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Conserved domains on  [gi|30681129|ref|NP_850003|]
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GCR2-like 2 [Arabidopsis thaliana]

Protein Classification

lanthionine synthetase C family protein( domain architecture ID 10141013)

lanthionine synthetase C (LanC) family protein similar to Homo sapiens LANCL2 (testes-specific adriamycin sensitivity protein) and LANCL3, which are peptide-modifying enzyme components in eukaryotic cells

CATH:  1.50.10.10
Gene Ontology:  GO:0031179|GO:0005975
PubMed:  23071302
SCOP:  4001568

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
euk_LANCL cd04794
Eukaryotic Lanthionine synthetase C-like protein; This family contains the lanthionine ...
69-401 7.17e-118

Eukaryotic Lanthionine synthetase C-like protein; This family contains the lanthionine synthetase C-like proteins 1 and 2 which are related to the bacterial lanthionine synthetase components C (LanC). LANCL1 and LANCL2 (testes-specific adriamycin sensitivity protein) were thought to be peptide-modifying enzyme components in eukaryotic cells. Both proteins are produced in large quantities in the brain and testes and may have role in the immune surveillance of these organs. More recently, they have been associated with signal transduction processes and insulin sensitization. In particular, LANCL2 has been shown to bind abscisic acid (ABA), and this interaction may play a role in signaling pathways triggered by ABA, such as in human granulocytes and rat insulinoma cells. This eukaryotic LANCL family also includes Arabidopsis GCR2.


:

Pssm-ID: 271202  Cd Length: 349  Bit Score: 346.62  E-value: 7.17e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681129  69 LYSGTLGAAFLLFRAYQVTGNAND-----LSLCLEIVKACDT--ASASSGDVTFLCGRAGVCGLGAVAAKLSG----EED 137
Cdd:cd04794   1 LYTGAAGIAYMFLRLSEQGPDLKAlsedyLELALEYIEASLTelARKGSSRISFLCGDAGILALAAVIYHALGdserDEE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681129 138 LLNYYLGQFRLIRLSSDLPNELLYGRVGYLWACLFINKYIGK-ETLSSDTIREVAQEIIKEGRSMAKKG--SSPLMFEWY 214
Cdd:cd04794  81 FLEQLLELAKEALPLDDGPDELLYGRAGYLYALLFLRKHLGEsLEISDAVIKKLVDAILESGRQGAKDYrsPPPLMYEWH 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681129 215 GKRYWGAAHGLAGIMHVLMDVQL---KPDEAEDVKGTLKYMIKNRFPSGNYPASEEDKKK-DILVHWCHGAPGIALTLGK 290
Cdd:cd04794 161 GKEYLGAAHGLAGILYMLLQAPPllqIPSLAPLIKETLDYLLSLQFPSGNWPSSLGERSRsDRLVQWCHGAPGVVYLLAK 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681129 291 AAEVFGEREFLEASAAAAEVVWNRGLLKR-VGICHGISGNAYVFLALYRATGRSEYLYRAKAFASFLLDRGPKLlskgEM 369
Cdd:cd04794 241 AYKVFLDPKYLEAAIRAGELVWERGLLRKgPGLCHGIAGNAYAFLLLYRLTGDEKYLYRALKFAEFALDYGFLT----GA 316
                       330       340       350
                ....*....|....*....|....*....|...
gi 30681129 370 HGGDSPYSLFEGVAGMAYLFLDMVD-PSEARFP 401
Cdd:cd04794 317 RTPDRPYSLFEGLAGTACFLADLLQgPRKARFP 349
 
Name Accession Description Interval E-value
euk_LANCL cd04794
Eukaryotic Lanthionine synthetase C-like protein; This family contains the lanthionine ...
69-401 7.17e-118

Eukaryotic Lanthionine synthetase C-like protein; This family contains the lanthionine synthetase C-like proteins 1 and 2 which are related to the bacterial lanthionine synthetase components C (LanC). LANCL1 and LANCL2 (testes-specific adriamycin sensitivity protein) were thought to be peptide-modifying enzyme components in eukaryotic cells. Both proteins are produced in large quantities in the brain and testes and may have role in the immune surveillance of these organs. More recently, they have been associated with signal transduction processes and insulin sensitization. In particular, LANCL2 has been shown to bind abscisic acid (ABA), and this interaction may play a role in signaling pathways triggered by ABA, such as in human granulocytes and rat insulinoma cells. This eukaryotic LANCL family also includes Arabidopsis GCR2.


Pssm-ID: 271202  Cd Length: 349  Bit Score: 346.62  E-value: 7.17e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681129  69 LYSGTLGAAFLLFRAYQVTGNAND-----LSLCLEIVKACDT--ASASSGDVTFLCGRAGVCGLGAVAAKLSG----EED 137
Cdd:cd04794   1 LYTGAAGIAYMFLRLSEQGPDLKAlsedyLELALEYIEASLTelARKGSSRISFLCGDAGILALAAVIYHALGdserDEE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681129 138 LLNYYLGQFRLIRLSSDLPNELLYGRVGYLWACLFINKYIGK-ETLSSDTIREVAQEIIKEGRSMAKKG--SSPLMFEWY 214
Cdd:cd04794  81 FLEQLLELAKEALPLDDGPDELLYGRAGYLYALLFLRKHLGEsLEISDAVIKKLVDAILESGRQGAKDYrsPPPLMYEWH 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681129 215 GKRYWGAAHGLAGIMHVLMDVQL---KPDEAEDVKGTLKYMIKNRFPSGNYPASEEDKKK-DILVHWCHGAPGIALTLGK 290
Cdd:cd04794 161 GKEYLGAAHGLAGILYMLLQAPPllqIPSLAPLIKETLDYLLSLQFPSGNWPSSLGERSRsDRLVQWCHGAPGVVYLLAK 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681129 291 AAEVFGEREFLEASAAAAEVVWNRGLLKR-VGICHGISGNAYVFLALYRATGRSEYLYRAKAFASFLLDRGPKLlskgEM 369
Cdd:cd04794 241 AYKVFLDPKYLEAAIRAGELVWERGLLRKgPGLCHGIAGNAYAFLLLYRLTGDEKYLYRALKFAEFALDYGFLT----GA 316
                       330       340       350
                ....*....|....*....|....*....|...
gi 30681129 370 HGGDSPYSLFEGVAGMAYLFLDMVD-PSEARFP 401
Cdd:cd04794 317 RTPDRPYSLFEGLAGTACFLADLLQgPRKARFP 349
LANC_like pfam05147
Lanthionine synthetase C-like protein; Lanthionines are thioether bridges that are putatively ...
63-405 1.33e-117

Lanthionine synthetase C-like protein; Lanthionines are thioether bridges that are putatively generated by dehydration of Ser and Thr residues followed by addition of cysteine residues within the peptide. This family contains the lanthionine synthetase C-like proteins 1 and 2 which are related to the bacterial lanthionine synthetase components C (LanC). LANCL1 (P40 seven-transmembrane-domain protein) and LANCL2 (testes-specific adriamycin sensitivity protein) are thought to be peptide-modifying enzyme components in eukaryotic cells. Both proteins are produced in large quantities in the brain and testes and may have role in the immune surveillance of these organs. Lanthionines are found in lantibiotics, which are peptide-derived, post-translationally modified antimicrobials produced by several bacterial strains. This region contains seven internal repeats.


Pssm-ID: 398697 [Multi-domain]  Cd Length: 350  Bit Score: 346.29  E-value: 1.33e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681129    63 TVEDFTLYSGTLGAAFLLFRAYQVTGNANDLSLCLEIVKACDTASASSG--DVTFLCGRAGVCGLGAVAAKLSGEEDLLN 140
Cdd:pfam05147   1 SPLDDSLYTGLAGIALFLLELYKVTGNEKYLKLAHKYLEKIARALSEKGlpDISFFCGAAGIAYALAVASKLLGDYQLLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681129   141 YYLGQFRLIRLSSDLP---NELLYGRVGYLWACLFINKYIGketLSSDTIREVAQEIIKEG-RSMAKKGSSPLMFEWYGK 216
Cdd:pfam05147  81 NYLDSALELIESNKLPdekYDLISGRAGILSYLLLLNEEFG---IEEDYLKLILKYLLRLGiRSENQFSWCPLMYEPYGN 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681129   217 RYWGAAHGLAGIMHVLMD---VQLKPDEAEDVKGTLKYMIKNRFP-SGNYPASEEDKKkDILVHWCHGAPGIALTLGKAA 292
Cdd:pfam05147 158 FNLGFAHGLSGIAYALLAlykGTKSEKLLELIKKALNYEKSLKFKsEGNWPDSRGDKN-DYLVAWCHGAPGILLALLLAY 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681129   293 EVFGEREFLEASAAAAEVVWNRG-LLKRVGICHGISGNAYVFLALYRATGRSEYLYRAKAFASFLLDRGPKLLSKGEMHG 371
Cdd:pfam05147 237 KALNDEEFLEEAIEALEVVWKRGlLLKNPSLCHGLSGNLYILLLLYRLTNDPKYLERAKKFIISLLDYGKKNGFKCGLPR 316
                         330       340       350
                  ....*....|....*....|....*....|....
gi 30681129   372 GDSPYSLFEGVAGMAYLFLDMVDPSEARFPGYEL 405
Cdd:pfam05147 317 GDESFGLMEGIAGIAYFLLDLLNPDESLFPSALL 350
LcnDR2 COG4403
Lantibiotic modifying enzyme [Defense mechanisms];
61-396 2.67e-33

Lantibiotic modifying enzyme [Defense mechanisms];


Pssm-ID: 443528 [Multi-domain]  Cd Length: 405  Bit Score: 128.70  E-value: 2.67e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681129  61 GQTVEDFTLYSGTLGAAFLLFRAYQVTGNANDLSLCLE----IVKACDTASASSGDVTFLCGRAGVCGLGAVAAKLSGEE 136
Cdd:COG4403  55 AAGPAAADLYDGAAGIALFLAELARLTGDERYRELARAalrpLRRLLREELAGAMGPGLFTGLGGIAYALAHLGELLGDP 134
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681129 137 DLLNYYLGQFRLIR--LSSDLPNELLYGRVGYLWACLFINKYIGKETLSsDTIREVAQEIIKEGRSMAKkGSSPLMFEWY 214
Cdd:COG4403 135 RLLEDALALAALLEelIAADESLDVISGAAGAILALLALYRATGDPAAL-DLAIRCGDRLLAAAVRDDG-GRAWPTPEPA 212
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681129 215 GKRYWGAAHGLAGIMHVLMDV-QLKPDE--AEDVKGTLKYMIKNRFPS-GNYPASEEDKKKDI-LVHWCHGAPGIALTLG 289
Cdd:COG4403 213 GRPLTGFAHGAAGIAYALLRLaAATGDEryLEAAREALAYERSLFDPEgGNWPDLREPDDGPRfRTAWCHGAAGIGLARL 292
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681129 290 KAAEVFGEREFLEASAAAAEVVWNRGLLKRVGICHGISGNAYVFLALYRATGRSEYLYRAKAFASFLLDRGPK---LLSK 366
Cdd:COG4403 293 ALLRALGDPELREDLERALETTLRRGFGRNDSLCHGDAGNLELLLRAARATGDPELLEAARRLAALLLARAERagpLGLP 372
                       330       340       350
                ....*....|....*....|....*....|
gi 30681129 367 GEMHGGDSPySLFEGVAGMAYLFLDMVDPS 396
Cdd:COG4403 373 GLPRGVESP-GLMTGLAGIGYGLLRLAAPE 401
lanti_2_LanM TIGR03897
type 2 lantibiotic biosynthesis protein LanM; Members of this family are known generally as ...
66-395 3.75e-22

type 2 lantibiotic biosynthesis protein LanM; Members of this family are known generally as LanM, a multifunctional enzyme of lantibiotic biosynthesis. This catalysis by LanM distinguishes the type 2 lantibiotics, such as mersacidin, cinnamycin, and lichenicidin, from LanBC-produced type 1 lantibiotics such as nisin and subtilin. The N-terminal domain contains regions associated with Ser and Thr dehydration. The C-terminal region contains a pfam05147 domain, which catalyzes the formation of the lanthionine bridge. [Cellular processes, Toxin production and resistance]


Pssm-ID: 274840 [Multi-domain]  Cd Length: 931  Bit Score: 98.87  E-value: 3.75e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681129    66 DFTLYSGTLGAAFLLFRAYQVTGNANDLSLCLEIVKAC----DTASASSGDVTFlcgrAGVCGLG------AVAAKLSGE 135
Cdd:TIGR03897 591 GNDLYDGLAGIALFLAYLAALTGDKRYRDLARKALQPLrkylETLVELARSMGL----GAFSGLGsiiyalAHLGQLLND 666
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681129   136 EDLLNYYLGQFRLIR---LSSDLPNELLYGRVGYLWACLFINKYIGKETLSsDTIREVAQEIIKegRSMAKKGSSPLMFE 212
Cdd:TIGR03897 667 PELLNDAKKILNRLEeliIKDEEFLDLIGGAAGAILVLLNLYEVTGDPEVL-ELAIACGEHLLK--QAVEQEGGAAWKTS 743
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681129   213 WYGKRYWGAAHGLAGIMHVL---MDVQLKPDEAEDVKGTLKYMiKNRF-PS-GNYPASEEDKKKDILVHWCHGAPGIALT 287
Cdd:TIGR03897 744 QSNKPLTGFSHGAAGIAWALlrlYKVTGDQRYLEAAKEALAYE-RSLFdPEeGNWPDLREDGGPQFPVAWCHGAPGILLS 822
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681129   288 LGKAAEVFGEREFLEASAAAAEVVWNRGLLKRVGICHGISGNAYVFLALYRATGRSEYLYRAKAFASFLLDRgpkLLSKG 367
Cdd:TIGR03897 823 RLGLLEILDDDEIREDIEIALETTLKYGFGDNDSLCHGDLGNLEILLEAAKVLDDEELQELARRIASQVLAR---LTKNG 899
                         330       340       350
                  ....*....|....*....|....*....|..
gi 30681129   368 E----MHGGDSPYSLFEGVAGMAYLFLDMVDP 395
Cdd:TIGR03897 900 RyrlgLPRGVESPGLMTGLAGIGYGLLRLANP 931
 
Name Accession Description Interval E-value
euk_LANCL cd04794
Eukaryotic Lanthionine synthetase C-like protein; This family contains the lanthionine ...
69-401 7.17e-118

Eukaryotic Lanthionine synthetase C-like protein; This family contains the lanthionine synthetase C-like proteins 1 and 2 which are related to the bacterial lanthionine synthetase components C (LanC). LANCL1 and LANCL2 (testes-specific adriamycin sensitivity protein) were thought to be peptide-modifying enzyme components in eukaryotic cells. Both proteins are produced in large quantities in the brain and testes and may have role in the immune surveillance of these organs. More recently, they have been associated with signal transduction processes and insulin sensitization. In particular, LANCL2 has been shown to bind abscisic acid (ABA), and this interaction may play a role in signaling pathways triggered by ABA, such as in human granulocytes and rat insulinoma cells. This eukaryotic LANCL family also includes Arabidopsis GCR2.


Pssm-ID: 271202  Cd Length: 349  Bit Score: 346.62  E-value: 7.17e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681129  69 LYSGTLGAAFLLFRAYQVTGNAND-----LSLCLEIVKACDT--ASASSGDVTFLCGRAGVCGLGAVAAKLSG----EED 137
Cdd:cd04794   1 LYTGAAGIAYMFLRLSEQGPDLKAlsedyLELALEYIEASLTelARKGSSRISFLCGDAGILALAAVIYHALGdserDEE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681129 138 LLNYYLGQFRLIRLSSDLPNELLYGRVGYLWACLFINKYIGK-ETLSSDTIREVAQEIIKEGRSMAKKG--SSPLMFEWY 214
Cdd:cd04794  81 FLEQLLELAKEALPLDDGPDELLYGRAGYLYALLFLRKHLGEsLEISDAVIKKLVDAILESGRQGAKDYrsPPPLMYEWH 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681129 215 GKRYWGAAHGLAGIMHVLMDVQL---KPDEAEDVKGTLKYMIKNRFPSGNYPASEEDKKK-DILVHWCHGAPGIALTLGK 290
Cdd:cd04794 161 GKEYLGAAHGLAGILYMLLQAPPllqIPSLAPLIKETLDYLLSLQFPSGNWPSSLGERSRsDRLVQWCHGAPGVVYLLAK 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681129 291 AAEVFGEREFLEASAAAAEVVWNRGLLKR-VGICHGISGNAYVFLALYRATGRSEYLYRAKAFASFLLDRGPKLlskgEM 369
Cdd:cd04794 241 AYKVFLDPKYLEAAIRAGELVWERGLLRKgPGLCHGIAGNAYAFLLLYRLTGDEKYLYRALKFAEFALDYGFLT----GA 316
                       330       340       350
                ....*....|....*....|....*....|...
gi 30681129 370 HGGDSPYSLFEGVAGMAYLFLDMVD-PSEARFP 401
Cdd:cd04794 317 RTPDRPYSLFEGLAGTACFLADLLQgPRKARFP 349
LANC_like pfam05147
Lanthionine synthetase C-like protein; Lanthionines are thioether bridges that are putatively ...
63-405 1.33e-117

Lanthionine synthetase C-like protein; Lanthionines are thioether bridges that are putatively generated by dehydration of Ser and Thr residues followed by addition of cysteine residues within the peptide. This family contains the lanthionine synthetase C-like proteins 1 and 2 which are related to the bacterial lanthionine synthetase components C (LanC). LANCL1 (P40 seven-transmembrane-domain protein) and LANCL2 (testes-specific adriamycin sensitivity protein) are thought to be peptide-modifying enzyme components in eukaryotic cells. Both proteins are produced in large quantities in the brain and testes and may have role in the immune surveillance of these organs. Lanthionines are found in lantibiotics, which are peptide-derived, post-translationally modified antimicrobials produced by several bacterial strains. This region contains seven internal repeats.


Pssm-ID: 398697 [Multi-domain]  Cd Length: 350  Bit Score: 346.29  E-value: 1.33e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681129    63 TVEDFTLYSGTLGAAFLLFRAYQVTGNANDLSLCLEIVKACDTASASSG--DVTFLCGRAGVCGLGAVAAKLSGEEDLLN 140
Cdd:pfam05147   1 SPLDDSLYTGLAGIALFLLELYKVTGNEKYLKLAHKYLEKIARALSEKGlpDISFFCGAAGIAYALAVASKLLGDYQLLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681129   141 YYLGQFRLIRLSSDLP---NELLYGRVGYLWACLFINKYIGketLSSDTIREVAQEIIKEG-RSMAKKGSSPLMFEWYGK 216
Cdd:pfam05147  81 NYLDSALELIESNKLPdekYDLISGRAGILSYLLLLNEEFG---IEEDYLKLILKYLLRLGiRSENQFSWCPLMYEPYGN 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681129   217 RYWGAAHGLAGIMHVLMD---VQLKPDEAEDVKGTLKYMIKNRFP-SGNYPASEEDKKkDILVHWCHGAPGIALTLGKAA 292
Cdd:pfam05147 158 FNLGFAHGLSGIAYALLAlykGTKSEKLLELIKKALNYEKSLKFKsEGNWPDSRGDKN-DYLVAWCHGAPGILLALLLAY 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681129   293 EVFGEREFLEASAAAAEVVWNRG-LLKRVGICHGISGNAYVFLALYRATGRSEYLYRAKAFASFLLDRGPKLLSKGEMHG 371
Cdd:pfam05147 237 KALNDEEFLEEAIEALEVVWKRGlLLKNPSLCHGLSGNLYILLLLYRLTNDPKYLERAKKFIISLLDYGKKNGFKCGLPR 316
                         330       340       350
                  ....*....|....*....|....*....|....
gi 30681129   372 GDSPYSLFEGVAGMAYLFLDMVDPSEARFPGYEL 405
Cdd:pfam05147 317 GDESFGLMEGIAGIAYFLLDLLNPDESLFPSALL 350
LanC_like cd04434
Cyclases involved in the biosynthesis of lantibiotics, and similar proteins; LanC is the ...
70-401 1.62e-46

Cyclases involved in the biosynthesis of lantibiotics, and similar proteins; LanC is the cyclase enzyme of the lanthionine synthetase. Lanthionine is a lantibiotic, a unique class of peptide antibiotics. They are ribosomally synthesized as a precursor peptide and then post-translationally modified to contain thioether cross-links called lanthionines (Lans) or methyllanthionines (MeLans), in addition to 2,3-didehydroalanine (Dha) and (Z)-2,3-didehydrobutyrine (Dhb). These unusual amino acids are introduced by the dehydration of serine and threonine residues, followed by thioether formation via addition of cysteine thiols, catalysed by LanB and LanC or LanM. LanC, the cyclase component, is a zinc metalloprotein, whose bound metal has been proposed to activate the thiol substrate for nucleophilic addition. A related domain is also present in LanM and other pro- and eukaryotic proteins with poorly characterized functions.


Pssm-ID: 271198 [Multi-domain]  Cd Length: 351  Bit Score: 163.06  E-value: 1.62e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681129  70 YSGTLGAAFLLFRAYQVTGNANDLSLCLEIVKACDTASASSGD----VTFLCGRAGVCGLGAVAAKLSGEEDLLNYYLGQ 145
Cdd:cd04434   1 YHGAAGIALFLLELYRATGDKEYLDEAKEGADYLLARLEGLGEplsgASLYSGLSGLLWALLELYEDLGDEKLLDALLDL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681129 146 FRLIRL----SSDLPNELLYGRVGYLWACLFINKYIGKETlSSDTIREVAQEIIKEGRSMAKKGSSPLmfeWYGKRYWGA 221
Cdd:cd04434  81 LDDIALeakeVWWSGNDLILGDAGIILYLLYAAEKTGDEK-YKELAAKIGDFLLQAAEELDNGGNWGL---PKGSIYPGF 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681129 222 AHGLAGIMHVLM---DVQLKPDEAEDVKGTLKYMIKNRFPSGNYPASEEDKKKDIL-VHWCHGAPGIALTLGKAAEVFGE 297
Cdd:cd04434 157 AHGTAGIAYALArlyEETGDEDFLDAAKEGAEYLEAIAVGDEDGFLIPLPDEKDLFyLGWCHGPAGTALLFYELYKATGD 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681129 298 REF-LEASAAAAEVVWNRGLLK----RVGICHGISGNAYVFLALYRATG----RSEYLYRAKAFASFLLDRGPKLLSKG- 367
Cdd:cd04434 237 LDLaDELLEGIIKTGAPEKLSPgfwnNLCLCHGTAGVLEHLLYVYRLTGdereYAKRLADKLLGRATRNGEGLRWYQAWt 316
                       330       340       350
                ....*....|....*....|....*....|....
gi 30681129 368 EMHGGDSPYSLFEGVAGMAYLFLDMVDPSEARFP 401
Cdd:cd04434 317 GPGRVDASLGLMVGAAGIASALLKLLRAETKARP 350
LcnDR2 COG4403
Lantibiotic modifying enzyme [Defense mechanisms];
61-396 2.67e-33

Lantibiotic modifying enzyme [Defense mechanisms];


Pssm-ID: 443528 [Multi-domain]  Cd Length: 405  Bit Score: 128.70  E-value: 2.67e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681129  61 GQTVEDFTLYSGTLGAAFLLFRAYQVTGNANDLSLCLE----IVKACDTASASSGDVTFLCGRAGVCGLGAVAAKLSGEE 136
Cdd:COG4403  55 AAGPAAADLYDGAAGIALFLAELARLTGDERYRELARAalrpLRRLLREELAGAMGPGLFTGLGGIAYALAHLGELLGDP 134
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681129 137 DLLNYYLGQFRLIR--LSSDLPNELLYGRVGYLWACLFINKYIGKETLSsDTIREVAQEIIKEGRSMAKkGSSPLMFEWY 214
Cdd:COG4403 135 RLLEDALALAALLEelIAADESLDVISGAAGAILALLALYRATGDPAAL-DLAIRCGDRLLAAAVRDDG-GRAWPTPEPA 212
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681129 215 GKRYWGAAHGLAGIMHVLMDV-QLKPDE--AEDVKGTLKYMIKNRFPS-GNYPASEEDKKKDI-LVHWCHGAPGIALTLG 289
Cdd:COG4403 213 GRPLTGFAHGAAGIAYALLRLaAATGDEryLEAAREALAYERSLFDPEgGNWPDLREPDDGPRfRTAWCHGAAGIGLARL 292
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681129 290 KAAEVFGEREFLEASAAAAEVVWNRGLLKRVGICHGISGNAYVFLALYRATGRSEYLYRAKAFASFLLDRGPK---LLSK 366
Cdd:COG4403 293 ALLRALGDPELREDLERALETTLRRGFGRNDSLCHGDAGNLELLLRAARATGDPELLEAARRLAALLLARAERagpLGLP 372
                       330       340       350
                ....*....|....*....|....*....|
gi 30681129 367 GEMHGGDSPySLFEGVAGMAYLFLDMVDPS 396
Cdd:COG4403 373 GLPRGVESP-GLMTGLAGIGYGLLRLAAPE 401
LanM-like cd04792
Cyclases involved in the biosynthesis of class II lantibiotics, and similar proteins; ...
66-397 1.02e-22

Cyclases involved in the biosynthesis of class II lantibiotics, and similar proteins; LanM-like proteins. LanM is a bifunctional enzyme, involved in the synthesis of class II lantibiotics. It is responsible for both the dehydration and the cyclization of the precursor-peptide during lantibiotic synthesis. The C-terminal domain shows similarity to LanC, the cyclase component of the lan operon, but the N terminus seems to be unrelated to the dehydratase, LanB.


Pssm-ID: 271200 [Multi-domain]  Cd Length: 836  Bit Score: 100.47  E-value: 1.02e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681129  66 DFTLYSGTLGAAFLLFRAYQVTGNANDLSLCLEIVKACDTASASSGDVTFLCGRAGVCGLGAVA------AKLSGEEDLL 139
Cdd:cd04792 489 GADLYDGLSGIALFLAALAALTGDEKYRDLARKALRPLRKLLRDLAADPRSLGIGGFTGLGSILyalshlARLLGDPELL 568
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681129 140 NYYLGQFRLI--RLSSDLPNELLYGRVGYLWACLFINKYIGKETLSsDTIREVAQEIIKEGRSMAKKGSSPLmfEWYGKR 217
Cdd:cd04792 569 EDALELADLLteAIIEDEELDIIGGSAGAILVLLALYERTGDERAL-ELAIACGDHLLKNAVENDGGARWKT--PASSRP 645
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681129 218 YWGAAHGLAGIMHVLM---DVQLKPDEAEDVKGTLKYmIKNRF-PS-GNYPASEEDKKKDiLVHWCHGAPGIALTLGKAA 292
Cdd:cd04792 646 LTGFAHGAAGIAWALLrlaAVTGDERYLEAAKEALAY-ERSLFdPEeGNWPDRRKRNNSF-SAAWCHGAAGIGLARLGLL 723
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681129 293 EVFGEREFLEASAAAAEVVWNRGLLKRVGICHGISGNAYVFLALYRATGRSEYLYRAKAFASFLLDRGPKL-LSKGEMHG 371
Cdd:cd04792 724 KILNDDEIEEEIEKALETTLKYGFGNNDSLCHGDLGNLELLLVAAKLLGDPELQEEAEELAAIVLNRAEEAgGWLCGLPT 803
                       330       340
                ....*....|....*....|....*.
gi 30681129 372 GDSPYSLFEGVAGMAYLFLDMVDPSE 397
Cdd:cd04792 804 GVESPGLMTGLSGIGYGLLRLAAPDK 829
lanti_2_LanM TIGR03897
type 2 lantibiotic biosynthesis protein LanM; Members of this family are known generally as ...
66-395 3.75e-22

type 2 lantibiotic biosynthesis protein LanM; Members of this family are known generally as LanM, a multifunctional enzyme of lantibiotic biosynthesis. This catalysis by LanM distinguishes the type 2 lantibiotics, such as mersacidin, cinnamycin, and lichenicidin, from LanBC-produced type 1 lantibiotics such as nisin and subtilin. The N-terminal domain contains regions associated with Ser and Thr dehydration. The C-terminal region contains a pfam05147 domain, which catalyzes the formation of the lanthionine bridge. [Cellular processes, Toxin production and resistance]


Pssm-ID: 274840 [Multi-domain]  Cd Length: 931  Bit Score: 98.87  E-value: 3.75e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681129    66 DFTLYSGTLGAAFLLFRAYQVTGNANDLSLCLEIVKAC----DTASASSGDVTFlcgrAGVCGLG------AVAAKLSGE 135
Cdd:TIGR03897 591 GNDLYDGLAGIALFLAYLAALTGDKRYRDLARKALQPLrkylETLVELARSMGL----GAFSGLGsiiyalAHLGQLLND 666
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681129   136 EDLLNYYLGQFRLIR---LSSDLPNELLYGRVGYLWACLFINKYIGKETLSsDTIREVAQEIIKegRSMAKKGSSPLMFE 212
Cdd:TIGR03897 667 PELLNDAKKILNRLEeliIKDEEFLDLIGGAAGAILVLLNLYEVTGDPEVL-ELAIACGEHLLK--QAVEQEGGAAWKTS 743
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681129   213 WYGKRYWGAAHGLAGIMHVL---MDVQLKPDEAEDVKGTLKYMiKNRF-PS-GNYPASEEDKKKDILVHWCHGAPGIALT 287
Cdd:TIGR03897 744 QSNKPLTGFSHGAAGIAWALlrlYKVTGDQRYLEAAKEALAYE-RSLFdPEeGNWPDLREDGGPQFPVAWCHGAPGILLS 822
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681129   288 LGKAAEVFGEREFLEASAAAAEVVWNRGLLKRVGICHGISGNAYVFLALYRATGRSEYLYRAKAFASFLLDRgpkLLSKG 367
Cdd:TIGR03897 823 RLGLLEILDDDEIREDIEIALETTLKYGFGDNDSLCHGDLGNLEILLEAAKVLDDEELQELARRIASQVLAR---LTKNG 899
                         330       340       350
                  ....*....|....*....|....*....|..
gi 30681129   368 E----MHGGDSPYSLFEGVAGMAYLFLDMVDP 395
Cdd:TIGR03897 900 RyrlgLPRGVESPGLMTGLAGIGYGLLRLANP 931
LanC cd04793
Cyclases involved in the biosynthesis of lantibiotics; LanC is the cyclase enzyme of the ...
68-386 6.64e-17

Cyclases involved in the biosynthesis of lantibiotics; LanC is the cyclase enzyme of the lanthionine synthetase. Lanthinoine is a lantibiotic, a unique class of peptide antibiotics. They are ribosomally synthesized as precursor peptides and then post-translationally modified to contain thioether cross-links called lanthionines (Lans) or methyllanthionines (MeLans) in addition to 2,3-didehydroalanine (Dha) and (Z)-2,3-didehydrobutyrine (Dhb). These unusual amino acids are introduced by the dehydration of serine and threonine residues, followed by thioether formation via addition of cysteine thiols, catalysed by LanB and LanC or LanM. LanC, the cyclase component, is a zinc metalloprotein, whose bound metal has been proposed to activate the thiol substrate for nucleophilic addition. Also contains SpaC (the cyclase involved in the biosynthesis of subtilin), NisC, and homologs.


Pssm-ID: 271201  Cd Length: 377  Bit Score: 81.63  E-value: 6.64e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681129  68 TLYSGTLGAAFLLFRAYQVTGNANDLSLCLE-IVKACDTASASSGDVTfLCGraGVCGLGAVAAKLSGE--------EDL 138
Cdd:cd04793   1 SLSSGLPGIALLLSELARLTPDEGWDEKAHQyLEAAIEELNSAGLSLS-LFS--GLAGLAFALLALSRNggryqnllSEL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681129 139 LNY-------YLGQFRLIRLSSDLPNELLYGRVG---YLWACLFINKYIGKETLssDTIREVAQEIIKEGRSMAKKGSSP 208
Cdd:cd04793  78 NEYidelaedRLAEAIAREGISPGEYDVISGLSGigrYLLERPPPADDLLEEIL--DYLVDLTEPIIEGGEKVPWPELQP 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681129 209 LMFEwygKRYW-------GAAHGLAGIMHVLMDVQLKPDEAEDV----KGTLKYMIKNRFPS-----GNYPASEEDKKKD 272
Cdd:cd04793 156 SESE---KKAYpsghfnlGLAHGIAGPLALLALALRRGIEVPGQreaiERIADWLLKWRQDDdegwwPTIVFPEELSNGR 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681129 273 ILVH-----WCHGAPGIALTLGKAAEVFGEREFLEASAAAAEVVWNR-GLLKRV---GICHGISGNAYVFLALYRATGRS 343
Cdd:cd04793 233 PPPVpsrdaWCYGDPGIARALLLAGKALGDPELQELAEEALLAALRRpDELTGLispTLCHGYAGLLQIARRMYRDTGEP 312
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 30681129 344 EYLYRAKAFASFLLDRGPKLLSKGEMHGGDSP-----YSLFEGVAGMA 386
Cdd:cd04793 313 ALLAAAEELIDKLLDLYDPDLPFGFYDTGGSItplddPGLLEGAAGIA 360
LanC_SerThrkinase cd04791
Lanthionine synthetase C-like domain associated with serine/threonine kinases; Some members of ...
219-392 1.33e-10

Lanthionine synthetase C-like domain associated with serine/threonine kinases; Some members of this subgroup lack the zinc binding site and the active site residues, and therefore are most likely inactive. The function of this domain is unknown.


Pssm-ID: 271199 [Multi-domain]  Cd Length: 327  Bit Score: 61.90  E-value: 1.33e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681129 219 WGAAHGLAGIMHVLMdvQLKPDEAEDVKGTLKYMIKNRFPSGN-------------YPASEEDKKKDIL----------- 274
Cdd:cd04791   3 LNVAYGAAGVLLALH--RAGGAVPEELEDWLVRRALRDLSLPPglydglagiawvlYELGRREEAERLLdralalpldsl 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681129 275 -VHWCHGAPGIALTLGKAAEVFGEREFLEASAAAAE------------VVWNRGLLKRVGICHGISGNAYVFLALYRATG 341
Cdd:cd04791  81 dPSLYSGLAGIGLALLHLARATGDPEFLERAARIAErlaarlreddpgVYWNDAGAVRAGLLHGWSGIALFLLRLYEATG 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 30681129 342 RSEYLYRAKAFASFLLDRGPKLLSKGEMHGGDS----PYsLFEGVAGMAYLFLDM 392
Cdd:cd04791 161 DPAYLDLAERALRKDLARCVEDDDGALLQVDEGnrllPY-LCSGSAGIGLVLLRY 214
LanC_SerThrkinase cd04791
Lanthionine synthetase C-like domain associated with serine/threonine kinases; Some members of ...
115-401 7.38e-07

Lanthionine synthetase C-like domain associated with serine/threonine kinases; Some members of this subgroup lack the zinc binding site and the active site residues, and therefore are most likely inactive. The function of this domain is unknown.


Pssm-ID: 271199 [Multi-domain]  Cd Length: 327  Bit Score: 50.73  E-value: 7.38e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681129 115 FLCGRAGVcglgAVAAKLSGEEDLLNYYLGQFRLIRLSSDLPNeLLYGRVGYLWACLFINKYIGKETLSsDTIREVAQEI 194
Cdd:cd04791  45 LYDGLAGI----AWVLYELGRREEAERLLDRALALPLDSLDPS-LYSGLAGIGLALLHLARATGDPEFL-ERAARIAERL 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681129 195 IKEgrsmAKKGSSPLMFEWYGKRYWGAAHGLAGIMHVLMDV--QLKPDEAEDV-KGTLKYMIKN--RFPSGNYPASEEDK 269
Cdd:cd04791 119 AAR----LREDDPGVYWNDAGAVRAGLLHGWSGIALFLLRLyeATGDPAYLDLaERALRKDLARcvEDDDGALLQVDEGN 194
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681129 270 KkdILVHWCHGAPGIALTLGKAAEVFGEREFLEASaaaaevvwnRGLLKRV--------GICHGISGNAYVFLALYRATG 341
Cdd:cd04791 195 R--LLPYLCSGSAGIGLVLLRYLRHRGDDRYRELL---------EGIARAVrsrftvqpGLFHGLAGLGLALLDLAAALG 263
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30681129 342 RSEYLYRAKAFAS----FLLDRGPKLLSkgemhGGDSPY----SLFEGVAGMAYLFLDMVDPSEARFP 401
Cdd:cd04791 264 DPRYRAAAERHARllnlHALPRDGGIAF-----PGDQLLrlstDLATGSAGVLLALLRLLHGGRSWLP 326
YyaL COG1331
Uncharacterized conserved protein YyaL, SSP411 family, contains thoiredoxin and six-hairpin ...
268-359 2.35e-03

Uncharacterized conserved protein YyaL, SSP411 family, contains thoiredoxin and six-hairpin glycosidase-like domains [General function prediction only];


Pssm-ID: 440942 [Multi-domain]  Cd Length: 672  Bit Score: 40.22  E-value: 2.35e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30681129 268 DKKkdILVHWchgaPGIALT-LGKAAEVFGEREFLEASAAAAEVVWNR-----GLLKRVgICHGISGN-------AYV-- 332
Cdd:COG1331 407 DDK--ILTSW----NGLMIAaLAEAGRVLGDPEYLEAAERAADFILDNlwdpdGRLLRS-YRDGEAGIpgfledyAFLie 479
                        90       100
                ....*....|....*....|....*...
gi 30681129 333 -FLALYRATGRSEYLYRAKAFASFLLDR 359
Cdd:COG1331 480 aLLALYEATGDPRWLERALELADEALEH 507
 
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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