NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2495702629|ref|WP_279946336|]
View 

radical SAM protein, partial [Stenotrophomonas sp. GD03777]

Protein Classification

GTP 3',8-cyclase MoaA family protein( domain architecture ID 1001430)

GTP 3',8-cyclase MoaA catalyzes, together with MoaC, the conversion of 5'-GTP to cyclic pyranopterin monophosphate (cPMP or molybdopterin precursor Z); belongs to the radical SAM superfamily

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
moaA super family cl47076
GTP 3',8-cyclase MoaA;
1-200 6.59e-105

GTP 3',8-cyclase MoaA;


The actual alignment was detected with superfamily member PRK00164:

Pssm-ID: 481416 [Multi-domain]  Cd Length: 331  Bit Score: 304.76  E-value: 6.59e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495702629   1 MSQLTDGFGRSFPYLRLSLTEACNFRCSYCLPDGYQA-DGRPRFLQVDEIARLVRAFAALGMSKIRLTGGEPSLRKDLDE 79
Cdd:PRK00164    5 TSQLIDRFGRKFTYLRISVTDRCNFRCTYCMPEGYLPfLPKEELLSLEEIERLVRAFVALGVRKVRLTGGEPLLRKDLED 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495702629  80 IIATVAAVPGIRKVAITTNGTLLPRRLPGWHRAGLTALNVSMDSLQRERFKTITGHDRLPEIQQGLALAQALGLPAIKLN 159
Cdd:PRK00164   85 IIAALAALPGIRDLALTTNGYLLARRAAALKDAGLDRVNVSLDSLDPERFKAITGRDRLDQVLAGIDAALAAGLTPVKVN 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2495702629 160 AVLLRGLNDDELPQWMDYLRDRPFSVRFIELMRTGDNEAYF 200
Cdd:PRK00164  165 AVLMKGVNDDEIPDLLEWAKDRGIQLRFIELMPTGEGNEWF 205
 
Name Accession Description Interval E-value
moaA PRK00164
GTP 3',8-cyclase MoaA;
1-200 6.59e-105

GTP 3',8-cyclase MoaA;


Pssm-ID: 234672 [Multi-domain]  Cd Length: 331  Bit Score: 304.76  E-value: 6.59e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495702629   1 MSQLTDGFGRSFPYLRLSLTEACNFRCSYCLPDGYQA-DGRPRFLQVDEIARLVRAFAALGMSKIRLTGGEPSLRKDLDE 79
Cdd:PRK00164    5 TSQLIDRFGRKFTYLRISVTDRCNFRCTYCMPEGYLPfLPKEELLSLEEIERLVRAFVALGVRKVRLTGGEPLLRKDLED 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495702629  80 IIATVAAVPGIRKVAITTNGTLLPRRLPGWHRAGLTALNVSMDSLQRERFKTITGHDRLPEIQQGLALAQALGLPAIKLN 159
Cdd:PRK00164   85 IIAALAALPGIRDLALTTNGYLLARRAAALKDAGLDRVNVSLDSLDPERFKAITGRDRLDQVLAGIDAALAAGLTPVKVN 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2495702629 160 AVLLRGLNDDELPQWMDYLRDRPFSVRFIELMRTGDNEAYF 200
Cdd:PRK00164  165 AVLMKGVNDDEIPDLLEWAKDRGIQLRFIELMPTGEGNEWF 205
MoaA COG2896
GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and ...
2-200 8.96e-105

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: 304.29  E-value: 8.96e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495702629   2 SQLTDGFGRSFPYLRLSLTEACNFRCSYCLP-DGYQADGRPRFLQVDEIARLVRAFAALGMSKIRLTGGEPSLRKDLDEI 80
Cdd:COG2896     3 SPLIDRFGRPIDYLRISVTDRCNFRCTYCMPeEGYQFLPKEELLSFEEIERLVRAFVELGVRKIRLTGGEPLLRKDLPEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495702629  81 IATVAAVPGIRKVAITTNGTLLPRRLPGWHRAGLTALNVSMDSLQRERFKTITGHDRLPEIQQGLALAQALGLPAIKLNA 160
Cdd:COG2896    83 IARLAALPGIEDLALTTNGSLLARYAEALKAAGLDRVNVSLDSLDPERFRRITRRDDLDKVLAGIDAALAAGLTPVKINA 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2495702629 161 VLLRGLNDDELPQWMDYLRDRPFSVRFIELMRTGDNEAYF 200
Cdd:COG2896   163 VVMRGVNDDEILDLLEFAKERGIDLRFIELMPLGEGGGWR 202
moaA TIGR02666
molybdenum cofactor biosynthesis protein A, bacterial; The model for this family describes ...
4-197 3.93e-88

molybdenum cofactor biosynthesis protein A, bacterial; The model for this family describes molybdenum cofactor biosynthesis protein A, or MoaA, as found in bacteria. It does not include the family of probable functional equivalent proteins from the archaea. MoaA works together with MoaC to synthesize precursor Z from guanine. [Biosynthesis of cofactors, prosthetic groups, and carriers, Molybdopterin]


Pssm-ID: 274250 [Multi-domain]  Cd Length: 334  Bit Score: 262.16  E-value: 3.93e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495702629   4 LTDGFGRSFPYLRLSLTEACNFRCSYCLPDGYQADGRPR--FLQVDEIARLVRAFAALGMSKIRLTGGEPSLRKDLDEII 81
Cdd:TIGR02666   1 LIDRFGRRIDYLRISVTDRCNLRCVYCMPEGGGLDFLPKeeLLTFEEIERLVRAFVGLGVRKVRLTGGEPLLRKDLVELV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495702629  82 ATVAAVPGIRKVAITTNGTLLPRRLPGWHRAGLTALNVSMDSLQRERFKTIT-GHDRLPEIQQGLALAQALGLPAIKLNA 160
Cdd:TIGR02666  81 ARLAALPGIEDIALTTNGLLLARHAKDLKEAGLKRVNVSLDSLDPERFAKITrRGGRLEQVLAGIDAALAAGLEPVKLNT 160
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2495702629 161 VLLRGLNDDELPQWMDYLRDRPFSVRFIELMRTGDNE 197
Cdd:TIGR02666 161 VVMRGVNDDEIVDLAEFAKERGVTLRFIELMPLGEGN 197
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
19-173 9.68e-31

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: 109.92  E-value: 9.68e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495702629  19 LTEACNFRCSYCLPDGYQADGRPRFLQVDEIARLVRAFAALGMSKIRLTGGEPSLRKDLDEIIATVA--AVPGIRKVAIT 96
Cdd:pfam04055   1 ITRGCNLRCTYCAFPSIRARGKGRELSPEEILEEAKELKRLGVEVVILGGGEPLLLPDLVELLERLLklELAEGIRITLE 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2495702629  97 TNGTLL-PRRLPGWHRAGLTALNVSMDSLQRERFKTITGHDRLPEIQQGLALAQALGLPAIKLNAVLLRGLNDDELPQ 173
Cdd:pfam04055  81 TNGTLLdEELLELLKEAGLDRVSIGLESGDDEVLKLINRGHTFEEVLEALELLREAGIPVVTDNIVGLPGETDEDLEE 158
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
17-197 9.59e-20

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: 82.77  E-value: 9.59e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495702629  17 LSLTEACNFRCSYCLPDGYQADGRPRFLQVDEIARLVRAFAALGMSKIRLTGGEPSLRKDLDEIIATVAAVPGIRKVAIT 96
Cdd:cd01335     1 LELTRGCNLNCGFCSNPASKGRGPESPPEIEEILDIVLEAKERGVEVVILTGGEPLLYPELAELLRRLKKELPGFEISIE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495702629  97 TNGTLL-PRRLPGWHRAGLTALNVSMDSLQRERFKTITGHDRLPEiqQGLALAQALGLPAIKLNAVLLRGLND---DELP 172
Cdd:cd01335    81 TNGTLLtEELLKELKELGLDGVGVSLDSGDEEVADKIRGSGESFK--ERLEALKELREAGLGLSTTLLVGLGDedeEDDL 158
                         170       180
                  ....*....|....*....|....*
gi 2495702629 173 QWMDYLRDRpFSVRFIELMRTGDNE 197
Cdd:cd01335   159 EELELLAEF-RSPDRVSLFRLLPEE 182
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
13-180 6.56e-10

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: 56.26  E-value: 6.56e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495702629   13 PYLRLSLTEACNFRCSYClpDGYQADGRPRFLQVDEIARLVRAFAALGMSKIRLT-----GGEPSL--RKDLDEIIATVA 85
Cdd:smart00729   1 PLALYIITRGCPRRCTFC--SFPSLRGKLRSRYLEALVREIELLAEKGEKEGLVGtvfigGGTPTLlsPEQLEELLEAIR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495702629   86 AVPGIRKVAI----TTNGTLLPRRLPGWHRAGLTALNVSMDSLQRERFKTI-TGHDRLpEIQQGLALAQALGLPAIKLNA 160
Cdd:smart00729  79 EILGLAKDVEitieTRPDTLTEELLEALKEAGVNRVSLGVQSGDDEVLKAInRGHTVE-DVLEAVELLREAGPIKVSTDL 157
                          170       180
                   ....*....|....*....|.
gi 2495702629  161 VL-LRGLNDDELPQWMDYLRD 180
Cdd:smart00729 158 IVgLPGETEEDFEETLKLLKE 178
N_Twi_rSAM NF033640
twitch domain-containing radical SAM protein; Members of this family are unusual among radical ...
14-122 2.63e-06

twitch domain-containing radical SAM protein; Members of this family are unusual among radical SAM proteins in several ways. First, the N-terminal region consists of an iron-sulfur cluster-binding twitch domain (half of a SPASM domain), something usually found C-terminal to the radical SAM domain. Second, the radical SAM domains in many of the members of this family score poorly vs. the Pfam HMM, PF04055 (version 19), used to identify radical SAM. Lastly, the majority of members sequenced to date come from uncultured bacteria from marine or aquifer sources rather than from conventionally cultured bacterial isolates. The function is unknown.


Pssm-ID: 468123 [Multi-domain]  Cd Length: 396  Bit Score: 46.88  E-value: 2.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495702629  14 YLRLSLTEACNFRCSYC--------------LPDGYQADGRP-RFLQVDEIARLVRAFaALGMSKIRLTGGEPSLRKD-- 76
Cdd:NF033640  111 YLDLRFGNLCNLKCRMCgphsssswakeakkLGGPKLGDKKKiSWFEDEEFWKWLEEL-LPSLKEIYFAGGEPLLIKEhy 189
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2495702629  77 --LDEIIATVAAvPGIRkVAITTNGTLLPRRLPG----WHRAGLTALNVSMD 122
Cdd:NF033640  190 klLEKLVEKGRA-KNIE-LRYNTNLTVLPDKLKDlldlWKKFKSVSISASID 239
 
Name Accession Description Interval E-value
moaA PRK00164
GTP 3',8-cyclase MoaA;
1-200 6.59e-105

GTP 3',8-cyclase MoaA;


Pssm-ID: 234672 [Multi-domain]  Cd Length: 331  Bit Score: 304.76  E-value: 6.59e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495702629   1 MSQLTDGFGRSFPYLRLSLTEACNFRCSYCLPDGYQA-DGRPRFLQVDEIARLVRAFAALGMSKIRLTGGEPSLRKDLDE 79
Cdd:PRK00164    5 TSQLIDRFGRKFTYLRISVTDRCNFRCTYCMPEGYLPfLPKEELLSLEEIERLVRAFVALGVRKVRLTGGEPLLRKDLED 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495702629  80 IIATVAAVPGIRKVAITTNGTLLPRRLPGWHRAGLTALNVSMDSLQRERFKTITGHDRLPEIQQGLALAQALGLPAIKLN 159
Cdd:PRK00164   85 IIAALAALPGIRDLALTTNGYLLARRAAALKDAGLDRVNVSLDSLDPERFKAITGRDRLDQVLAGIDAALAAGLTPVKVN 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2495702629 160 AVLLRGLNDDELPQWMDYLRDRPFSVRFIELMRTGDNEAYF 200
Cdd:PRK00164  165 AVLMKGVNDDEIPDLLEWAKDRGIQLRFIELMPTGEGNEWF 205
MoaA COG2896
GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and ...
2-200 8.96e-105

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: 304.29  E-value: 8.96e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495702629   2 SQLTDGFGRSFPYLRLSLTEACNFRCSYCLP-DGYQADGRPRFLQVDEIARLVRAFAALGMSKIRLTGGEPSLRKDLDEI 80
Cdd:COG2896     3 SPLIDRFGRPIDYLRISVTDRCNFRCTYCMPeEGYQFLPKEELLSFEEIERLVRAFVELGVRKIRLTGGEPLLRKDLPEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495702629  81 IATVAAVPGIRKVAITTNGTLLPRRLPGWHRAGLTALNVSMDSLQRERFKTITGHDRLPEIQQGLALAQALGLPAIKLNA 160
Cdd:COG2896    83 IARLAALPGIEDLALTTNGSLLARYAEALKAAGLDRVNVSLDSLDPERFRRITRRDDLDKVLAGIDAALAAGLTPVKINA 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2495702629 161 VLLRGLNDDELPQWMDYLRDRPFSVRFIELMRTGDNEAYF 200
Cdd:COG2896   163 VVMRGVNDDEILDLLEFAKERGIDLRFIELMPLGEGGGWR 202
moaA TIGR02666
molybdenum cofactor biosynthesis protein A, bacterial; The model for this family describes ...
4-197 3.93e-88

molybdenum cofactor biosynthesis protein A, bacterial; The model for this family describes molybdenum cofactor biosynthesis protein A, or MoaA, as found in bacteria. It does not include the family of probable functional equivalent proteins from the archaea. MoaA works together with MoaC to synthesize precursor Z from guanine. [Biosynthesis of cofactors, prosthetic groups, and carriers, Molybdopterin]


Pssm-ID: 274250 [Multi-domain]  Cd Length: 334  Bit Score: 262.16  E-value: 3.93e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495702629   4 LTDGFGRSFPYLRLSLTEACNFRCSYCLPDGYQADGRPR--FLQVDEIARLVRAFAALGMSKIRLTGGEPSLRKDLDEII 81
Cdd:TIGR02666   1 LIDRFGRRIDYLRISVTDRCNLRCVYCMPEGGGLDFLPKeeLLTFEEIERLVRAFVGLGVRKVRLTGGEPLLRKDLVELV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495702629  82 ATVAAVPGIRKVAITTNGTLLPRRLPGWHRAGLTALNVSMDSLQRERFKTIT-GHDRLPEIQQGLALAQALGLPAIKLNA 160
Cdd:TIGR02666  81 ARLAALPGIEDIALTTNGLLLARHAKDLKEAGLKRVNVSLDSLDPERFAKITrRGGRLEQVLAGIDAALAAGLEPVKLNT 160
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2495702629 161 VLLRGLNDDELPQWMDYLRDRPFSVRFIELMRTGDNE 197
Cdd:TIGR02666 161 VVMRGVNDDEIVDLAEFAKERGVTLRFIELMPLGEGN 197
PLN02951 PLN02951
Molybderin biosynthesis protein CNX2
4-196 2.32e-68

Molybderin biosynthesis protein CNX2


Pssm-ID: 215513 [Multi-domain]  Cd Length: 373  Bit Score: 213.08  E-value: 2.32e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495702629   4 LTDGFGRSFPYLRLSLTEACNFRCSYCLP-DGYQADGRPRFLQVDEIARLVRAFAALGMSKIRLTGGEPSLRKDLDEIIA 82
Cdd:PLN02951   49 LVDSFGRRHNYLRISLTERCNLRCQYCMPeEGVELTPKSHLLSQDEIVRLAGLFVAAGVDKIRLTGGEPTLRKDIEDICL 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495702629  83 TVAAVPGIRKVAITTNGTLLPRRLPGWHRAGLTALNVSMDSLQRERFKTIT---GHDRlpeIQQGLALAQALGLPAIKLN 159
Cdd:PLN02951  129 QLSSLKGLKTLAMTTNGITLSRKLPRLKEAGLTSLNISLDTLVPAKFEFLTrrkGHDR---VLESIDTAIELGYNPVKVN 205
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2495702629 160 AVLLRGLNDDELPQWMDYLRDRPFSVRFIELMRTGDN 196
Cdd:PLN02951  206 CVVMRGFNDDEICDFVELTRDKPINVRFIEFMPFDGN 242
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
19-173 9.68e-31

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: 109.92  E-value: 9.68e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495702629  19 LTEACNFRCSYCLPDGYQADGRPRFLQVDEIARLVRAFAALGMSKIRLTGGEPSLRKDLDEIIATVA--AVPGIRKVAIT 96
Cdd:pfam04055   1 ITRGCNLRCTYCAFPSIRARGKGRELSPEEILEEAKELKRLGVEVVILGGGEPLLLPDLVELLERLLklELAEGIRITLE 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2495702629  97 TNGTLL-PRRLPGWHRAGLTALNVSMDSLQRERFKTITGHDRLPEIQQGLALAQALGLPAIKLNAVLLRGLNDDELPQ 173
Cdd:pfam04055  81 TNGTLLdEELLELLKEAGLDRVSIGLESGDDEVLKLINRGHTFEEVLEALELLREAGIPVVTDNIVGLPGETDEDLEE 158
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
14-162 2.01e-28

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: 104.21  E-value: 2.01e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495702629  14 YLRLSLTEACNFRCSYCLPDGYqaDGRPRFLQVDEIARLVRAFAALGMSKIRLTGGEPSLRKDLDEIIATVAAVpGIRkV 93
Cdd:COG0535     1 RLQIELTNRCNLRCKHCYADAG--PKRPGELSTEEAKRILDELAELGVKVVGLTGGEPLLRPDLFELVEYAKEL-GIR-V 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2495702629  94 AITTNGTLLPR-RLPGWHRAGLTALNVSMDSLQRERFKTITG----HDRlpeIQQGLALAQALGLPaIKLNAVL 162
Cdd:COG0535    77 NLSTNGTLLTEeLAERLAEAGLDHVTISLDGVDPETHDKIRGvpgaFDK---VLEAIKLLKEAGIP-VGINTVY 146
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
17-197 9.59e-20

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: 82.77  E-value: 9.59e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495702629  17 LSLTEACNFRCSYCLPDGYQADGRPRFLQVDEIARLVRAFAALGMSKIRLTGGEPSLRKDLDEIIATVAAVPGIRKVAIT 96
Cdd:cd01335     1 LELTRGCNLNCGFCSNPASKGRGPESPPEIEEILDIVLEAKERGVEVVILTGGEPLLYPELAELLRRLKKELPGFEISIE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495702629  97 TNGTLL-PRRLPGWHRAGLTALNVSMDSLQRERFKTITGHDRLPEiqQGLALAQALGLPAIKLNAVLLRGLND---DELP 172
Cdd:cd01335    81 TNGTLLtEELLKELKELGLDGVGVSLDSGDEEVADKIRGSGESFK--ERLEALKELREAGLGLSTTLLVGLGDedeEDDL 158
                         170       180
                  ....*....|....*....|....*
gi 2495702629 173 QWMDYLRDRpFSVRFIELMRTGDNE 197
Cdd:cd01335   159 EELELLAEF-RSPDRVSLFRLLPEE 182
Tyw1 COG0731
Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily [Translation, ribosomal ...
22-192 4.04e-16

Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily [Translation, ribosomal structure and biogenesis]; Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440495 [Multi-domain]  Cd Length: 248  Bit Score: 74.07  E-value: 4.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495702629  22 ACNFRCSYC-LPD-GYQADGRPRFLQVDEIARLVRAFAALGMSKIR------LTG-GEPSLRKDLDEIIATVAAVPGIrK 92
Cdd:COG0731    33 TCNFDCVYCqRGRtTDLTRERREFDDPEEILEELIEFLRKLPEEARepdhitFSGsGEPTLYPNLGELIEEIKKLRGI-K 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495702629  93 VAITTNGTLLPRRlpgWHRAGLTALN---VSMDSLQRERFKTIT---GHDRLPEIQQGLALAQALGLPAIKLNAVLLRGL 166
Cdd:COG0731   112 TALLTNGSLLHRP---EVREELLKADqvyPSLDAADEETFRKINrphPGLSWERIIEGLELFRKLYKGRTVIETMLVKGI 188
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2495702629 167 NDD--ELPQWMDYLRD-RPfsvRFIEL---MR 192
Cdd:COG0731   189 NDSeeELEAYAELIKRiNP---DFVELktyMR 217
AslB COG0641
Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, ...
17-200 5.33e-13

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


Pssm-ID: 440406 [Multi-domain]  Cd Length: 349  Bit Score: 66.16  E-value: 5.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495702629  17 LSLTEACNFRCSYC-LPDGYqaDGRPRFLQVDEIARLVRAFAALGMSKIRLT----GGEPSLRKDL-DEIIATV--AAVP 88
Cdd:COG0641     5 LKPTSRCNLRCSYCyYSEGD--EGSRRRMSEETAEKAIDFLIESSGPGKELTitffGGEPLLNFDFiKEIVEYArkYAKK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495702629  89 GIR-KVAITTNGTLLPRRLpgwhragltalnvsMDSLQRERFK---TITG----HDRL----------PEIQQGLALAQA 150
Cdd:COG0641    83 GKKiRFSIQTNGTLLDDEW--------------IDFLKENGFSvgiSLDGpkeiHDRNrvtkngkgsfDRVMRNIKLLKE 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2495702629 151 LGLPaIKLNAVLLRGlNDDELPQWMDYLRDRPF-SVRFIELMRTGDNEAYF 200
Cdd:COG0641   149 HGVE-VNIRCTVTRE-NLDDPEELYDFLKELGFrSIQFNPVVEEGEADYSL 197
COG2100 COG2100
Uncharacterized Fe-S cluster-containing enzyme, radical SAM superfamily [General function ...
69-180 5.38e-10

Uncharacterized Fe-S cluster-containing enzyme, radical SAM superfamily [General function prediction only];


Pssm-ID: 441703 [Multi-domain]  Cd Length: 344  Bit Score: 57.61  E-value: 5.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495702629  69 GEPSLRKDLDEIIATVAAVPGIRKVAITTNGTLLPRRLPG-WHRAGLTALNVSMDSLQRERFKTITGHDRLPeIQQGLAL 147
Cdd:COG2100    98 GEPLLYPYIVELVKGLKEIKGVKVVSMQTNGTLLSEKLIDeLEEAGLDRINLSIDTLDPEKAKKLAGTKWYD-VEKVLEL 176
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2495702629 148 AQalglpAIKLNA--------VLLRGLNDDELPQWMDYLRD 180
Cdd:COG2100   177 AE-----YIARETkidlliapVWLPGINDEDIPKIIEWALE 212
QueE COG0602
Organic radical activating enzyme NrdG/QueE [Coenzyme transport and metabolism]; Organic ...
23-101 6.12e-10

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: 56.30  E-value: 6.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495702629  23 CNFRCSYClpD-GYQADGRP-RFLQVDEIARLVRAFAAlgmSKIRLTGGEPSLRKDLDEIIATVAAvPGIRkVAITTNGT 100
Cdd:COG0602    30 CNLRCSWC--DtKYAWDGEGgKRMSAEEILEEVAALGA---RHVVITGGEPLLQDDLAELLEALKD-AGYE-VALETNGT 102

                  .
gi 2495702629 101 L 101
Cdd:COG0602   103 L 103
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
13-180 6.56e-10

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: 56.26  E-value: 6.56e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495702629   13 PYLRLSLTEACNFRCSYClpDGYQADGRPRFLQVDEIARLVRAFAALGMSKIRLT-----GGEPSL--RKDLDEIIATVA 85
Cdd:smart00729   1 PLALYIITRGCPRRCTFC--SFPSLRGKLRSRYLEALVREIELLAEKGEKEGLVGtvfigGGTPTLlsPEQLEELLEAIR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495702629   86 AVPGIRKVAI----TTNGTLLPRRLPGWHRAGLTALNVSMDSLQRERFKTI-TGHDRLpEIQQGLALAQALGLPAIKLNA 160
Cdd:smart00729  79 EILGLAKDVEitieTRPDTLTEELLEALKEAGVNRVSLGVQSGDDEVLKAInRGHTVE-DVLEAVELLREAGPIKVSTDL 157
                          170       180
                   ....*....|....*....|.
gi 2495702629  161 VL-LRGLNDDELPQWMDYLRD 180
Cdd:smart00729 158 IVgLPGETEEDFEETLKLLKE 178
SCM_rSAM_ScmF TIGR04251
SynChlorMet cassette radical SAM/SPASM protein ScmF; A biosynthesis cassette found in ...
19-161 1.50e-08

SynChlorMet cassette radical SAM/SPASM protein ScmF; 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 more distant in sequence.


Pssm-ID: 211974 [Multi-domain]  Cd Length: 353  Bit Score: 53.30  E-value: 1.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495702629  19 LTEACNFRCSYCLPD-GYQADG-RPRFLQVDEIARLVRAFAALGMSKIRLTGGEPSLRKDLDEIIATVAAvpGIRKVAIT 96
Cdd:TIGR04251  10 LTEGCNLKCRHCWIDpKYQGEGeQHPSLDPSLFRSIIRQAIPLGLTSVKLTGGEPLLHPAIGEILECIGE--NNLQLSVE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495702629  97 TNGTL----LPRRLPG-------------------WHRAGLTALNVSMDSLQR--------ERFKTITGHDRlPEIQQGL 145
Cdd:TIGR04251  88 TNGLLctpqTARDLAScetpfvsvsldgvdaathdWMRGVKGAFDKAVRGIHNlveagihpQIIMTVTRRNV-GQMEQIV 166
                         170
                  ....*....|....*.
gi 2495702629 146 ALAQALGLPAIKLNAV 161
Cdd:TIGR04251 167 RLAESLGAESVKFNHV 182
PflA COG1180
Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, ...
23-170 2.17e-07

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


Pssm-ID: 440793 [Multi-domain]  Cd Length: 242  Bit Score: 49.41  E-value: 2.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495702629  23 CNFRCSYCL-PDG--YQADGRPRFLQVDEIARLVRAFAALGMSK--IRLTGGEPSLrkDLDEIIATVAAV--PGIrKVAI 95
Cdd:COG1180    31 CNLRCPYCHnPEIsqGRPDAAGRELSPEELVEEALKDRGFLDSCggVTFSGGEPTL--QPEFLLDLAKLAkeLGL-HTAL 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495702629  96 TTNGTLLPRRL----PgwhraGLTALNV---SMDSlqrERFKTITGHDrLPEIQQGLALAQALGLPaIKLNAVLLRGLND 168
Cdd:COG1180   108 DTNGYIPEEALeellP-----YLDAVNIdlkAFDD---EFYRKLTGVS-LEPVLENLELLAESGVH-VEIRTLVIPGLND 177

                  ..
gi 2495702629 169 DE 170
Cdd:COG1180   178 SE 179
SCM_rSAM_ScmE TIGR04250
SynChlorMet cassette radical SAM/SPASM protein ScmE; A biosynthesis cassette found in ...
17-102 5.68e-07

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: 48.70  E-value: 5.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495702629  17 LSLTEACNFRCSYClpDGYQADGR-PRFLQVDEIARLVRAFAALGMSKIRLTGGEPSLRKDLDEIIATVaaVPGIRKVAI 95
Cdd:TIGR04250   7 IDITGRCNLRCRYC--SHFSSAAEtPTDLETAEWLRFFRELNRCSVLRVVLSGGEPFMRSDFREIIDGI--VKNRMRFSI 82

                  ....*..
gi 2495702629  96 TTNGTLL 102
Cdd:TIGR04250  83 LSNGTLI 89
N_Twi_rSAM NF033640
twitch domain-containing radical SAM protein; Members of this family are unusual among radical ...
14-122 2.63e-06

twitch domain-containing radical SAM protein; Members of this family are unusual among radical SAM proteins in several ways. First, the N-terminal region consists of an iron-sulfur cluster-binding twitch domain (half of a SPASM domain), something usually found C-terminal to the radical SAM domain. Second, the radical SAM domains in many of the members of this family score poorly vs. the Pfam HMM, PF04055 (version 19), used to identify radical SAM. Lastly, the majority of members sequenced to date come from uncultured bacteria from marine or aquifer sources rather than from conventionally cultured bacterial isolates. The function is unknown.


Pssm-ID: 468123 [Multi-domain]  Cd Length: 396  Bit Score: 46.88  E-value: 2.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495702629  14 YLRLSLTEACNFRCSYC--------------LPDGYQADGRP-RFLQVDEIARLVRAFaALGMSKIRLTGGEPSLRKD-- 76
Cdd:NF033640  111 YLDLRFGNLCNLKCRMCgphsssswakeakkLGGPKLGDKKKiSWFEDEEFWKWLEEL-LPSLKEIYFAGGEPLLIKEhy 189
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2495702629  77 --LDEIIATVAAvPGIRkVAITTNGTLLPRRLPG----WHRAGLTALNVSMD 122
Cdd:NF033640  190 klLEKLVEKGRA-KNIE-LRYNTNLTVLPDKLKDlldlWKKFKSVSISASID 239
TM0948 COG5014
Uncharacterized conserved protein TM0948, MoaA-related, radical SAM superfamily [General ...
23-137 4.23e-05

Uncharacterized conserved protein TM0948, MoaA-related, radical SAM superfamily [General function prediction only];


Pssm-ID: 444038  Cd Length: 261  Bit Score: 43.05  E-value: 4.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495702629  23 CNFRCSYCLpDGYQADGRPR---FLQVDEIA-RLVRAFAALGMSKIRLTGGEPSL-RKDLDEIIATVAAVpGIRKVaITT 97
Cdd:COG5014    50 CNLRCGFCW-SWRFRDFPLTigkFYSPEEVAeRLIEIARERGYRQVRLSGGEPTIgFEHLLKVLELFSER-GLTFI-LET 126
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2495702629  98 NGTL------LPRRLPGWHRAgltALNVSMDSLQRERFKTITGHDR 137
Cdd:COG5014   127 NGILigydreLARELASFRNI---VVRVSIKGCTPEEFSMLTGADP 169
NrdG2 TIGR02495
anaerobic ribonucleoside-triphosphate reductase activating protein; This enzyme is a member of ...
20-106 1.12e-04

anaerobic ribonucleoside-triphosphate reductase activating protein; This enzyme is a member of the radical-SAM family (pfam04055). It is often gene clustered with the class III (anaerobic) ribonucleotide triphosphate reductase (NrdD, TIGR02487) and presumably fulfills the identical function as NrdG, which utilizes S-adenosyl methionine, an iron-sulfur cluster and a reductant (dihydroflavodoxin) to produce a glycine-centered radical in NrdD. [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism, Protein fate, Protein modification and repair]


Pssm-ID: 274164 [Multi-domain]  Cd Length: 192  Bit Score: 41.20  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495702629  20 TEACNFRCSYCLPDGYQADGRPRFLQVDEIARLVRAFAALgMSKIRLTGGEPSLRKDLDEIIATVAAVpGIrKVAITTNG 99
Cdd:TIGR02495  23 LQGCNLKCPYCHNPLLIPRRGSGEIEVEELLEFLRRRRGL-LDGVVITGGEPTLQAGLPDFLREVREL-GF-EVKLDTNG 99

                  ....*..
gi 2495702629 100 TlLPRRL 106
Cdd:TIGR02495 100 S-NPRRL 105
TIGR00089 TIGR00089
radical SAM methylthiotransferase, MiaB/RimO family; This subfamily contains the tRNA-i(6)A37 ...
10-97 1.97e-04

radical SAM methylthiotransferase, MiaB/RimO family; This subfamily contains the tRNA-i(6)A37 modification enzyme, MiaB (TIGR01574). The phylogenetic tree indicates 4 distinct clades, one of which corresponds to MiaB. The other three clades are modelled by hypothetical equivalogs (TIGR01125, TIGR01579 and TIGR01578). Together, the four models hit every sequence hit by the subfamily model without any overlap between them. This subfamily is aparrently a part of a larger superfamily of enzymes utilizing both a 4Fe4S cluster and S-adenosyl methionine (SAM) to initiate radical reactions. MiaB acts on a particular isoprenylated Adenine base of certain tRNAs causing thiolation at an aromatic carbon, and probably also transferring a methyl grouyp from SAM to the thiol. The particular substrate of the three other clades is unknown but may be very closely related.


Pssm-ID: 272900 [Multi-domain]  Cd Length: 429  Bit Score: 41.46  E-value: 1.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495702629  10 RSFPYLR--LSLTEACNFRCSYC-LPdgyQADGRPRFLQVDEIARLVRAFAALGMSKIRLTG-----------GEPSLRK 75
Cdd:TIGR00089 134 RSFGKTRafLKIQEGCDKFCTYCiIP---YARGRERSRPPEDILEEVKELVSKGVKEIVLLGqnvgaygkdleGKTNLAD 210
                          90       100
                  ....*....|....*....|..
gi 2495702629  76 DLDEIiatvAAVPGIRKVAITT 97
Cdd:TIGR00089 211 LLREL----SKIDGIFRIRFGS 228
viperin TIGR04278
antiviral radical SAM protein viperin; Viperin (Virus Inhibitory Protein, ER-associated, ...
20-132 3.47e-04

antiviral radical SAM protein viperin; Viperin (Virus Inhibitory Protein, ER-associated, Iterferon-inducible) is a radical SAM enzyme found in human and other vertebrates. It is both induced by interferon and demonstrably active in blocking replication by several types of virus, apparently by modifying lipid chemistries in lipid droplets and membrane rafts.


Pssm-ID: 212001  Cd Length: 347  Bit Score: 40.48  E-value: 3.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495702629  20 TEACNFRCSYCLpdgYQAdgRPRF-LQVDEIARLVRAFAALGMSKIRLTGGEPSLRKD---LDEIIATVAAVPGIRKVAI 95
Cdd:TIGR04278  66 TRQCNYKCGFCF---HTA--KTSFvLPLEEAKRGLRLLKEAGMEKINFSGGEPFLHDRgefLGKLVQFCKEELQLPSVSI 140
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2495702629  96 TTNGTLLPRRlpgWHRA-G--LTALNVSMDSLQRERFKTI 132
Cdd:TIGR04278 141 VSNGSLIRER---WFKKyGeyLDILAISCDSFDEQVNVLI 177
MiaB-like-C TIGR01579
MiaB-like tRNA modifying enzyme; This clade of sequences is closely related to MiaB, a ...
8-95 5.69e-04

MiaB-like tRNA modifying enzyme; This clade of sequences is closely related to MiaB, a modifier of isopentenylated adenosine-37 of certain eukaryotic and bacterial tRNAs (see TIGR01574). Sequence alignments suggest that this equivalog performs the same chemical transformation as MiaB, perhaps on a different (or differently modified) tRNA base substrate. This clade is a member of a subfamily (TIGR00089) and spans low GC Gram positive bacteria, alpha and epsilon proteobacteria, Campylobacter, Porphyromonas, Aquifex, Thermotoga, Chlamydia, Treponema and Fusobacterium. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 273704 [Multi-domain]  Cd Length: 414  Bit Score: 40.05  E-value: 5.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495702629   8 FGRSFPYLRLSltEACNFRCSYC-LPdgyQADGRPRFLQVDEIARLVRAFAALGMSKIRLTG--------GEPSLRkDLD 78
Cdd:TIGR01579 135 EGHTRAFIKVQ--DGCNFFCSYCiIP---FARGRSRSVPMEAILKQVKILVAKGYKEIVLTGvnlgsygdDLKNGT-SLA 208
                          90
                  ....*....|....*..
gi 2495702629  79 EIIATVAAVPGIRKVAI 95
Cdd:TIGR01579 209 KLLEQILQIPGIKRIRL 225
ThiH COG1060
2-iminoacetate synthase ThiH/Menaquinone biosynthesis enzymes MqnC and MqnE [Coenzyme ...
19-90 1.81e-03

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: 38.19  E-value: 1.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495702629  19 LTEACNFRCSYClpdGYQADGR---PRFLQVDEIARLVRAFAALGMSKIRLTGGE-PSLrkDLD---EIIATV-AAVPGI 90
Cdd:COG1060    57 LTNVCVNGCKFC---AFSRDNGdidRYTLSPEEILEEAEEAKALGATEILLVGGEhPDL--PLEyylDLLRAIkERFPNI 131
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH