTGRLALALARR--GADVTGVDISPEALEIAR-------ERAAELNVDFVQGDLE-DLPLEDGSFDL 90


                  ..
gi 2111842747 186 II 187
Cdd:COG2227    91 VI 92
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 135-223 2.27e-04

tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; tRNA 5-hydroxyU34 O-methylase TrmR/YrrM is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443298  Cd Length: 173  Bit Score: 41.71  E-value: 2.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111842747 135 KVVMCDIDEEVVEFCKSYLivnSEAFCDPRLELIINDARAELEH-REEQYDVIIGDlADPIEggpcYKLYtksfYELIVk 213
Cdd:COG4122    43 RLTTIEIDPERAAIARENF---ARAGLADRIRLILGDALEVLPRlADGPFDLVFID-ADKSN----YPDY----LELAL- 109

                          90
                  ....*....|
gi 2111842747 214 PRLSKEGIFV 223
Cdd:COG4122   110 PLLRPGGLIV 119
PRK04338 PRK04338
N(2),N(2)-dimethylguanosine tRNA methyltransferase; Provisional
 133-193 3.34e-03

N(2),N(2)-dimethylguanosine tRNA methyltransferase; Provisional


Pssm-ID: 235286  Cd Length: 382  Bit Score: 39.51  E-value: 3.34e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2111842747 133 VEKVVMCDIDEEVVEFCKSYL----IVNSEAFCDprleliinDARAELeHREEQYDVIigDLaDP 193
Cdd:PRK04338   81 VEKVTLNDINPDAVELIKKNLelngLENEKVFNK--------DANALL-HEERKFDVV--DI-DP 133
TIGR02646 TIGR02646
TIGR02646 family protein; Members of this uncharacterized protein family are found exclusively ...
 355-388 3.40e-03

TIGR02646 family protein; Members of this uncharacterized protein family are found exclusively in bacteria. Neighboring genes in various genomes are also uncharacterized or may annotated as similar to restriction system proteins. [Hypothetical proteins, Conserved]


Pssm-ID: 131694 [Multi-domain]  Cd Length: 144  Bit Score: 37.88  E-value: 3.40e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2111842747 355 CCMCKGVMDLEDEHVERF--QSHYPILEFEQHNPFA 388
Cdd:TIGR02646  27 CAYCEREIELLGSHIEHFrpKGAYPPLTLDWSNLFG 62
 
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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