NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1084141239|gb|OGL37912|]
View 

hypothetical protein A3E49_01400 [Candidatus Saccharibacteria bacterium RIFCSPHIGHO2_12_FULL_49_19]

Protein Classification

fused MFS transporter/spermidine synthase family protein( domain architecture ID 1751050)

fused MFS transporter/spermidine synthase family protein may have a role outside of polyamine biosynthesis

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
MFS_SpdSyn super family cl41587
fused MFS/spermidine synthase; Proteins of this family are fusion of a N-terminal MFS (Major ...
 1-461 7.94e-61

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.


The actual alignment was detected with superfamily member NF037959:

Pssm-ID: 468290 [Multi-domain]  Cd Length: 480  Bit Score: 205.85  E-value: 7.94e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084141239   1 MIIELVGVRFIAPDFGTSIYVWTAIIGVILGALAFGYWYGGRLADKSAtDEGLMVI---FLLASVAWLASVWLRDSILEL 77
Cdd:NF037959    5 LVVEIVAGRMLAPYVGMSLYTWTAIIAVVLAGFSAGHWWGGRLAERPA-GRALRRTgwaLLAAALTTAAALLLLRLVAGP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084141239  78 AGAMPGGLRGQAFVASLLLFAPVSALLGMVSPYLVKLKLVNLKTAGRYVGGLYAAGTVGSIAGTFAAGYWLIPLFNSRAV 157
Cdd:NF037959   84 VLAAVLHPVAAIVALTLLLFFLPSLFAGVPAPVLTQLAVRGAERSGRALGAMFAAGAIGAIAGTLLAGFLFISWLGSAGT 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084141239 158 GWAM--VFALLGISLL---AQRRKLLIHRLIVAVAAVLLLVMPTQSSSNSGViydgdglYSRY---QVID-GRYHGRPVR 228
Cdd:NF037959  164 LLVVaaVYALLALLFLwlaGGRRRGLAAAALALLAALALAGLALAAPSPCDV-------ESRYfciRVVDvSADPGGPAR 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084141239 229 HLVTDKftLQSSIYIGD-------PYTPVLDYSTRMDeviVQSQPRRMLLIGGGSYTL--AQLAVLKNPKVTvdVVEIDP 299
Cdd:NF037959  237 LMVLDH--LAHGINARDdptvlftPYAAMLDELARLR---MGRADFSAFFIGGGAYTLprAWAARRPAGRIT--VAEIDP 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084141239 300 MLDELAVKYFSFKPDkRIKIIHEDGRTFLNKL-ETKYDLIVMDAFSSQFPPFQLTTVEVLEKIKESLTPGGLVMANIISA 378
Cdd:NF037959  310 AVTRVAAEDFWFDPA-SATVLHEDARRALRRRpEERFDVIVGDAFTDIAVPAHLVTREFFELVRARLTPDGVYLMNVIDH 388

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084141239 379 AEGPEAgfLQAQYLTYQEVF-NKAVAFQATPGANKAARLNVILLAAEDNNLSEYQKP----------EEGRVFLSINTSH 447
Cdd:NF037959  389 ADRLRA--LAALVATLREVFpVVEVWTEARPPAPGERRTFVLLAGDAPTPVSTIRARapeprrfarlPPAFVDALAARRS 466

                         490
                  ....*....|....
gi 1084141239 448 SKVLTDDFAPVEAL 461
Cdd:NF037959  467 PPVLTDDYAPIDRL 480
 
Name Accession Description Interval E-value
MFS_SpdSyn NF037959
fused MFS/spermidine synthase; Proteins of this family are fusion of a N-terminal MFS (Major ...
 1-461 7.94e-61

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: 205.85  E-value: 7.94e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084141239   1 MIIELVGVRFIAPDFGTSIYVWTAIIGVILGALAFGYWYGGRLADKSAtDEGLMVI---FLLASVAWLASVWLRDSILEL 77
Cdd:NF037959    5 LVVEIVAGRMLAPYVGMSLYTWTAIIAVVLAGFSAGHWWGGRLAERPA-GRALRRTgwaLLAAALTTAAALLLLRLVAGP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084141239  78 AGAMPGGLRGQAFVASLLLFAPVSALLGMVSPYLVKLKLVNLKTAGRYVGGLYAAGTVGSIAGTFAAGYWLIPLFNSRAV 157
Cdd:NF037959   84 VLAAVLHPVAAIVALTLLLFFLPSLFAGVPAPVLTQLAVRGAERSGRALGAMFAAGAIGAIAGTLLAGFLFISWLGSAGT 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084141239 158 GWAM--VFALLGISLL---AQRRKLLIHRLIVAVAAVLLLVMPTQSSSNSGViydgdglYSRY---QVID-GRYHGRPVR 228
Cdd:NF037959  164 LLVVaaVYALLALLFLwlaGGRRRGLAAAALALLAALALAGLALAAPSPCDV-------ESRYfciRVVDvSADPGGPAR 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084141239 229 HLVTDKftLQSSIYIGD-------PYTPVLDYSTRMDeviVQSQPRRMLLIGGGSYTL--AQLAVLKNPKVTvdVVEIDP 299
Cdd:NF037959  237 LMVLDH--LAHGINARDdptvlftPYAAMLDELARLR---MGRADFSAFFIGGGAYTLprAWAARRPAGRIT--VAEIDP 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084141239 300 MLDELAVKYFSFKPDkRIKIIHEDGRTFLNKL-ETKYDLIVMDAFSSQFPPFQLTTVEVLEKIKESLTPGGLVMANIISA 378
Cdd:NF037959  310 AVTRVAAEDFWFDPA-SATVLHEDARRALRRRpEERFDVIVGDAFTDIAVPAHLVTREFFELVRARLTPDGVYLMNVIDH 388

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084141239 379 AEGPEAgfLQAQYLTYQEVF-NKAVAFQATPGANKAARLNVILLAAEDNNLSEYQKP----------EEGRVFLSINTSH 447
Cdd:NF037959  389 ADRLRA--LAALVATLREVFpVVEVWTEARPPAPGERRTFVLLAGDAPTPVSTIRARapeprrfarlPPAFVDALAARRS 466

                         490
                  ....*....|....
gi 1084141239 448 SKVLTDDFAPVEAL 461
Cdd:NF037959  467 PPVLTDDYAPIDRL 480
COG4262 COG4262
Predicted spermidine synthase with an N-terminal membrane domain [General function prediction ...
 1-384 1.46e-39

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


Pssm-ID: 443404 [Multi-domain]  Cd Length: 426  Bit Score: 147.70  E-value: 1.46e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084141239   1 MIIELVGVRFIAPDFGTSIYVWTAIIGVILGALAFGYWYGGRLADKSATdeGLMVIFLLASVAWLASVWLrdsILELAGA 80
Cdd:COG4262    24 LVYELLLGRLASYLLGDSVLQFSIVIGVFLFAMGLGSYLSRRVADRLLR--AFIRLELLLALLGGLSALL---LFALFAF 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084141239  81 MPGGLrgqAFVASLLLFAPVSALLGMVSPYLVKLKLVNLKTAGRYVGGLYAAGTVGSIAGTFAAGYWLIPLFN-SRAVGW 159
Cdd:COG4262    99 LLGAL---FLLALYLLVLLIGLLIGAEIPLLMRLLERRREELGSAVGRVYAADYLGALVGSLLFPFLLLPALGlVRTALL 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084141239 160 -AMVFALLGISLLAQRRKLLIHRLIVAVAAVLLLVM--------PTQSSSNSGViYDGDGLY---SRYQVIDgRYHGRPV 227
Cdd:COG4262   176 fGLLNAAVALVLLWLFRKRLRRKALLAAAALVLAALlvglvfadPIESSAEQKL-YGDPVVYseqTPYQRIV-VTRDKDD 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084141239 228 RHLVTDKfTLQSSIYIGDPYT-----PVLdystrmdevIVQSQPRRMLLIGGGSyTLAQLAVLKNPKV-TVDVVEIDPML 301
Cdd:COG4262   254 RRLYLNG-NLQFSSLDEYRYHealvhPPM---------AAHPRPRRVLVLGGGD-GLAAREVLKYPDVeSVTLVDLDPEV 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084141239 302 DELAVKYFSFKP-------DKRIKIIHEDGRTFLNKLETKYDLIVMDAF-SSQFPPFQLTTVEVLEKIKESLTPGGLVMA 373
Cdd:COG4262   323 TDLAKTNPFLRElnggalnDPRVTVVNADAFQFLRETDEKYDVIIVDLPdPSNFSLGKLYSVEFYRLVRRHLAPGGVLVV 402

                         410
                  ....*....|.
gi 1084141239 374 NIISAAEGPEA 384
Cdd:COG4262   403 QATSPYFAPKA 413
PRK04457 PRK04457
polyamine aminopropyltransferase;
229-377 4.40e-15

polyamine aminopropyltransferase;


Pssm-ID: 179854 [Multi-domain]  Cd Length: 262  Bit Score: 75.08  E-value: 4.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084141239 229 HLVTDkfTLQSSIYIGDPYTPVLDYsTR--MDEVIVQSQPRRMLLIG--GGS---YTLAQLavlknPKVTVDVVEIDPML 301
Cdd:PRK04457   31 HLGSD--TVQSSMRIDDPSELELAY-TRamMGFLLFNPRPQHILQIGlgGGSlakFIYTYL-----PDTRQTAVEINPQV 102

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1084141239 302 DELAVKYFsFKP--DKRIKIIHEDGRTFLNKLETKYDLIVMDAFSSQFPPFQLTTVEVLEKIKESLTPGGLVMANIIS 377
Cdd:PRK04457  103 IAVARNHF-ELPenGERFEVIEADGAEYIAVHRHSTDVILVDGFDGEGIIDALCTQPFFDDCRNALSSDGIFVVNLWS 179
Spermine_synth pfam01564
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ...
 266-408 1.02e-10

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: 60.80  E-value: 1.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084141239 266 PRRMLLIGGGSytLAQL-AVLKNPKVT-VDVVEIDPMLDELAVKYF-SFK---PDKRIKIIHEDGRTFLNKLETKYDLIV 339
Cdd:pfam01564  19 PKKVLIIGGGD--GGVLrEVVKHPSVEkITLVDIDEKVIDFSKKFLpSLAigfQDPRVKVVIGDGFKFLKDYLNTFDVII 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1084141239 340 MDAFSSQFPPFQLTTVEVLEKIKESLTPGGLvmanIISAAEGPeagFLQAQYLTYQEVFNKAVAFQATP 408
Cdd:pfam01564  97 VDSTDPVGPAENLFSKPFFDLLKKALKEDGV----FITQAESP---WLHLELIINILKNGKQVFPVVMP 158
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 268-372 1.01e-07

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: 50.12  E-value: 1.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084141239 268 RMLLIGGGSYTLAqLAVLKNPKVTVDVVEIDPMLDELAVKYFSFKPDKRIKIIHEDGRTFLNKLETKYDLIVMDAFssqF 347
Cdd:cd02440     1 RVLDLGCGTGALA-LALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPEADESFDVIISDPP---L 76

                          90       100
                  ....*....|....*....|....*
gi 1084141239 348 PPFQLTTVEVLEKIKESLTPGGLVM 372
Cdd:cd02440    77 HHLVEDLARFLEEARRLLKPGGVLV 101
 
Name Accession Description Interval E-value
MFS_SpdSyn NF037959
fused MFS/spermidine synthase; Proteins of this family are fusion of a N-terminal MFS (Major ...
 1-461 7.94e-61

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: 205.85  E-value: 7.94e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084141239   1 MIIELVGVRFIAPDFGTSIYVWTAIIGVILGALAFGYWYGGRLADKSAtDEGLMVI---FLLASVAWLASVWLRDSILEL 77
Cdd:NF037959    5 LVVEIVAGRMLAPYVGMSLYTWTAIIAVVLAGFSAGHWWGGRLAERPA-GRALRRTgwaLLAAALTTAAALLLLRLVAGP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084141239  78 AGAMPGGLRGQAFVASLLLFAPVSALLGMVSPYLVKLKLVNLKTAGRYVGGLYAAGTVGSIAGTFAAGYWLIPLFNSRAV 157
Cdd:NF037959   84 VLAAVLHPVAAIVALTLLLFFLPSLFAGVPAPVLTQLAVRGAERSGRALGAMFAAGAIGAIAGTLLAGFLFISWLGSAGT 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084141239 158 GWAM--VFALLGISLL---AQRRKLLIHRLIVAVAAVLLLVMPTQSSSNSGViydgdglYSRY---QVID-GRYHGRPVR 228
Cdd:NF037959  164 LLVVaaVYALLALLFLwlaGGRRRGLAAAALALLAALALAGLALAAPSPCDV-------ESRYfciRVVDvSADPGGPAR 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084141239 229 HLVTDKftLQSSIYIGD-------PYTPVLDYSTRMDeviVQSQPRRMLLIGGGSYTL--AQLAVLKNPKVTvdVVEIDP 299
Cdd:NF037959  237 LMVLDH--LAHGINARDdptvlftPYAAMLDELARLR---MGRADFSAFFIGGGAYTLprAWAARRPAGRIT--VAEIDP 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084141239 300 MLDELAVKYFSFKPDkRIKIIHEDGRTFLNKL-ETKYDLIVMDAFSSQFPPFQLTTVEVLEKIKESLTPGGLVMANIISA 378
Cdd:NF037959  310 AVTRVAAEDFWFDPA-SATVLHEDARRALRRRpEERFDVIVGDAFTDIAVPAHLVTREFFELVRARLTPDGVYLMNVIDH 388

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084141239 379 AEGPEAgfLQAQYLTYQEVF-NKAVAFQATPGANKAARLNVILLAAEDNNLSEYQKP----------EEGRVFLSINTSH 447
Cdd:NF037959  389 ADRLRA--LAALVATLREVFpVVEVWTEARPPAPGERRTFVLLAGDAPTPVSTIRARapeprrfarlPPAFVDALAARRS 466

                         490
                  ....*....|....
gi 1084141239 448 SKVLTDDFAPVEAL 461
Cdd:NF037959  467 PPVLTDDYAPIDRL 480
COG4262 COG4262
Predicted spermidine synthase with an N-terminal membrane domain [General function prediction ...
 1-384 1.46e-39

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


Pssm-ID: 443404 [Multi-domain]  Cd Length: 426  Bit Score: 147.70  E-value: 1.46e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084141239   1 MIIELVGVRFIAPDFGTSIYVWTAIIGVILGALAFGYWYGGRLADKSATdeGLMVIFLLASVAWLASVWLrdsILELAGA 80
Cdd:COG4262    24 LVYELLLGRLASYLLGDSVLQFSIVIGVFLFAMGLGSYLSRRVADRLLR--AFIRLELLLALLGGLSALL---LFALFAF 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084141239  81 MPGGLrgqAFVASLLLFAPVSALLGMVSPYLVKLKLVNLKTAGRYVGGLYAAGTVGSIAGTFAAGYWLIPLFN-SRAVGW 159
Cdd:COG4262    99 LLGAL---FLLALYLLVLLIGLLIGAEIPLLMRLLERRREELGSAVGRVYAADYLGALVGSLLFPFLLLPALGlVRTALL 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084141239 160 -AMVFALLGISLLAQRRKLLIHRLIVAVAAVLLLVM--------PTQSSSNSGViYDGDGLY---SRYQVIDgRYHGRPV 227
Cdd:COG4262   176 fGLLNAAVALVLLWLFRKRLRRKALLAAAALVLAALlvglvfadPIESSAEQKL-YGDPVVYseqTPYQRIV-VTRDKDD 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084141239 228 RHLVTDKfTLQSSIYIGDPYT-----PVLdystrmdevIVQSQPRRMLLIGGGSyTLAQLAVLKNPKV-TVDVVEIDPML 301
Cdd:COG4262   254 RRLYLNG-NLQFSSLDEYRYHealvhPPM---------AAHPRPRRVLVLGGGD-GLAAREVLKYPDVeSVTLVDLDPEV 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084141239 302 DELAVKYFSFKP-------DKRIKIIHEDGRTFLNKLETKYDLIVMDAF-SSQFPPFQLTTVEVLEKIKESLTPGGLVMA 373
Cdd:COG4262   323 TDLAKTNPFLRElnggalnDPRVTVVNADAFQFLRETDEKYDVIIVDLPdPSNFSLGKLYSVEFYRLVRRHLAPGGVLVV 402

                         410
                  ....*....|.
gi 1084141239 374 NIISAAEGPEA 384
Cdd:COG4262   403 QATSPYFAPKA 413
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
228-422 9.58e-33

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


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 123.01  E-value: 9.58e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084141239 228 RHLVTDKfTLQSSIYIGdpytpVLDYSTRMDEV--IVQSQPRRMLLIGGGSYTLAQlAVLKNPKVT-VDVVEIDPMLDEL 304
Cdd:COG0421     4 RVLVLDG-VVQSTMELD-----EFEYHEMMAHVplLFHPNPKRVLIIGGGDGGLAR-ELLKHPPVErVDVVEIDPEVVEL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084141239 305 AVKYF----SFKPDKRIKIIHEDGRTFLNKLETKYDLIVMDAFSSQFPPFQLTTVEVLEKIKESLTPGGLVMANIISAAE 380
Cdd:COG0421    77 AREYFpllaPAFDDPRLRVVIGDGRAFLREAEESYDVIIVDLTDPVGPAEGLFTREFYEDCRRALKPGGVLVVNLGSPFY 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1084141239 381 GPEagFLQAQYLTYQEVFNKAVAFQAT-PGankAARLNVILLA 422
Cdd:COG0421   157 GLD--LLRRVLATLREVFPHVVLYAAPvPT---YGGGNVFLLA 194
PRK04457 PRK04457
polyamine aminopropyltransferase;
229-377 4.40e-15

polyamine aminopropyltransferase;


Pssm-ID: 179854 [Multi-domain]  Cd Length: 262  Bit Score: 75.08  E-value: 4.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084141239 229 HLVTDkfTLQSSIYIGDPYTPVLDYsTR--MDEVIVQSQPRRMLLIG--GGS---YTLAQLavlknPKVTVDVVEIDPML 301
Cdd:PRK04457   31 HLGSD--TVQSSMRIDDPSELELAY-TRamMGFLLFNPRPQHILQIGlgGGSlakFIYTYL-----PDTRQTAVEINPQV 102

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1084141239 302 DELAVKYFsFKP--DKRIKIIHEDGRTFLNKLETKYDLIVMDAFSSQFPPFQLTTVEVLEKIKESLTPGGLVMANIIS 377
Cdd:PRK04457  103 IAVARNHF-ELPenGERFEVIEADGAEYIAVHRHSTDVILVDGFDGEGIIDALCTQPFFDDCRNALSSDGIFVVNLWS 179
PRK00811 PRK00811
polyamine aminopropyltransferase;
265-370 4.26e-11

polyamine aminopropyltransferase;


Pssm-ID: 234843 [Multi-domain]  Cd Length: 283  Bit Score: 63.64  E-value: 4.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084141239 265 QPRRMLLIGGGSY-TLAQlaVLKNPKV-TVDVVEIDPMLDELAVKYF-----SFKPDKRIKIIHEDGRTFLNKLETKYDL 337
Cdd:PRK00811   76 NPKRVLIIGGGDGgTLRE--VLKHPSVeKITLVEIDERVVEVCRKYLpeiagGAYDDPRVELVIGDGIKFVAETENSFDV 153

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1084141239 338 IVMDafSSqfPPF----QLTTVEVLEKIKESLTPGGL 370
Cdd:PRK00811  154 IIVD--ST--DPVgpaeGLFTKEFYENCKRALKEDGI 186
Spermine_synth pfam01564
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ...
 266-408 1.02e-10

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: 60.80  E-value: 1.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084141239 266 PRRMLLIGGGSytLAQL-AVLKNPKVT-VDVVEIDPMLDELAVKYF-SFK---PDKRIKIIHEDGRTFLNKLETKYDLIV 339
Cdd:pfam01564  19 PKKVLIIGGGD--GGVLrEVVKHPSVEkITLVDIDEKVIDFSKKFLpSLAigfQDPRVKVVIGDGFKFLKDYLNTFDVII 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1084141239 340 MDAFSSQFPPFQLTTVEVLEKIKESLTPGGLvmanIISAAEGPeagFLQAQYLTYQEVFNKAVAFQATP 408
Cdd:pfam01564  97 VDSTDPVGPAENLFSKPFFDLLKKALKEDGV----FITQAESP---WLHLELIINILKNGKQVFPVVMP 158
PLN02366 PLN02366
spermidine synthase
 264-371 8.90e-10

spermidine synthase


Pssm-ID: 215208 [Multi-domain]  Cd Length: 308  Bit Score: 59.66  E-value: 8.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084141239 264 SQPRRMLLIGGGSY-TLAQLAvlKNPKV-TVDVVEIDPMLDELAVKYFS-----FKpDKRIKIIHEDGRTFL-NKLETKY 335
Cdd:PLN02366   90 PNPKKVLVVGGGDGgVLREIA--RHSSVeQIDICEIDKMVIDVSKKFFPdlavgFD-DPRVNLHIGDGVEFLkNAPEGTY 166

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1084141239 336 DLIVMDAFSSQFPPFQLTTVEVLEKIKESLTPGGLV 371
Cdd:PLN02366  167 DAIIVDSSDPVGPAQELFEKPFFESVARALRPGGVV 202
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 268-372 1.01e-07

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: 50.12  E-value: 1.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084141239 268 RMLLIGGGSYTLAqLAVLKNPKVTVDVVEIDPMLDELAVKYFSFKPDKRIKIIHEDGRTFLNKLETKYDLIVMDAFssqF 347
Cdd:cd02440     1 RVLDLGCGTGALA-LALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPEADESFDVIISDPP---L 76

                          90       100
                  ....*....|....*....|....*
gi 1084141239 348 PPFQLTTVEVLEKIKESLTPGGLVM 372
Cdd:cd02440    77 HHLVEDLARFLEEARRLLKPGGVLV 101
PLN02823 PLN02823
spermine synthase
 264-406 3.29e-07

spermine synthase


Pssm-ID: 178418 [Multi-domain]  Cd Length: 336  Bit Score: 51.99  E-value: 3.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084141239 264 SQPRRMLLIGGGSYTLAQlAVLKNPKVT-VDVVEIDPMLDELAVKYFSFKP----DKRIKIIHEDGRTFLNKLETKYDLI 338
Cdd:PLN02823  102 PNPKTVFIMGGGEGSTAR-EVLRHKTVEkVVMCDIDQEVVDFCRKHLTVNReafcDKRLELIINDARAELEKRDEKFDVI 180

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1084141239 339 VMDaFSSQF---PPFQLTTVEVLEKI-KESLTPGGlvmanIISAAEGPeAGFLQAQ------YLTYQEVFNKAVAFQA 406
Cdd:PLN02823  181 IGD-LADPVeggPCYQLYTKSFYERIvKPKLNPGG-----IFVTQAGP-AGILTHKevfssiYNTLRQVFKYVVPYTA 251
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 264-373 1.06e-06

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: 48.64  E-value: 1.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084141239 264 SQPRRMLLIG---GGSyTLAQLAVLKnPKVTVDVVEIDPMLDELAVKYFS-FKPDKRIKIIHEDGRTFLNKLET-KYDLI 338
Cdd:COG4122    15 LGAKRILEIGtgtGYS-TLWLARALP-DDGRLTTIEIDPERAAIARENFArAGLADRIRLILGDALEVLPRLADgPFDLV 92

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1084141239 339 VMDAFSSQFPPFqlttvevLEKIKESLTPGGLVMA 373
Cdd:COG4122    93 FIDADKSNYPDY-------LELALPLLRPGGLIVA 120
speE PRK01581
polyamine aminopropyltransferase;
266-419 1.56e-06

polyamine aminopropyltransferase;


Pssm-ID: 234961 [Multi-domain]  Cd Length: 374  Bit Score: 49.96  E-value: 1.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084141239 266 PRRMLLIGGGSyTLAQLAVLKNPKVT-VDVVEIDPMLDELAVKYFSFKP-------DKRIKIIHEDGRTFLNKLETKYDL 337
Cdd:PRK01581  151 PKRVLILGGGD-GLALREVLKYETVLhVDLVDLDGSMINMARNVPELVSlnksaffDNRVNVHVCDAKEFLSSPSSLYDV 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084141239 338 IVMDafssqFPP------FQLTTVEVLEKIKESLTPGGLVMANIISAAEGP-----------EAGFLQAQYLTYQEVFNK 400
Cdd:PRK01581  230 IIID-----FPDpatellSTLYTSELFARIATFLTEDGAFVCQSNSPADAPlvywsigntieHAGLTVKSYHTIVPSFGT 304

                         170
                  ....*....|....*....
gi 1084141239 401 AVAFQAtpGANKAARLNVI 419
Cdd:PRK01581  305 DWGFHI--AANSAYVLDQI 321
PRK03612 PRK03612
polyamine aminopropyltransferase;
265-372 3.75e-06

polyamine aminopropyltransferase;


Pssm-ID: 235139 [Multi-domain]  Cd Length: 521  Bit Score: 49.07  E-value: 3.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084141239 265 QPRRMLLIGGGSyTLAQLAVLKNPKV-TVDVVEIDPMLDELAVKYF--------SFKpDKRIKIIHEDGRTFLNKLETKY 335
Cdd:PRK03612  297 RPRRVLVLGGGD-GLALREVLKYPDVeQVTLVDLDPAMTELARTSPalralnggALD-DPRVTVVNDDAFNWLRKLAEKF 374

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1084141239 336 DLIVMDafssqFP-P--FQLT---TVEVLEKIKESLTPGGLVM 372
Cdd:PRK03612  375 DVIIVD-----LPdPsnPALGklySVEFYRLLKRRLAPDGLLV 412
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 272-371 3.83e-06

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 45.44  E-value: 3.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084141239 272 IGGGSYTLAQLAVLKNPKVTVDVVEIDPMLDELAVKYFSFKPDKRIKIIHEDGRTFLNKLETKYDLIVMDAFSSQFPpfq 351
Cdd:pfam08242   3 IGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERLAALGLLNAVRVELFQLDLGELDPGSFDVVVASNVLHHLA--- 79

                          90       100
                  ....*....|....*....|
gi 1084141239 352 lTTVEVLEKIKESLTPGGLV 371
Cdd:pfam08242  80 -DPRAVLRNIRRLLKPGGVL 98
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 265-381 2.93e-04

tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443299 [Multi-domain]  Cd Length: 238  Bit Score: 42.44  E-value: 2.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084141239 265 QPRRMLLIGGGSYTLAQLAVLKNPKVTVDVVEIDPMLDELAVKYFSFKP-DKRIKIIHEDGRTFLNKLET-KYDLIVMDa 342
Cdd:COG4123    37 KGGRVLDLGTGTGVIALMLAQRSPGARITGVEIQPEAAELARRNVALNGlEDRITVIHGDLKEFAAELPPgSFDLVVSN- 115

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1084141239 343 fssqfPPF---------------------QLTTVEVLEKIKESLTPGGLV--------MANIISAAEG 381
Cdd:COG4123   116 -----PPYfkagsgrkspdearaiarhedALTLEDLIRAAARLLKPGGRFalihpaerLAEILAALRK 178
NarK COG2223
Nitrate/nitrite transporter NarK [Inorganic ion transport and metabolism];
6-172 4.59e-04

Nitrate/nitrite transporter NarK [Inorganic ion transport and metabolism];


Pssm-ID: 441825 [Multi-domain]  Cd Length: 392  Bit Score: 42.56  E-value: 4.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084141239   6 VGVRFIAPDFGTSIYVWTAIIGVILGAL-----AFGYWYGGRLADKSATDEGLMVIFLLASVAWLASVWLRDSIlelaga 80
Cdd:COG2223   222 IGFSSWLPPYLVDQFGLSAATAGLLAALfallgALGRPLGGWLSDRIGGRRVLLIVFALMALGLLLLALALGSL------ 295

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084141239  81 mpgglrGQAFVASLLLFAPVSALLGMVSPYLVKLklVNLKTAGRYVGGLYAAGTVGSIAGTFAAGyWLIPLFNSRAVGWA 160
Cdd:COG2223   296 ------WLFLVLFLLLGLALGGGNGAVFALVPDI--FPTKNAGAVYGLVGAAGGLGGFLGPLLFG-ALLDATGSYTAAFL 366

                         170
                  ....*....|..
gi 1084141239 161 MVFALLGISLLA 172
Cdd:COG2223   367 VFAVLALVALVL 378
UhpC COG2271
Sugar phosphate permease [Carbohydrate transport and metabolism];
15-172 1.19e-03

Sugar phosphate permease [Carbohydrate transport and metabolism];


Pssm-ID: 441872 [Multi-domain]  Cd Length: 363  Bit Score: 41.01  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084141239  15 FGTSIYVWTAIIGVILGALAFGYWYGGRLADK-SATDEGLMVIFLLASVAWLASVWLRDSILELAGAMpgglrgqaFVAS 93
Cdd:COG2271   211 RGLSLAQAGLLLSLPFLAGIVGSLLGGWLSDRlGRRRKLVLAIGLLLAALALLLLALLPSPALAIALL--------FLAG 282

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1084141239  94 LLLFAPVSALLGMVSpylvklKLVNLKTAGRYVGGLYAAGTVGSIAGTFAAGYWLiplfnsRAVGWAMVFALLGISLLA 172
Cdd:COG2271   283 FGLGGAFGLLWALAA------ELFPKKARGTASGLVNTFGFLGGALGPLLVGYLL------DATGYQAAFLLLAALALL 349
Methyltrans_SAM pfam10672
S-adenosylmethionine-dependent methyltransferase; Members of this family are ...
 335-421 3.00e-03

S-adenosylmethionine-dependent methyltransferase; Members of this family are S-adenosylmethionine-dependent methyltransferases from gamma-proteobacterial species. The diversity in the roles of methylation is matched by the almost bewildering number of methyltransferase enzymes that catalyze the methylation reaction. Although several classes of methyltransferase enzymes are known, the great majority of methylation reactions are catalyzed by the S-adenosylmethionine-dependent methyltransferases.


Pssm-ID: 287624 [Multi-domain]  Cd Length: 286  Bit Score: 39.48  E-value: 3.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084141239 335 YDLIVMDAFSSQFPPFQLTT--VEVLEKIKESLTPGGLVMANIISAAEGPEagFL------QAQYLTYQEVFNKAVAFqa 406
Cdd:pfam10672 196 YDLVIIDPPSFQKGSFALTKdyKKILRRLPELLVEGGTVLACVNSPAVGPD--FLieemaeEAPSLHFVERLDNPPEF-- 271

                          90
                  ....*....|....*
gi 1084141239 407 tPGANKAARLNVILL 421
Cdd:pfam10672 272 -PDVDPAAGLKVLLF 285
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
265-373 6.14e-03

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 36.34  E-value: 6.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084141239 265 QPRRMLLIGGGSYTLAQLAVLKNPKVTVDVVEIDP-MLDELAVKYfsfkpdKRIKIIHEDGRTFlnKLETKYDLIVMdAF 343
Cdd:COG4106     1 PPRRVLDLGCGTGRLTALLAERFPGARVTGVDLSPeMLARARARL------PNVRFVVADLRDL--DPPEPFDLVVS-NA 71

                          90       100       110
                  ....*....|....*....|....*....|
gi 1084141239 344 SSQFPPfqlTTVEVLEKIKESLTPGGLVMA 373
Cdd:COG4106    72 ALHWLP---DHAALLARLAAALAPGGVLAV 98
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 251-374 7.98e-03

Methyltransferase small domain; This domain is found in ribosomal RNA small subunit methyltransferase C as well as other methyltransferases.


Pssm-ID: 428349 [Multi-domain]  Cd Length: 170  Bit Score: 37.18  E-value: 7.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084141239 251 LDYSTR-MDEVIVQSQPRRMLLIGGGSYTLAQLAVLKNPKVTVDVVEIDPMLDELAVKYFSFKPDKRIKIIHEDGrtFLN 329
Cdd:pfam05175  16 LDIGSRlLLEHLPKDLSGKVLDLGCGAGVLGAALAKESPDAELTMVDINARALESARENLAANGLENGEVVASDV--YSG 93

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1084141239 330 KLETKYDLIVMDafssqfPPF---QLTTVEVLEKI----KESLTPGG--LVMAN 374
Cdd:pfam05175  94 VEDGKFDLIISN------PPFhagLATTYNVAQRFiadaKRHLRPGGelWIVAN 141
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH