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Conserved domains on  [gi|495658291|ref|WP_008382870|]
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adenosyl-hopene transferase HpnH [Rhodovulum sp. PH10]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HpnH super family cl37275
hopanoid biosynthesis associated radical SAM protein HpnH; The sequences represented by this ...
 1-317 0e+00

hopanoid biosynthesis associated radical SAM protein HpnH; The sequences represented by this model are members of the radical SAM superfamily of enzymes (pfam04055). These enzymes utilize an iron-sulfur redox cluster and S-adenosylmethionine to carry out diverse radical mediated reactions. The members of this clade are frequently found in the same locus as squalene-hopene cyclase (SHC, TIGR01507) and other genes associated with the biosynthesis of hopanoid natural products. The linkage between SHC and this radical SAM enzyme is strong; one is nearly always observed in the same genome where the other is found. A hopanoid biosynthesis locus was described in Zymomonas mobilis consisting of the genes HpnA-E and SHC (HpnF). Continuing past SHC are found a phosphorylase enzyme (ZMO0873, i.e. HpnG, TIGR03468) and this radical SAM enzyme (ZMO0874) which we name here HpnH. Granted, in Z. mobilis, HpnH is in a convergent orientation with respect to HpnA-G, but one gene beyond HpnH and running in the same convergent direction is IspH (ZM0875, 4-hydroxy-3-methylbut-2-enyl diphosphate reductase), an essential enzyme of IPP biosynthesis and therefore essential for the biosynthesis of hopanoids. One of the well-described hopanoid intermediates is bacteriohopanetetrol. In the conversion from hopene several reactions must occur in the side chain for which a radical mechanism might be reasonable. These include the four (presumably anaerobic) hydroxylations and a methyl shift.


The actual alignment was detected with superfamily member TIGR03470:

Pssm-ID: 274595 [Multi-domain]  Cd Length: 318  Bit Score: 577.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495658291    1 MAIPFFKEMRIGAYVAKQKLMGRKRYPLVLMLEPLFRCNLACAGCGKIDYPDAILDQRMSVEECLAAADECGAPMVAIPG 80
Cdd:TIGR03470   1 MAVPLRQKLRVGAYIIKQKLKGRKRYPLVLMLEPLFRCNLACAGCGKIQYPDEILKRRLSVEECVAAVEECGAPMVSIPG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495658291   81 GEPLVHKEIGEIVKGLVAKKKFVSLCTNALLLEKKLHLFEPSPYLFFSVHLDGLKEHHDRSVCRAGTFDKAVAAIKAAKA 160
Cdd:TIGR03470  81 GEPLMHPEIDEIVRGLVARKKFVYLCTNALLLEKKLDKFEPSPYLTFSVHLDGLREHHDASVCQEGVFDRAVEAIREAKA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495658291  161 KGFAVNVNATIFEGISAEEIAKYLDFTAELGV-GVSISPGYAYERAPDQQHFLARKRTKELFRKVFALGKGKKWQFMHSS 239
Cdd:TIGR03470 161 RGFRVTTNSTLFNGETPESVAEFFDYLQELGVdGMTISPGYAYEKAPDQDHFLGREQTKELFRDVLANGNGRGWRFNHSP 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495658291  240 LFLDFLAGNQEFLCSPWGMPTRNIFGWQKPCYLVGEGYAKTFKELMETTDWDSYGTGRYEKCADCMAHCGYEPTAADA 317
Cdd:TIGR03470 241 LFLDFLAGNQDYACTPWGMPAYNVFGWQKPCYLLNEGYVPTFRELMEETDWEKYGTGRNPKCANCMVHCGYEPTAVLD 318
 
Name Accession Description Interval E-value
HpnH TIGR03470
hopanoid biosynthesis associated radical SAM protein HpnH; The sequences represented by this ...
 1-317 0e+00

hopanoid biosynthesis associated radical SAM protein HpnH; The sequences represented by this model are members of the radical SAM superfamily of enzymes (pfam04055). These enzymes utilize an iron-sulfur redox cluster and S-adenosylmethionine to carry out diverse radical mediated reactions. The members of this clade are frequently found in the same locus as squalene-hopene cyclase (SHC, TIGR01507) and other genes associated with the biosynthesis of hopanoid natural products. The linkage between SHC and this radical SAM enzyme is strong; one is nearly always observed in the same genome where the other is found. A hopanoid biosynthesis locus was described in Zymomonas mobilis consisting of the genes HpnA-E and SHC (HpnF). Continuing past SHC are found a phosphorylase enzyme (ZMO0873, i.e. HpnG, TIGR03468) and this radical SAM enzyme (ZMO0874) which we name here HpnH. Granted, in Z. mobilis, HpnH is in a convergent orientation with respect to HpnA-G, but one gene beyond HpnH and running in the same convergent direction is IspH (ZM0875, 4-hydroxy-3-methylbut-2-enyl diphosphate reductase), an essential enzyme of IPP biosynthesis and therefore essential for the biosynthesis of hopanoids. One of the well-described hopanoid intermediates is bacteriohopanetetrol. In the conversion from hopene several reactions must occur in the side chain for which a radical mechanism might be reasonable. These include the four (presumably anaerobic) hydroxylations and a methyl shift.


Pssm-ID: 274595 [Multi-domain]  Cd Length: 318  Bit Score: 577.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495658291    1 MAIPFFKEMRIGAYVAKQKLMGRKRYPLVLMLEPLFRCNLACAGCGKIDYPDAILDQRMSVEECLAAADECGAPMVAIPG 80
Cdd:TIGR03470   1 MAVPLRQKLRVGAYIIKQKLKGRKRYPLVLMLEPLFRCNLACAGCGKIQYPDEILKRRLSVEECVAAVEECGAPMVSIPG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495658291   81 GEPLVHKEIGEIVKGLVAKKKFVSLCTNALLLEKKLHLFEPSPYLFFSVHLDGLKEHHDRSVCRAGTFDKAVAAIKAAKA 160
Cdd:TIGR03470  81 GEPLMHPEIDEIVRGLVARKKFVYLCTNALLLEKKLDKFEPSPYLTFSVHLDGLREHHDASVCQEGVFDRAVEAIREAKA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495658291  161 KGFAVNVNATIFEGISAEEIAKYLDFTAELGV-GVSISPGYAYERAPDQQHFLARKRTKELFRKVFALGKGKKWQFMHSS 239
Cdd:TIGR03470 161 RGFRVTTNSTLFNGETPESVAEFFDYLQELGVdGMTISPGYAYEKAPDQDHFLGREQTKELFRDVLANGNGRGWRFNHSP 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495658291  240 LFLDFLAGNQEFLCSPWGMPTRNIFGWQKPCYLVGEGYAKTFKELMETTDWDSYGTGRYEKCADCMAHCGYEPTAADA 317
Cdd:TIGR03470 241 LFLDFLAGNQDYACTPWGMPAYNVFGWQKPCYLLNEGYVPTFRELMEETDWEKYGTGRNPKCANCMVHCGYEPTAVLD 318
DUF3463 pfam11946
Domain of unknown function (DUF3463); This presumed domain is functionally uncharacterized. ...
 194-328 2.99e-91

Domain of unknown function (DUF3463); This presumed domain is functionally uncharacterized. This domain is found in bacteria and archaea. This domain is about 140 amino acids in length. This domain is found associated with pfam04055. This domain has two conserved sequence motifs: CTPWG and PCYL, plus a highly conserved CxxCxxHC motif.


Pssm-ID: 432210  Cd Length: 134  Bit Score: 270.23  E-value: 2.99e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495658291  194 VSISPGYAYERAPDQQHFLARKRTKELFRKVFALGKgKKWQFMHSSLFLDFLAGNQEFLCSPWGMPTRNIFGWQKPCYLV 273
Cdd:pfam11946   1 MTVSPGYSYETAPDQDHFLGREKTKELFRKIFELGK-KGWRFNHSPLYLDFLAGNQEYECTPWGNPTRNPFGWQKPCYLL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 495658291  274 GEGYAKTFKELMETTDWDSYGTGRYEKCADCMAHCGYEPTAADAAFSNPLKLAKL 328
Cdd:pfam11946  80 GEGYAGTFKELMETTDWDKYGVGNNPKCANCMVHCGYEPSAVSDTNGSPLKALRV 134
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
 29-149 7.86e-19

Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, chromosome partitioning, Coenzyme transport and metabolism];


Pssm-ID: 440301 [Multi-domain]  Cd Length: 159  Bit Score: 82.64  E-value: 7.86e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495658291  29 VLMLEPLFRCNLACAGCgkidYPDAILDQR--MSVEECLAAADE---CGAPMVAIPGGEPLVHKEIGEIVKGLVAKKKFV 103
Cdd:COG0535    1 RLQIELTNRCNLRCKHC----YADAGPKRPgeLSTEEAKRILDElaeLGVKVVGLTGGEPLLRPDLFELVEYAKELGIRV 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 495658291 104 SLCTNALLL-EKKLHLFEPSPYLFFSVHLDGL-KEHHDRSVCRAGTFD 149
Cdd:COG0535   77 NLSTNGTLLtEELAERLAEAGLDHVTISLDGVdPETHDKIRGVPGAFD 124
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
 32-206 1.71e-11

Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S cluster and S-adenosylmethionine (SAM) in close proximity. They are characterized by a conserved CxxxCxxC motif, which coordinates the conserved iron-sulfur cluster. Mechanistically, they share the transfer of a single electron from the iron-sulfur cluster to SAM, which leads to its reductive cleavage to methionine and a 5'-deoxyadenosyl radical, which, in turn, abstracts a hydrogen from the appropriately positioned carbon atom. Depending on the enzyme, SAM is consumed during this process or it is restored and reused. Radical SAM enzymes catalyze steps in metabolism, DNA repair, the biosynthesis of vitamins and coenzymes, and the biosynthesis of many antibiotics. Examples are biotin synthase (BioB), lipoyl synthase (LipA), pyruvate formate-lyase (PFL), coproporphyrinogen oxidase (HemN), lysine 2,3-aminomutase (LAM), anaerobic ribonucleotide reductase (ARR), and MoaA, an enzyme of the biosynthesis of molybdopterin.


Pssm-ID: 100105 [Multi-domain]  Cd Length: 204  Bit Score: 63.12  E-value: 1.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495658291  32 LEPLFRCNLACAGCG---KIDYPDAILDQRMSVEECLAAADECGAPMVAIPGGEPLVHKEIGEIVKGLVAKKKF--VSLC 106
Cdd:cd01335    1 LELTRGCNLNCGFCSnpaSKGRGPESPPEIEEILDIVLEAKERGVEVVILTGGEPLLYPELAELLRRLKKELPGfeISIE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495658291 107 TNALLLEKK-LHLFEPSPYLFFSVHLDGLKEHHDRSVCRAG-TFDKAVAAIKAAKAKGFAVNVNATIFEG-ISAEEIAKY 183
Cdd:cd01335   81 TNGTLLTEElLKELKELGLDGVGVSLDSGDEEVADKIRGSGeSFKERLEALKELREAGLGLSTTLLVGLGdEDEEDDLEE 160

                        170       180
                 ....*....|....*....|....*
gi 495658291 184 LDFTAELGV--GVSISPGYAYERAP 206
Cdd:cd01335  161 LELLAEFRSpdRVSLFRLLPEEGTP 185
moaA PRK00164
GTP 3',8-cyclase MoaA;
37-115 3.63e-05

GTP 3',8-cyclase MoaA;


Pssm-ID: 234672 [Multi-domain]  Cd Length: 331  Bit Score: 45.13  E-value: 3.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495658291  37 RCNLACAGCgkidYPDAILD-----QRMSVEE----CLAAADEcGAPMVAIPGGEPLVHKEIGEIVKGLVAKKKF--VSL 105
Cdd:PRK00164  26 RCNFRCTYC----MPEGYLPflpkeELLSLEEierlVRAFVAL-GVRKVRLTGGEPLLRKDLEDIIAALAALPGIrdLAL 100

                         90
                 ....*....|
gi 495658291 106 CTNALLLEKK 115
Cdd:PRK00164 101 TTNGYLLARR 110
 
Name Accession Description Interval E-value
HpnH TIGR03470
hopanoid biosynthesis associated radical SAM protein HpnH; The sequences represented by this ...
 1-317 0e+00

hopanoid biosynthesis associated radical SAM protein HpnH; The sequences represented by this model are members of the radical SAM superfamily of enzymes (pfam04055). These enzymes utilize an iron-sulfur redox cluster and S-adenosylmethionine to carry out diverse radical mediated reactions. The members of this clade are frequently found in the same locus as squalene-hopene cyclase (SHC, TIGR01507) and other genes associated with the biosynthesis of hopanoid natural products. The linkage between SHC and this radical SAM enzyme is strong; one is nearly always observed in the same genome where the other is found. A hopanoid biosynthesis locus was described in Zymomonas mobilis consisting of the genes HpnA-E and SHC (HpnF). Continuing past SHC are found a phosphorylase enzyme (ZMO0873, i.e. HpnG, TIGR03468) and this radical SAM enzyme (ZMO0874) which we name here HpnH. Granted, in Z. mobilis, HpnH is in a convergent orientation with respect to HpnA-G, but one gene beyond HpnH and running in the same convergent direction is IspH (ZM0875, 4-hydroxy-3-methylbut-2-enyl diphosphate reductase), an essential enzyme of IPP biosynthesis and therefore essential for the biosynthesis of hopanoids. One of the well-described hopanoid intermediates is bacteriohopanetetrol. In the conversion from hopene several reactions must occur in the side chain for which a radical mechanism might be reasonable. These include the four (presumably anaerobic) hydroxylations and a methyl shift.


Pssm-ID: 274595 [Multi-domain]  Cd Length: 318  Bit Score: 577.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495658291    1 MAIPFFKEMRIGAYVAKQKLMGRKRYPLVLMLEPLFRCNLACAGCGKIDYPDAILDQRMSVEECLAAADECGAPMVAIPG 80
Cdd:TIGR03470   1 MAVPLRQKLRVGAYIIKQKLKGRKRYPLVLMLEPLFRCNLACAGCGKIQYPDEILKRRLSVEECVAAVEECGAPMVSIPG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495658291   81 GEPLVHKEIGEIVKGLVAKKKFVSLCTNALLLEKKLHLFEPSPYLFFSVHLDGLKEHHDRSVCRAGTFDKAVAAIKAAKA 160
Cdd:TIGR03470  81 GEPLMHPEIDEIVRGLVARKKFVYLCTNALLLEKKLDKFEPSPYLTFSVHLDGLREHHDASVCQEGVFDRAVEAIREAKA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495658291  161 KGFAVNVNATIFEGISAEEIAKYLDFTAELGV-GVSISPGYAYERAPDQQHFLARKRTKELFRKVFALGKGKKWQFMHSS 239
Cdd:TIGR03470 161 RGFRVTTNSTLFNGETPESVAEFFDYLQELGVdGMTISPGYAYEKAPDQDHFLGREQTKELFRDVLANGNGRGWRFNHSP 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495658291  240 LFLDFLAGNQEFLCSPWGMPTRNIFGWQKPCYLVGEGYAKTFKELMETTDWDSYGTGRYEKCADCMAHCGYEPTAADA 317
Cdd:TIGR03470 241 LFLDFLAGNQDYACTPWGMPAYNVFGWQKPCYLLNEGYVPTFRELMEETDWEKYGTGRNPKCANCMVHCGYEPTAVLD 318
DUF3463 pfam11946
Domain of unknown function (DUF3463); This presumed domain is functionally uncharacterized. ...
 194-328 2.99e-91

Domain of unknown function (DUF3463); This presumed domain is functionally uncharacterized. This domain is found in bacteria and archaea. This domain is about 140 amino acids in length. This domain is found associated with pfam04055. This domain has two conserved sequence motifs: CTPWG and PCYL, plus a highly conserved CxxCxxHC motif.


Pssm-ID: 432210  Cd Length: 134  Bit Score: 270.23  E-value: 2.99e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495658291  194 VSISPGYAYERAPDQQHFLARKRTKELFRKVFALGKgKKWQFMHSSLFLDFLAGNQEFLCSPWGMPTRNIFGWQKPCYLV 273
Cdd:pfam11946   1 MTVSPGYSYETAPDQDHFLGREKTKELFRKIFELGK-KGWRFNHSPLYLDFLAGNQEYECTPWGNPTRNPFGWQKPCYLL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 495658291  274 GEGYAKTFKELMETTDWDSYGTGRYEKCADCMAHCGYEPTAADAAFSNPLKLAKL 328
Cdd:pfam11946  80 GEGYAGTFKELMETTDWDKYGVGNNPKCANCMVHCGYEPSAVSDTNGSPLKALRV 134
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
 29-149 7.86e-19

Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, chromosome partitioning, Coenzyme transport and metabolism];


Pssm-ID: 440301 [Multi-domain]  Cd Length: 159  Bit Score: 82.64  E-value: 7.86e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495658291  29 VLMLEPLFRCNLACAGCgkidYPDAILDQR--MSVEECLAAADE---CGAPMVAIPGGEPLVHKEIGEIVKGLVAKKKFV 103
Cdd:COG0535    1 RLQIELTNRCNLRCKHC----YADAGPKRPgeLSTEEAKRILDElaeLGVKVVGLTGGEPLLRPDLFELVEYAKELGIRV 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 495658291 104 SLCTNALLL-EKKLHLFEPSPYLFFSVHLDGL-KEHHDRSVCRAGTFD 149
Cdd:COG0535   77 NLSTNGTLLtEELAERLAEAGLDHVTISLDGVdPETHDKIRGVPGAFD 124
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
 32-206 1.71e-11

Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S cluster and S-adenosylmethionine (SAM) in close proximity. They are characterized by a conserved CxxxCxxC motif, which coordinates the conserved iron-sulfur cluster. Mechanistically, they share the transfer of a single electron from the iron-sulfur cluster to SAM, which leads to its reductive cleavage to methionine and a 5'-deoxyadenosyl radical, which, in turn, abstracts a hydrogen from the appropriately positioned carbon atom. Depending on the enzyme, SAM is consumed during this process or it is restored and reused. Radical SAM enzymes catalyze steps in metabolism, DNA repair, the biosynthesis of vitamins and coenzymes, and the biosynthesis of many antibiotics. Examples are biotin synthase (BioB), lipoyl synthase (LipA), pyruvate formate-lyase (PFL), coproporphyrinogen oxidase (HemN), lysine 2,3-aminomutase (LAM), anaerobic ribonucleotide reductase (ARR), and MoaA, an enzyme of the biosynthesis of molybdopterin.


Pssm-ID: 100105 [Multi-domain]  Cd Length: 204  Bit Score: 63.12  E-value: 1.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495658291  32 LEPLFRCNLACAGCG---KIDYPDAILDQRMSVEECLAAADECGAPMVAIPGGEPLVHKEIGEIVKGLVAKKKF--VSLC 106
Cdd:cd01335    1 LELTRGCNLNCGFCSnpaSKGRGPESPPEIEEILDIVLEAKERGVEVVILTGGEPLLYPELAELLRRLKKELPGfeISIE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495658291 107 TNALLLEKK-LHLFEPSPYLFFSVHLDGLKEHHDRSVCRAG-TFDKAVAAIKAAKAKGFAVNVNATIFEG-ISAEEIAKY 183
Cdd:cd01335   81 TNGTLLTEElLKELKELGLDGVGVSLDSGDEEVADKIRGSGeSFKERLEALKELREAGLGLSTTLLVGLGdEDEEDDLEE 160

                        170       180
                 ....*....|....*....|....*
gi 495658291 184 LDFTAELGV--GVSISPGYAYERAP 206
Cdd:cd01335  161 LELLAEFRSpdRVSLFRLLPEEGTP 185
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
 37-182 5.21e-09

Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual methylations, isomerization, sulphur insertion, ring formation, anaerobic oxidation and protein radical formation.


Pssm-ID: 427681 [Multi-domain]  Cd Length: 159  Bit Score: 54.84  E-value: 5.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495658291   37 RCNLACAGCGKIDYPDAILDQRMSVEECLAAADEC---GAPMVAIPGGEPLVHKEIGEIVKGLVAKK----KFVSLCTNA 109
Cdd:pfam04055   4 GCNLRCTYCAFPSIRARGKGRELSPEEILEEAKELkrlGVEVVILGGGEPLLLPDLVELLERLLKLElaegIRITLETNG 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495658291  110 LLL-EKKLHLFEPSPYLFFSVHLDGLKEHHDRSVCRAGTFDKAVAAIKAAKAKGFAVNV-NATIFEGISAEEIAK 182
Cdd:pfam04055  84 TLLdEELLELLKEAGLDRVSIGLESGDDEVLKLINRGHTFEEVLEALELLREAGIPVVTdNIVGLPGETDEDLEE 158
QueE COG0602
Organic radical activating enzyme NrdG/QueE [Coenzyme transport and metabolism]; Organic ...
 35-108 2.43e-08

Organic radical activating enzyme NrdG/QueE [Coenzyme transport and metabolism]; Organic radical activating enzyme NrdG/QueE is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440367 [Multi-domain]  Cd Length: 205  Bit Score: 53.60  E-value: 2.43e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495658291  35 LFRCNLACAGCgkiDYP---DAILDQRMSVEECLAAADECGAPMVAIPGGEPLVHKEIGEIVKGLVAKKKFVSLCTN 108
Cdd:COG0602   27 LAGCNLRCSWC---DTKyawDGEGGKRMSAEEILEEVAALGARHVVITGGEPLLQDDLAELLEALKDAGYEVALETN 100
AslB COG0641
Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, ...
 30-309 3.66e-08

Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440406 [Multi-domain]  Cd Length: 349  Bit Score: 54.61  E-value: 3.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495658291  30 LMLEPLFRCNLACAGC--GKIDYPDailDQRMSVEECLAAAD-------ECGAPMVAIPGGEPLVHKE-----IGEIVKG 95
Cdd:COG0641    3 LVLKPTSRCNLRCSYCyySEGDEGS---RRRMSEETAEKAIDfliessgPGKELTITFFGGEPLLNFDfikeiVEYARKY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495658291  96 LVAKKKFV-SLCTNALLL-EKKLHLFEPspyLFFSVH--LDGLKEHHDRSvcR-----AGTFDKAVAAIKAAKAKGFAVN 166
Cdd:COG0641   80 AKKGKKIRfSIQTNGTLLdDEWIDFLKE---NGFSVGisLDGPKEIHDRN--RvtkngKGSFDRVMRNIKLLKEHGVEVN 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495658291 167 VNATIFEGiSAEEIAKYLDFTAELGV-GVSISPGYAYERAPdqqHFLARKRTKELFRKVFAL---GKGKKWQFMHSSLFL 242
Cdd:COG0641  155 IRCTVTRE-NLDDPEELYDFLKELGFrSIQFNPVVEEGEAD---YSLTPEDYGEFLIELFDEwleRDGGKIFVREFDILL 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495658291 243 DFLAGNQEFLC----------SPWGmptrNIFgwqkPCY-LVGEGYAK-------TFKELMETTDWDSYGTGRY----EK 300
Cdd:COG0641  231 AGLLPPCSSPCvgaggnylvvDPDG----DIY----PCDeFVGDPEFRlgnvfdgSLAELLDSPKLRAFGREKNvlldEE 302

                        330
                 ....*....|.
gi 495658291 301 CADCMAH--CG 309
Cdd:COG0641  303 CRSCPYLplCG 313
MoaA COG2896
GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and ...
 37-117 3.18e-06

GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and metabolism]; GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 442141 [Multi-domain]  Cd Length: 329  Bit Score: 48.52  E-value: 3.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495658291  37 RCNLACAGC---GKIDYPDAilDQRMSVEECL---AAADECGAPMVAIPGGEPLVHKEIGEIVKGLVAKKKF--VSLCTN 108
Cdd:COG2896   23 RCNFRCTYCmpeEGYQFLPK--EELLSFEEIErlvRAFVELGVRKIRLTGGEPLLRKDLPELIARLAALPGIedLALTTN 100


                 ....*....
gi 495658291 109 ALLLEKKLH 117
Cdd:COG2896  101 GSLLARYAE 109
moaA PRK00164
GTP 3',8-cyclase MoaA;
37-115 3.63e-05

GTP 3',8-cyclase MoaA;


Pssm-ID: 234672 [Multi-domain]  Cd Length: 331  Bit Score: 45.13  E-value: 3.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495658291  37 RCNLACAGCgkidYPDAILD-----QRMSVEE----CLAAADEcGAPMVAIPGGEPLVHKEIGEIVKGLVAKKKF--VSL 105
Cdd:PRK00164  26 RCNFRCTYC----MPEGYLPflpkeELLSLEEierlVRAFVAL-GVRKVRLTGGEPLLRKDLEDIIAALAALPGIrdLAL 100

                         90
                 ....*....|
gi 495658291 106 CTNALLLEKK 115
Cdd:PRK00164 101 TTNGYLLARR 110
PLN02951 PLN02951
Molybderin biosynthesis protein CNX2
 37-117 4.50e-05

Molybderin biosynthesis protein CNX2


Pssm-ID: 215513 [Multi-domain]  Cd Length: 373  Bit Score: 45.13  E-value: 4.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495658291  37 RCNLACAGCgkidYPDAILD-----QRMSVEECLAAAD---ECGAPMVAIPGGEPLVHKEIGEIVKGLVAKK--KFVSLC 106
Cdd:PLN02951  67 RCNLRCQYC----MPEEGVEltpksHLLSQDEIVRLAGlfvAAGVDKIRLTGGEPTLRKDIEDICLQLSSLKglKTLAMT 142

                         90
                 ....*....|.
gi 495658291 107 TNALLLEKKLH 117
Cdd:PLN02951 143 TNGITLSRKLP 153
SCM_rSAM_ScmE TIGR04250
SynChlorMet cassette radical SAM/SPASM protein ScmE; A biosynthesis cassette found in ...
 37-148 4.85e-04

SynChlorMet cassette radical SAM/SPASM protein ScmE; A biosynthesis cassette found in Syntrophobacter fumaroxidans MPOB, Chlorobium limicola DSM 245, Methanocella paludicola SANAE, and delta proteobacterium NaphS2 contains two PqqE-like radical SAM/SPASM domain proteins, a PqqD homolog, and a conserved hypothetical protein. These components suggest modification of a ribosomally produced peptide precursor, but the precursor has not been identified. Of the two PqqE homologs of the cassette, this family is the closer in sequence.


Pssm-ID: 211973 [Multi-domain]  Cd Length: 358  Bit Score: 41.77  E-value: 4.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495658291   37 RCNLACAGCGKIDyPDAILDQRMSVEECL---AAADECGAPMVAIPGGEPLVHKEIGEIVKGLVAKKKFVSLCTNALLLE 113
Cdd:TIGR04250  12 RCNLRCRYCSHFS-SAAETPTDLETAEWLrffRELNRCSVLRVVLSGGEPFMRSDFREIIDGIVKNRMRFSILSNGTLIT 90

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 495658291  114 KKLHLFEPSPYL--FFSVHLDG-LKEHHDRsvCRA-GTF 148
Cdd:TIGR04250  91 DAIASFLAATRRcdYVQVSIDGsTPGTHDR--LRGtGSF 127
 
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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