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Conserved domains on  [gi|20270243|ref|NP_612468|]
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dehydrodolichyl diphosphate synthase complex subunit NUS1 [Homo sapiens]

Protein Classification

UppS superfamily protein( domain architecture ID 1904676)

UppS superfamily protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UppS super family cl42290
Undecaprenyl pyrophosphate synthase [Lipid transport and metabolism];
196-293 2.04e-10

Undecaprenyl pyrophosphate synthase [Lipid transport and metabolism];


The actual alignment was detected with superfamily member COG0020:

Pssm-ID: 439791  Cd Length: 248  Bit Score: 59.68  E-value: 2.04e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20270243 196 GKADIVRAAQDFCQLVAQKQKRPTDLDVDTLASLLSSNGCPDPDLVLKfgpvdsTLG------FLPWHIRLTEIVSLPSH 269
Cdd:COG0020 145 GRWEIVDAVRKIARDVAAGELDPEDIDEETISRYLYTADLPDPDLLIR------TSGeqrisnFLLWQLAYAELYFTDVL 218

                        90       100
                ....*....|....*....|....*
gi 20270243 270 L-NISYEDFFSALRQYAACEQRLGK 293
Cdd:COG0020 219 WpDFDKEDLLRAIRDYQRRERRFGG 243
 
Name Accession Description Interval E-value
UppS COG0020
Undecaprenyl pyrophosphate synthase [Lipid transport and metabolism];
196-293 2.04e-10

Undecaprenyl pyrophosphate synthase [Lipid transport and metabolism];


Pssm-ID: 439791  Cd Length: 248  Bit Score: 59.68  E-value: 2.04e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20270243 196 GKADIVRAAQDFCQLVAQKQKRPTDLDVDTLASLLSSNGCPDPDLVLKfgpvdsTLG------FLPWHIRLTEIVSLPSH 269
Cdd:COG0020 145 GRWEIVDAVRKIARDVAAGELDPEDIDEETISRYLYTADLPDPDLLIR------TSGeqrisnFLLWQLAYAELYFTDVL 218

                        90       100
                ....*....|....*....|....*
gi 20270243 270 L-NISYEDFFSALRQYAACEQRLGK 293
Cdd:COG0020 219 WpDFDKEDLLRAIRDYQRRERRFGG 243
Cis_IPPS cd00475
Cis (Z)-Isoprenyl Diphosphate Synthases; Cis (Z)-Isoprenyl Diphosphate Synthases (cis-IPPS) ...
 196-285 3.78e-10

Cis (Z)-Isoprenyl Diphosphate Synthases; Cis (Z)-Isoprenyl Diphosphate Synthases (cis-IPPS) catalyze the successive 1'-4 condensation of the isopentenyl diphosphate (IPP) molecule to trans,trans-farnesyl diphosphate (FPP) or to cis,trans-FPP to form long-chain polyprenyl diphosphates. A few can also catalyze the condensation of IPP to trans-geranyl diphosphate to form the short-chain cis,trans- FPP. In prokaryotes, the cis-IPPS, undecaprenyl diphosphate synthase (UPP synthase), catalyzes the formation of the carrier lipid UPP in bacterial cell wall peptidoglycan biosynthesis. Similarly, in eukaryotes, the cis-IPPS, dehydrodolichyl diphosphate (dedol-PP) synthase catalyzes the formation of the polyisoprenoid glycosyl carrier lipid dolichyl monophosphate. cis-IPPS form homodimers and are mechanistically and structurally distinct from trans-IPPS, which lack the DDXXD motifs, yet require Mg2+ for activity.


Pssm-ID: 259850  Cd Length: 219  Bit Score: 58.54  E-value: 3.78e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20270243 196 GKADIVRAAQDFCQLVAQKQKRPTDLDVDTLASLLSSNGCPDPDLVLKfgpvdsTLG------FLPWHIRLTEIVSLPSH 269
Cdd:cd00475 128 GRDEIVRAVRKIARDVKAGELDPEDITEELISKHLYTADLPDPDLLIR------TSGeqrlsnFLLWQSAYAELYFTDVL 201

                        90
                ....*....|....*..
gi 20270243 270 -LNISYEDFFSALRQYA 285
Cdd:cd00475 202 wPDFRKEDLLRAILDYQ 218
Prenyltransf pfam01255
Putative undecaprenyl diphosphate synthase; Previously known as uncharacterized protein family ...
 196-292 3.48e-09

Putative undecaprenyl diphosphate synthase; Previously known as uncharacterized protein family UPF0015, a single member of this family has been identified as an undecaprenyl diphosphate synthase.


Pssm-ID: 460138  Cd Length: 220  Bit Score: 55.83  E-value: 3.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20270243   196 GKADIVRAAQDFCQlvAQKQKRPTDLDVDTLASLLSSNGCPDPDLVLKfgpvdsTLG------FLPWHIRLTEIVSLPSH 269
Cdd:pfam01255 125 GRDEIVDAVRKIVK--EGKKLDPEDIDEELISSHLYTAGLPDPDLLIR------TSGeqrlsnFLLWQSAYSELYFTDVL 196

                          90       100
                  ....*....|....*....|....
gi 20270243   270 L-NISYEDFFSALRQYAACEQRLG 292
Cdd:pfam01255 197 WpDFRKEDLLRAIRDYQRRERRFG 220
PRK14840 PRK14840
undecaprenyl pyrophosphate synthase; Provisional
 196-293 6.11e-05

undecaprenyl pyrophosphate synthase; Provisional


Pssm-ID: 173301  Cd Length: 250  Bit Score: 43.68  E-value: 6.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20270243  196 GKADIVRAAQDFCQLVAQKQKRPTDLDVDTLASLLSSNGCPDPDLVLKFGPVDSTLGFLPWHIRLTEI----VSLPshlN 271
Cdd:PRK14840 152 GKDELVRAFKKLHQDLANKKISSDDISEELISSYLDTSGLPDPDLLIRTGGEMRVSNFLLWQIAYTELyvtdVLWP---D 228

                         90       100
                 ....*....|....*....|..
gi 20270243  272 ISYEDFFSALRQYAACEQRLGK 293
Cdd:PRK14840 229 FTPNDLLEAIKTYQQRSRRGGK 250
 
Name Accession Description Interval E-value
UppS COG0020
Undecaprenyl pyrophosphate synthase [Lipid transport and metabolism];
196-293 2.04e-10

Undecaprenyl pyrophosphate synthase [Lipid transport and metabolism];


Pssm-ID: 439791  Cd Length: 248  Bit Score: 59.68  E-value: 2.04e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20270243 196 GKADIVRAAQDFCQLVAQKQKRPTDLDVDTLASLLSSNGCPDPDLVLKfgpvdsTLG------FLPWHIRLTEIVSLPSH 269
Cdd:COG0020 145 GRWEIVDAVRKIARDVAAGELDPEDIDEETISRYLYTADLPDPDLLIR------TSGeqrisnFLLWQLAYAELYFTDVL 218

                        90       100
                ....*....|....*....|....*
gi 20270243 270 L-NISYEDFFSALRQYAACEQRLGK 293
Cdd:COG0020 219 WpDFDKEDLLRAIRDYQRRERRFGG 243
Cis_IPPS cd00475
Cis (Z)-Isoprenyl Diphosphate Synthases; Cis (Z)-Isoprenyl Diphosphate Synthases (cis-IPPS) ...
 196-285 3.78e-10

Cis (Z)-Isoprenyl Diphosphate Synthases; Cis (Z)-Isoprenyl Diphosphate Synthases (cis-IPPS) catalyze the successive 1'-4 condensation of the isopentenyl diphosphate (IPP) molecule to trans,trans-farnesyl diphosphate (FPP) or to cis,trans-FPP to form long-chain polyprenyl diphosphates. A few can also catalyze the condensation of IPP to trans-geranyl diphosphate to form the short-chain cis,trans- FPP. In prokaryotes, the cis-IPPS, undecaprenyl diphosphate synthase (UPP synthase), catalyzes the formation of the carrier lipid UPP in bacterial cell wall peptidoglycan biosynthesis. Similarly, in eukaryotes, the cis-IPPS, dehydrodolichyl diphosphate (dedol-PP) synthase catalyzes the formation of the polyisoprenoid glycosyl carrier lipid dolichyl monophosphate. cis-IPPS form homodimers and are mechanistically and structurally distinct from trans-IPPS, which lack the DDXXD motifs, yet require Mg2+ for activity.


Pssm-ID: 259850  Cd Length: 219  Bit Score: 58.54  E-value: 3.78e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20270243 196 GKADIVRAAQDFCQLVAQKQKRPTDLDVDTLASLLSSNGCPDPDLVLKfgpvdsTLG------FLPWHIRLTEIVSLPSH 269
Cdd:cd00475 128 GRDEIVRAVRKIARDVKAGELDPEDITEELISKHLYTADLPDPDLLIR------TSGeqrlsnFLLWQSAYAELYFTDVL 201

                        90
                ....*....|....*..
gi 20270243 270 -LNISYEDFFSALRQYA 285
Cdd:cd00475 202 wPDFRKEDLLRAILDYQ 218
Prenyltransf pfam01255
Putative undecaprenyl diphosphate synthase; Previously known as uncharacterized protein family ...
 196-292 3.48e-09

Putative undecaprenyl diphosphate synthase; Previously known as uncharacterized protein family UPF0015, a single member of this family has been identified as an undecaprenyl diphosphate synthase.


Pssm-ID: 460138  Cd Length: 220  Bit Score: 55.83  E-value: 3.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20270243   196 GKADIVRAAQDFCQlvAQKQKRPTDLDVDTLASLLSSNGCPDPDLVLKfgpvdsTLG------FLPWHIRLTEIVSLPSH 269
Cdd:pfam01255 125 GRDEIVDAVRKIVK--EGKKLDPEDIDEELISSHLYTAGLPDPDLLIR------TSGeqrlsnFLLWQSAYSELYFTDVL 196

                          90       100
                  ....*....|....*....|....
gi 20270243   270 L-NISYEDFFSALRQYAACEQRLG 292
Cdd:pfam01255 197 WpDFRKEDLLRAIRDYQRRERRFG 220
PRK14840 PRK14840
undecaprenyl pyrophosphate synthase; Provisional
 196-293 6.11e-05

undecaprenyl pyrophosphate synthase; Provisional


Pssm-ID: 173301  Cd Length: 250  Bit Score: 43.68  E-value: 6.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20270243  196 GKADIVRAAQDFCQLVAQKQKRPTDLDVDTLASLLSSNGCPDPDLVLKFGPVDSTLGFLPWHIRLTEI----VSLPshlN 271
Cdd:PRK14840 152 GKDELVRAFKKLHQDLANKKISSDDISEELISSYLDTSGLPDPDLLIRTGGEMRVSNFLLWQIAYTELyvtdVLWP---D 228

                         90       100
                 ....*....|....*....|..
gi 20270243  272 ISYEDFFSALRQYAACEQRLGK 293
Cdd:PRK14840 229 FTPNDLLEAIKTYQQRSRRGGK 250
PRK10240 PRK10240
(2E,6E)-farnesyl-diphosphate-specific ditrans,polycis-undecaprenyl-diphosphate synthase;
115-292 6.49e-05

(2E,6E)-farnesyl-diphosphate-specific ditrans,polycis-undecaprenyl-diphosphate synthase;


Pssm-ID: 182326  Cd Length: 229  Bit Score: 43.43  E-value: 6.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20270243  115 SDIASLVVWCMAVGISyiSVYDHQ------GIFKRNNSRLMDEILKqqqellgldcskySPEFANSNDKddqvlnchLAV 188
Cdd:PRK10240  59 SALMELFVWALDSEVK--SLHRHNvrlriiGDTSRFNSRLQERIRK-------------SEALTAGNTG--------LTL 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20270243  189 KVLSPEDGKADIVRAAQDFCQLVAQKQKRPTDLDVDTLASLLSSNGCPDPDLVLKFGPVDSTLGFLPWHIRLTEI----V 264
Cdd:PRK10240 116 NIAANYGGRWDIVQGVRQLAEQVQQGNLQPDQIDEEMLNQHICMHELAPVDLVIRTGGEHRISNFLLWQIAYAELyftdV 195

                        170       180
                 ....*....|....*....|....*...
gi 20270243  265 SLPshlNISYEDFFSALRQYAACEQRLG 292
Cdd:PRK10240 196 LWP---DFDEQDFEGALNAFANRERRFG 220
PRK14828 PRK14828
undecaprenyl pyrophosphate synthase; Provisional
 196-293 6.85e-05

undecaprenyl pyrophosphate synthase; Provisional


Pssm-ID: 237825  Cd Length: 256  Bit Score: 43.58  E-value: 6.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20270243  196 GKADIVRAAQDFCQLVAQKQKRPTDL----DVDTLASLLSSNGCPDPDLVLKFGPVDSTLGFLPWHIRLTEI----VSLP 267
Cdd:PRK14828 154 GRQEIVDAVRSLLTEHKDKGTSIDELaesvTVDAISTHLYTGGQPDPDLVIRTSGEQRLSGFMLWQSAHSEYyfceTYWP 233

                         90       100
                 ....*....|....*....|....*.
gi 20270243  268 SHLNIsyeDFFSALRQYAACEQRLGK 293
Cdd:PRK14828 234 AFRKV---DFLRALRDYSQRERRFGK 256
 
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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