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Conserved domains on  [gi|755492095|ref|XP_011236737|]
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glutathione S-transferase LANCL1 isoform X1 [Mus musculus]

Protein Classification

LanC-like protein( domain architecture ID 10141013)

lanthionine synthetase components C (LanC)-like protein similar to LANCL1 and LANCL2 (testes-specific adriamycin sensitivity protein), which are peptide-modifying enzyme components in eukaryotic cells

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 ...
16-349 1.06e-149

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: 425.59  E-value: 1.06e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492095  16 YTGWAGIAVLYLHLHNVFGDP-----AYLQMAHSYVKQSLNCLSRR---SITFLCGDAGPLAVAAVLYHKMNSEKQAEEC 87
Cdd:cd04794    2 YTGAAGIAYMFLRLSEQGPDLkalseDYLELALEYIEASLTELARKgssRISFLCGDAGILALAAVIYHALGDSERDEEF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492095  88 ITRLIHL---NKIDPHVPNEMLYGRIGYIFALLFVNKNFGE-EKIPQSHIQQICENILTSGENLSRKRNlaAKSPLMYEW 163
Cdd:cd04794   82 LEQLLELakeALPLDDGPDELLYGRAGYLYALLFLRKHLGEsLEISDAVIKKLVDAILESGRQGAKDYR--SPPPLMYEW 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492095 164 YQEYYVGAAHGLAGIYYYLMQPSLQVNQGKLHSLVKPSVDFVCRLKFPSGNYPPCLDD--TRDLLVHWCHGAPGVIYMLI 241
Cdd:cd04794  160 HGKEYLGAAHGLAGILYMLLQAPPLLQIPSLAPLIKETLDYLLSLQFPSGNWPSSLGErsRSDRLVQWCHGAPGVVYLLA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492095 242 QAYKVFKEERYLCDAQQCADVIWQYGLLKKGYGLCHGAAGNAYAFLALYNLTQDLKYLYRACKFAEWCLDYGEH-GCRTA 320
Cdd:cd04794  240 KAYKVFLDPKYLEAAIRAGELVWERGLLRKGPGLCHGIAGNAYAFLLLYRLTGDEKYLYRALKFAEFALDYGFLtGARTP 319
                        330       340       350
                 ....*....|....*....|....*....|
gi 755492095 321 DTPFSLFEGMAGTIYFLADLLV-PTKAKFP 349
Cdd:cd04794  320 DRPYSLFEGLAGTACFLADLLQgPRKARFP 349
 
Name Accession Description Interval E-value
euk_LANCL cd04794
Eukaryotic Lanthionine synthetase C-like protein; This family contains the lanthionine ...
16-349 1.06e-149

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: 425.59  E-value: 1.06e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492095  16 YTGWAGIAVLYLHLHNVFGDP-----AYLQMAHSYVKQSLNCLSRR---SITFLCGDAGPLAVAAVLYHKMNSEKQAEEC 87
Cdd:cd04794    2 YTGAAGIAYMFLRLSEQGPDLkalseDYLELALEYIEASLTELARKgssRISFLCGDAGILALAAVIYHALGDSERDEEF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492095  88 ITRLIHL---NKIDPHVPNEMLYGRIGYIFALLFVNKNFGE-EKIPQSHIQQICENILTSGENLSRKRNlaAKSPLMYEW 163
Cdd:cd04794   82 LEQLLELakeALPLDDGPDELLYGRAGYLYALLFLRKHLGEsLEISDAVIKKLVDAILESGRQGAKDYR--SPPPLMYEW 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492095 164 YQEYYVGAAHGLAGIYYYLMQPSLQVNQGKLHSLVKPSVDFVCRLKFPSGNYPPCLDD--TRDLLVHWCHGAPGVIYMLI 241
Cdd:cd04794  160 HGKEYLGAAHGLAGILYMLLQAPPLLQIPSLAPLIKETLDYLLSLQFPSGNWPSSLGErsRSDRLVQWCHGAPGVVYLLA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492095 242 QAYKVFKEERYLCDAQQCADVIWQYGLLKKGYGLCHGAAGNAYAFLALYNLTQDLKYLYRACKFAEWCLDYGEH-GCRTA 320
Cdd:cd04794  240 KAYKVFLDPKYLEAAIRAGELVWERGLLRKGPGLCHGIAGNAYAFLLLYRLTGDEKYLYRALKFAEFALDYGFLtGARTP 319
                        330       340       350
                 ....*....|....*....|....*....|
gi 755492095 321 DTPFSLFEGMAGTIYFLADLLV-PTKAKFP 349
Cdd:cd04794  320 DRPYSLFEGLAGTACFLADLLQgPRKARFP 349
LANC_like pfam05147
Lanthionine synthetase C-like protein; Lanthionines are thioether bridges that are putatively ...
9-353 9.24e-122

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: 354.77  E-value: 9.24e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492095    9 DPRDGTGYTGWAGIAVLYLHLHNVFGDPAYLQMAHSYVKQSLNCLSR---RSITFLCGDAGPLAVAAVLYHKMNSEKQAE 85
Cdd:pfam05147   1 SPLDDSLYTGLAGIALFLLELYKVTGNEKYLKLAHKYLEKIARALSEkglPDISFFCGAAGIAYALAVASKLLGDYQLLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492095   86 ECITRLIHL--NKIDPHVPNEMLYGRIGYIFALLFVNKNFGeekIPQSHIQQICENILTSGenlSRKRNLAAKSPLMYEW 163
Cdd:pfam05147  81 NYLDSALELieSNKLPDEKYDLISGRAGILSYLLLLNEEFG---IEEDYLKLILKYLLRLG---IRSENQFSWCPLMYEP 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492095  164 YQEYYVGAAHGLAGIYYYLMQPSLQVNQGKLHSLVKPSVDFVCRLKFP-SGNYPPCLDDTRDLLVHWCHGAPGVIYMLIQ 242
Cdd:pfam05147 155 YGNFNLGFAHGLSGIAYALLALYKGTKSEKLLELIKKALNYEKSLKFKsEGNWPDSRGDKNDYLVAWCHGAPGILLALLL 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492095  243 AYKVFKEERYLCDAQQCADVIWQYGLLKKGYGLCHGAAGNAYAFLALYNLTQDLKYLYRACKFAEWCLDYGEHGCR---- 318
Cdd:pfam05147 235 AYKALNDEEFLEEAIEALEVVWKRGLLLKNPSLCHGLSGNLYILLLLYRLTNDPKYLERAKKFIISLLDYGKKNGFkcgl 314
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 755492095  319 -TADTPFSLFEGMAGTIYFLADLLVPTKAKFPAFEL 353
Cdd:pfam05147 315 pRGDESFGLMEGIAGIAYFLLDLLNPDESLFPSALL 350
LcnDR2 COG4403
Lantibiotic modifying enzyme [Defense mechanisms];
16-344 8.46e-30

Lantibiotic modifying enzyme [Defense mechanisms];


Pssm-ID: 443528 [Multi-domain]  Cd Length: 405  Bit Score: 117.92  E-value: 8.46e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492095  16 YTGWAGIAVLYLHLHNVFGDPAYLQMAHSYVKQSLNCLSR-----RSITFLCGDAGpLAVAAVLYHKMNSEKQAEECITR 90
Cdd:COG4403   64 YDGAAGIALFLAELARLTGDERYRELARAALRPLRRLLREelagaMGPGLFTGLGG-IAYALAHLGELLGDPRLLEDALA 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492095  91 LIHL--NKIDPHVPNEMLYGRIGYIFALLFVNKNFGEE---KIPQSHIQQICENILTSGENLSRKRNLAAKSPLmyewyq 165
Cdd:COG4403  143 LAALleELIAADESLDVISGAAGAILALLALYRATGDPaalDLAIRCGDRLLAAAVRDDGGRAWPTPEPAGRPL------ 216
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492095 166 eyyVGAAHGLAGIYYYLMQPSLQVNQGKLHSLVKPSVDFVCRLKFPS-GNYPP--CLDDTRDLLVHWCHGAPGVIYMLIQ 242
Cdd:COG4403  217 ---TGFAHGAAGIAYALLRLAAATGDERYLEAAREALAYERSLFDPEgGNWPDlrEPDDGPRFRTAWCHGAAGIGLARLA 293
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492095 243 AYKVFKEERYLCDAQQCADVIWQYGLLkKGYGLCHGAAGNAYAFLALYNLTQDLKYLYRACKFAEWCLD-YGEHGC---- 317
Cdd:COG4403  294 LLRALGDPELREDLERALETTLRRGFG-RNDSLCHGDAGNLELLLRAARATGDPELLEAARRLAALLLArAERAGPlglp 372
                        330       340       350
                 ....*....|....*....|....*....|
gi 755492095 318 ---RTADTPfSLFEGMAGTIYFLADLLVPT 344
Cdd:COG4403  373 glpRGVESP-GLMTGLAGIGYGLLRLAAPE 401
lanti_2_LanM TIGR03897
type 2 lantibiotic biosynthesis protein LanM; Members of this family are known generally as ...
16-337 1.75e-21

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: 95.79  E-value: 1.75e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492095   16 YTGWAGIAVLYLHLHNVFGDPAYLQMAHSYVKQSLNCLSRRSIT-------FLCGDAGPLAVAAVLYhKMNSEKQAEECI 88
Cdd:TIGR03897 595 YDGLAGIALFLAYLAALTGDKRYRDLARKALQPLRKYLETLVELarsmglgAFSGLGSIIYALAHLG-QLLNDPELLNDA 673
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492095   89 TRLIhlNKIDPHVPNE-----MLYGRIGYIFALLFVNKNFGEEKIPQSHIQqiCENILtsgenLSRKRNLAAKSPLMYEW 163
Cdd:TIGR03897 674 KKIL--NRLEELIIKDeefldLIGGAAGAILVLLNLYEVTGDPEVLELAIA--CGEHL-----LKQAVEQEGGAAWKTSQ 744
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492095  164 YQEYYVGAAHGLAGIYYYLMQPSLQVNQGKLHSLVKPSVDFVCRLKFPS-GNYP-PCLDDTRDLLVHWCHGAPGVIYMLI 241
Cdd:TIGR03897 745 SNKPLTGFSHGAAGIAWALLRLYKVTGDQRYLEAAKEALAYERSLFDPEeGNWPdLREDGGPQFPVAWCHGAPGILLSRL 824
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492095  242 QAYKVFKEERYLCDAQQCADVIWQYGlLKKGYGLCHGAAGNAYAFLALYNLTQDLKYLYRACKFAEWCLD-YGEHG---C 317
Cdd:TIGR03897 825 GLLEILDDDEIREDIEIALETTLKYG-FGDNDSLCHGDLGNLEILLEAAKVLDDEELQELARRIASQVLArLTKNGryrL 903
                         330       340
                  ....*....|....*....|..
gi 755492095  318 RTADT--PFSLFEGMAGTIYFL 337
Cdd:TIGR03897 904 GLPRGveSPGLMTGLAGIGYGL 925
 
Name Accession Description Interval E-value
euk_LANCL cd04794
Eukaryotic Lanthionine synthetase C-like protein; This family contains the lanthionine ...
16-349 1.06e-149

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: 425.59  E-value: 1.06e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492095  16 YTGWAGIAVLYLHLHNVFGDP-----AYLQMAHSYVKQSLNCLSRR---SITFLCGDAGPLAVAAVLYHKMNSEKQAEEC 87
Cdd:cd04794    2 YTGAAGIAYMFLRLSEQGPDLkalseDYLELALEYIEASLTELARKgssRISFLCGDAGILALAAVIYHALGDSERDEEF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492095  88 ITRLIHL---NKIDPHVPNEMLYGRIGYIFALLFVNKNFGE-EKIPQSHIQQICENILTSGENLSRKRNlaAKSPLMYEW 163
Cdd:cd04794   82 LEQLLELakeALPLDDGPDELLYGRAGYLYALLFLRKHLGEsLEISDAVIKKLVDAILESGRQGAKDYR--SPPPLMYEW 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492095 164 YQEYYVGAAHGLAGIYYYLMQPSLQVNQGKLHSLVKPSVDFVCRLKFPSGNYPPCLDD--TRDLLVHWCHGAPGVIYMLI 241
Cdd:cd04794  160 HGKEYLGAAHGLAGILYMLLQAPPLLQIPSLAPLIKETLDYLLSLQFPSGNWPSSLGErsRSDRLVQWCHGAPGVVYLLA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492095 242 QAYKVFKEERYLCDAQQCADVIWQYGLLKKGYGLCHGAAGNAYAFLALYNLTQDLKYLYRACKFAEWCLDYGEH-GCRTA 320
Cdd:cd04794  240 KAYKVFLDPKYLEAAIRAGELVWERGLLRKGPGLCHGIAGNAYAFLLLYRLTGDEKYLYRALKFAEFALDYGFLtGARTP 319
                        330       340       350
                 ....*....|....*....|....*....|
gi 755492095 321 DTPFSLFEGMAGTIYFLADLLV-PTKAKFP 349
Cdd:cd04794  320 DRPYSLFEGLAGTACFLADLLQgPRKARFP 349
LANC_like pfam05147
Lanthionine synthetase C-like protein; Lanthionines are thioether bridges that are putatively ...
9-353 9.24e-122

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: 354.77  E-value: 9.24e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492095    9 DPRDGTGYTGWAGIAVLYLHLHNVFGDPAYLQMAHSYVKQSLNCLSR---RSITFLCGDAGPLAVAAVLYHKMNSEKQAE 85
Cdd:pfam05147   1 SPLDDSLYTGLAGIALFLLELYKVTGNEKYLKLAHKYLEKIARALSEkglPDISFFCGAAGIAYALAVASKLLGDYQLLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492095   86 ECITRLIHL--NKIDPHVPNEMLYGRIGYIFALLFVNKNFGeekIPQSHIQQICENILTSGenlSRKRNLAAKSPLMYEW 163
Cdd:pfam05147  81 NYLDSALELieSNKLPDEKYDLISGRAGILSYLLLLNEEFG---IEEDYLKLILKYLLRLG---IRSENQFSWCPLMYEP 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492095  164 YQEYYVGAAHGLAGIYYYLMQPSLQVNQGKLHSLVKPSVDFVCRLKFP-SGNYPPCLDDTRDLLVHWCHGAPGVIYMLIQ 242
Cdd:pfam05147 155 YGNFNLGFAHGLSGIAYALLALYKGTKSEKLLELIKKALNYEKSLKFKsEGNWPDSRGDKNDYLVAWCHGAPGILLALLL 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492095  243 AYKVFKEERYLCDAQQCADVIWQYGLLKKGYGLCHGAAGNAYAFLALYNLTQDLKYLYRACKFAEWCLDYGEHGCR---- 318
Cdd:pfam05147 235 AYKALNDEEFLEEAIEALEVVWKRGLLLKNPSLCHGLSGNLYILLLLYRLTNDPKYLERAKKFIISLLDYGKKNGFkcgl 314
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 755492095  319 -TADTPFSLFEGMAGTIYFLADLLVPTKAKFPAFEL 353
Cdd:pfam05147 315 pRGDESFGLMEGIAGIAYFLLDLLNPDESLFPSALL 350
LanC_like cd04434
Cyclases involved in the biosynthesis of lantibiotics, and similar proteins; LanC is the ...
16-350 4.41e-64

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: 207.36  E-value: 4.41e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492095  16 YTGWAGIAVLYLHLHNVFGDPAYLQMAHSYVKQSLNCLSRRS-----ITFLCGDAGPLAVAAVLYHKMNSEKQAEECITR 90
Cdd:cd04434    1 YHGAAGIALFLLELYRATGDKEYLDEAKEGADYLLARLEGLGeplsgASLYSGLSGLLWALLELYEDLGDEKLLDALLDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492095  91 LIHLNKIDPHV---PNEMLYGRIGYIFALLFVNKNFGEEKIpQSHIQQICENILTSGENLSRKRNLaaksplmYEWYQEY 167
Cdd:cd04434   81 LDDIALEAKEVwwsGNDLILGDAGIILYLLYAAEKTGDEKY-KELAAKIGDFLLQAAEELDNGGNW-------GLPKGSI 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492095 168 YVGAAHGLAGIYYYLMQPSLQVNQGKLHSLVKPSVDFVCRLKFPSGNYPPCL--DDTRDLLVHWCHGAPGVIYMLIQAYK 245
Cdd:cd04434  153 YPGFAHGTAGIAYALARLYEETGDEDFLDAAKEGAEYLEAIAVGDEDGFLIPlpDEKDLFYLGWCHGPAGTALLFYELYK 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492095 246 VFKE-ERYLCDAQQCADVIWQYGLLK---KGYGLCHGAAGNAYAFLALYNLTQD----LKYLYRACKFAEWCLDYGEHGC 317
Cdd:cd04434  233 ATGDlDLADELLEGIIKTGAPEKLSPgfwNNLCLCHGTAGVLEHLLYVYRLTGDereyAKRLADKLLGRATRNGEGLRWY 312
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 755492095 318 R------TADTPFSLFEGMAGTIYFLADLLVPTKAKFPA 350
Cdd:cd04434  313 QawtgpgRVDASLGLMVGAAGIASALLKLLRAETKARPL 351
LcnDR2 COG4403
Lantibiotic modifying enzyme [Defense mechanisms];
16-344 8.46e-30

Lantibiotic modifying enzyme [Defense mechanisms];


Pssm-ID: 443528 [Multi-domain]  Cd Length: 405  Bit Score: 117.92  E-value: 8.46e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492095  16 YTGWAGIAVLYLHLHNVFGDPAYLQMAHSYVKQSLNCLSR-----RSITFLCGDAGpLAVAAVLYHKMNSEKQAEECITR 90
Cdd:COG4403   64 YDGAAGIALFLAELARLTGDERYRELARAALRPLRRLLREelagaMGPGLFTGLGG-IAYALAHLGELLGDPRLLEDALA 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492095  91 LIHL--NKIDPHVPNEMLYGRIGYIFALLFVNKNFGEE---KIPQSHIQQICENILTSGENLSRKRNLAAKSPLmyewyq 165
Cdd:COG4403  143 LAALleELIAADESLDVISGAAGAILALLALYRATGDPaalDLAIRCGDRLLAAAVRDDGGRAWPTPEPAGRPL------ 216
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492095 166 eyyVGAAHGLAGIYYYLMQPSLQVNQGKLHSLVKPSVDFVCRLKFPS-GNYPP--CLDDTRDLLVHWCHGAPGVIYMLIQ 242
Cdd:COG4403  217 ---TGFAHGAAGIAYALLRLAAATGDERYLEAAREALAYERSLFDPEgGNWPDlrEPDDGPRFRTAWCHGAAGIGLARLA 293
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492095 243 AYKVFKEERYLCDAQQCADVIWQYGLLkKGYGLCHGAAGNAYAFLALYNLTQDLKYLYRACKFAEWCLD-YGEHGC---- 317
Cdd:COG4403  294 LLRALGDPELREDLERALETTLRRGFG-RNDSLCHGDAGNLELLLRAARATGDPELLEAARRLAALLLArAERAGPlglp 372
                        330       340       350
                 ....*....|....*....|....*....|
gi 755492095 318 ---RTADTPfSLFEGMAGTIYFLADLLVPT 344
Cdd:COG4403  373 glpRGVESP-GLMTGLAGIGYGLLRLAAPE 401
LanM-like cd04792
Cyclases involved in the biosynthesis of class II lantibiotics, and similar proteins; ...
16-345 3.09e-24

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: 103.93  E-value: 3.09e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492095  16 YTGWAGIAVLYLHLHNVFGDPAYLQMA-------HSYVKQSLNCLSRRSITFLCGDAG---PLAVAAVLYHKMNSEKQAE 85
Cdd:cd04792  493 YDGLSGIALFLAALAALTGDEKYRDLArkalrplRKLLRDLAADPRSLGIGGFTGLGSilyALSHLARLLGDPELLEDAL 572
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492095  86 ECITRLIHLNKIDPHvpNEMLYGRIGYIFALLFVNKNFGEEKIpqSHIQQICENILtsgenLSRKRNLAAKSPLMYEWYQ 165
Cdd:cd04792  573 ELADLLTEAIIEDEE--LDIIGGSAGAILVLLALYERTGDERA--LELAIACGDHL-----LKNAVENDGGARWKTPASS 643
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492095 166 EYYVGAAHGLAGIYYYLMQPSLQVNQGKLHSLVKPSVDFVCRLKFPS-GNYPPCLDDTRDLLVHWCHGAPGVIYMLIQAY 244
Cdd:cd04792  644 RPLTGFAHGAAGIAWALLRLAAVTGDERYLEAAKEALAYERSLFDPEeGNWPDRRKRNNSFSAAWCHGAAGIGLARLGLL 723
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492095 245 KVFKEERYLCDAQQCADVIWQYGlLKKGYGLCHGAAGNAYAFLALYNLTQDLKYLYRACKFAEWCLDYGE--HGCRTADT 322
Cdd:cd04792  724 KILNDDEIEEEIEKALETTLKYG-FGNNDSLCHGDLGNLELLLVAAKLLGDPELQEEAEELAAIVLNRAEeaGGWLCGLP 802
                        330       340
                 ....*....|....*....|....*..
gi 755492095 323 P----FSLFEGMAGTIYFLADLLVPTK 345
Cdd:cd04792  803 TgvesPGLMTGLSGIGYGLLRLAAPDK 829
lanti_2_LanM TIGR03897
type 2 lantibiotic biosynthesis protein LanM; Members of this family are known generally as ...
16-337 1.75e-21

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: 95.79  E-value: 1.75e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492095   16 YTGWAGIAVLYLHLHNVFGDPAYLQMAHSYVKQSLNCLSRRSIT-------FLCGDAGPLAVAAVLYhKMNSEKQAEECI 88
Cdd:TIGR03897 595 YDGLAGIALFLAYLAALTGDKRYRDLARKALQPLRKYLETLVELarsmglgAFSGLGSIIYALAHLG-QLLNDPELLNDA 673
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492095   89 TRLIhlNKIDPHVPNE-----MLYGRIGYIFALLFVNKNFGEEKIPQSHIQqiCENILtsgenLSRKRNLAAKSPLMYEW 163
Cdd:TIGR03897 674 KKIL--NRLEELIIKDeefldLIGGAAGAILVLLNLYEVTGDPEVLELAIA--CGEHL-----LKQAVEQEGGAAWKTSQ 744
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492095  164 YQEYYVGAAHGLAGIYYYLMQPSLQVNQGKLHSLVKPSVDFVCRLKFPS-GNYP-PCLDDTRDLLVHWCHGAPGVIYMLI 241
Cdd:TIGR03897 745 SNKPLTGFSHGAAGIAWALLRLYKVTGDQRYLEAAKEALAYERSLFDPEeGNWPdLREDGGPQFPVAWCHGAPGILLSRL 824
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492095  242 QAYKVFKEERYLCDAQQCADVIWQYGlLKKGYGLCHGAAGNAYAFLALYNLTQDLKYLYRACKFAEWCLD-YGEHG---C 317
Cdd:TIGR03897 825 GLLEILDDDEIREDIEIALETTLKYG-FGDNDSLCHGDLGNLEILLEAAKVLDDEELQELARRIASQVLArLTKNGryrL 903
                         330       340
                  ....*....|....*....|..
gi 755492095  318 RTADT--PFSLFEGMAGTIYFL 337
Cdd:TIGR03897 904 GLPRGveSPGLMTGLAGIGYGL 925
LanC cd04793
Cyclases involved in the biosynthesis of lantibiotics; LanC is the cyclase enzyme of the ...
17-340 2.85e-12

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: 66.99  E-value: 2.85e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492095  17 TGWAGIAVLYLHLHNVFGDPAYLQMAHSYVKQSLNCLSRRSITF-LCGdaGPLAVAAVLYHKMNSEKQAEECITRLihLN 95
Cdd:cd04793    4 SGLPGIALLLSELARLTPDEGWDEKAHQYLEAAIEELNSAGLSLsLFS--GLAGLAFALLALSRNGGRYQNLLSEL--NE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492095  96 KIDPHVPNEMLYGRI----------------GYIFALLFVNKNFgEEKIPQ--SHIQQICENILTSGENLSRKRNlaAKS 157
Cdd:cd04793   80 YIDELAEDRLAEAIAregispgeydvisglsGIGRYLLERPPPA-DDLLEEilDYLVDLTEPIIEGGEKVPWPEL--QPS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492095 158 PLMYEWYQEYYV--GAAHGLAGIYYYLmqpSLQVNQG----KLHSLVKPSVDFV--CRLKFPSGNYP----PCLDDTRDL 225
Cdd:cd04793  157 ESEKKAYPSGHFnlGLAHGIAGPLALL---ALALRRGievpGQREAIERIADWLlkWRQDDDEGWWPtivfPEELSNGRP 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492095 226 LVH-----WCHGAPGVIYMLIQAYKVFKEERYLCDAQQCADVIWQYGLLKKG---YGLCHGAAGNAYAFLALYNLTQDLK 297
Cdd:cd04793  234 PPVpsrdaWCYGDPGIARALLLAGKALGDPELQELAEEALLAALRRPDELTGlisPTLCHGYAGLLQIARRMYRDTGEPA 313
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 755492095 298 YLYRACKFAEWCLDYGEHGCR----------TADTPFSLFEGMAGTIYFLADL 340
Cdd:cd04793  314 LLAAAEELIDKLLDLYDPDLPfgfydtggsiTPLDDPGLLEGAAGIALALLSA 366
LanC_SerThrkinase cd04791
Lanthionine synthetase C-like domain associated with serine/threonine kinases; Some members of ...
16-341 2.87e-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: 60.75  E-value: 2.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492095  16 YTGWAGIA-VLYLHLHNVfgDPAYLQMAHSYVKQSLNCLSrrsiTFLCGDAGplaVAAVLYHkMNSEKQAEECITRLIHL 94
Cdd:cd04791    6 AYGAAGVLlALHRAGGAV--PEELEDWLVRRALRDLSLPP----GLYDGLAG---IAWVLYE-LGRREEAERLLDRALAL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492095  95 nkIDPHVPNEMLYGRIGYIFALLFVNKNFGEEKIPQsHIQQICENILTSGEnlsrkrnlAAKSPLMYEWYQEYYVGAAHG 174
Cdd:cd04791   76 --PLDSLDPSLYSGLAGIGLALLHLARATGDPEFLE-RAARIAERLAARLR--------EDDPGVYWNDAGAVRAGLLHG 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492095 175 LAGIYYYLMQPSLQVNQGKLHSLVKPSVDF-VCRLKFPSGNYPPCLDDTRDLLVHWCHGAPGVIYMLIQAYKVFKEERY- 252
Cdd:cd04791  145 WSGIALFLLRLYEATGDPAYLDLAERALRKdLARCVEDDDGALLQVDEGNRLLPYLCSGSAGIGLVLLRYLRHRGDDRYr 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492095 253 --LCDAQQCADVIWQYGLlkkgyGLCHGAAGNAYAFLALYNLTQDLKYLYRACKFAE---W-CLDY-------GEHGCR- 318
Cdd:cd04791  225 elLEGIARAVRSRFTVQP-----GLFHGLAGLGLALLDLAAALGDPRYRAAAERHARllnLhALPRdggiafpGDQLLRl 299
                        330       340
                 ....*....|....*....|...
gi 755492095 319 TADtpfsLFEGMAGTIYFLADLL 341
Cdd:cd04791  300 STD----LATGSAGVLLALLRLL 318
YyaL COG1331
Uncharacterized conserved protein YyaL, SSP411 family, contains thoiredoxin and six-hairpin ...
237-311 9.34e-07

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: 50.62  E-value: 9.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492095 237 IYMLIQAYKVFKEERYLCDAQQCADVIWQYgLLKKGYGLCH----GAAGNA-----YAF-----LALYNLTQDLKYLYRA 302
Cdd:COG1331  419 IAALAEAGRVLGDPEYLEAAERAADFILDN-LWDPDGRLLRsyrdGEAGIPgfledYAFliealLALYEATGDPRWLERA 497

                 ....*....
gi 755492095 303 CKFAEWCLD 311
Cdd:COG1331  498 LELADEALE 506
LanC_SerThrkinase cd04791
Lanthionine synthetase C-like domain associated with serine/threonine kinases; Some members of ...
169-340 5.13e-04

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: 41.49  E-value: 5.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492095 169 VGAAHGLAGIYYYLMQPSLQVNQgklhslvkPSVDFVCRLKFPSGNYPPCLDDtrdllvhwchGAPGVIYMLiqaYKVFK 248
Cdd:cd04791    3 LNVAYGAAGVLLALHRAGGAVPE--------ELEDWLVRRALRDLSLPPGLYD----------GLAGIAWVL---YELGR 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492095 249 EErylcDAQQCADVIWQYGLLKKGYGLCHGAAGNAYAFLALYNLTQDLKYLYRACKFAEWCLD------YGEHGCRTADT 322
Cdd:cd04791   62 RE----EAERLLDRALALPLDSLDPSLYSGLAGIGLALLHLARATGDPEFLERAARIAERLAArlreddPGVYWNDAGAV 137
                        170
                 ....*....|....*...
gi 755492095 323 PFSLFEGMAGTIYFLADL 340
Cdd:cd04791  138 RAGLLHGWSGIALFLLRL 155
LcnDR2 COG4403
Lantibiotic modifying enzyme [Defense mechanisms];
274-340 3.05e-03

Lantibiotic modifying enzyme [Defense mechanisms];


Pssm-ID: 443528 [Multi-domain]  Cd Length: 405  Bit Score: 39.34  E-value: 3.05e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755492095 274 GLCHGAAGNAYAFLALYNLTQDLKYLYRACKFAEWCLDYGEHGcRTADTPFSLFEGMAGTIYFLADL 340
Cdd:COG4403   62 DLYDGAAGIALFLAELARLTGDERYRELARAALRPLRRLLREE-LAGAMGPGLFTGLGGIAYALAHL 127
LanM-like cd04792
Cyclases involved in the biosynthesis of class II lantibiotics, and similar proteins; ...
264-338 8.82e-03

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: 38.06  E-value: 8.82e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755492095 264 WQYGLLkkGYGLCHGAAGNAYAFLALYNLTQDLKY--LYRAC-KFAEWCLDYGEHgcRTADTPFSLFEGMAGTIYFLA 338
Cdd:cd04792  483 WELSPL--GADLYDGLSGIALFLAALAALTGDEKYrdLARKAlRPLRKLLRDLAA--DPRSLGIGGFTGLGSILYALS 556
 
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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