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Conserved domains on  [gi|42543470|pdb|1R30|A]
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Chain A, Biotin synthase

Protein Classification

biotin synthase BioB( domain architecture ID 11423440)

biotin synthase BioB catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
BioB COG0502
Biotin synthase or related enzyme [Coenzyme transport and metabolism]; Biotin synthase or ...
29-335 0e+00

Biotin synthase or related enzyme [Coenzyme transport and metabolism]; Biotin synthase or related enzyme is part of the Pathway/BioSystem: Biotin biosynthesis


:

Pssm-ID: 440268 [Multi-domain]  Cd Length: 308  Bit Score: 514.60  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R30_A       29 RWTLSQVTELFEKP---LLDLLFEAQQVhRQHFDPRQVQVSTLLSIKTGACPEDCKYCPQSSRYKTGLEAERLMEVEQVL 105
Cdd:COG0502   1 DLTREEALALLELPdeeLEDLLAAADEV-REHFFGNKVQLCGLINIKSGGCPEDCKYCGQSAHNKTGIERYRLLSVEEIL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R30_A      106 ESARKAKAAGSTRFCMGAAWKNPHERDMPYLEQMVQGVK-AMGLEACMTLGTLSESQAQRLANAGLDYYNHNLDTSPEFY 184
Cdd:COG0502  80 EAARAAKEAGARRFCLVASGRDPSDRDFEKVLEIVRAIKeELGLEVCASLGELSEEQAKRLKEAGVDRYNHNLETSPELY 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R30_A      185 GNIITTRTYQERLDTLEKVRDAGIKVCSGGIVGLGETVKDRAGLLLQLANLptPPESVPINMLVKVKGTPLADNDDVDAF 264
Cdd:COG0502 160 PKICTTHTYEDRLDTLKNAREAGLEVCSGGIVGMGETLEDRADLLLTLAEL--DPDSVPINPLIPIPGTPLEDAPPLDPE 237
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1R30_A      265 DFIRTIAVARIMMPTSYVRLSAGREQMNEQTQAMCFMAGANSIFYGCKLLTTPNPEEDKDLQLFRKLGLNP 335
Cdd:COG0502 238 EFLRTIAVARLLLPDALIRLSGGRETLLRDGQALALLAGANSIMPGNKYLTTPGRSVEEDLAMIEDLGLEV 308
 
Name Accession Description Interval E-value
BioB COG0502
Biotin synthase or related enzyme [Coenzyme transport and metabolism]; Biotin synthase or ...
29-335 0e+00

Biotin synthase or related enzyme [Coenzyme transport and metabolism]; Biotin synthase or related enzyme is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 440268 [Multi-domain]  Cd Length: 308  Bit Score: 514.60  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R30_A       29 RWTLSQVTELFEKP---LLDLLFEAQQVhRQHFDPRQVQVSTLLSIKTGACPEDCKYCPQSSRYKTGLEAERLMEVEQVL 105
Cdd:COG0502   1 DLTREEALALLELPdeeLEDLLAAADEV-REHFFGNKVQLCGLINIKSGGCPEDCKYCGQSAHNKTGIERYRLLSVEEIL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R30_A      106 ESARKAKAAGSTRFCMGAAWKNPHERDMPYLEQMVQGVK-AMGLEACMTLGTLSESQAQRLANAGLDYYNHNLDTSPEFY 184
Cdd:COG0502  80 EAARAAKEAGARRFCLVASGRDPSDRDFEKVLEIVRAIKeELGLEVCASLGELSEEQAKRLKEAGVDRYNHNLETSPELY 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R30_A      185 GNIITTRTYQERLDTLEKVRDAGIKVCSGGIVGLGETVKDRAGLLLQLANLptPPESVPINMLVKVKGTPLADNDDVDAF 264
Cdd:COG0502 160 PKICTTHTYEDRLDTLKNAREAGLEVCSGGIVGMGETLEDRADLLLTLAEL--DPDSVPINPLIPIPGTPLEDAPPLDPE 237
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1R30_A      265 DFIRTIAVARIMMPTSYVRLSAGREQMNEQTQAMCFMAGANSIFYGCKLLTTPNPEEDKDLQLFRKLGLNP 335
Cdd:COG0502 238 EFLRTIAVARLLLPDALIRLSGGRETLLRDGQALALLAGANSIMPGNKYLTTPGRSVEEDLAMIEDLGLEV 308
bioB TIGR00433
biotin synthase; Catalyzes the last step of the biotin biosynthesis pathway. All members of ...
37-334 0e+00

biotin synthase; Catalyzes the last step of the biotin biosynthesis pathway. All members of the seed alignment are in the immediate gene neighborhood of a bioA gene. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273075 [Multi-domain]  Cd Length: 296  Bit Score: 510.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R30_A         37 ELFEKPLLDLLFEAQQVHRQHFdPRQVQVSTLLSIKTGACPEDCKYCPQSSRYKTGLEAERLMEVEQVLESARKAKAAGS 116
Cdd:TIGR00433   2 ELPDEPLLDLLAAAQRIRRHFF-GNKVDLCSIINAKSGGCPEDCKYCAQSAHYKTGIEKYPLLSVEEVLEAAKKAKAAGA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R30_A        117 TRFCMGAAWKNPHERDMPYLEQMVQGVKAM-GLEACMTLGTLSESQAQRLANAGLDYYNHNLDTSPEFYGNIITTRTYQE 195
Cdd:TIGR00433  81 TRFCMVTSGRGPSDREFEKVLEAIREIKEEtGLEVCASLGLLSEEQAQRLKEAGVDRYNHNLETSPSYYPNICTTHTYDD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R30_A        196 RLDTLEKVRDAGIKVCSGGIVGLGETVKDRAGLLLQLANLptPPESVPINMLVKVKGTPLADNDDVDAFDFIRTIAVARI 275
Cdd:TIGR00433 161 RLETLKRARKAGLSVCSGGIIGMGETMEDRIELAFALAEL--DVDSVPINFLVPIPGTPLEDAPPLDPEECLRTIALFRF 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
1R30_A        276 MMPTSYVRLSAGREQMNEQTQAMCFMAGANSIFYGCkLLTTPNPEEDKDLQLFRKLGLN 334
Cdd:TIGR00433 239 IMPDAEIRLAGGRELMLRELQALCFLAGANSIFTGD-YLTTAGPEAEEDLEMIEDLGLE 296
PLN02389 PLN02389
biotin synthase
27-336 1.56e-165

biotin synthase


Pssm-ID: 215219 [Multi-domain]  Cd Length: 379  Bit Score: 467.79  E-value: 1.56e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R30_A        27 RPRWTLSQVTELFEKPLLDLLFEAQQVHRQHFDPRQVQVSTLLSIKTGACPEDCKYCPQSSRYKTGLEAERLMEVEQVLE 106
Cdd:PLN02389  44 RNDWTRDEIKEVYDSPLLDLLFHGAQVHRHAHDPREVQQCTLLSIKTGGCSEDCSYCPQSSRYDTGVKAQKLMSKDDVLE 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R30_A       107 SARKAKAAGSTRFCMGAAWKNPHERDMPY--LEQMVQGVKAMGLEACMTLGTLSESQAQRLANAGLDYYNHNLDTSPEFY 184
Cdd:PLN02389 124 AAKRAKEAGSTRFCMGAAWRDTVGRKTNFnqILEYVKEIRGMGMEVCCTLGMLEKEQAAQLKEAGLTAYNHNLDTSREYY 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R30_A       185 GNIITTRTYQERLDTLEKVRDAGIKVCSGGIVGLGETVKDRAGLLLQLANLPTPPESVPINMLVKVKGTPLADNDDVDAF 264
Cdd:PLN02389 204 PNVITTRSYDDRLETLEAVREAGISVCSGGIIGLGEAEEDRVGLLHTLATLPEHPESVPINALVAVKGTPLEDQKPVEIW 283
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1R30_A       265 DFIRTIAVARIMMPTSYVRLSAGREQMNEQTQAMCFMAGANSIFYGCKLLTTPNPEEDKDLQLFRKLGLNPQ 336
Cdd:PLN02389 284 EMVRMIATARIVMPKAMVRLSAGRVRFSMAEQALCFLAGANSIFTGDKLLTTPNNDFDADQAMFKELGLIPK 355
BATS smart00876
Biotin and Thiamin Synthesis associated domain; Biotin synthase (BioB), , catalyses the last ...
243-335 2.57e-42

Biotin and Thiamin Synthesis associated domain; Biotin synthase (BioB), , catalyses the last step of the biotin biosynthetic pathway. The reaction consists in the introduction of a sulphur atom into dethiobiotin. BioB functions as a homodimer. Thiamin synthesis if a complex process involving at least six gene products (ThiFSGH, ThiI and ThiJ). Two of the proteins required for the biosynthesis of the thiazole moiety of thiamine (vitamin B(1)) are ThiG and ThiH (this entry) and form a heterodimer. Both of these reactions are thought of involve the binding of co-factors, and both function as dimers.. This domain therefore may be involved in co-factor binding or dimerisation.


Pssm-ID: 214877 [Multi-domain]  Cd Length: 94  Bit Score: 142.62  E-value: 2.57e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R30_A         243 PINMLVKVKGTPLADN-DDVDAFDFIRTIAVARIMMPTSYVRLSAGREQMNEQTQAMCFMAGANSIFYGCKLLTTPNPEE 321
Cdd:smart00876   1 PINRLRPIEGTPLEDPpPPVSPEEFLRTIAAARLALPDAGIRLSTGREALLRDLQALCFSAGANSIFGGDKYLTTSGPRS 80
                           90
                   ....*....|....
1R30_A         322 DKDLQLFRKLGLNP 335
Cdd:smart00876  81 ADDVAMLEKLGLEP 94
BATS pfam06968
Biotin and Thiamin Synthesis associated domain; Biotin synthase (BioB), EC:2.8.1.6, catalyzes ...
247-332 9.13e-39

Biotin and Thiamin Synthesis associated domain; Biotin synthase (BioB), EC:2.8.1.6, catalyzes the last step of the biotin biosynthetic pathway. The reaction consists in the introduction of a sulphur atom into dethiobiotin. BioB functions as a homodimer. Thiamin synthesis if a complex process involving at least six gene products (ThiFSGH, ThiI and ThiJ). Two of the proteins required for the biosynthesis of the thiazole moiety of thiamine (vitamin B(1)) are ThiG and ThiH (this family) and form a heterodimer. Both of these reactions are thought of involve the binding of co-factors, and both function as dimers. This domain therefore may be involved in co-factor binding or dimerization (Finn, RD personal observation).


Pssm-ID: 462054 [Multi-domain]  Cd Length: 85  Bit Score: 133.35  E-value: 9.13e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R30_A        247 LVKVKGTPLADNDDVDAFDFIRTIAVARIMMPTSYVRLSAGREQMNEqTQAMCFMAGANSIFYGCKLLTTPNPEEDKDLQ 326
Cdd:pfam06968   1 LRPIPGTPLENQPPLSPEEALRTIAAFRLILPDAGIRLAGGRESMLF-RQALLFLAGANSISAGSKFLTTDGRSPDEDIA 79

                  ....*.
1R30_A        327 LFRKLG 332
Cdd:pfam06968  80 MLEDLG 85
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
73-272 1.01e-21

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: 91.63  E-value: 1.01e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R30_A       73 TGACPEDCKYCPQSSRYKTGLEAERlmEVEQVLESARKAKAAGSTRFCMGAAWKNPHERDMPYLEQMVQgvKAMGLEACM 152
Cdd:cd01335   4 TRGCNLNCGFCSNPASKGRGPESPP--EIEEILDIVLEAKERGVEVVILTGGEPLLYPELAELLRRLKK--ELPGFEISI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R30_A      153 -TLGT-LSESQAQRLANAGLDYYNHNLDTSPEFYGNII--TTRTYQERLDTLEKVRDAGIKVCSGGIVGLG-ETVKDRAG 227
Cdd:cd01335  80 eTNGTlLTEELLKELKELGLDGVGVSLDSGDEEVADKIrgSGESFKERLEALKELREAGLGLSTTLLVGLGdEDEEDDLE 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
1R30_A      228 LLLQLANLPtPPESVPINMLVKVKGTPLADNDDV-DAFDFIRTIAV 272
Cdd:cd01335 160 ELELLAEFR-SPDRVSLFRLLPEEGTPLELAAPVvPAEKLLRLIAA 204
 
Name Accession Description Interval E-value
BioB COG0502
Biotin synthase or related enzyme [Coenzyme transport and metabolism]; Biotin synthase or ...
29-335 0e+00

Biotin synthase or related enzyme [Coenzyme transport and metabolism]; Biotin synthase or related enzyme is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 440268 [Multi-domain]  Cd Length: 308  Bit Score: 514.60  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R30_A       29 RWTLSQVTELFEKP---LLDLLFEAQQVhRQHFDPRQVQVSTLLSIKTGACPEDCKYCPQSSRYKTGLEAERLMEVEQVL 105
Cdd:COG0502   1 DLTREEALALLELPdeeLEDLLAAADEV-REHFFGNKVQLCGLINIKSGGCPEDCKYCGQSAHNKTGIERYRLLSVEEIL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R30_A      106 ESARKAKAAGSTRFCMGAAWKNPHERDMPYLEQMVQGVK-AMGLEACMTLGTLSESQAQRLANAGLDYYNHNLDTSPEFY 184
Cdd:COG0502  80 EAARAAKEAGARRFCLVASGRDPSDRDFEKVLEIVRAIKeELGLEVCASLGELSEEQAKRLKEAGVDRYNHNLETSPELY 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R30_A      185 GNIITTRTYQERLDTLEKVRDAGIKVCSGGIVGLGETVKDRAGLLLQLANLptPPESVPINMLVKVKGTPLADNDDVDAF 264
Cdd:COG0502 160 PKICTTHTYEDRLDTLKNAREAGLEVCSGGIVGMGETLEDRADLLLTLAEL--DPDSVPINPLIPIPGTPLEDAPPLDPE 237
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1R30_A      265 DFIRTIAVARIMMPTSYVRLSAGREQMNEQTQAMCFMAGANSIFYGCKLLTTPNPEEDKDLQLFRKLGLNP 335
Cdd:COG0502 238 EFLRTIAVARLLLPDALIRLSGGRETLLRDGQALALLAGANSIMPGNKYLTTPGRSVEEDLAMIEDLGLEV 308
bioB TIGR00433
biotin synthase; Catalyzes the last step of the biotin biosynthesis pathway. All members of ...
37-334 0e+00

biotin synthase; Catalyzes the last step of the biotin biosynthesis pathway. All members of the seed alignment are in the immediate gene neighborhood of a bioA gene. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273075 [Multi-domain]  Cd Length: 296  Bit Score: 510.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R30_A         37 ELFEKPLLDLLFEAQQVHRQHFdPRQVQVSTLLSIKTGACPEDCKYCPQSSRYKTGLEAERLMEVEQVLESARKAKAAGS 116
Cdd:TIGR00433   2 ELPDEPLLDLLAAAQRIRRHFF-GNKVDLCSIINAKSGGCPEDCKYCAQSAHYKTGIEKYPLLSVEEVLEAAKKAKAAGA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R30_A        117 TRFCMGAAWKNPHERDMPYLEQMVQGVKAM-GLEACMTLGTLSESQAQRLANAGLDYYNHNLDTSPEFYGNIITTRTYQE 195
Cdd:TIGR00433  81 TRFCMVTSGRGPSDREFEKVLEAIREIKEEtGLEVCASLGLLSEEQAQRLKEAGVDRYNHNLETSPSYYPNICTTHTYDD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R30_A        196 RLDTLEKVRDAGIKVCSGGIVGLGETVKDRAGLLLQLANLptPPESVPINMLVKVKGTPLADNDDVDAFDFIRTIAVARI 275
Cdd:TIGR00433 161 RLETLKRARKAGLSVCSGGIIGMGETMEDRIELAFALAEL--DVDSVPINFLVPIPGTPLEDAPPLDPEECLRTIALFRF 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
1R30_A        276 MMPTSYVRLSAGREQMNEQTQAMCFMAGANSIFYGCkLLTTPNPEEDKDLQLFRKLGLN 334
Cdd:TIGR00433 239 IMPDAEIRLAGGRELMLRELQALCFLAGANSIFTGD-YLTTAGPEAEEDLEMIEDLGLE 296
PLN02389 PLN02389
biotin synthase
27-336 1.56e-165

biotin synthase


Pssm-ID: 215219 [Multi-domain]  Cd Length: 379  Bit Score: 467.79  E-value: 1.56e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R30_A        27 RPRWTLSQVTELFEKPLLDLLFEAQQVHRQHFDPRQVQVSTLLSIKTGACPEDCKYCPQSSRYKTGLEAERLMEVEQVLE 106
Cdd:PLN02389  44 RNDWTRDEIKEVYDSPLLDLLFHGAQVHRHAHDPREVQQCTLLSIKTGGCSEDCSYCPQSSRYDTGVKAQKLMSKDDVLE 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R30_A       107 SARKAKAAGSTRFCMGAAWKNPHERDMPY--LEQMVQGVKAMGLEACMTLGTLSESQAQRLANAGLDYYNHNLDTSPEFY 184
Cdd:PLN02389 124 AAKRAKEAGSTRFCMGAAWRDTVGRKTNFnqILEYVKEIRGMGMEVCCTLGMLEKEQAAQLKEAGLTAYNHNLDTSREYY 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R30_A       185 GNIITTRTYQERLDTLEKVRDAGIKVCSGGIVGLGETVKDRAGLLLQLANLPTPPESVPINMLVKVKGTPLADNDDVDAF 264
Cdd:PLN02389 204 PNVITTRSYDDRLETLEAVREAGISVCSGGIIGLGEAEEDRVGLLHTLATLPEHPESVPINALVAVKGTPLEDQKPVEIW 283
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1R30_A       265 DFIRTIAVARIMMPTSYVRLSAGREQMNEQTQAMCFMAGANSIFYGCKLLTTPNPEEDKDLQLFRKLGLNPQ 336
Cdd:PLN02389 284 EMVRMIATARIVMPKAMVRLSAGRVRFSMAEQALCFLAGANSIFTGDKLLTTPNNDFDADQAMFKELGLIPK 355
PRK08508 PRK08508
biotin synthase; Provisional
70-334 1.75e-62

biotin synthase; Provisional


Pssm-ID: 236279 [Multi-domain]  Cd Length: 279  Bit Score: 201.39  E-value: 1.75e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R30_A        70 SIKTGACPEDCKYCPQSSRYKTGLEAERLMEVEQVLESARKAKAAGSTRFCMGAAWKNPHERDMPYLEQMVQGVKAMGLE 149
Cdd:PRK08508  11 NISSGNCKEDCKYCTQSAHYKADIKRYKRKDIEQIVQEAKMAKANGALGFCLVTSGRGLDDKKLEYVAEAAKAVKKEVPG 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R30_A       150 ----ACMtlGTLSESQAQRLANAGLDYYNHNLDTSPEFYGNIITTRTYQERLDTLEKVRDAGIKVCSGGIVGLGETVKDR 225
Cdd:PRK08508  91 lhliACN--GTASVEQLKELKKAGIFSYNHNLETSKEFFPKICTTHTWEERFQTCENAKEAGLGLCSGGIFGLGESWEDR 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R30_A       226 AGLLLQLANLptPPESVPINMLVKVKGTPLADN--DDVDAFDFIRTiavARIMMPTSYVRLSAGREQMNEQTQAMCFMAG 303
Cdd:PRK08508 169 ISFLKSLASL--SPHSTPINFFIPNPALPLKAPtlSADEALEIVRL---AKEALPNARLMVAGGREVVFGERQYEIFEAG 243
                        250       260       270
                 ....*....|....*....|....*....|.
1R30_A       304 ANSIFYGcKLLTTPNPEEDKDLQLFRKLGLN 334
Cdd:PRK08508 244 ANAIVIG-DYLTTKGEAPKKDIEKLKSLGFE 273
BATS smart00876
Biotin and Thiamin Synthesis associated domain; Biotin synthase (BioB), , catalyses the last ...
243-335 2.57e-42

Biotin and Thiamin Synthesis associated domain; Biotin synthase (BioB), , catalyses the last step of the biotin biosynthetic pathway. The reaction consists in the introduction of a sulphur atom into dethiobiotin. BioB functions as a homodimer. Thiamin synthesis if a complex process involving at least six gene products (ThiFSGH, ThiI and ThiJ). Two of the proteins required for the biosynthesis of the thiazole moiety of thiamine (vitamin B(1)) are ThiG and ThiH (this entry) and form a heterodimer. Both of these reactions are thought of involve the binding of co-factors, and both function as dimers.. This domain therefore may be involved in co-factor binding or dimerisation.


Pssm-ID: 214877 [Multi-domain]  Cd Length: 94  Bit Score: 142.62  E-value: 2.57e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R30_A         243 PINMLVKVKGTPLADN-DDVDAFDFIRTIAVARIMMPTSYVRLSAGREQMNEQTQAMCFMAGANSIFYGCKLLTTPNPEE 321
Cdd:smart00876   1 PINRLRPIEGTPLEDPpPPVSPEEFLRTIAAARLALPDAGIRLSTGREALLRDLQALCFSAGANSIFGGDKYLTTSGPRS 80
                           90
                   ....*....|....
1R30_A         322 DKDLQLFRKLGLNP 335
Cdd:smart00876  81 ADDVAMLEKLGLEP 94
BATS pfam06968
Biotin and Thiamin Synthesis associated domain; Biotin synthase (BioB), EC:2.8.1.6, catalyzes ...
247-332 9.13e-39

Biotin and Thiamin Synthesis associated domain; Biotin synthase (BioB), EC:2.8.1.6, catalyzes the last step of the biotin biosynthetic pathway. The reaction consists in the introduction of a sulphur atom into dethiobiotin. BioB functions as a homodimer. Thiamin synthesis if a complex process involving at least six gene products (ThiFSGH, ThiI and ThiJ). Two of the proteins required for the biosynthesis of the thiazole moiety of thiamine (vitamin B(1)) are ThiG and ThiH (this family) and form a heterodimer. Both of these reactions are thought of involve the binding of co-factors, and both function as dimers. This domain therefore may be involved in co-factor binding or dimerization (Finn, RD personal observation).


Pssm-ID: 462054 [Multi-domain]  Cd Length: 85  Bit Score: 133.35  E-value: 9.13e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R30_A        247 LVKVKGTPLADNDDVDAFDFIRTIAVARIMMPTSYVRLSAGREQMNEqTQAMCFMAGANSIFYGCKLLTTPNPEEDKDLQ 326
Cdd:pfam06968   1 LRPIPGTPLENQPPLSPEEALRTIAAFRLILPDAGIRLAGGRESMLF-RQALLFLAGANSISAGSKFLTTDGRSPDEDIA 79

                  ....*.
1R30_A        327 LFRKLG 332
Cdd:pfam06968  80 MLEDLG 85
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
66-276 2.60e-38

Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, coproporphyrinogen III oxidase, biotin synthase and MiaB families, and includes a representative in the eukaryotic elongator subunit, Elp-3. Some members of the family are methyltransferases.


Pssm-ID: 214792 [Multi-domain]  Cd Length: 216  Bit Score: 136.38  E-value: 2.60e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R30_A          66 STLLSIKTGACPEDCKYCPQSSRYKTgleaERLMEVEQVLESARKAKAAG-----STRFCMGAAWKNPHERD-MPYLEQM 139
Cdd:smart00729   1 PLALYIITRGCPRRCTFCSFPSLRGK----LRSRYLEALVREIELLAEKGekeglVGTVFIGGGTPTLLSPEqLEELLEA 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R30_A         140 VQGVKA----MGLEACMTLGTLSESQAQRLANAGLDYYNHNLDT-SPEFYGNIITTRTYQERLDTLEKVRDAG-IKVCSG 213
Cdd:smart00729  77 IREILGlakdVEITIETRPDTLTEELLEALKEAGVNRVSLGVQSgDDEVLKAINRGHTVEDVLEAVELLREAGpIKVSTD 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
1R30_A         214 GIVGL-GETVKDRAGLLLQLANLptPPESVPINMLVKVKGTPLAdnDDVDAFDFIRTIAVARIM 276
Cdd:smart00729 157 LIVGLpGETEEDFEETLKLLKEL--GPDRVSIFPLSPRPGTPLA--KMYKRLKPPTKEERAELL 216
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
73-272 1.01e-21

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: 91.63  E-value: 1.01e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R30_A       73 TGACPEDCKYCPQSSRYKTGLEAERlmEVEQVLESARKAKAAGSTRFCMGAAWKNPHERDMPYLEQMVQgvKAMGLEACM 152
Cdd:cd01335   4 TRGCNLNCGFCSNPASKGRGPESPP--EIEEILDIVLEAKERGVEVVILTGGEPLLYPELAELLRRLKK--ELPGFEISI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R30_A      153 -TLGT-LSESQAQRLANAGLDYYNHNLDTSPEFYGNII--TTRTYQERLDTLEKVRDAGIKVCSGGIVGLG-ETVKDRAG 227
Cdd:cd01335  80 eTNGTlLTEELLKELKELGLDGVGVSLDSGDEEVADKIrgSGESFKERLEALKELREAGLGLSTTLLVGLGdEDEEDDLE 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
1R30_A      228 LLLQLANLPtPPESVPINMLVKVKGTPLADNDDV-DAFDFIRTIAV 272
Cdd:cd01335 160 ELELLAEFR-SPDRVSLFRLLPEEGTPLELAAPVvPAEKLLRLIAA 204
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
73-225 2.59e-21

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: 89.51  E-value: 2.59e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R30_A         73 TGACPEDCKYCPQSSRYKTGleAERLMEVEQVLESARKAKAAGSTRFCMG-----AAWKNPHERDMpYLEQMVQGVKAMG 147
Cdd:pfam04055   2 TRGCNLRCTYCAFPSIRARG--KGRELSPEEILEEAKELKRLGVEVVILGggeplLLPDLVELLER-LLKLELAEGIRIT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R30_A        148 LEACMTLgtLSESQAQRLANAGLDYYNHNLDTSPEFYGNII-TTRTYQERLDTLEKVRDAGIKVCSGGIVGL-GETVKDR 225
Cdd:pfam04055  79 LETNGTL--LDEELLELLKEAGLDRVSIGLESGDDEVLKLInRGHTFEEVLEALELLREAGIPVVTDNIVGLpGETDEDL 156
ThiH COG1060
2-iminoacetate synthase ThiH/Menaquinone biosynthesis enzymes MqnC and MqnE [Coenzyme ...
31-278 9.49e-20

2-iminoacetate synthase ThiH/Menaquinone biosynthesis enzymes MqnC and MqnE [Coenzyme transport and metabolism]; 2-iminoacetate synthase ThiH/Menaquinone biosynthesis enzymes MqnC and MqnE is part of the Pathway/BioSystem: Thiamine biosynthesis


Pssm-ID: 440680 [Multi-domain]  Cd Length: 351  Bit Score: 89.03  E-value: 9.49e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R30_A       31 TLSQVTELFE---KPLLDLLFEAQQVHRQHFDPRQvqvstLLSIK-----TGACPEDCKYCPqSSRYKTGLEAeRLMEVE 102
Cdd:COG1060  13 SLEDALALLSpaaADLEELAELADELRRRRFGNTV-----TFVVNrpinlTNVCVNGCKFCA-FSRDNGDIDR-YTLSPE 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R30_A      103 QVLESARKAKAAGSTRFCM--GaawKNPHErDMPYLEQMVQGVKAM--GLE-ACMT----------LGTLSESQAQRLAN 167
Cdd:COG1060  86 EILEEAEEAKALGATEILLvgG---EHPDL-PLEYYLDLLRAIKERfpNIHiHALSpeeiahlaraSGLSVEEVLERLKE 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R30_A      168 AGLDYYnhnldtsPEF--------YGNIITT--RTYQERLDTLEKVRDAGIKVCSGGIVGLGETVKDRAGLLLQLANLP- 236
Cdd:COG1060 162 AGLDSL-------PGGgaeilddeVRHPIGPgkIDYEEWLEVMERAHELGIRTTATMLYGHVETREERVDHLLHLRELQd 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
1R30_A      237 -TP--PESVPINMlvKVKGTPLADN-DDVDAFDFIRTIAVARIMMP 278
Cdd:COG1060 235 eTGgfTEFIPLRF--RPANTPLYLErPGVSDRELLKLIAVARLFLP 278
F420_cofG TIGR03550
7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase, CofG subunit; This model represents ...
73-278 1.68e-11

7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase, CofG subunit; This model represents either a subunit or a domain, depending on whether or not the genes are fused, of a bifunctional protein that completes the synthesis of 7,8-didemethyl-8-hydroxy-5-deazariboflavin, or FO. FO is the chromophore of coenzyme F(420), involved in methanogenesis in methanogenic archaea but found in certain other lineages as well. The chromophore also occurs as a cofactor in DNA photolyases in Cyanobacteria. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 132589 [Multi-domain]  Cd Length: 322  Bit Score: 64.62  E-value: 1.68e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R30_A         73 TGACPEDCKYCpqsSRYKTGLEAER-LMEVEQVLESARKAKAAGSTR--FCMGaawKNPHERDMPYLEQ--------MVQ 141
Cdd:TIGR03550  11 TRLCRNRCGYC---TFRRPPGELEAaLLSPEEVLEILRKGAAAGCTEalFTFG---EKPEERYPEAREWlaemgydsTLE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R30_A        142 GVKAMG---LEACMTL-----GTLSESQAQRLA--NA--GLdyynhNLDTSPEFYGNIITTRTY-----QERLDTLEKVR 204
Cdd:TIGR03550  85 YLRELCelaLEETGLLphtnpGVMSRDELARLKpvNAsmGL-----MLETTSERLCKGEAHYGSpgkdpAVRLETIEDAG 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
1R30_A        205 DAGIKVCSGGIVGLGETVKDRAGLLLQLANLPTP----PESVPINMLVKvKGTPLADNDDVDAFDFIRTIAVARIMMP 278
Cdd:TIGR03550 160 RLKIPFTTGILIGIGETREERAESLLAIRELHERyghiQEVIVQNFRAK-PGTPMENHPEPSLEEMLRTVAVARLILP 236
COG2516 COG2516
Biotin synthase-related protein, radical SAM superfamily [General function prediction only];
57-318 8.13e-07

Biotin synthase-related protein, radical SAM superfamily [General function prediction only];


Pssm-ID: 442006 [Multi-domain]  Cd Length: 322  Bit Score: 50.36  E-value: 8.13e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R30_A       57 HFDPRQVQVS----TLLSIKTGA---------------CPEDCKYCPQS----------SRYKTGLEAErlmevEQVLES 107
Cdd:COG2516  20 TISGETVRVSvgtaTALGYSKIAflhgptvlaltvlqgCIRNCQFCGIArslaagrdrtIRVKWPTYDL-----EQLAEV 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R30_A      108 ARKAKA-AGSTRFCMGAAWKNPHERDMpylEQMVQGVKA---MGLEACMTLgTLSESQAQRLANAGLDYYNHNLDT-SPE 182
Cdd:COG2516  95 AKAAVElDGVKRMCMTTGTPPGSDRGA---AESARAIKAavdLPISVQCEP-PDDDAWLERLKDAGADRLGIHLDAaTPE 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R30_A      183 FYgNIITTRTYQERLDTLEKVRDAGIKVCSGG------IVGLGETVKDRAGLLLQLANLPTPPESVPinmLVKVKGTPLA 256
Cdd:COG2516 171 VF-ERIRGGKARVSWERYWEAIEEAVEVFGPGqvsthlIVGLGETEEEIVELCQRLIDMGVYPFLFA---FTPIPGTPLE 246
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
1R30_A      257 DNDDVDAfDFIRTIAVARIMMPTSYVRLSagreqmneqtqAMCFMAGANSIFYGCKLLTTPN 318
Cdd:COG2516 247 DHPAPPI-AFYRRIQLARYLIDKGLRSED-----------IFRFDDGGQVVDFGVELLRLIN 296
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
73-210 8.44e-07

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: 48.36  E-value: 8.44e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R30_A       73 TGACPEDCKYCPQSSRYKTGLEaerlMEVEQVLESARKAKAAGSTRFCM--GAAWKNPHerdmpyLEQMVQGVKAMGLEA 150
Cdd:COG0535   7 TNRCNLRCKHCYADAGPKRPGE----LSTEEAKRILDELAELGVKVVGLtgGEPLLRPD------LFELVEYAKELGIRV 76
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
1R30_A      151 CM-TLGT-LSESQAQRLANAGLDYYNHNLD-TSPEFYGNI-ITTRTYQERLDTLEKVRDAGIKV 210
Cdd:COG0535  77 NLsTNGTlLTEELAERLAEAGLDHVTISLDgVDPETHDKIrGVPGAFDKVLEAIKLLKEAGIPV 140
PRK12928 PRK12928
lipoyl synthase; Provisional
161-221 1.52e-06

lipoyl synthase; Provisional


Pssm-ID: 237261  Cd Length: 290  Bit Score: 49.15  E-value: 1.52e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
1R30_A       161 QAQRLA---NAGLDYYNHNLDTSPEFYGNIITTRTYQERLDTLEKVR--DAGIKVCSGGIVGLGET 221
Cdd:PRK12928 152 QRERLAtvlAAKPDVFNHNLETVPRLQKAVRRGADYQRSLDLLARAKelAPDIPTKSGLMLGLGET 217
PflA COG1180
Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, ...
76-210 1.41e-05

Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440793 [Multi-domain]  Cd Length: 242  Bit Score: 45.95  E-value: 1.41e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R30_A       76 CPEDCKYC--PQSSRYKTGLEAERlMEVEQVLESARKAKAAGSTR----FCMG--AAWknpherdMPYLEQMVQGVKAMG 147
Cdd:COG1180  31 CNLRCPYChnPEISQGRPDAAGRE-LSPEELVEEALKDRGFLDSCggvtFSGGepTLQ-------PEFLLDLAKLAKELG 102
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
1R30_A      148 LEACM-TLGTLSESQAQRLAnAGLDYYnhNLD---TSPEFYGNiITTRTYQERLDTLEKVRDAGIKV 210
Cdd:COG1180 103 LHTALdTNGYIPEEALEELL-PYLDAV--NIDlkaFDDEFYRK-LTGVSLEPVLENLELLAESGVHV 165
PRK05481 PRK05481
lipoyl synthase; Provisional
159-221 2.15e-05

lipoyl synthase; Provisional


Pssm-ID: 235493 [Multi-domain]  Cd Length: 289  Bit Score: 45.46  E-value: 2.15e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
1R30_A       159 ESQAQRLANAGLDYYNHNLDTSPEFYGNIittR---TYQERLDTLEKVRDA--GIKVCSGGIVGLGET 221
Cdd:PRK05481 145 MDALLTVLDARPDVFNHNLETVPRLYKRV---RpgaDYERSLELLKRAKELhpGIPTKSGLMVGLGET 209
LipA COG0320
Lipoate synthase [Coenzyme transport and metabolism]; Lipoate synthase is part of the Pathway ...
163-221 4.12e-05

Lipoate synthase [Coenzyme transport and metabolism]; Lipoate synthase is part of the Pathway/BioSystem: Lipoate biosynthesis


Pssm-ID: 440089 [Multi-domain]  Cd Length: 306  Bit Score: 44.71  E-value: 4.12e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
1R30_A      163 QRLANAGLDYYNHNLDTSPEFYGNIittR---TYQERLDTLEKVRDA--GIKVCSGGIVGLGET 221
Cdd:COG0320 164 DIVVDARPDVFNHNLETVPRLYKRV---RpgaDYERSLELLKRAKELdpGIPTKSGLMLGLGET 224
YgiQ COG1032
Radical SAM superfamily enzyme YgiQ, UPF0313 family [General function prediction only];
76-257 5.01e-05

Radical SAM superfamily enzyme YgiQ, UPF0313 family [General function prediction only];


Pssm-ID: 440655 [Multi-domain]  Cd Length: 394  Bit Score: 44.94  E-value: 5.01e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R30_A       76 CPEDCKYCPQSSRYKTGLeaeRLMEVEQVLESARKAKAAGSTR--FCMGAAWKNPHERdmpyLEQMVQGVKAMGLE---- 149
Cdd:COG1032 184 CPFGCSFCSISALYGRKV---RYRSPESVVEEIEELVKRYGIReiFFVDDNFNVDKKR----LKELLEELIERGLNvsfp 256
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R30_A      150 ACMTLGTLSESQAQRLANAGLDY--------YNHNLDtspefygNI---ITTRTYqerLDTLEKVRDAGIKVCSGGIVGL 218
Cdd:COG1032 257 SEVRVDLLDEELLELLKKAGCRGlfigiesgSQRVLK-------AMnkgITVEDI---LEAVRLLKKAGIRVKLYFIIGL 326
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
1R30_A      219 -GETVKDRAGLLLQLANLptPPESVPINMLVKVKGTPLAD 257
Cdd:COG1032 327 pGETEEDIEETIEFIKEL--GPDQAQVSIFTPLPGTPLYE 364
 
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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