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Conserved domains on  [gi|178847575|pdb|3CIW|A]
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Chain A, FeFe-Hydrogenase maturase

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
rSAM_HydE super family cl37353
[FeFe] hydrogenase H-cluster radical SAM maturase HydE; This model describes the radical SAM ...
6-311 1.02e-126

[FeFe] hydrogenase H-cluster radical SAM maturase HydE; This model describes the radical SAM protein HydE, one of a pair of radical SAM proteins, along with GTP-binding protein HydF, for maturation of [Fe] hydrogenase in Chlamydomonas reinhardtii and numerous bacteria. [Protein fate, Protein modification and repair]


The actual alignment was detected with superfamily member TIGR03956:

Pssm-ID: 274880 [Multi-domain]  Cd Length: 340  Bit Score: 366.50  E-value: 1.02e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A          6 ILEKLER-REFTREVLKEALSINDRGFNEALFKLADEIRRKYVGDEVHIRAIIEFSNVCRKNCLYCGLRRDNKNLKRYRM 84
Cdd:TIGR03956   1 LIDKLRKeHTLSKEEFKRLLENRDEEDAEYLFELAREVRLRYYGNKVYIRGLIEFTNYCKNDCYYCGIRKSNPNAERYRL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A         85 TPEEIVERARLAVQFGAKTIVLQSGEDPY*MPDVISDIVKEIKKM--GVAVTLSLGEWPREYYEKWKEAGADRYLLRHET 162
Cdd:TIGR03956  81 TKEEILSCCREGYELGFRTFVLQGGEDPYFTDERIVEIVSAIKEEypDCAITLSLGEKSYESYQRYFDAGADRYLLRHET 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A        163 ANPVLHRKLRP-DTSFENRLN*LLTLKELGYETGAGSMVGLPGQTIDDLVDDLLFLKEHDFDMVGIGPFIPHPDTPLANE 241
Cdd:TIGR03956 161 ANEEHYRKLHPpEMSLENRKQCLWDLKEIGYQTGTGFMVGSPYQTVEHLAEDLLFIKELNPEMVGIGPFIPHHDTPFADE 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A        242 KKGDFTLTLKMVALTRILLPDSNIPATTAMGTIVPGGREITLRCGANVIMPNWTPSPYRQLYQLYPGKIC 311
Cdd:TIGR03956 241 PAGTLELTLFLLSIIRLMLPKVLLPATTALGTIDPDGREKGILAGANVVMPNLSPVEVRKKYLLYDNKIC 310
 
Name Accession Description Interval E-value
rSAM_HydE TIGR03956
[FeFe] hydrogenase H-cluster radical SAM maturase HydE; This model describes the radical SAM ...
6-311 1.02e-126

[FeFe] hydrogenase H-cluster radical SAM maturase HydE; This model describes the radical SAM protein HydE, one of a pair of radical SAM proteins, along with GTP-binding protein HydF, for maturation of [Fe] hydrogenase in Chlamydomonas reinhardtii and numerous bacteria. [Protein fate, Protein modification and repair]


Pssm-ID: 274880 [Multi-domain]  Cd Length: 340  Bit Score: 366.50  E-value: 1.02e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A          6 ILEKLER-REFTREVLKEALSINDRGFNEALFKLADEIRRKYVGDEVHIRAIIEFSNVCRKNCLYCGLRRDNKNLKRYRM 84
Cdd:TIGR03956   1 LIDKLRKeHTLSKEEFKRLLENRDEEDAEYLFELAREVRLRYYGNKVYIRGLIEFTNYCKNDCYYCGIRKSNPNAERYRL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A         85 TPEEIVERARLAVQFGAKTIVLQSGEDPY*MPDVISDIVKEIKKM--GVAVTLSLGEWPREYYEKWKEAGADRYLLRHET 162
Cdd:TIGR03956  81 TKEEILSCCREGYELGFRTFVLQGGEDPYFTDERIVEIVSAIKEEypDCAITLSLGEKSYESYQRYFDAGADRYLLRHET 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A        163 ANPVLHRKLRP-DTSFENRLN*LLTLKELGYETGAGSMVGLPGQTIDDLVDDLLFLKEHDFDMVGIGPFIPHPDTPLANE 241
Cdd:TIGR03956 161 ANEEHYRKLHPpEMSLENRKQCLWDLKEIGYQTGTGFMVGSPYQTVEHLAEDLLFIKELNPEMVGIGPFIPHHDTPFADE 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A        242 KKGDFTLTLKMVALTRILLPDSNIPATTAMGTIVPGGREITLRCGANVIMPNWTPSPYRQLYQLYPGKIC 311
Cdd:TIGR03956 241 PAGTLELTLFLLSIIRLMLPKVLLPATTALGTIDPDGREKGILAGANVVMPNLSPVEVRKKYLLYDNKIC 310
BioB COG0502
Biotin synthase or related enzyme [Coenzyme transport and metabolism]; Biotin synthase or ...
14-334 1.93e-115

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: 336.64  E-value: 1.93e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A       14 EFTREVLKEALSINDRGFNEaLFKLADEIRRKYVGDEVHIRAIIEF-SNVCRKNCLYCGLRRDNK-NLKRYR-MTPEEIV 90
Cdd:COG0502   1 DLTREEALALLELPDEELED-LLAAADEVREHFFGNKVQLCGLINIkSGGCPEDCKYCGQSAHNKtGIERYRlLSVEEIL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A       91 ERARLAVQFGAKTIVL-QSGEDPY*M-PDVISDIVKEIKK-MGVAVTLSLGEWPREYYEKWKEAGADRYLLRHETAnPVL 167
Cdd:COG0502  80 EAARAAKEAGARRFCLvASGRDPSDRdFEKVLEIVRAIKEeLGLEVCASLGELSEEQAKRLKEAGVDRYNHNLETS-PEL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A      168 HRKLRPDTSFENRLN*LLTLKELGYETGAGSMVGLpGQTIDDLVDDLLFLKEHDFDMVGIGPFIPHPDTPLANEKKGDFT 247
Cdd:COG0502 159 YPKICTTHTYEDRLDTLKNAREAGLEVCSGGIVGM-GETLEDRADLLLTLAELDPDSVPINPLIPIPGTPLEDAPPLDPE 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A      248 LTLKMVALTRILLPDSNIPATTAMGTIVPGGREITLRCGANVIMPNwtpspyrQLYQLYPGkicvfekdtACIP*VMKMI 327
Cdd:COG0502 238 EFLRTIAVARLLLPDALIRLSGGRETLLRDGQALALLAGANSIMPG-------NKYLTTPG---------RSVEEDLAMI 301

                ....*..
3CIW_A      328 ELLGRKP 334
Cdd:COG0502 302 EDLGLEV 308
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
53-254 2.24e-26

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: 104.41  E-value: 2.24e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A          53 IRAIIEFSNVCRKNCLYCGLRRDNKNLKRYRmtPEEIVERARLAVQFGAKTIVLQS-----GEDPY*MPDVISDIVKEIK 127
Cdd:smart00729   1 PLALYIITRGCPRRCTFCSFPSLRGKLRSRY--LEALVREIELLAEKGEKEGLVGTvfiggGTPTLLSPEQLEELLEAIR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A         128 K-------MGVAVTLSLGEWPREYYEKWKEAGADRYLLRHETANPVLHRKLRPDTSFENRLN*LLTLKELG-YETGAGSM 199
Cdd:smart00729  79 EilglakdVEITIETRPDTLTEELLEALKEAGVNRVSLGVQSGDDEVLKAINRGHTVEDVLEAVELLREAGpIKVSTDLI 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
3CIW_A         200 VGLPGQTIDDLVDDLLFLKEHDFDMVGIGPFIPHPDTPLANEKKGDFTLTLKMVA 254
Cdd:smart00729 159 VGLPGETEEDFEETLKLLKELGPDRVSIFPLSPRPGTPLAKMYKRLKPPTKEERA 213
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
59-207 5.52e-22

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: 90.66  E-value: 5.52e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A         59 FSNVCRKNCLYCGLRRDNKNLKRYRMTPEEIVERARLAVQFGAKTIVLQSGEdPY*MPDVISDIVKEIKK-----MGVAV 133
Cdd:pfam04055   1 ITRGCNLRCTYCAFPSIRARGKGRELSPEEILEEAKELKRLGVEVVILGGGE-PLLLPDLVELLERLLKLelaegIRITL 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
3CIW_A        134 TLSLGEWPREYYEKWKEAGADRYLLRHETANPVLHRKLRPDTSFENRLN*LLTLKELGYETGAGSMVGLPGQTI 207
Cdd:pfam04055  80 ETNGTLLDEELLELLKEAGLDRVSIGLESGDDEVLKLINRGHTFEEVLEALELLREAGIPVVTDNIVGLPGETD 153
PRK07360 PRK07360
FO synthase subunit 2; Reviewed
6-291 2.50e-21

FO synthase subunit 2; Reviewed


Pssm-ID: 236000 [Multi-domain]  Cd Length: 371  Bit Score: 93.42  E-value: 2.50e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A         6 ILEKLERREFTREVLKEALSINDRGFNEALFKLADEIRRKYVGDEVH--IRAIIEFSNVCRKNCLYCGLRRDNKNLKRYR 83
Cdd:PRK07360  11 LERARKGKDLSKEDALELLETTEPRRIFEILELADRLRKEQVGDTVTyvVNRNINFTNICEGHCGFCAFRRDEGDHGAFW 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A        84 MTPEEIVERARLAVQFGAKTIVLQSGedpy*MPDVIS-----DIVKEIKK------------MGVAVTLSLGEWP-REYY 145
Cdd:PRK07360  91 LTIAEILEKAAEAVKRGATEVCIQGG----LHPAADSlefylEILEAIKEefpdihlhafspMEVYFAAREDGLSyEEVL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A       146 EKWKEAGADRYllrHETANPVLHRKLR-------------------------PDTS---------FENRLN*LLTLKELG 191
Cdd:PRK07360 167 KALKDAGLDSM---PGTAAEILVDEVRriicpekiktaewieivktahklglPTTStmmyghvetPEHRIDHLLILREIQ 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A       192 YETGagsmvglpgqtiddlvddllflkehdfdmvGIGPFIP----HPDTPLANEK--KGDFT--LTLKMVALTRILLPDS 263
Cdd:PRK07360 244 QETG------------------------------GITEFVPlpfvHENAPLYERGrvKGGAPglEDLLLYAVSRIFLGNW 293
                        330       340       350
                 ....*....|....*....|....*....|....*
3CIW_A       264 --NIPAT-----TAMGTivpggreITLRCGANVIM 291
Cdd:PRK07360 294 ikNIQASwvklgLKLAQ-------VALNCGANDLG 321
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
57-243 9.72e-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: 60.42  E-value: 9.72e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A       57 IEFSNVCRKNCLYCGLRRDNKNlKRYRMTPEEIVERARLAVQFGAKTIVLQSGEDPY*MPDV---ISDIVKEIKKMGVAV 133
Cdd:cd01335   1 LELTRGCNLNCGFCSNPASKGR-GPESPPEIEEILDIVLEAKERGVEVVILTGGEPLLYPELaelLRRLKKELPGFEISI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A      134 TLSLGEWPREYYEKWKEAGADRYLLRHETANPVLHRKLRPDT-SFENRLN*LLTLKELGYETGAGSMVGLPGQTIDDLVD 212
Cdd:cd01335  80 ETNGTLLTEELLKELKELGLDGVGVSLDSGDEEVADKIRGSGeSFKERLEALKELREAGLGLSTTLLVGLGDEDEEDDLE 159
                       170       180       190
                ....*....|....*....|....*....|..
3CIW_A      213 DLLFLKEHD-FDMVGIGPFIPHPDTPLANEKK 243
Cdd:cd01335 160 ELELLAEFRsPDRVSLFRLLPEEGTPLELAAP 191
 
Name Accession Description Interval E-value
rSAM_HydE TIGR03956
[FeFe] hydrogenase H-cluster radical SAM maturase HydE; This model describes the radical SAM ...
6-311 1.02e-126

[FeFe] hydrogenase H-cluster radical SAM maturase HydE; This model describes the radical SAM protein HydE, one of a pair of radical SAM proteins, along with GTP-binding protein HydF, for maturation of [Fe] hydrogenase in Chlamydomonas reinhardtii and numerous bacteria. [Protein fate, Protein modification and repair]


Pssm-ID: 274880 [Multi-domain]  Cd Length: 340  Bit Score: 366.50  E-value: 1.02e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A          6 ILEKLER-REFTREVLKEALSINDRGFNEALFKLADEIRRKYVGDEVHIRAIIEFSNVCRKNCLYCGLRRDNKNLKRYRM 84
Cdd:TIGR03956   1 LIDKLRKeHTLSKEEFKRLLENRDEEDAEYLFELAREVRLRYYGNKVYIRGLIEFTNYCKNDCYYCGIRKSNPNAERYRL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A         85 TPEEIVERARLAVQFGAKTIVLQSGEDPY*MPDVISDIVKEIKKM--GVAVTLSLGEWPREYYEKWKEAGADRYLLRHET 162
Cdd:TIGR03956  81 TKEEILSCCREGYELGFRTFVLQGGEDPYFTDERIVEIVSAIKEEypDCAITLSLGEKSYESYQRYFDAGADRYLLRHET 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A        163 ANPVLHRKLRP-DTSFENRLN*LLTLKELGYETGAGSMVGLPGQTIDDLVDDLLFLKEHDFDMVGIGPFIPHPDTPLANE 241
Cdd:TIGR03956 161 ANEEHYRKLHPpEMSLENRKQCLWDLKEIGYQTGTGFMVGSPYQTVEHLAEDLLFIKELNPEMVGIGPFIPHHDTPFADE 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A        242 KKGDFTLTLKMVALTRILLPDSNIPATTAMGTIVPGGREITLRCGANVIMPNWTPSPYRQLYQLYPGKIC 311
Cdd:TIGR03956 241 PAGTLELTLFLLSIIRLMLPKVLLPATTALGTIDPDGREKGILAGANVVMPNLSPVEVRKKYLLYDNKIC 310
BioB COG0502
Biotin synthase or related enzyme [Coenzyme transport and metabolism]; Biotin synthase or ...
14-334 1.93e-115

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: 336.64  E-value: 1.93e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A       14 EFTREVLKEALSINDRGFNEaLFKLADEIRRKYVGDEVHIRAIIEF-SNVCRKNCLYCGLRRDNK-NLKRYR-MTPEEIV 90
Cdd:COG0502   1 DLTREEALALLELPDEELED-LLAAADEVREHFFGNKVQLCGLINIkSGGCPEDCKYCGQSAHNKtGIERYRlLSVEEIL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A       91 ERARLAVQFGAKTIVL-QSGEDPY*M-PDVISDIVKEIKK-MGVAVTLSLGEWPREYYEKWKEAGADRYLLRHETAnPVL 167
Cdd:COG0502  80 EAARAAKEAGARRFCLvASGRDPSDRdFEKVLEIVRAIKEeLGLEVCASLGELSEEQAKRLKEAGVDRYNHNLETS-PEL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A      168 HRKLRPDTSFENRLN*LLTLKELGYETGAGSMVGLpGQTIDDLVDDLLFLKEHDFDMVGIGPFIPHPDTPLANEKKGDFT 247
Cdd:COG0502 159 YPKICTTHTYEDRLDTLKNAREAGLEVCSGGIVGM-GETLEDRADLLLTLAELDPDSVPINPLIPIPGTPLEDAPPLDPE 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A      248 LTLKMVALTRILLPDSNIPATTAMGTIVPGGREITLRCGANVIMPNwtpspyrQLYQLYPGkicvfekdtACIP*VMKMI 327
Cdd:COG0502 238 EFLRTIAVARLLLPDALIRLSGGRETLLRDGQALALLAGANSIMPG-------NKYLTTPG---------RSVEEDLAMI 301

                ....*..
3CIW_A      328 ELLGRKP 334
Cdd:COG0502 302 EDLGLEV 308
ThiH COG1060
2-iminoacetate synthase ThiH/Menaquinone biosynthesis enzymes MqnC and MqnE [Coenzyme ...
5-288 4.99e-36

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: 133.33  E-value: 4.99e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A        5 EILEK-LERREFTREVLKEALSINDRGFnEALFKLADEIRRKYVGDEVH--IRAIIEFSNVCRKNCLYCGLRRDNKNLKR 81
Cdd:COG1060   1 EILEKaLAGERLSLEDALALLSPAAADL-EELAELADELRRRRFGNTVTfvVNRPINLTNVCVNGCKFCAFSRDNGDIDR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A       82 YRMTPEEIVERARLAVQFGAKTIVLQSGEDPY*MPDVISDIVKEIKK----MGVAVtLS----------LGEWPREYYEK 147
Cdd:COG1060  80 YTLSPEEILEEAEEAKALGATEILLVGGEHPDLPLEYYLDLLRAIKErfpnIHIHA-LSpeeiahlaraSGLSVEEVLER 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A      148 WKEAGADRYLLRHETANP--VLHRKLRPDTSFENRLN*LLTLKELGYETGAGSMVGLpGQTiddlvddllflKEHDFDMV 225
Cdd:COG1060 159 LKEAGLDSLPGGGAEILDdeVRHPIGPGKIDYEEWLEVMERAHELGIRTTATMLYGH-VET-----------REERVDHL 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A      226 ----------GIGP-FIP----HPDTPLANEKKG--DFTLtLKMVALTRILLPD-SNIPATTAMGTivPGGREITLRCGA 287
Cdd:COG1060 227 lhlrelqdetGGFTeFIPlrfrPANTPLYLERPGvsDREL-LKLIAVARLFLPNiGNIQASWVSLG--TRLRQLALSLGA 303

                .
3CIW_A      288 N 288
Cdd:COG1060 304 N 304
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
53-254 2.24e-26

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: 104.41  E-value: 2.24e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A          53 IRAIIEFSNVCRKNCLYCGLRRDNKNLKRYRmtPEEIVERARLAVQFGAKTIVLQS-----GEDPY*MPDVISDIVKEIK 127
Cdd:smart00729   1 PLALYIITRGCPRRCTFCSFPSLRGKLRSRY--LEALVREIELLAEKGEKEGLVGTvfiggGTPTLLSPEQLEELLEAIR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A         128 K-------MGVAVTLSLGEWPREYYEKWKEAGADRYLLRHETANPVLHRKLRPDTSFENRLN*LLTLKELG-YETGAGSM 199
Cdd:smart00729  79 EilglakdVEITIETRPDTLTEELLEALKEAGVNRVSLGVQSGDDEVLKAINRGHTVEDVLEAVELLREAGpIKVSTDLI 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
3CIW_A         200 VGLPGQTIDDLVDDLLFLKEHDFDMVGIGPFIPHPDTPLANEKKGDFTLTLKMVA 254
Cdd:smart00729 159 VGLPGETEEDFEETLKLLKELGPDRVSIFPLSPRPGTPLAKMYKRLKPPTKEERA 213
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
59-207 5.52e-22

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: 90.66  E-value: 5.52e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A         59 FSNVCRKNCLYCGLRRDNKNLKRYRMTPEEIVERARLAVQFGAKTIVLQSGEdPY*MPDVISDIVKEIKK-----MGVAV 133
Cdd:pfam04055   1 ITRGCNLRCTYCAFPSIRARGKGRELSPEEILEEAKELKRLGVEVVILGGGE-PLLLPDLVELLERLLKLelaegIRITL 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
3CIW_A        134 TLSLGEWPREYYEKWKEAGADRYLLRHETANPVLHRKLRPDTSFENRLN*LLTLKELGYETGAGSMVGLPGQTI 207
Cdd:pfam04055  80 ETNGTLLDEELLELLKEAGLDRVSIGLESGDDEVLKLINRGHTFEEVLEALELLREAGIPVVTDNIVGLPGETD 153
PRK07360 PRK07360
FO synthase subunit 2; Reviewed
6-291 2.50e-21

FO synthase subunit 2; Reviewed


Pssm-ID: 236000 [Multi-domain]  Cd Length: 371  Bit Score: 93.42  E-value: 2.50e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A         6 ILEKLERREFTREVLKEALSINDRGFNEALFKLADEIRRKYVGDEVH--IRAIIEFSNVCRKNCLYCGLRRDNKNLKRYR 83
Cdd:PRK07360  11 LERARKGKDLSKEDALELLETTEPRRIFEILELADRLRKEQVGDTVTyvVNRNINFTNICEGHCGFCAFRRDEGDHGAFW 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A        84 MTPEEIVERARLAVQFGAKTIVLQSGedpy*MPDVIS-----DIVKEIKK------------MGVAVTLSLGEWP-REYY 145
Cdd:PRK07360  91 LTIAEILEKAAEAVKRGATEVCIQGG----LHPAADSlefylEILEAIKEefpdihlhafspMEVYFAAREDGLSyEEVL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A       146 EKWKEAGADRYllrHETANPVLHRKLR-------------------------PDTS---------FENRLN*LLTLKELG 191
Cdd:PRK07360 167 KALKDAGLDSM---PGTAAEILVDEVRriicpekiktaewieivktahklglPTTStmmyghvetPEHRIDHLLILREIQ 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A       192 YETGagsmvglpgqtiddlvddllflkehdfdmvGIGPFIP----HPDTPLANEK--KGDFT--LTLKMVALTRILLPDS 263
Cdd:PRK07360 244 QETG------------------------------GITEFVPlpfvHENAPLYERGrvKGGAPglEDLLLYAVSRIFLGNW 293
                        330       340       350
                 ....*....|....*....|....*....|....*
3CIW_A       264 --NIPAT-----TAMGTivpggreITLRCGANVIM 291
Cdd:PRK07360 294 ikNIQASwvklgLKLAQ-------VALNCGANDLG 321
F420_cofH TIGR03551
7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase, CofH subunit; This enzyme, together with ...
21-288 1.28e-19

7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase, CofH subunit; This enzyme, together with CofG, complete the biosynthesis of 7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase, the chromophore of coenzyme F420. The chromophore is also used in cyanobacteria DNA photolyases. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 132590 [Multi-domain]  Cd Length: 343  Bit Score: 88.49  E-value: 1.28e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A         21 KEALSI-NDRGFNEALFKLADEIRRKYVGDEVH--IRAIIEFSNVCRKNCLYCGLRRDNKNLKRYRMTPEEIVERARLAV 97
Cdd:TIGR03551   4 EEALELfEARGNLFELFRLADELRRDIVGDTVTyvVNRNINFTNVCYGGCGFCAFRKRKGDADAYLLSLEEIAERAAEAW 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A         98 QFGAKTIVLQSGEDPY*MPDVISDIVKEIKK------------MGV--AVTLSlGEWPREYYEKWKEAGAD--------- 154
Cdd:TIGR03551  84 KAGATEVCIQGGIHPDLDGDFYLDILRAVKEevpgmhihafspMEVyyGARNS-GLSVEEALKRLKEAGLDsmpgtaaei 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A        155 -----RYLL---RHETANPV-----LHRKLRPDTS---------FENRLN*LLTLKELGYETGagsmvglpgqtiddlvd 212
Cdd:TIGR03551 163 lddevRKVIcpdKLSTAEWIeiiktAHKLGIPTTAtimyghvetPEHWVDHLLILREIQEETG----------------- 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A        213 dllflkehdfdmvGIGPFIP----HPDTPLANE---KKGDFTLT-LKMVALTRILLPD--SNIPAT-TAMGTivpGGREI 281
Cdd:TIGR03551 226 -------------GFTEFVPlpfvHYNAPLYLKgmaRPGPTGREdLKVHAIARILLHGliDNIQASwVKLGK---KLAQV 289

                  ....*..
3CIW_A        282 TLRCGAN 288
Cdd:TIGR03551 290 ALRCGAN 296
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
54-195 3.75e-14

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: 69.16  E-value: 3.75e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A       54 RAIIEFSNVCRKNCLYCglRRDNKNLKRYRMTPEEIVERARLAVQFGAKTIVLqSGEDPY*MPDVIsDIVKEIKKMGVAV 133
Cdd:COG0535   1 RLQIELTNRCNLRCKHC--YADAGPKRPGELSTEEAKRILDELAELGVKVVGL-TGGEPLLRPDLF-ELVEYAKELGIRV 76
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
3CIW_A      134 TLS--LGEWPREYYEKWKEAGADRYLLRHETANPVLHRKLR-PDTSFENRLN*LLTLKELGYETG 195
Cdd:COG0535  77 NLStnGTLLTEELAERLAEAGLDHVTISLDGVDPETHDKIRgVPGAFDKVLEAIKLLKEAGIPVG 141
PRK08444 PRK08444
aminofutalosine synthase MqnE;
5-128 7.81e-12

aminofutalosine synthase MqnE;


Pssm-ID: 181426 [Multi-domain]  Cd Length: 353  Bit Score: 65.49  E-value: 7.81e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A         5 EILEKLERREftREVLKEALSINDRGFNEaLFKLADEIRRKYVGDEVH--IRAIIEFSNVCRKNCLYCGLRRDNKNLKRY 82
Cdd:PRK08444   2 DLIEKLENNE--RLNQEEAVKLYDLDLFT-LGKYADKKRTKLHGKKVYfnVNRHINPTNICADVCKFCAFSAHRKNPNPY 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
3CIW_A        83 RMTPEEIVERARLAVQFGAKTIVLQSGEDPY*MPDVISDIVKEIKK 128
Cdd:PRK08444  79 TMSHEEILEIVKNSVKRGIKEVHIVSAHNPNYGYEWYLEIFKKIKE 124
TIGR00423 TIGR00423
radical SAM domain protein, CofH subfamily; This protein family includes the CofH protein of ...
57-288 1.39e-11

radical SAM domain protein, CofH subfamily; This protein family includes the CofH protein of coenzyme F(420) biosynthesis from Methanocaldococcus jannaschii, but appears to hit genomes more broadly than just the subset that make coenzyme F(420), so that narrower group is being built as a separate family. [Hypothetical proteins, Conserved]


Pssm-ID: 273071 [Multi-domain]  Cd Length: 309  Bit Score: 64.34  E-value: 1.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A         57 IEFSNVCRKNCLYCGLRRDNKNLKRYRMTPEEIVERARLAVQFGAKTIVLQSGEDPY*MPDVISDIVKEIKKMGVAVTLS 136
Cdd:TIGR00423   9 INFTNICVGKCKFCAFRAREKDKDAYVLSLEEILEKVKEAVAKGATEVCIQGGLNPQLDIEYYEELFRAIKQEFPDVHIH 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A        137 lGEWPREYY--------------EKWKEAG--------------------------ADRYLLRHETAnpvlHRKLRPDTS 176
Cdd:TIGR00423  89 -AFSPMEVYflakneglsieevlKRLKKAGldsmpgtgaeilddsvrrkicpnklsSDEWLEVIKTA----HRLGIPTTA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A        177 ---------FENRLN*LLTLKELGYETGagsmvglpgqtiddlvddllflkehdfdmvGIGPFIP----HPDTPLAN--- 240
Cdd:TIGR00423 164 tmmfghvenPEHRVEHLLRIRKIQEKTG------------------------------GFTEFIPlpfqPENNPYLEgev 213
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
3CIW_A        241 EKKGDFTLTLKMVALTRILLpdSNIPATTAmgTIVPGGREIT---LRCGAN 288
Cdd:TIGR00423 214 RKGASGIDDLKVIAISRILL--NNIRNIQA--SWVKLGLKLAqvaLEFGAN 260
fbiC PRK09234
FO synthase; Reviewed
33-154 2.64e-11

FO synthase; Reviewed


Pssm-ID: 236422 [Multi-domain]  Cd Length: 843  Bit Score: 64.64  E-value: 2.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A        33 EALFKLADEIRRKYVGDEVH--IRAIIEFSNVCRKNCLYCGLRRDNKNLKRYRMTPEEIVERARLAVQFGAKTIVLQSGE 110
Cdd:PRK09234 504 EAVCRLADDLRRDVVGDDVTyvVNRNINFTNICYTGCRFCAFAQRKTDADAYTLSLDEVADRAWEAWVAGATEVCMQGGI 583
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
3CIW_A       111 DPY*MPDVISDIVKEIKK----M------------GVAVT-LSLGEWPREYyekwKEAGAD 154
Cdd:PRK09234 584 HPELPGTGYADLVRAVKArvpsMhvhafspmeivnGAARLgLSIREWLTAL----REAGLD 640
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
57-243 9.72e-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: 60.42  E-value: 9.72e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A       57 IEFSNVCRKNCLYCGLRRDNKNlKRYRMTPEEIVERARLAVQFGAKTIVLQSGEDPY*MPDV---ISDIVKEIKKMGVAV 133
Cdd:cd01335   1 LELTRGCNLNCGFCSNPASKGR-GPESPPEIEEILDIVLEAKERGVEVVILTGGEPLLYPELaelLRRLKKELPGFEISI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A      134 TLSLGEWPREYYEKWKEAGADRYLLRHETANPVLHRKLRPDT-SFENRLN*LLTLKELGYETGAGSMVGLPGQTIDDLVD 212
Cdd:cd01335  80 ETNGTLLTEELLKELKELGLDGVGVSLDSGDEEVADKIRGSGeSFKERLEALKELREAGLGLSTTLLVGLGDEDEEDDLE 159
                       170       180       190
                ....*....|....*....|....*....|..
3CIW_A      213 DLLFLKEHD-FDMVGIGPFIPHPDTPLANEKK 243
Cdd:cd01335 160 ELELLAEFRsPDRVSLFRLLPEEGTPLELAAP 191
BATS smart00876
Biotin and Thiamin Synthesis associated domain; Biotin synthase (BioB), , catalyses the last ...
226-292 1.19e-10

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: 57.49  E-value: 1.19e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
3CIW_A         226 GIGPFIPHPDTPLAN-EKKGDFTLTLKMVALTRILLPDSNIPATTAMGTIVPGGREITLRCGANVIMP 292
Cdd:smart00876   1 PINRLRPIEGTPLEDpPPPVSPEEFLRTIAAARLALPDAGIRLSTGREALLRDLQALCFSAGANSIFG 68
YgiQ COG1032
Radical SAM superfamily enzyme YgiQ, UPF0313 family [General function prediction only];
4-243 2.90e-10

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


Pssm-ID: 440655 [Multi-domain]  Cd Length: 394  Bit Score: 61.12  E-value: 2.90e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A        4 REILEKLERREFTREVLKEALSINDRGFNEALFKLADEI-------RRKYVGDEVHIRAIIEFSNVCRKNCLYCGLRRDN 76
Cdd:COG1032 118 PELLEALEEGRDLADIPGLAYRDDGRIVQNPPRPLIEDLdelpfpaYDLLDLEAYHRRASIETSRGCPFGCSFCSISALY 197
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A       77 KNLKRYRmTPEEIVERARLAVQ-FGAKTIVLqSGEDPY*MPDVISDIVKEIKKMGVAVTLSLG----EWPREYYEKWKEA 151
Cdd:COG1032 198 GRKVRYR-SPESVVEEIEELVKrYGIREIFF-VDDNFNVDKKRLKELLEELIERGLNVSFPSEvrvdLLDEELLELLKKA 275
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A      152 GADRYLLRHETANPVLHRKLRPDTSFENRLN*LLTLKELGYETGAGSMVGLPGQTIDDLVDDLLFLKEHDFDMVGIGPFI 231
Cdd:COG1032 276 GCRGLFIGIESGSQRVLKAMNKGITVEDILEAVRLLKKAGIRVKLYFIIGLPGETEEDIEETIEFIKELGPDQAQVSIFT 355
                       250
                ....*....|..
3CIW_A      232 PHPDTPLANEKK 243
Cdd:COG1032 356 PLPGTPLYEELE 367
BATS pfam06968
Biotin and Thiamin Synthesis associated domain; Biotin synthase (BioB), EC:2.8.1.6, catalyzes ...
230-291 4.94e-10

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: 55.54  E-value: 4.94e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
3CIW_A        230 FIPHPDTPLANEKKGDFTLTLKMVALTRILLPDSNIpattamgtIVPGGREITLR-------CGANVIM 291
Cdd:pfam06968   1 LRPIPGTPLENQPPLSPEEALRTIAAFRLILPDAGI--------RLAGGRESMLFrqallflAGANSIS 61
F420_cofG TIGR03550
7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase, CofG subunit; This model represents ...
57-261 9.59e-10

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: 58.84  E-value: 9.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A         57 IEFSNVCRKNCLYCGLRRDNKNLKRYRMTPEEIVERARLAVQFGAKTIVLQSGEDPy*mPDVISDIVKEIKKMGVAVTLs 136
Cdd:TIGR03550   8 IPLTRLCRNRCGYCTFRRPPGELEAALLSPEEVLEILRKGAAAGCTEALFTFGEKP---EERYPEAREWLAEMGYDSTL- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A        137 lgewprEY-YEKWKEAGADRYLLRH-------------------------ETANPVL-----HRKlRPDTSFENRLN*LL 185
Cdd:TIGR03550  84 ------EYlRELCELALEETGLLPHtnpgvmsrdelarlkpvnasmglmlETTSERLckgeaHYG-SPGKDPAVRLETIE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A        186 TLKELGYETGAGSMVGLpGQTIDDLVDDLLFLKE-HD----FDMVGIGPFIPHPDTPLANEKKGDFTLTLKMVALTRILL 260
Cdd:TIGR03550 157 DAGRLKIPFTTGILIGI-GETREERAESLLAIRElHEryghIQEVIVQNFRAKPGTPMENHPEPSLEEMLRTVAVARLIL 235

                  .
3CIW_A        261 P 261
Cdd:TIGR03550 236 P 236
COG2516 COG2516
Biotin synthase-related protein, radical SAM superfamily [General function prediction only];
63-184 1.69e-09

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


Pssm-ID: 442006 [Multi-domain]  Cd Length: 322  Bit Score: 58.45  E-value: 1.69e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A       63 CRKNCLYCGLRR----DNKNLKRyRMTP----EEIVERARLAV-QFGAKTIVLQSGEDPY*MPDVIsDIVKEIKKmGVAV 133
Cdd:COG2516  58 CIRNCQFCGIARslaaGRDRTIR-VKWPtydlEQLAEVAKAAVeLDGVKRMCMTTGTPPGSDRGAA-ESARAIKA-AVDL 134
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
3CIW_A      134 TLSLGEWP---REYYEKWKEAGADRYLLRHETANPVLHRKLRP---DTSFENRLN*L 184
Cdd:COG2516 135 PISVQCEPpddDAWLERLKDAGADRLGIHLDAATPEVFERIRGgkaRVSWERYWEAI 191
PLN02389 PLN02389
biotin synthase
12-261 1.25e-08

biotin synthase


Pssm-ID: 215219 [Multi-domain]  Cd Length: 379  Bit Score: 56.01  E-value: 1.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A        12 RREFTREVLKEalsINDRGFNEALFKladeirrkyvGDEVHiRAIIEFSNV------------CRKNCLYCGLR-RDNKN 78
Cdd:PLN02389  44 RNDWTRDEIKE---VYDSPLLDLLFH----------GAQVH-RHAHDPREVqqctllsiktggCSEDCSYCPQSsRYDTG 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A        79 LKRYR-MTPEEIVERARLAVQFGAKTIVL------QSGEDPY*mpDVISDIVKEIKKMGVAVTLSLGEWPREYYEKWKEA 151
Cdd:PLN02389 110 VKAQKlMSKDDVLEAAKRAKEAGSTRFCMgaawrdTVGRKTNF--NQILEYVKEIRGMGMEVCCTLGMLEKEQAAQLKEA 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A       152 GADRYLLRHETAnPVLHRKLRPDTSFENRLN*LLTLKELGYETGAGSMVGL--PGQTIDDLVDDLLFLKEHDfDMVGIGP 229
Cdd:PLN02389 188 GLTAYNHNLDTS-REYYPNVITTRSYDDRLETLEAVREAGISVCSGGIIGLgeAEEDRVGLLHTLATLPEHP-ESVPINA 265
                        250       260       270
                 ....*....|....*....|....*....|..
3CIW_A       230 FIPHPDTPLANEKKGDFTLTLKMVALTRILLP 261
Cdd:PLN02389 266 LVAVKGTPLEDQKPVEIWEMVRMIATARIVMP 297
PRK06267 PRK06267
hypothetical protein; Provisional
39-290 3.53e-08

hypothetical protein; Provisional


Pssm-ID: 235762 [Multi-domain]  Cd Length: 350  Bit Score: 54.37  E-value: 3.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A        39 ADEIRRKYVGDEVHI-RAII-----EFSNVCrKNCLYCGLRRDNKNLKRYRMTPEEIVERARLAVQFGAKtIVLQSGEDP 112
Cdd:PRK06267  13 AFKLTEKHHGNIVSLeRALFlgwycNLKGPC-KFCYMSTQKDKIKDPLKARRRVESILAEAILMKRIGWK-LEFISGGYG 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A       113 Y*MPDV--ISDIVKEIKKMGVAVTLSLGEWPREYYEKWKE-AGAdryllrHETANPVLHRKLRPDTSFENRLN*LLTLKE 189
Cdd:PRK06267  91 YTTEEIndIAEMIAYIQGCKQYLNVGIIDFLNINLNEIEGvVGA------VETVNPKLHREICPGKPLDKIKEMLLKAKD 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A       190 LGYETGAGSMVGLpGQTIDDLVDDLLFLKEHDFDMVGIGPFIPHPDTPLANEKKGDFTLTLKMVALTRILLPDSNIPATT 269
Cdd:PRK06267 165 LGLKTGITIILGL-GETEDDIEKLLNLIEELDLDRITFYSLNPQKGTIFENKPSVTTLEYMNWVSSVRLNFPKIKIITGT 243
                        250       260
                 ....*....|....*....|.
3CIW_A       270 AMGTIVPGGreITLRCGANVI 290
Cdd:PRK06267 244 WVDKLTNIG--PLIMSGSNVI 262
cofG PRK06245
FO synthase subunit 1; Reviewed
50-263 3.62e-07

FO synthase subunit 1; Reviewed


Pssm-ID: 180485 [Multi-domain]  Cd Length: 336  Bit Score: 51.05  E-value: 3.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A        50 EVHIRAIIEFS--------NVCRKNCLYCGLRRDNKNLKRyrMTPEEIVERARLAVQFGAKTIVLQSGEDPy*mPDVISD 121
Cdd:PRK06245   1 DVNMSKIVTYSrnvfipltYECRNRCGYCTFRRDPGQPSL--LSPEEVKEILRRGADAGCTEALFTFGEVP---DESYER 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A       122 IVKEIKKMGV-----------AVTLSLGEWP--------REYYEKWKEAGADRYLLRhETANPVL----HRKlRPDTSFE 178
Cdd:PRK06245  76 IKEQLAEMGYssileylydlcELALEEGLLPhtnagiltREEMEKLKEVNASMGLML-EQTSPRLlntvHRG-SPGKDPE 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A       179 NRLN*LLTLKELGYETGAGSMVGLpGQTIDDLVDDLLFLKE-HD----FDMVGIGPFIPHPDTPLANEKKGDFTLTLKMV 253
Cdd:PRK06245 154 LRLETIENAGKLKIPFTTGILIGI-GETWEDRAESLEAIAElHEryghIQEVIIQNFSPKPGIPMENHPEPSLEEMLRVV 232
                        250
                 ....*....|
3CIW_A       254 ALTRILLPDS 263
Cdd:PRK06245 233 ALARLILPPD 242
PRK05927 PRK05927
dehypoxanthine futalosine cyclase;
15-128 5.37e-05

dehypoxanthine futalosine cyclase;


Pssm-ID: 135660 [Multi-domain]  Cd Length: 350  Bit Score: 44.49  E-value: 5.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A        15 FTREVLKEALSINDRGFNEALFKLADEIRR-KYVGDEVH--IRAIIEFSNVCRKNCLYCGLRRDNKNLKRYRMTPEEIVE 91
Cdd:PRK05927   4 PARISFQEGLELFLYSPLEELQEHADSLRKqRYPQNTVTyvLDANPNYTNICKIDCTFCAFYRKPHSSDAYLLSFDEFRS 83
                         90       100       110
                 ....*....|....*....|....*....|....*..
3CIW_A        92 RARLAVQFGAKTIVLQSGEDPY*MPDVISDIVKEIKK 128
Cdd:PRK05927  84 LMQRYVSAGVKTVLLQGGVHPQLGIDYLEELVRITVK 120
PRK05926 PRK05926
hypothetical protein; Provisional
10-94 8.16e-05

hypothetical protein; Provisional


Pssm-ID: 168296 [Multi-domain]  Cd Length: 370  Bit Score: 44.07  E-value: 8.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A        10 LERREFTREVLKEALSINDRGFNEALFKLADEIRRKYVGDEVHIRAIIEF--SNVCRKNCLYCGLRRDNKNLKRYRMTPE 87
Cdd:PRK05926  23 LSGARLSEEDALQLLLLTDAEDQRALWSFADLIRANRVGDTVYYSSTLYLypTNFCQFNCTFCSFYAKPGDPKGWFYTPD 102

                 ....*..
3CIW_A        88 EIVERAR 94
Cdd:PRK05926 103 QLVQSIK 109
PflA COG1180
Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, ...
52-135 1.72e-03

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


Pssm-ID: 440793 [Multi-domain]  Cd Length: 242  Bit Score: 39.40  E-value: 1.72e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A       52 HIRAIIeFSNVCRKNCLYC---GLRRDNKNLKRYRMTPEEIVERARLAVQF--GAKTIVLqSGEDPY*MPDVISDIVKEI 126
Cdd:COG1180  21 SIRLSV-FTQGCNLRCPYChnpEISQGRPDAAGRELSPEELVEEALKDRGFldSCGGVTF-SGGEPTLQPEFLLDLAKLA 98

                ....*....
3CIW_A      127 KKMGVAVTL 135
Cdd:COG1180  99 KELGLHTAL 107
moaA PRK00164
GTP 3',8-cyclase MoaA;
61-155 4.68e-03

GTP 3',8-cyclase MoaA;


Pssm-ID: 234672 [Multi-domain]  Cd Length: 331  Bit Score: 38.58  E-value: 4.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3CIW_A        61 NVCRKNCLYC-------GLRRDNknlkryRMTPEEIVERARLAVQFGAKTIVLQSGEdPY*MPDVIsDIVKEIKKMGVAV 133
Cdd:PRK00164  25 DRCNFRCTYCmpegylpFLPKEE------LLSLEEIERLVRAFVALGVRKVRLTGGE-PLLRKDLE-DIIAALAALPGIR 96
                         90       100
                 ....*....|....*....|....*
3CIW_A       134 TLSL---GEWPREYYEKWKEAGADR 155
Cdd:PRK00164  97 DLALttnGYLLARRAAALKDAGLDR 121
 
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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