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Conserved domains on  [gi|1080381801|gb|OFL69451|]
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1,4-dihydroxy-2-naphthoate polyprenyltransferase [Corynebacterium sp. HMSC077C02]

Protein Classification

prenyltransferase( domain architecture ID 10792743)

prenyltransferase transfers an isoprenyl group to an aromatic substrate acceptor; may be involved in the biosynthesis of menaquinone or phylloquinone

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK06080 PRK06080
1,4-dihydroxy-2-naphthoate octaprenyltransferase; Validated
11-298 1.74e-121

1,4-dihydroxy-2-naphthoate octaprenyltransferase; Validated


:

Pssm-ID: 235695  Cd Length: 293  Bit Score: 349.44  E-value: 1.74e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381801  11 ASLSDWLEGARPHTWANAFAPVIVGVGAASTHAPIIWGRAVLALVVAWALIVGVNFANDYSDGIRGTD-DDRSGPLRLTG 89
Cdd:PRK06080    1 STFKAWLELARPKTLPAAFAPVLVGTALAYWLGSFHPLLALLALLAALLLQIATNLANDYGDYVKGTDtEDRVGPLRAIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381801  90 SGLVEPKVVKYAAFGSFGVAGLAGVALSLMSAWWLILVGALCIAAAWFYTGGKNPYGYRGLGEVSVFVFFGLVAVLGTEF 169
Cdd:PRK06080   81 RGGISPKQVKRAAIAFFGLAALLGLYLVAVSGWWLLLLGLLCIAAAILYTGGPKPYGYTGLGELFVGVFFGLVIVLGTYY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381801 170 TQTGSLSWVGLACAIGIGSVSSAVNLANNLRDIPTDAATGKITLAVRLGDFRTRIVWQILSLMPALA---SSFIAFWRPW 246
Cdd:PRK06080  161 LQAGTVDSAVFLPALPCGLLIGAVLLANNIRDIETDRENGKNTLAVRLGDKNARRLHAALLALAYLCivlLALLGLASPW 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1080381801 247 ALVGLLIVPLWVKASEPIRMHKKGKELIPVLGLTGKMMLAWSVITALALALS 298
Cdd:PRK06080  241 GLLFLLSLPLAVKAARPVLRKQKPETLIPALKATGKTNLLFGLLFAIGLLLS 292
 
Name Accession Description Interval E-value
PRK06080 PRK06080
1,4-dihydroxy-2-naphthoate octaprenyltransferase; Validated
11-298 1.74e-121

1,4-dihydroxy-2-naphthoate octaprenyltransferase; Validated


Pssm-ID: 235695  Cd Length: 293  Bit Score: 349.44  E-value: 1.74e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381801  11 ASLSDWLEGARPHTWANAFAPVIVGVGAASTHAPIIWGRAVLALVVAWALIVGVNFANDYSDGIRGTD-DDRSGPLRLTG 89
Cdd:PRK06080    1 STFKAWLELARPKTLPAAFAPVLVGTALAYWLGSFHPLLALLALLAALLLQIATNLANDYGDYVKGTDtEDRVGPLRAIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381801  90 SGLVEPKVVKYAAFGSFGVAGLAGVALSLMSAWWLILVGALCIAAAWFYTGGKNPYGYRGLGEVSVFVFFGLVAVLGTEF 169
Cdd:PRK06080   81 RGGISPKQVKRAAIAFFGLAALLGLYLVAVSGWWLLLLGLLCIAAAILYTGGPKPYGYTGLGELFVGVFFGLVIVLGTYY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381801 170 TQTGSLSWVGLACAIGIGSVSSAVNLANNLRDIPTDAATGKITLAVRLGDFRTRIVWQILSLMPALA---SSFIAFWRPW 246
Cdd:PRK06080  161 LQAGTVDSAVFLPALPCGLLIGAVLLANNIRDIETDRENGKNTLAVRLGDKNARRLHAALLALAYLCivlLALLGLASPW 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1080381801 247 ALVGLLIVPLWVKASEPIRMHKKGKELIPVLGLTGKMMLAWSVITALALALS 298
Cdd:PRK06080  241 GLLFLLSLPLAVKAARPVLRKQKPETLIPALKATGKTNLLFGLLFAIGLLLS 292
MenA COG1575
1,4-dihydroxy-2-naphthoate polyprenyltransferase [Coenzyme transport and metabolism]; 1, ...
16-298 1.29e-96

1,4-dihydroxy-2-naphthoate polyprenyltransferase [Coenzyme transport and metabolism]; 1,4-dihydroxy-2-naphthoate polyprenyltransferase is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 441183  Cd Length: 290  Bit Score: 286.27  E-value: 1.29e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381801  16 WLEGARPHTWANAFAPVIVGVGAASTHA-PIIWGRAVLALVVAWALIVGVNFANDYSDGIRGTD-DDRSGPLRLTGSGLV 93
Cdd:COG1575     2 WLEAARPRTLPAAVAPVLLGTALAYYETgSFNWLLFLLALLAALLLQIGVNLANDYFDYKKGTDtEERVGPSRVIVSGLL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381801  94 EPKVVKYAAFGSFGVAGLAGVALSLMSAWWLILVGALCIAAAWFYTGGKNPYGYRGLGEVSVFVFFGLVAVLGTEFTQTG 173
Cdd:COG1575    82 SPKQVLRAALLLLALALLLGLYLVLLSGWPLLLLGLLGILAAIFYTGGPFPLGYRGLGELFVFLFFGLVAVLGTYYVQTG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381801 174 SLSWVGLACAIGIGSVSSAVNLANNLRDIPTDAATGKITLAVRLGDFRTRIVWQILSLMP---ALASSFIAFWRPWALVG 250
Cdd:COG1575   162 TLSWAALLASLPVGLLSAAVLLANNLRDIETDRAAGKRTLAVRLGRKRARRLYAALLLLAyllILLLVLLGLLPPWALLA 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1080381801 251 LLIVPLWVKASEPIRMHKKGKELIPVLGLTGKMMLAWSVITALALALS 298
Cdd:COG1575   242 LLSLPLALKLVRRVLRGAKPEALIPALKNTALLNLLFGLLLALGLLLG 289
PT_UbiA_UBIAD1 cd13962
1,4-Dihydroxy-2-naphthoate octaprenyltransferase; Human UBIAD1 is an enzyme involved in the ...
17-294 8.90e-83

1,4-Dihydroxy-2-naphthoate octaprenyltransferase; Human UBIAD1 is an enzyme involved in the synthesis of MK-4. Menaquinones (MKs, also called bacterial forms) are one of the two forms of natural vitamin K, the other being the plant form, phylloquinone (PK). All forms of vitamin K have a 2-methyl-1,4-naphthoquinone (menadione; K3) ring structure in common. At the 3-position of the ring, PK has a phytyl side chain while MKs have several repeating prenyl units. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways.


Pssm-ID: 260125  Cd Length: 283  Bit Score: 250.89  E-value: 8.90e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381801  17 LEGARPHTWANAFAPVIVGVGAA-STHAPIIWGRAVLALVVAWALIVGVNFANDYSDGIRGTDD-DRSGPLRLTGSGLVE 94
Cdd:cd13962     1 LLAARPRTLPASLAPVLLGTALAyYLGGFFNWLLFLLALLAALLLQIGVNLANDYFDYKKGTDTePRSGPSRVLVSGLLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381801  95 PKVVKYAAFGSFGVAGLAGVALSLMSAWWLILVGALCIAAAWFYTGGKNPYGYRGLGEVSVFVFFGLVAVLGTEFTQTGS 174
Cdd:cd13962    81 PRQVLRAALVLLLLAALLGLYLVALGGWLLLLLGLLGILAGYFYTGGPFPLSYRGLGELFVFLFFGLLAVLGTYYVQTGS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381801 175 LSWVGLACAIGIGSVSSAVNLANNLRDIPTDAATGKITLAVRLGDFRTRIVWQILSLMPALASSFIAFWR---PWALVGL 251
Cdd:cd13962   161 LSWEVLLAALPLGLLIAAILLANNIRDIEADRAAGKRTLAVRLGRKRARRLYAALLLLAYLLLLLLVLLGllpLWSLLAL 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1080381801 252 LIVPLWVKASEPIRMHKKGKELIPVLGLTGKMMLAWSVITALA 294
Cdd:cd13962   241 LSLPLAIKLLRRLLRKADKPLLLIALKLTALLTLLFGLLLALG 283
menA TIGR00751
1,4-dihydroxy-2-naphthoate octaprenyltransferase; This membrane-associated enzyme converts 1, ...
21-294 1.63e-81

1,4-dihydroxy-2-naphthoate octaprenyltransferase; This membrane-associated enzyme converts 1,4-dihydroxy-2-naphthoic acid (DHNA) to demethylmenaquinone, a step in menaquinone biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 129834  Cd Length: 284  Bit Score: 247.87  E-value: 1.63e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381801  21 RPHTWANAFAPVIVGVGAASTHAPIIWGRAVLALVVAWALIVGVNFANDYSDGIRGTD-DDRSGPLRLTGSGLVEPKVVK 99
Cdd:TIGR00751   1 RPKTLPLAIAPIVAGTALAAWLHAFVWLVALLALATAVLLQILSNYANDYGDGIKGSDtDDRIGPLRGVQKGLITPREVK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381801 100 YAAFGSFGVAGLAGVALSLMSA------WWLILVGALCIAAAWFYTGGKNPYGYRGLGEVSVFVFFGLVAVLGTEFTQTG 173
Cdd:TIGR00751  81 TALITSVALGALSGLVLALLAApnlsdlFWFIALGALCIAAAITYTVGSKPYGYAGLGDISVLVFFGPLAVLGTQYLQAH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381801 174 SLSWVGLACAIGIGSVSSAVNLANNLRDIPTDAATGKITLAVRLGDFRTRIVWQILSLMPALASSFIAFWRP---WALVG 250
Cdd:TIGR00751 161 RVDWVGILPAVATGLLACAVLNINNLRDIPTDARAGKNTLAVRLGDARTRMYHQGLLAVAGVCTFVFMLATPiswWCVLF 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1080381801 251 LLIVPLWVKASEPIRMHKKGKELIPVLGLTGKMMLAWSVITALA 294
Cdd:TIGR00751 241 LLAAPLLLKAAGPVRSGRGPRELRPVLRDTGLAMLLWNLLFALG 284
UbiA pfam01040
UbiA prenyltransferase family;
28-258 3.47e-19

UbiA prenyltransferase family;


Pssm-ID: 460038 [Multi-domain]  Cd Length: 250  Bit Score: 84.59  E-value: 3.47e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381801  28 AFAPVIVGVGAASTHaPIIWGRAVLALVVAWALIVGVNFANDYSDGIRGTDDDRSgPLRLTGSGLVEPKVVKYAAFgsfg 107
Cdd:pfam01040   1 LLIPALAGLALAAGG-VPDLLLLLLALLGTVLARAAANALNDYYDRDIDAIMPRT-PNRPLPSGRISPREALIFAL---- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381801 108 VAGLAGVALSLMSAWWLILVGALCIAAAWFYTggkNPYGYRGL-GEVSVFVFFGLVAVLGTeFTQTGSLSWVGLACAIGI 186
Cdd:pfam01040  75 VLLALGLLLLLLLNPLTALLGLAALLLYVLYT---LRLKRRTLlGQLVGGLAFGLPPLLGW-AAVTGSLSPLALLLALAL 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1080381801 187 GSVSSAVNLANNLRDIPTDAATGKITLAVRLGDFRTRIVWQILSLMPALASSFI---AFWRPWALVGLLIVPLWV 258
Cdd:pfam01040 151 FLWTWAIALANDLRDREDDRKAGIKTLPVVLGRKAARILLALLLAVALLLLLLLlllLLGGLYLLLALLLAALAL 225
 
Name Accession Description Interval E-value
PRK06080 PRK06080
1,4-dihydroxy-2-naphthoate octaprenyltransferase; Validated
11-298 1.74e-121

1,4-dihydroxy-2-naphthoate octaprenyltransferase; Validated


Pssm-ID: 235695  Cd Length: 293  Bit Score: 349.44  E-value: 1.74e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381801  11 ASLSDWLEGARPHTWANAFAPVIVGVGAASTHAPIIWGRAVLALVVAWALIVGVNFANDYSDGIRGTD-DDRSGPLRLTG 89
Cdd:PRK06080    1 STFKAWLELARPKTLPAAFAPVLVGTALAYWLGSFHPLLALLALLAALLLQIATNLANDYGDYVKGTDtEDRVGPLRAIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381801  90 SGLVEPKVVKYAAFGSFGVAGLAGVALSLMSAWWLILVGALCIAAAWFYTGGKNPYGYRGLGEVSVFVFFGLVAVLGTEF 169
Cdd:PRK06080   81 RGGISPKQVKRAAIAFFGLAALLGLYLVAVSGWWLLLLGLLCIAAAILYTGGPKPYGYTGLGELFVGVFFGLVIVLGTYY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381801 170 TQTGSLSWVGLACAIGIGSVSSAVNLANNLRDIPTDAATGKITLAVRLGDFRTRIVWQILSLMPALA---SSFIAFWRPW 246
Cdd:PRK06080  161 LQAGTVDSAVFLPALPCGLLIGAVLLANNIRDIETDRENGKNTLAVRLGDKNARRLHAALLALAYLCivlLALLGLASPW 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1080381801 247 ALVGLLIVPLWVKASEPIRMHKKGKELIPVLGLTGKMMLAWSVITALALALS 298
Cdd:PRK06080  241 GLLFLLSLPLAVKAARPVLRKQKPETLIPALKATGKTNLLFGLLFAIGLLLS 292
MenA COG1575
1,4-dihydroxy-2-naphthoate polyprenyltransferase [Coenzyme transport and metabolism]; 1, ...
16-298 1.29e-96

1,4-dihydroxy-2-naphthoate polyprenyltransferase [Coenzyme transport and metabolism]; 1,4-dihydroxy-2-naphthoate polyprenyltransferase is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 441183  Cd Length: 290  Bit Score: 286.27  E-value: 1.29e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381801  16 WLEGARPHTWANAFAPVIVGVGAASTHA-PIIWGRAVLALVVAWALIVGVNFANDYSDGIRGTD-DDRSGPLRLTGSGLV 93
Cdd:COG1575     2 WLEAARPRTLPAAVAPVLLGTALAYYETgSFNWLLFLLALLAALLLQIGVNLANDYFDYKKGTDtEERVGPSRVIVSGLL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381801  94 EPKVVKYAAFGSFGVAGLAGVALSLMSAWWLILVGALCIAAAWFYTGGKNPYGYRGLGEVSVFVFFGLVAVLGTEFTQTG 173
Cdd:COG1575    82 SPKQVLRAALLLLALALLLGLYLVLLSGWPLLLLGLLGILAAIFYTGGPFPLGYRGLGELFVFLFFGLVAVLGTYYVQTG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381801 174 SLSWVGLACAIGIGSVSSAVNLANNLRDIPTDAATGKITLAVRLGDFRTRIVWQILSLMP---ALASSFIAFWRPWALVG 250
Cdd:COG1575   162 TLSWAALLASLPVGLLSAAVLLANNLRDIETDRAAGKRTLAVRLGRKRARRLYAALLLLAyllILLLVLLGLLPPWALLA 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1080381801 251 LLIVPLWVKASEPIRMHKKGKELIPVLGLTGKMMLAWSVITALALALS 298
Cdd:COG1575   242 LLSLPLALKLVRRVLRGAKPEALIPALKNTALLNLLFGLLLALGLLLG 289
PT_UbiA_UBIAD1 cd13962
1,4-Dihydroxy-2-naphthoate octaprenyltransferase; Human UBIAD1 is an enzyme involved in the ...
17-294 8.90e-83

1,4-Dihydroxy-2-naphthoate octaprenyltransferase; Human UBIAD1 is an enzyme involved in the synthesis of MK-4. Menaquinones (MKs, also called bacterial forms) are one of the two forms of natural vitamin K, the other being the plant form, phylloquinone (PK). All forms of vitamin K have a 2-methyl-1,4-naphthoquinone (menadione; K3) ring structure in common. At the 3-position of the ring, PK has a phytyl side chain while MKs have several repeating prenyl units. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways.


Pssm-ID: 260125  Cd Length: 283  Bit Score: 250.89  E-value: 8.90e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381801  17 LEGARPHTWANAFAPVIVGVGAA-STHAPIIWGRAVLALVVAWALIVGVNFANDYSDGIRGTDD-DRSGPLRLTGSGLVE 94
Cdd:cd13962     1 LLAARPRTLPASLAPVLLGTALAyYLGGFFNWLLFLLALLAALLLQIGVNLANDYFDYKKGTDTePRSGPSRVLVSGLLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381801  95 PKVVKYAAFGSFGVAGLAGVALSLMSAWWLILVGALCIAAAWFYTGGKNPYGYRGLGEVSVFVFFGLVAVLGTEFTQTGS 174
Cdd:cd13962    81 PRQVLRAALVLLLLAALLGLYLVALGGWLLLLLGLLGILAGYFYTGGPFPLSYRGLGELFVFLFFGLLAVLGTYYVQTGS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381801 175 LSWVGLACAIGIGSVSSAVNLANNLRDIPTDAATGKITLAVRLGDFRTRIVWQILSLMPALASSFIAFWR---PWALVGL 251
Cdd:cd13962   161 LSWEVLLAALPLGLLIAAILLANNIRDIEADRAAGKRTLAVRLGRKRARRLYAALLLLAYLLLLLLVLLGllpLWSLLAL 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1080381801 252 LIVPLWVKASEPIRMHKKGKELIPVLGLTGKMMLAWSVITALA 294
Cdd:cd13962   241 LSLPLAIKLLRRLLRKADKPLLLIALKLTALLTLLFGLLLALG 283
menA TIGR00751
1,4-dihydroxy-2-naphthoate octaprenyltransferase; This membrane-associated enzyme converts 1, ...
21-294 1.63e-81

1,4-dihydroxy-2-naphthoate octaprenyltransferase; This membrane-associated enzyme converts 1,4-dihydroxy-2-naphthoic acid (DHNA) to demethylmenaquinone, a step in menaquinone biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 129834  Cd Length: 284  Bit Score: 247.87  E-value: 1.63e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381801  21 RPHTWANAFAPVIVGVGAASTHAPIIWGRAVLALVVAWALIVGVNFANDYSDGIRGTD-DDRSGPLRLTGSGLVEPKVVK 99
Cdd:TIGR00751   1 RPKTLPLAIAPIVAGTALAAWLHAFVWLVALLALATAVLLQILSNYANDYGDGIKGSDtDDRIGPLRGVQKGLITPREVK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381801 100 YAAFGSFGVAGLAGVALSLMSA------WWLILVGALCIAAAWFYTGGKNPYGYRGLGEVSVFVFFGLVAVLGTEFTQTG 173
Cdd:TIGR00751  81 TALITSVALGALSGLVLALLAApnlsdlFWFIALGALCIAAAITYTVGSKPYGYAGLGDISVLVFFGPLAVLGTQYLQAH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381801 174 SLSWVGLACAIGIGSVSSAVNLANNLRDIPTDAATGKITLAVRLGDFRTRIVWQILSLMPALASSFIAFWRP---WALVG 250
Cdd:TIGR00751 161 RVDWVGILPAVATGLLACAVLNINNLRDIPTDARAGKNTLAVRLGDARTRMYHQGLLAVAGVCTFVFMLATPiswWCVLF 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1080381801 251 LLIVPLWVKASEPIRMHKKGKELIPVLGLTGKMMLAWSVITALA 294
Cdd:TIGR00751 241 LLAAPLLLKAAGPVRSGRGPRELRPVLRDTGLAMLLWNLLFALG 284
PRK13387 PRK13387
1,4-dihydroxy-2-naphthoate octaprenyltransferase; Provisional
12-270 2.50e-23

1,4-dihydroxy-2-naphthoate octaprenyltransferase; Provisional


Pssm-ID: 237373  Cd Length: 317  Bit Score: 97.17  E-value: 2.50e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381801  12 SLSDWLEGARPHTWANAFAPVIVGVGAASTHAPII-WGRAVLALVVAWALIVGVNFANDYSDGIRGTDD-DRSGPLRLTG 89
Cdd:PRK13387    2 SAKLFLKLVEIHTKIASFFPVILGTLFSLYVAKIFdWLLFLAFMVAMLAFDIATTAINNYMDFKKALDTaDYVGIGNGIG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381801  90 SGLVEPKVVKYAAFGSFGVAGLAGVALSLMSAWWLILVGALCIAAAWFYTGGKNPYGYRGLGEVSV-----FVFFGLVAV 164
Cdd:PRK13387   82 QHGLKPRNVLTVILLMYVVAAILGVYLCMNTSWLLLVIGLICFAIGILYTGGPLPLSRMPLGEIFSgltmgFGIFLLAVY 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381801 165 LGTEFTQTGSLSWVG--------LACAIGIGSVS-------SAVNLANNLRDIPTDAATGKITLAVRLGDFRTRIVWQIL 229
Cdd:PRK13387  162 INTNTITIESLLFQGemftiqgnLIAIIAIGVISlpiiftiANIMLANNLRDLDEDIKNHRYTLVYYIGREKGVVLFAIL 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1080381801 230 SLMPALA---SSFIAFWRPWALVGLLIVPLWVKAsepIRMHKKG 270
Cdd:PRK13387  242 FYASYLAiavIVLMGYISPWALLSFLTLRKPISN---LQSFQKE 282
PRK07419 PRK07419
2-carboxy-1,4-naphthoquinone phytyltransferase;
2-259 1.19e-19

2-carboxy-1,4-naphthoquinone phytyltransferase;


Pssm-ID: 236015  Cd Length: 304  Bit Score: 86.88  E-value: 1.19e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381801   2 SEAPKSPATASLSDWLEGARPHTWANAFAPVIVGVGAA-STHAPIIWGRAVLALVVAWALIVGVNFANDYSDGIRGTDDD 80
Cdd:PRK07419    1 VMTTTSMSPSRRKLWLAAIKPPMYSVAIMPILVGTAWAlGETGVFRLDQFITFLLAAILILAWENLSNDVFDADTGIDKN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381801  81 RSGPL-RLTGSglvePKVVKYAAFGSFGvAGLAGV-ALSLMSAWWLILVGALCIAAAWFYTGGKNPYGYRGLGEVSVFVF 158
Cdd:PRK07419   81 KFHSVvNLTGN----KSLVFWLANLFLL-LGLLGIlAIALQSDWTVLGLVLLCCFLGYLYQGPPFRLGYQGLGEPLCFLA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381801 159 FGLVAVLGTEFTQTGSLSWVGLACAIGIGSVSSAVNLANNLRDIPTDAATGKITLAVRLGDFR-TRIVWQILSLMPALAS 237
Cdd:PRK07419  156 FGPLAVAAALYSQTPSWSLIPLAASIILGLATSLILFCSHFHQVEDDLAAGKRSPIVRLGTKRgAQLLPWIVGLIYALEL 235
                         250       260
                  ....*....|....*....|....
gi 1080381801 238 SFIA--FWRPWALVGLLIVPLWVK 259
Cdd:PRK07419  236 LPVLlgFWPWTTLLSLLSLPFAIK 259
UbiA pfam01040
UbiA prenyltransferase family;
28-258 3.47e-19

UbiA prenyltransferase family;


Pssm-ID: 460038 [Multi-domain]  Cd Length: 250  Bit Score: 84.59  E-value: 3.47e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381801  28 AFAPVIVGVGAASTHaPIIWGRAVLALVVAWALIVGVNFANDYSDGIRGTDDDRSgPLRLTGSGLVEPKVVKYAAFgsfg 107
Cdd:pfam01040   1 LLIPALAGLALAAGG-VPDLLLLLLALLGTVLARAAANALNDYYDRDIDAIMPRT-PNRPLPSGRISPREALIFAL---- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381801 108 VAGLAGVALSLMSAWWLILVGALCIAAAWFYTggkNPYGYRGL-GEVSVFVFFGLVAVLGTeFTQTGSLSWVGLACAIGI 186
Cdd:pfam01040  75 VLLALGLLLLLLLNPLTALLGLAALLLYVLYT---LRLKRRTLlGQLVGGLAFGLPPLLGW-AAVTGSLSPLALLLALAL 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1080381801 187 GSVSSAVNLANNLRDIPTDAATGKITLAVRLGDFRTRIVWQILSLMPALASSFI---AFWRPWALVGLLIVPLWV 258
Cdd:pfam01040 151 FLWTWAIALANDLRDREDDRKAGIKTLPVVLGRKAARILLALLLAVALLLLLLLlllLLGGLYLLLALLLAALAL 225
PT_UbiA cd13956
UbiA family of prenyltransferases (PTases); Many characterized members of the UbiA ...
20-258 1.20e-17

UbiA family of prenyltransferases (PTases); Many characterized members of the UbiA prenyltransferase family are aromatic prenyltransferases and play an important role in the biosynthesis of heme, chlorophyll, vitamin E, and vitamin K. They contain two copies of a motif similar to the active site DxxD motif of trans-prenyltransferases and are potentially related. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways.


Pssm-ID: 260119 [Multi-domain]  Cd Length: 271  Bit Score: 80.86  E-value: 1.20e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381801  20 ARPHTWANAFAPVIVGVGAASTHAPIIWGRAVLALVVAWALIVGVNFANDYSDGIRGTDDDRSGPLRltgSGLVEPKvvk 99
Cdd:cd13956     4 MRPYTLLYVLAPALAGAALAGAFAGPLPALLLLALLAVFLGAGAGYALNDYTDRELDAINKPDRPLP---SGRLSPR--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381801 100 yAAFGSFGVAGLAGVALSLMSAWWLILVGALCIAAAWFYTGGKNPYGYRGLGevSVFVFFGLVAVLGTEFTQTGSLSWVG 179
Cdd:cd13956    78 -QALAFAAALLLVGLALALALGPLALLLLLAGLLLGLAYSLGLKRLKLGGWG--VLGYATGLALLPGLGAVAAGGLVPLA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381801 180 LACAIGIGSVSSAVNLANNLRDIPTDAATGKITLAVRLGdfRTRIVWQILSLMPA-----LASSFIAFWRPWALVGLLIV 254
Cdd:cd13956   155 LLLALVFLLLGLGINLYNDLPDVEGDRAAGIRTLPVRLG--PRRARRLAAGLLLAalilvVLLAVAGLLGPLALLALLAV 232

                  ....
gi 1080381801 255 PLWV 258
Cdd:cd13956   233 ALLA 236
ubiA PRK05951
prenyltransferase; Reviewed
51-254 5.49e-12

prenyltransferase; Reviewed


Pssm-ID: 180323  Cd Length: 296  Bit Score: 64.80  E-value: 5.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381801  51 VLALVVAWALIVGVNFANDYSDGIRGTD--DDRSGPLRLTGSGLVEPKVVKyaafgsfgVAGLAGVALSLMSAWWLILVG 128
Cdd:PRK05951   43 ALMLLGYFLLHASLNVFNDYKDYVLDCDhhETTGYRQHPIQAGIMTLGHLR--------VLGIALGAIALQLGWSLVLDR 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381801 129 -------ALCIAAAWF-YTGGKNPYGYRGLGEVSVFVFFGLVAVLGTEFTQTGSLSWVGLACAIGIGSVSSAVNLANNLR 200
Cdd:PRK05951  115 gigavtlALLGVFLWTcYMGPPFFLKYRWLGEHLVFYAWSHMLVMGLIYVWLGNLSSPNLLAGVPLGLLMALVLLSNNLR 194
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1080381801 201 DIPTDAATGKITLAVRLGDFRTR-IVWQILSLMPALASSFIAFWRP----WALVGLLIV 254
Cdd:PRK05951  195 DIEDDERKGIPTLAVIFGRRGAAlYIFALLSPYVILQILLIAILTPlislWALLSLLVA 253
UbiA COG0382
4-hydroxybenzoate polyprenyltransferase [Coenzyme transport and metabolism]; 4-hydroxybenzoate ...
15-258 5.09e-11

4-hydroxybenzoate polyprenyltransferase [Coenzyme transport and metabolism]; 4-hydroxybenzoate polyprenyltransferase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 440151  Cd Length: 280  Bit Score: 61.78  E-value: 5.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381801  15 DWLEGARPHTWANAFAPVIVGVGAA--STHAPIIWGRAVLALVVAWALIVGVNFANDYSDgirgTDDDR---SGPLRLTG 89
Cdd:COG0382     2 AYLRLLRLDRPIGILLLLWPTLWALflAAGGLPDLLLLLLAVLGTVLMRSAGYVINDYFD----REIDRineRKPNRPLA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381801  90 SGLVEPKvvkyAAFGSFGVAGLAGVALSLMSAWWLILVGALCIAAAWFYTGGKNPYGYrgLGEVSVFVFFGLVAVLGTeF 169
Cdd:COG0382    78 SGRISLR----EALLLAIVLLLLALALALLLNPLTFLLALAALALAWAYSLFLKRFTL--LGNLVLGLLFGLGILMGF-A 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381801 170 TQTGSLSWVGLACAIGIGSVSSAVNLANNLRDIPTDAATGKITLAVRLGDFRTRI---VWQILSLMPALASSFIAFWRPW 246
Cdd:COG0382   151 AVTGSLPLSAWLLALAAFLWTLAYDTIYDLEDREGDRKIGIKTLAILFGVRDALIiagVLYALAVLLLLLLGLLAGLGLL 230
                         250
                  ....*....|..
gi 1080381801 247 ALVGLLIVPLWV 258
Cdd:COG0382   231 YLLGLLAALLLL 242
PLN02922 PLN02922
prenyltransferase
28-256 1.20e-08

prenyltransferase


Pssm-ID: 215499  Cd Length: 315  Bit Score: 55.13  E-value: 1.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381801  28 AFAPVIVGVGAASTHAPII-WGRAVLALVVAWALIVGVNFANDYSDGIRGTDDDR-SGPLRLTGSglvePKVVKYAAFGS 105
Cdd:PLN02922   30 ALVPLTVGAAAAYLQTGLFdARRYGTLLLSSVLVITWLNLSNDAYDADTGVDKNKkESVVNLVGS----RRGVLAAAIGC 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381801 106 --FGVAGLAGVALSLMSAWWLILVGAlCIAAAWFYTGGKNPYGYRGLGEVSVFVFFGLVAVLGTEFTQ---TGSLSWVGL 180
Cdd:PLN02922  106 laLGAAGLVWASLVAGNIRVILLLAA-AILCGYVYQCPPFRLSYKGLGEPLCFAAFGPLATTAFYLALasgAGGSEMAIL 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381801 181 ACAIGIGSVSSAVNLANNL-------RDIPTDAATGKITLAVRLGDFR-TRIV-WQILSLMPALASSFIAFWRPWALVGL 251
Cdd:PLN02922  185 PLTPTVLSASVLVGLTTTLilfcshfHQIDGDRAVGKMSPLVRLGTEKgSRVVrWAVLLLYSLLAALGLLKALPLPCALL 264

                  ....*
gi 1080381801 252 LIVPL 256
Cdd:PLN02922  265 CFLTL 269
PT_UbiA_DGGGPS cd13961
Geranylgeranylglycerol-phosphate geranylgeranyltransferase; Digeranylgeranylglyceryl phosphate ...
28-258 8.57e-05

Geranylgeranylglycerol-phosphate geranylgeranyltransferase; Digeranylgeranylglyceryl phosphate synthase (DGGGPS) transfers a geranylgeranyl group from geranylgeranyl diphosphate to (S)-3-O-geranylgeranylglyceryl phosphate to form (S)-2,3-di-O-geranylgeranylglyceryl phosphate, as part of the isoprenoid ether lipid biosynthesis. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways.


Pssm-ID: 260124  Cd Length: 270  Bit Score: 43.26  E-value: 8.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381801  28 AFAPVIVGVGAASTHAPIIWGRAVLALVVAWALIVGVNFANDYSDgirgTDDDR-SGPLRLTGSGLVEPKVVKYAAFGSF 106
Cdd:cd13961    15 ALAQYLGALFALGPLLSLNDLELLLLFLSVFLIAAAGYIINDYFD----VEIDRiNKPDRPIPSGRISRREALILSILLN 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080381801 107 gvagLAGVALSLMSAWWLILVGALCIAAAWFYTGGKNPYGyrGLGEVSVFVFFGLVAVLGTEFtqTGSLSWVGLACAIGI 186
Cdd:cd13961    91 ----ALGLILAFLLSPLALLIALLNSLLLWLYSHKLKRTP--LIGNLLVALLTGLPFLFGGLA--AGNLLLIILLLALFA 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1080381801 187 GSVSSAVNLANNLRDIPTDAATGKITLAVRLGDFRTRIVWQILSLMPALASSFIAFWRPWA---LVGLLIVPLWV 258
Cdd:cd13961   163 FLITLGREIVKDIEDVEGDRAEGARTLPIVYGIKKAKKIAALLLLLAILLSPLPYLLGGLGilyLILIIIADLLF 237
 
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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