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Conserved domains on  [gi|109732483|gb|AAI15945|]
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Lancl3 protein [Mus musculus]

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 ...
 1-171 9.34e-84

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: 250.71  E-value: 9.34e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109732483   1 MLLSYQEHL-KPSDRELVWQSVDFLME-QEQNCNWPPELGEtIERENELVHWCHGAPGIAYLFAKAYLISKKPQYLDTCI 78
Cdd:cd04794  177 MLLQAPPLLqIPSLAPLIKETLDYLLSlQFPSGNWPSSLGE-RSRSDRLVQWCHGAPGVVYLLAKAYKVFLDPKYLEAAI 255

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109732483  79 RCGELTWQKGLLKKGPGICHGVAGSAYVFLLLYRLTGNSKYIYRAQRFAQFLFTEEFKSGSRVLESIYSLYEGFSGTVCF 158
Cdd:cd04794  256 RAGELVWERGLLRKGPGLCHGIAGNAYAFLLLYRLTGDEKYLYRALKFAEFALDYGFLTGARTPDRPYSLFEGLAGTACF 335

                        170
                 ....*....|....
gi 109732483 159 LIDLLQ-PNQAEFP 171
Cdd:cd04794  336 LADLLQgPRKARFP 349
 
Name Accession Description Interval E-value
euk_LANCL cd04794
Eukaryotic Lanthionine synthetase C-like protein; This family contains the lanthionine ...
 1-171 9.34e-84

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: 250.71  E-value: 9.34e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109732483   1 MLLSYQEHL-KPSDRELVWQSVDFLME-QEQNCNWPPELGEtIERENELVHWCHGAPGIAYLFAKAYLISKKPQYLDTCI 78
Cdd:cd04794  177 MLLQAPPLLqIPSLAPLIKETLDYLLSlQFPSGNWPSSLGE-RSRSDRLVQWCHGAPGVVYLLAKAYKVFLDPKYLEAAI 255

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109732483  79 RCGELTWQKGLLKKGPGICHGVAGSAYVFLLLYRLTGNSKYIYRAQRFAQFLFTEEFKSGSRVLESIYSLYEGFSGTVCF 158
Cdd:cd04794  256 RAGELVWERGLLRKGPGLCHGIAGNAYAFLLLYRLTGDEKYLYRALKFAEFALDYGFLTGARTPDRPYSLFEGLAGTACF 335

                        170
                 ....*....|....
gi 109732483 159 LIDLLQ-PNQAEFP 171
Cdd:cd04794  336 LADLLQgPRKARFP 349
LANC_like pfam05147
Lanthionine synthetase C-like protein; Lanthionines are thioether bridges that are putatively ...
 2-171 6.94e-50

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: 164.09  E-value: 6.94e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109732483    2 LLSYQEHLKPSDRELVWQSVDFLME--QEQNCNWPPELGEtieRENELVHWCHGAPGIAYLFAKAYLISKKPQYLDTCIR 79
Cdd:pfam05147 174 LALYKGTKSEKLLELIKKALNYEKSlkFKSEGNWPDSRGD---KNDYLVAWCHGAPGILLALLLAYKALNDEEFLEEAIE 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109732483   80 CGELTWQKGLLKKGPGICHGVAGSAYVFLLLYRLTGNSKYIYRAQRFAQFLFTEE----FKSGSRVLESIYSLYEGFSGT 155
Cdd:pfam05147 251 ALEVVWKRGLLLKNPSLCHGLSGNLYILLLLYRLTNDPKYLERAKKFIISLLDYGkkngFKCGLPRGDESFGLMEGIAGI 330

                         170
                  ....*....|....*.
gi 109732483  156 VCFLIDLLQPNQAEFP 171
Cdd:pfam05147 331 AYFLLDLLNPDESLFP 346
LcnDR2 COG4403
Lantibiotic modifying enzyme [Defense mechanisms];
14-167 3.20e-15

Lantibiotic modifying enzyme [Defense mechanisms];


Pssm-ID: 443528 [Multi-domain]  Cd Length: 405  Bit Score: 72.08  E-value: 3.20e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109732483  14 RELVWQSVDFLMEQ--EQNCNWPPeLGETIERENELVHWCHGAPGIAYLFAKAYLISKKPQYLDTCIRCGELTWQKGLLk 91
Cdd:COG4403  243 LEAAREALAYERSLfdPEGGNWPD-LREPDDGPRFRTAWCHGAAGIGLARLALLRALGDPELREDLERALETTLRRGFG- 320

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109732483  92 KGPGICHGVAGSAYVFLLLYRLTGNSKYIYRAQRFAQFLFTEEFKSGSRVLESI------YSLYEGFSGTVCFLIDLLQP 165
Cdd:COG4403  321 RNDSLCHGDAGNLELLLRAARATGDPELLEAARRLAALLLARAERAGPLGLPGLprgvesPGLMTGLAGIGYGLLRLAAP 400


                 ..
gi 109732483 166 NQ 167
Cdd:COG4403  401 ER 402
lanti_2_LanM TIGR03897
type 2 lantibiotic biosynthesis protein LanM; Members of this family are known generally as ...
 24-154 1.20e-09

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: 56.11  E-value: 1.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109732483   24 LMEQEQNC------NWPpELGETIErENELVHWCHGAPGIaylfAKAYLISKKPQYLDTC---IRCGELTWQKGLLKKGP 94
Cdd:TIGR03897 782 ALAYERSLfdpeegNWP-DLREDGG-PQFPVAWCHGAPGI----LLSRLGLLEILDDDEIredIEIALETTLKYGFGDND 855

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109732483   95 GICHGVAGSAYVFLLLYRLTGNSKYIYRAQRFAQFLF-----TEEFKSG-SRVLESiYSLYEGFSG 154
Cdd:TIGR03897 856 SLCHGDLGNLEILLEAAKVLDDEELQELARRIASQVLarltkNGRYRLGlPRGVES-PGLMTGLAG 920
 
Name Accession Description Interval E-value
euk_LANCL cd04794
Eukaryotic Lanthionine synthetase C-like protein; This family contains the lanthionine ...
 1-171 9.34e-84

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: 250.71  E-value: 9.34e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109732483   1 MLLSYQEHL-KPSDRELVWQSVDFLME-QEQNCNWPPELGEtIERENELVHWCHGAPGIAYLFAKAYLISKKPQYLDTCI 78
Cdd:cd04794  177 MLLQAPPLLqIPSLAPLIKETLDYLLSlQFPSGNWPSSLGE-RSRSDRLVQWCHGAPGVVYLLAKAYKVFLDPKYLEAAI 255

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109732483  79 RCGELTWQKGLLKKGPGICHGVAGSAYVFLLLYRLTGNSKYIYRAQRFAQFLFTEEFKSGSRVLESIYSLYEGFSGTVCF 158
Cdd:cd04794  256 RAGELVWERGLLRKGPGLCHGIAGNAYAFLLLYRLTGDEKYLYRALKFAEFALDYGFLTGARTPDRPYSLFEGLAGTACF 335

                        170
                 ....*....|....
gi 109732483 159 LIDLLQ-PNQAEFP 171
Cdd:cd04794  336 LADLLQgPRKARFP 349
LANC_like pfam05147
Lanthionine synthetase C-like protein; Lanthionines are thioether bridges that are putatively ...
 2-171 6.94e-50

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: 164.09  E-value: 6.94e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109732483    2 LLSYQEHLKPSDRELVWQSVDFLME--QEQNCNWPPELGEtieRENELVHWCHGAPGIAYLFAKAYLISKKPQYLDTCIR 79
Cdd:pfam05147 174 LALYKGTKSEKLLELIKKALNYEKSlkFKSEGNWPDSRGD---KNDYLVAWCHGAPGILLALLLAYKALNDEEFLEEAIE 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109732483   80 CGELTWQKGLLKKGPGICHGVAGSAYVFLLLYRLTGNSKYIYRAQRFAQFLFTEE----FKSGSRVLESIYSLYEGFSGT 155
Cdd:pfam05147 251 ALEVVWKRGLLLKNPSLCHGLSGNLYILLLLYRLTNDPKYLERAKKFIISLLDYGkkngFKCGLPRGDESFGLMEGIAGI 330

                         170
                  ....*....|....*.
gi 109732483  156 VCFLIDLLQPNQAEFP 171
Cdd:pfam05147 331 AYFLLDLLNPDESLFP 346
LcnDR2 COG4403
Lantibiotic modifying enzyme [Defense mechanisms];
14-167 3.20e-15

Lantibiotic modifying enzyme [Defense mechanisms];


Pssm-ID: 443528 [Multi-domain]  Cd Length: 405  Bit Score: 72.08  E-value: 3.20e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109732483  14 RELVWQSVDFLMEQ--EQNCNWPPeLGETIERENELVHWCHGAPGIAYLFAKAYLISKKPQYLDTCIRCGELTWQKGLLk 91
Cdd:COG4403  243 LEAAREALAYERSLfdPEGGNWPD-LREPDDGPRFRTAWCHGAAGIGLARLALLRALGDPELREDLERALETTLRRGFG- 320

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109732483  92 KGPGICHGVAGSAYVFLLLYRLTGNSKYIYRAQRFAQFLFTEEFKSGSRVLESI------YSLYEGFSGTVCFLIDLLQP 165
Cdd:COG4403  321 RNDSLCHGDAGNLELLLRAARATGDPELLEAARRLAALLLARAERAGPLGLPGLprgvesPGLMTGLAGIGYGLLRLAAP 400


                 ..
gi 109732483 166 NQ 167
Cdd:COG4403  401 ER 402
LanC_like cd04434
Cyclases involved in the biosynthesis of lantibiotics, and similar proteins; LanC is the ...
 1-172 8.79e-15

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: 70.61  E-value: 8.79e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109732483   1 MLLSYQEHLKPSDR-ELVWQSVDFLMEQE-QNCNWPPELGETiERENELVHWCHGAPGIAYLFAKAYLISKKPQYLD--- 75
Cdd:cd04434  166 ALARLYEETGDEDFlDAAKEGAEYLEAIAvGDEDGFLIPLPD-EKDLFYLGWCHGPAGTALLFYELYKATGDLDLADell 244

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109732483  76 -TCIRCGELTWQKGLLKKGPGICHGVAGSAYVFLLLYRLTGNSKY---------IYRAQRFAQFLFTEEFKSGSRVLESI 145
Cdd:cd04434  245 eGIIKTGAPEKLSPGFWNNLCLCHGTAGVLEHLLYVYRLTGDEREyakrladklLGRATRNGEGLRWYQAWTGPGRVDAS 324

                        170       180
                 ....*....|....*....|....*..
gi 109732483 146 YSLYEGFSGTVCFLIDLLQPNQAEFPL 172
Cdd:cd04434  325 LGLMVGAAGIASALLKLLRAETKARPL 351
LanC cd04793
Cyclases involved in the biosynthesis of lantibiotics; LanC is the cyclase enzyme of the ...
 14-166 1.91e-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: 64.29  E-value: 1.91e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109732483  14 RELVWQSVDFLMEQEQ--NCNWPPELG--ETIERENELVH-----WCHGAPGIAYLFAKAYLISKKPQYLDTCIRCGELT 84
Cdd:cd04793  197 REAIERIADWLLKWRQddDEGWWPTIVfpEELSNGRPPPVpsrdaWCYGDPGIARALLLAGKALGDPELQELAEEALLAA 276

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109732483  85 WQKGLLKKG---PGICHGVAGSAYVFLLLYRLTGNSKYIYRAQR-------FAQFLFTEEFKS--GSRVLESIYSLYEGF 152
Cdd:cd04793  277 LRRPDELTGlisPTLCHGYAGLLQIARRMYRDTGEPALLAAAEElidklldLYDPDLPFGFYDtgGSITPLDDPGLLEGA 356

                        170
                 ....*....|....
gi 109732483 153 SGTVCFLIDLLQPN 166
Cdd:cd04793  357 AGIALALLSAITDK 370
lanti_2_LanM TIGR03897
type 2 lantibiotic biosynthesis protein LanM; Members of this family are known generally as ...
 24-154 1.20e-09

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: 56.11  E-value: 1.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109732483   24 LMEQEQNC------NWPpELGETIErENELVHWCHGAPGIaylfAKAYLISKKPQYLDTC---IRCGELTWQKGLLKKGP 94
Cdd:TIGR03897 782 ALAYERSLfdpeegNWP-DLREDGG-PQFPVAWCHGAPGI----LLSRLGLLEILDDDEIredIEIALETTLKYGFGDND 855

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109732483   95 GICHGVAGSAYVFLLLYRLTGNSKYIYRAQRFAQFLF-----TEEFKSG-SRVLESiYSLYEGFSG 154
Cdd:TIGR03897 856 SLCHGDLGNLEILLEAAKVLDDEELQELARRIASQVLarltkNGRYRLGlPRGVES-PGLMTGLAG 920
LanC_SerThrkinase cd04791
Lanthionine synthetase C-like domain associated with serine/threonine kinases; Some members of ...
 50-164 2.17e-08

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: 52.27  E-value: 2.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109732483  50 WCHGAPGIAYLFAKAYLISKKPQYLDTCIRCGEL---TWQKGLL--------KKGPGICHGVAGSAYVFLLLYRLTGNSK 118
Cdd:cd04791   84 LYSGLAGIGLALLHLARATGDPEFLERAARIAERlaaRLREDDPgvywndagAVRAGLLHGWSGIALFLLRLYEATGDPA 163

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 109732483 119 YIYRAQRFAQFLFTE----------EFKSGSRVLesiYSLYEGFSGTVCFLIDLLQ 164
Cdd:cd04791  164 YLDLAERALRKDLARcvedddgallQVDEGNRLL---PYLCSGSAGIGLVLLRYLR 216
LanC_like cd04434
Cyclases involved in the biosynthesis of lantibiotics, and similar proteins; LanC is the ...
 53-164 2.61e-08

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: 52.12  E-value: 2.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109732483  53 GAPGIAYLFAKAYLISKKPQYLDTCIRCGEL---------TWQKGLLKKG---PGICHGVAGSAYVFLLLYRLTGNSKYI 120
Cdd:cd04434  101 GDAGIILYLLYAAEKTGDEKYKELAAKIGDFllqaaeeldNGGNWGLPKGsiyPGFAHGTAGIAYALARLYEETGDEDFL 180

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 109732483 121 YRAQRFAQFLFTEEFKSGSRVL------ESIYSLY--EGFSGTVCFLIDLLQ 164
Cdd:cd04434  181 DAAKEGAEYLEAIAVGDEDGFLiplpdeKDLFYLGwcHGPAGTALLFYELYK 232
LanC_SerThrkinase cd04791
Lanthionine synthetase C-like domain associated with serine/threonine kinases; Some members of ...
 47-172 3.56e-08

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: 51.50  E-value: 3.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109732483  47 LVHWCHGAPGIAYLFAKAYLISKKPQY---LDTCIRC--GELTWQkgllkkgPGICHGVAGSAYVFLLLYRLTGNSKYIY 121
Cdd:cd04791  197 LPYLCSGSAGIGLVLLRYLRHRGDDRYrelLEGIARAvrSRFTVQ-------PGLFHGLAGLGLALLDLAAALGDPRYRA 269

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 109732483 122 RAQRFAQFLFTEEFKSGSRVL---ESIY----SLYEGFSGTVCFLIDLLQPNQAEFPL 172
Cdd:cd04791  270 AAERHARLLNLHALPRDGGIAfpgDQLLrlstDLATGSAGVLLALLRLLHGGRSWLPL 327
LcnDR2 COG4403
Lantibiotic modifying enzyme [Defense mechanisms];
51-130 1.59e-07

Lantibiotic modifying enzyme [Defense mechanisms];


Pssm-ID: 443528 [Multi-domain]  Cd Length: 405  Bit Score: 49.74  E-value: 1.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109732483  51 CHGAPGIAYLFAKAYLISKKPQYLDTCIRCGELTWQKGLLKKGPGICHGVAGSAYVFLLLYRLTGNSKYIYRAQRFAQFL 130
Cdd:COG4403  114 FTGLGGIAYALAHLGELLGDPRLLEDALALAALLEELIAADESLDVISGAAGAILALLALYRATGDPAALDLAIRCGDRL 193
LanC_like cd04434
Cyclases involved in the biosynthesis of lantibiotics, and similar proteins; LanC is the ...
 1-120 2.78e-07

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: 49.04  E-value: 2.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109732483   1 MLLSYQEHLK-PSDRELVWQSVDFLMEQEQNCNWPPELGETIERENelVHWCHGAPGIAYLFAKAYLISKKPQYLDTCIR 79
Cdd:cd04434  108 YLLYAAEKTGdEKYKELAAKIGDFLLQAAEELDNGGNWGLPKGSIY--PGFAHGTAGIAYALARLYEETGDEDFLDAAKE 185

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 109732483  80 CGE------LTWQKGLLKKGP--------GICHGVAGSAYVFLLLYRLTGNSKYI 120
Cdd:cd04434  186 GAEyleaiaVGDEDGFLIPLPdekdlfylGWCHGPAGTALLFYELYKATGDLDLA 240
LanM-like cd04792
Cyclases involved in the biosynthesis of class II lantibiotics, and similar proteins; ...
 2-167 3.41e-07

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: 49.23  E-value: 3.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109732483   2 LLSYQEHLKPSD-RELVWQSVDFlmEQ----EQNCNWPpelGETIERENELVHWCHGAPGIAY--LFAKAYLISKKP-QY 73
Cdd:cd04792  660 LLRLAAVTGDERyLEAAKEALAY--ERslfdPEEGNWP---DRRKRNNSFSAAWCHGAAGIGLarLGLLKILNDDEIeEE 734

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109732483  74 LDTCIRCgeltwqkgLLKKGPG----ICHGVAGSAYVFLLLYRLTGNSKYIYRAQRFAQFLFtEEFKSGSRVLESI---- 145
Cdd:cd04792  735 IEKALET--------TLKYGFGnndsLCHGDLGNLELLLVAAKLLGDPELQEEAEELAAIVL-NRAEEAGGWLCGLptgv 805

                        170       180
                 ....*....|....*....|....
gi 109732483 146 --YSLYEGFSGTVCFLIDLLQPNQ 167
Cdd:cd04792  806 esPGLMTGLSGIGYGLLRLAAPDK 829
LcnDR2 COG4403
Lantibiotic modifying enzyme [Defense mechanisms];
52-130 9.16e-07

Lantibiotic modifying enzyme [Defense mechanisms];


Pssm-ID: 443528 [Multi-domain]  Cd Length: 405  Bit Score: 47.81  E-value: 9.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109732483  52 HGAPGIAYLFAKAYLISKKPQYLDTCIRCgeLTWQKGLLK------KGPGICHGVAGSAYVFLLLYRLTGNSKYIYRAQR 125
Cdd:COG4403   65 DGAAGIALFLAELARLTGDERYRELARAA--LRPLRRLLReelagaMGPGLFTGLGGIAYALAHLGELLGDPRLLEDALA 142


                 ....*
gi 109732483 126 FAQFL 130
Cdd:COG4403  143 LAALL 147
LanM-like cd04792
Cyclases involved in the biosynthesis of class II lantibiotics, and similar proteins; ...
 36-120 9.47e-07

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: 47.69  E-value: 9.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109732483  36 ELGETIERENELvHWCHGAPG-IAYLFAkAYLISKKPQYLDTCIRCGE------------LTWQKGLLKKG-PGICHGVA 101
Cdd:cd04792  577 LLTEAIIEDEEL-DIIGGSAGaILVLLA-LYERTGDERALELAIACGDhllknavendggARWKTPASSRPlTGFAHGAA 654

                         90
                 ....*....|....*....
gi 109732483 102 GSAYVFLLLYRLTGNSKYI 120
Cdd:cd04792  655 GIAWALLRLAAVTGDERYL 673
LcnDR2 COG4403
Lantibiotic modifying enzyme [Defense mechanisms];
52-130 1.22e-06

Lantibiotic modifying enzyme [Defense mechanisms];


Pssm-ID: 443528 [Multi-domain]  Cd Length: 405  Bit Score: 47.43  E-value: 1.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109732483  52 HGAPGIAYLFAKAYLISKKPQYLDTCIRCGE------------LTWQKGLLKKGP--GICHGVAGSAYVFLLLYRLTGNS 117
Cdd:COG4403  161 SGAAGAILALLALYRATGDPAALDLAIRCGDrllaaavrddggRAWPTPEPAGRPltGFAHGAAGIAYALLRLAAATGDE 240

                         90
                 ....*....|...
gi 109732483 118 KYIYRAQRFAQFL 130
Cdd:COG4403  241 RYLEAAREALAYE 253
LanC_like cd04434
Cyclases involved in the biosynthesis of lantibiotics, and similar proteins; LanC is the ...
 52-127 3.13e-05

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: 43.26  E-value: 3.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109732483  52 HGAPGIAYLFAKAYLISKKPQYLDTCIRCGEL---TW-QKGLLKKGPGICHGVAGSAYVFLLLYRLTGNSKYIYRAQRFA 127
Cdd:cd04434    2 HGAAGIALFLLELYRATGDKEYLDEAKEGADYllaRLeGLGEPLSGASLYSGLSGLLWALLELYEDLGDEKLLDALLDLL 81
LanM-like cd04792
Cyclases involved in the biosynthesis of class II lantibiotics, and similar proteins; ...
 52-130 4.66e-05

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: 42.69  E-value: 4.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109732483  52 HGAPGIAYLFAKAYLISKKPQYLDTCIRCGELT------WQKGLLKKGPGICHGVAGSAYVFLLLYRLTGNSKYIYRAQR 125
Cdd:cd04792  494 DGLSGIALFLAALAALTGDEKYRDLARKALRPLrkllrdLAADPRSLGIGGFTGLGSILYALSHLARLLGDPELLEDALE 573


                 ....*
gi 109732483 126 FAQFL 130
Cdd:cd04792  574 LADLL 578
LanC_like cd04434
Cyclases involved in the biosynthesis of lantibiotics, and similar proteins; LanC is the ...
 98-163 1.07e-04

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: 41.72  E-value: 1.07e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109732483  98 HGVAGSAYVFLLLYRLTGNSKYIYRAQRFAQFLFTEEFKSGSrvLESIYSLYEGFSGtVCFLIDLL 163
Cdd:cd04434    2 HGAAGIALFLLELYRATGDKEYLDEAKEGADYLLARLEGLGE--PLSGASLYSGLSG-LLWALLEL 64
LANC_like pfam05147
Lanthionine synthetase C-like protein; Lanthionines are thioether bridges that are putatively ...
 52-136 1.15e-04

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: 41.60  E-value: 1.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109732483   52 HGAPGIAYLFAKAYLISKKPQYLDTC---IRCGELTWQKGLLKKGPGIChGVAGSAYVFLLLYRLTGNS----KYIYRAQ 124
Cdd:pfam05147   9 TGLAGIALFLLELYKVTGNEKYLKLAhkyLEKIARALSEKGLPDISFFC-GAAGIAYALAVASKLLGDYqlllNYLDSAL 87

                          90
                  ....*....|..
gi 109732483  125 RFAQFLFTEEFK 136
Cdd:pfam05147  88 ELIESNKLPDEK 99
LanC_SerThrkinase cd04791
Lanthionine synthetase C-like domain associated with serine/threonine kinases; Some members of ...
 53-130 4.46e-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: 39.56  E-value: 4.46e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 109732483  53 GAPGIAYLFAKAYLISKKPQYLDTCIRCGeltwqkgLLKKGPGICHGVAGSAYVFLLLYRLTGNSKYIYRAQRFAQFL 130
Cdd:cd04791   48 GLAGIAWVLYELGRREEAERLLDRALALP-------LDSLDPSLYSGLAGIGLALLHLARATGDPEFLERAARIAERL 118
YesR COG4225
Rhamnogalacturonyl hydrolase YesR [Carbohydrate transport and metabolism];
49-136 1.50e-03

Rhamnogalacturonyl hydrolase YesR [Carbohydrate transport and metabolism];


Pssm-ID: 443369  Cd Length: 336  Bit Score: 38.25  E-value: 1.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109732483  49 HWCHGApgIAYLFAKAYLISKKPQYLDTCIRCGELTWQKGLLKKGPGIC--HGVAGSAYvfLLLYRLTGNSKYIYRAQRF 126
Cdd:COG4225   21 DYTQGV--TLYGLLKLAEATGDKKYLDYIKRWFDFFIDEGNTYKLPPYNldDIAPGLAL--LELYEQTGDPKYLKAADTL 96

                         90
                 ....*....|
gi 109732483 127 AQFLFTEEFK 136
Cdd:COG4225   97 ADWQLNTQPR 106
YyaL COG1331
Uncharacterized conserved protein YyaL, SSP411 family, contains thoiredoxin and six-hairpin ...
 61-135 1.57e-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: 38.29  E-value: 1.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109732483  61 FAKAYLISKKPQYLDTCIRCGELTWQKgLLKKGPGICH----GVAGSA-----YVFLL-----LYRLTGNSKYIYRAQRF 126
Cdd:COG1331  422 LAEAGRVLGDPEYLEAAERAADFILDN-LWDPDGRLLRsyrdGEAGIPgfledYAFLIeallaLYEATGDPRWLERALEL 500


                 ....*....
gi 109732483 127 AQFLFtEEF 135
Cdd:COG1331  501 ADEAL-EHF 508
 
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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