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Conserved domains on  [gi|300795817|ref|NP_001177914|]
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glutathione S-transferase LANCL1 [Mus musculus]

Protein Classification

type 2 lanthipeptide synthetase LanM family protein( domain architecture ID 10268979)

type 2 lanthipeptide synthetase LanM family protein similar to Lactococcus lactis lcnDR2 which maybe implicated in the processing or the export process of the lantibiotic lacticin 481/lactococcin DR

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 ...
62-395 1.26e-150

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: 429.82  E-value: 1.26e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795817  62 YTGWAGIAVLYLHLHNVFGDP-----AYLQMAHSYVKQSLNCLSRR---SITFLCGDAGPLAVAAVLYHKMNSEKQAEEC 133
Cdd:cd04794    2 YTGAAGIAYMFLRLSEQGPDLkalseDYLELALEYIEASLTELARKgssRISFLCGDAGILALAAVIYHALGDSERDEEF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795817 134 ITRLIHL---NKIDPHVPNEMLYGRIGYIFALLFVNKNFGE-EKIPQSHIQQICENILTSGENLSRKRNlaAKSPLMYEW 209
Cdd:cd04794   82 LEQLLELakeALPLDDGPDELLYGRAGYLYALLFLRKHLGEsLEISDAVIKKLVDAILESGRQGAKDYR--SPPPLMYEW 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795817 210 YQEYYVGAAHGLAGIYYYLMQPSLQVNQGKLHSLVKPSVDFVCRLKFPSGNYPPCLDD--TRDLLVHWCHGAPGVIYMLI 287
Cdd:cd04794  160 HGKEYLGAAHGLAGILYMLLQAPPLLQIPSLAPLIKETLDYLLSLQFPSGNWPSSLGErsRSDRLVQWCHGAPGVVYLLA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795817 288 QAYKVFKEERYLCDAQQCADVIWQYGLLKKGYGLCHGAAGNAYAFLALYNLTQDLKYLYRACKFAEWCLDYGEH-GCRTA 366
Cdd:cd04794  240 KAYKVFLDPKYLEAAIRAGELVWERGLLRKGPGLCHGIAGNAYAFLLLYRLTGDEKYLYRALKFAEFALDYGFLtGARTP 319
                        330       340       350
                 ....*....|....*....|....*....|
gi 300795817 367 DTPFSLFEGMAGTIYFLADLLV-PTKAKFP 395
Cdd:cd04794  320 DRPYSLFEGLAGTACFLADLLQgPRKARFP 349
LanC_like super family cl04955
Cyclases involved in the biosynthesis of lantibiotics, and similar proteins; LanC is the ...
1-89 3.54e-03

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.


The actual alignment was detected with superfamily member cd04791:

Pssm-ID: 471159 [Multi-domain]  Cd Length: 327  Bit Score: 39.18  E-value: 3.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795817   1 MAQRAFPNPYADYNKSLAE----------NYFDSTGRLT-PEFSHRLTNKIRELLQQMERGLKSADPRDGT-GY-TGWAG 67
Cdd:cd04791   68 LLDRALALPLDSLDPSLYSglagiglallHLARATGDPEfLERAARIAERLAARLREDDPGVYWNDAGAVRaGLlHGWSG 147
                         90       100
                 ....*....|....*....|..
gi 300795817  68 IAVLYLHLHNVFGDPAYLQMAH 89
Cdd:cd04791  148 IALFLLRLYEATGDPAYLDLAE 169
 
Name Accession Description Interval E-value
euk_LANCL cd04794
Eukaryotic Lanthionine synthetase C-like protein; This family contains the lanthionine ...
62-395 1.26e-150

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: 429.82  E-value: 1.26e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795817  62 YTGWAGIAVLYLHLHNVFGDP-----AYLQMAHSYVKQSLNCLSRR---SITFLCGDAGPLAVAAVLYHKMNSEKQAEEC 133
Cdd:cd04794    2 YTGAAGIAYMFLRLSEQGPDLkalseDYLELALEYIEASLTELARKgssRISFLCGDAGILALAAVIYHALGDSERDEEF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795817 134 ITRLIHL---NKIDPHVPNEMLYGRIGYIFALLFVNKNFGE-EKIPQSHIQQICENILTSGENLSRKRNlaAKSPLMYEW 209
Cdd:cd04794   82 LEQLLELakeALPLDDGPDELLYGRAGYLYALLFLRKHLGEsLEISDAVIKKLVDAILESGRQGAKDYR--SPPPLMYEW 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795817 210 YQEYYVGAAHGLAGIYYYLMQPSLQVNQGKLHSLVKPSVDFVCRLKFPSGNYPPCLDD--TRDLLVHWCHGAPGVIYMLI 287
Cdd:cd04794  160 HGKEYLGAAHGLAGILYMLLQAPPLLQIPSLAPLIKETLDYLLSLQFPSGNWPSSLGErsRSDRLVQWCHGAPGVVYLLA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795817 288 QAYKVFKEERYLCDAQQCADVIWQYGLLKKGYGLCHGAAGNAYAFLALYNLTQDLKYLYRACKFAEWCLDYGEH-GCRTA 366
Cdd:cd04794  240 KAYKVFLDPKYLEAAIRAGELVWERGLLRKGPGLCHGIAGNAYAFLLLYRLTGDEKYLYRALKFAEFALDYGFLtGARTP 319
                        330       340       350
                 ....*....|....*....|....*....|
gi 300795817 367 DTPFSLFEGMAGTIYFLADLLV-PTKAKFP 395
Cdd:cd04794  320 DRPYSLFEGLAGTACFLADLLQgPRKARFP 349
LANC_like pfam05147
Lanthionine synthetase C-like protein; Lanthionines are thioether bridges that are putatively ...
55-399 5.03e-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: 357.08  E-value: 5.03e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795817   55 DPRDGTGYTGWAGIAVLYLHLHNVFGDPAYLQMAHSYVKQSLNCLSR---RSITFLCGDAGPLAVAAVLYHKMNSEKQAE 131
Cdd:pfam05147   1 SPLDDSLYTGLAGIALFLLELYKVTGNEKYLKLAHKYLEKIARALSEkglPDISFFCGAAGIAYALAVASKLLGDYQLLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795817  132 ECITRLIHL--NKIDPHVPNEMLYGRIGYIFALLFVNKNFGeekIPQSHIQQICENILTSGEnlsRKRNLAAKSPLMYEW 209
Cdd:pfam05147  81 NYLDSALELieSNKLPDEKYDLISGRAGILSYLLLLNEEFG---IEEDYLKLILKYLLRLGI---RSENQFSWCPLMYEP 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795817  210 YQEYYVGAAHGLAGIYYYLMQPSLQVNQGKLHSLVKPSVDFVCRLKFP-SGNYPPCLDDTRDLLVHWCHGAPGVIYMLIQ 288
Cdd:pfam05147 155 YGNFNLGFAHGLSGIAYALLALYKGTKSEKLLELIKKALNYEKSLKFKsEGNWPDSRGDKNDYLVAWCHGAPGILLALLL 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795817  289 AYKVFKEERYLCDAQQCADVIWQYGLLKKGYGLCHGAAGNAYAFLALYNLTQDLKYLYRACKFAEWCLDYGEHGCR---- 364
Cdd:pfam05147 235 AYKALNDEEFLEEAIEALEVVWKRGLLLKNPSLCHGLSGNLYILLLLYRLTNDPKYLERAKKFIISLLDYGKKNGFkcgl 314
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 300795817  365 -TADTPFSLFEGMAGTIYFLADLLVPTKAKFPAFEL 399
Cdd:pfam05147 315 pRGDESFGLMEGIAGIAYFLLDLLNPDESLFPSALL 350
LcnDR2 COG4403
Lantibiotic modifying enzyme [Defense mechanisms];
62-390 8.18e-30

Lantibiotic modifying enzyme [Defense mechanisms];


Pssm-ID: 443528 [Multi-domain]  Cd Length: 405  Bit Score: 119.07  E-value: 8.18e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795817  62 YTGWAGIAVLYLHLHNVFGDPAYLQMAHSYVKQSLNCLSR-----RSITFLCGDAGpLAVAAVLYHKMNSEKQAEECITR 136
Cdd:COG4403   64 YDGAAGIALFLAELARLTGDERYRELARAALRPLRRLLREelagaMGPGLFTGLGG-IAYALAHLGELLGDPRLLEDALA 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795817 137 LIHL--NKIDPHVPNEMLYGRIGYIFALLFVNKNFGEE---KIPQSHIQQICENILTSGENLSRKRNLAAKSPLmyewyq 211
Cdd:COG4403  143 LAALleELIAADESLDVISGAAGAILALLALYRATGDPaalDLAIRCGDRLLAAAVRDDGGRAWPTPEPAGRPL------ 216
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795817 212 eyyVGAAHGLAGIYYYLMQPSLQVNQGKLHSLVKPSVDFVCRLKFPS-GNYPP--CLDDTRDLLVHWCHGAPGVIYMLIQ 288
Cdd:COG4403  217 ---TGFAHGAAGIAYALLRLAAATGDERYLEAAREALAYERSLFDPEgGNWPDlrEPDDGPRFRTAWCHGAAGIGLARLA 293
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795817 289 AYKVFKEERYLCDAQQCADVIWQYGLLkKGYGLCHGAAGNAYAFLALYNLTQDLKYLYRACKFAEWCLD-YGEHGC---- 363
Cdd:COG4403  294 LLRALGDPELREDLERALETTLRRGFG-RNDSLCHGDAGNLELLLRAARATGDPELLEAARRLAALLLArAERAGPlglp 372
                        330       340       350
                 ....*....|....*....|....*....|
gi 300795817 364 ---RTADTPfSLFEGMAGTIYFLADLLVPT 390
Cdd:COG4403  373 glpRGVESP-GLMTGLAGIGYGLLRLAAPE 401
lanti_2_LanM TIGR03897
type 2 lantibiotic biosynthesis protein LanM; Members of this family are known generally as ...
62-383 4.47e-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: 95.40  E-value: 4.47e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795817   62 YTGWAGIAVLYLHLHNVFGDPAYLQMAHSYVKQSLNCLSRRSIT-------FLCGDAGPLAVAAVLYhKMNSEKQAEECI 134
Cdd:TIGR03897 595 YDGLAGIALFLAYLAALTGDKRYRDLARKALQPLRKYLETLVELarsmglgAFSGLGSIIYALAHLG-QLLNDPELLNDA 673
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795817  135 TRLIhlNKIDPHVPNE-----MLYGRIGYIFALLFVNKNFGEEKIPQSHIQqiCENILtsgenLSRKRNLAAKSPLMYEW 209
Cdd:TIGR03897 674 KKIL--NRLEELIIKDeefldLIGGAAGAILVLLNLYEVTGDPEVLELAIA--CGEHL-----LKQAVEQEGGAAWKTSQ 744
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795817  210 YQEYYVGAAHGLAGIYYYLMQPSLQVNQGKLHSLVKPSVDFVCRLKFPS-GNYP-PCLDDTRDLLVHWCHGAPGVIYMLI 287
Cdd:TIGR03897 745 SNKPLTGFSHGAAGIAWALLRLYKVTGDQRYLEAAKEALAYERSLFDPEeGNWPdLREDGGPQFPVAWCHGAPGILLSRL 824
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795817  288 QAYKVFKEERYLCDAQQCADVIWQYGlLKKGYGLCHGAAGNAYAFLALYNLTQDLKYLYRACKFAEWCLD-YGEHG---C 363
Cdd:TIGR03897 825 GLLEILDDDEIREDIEIALETTLKYG-FGDNDSLCHGDLGNLEILLEAAKVLDDEELQELARRIASQVLArLTKNGryrL 903
                         330       340
                  ....*....|....*....|..
gi 300795817  364 RTADT--PFSLFEGMAGTIYFL 383
Cdd:TIGR03897 904 GLPRGveSPGLMTGLAGIGYGL 925
LanC_SerThrkinase cd04791
Lanthionine synthetase C-like domain associated with serine/threonine kinases; Some members of ...
1-89 3.54e-03

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: 39.18  E-value: 3.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795817   1 MAQRAFPNPYADYNKSLAE----------NYFDSTGRLT-PEFSHRLTNKIRELLQQMERGLKSADPRDGT-GY-TGWAG 67
Cdd:cd04791   68 LLDRALALPLDSLDPSLYSglagiglallHLARATGDPEfLERAARIAERLAARLREDDPGVYWNDAGAVRaGLlHGWSG 147
                         90       100
                 ....*....|....*....|..
gi 300795817  68 IAVLYLHLHNVFGDPAYLQMAH 89
Cdd:cd04791  148 IALFLLRLYEATGDPAYLDLAE 169
 
Name Accession Description Interval E-value
euk_LANCL cd04794
Eukaryotic Lanthionine synthetase C-like protein; This family contains the lanthionine ...
62-395 1.26e-150

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: 429.82  E-value: 1.26e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795817  62 YTGWAGIAVLYLHLHNVFGDP-----AYLQMAHSYVKQSLNCLSRR---SITFLCGDAGPLAVAAVLYHKMNSEKQAEEC 133
Cdd:cd04794    2 YTGAAGIAYMFLRLSEQGPDLkalseDYLELALEYIEASLTELARKgssRISFLCGDAGILALAAVIYHALGDSERDEEF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795817 134 ITRLIHL---NKIDPHVPNEMLYGRIGYIFALLFVNKNFGE-EKIPQSHIQQICENILTSGENLSRKRNlaAKSPLMYEW 209
Cdd:cd04794   82 LEQLLELakeALPLDDGPDELLYGRAGYLYALLFLRKHLGEsLEISDAVIKKLVDAILESGRQGAKDYR--SPPPLMYEW 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795817 210 YQEYYVGAAHGLAGIYYYLMQPSLQVNQGKLHSLVKPSVDFVCRLKFPSGNYPPCLDD--TRDLLVHWCHGAPGVIYMLI 287
Cdd:cd04794  160 HGKEYLGAAHGLAGILYMLLQAPPLLQIPSLAPLIKETLDYLLSLQFPSGNWPSSLGErsRSDRLVQWCHGAPGVVYLLA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795817 288 QAYKVFKEERYLCDAQQCADVIWQYGLLKKGYGLCHGAAGNAYAFLALYNLTQDLKYLYRACKFAEWCLDYGEH-GCRTA 366
Cdd:cd04794  240 KAYKVFLDPKYLEAAIRAGELVWERGLLRKGPGLCHGIAGNAYAFLLLYRLTGDEKYLYRALKFAEFALDYGFLtGARTP 319
                        330       340       350
                 ....*....|....*....|....*....|
gi 300795817 367 DTPFSLFEGMAGTIYFLADLLV-PTKAKFP 395
Cdd:cd04794  320 DRPYSLFEGLAGTACFLADLLQgPRKARFP 349
LANC_like pfam05147
Lanthionine synthetase C-like protein; Lanthionines are thioether bridges that are putatively ...
55-399 5.03e-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: 357.08  E-value: 5.03e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795817   55 DPRDGTGYTGWAGIAVLYLHLHNVFGDPAYLQMAHSYVKQSLNCLSR---RSITFLCGDAGPLAVAAVLYHKMNSEKQAE 131
Cdd:pfam05147   1 SPLDDSLYTGLAGIALFLLELYKVTGNEKYLKLAHKYLEKIARALSEkglPDISFFCGAAGIAYALAVASKLLGDYQLLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795817  132 ECITRLIHL--NKIDPHVPNEMLYGRIGYIFALLFVNKNFGeekIPQSHIQQICENILTSGEnlsRKRNLAAKSPLMYEW 209
Cdd:pfam05147  81 NYLDSALELieSNKLPDEKYDLISGRAGILSYLLLLNEEFG---IEEDYLKLILKYLLRLGI---RSENQFSWCPLMYEP 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795817  210 YQEYYVGAAHGLAGIYYYLMQPSLQVNQGKLHSLVKPSVDFVCRLKFP-SGNYPPCLDDTRDLLVHWCHGAPGVIYMLIQ 288
Cdd:pfam05147 155 YGNFNLGFAHGLSGIAYALLALYKGTKSEKLLELIKKALNYEKSLKFKsEGNWPDSRGDKNDYLVAWCHGAPGILLALLL 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795817  289 AYKVFKEERYLCDAQQCADVIWQYGLLKKGYGLCHGAAGNAYAFLALYNLTQDLKYLYRACKFAEWCLDYGEHGCR---- 364
Cdd:pfam05147 235 AYKALNDEEFLEEAIEALEVVWKRGLLLKNPSLCHGLSGNLYILLLLYRLTNDPKYLERAKKFIISLLDYGKKNGFkcgl 314
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 300795817  365 -TADTPFSLFEGMAGTIYFLADLLVPTKAKFPAFEL 399
Cdd:pfam05147 315 pRGDESFGLMEGIAGIAYFLLDLLNPDESLFPSALL 350
LanC_like cd04434
Cyclases involved in the biosynthesis of lantibiotics, and similar proteins; LanC is the ...
62-396 2.36e-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: 209.67  E-value: 2.36e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795817  62 YTGWAGIAVLYLHLHNVFGDPAYLQMAHSYVKQSLNCLSRRS-----ITFLCGDAGPLAVAAVLYHKMNSEKQAEECITR 136
Cdd:cd04434    1 YHGAAGIALFLLELYRATGDKEYLDEAKEGADYLLARLEGLGeplsgASLYSGLSGLLWALLELYEDLGDEKLLDALLDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795817 137 LIHLNKIDPHV---PNEMLYGRIGYIFALLFVNKNFGEEKIpQSHIQQICENILTSGENLSRKRNLaaksplmYEWYQEY 213
Cdd:cd04434   81 LDDIALEAKEVwwsGNDLILGDAGIILYLLYAAEKTGDEKY-KELAAKIGDFLLQAAEELDNGGNW-------GLPKGSI 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795817 214 YVGAAHGLAGIYYYLMQPSLQVNQGKLHSLVKPSVDFVCRLKFPSGNYPPCL--DDTRDLLVHWCHGAPGVIYMLIQAYK 291
Cdd:cd04434  153 YPGFAHGTAGIAYALARLYEETGDEDFLDAAKEGAEYLEAIAVGDEDGFLIPlpDEKDLFYLGWCHGPAGTALLFYELYK 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795817 292 VFKE-ERYLCDAQQCADVIWQYGLLK---KGYGLCHGAAGNAYAFLALYNLTQD----LKYLYRACKFAEWCLDYGEHGC 363
Cdd:cd04434  233 ATGDlDLADELLEGIIKTGAPEKLSPgfwNNLCLCHGTAGVLEHLLYVYRLTGDereyAKRLADKLLGRATRNGEGLRWY 312
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 300795817 364 R------TADTPFSLFEGMAGTIYFLADLLVPTKAKFPA 396
Cdd:cd04434  313 QawtgpgRVDASLGLMVGAAGIASALLKLLRAETKARPL 351
LcnDR2 COG4403
Lantibiotic modifying enzyme [Defense mechanisms];
62-390 8.18e-30

Lantibiotic modifying enzyme [Defense mechanisms];


Pssm-ID: 443528 [Multi-domain]  Cd Length: 405  Bit Score: 119.07  E-value: 8.18e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795817  62 YTGWAGIAVLYLHLHNVFGDPAYLQMAHSYVKQSLNCLSR-----RSITFLCGDAGpLAVAAVLYHKMNSEKQAEECITR 136
Cdd:COG4403   64 YDGAAGIALFLAELARLTGDERYRELARAALRPLRRLLREelagaMGPGLFTGLGG-IAYALAHLGELLGDPRLLEDALA 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795817 137 LIHL--NKIDPHVPNEMLYGRIGYIFALLFVNKNFGEE---KIPQSHIQQICENILTSGENLSRKRNLAAKSPLmyewyq 211
Cdd:COG4403  143 LAALleELIAADESLDVISGAAGAILALLALYRATGDPaalDLAIRCGDRLLAAAVRDDGGRAWPTPEPAGRPL------ 216
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795817 212 eyyVGAAHGLAGIYYYLMQPSLQVNQGKLHSLVKPSVDFVCRLKFPS-GNYPP--CLDDTRDLLVHWCHGAPGVIYMLIQ 288
Cdd:COG4403  217 ---TGFAHGAAGIAYALLRLAAATGDERYLEAAREALAYERSLFDPEgGNWPDlrEPDDGPRFRTAWCHGAAGIGLARLA 293
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795817 289 AYKVFKEERYLCDAQQCADVIWQYGLLkKGYGLCHGAAGNAYAFLALYNLTQDLKYLYRACKFAEWCLD-YGEHGC---- 363
Cdd:COG4403  294 LLRALGDPELREDLERALETTLRRGFG-RNDSLCHGDAGNLELLLRAARATGDPELLEAARRLAALLLArAERAGPlglp 372
                        330       340       350
                 ....*....|....*....|....*....|
gi 300795817 364 ---RTADTPfSLFEGMAGTIYFLADLLVPT 390
Cdd:COG4403  373 glpRGVESP-GLMTGLAGIGYGLLRLAAPE 401
LanM-like cd04792
Cyclases involved in the biosynthesis of class II lantibiotics, and similar proteins; ...
62-391 6.56e-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: 6.56e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795817  62 YTGWAGIAVLYLHLHNVFGDPAYLQMA-------HSYVKQSLNCLSRRSITFLCGDAG---PLAVAAVLYHKMNSEKQAE 131
Cdd:cd04792  493 YDGLSGIALFLAALAALTGDEKYRDLArkalrplRKLLRDLAADPRSLGIGGFTGLGSilyALSHLARLLGDPELLEDAL 572
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795817 132 ECITRLIHLNKIDPHvpNEMLYGRIGYIFALLFVNKNFGEEKIpqSHIQQICENILtsgenLSRKRNLAAKSPLMYEWYQ 211
Cdd:cd04792  573 ELADLLTEAIIEDEE--LDIIGGSAGAILVLLALYERTGDERA--LELAIACGDHL-----LKNAVENDGGARWKTPASS 643
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795817 212 EYYVGAAHGLAGIYYYLMQPSLQVNQGKLHSLVKPSVDFVCRLKFPS-GNYPPCLDDTRDLLVHWCHGAPGVIYMLIQAY 290
Cdd:cd04792  644 RPLTGFAHGAAGIAWALLRLAAVTGDERYLEAAKEALAYERSLFDPEeGNWPDRRKRNNSFSAAWCHGAAGIGLARLGLL 723
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795817 291 KVFKEERYLCDAQQCADVIWQYGlLKKGYGLCHGAAGNAYAFLALYNLTQDLKYLYRACKFAEWCLDYGE--HGCRTADT 368
Cdd:cd04792  724 KILNDDEIEEEIEKALETTLKYG-FGNNDSLCHGDLGNLELLLVAAKLLGDPELQEEAEELAAIVLNRAEeaGGWLCGLP 802
                        330       340
                 ....*....|....*....|....*..
gi 300795817 369 P----FSLFEGMAGTIYFLADLLVPTK 391
Cdd:cd04792  803 TgvesPGLMTGLSGIGYGLLRLAAPDK 829
lanti_2_LanM TIGR03897
type 2 lantibiotic biosynthesis protein LanM; Members of this family are known generally as ...
62-383 4.47e-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: 95.40  E-value: 4.47e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795817   62 YTGWAGIAVLYLHLHNVFGDPAYLQMAHSYVKQSLNCLSRRSIT-------FLCGDAGPLAVAAVLYhKMNSEKQAEECI 134
Cdd:TIGR03897 595 YDGLAGIALFLAYLAALTGDKRYRDLARKALQPLRKYLETLVELarsmglgAFSGLGSIIYALAHLG-QLLNDPELLNDA 673
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795817  135 TRLIhlNKIDPHVPNE-----MLYGRIGYIFALLFVNKNFGEEKIPQSHIQqiCENILtsgenLSRKRNLAAKSPLMYEW 209
Cdd:TIGR03897 674 KKIL--NRLEELIIKDeefldLIGGAAGAILVLLNLYEVTGDPEVLELAIA--CGEHL-----LKQAVEQEGGAAWKTSQ 744
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795817  210 YQEYYVGAAHGLAGIYYYLMQPSLQVNQGKLHSLVKPSVDFVCRLKFPS-GNYP-PCLDDTRDLLVHWCHGAPGVIYMLI 287
Cdd:TIGR03897 745 SNKPLTGFSHGAAGIAWALLRLYKVTGDQRYLEAAKEALAYERSLFDPEeGNWPdLREDGGPQFPVAWCHGAPGILLSRL 824
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795817  288 QAYKVFKEERYLCDAQQCADVIWQYGlLKKGYGLCHGAAGNAYAFLALYNLTQDLKYLYRACKFAEWCLD-YGEHG---C 363
Cdd:TIGR03897 825 GLLEILDDDEIREDIEIALETTLKYG-FGDNDSLCHGDLGNLEILLEAAKVLDDEELQELARRIASQVLArLTKNGryrL 903
                         330       340
                  ....*....|....*....|..
gi 300795817  364 RTADT--PFSLFEGMAGTIYFL 383
Cdd:TIGR03897 904 GLPRGveSPGLMTGLAGIGYGL 925
LanC cd04793
Cyclases involved in the biosynthesis of lantibiotics; LanC is the cyclase enzyme of the ...
63-386 2.29e-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: 67.76  E-value: 2.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795817  63 TGWAGIAVLYLHLHNVFGDPAYLQMAHSYVKQSLNCLSRRSITF-LCGdaGPLAVAAVLYHKMNSEKQAEECITRLihLN 141
Cdd:cd04793    4 SGLPGIALLLSELARLTPDEGWDEKAHQYLEAAIEELNSAGLSLsLFS--GLAGLAFALLALSRNGGRYQNLLSEL--NE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795817 142 KIDPHVPNEMLYGRI----------------GYIFALLFVNKNFgEEKIPQ--SHIQQICENILTSGENLSRKRNlaAKS 203
Cdd:cd04793   80 YIDELAEDRLAEAIAregispgeydvisglsGIGRYLLERPPPA-DDLLEEilDYLVDLTEPIIEGGEKVPWPEL--QPS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795817 204 PLMYEWYQEYYV--GAAHGLAGIYYYLmqpSLQVNQG----KLHSLVKPSVDFV--CRLKFPSGNYP----PCLDDTRDL 271
Cdd:cd04793  157 ESEKKAYPSGHFnlGLAHGIAGPLALL---ALALRRGievpGQREAIERIADWLlkWRQDDDEGWWPtivfPEELSNGRP 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795817 272 LVH-----WCHGAPGVIYMLIQAYKVFKEERYLCDAQQCADVIWQYGLLKKG---YGLCHGAAGNAYAFLALYNLTQDLK 343
Cdd:cd04793  234 PPVpsrdaWCYGDPGIARALLLAGKALGDPELQELAEEALLAALRRPDELTGlisPTLCHGYAGLLQIARRMYRDTGEPA 313
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 300795817 344 YLYRACKFAEWCLDYGEHGCR----------TADTPFSLFEGMAGTIYFLADL 386
Cdd:cd04793  314 LLAAAEELIDKLLDLYDPDLPfgfydtggsiTPLDDPGLLEGAAGIALALLSA 366
LanC_SerThrkinase cd04791
Lanthionine synthetase C-like domain associated with serine/threonine kinases; Some members of ...
62-387 1.70e-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: 1.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795817  62 YTGWAGIA-VLYLHLHNVfgDPAYLQMAHSYVKQSLNCLSrrsiTFLCGDAGplaVAAVLYHkMNSEKQAEECITRLIHL 140
Cdd:cd04791    6 AYGAAGVLlALHRAGGAV--PEELEDWLVRRALRDLSLPP----GLYDGLAG---IAWVLYE-LGRREEAERLLDRALAL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795817 141 nkIDPHVPNEMLYGRIGYIFALLFVNKNFGEEKIPQsHIQQICENILTSGEnlsrkrnlAAKSPLMYEWYQEYYVGAAHG 220
Cdd:cd04791   76 --PLDSLDPSLYSGLAGIGLALLHLARATGDPEFLE-RAARIAERLAARLR--------EDDPGVYWNDAGAVRAGLLHG 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795817 221 LAGIYYYLMQPSLQVNQGKLHSLVKPSVDF-VCRLKFPSGNYPPCLDDTRDLLVHWCHGAPGVIYMLIQAYKVFKEERY- 298
Cdd:cd04791  145 WSGIALFLLRLYEATGDPAYLDLAERALRKdLARCVEDDDGALLQVDEGNRLLPYLCSGSAGIGLVLLRYLRHRGDDRYr 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795817 299 --LCDAQQCADVIWQYGLlkkgyGLCHGAAGNAYAFLALYNLTQDLKYLYRACKFAE---W-CLDY-------GEHGCR- 364
Cdd:cd04791  225 elLEGIARAVRSRFTVQP-----GLFHGLAGLGLALLDLAAALGDPRYRAAAERHARllnLhALPRdggiafpGDQLLRl 299
                        330       340
                 ....*....|....*....|...
gi 300795817 365 TADtpfsLFEGMAGTIYFLADLL 387
Cdd:cd04791  300 STD----LATGSAGVLLALLRLL 318
YyaL COG1331
Uncharacterized conserved protein YyaL, SSP411 family, contains thoiredoxin and six-hairpin ...
283-357 1.33e-06

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: 1.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795817 283 IYMLIQAYKVFKEERYLCDAQQCADVIWQYgLLKKGYGLCH----GAAGNA-----YAF-----LALYNLTQDLKYLYRA 348
Cdd:COG1331  419 IAALAEAGRVLGDPEYLEAAERAADFILDN-LWDPDGRLLRsyrdGEAGIPgfledYAFliealLALYEATGDPRWLERA 497

                 ....*....
gi 300795817 349 CKFAEWCLD 357
Cdd:COG1331  498 LELADEALE 506
LanC_SerThrkinase cd04791
Lanthionine synthetase C-like domain associated with serine/threonine kinases; Some members of ...
215-386 3.97e-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: 42.26  E-value: 3.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795817 215 VGAAHGLAGIYYYLMQPSLQVNQgklhslvkPSVDFVCRLKFPSGNYPPCLDDtrdllvhwchGAPGVIYMLiqaYKVFK 294
Cdd:cd04791    3 LNVAYGAAGVLLALHRAGGAVPE--------ELEDWLVRRALRDLSLPPGLYD----------GLAGIAWVL---YELGR 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795817 295 EErylcDAQQCADVIWQYGLLKKGYGLCHGAAGNAYAFLALYNLTQDLKYLYRACKFAEWCLD------YGEHGCRTADT 368
Cdd:cd04791   62 RE----EAERLLDRALALPLDSLDPSLYSGLAGIGLALLHLARATGDPEFLERAARIAERLAArlreddPGVYWNDAGAV 137
                        170
                 ....*....|....*...
gi 300795817 369 PFSLFEGMAGTIYFLADL 386
Cdd:cd04791  138 RAGLLHGWSGIALFLLRL 155
LcnDR2 COG4403
Lantibiotic modifying enzyme [Defense mechanisms];
320-386 3.02e-03

Lantibiotic modifying enzyme [Defense mechanisms];


Pssm-ID: 443528 [Multi-domain]  Cd Length: 405  Bit Score: 39.34  E-value: 3.02e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300795817 320 GLCHGAAGNAYAFLALYNLTQDLKYLYRACKFAEWCLDYGEHGcRTADTPFSLFEGMAGTIYFLADL 386
Cdd:COG4403   62 DLYDGAAGIALFLAELARLTGDERYRELARAALRPLRRLLREE-LAGAMGPGLFTGLGGIAYALAHL 127
LanC_SerThrkinase cd04791
Lanthionine synthetase C-like domain associated with serine/threonine kinases; Some members of ...
1-89 3.54e-03

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: 39.18  E-value: 3.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795817   1 MAQRAFPNPYADYNKSLAE----------NYFDSTGRLT-PEFSHRLTNKIRELLQQMERGLKSADPRDGT-GY-TGWAG 67
Cdd:cd04791   68 LLDRALALPLDSLDPSLYSglagiglallHLARATGDPEfLERAARIAERLAARLREDDPGVYWNDAGAVRaGLlHGWSG 147
                         90       100
                 ....*....|....*....|..
gi 300795817  68 IAVLYLHLHNVFGDPAYLQMAH 89
Cdd:cd04791  148 IALFLLRLYEATGDPAYLDLAE 169
 
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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