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Conserved domains on  [gi|768033141|ref|XP_011542206|]
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lanC-like protein 3 isoform X1 [Homo sapiens]

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 ...
 7-232 3.52e-114

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: 330.44  E-value: 3.52e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033141   7 DVEVLTPAQIKSICQAILDSGKQYAIKKRKPFPLMYSYYGTEYLGAAHGLSSILQMLLSYHEHL-KPSDRELVWQSVDFL 85
Cdd:cd04794  122 ESLEISDAVIKKLVDAILESGRQGAKDYRSPPPLMYEWHGKEYLGAAHGLAGILYMLLQAPPLLqIPSLAPLIKETLDYL 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033141  86 ME-QEQNCNWPPELGEtIERENELVHWCHGAPGIAYLFAKAYLVSKKPQYLDTCIRCGELTWQKGLLKKGPGICHGVAGS 164
Cdd:cd04794  202 LSlQFPSGNWPSSLGE-RSRSDRLVQWCHGAPGVVYLLAKAYKVFLDPKYLEAAIRAGELVWERGLLRKGPGLCHGIAGN 280

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768033141 165 AYVFLLLYRLTGNSKYIYRAQRFAQFLFTEEFKAGSRVLESIYSLYEGFSGTVCFLIDLLQ-PNQAEFP 232
Cdd:cd04794  281 AYAFLLLYRLTGDEKYLYRALKFAEFALDYGFLTGARTPDRPYSLFEGLAGTACFLADLLQgPRKARFP 349
 
Name Accession Description Interval E-value
euk_LANCL cd04794
Eukaryotic Lanthionine synthetase C-like protein; This family contains the lanthionine ...
 7-232 3.52e-114

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: 330.44  E-value: 3.52e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033141   7 DVEVLTPAQIKSICQAILDSGKQYAIKKRKPFPLMYSYYGTEYLGAAHGLSSILQMLLSYHEHL-KPSDRELVWQSVDFL 85
Cdd:cd04794  122 ESLEISDAVIKKLVDAILESGRQGAKDYRSPPPLMYEWHGKEYLGAAHGLAGILYMLLQAPPLLqIPSLAPLIKETLDYL 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033141  86 ME-QEQNCNWPPELGEtIERENELVHWCHGAPGIAYLFAKAYLVSKKPQYLDTCIRCGELTWQKGLLKKGPGICHGVAGS 164
Cdd:cd04794  202 LSlQFPSGNWPSSLGE-RSRSDRLVQWCHGAPGVVYLLAKAYKVFLDPKYLEAAIRAGELVWERGLLRKGPGLCHGIAGN 280

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768033141 165 AYVFLLLYRLTGNSKYIYRAQRFAQFLFTEEFKAGSRVLESIYSLYEGFSGTVCFLIDLLQ-PNQAEFP 232
Cdd:cd04794  281 AYAFLLLYRLTGDEKYLYRALKFAEFALDYGFLTGARTPDRPYSLFEGLAGTACFLADLLQgPRKARFP 349
LANC_like pfam05147
Lanthionine synthetase C-like protein; Lanthionines are thioether bridges that are putatively ...
 16-232 5.13e-63

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: 200.30  E-value: 5.13e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033141   16 IKSICQAILDSGKQYAiKKRKPFPLMYSYYGTEYLGAAHGLSSILQMLLSYHEHLK-PSDRELVWQSVDFLME--QEQNC 92
Cdd:pfam05147 127 LKLILKYLLRLGIRSE-NQFSWCPLMYEPYGNFNLGFAHGLSGIAYALLALYKGTKsEKLLELIKKALNYEKSlkFKSEG 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033141   93 NWPPELGEtieRENELVHWCHGAPGIAYLFAKAYLVSKKPQYLDTCIRCGELTWQKGLLKKGPGICHGVAGSAYVFLLLY 172
Cdd:pfam05147 206 NWPDSRGD---KNDYLVAWCHGAPGILLALLLAYKALNDEEFLEEAIEALEVVWKRGLLLKNPSLCHGLSGNLYILLLLY 282

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768033141  173 RLTGNSKYIYRAQRFAQFLFTEEFKAGSRVLESI----YSLYEGFSGTVCFLIDLLQPNQAEFP 232
Cdd:pfam05147 283 RLTNDPKYLERAKKFIISLLDYGKKNGFKCGLPRgdesFGLMEGIAGIAYFLLDLLNPDESLFP 346
LcnDR2 COG4403
Lantibiotic modifying enzyme [Defense mechanisms];
49-228 2.46e-19

Lantibiotic modifying enzyme [Defense mechanisms];


Pssm-ID: 443528 [Multi-domain]  Cd Length: 405  Bit Score: 85.56  E-value: 2.46e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033141  49 YLGAAHGLSSILQMLLSYHEHLK-PSDRELVWQSVDFLMEQ--EQNCNWPPeLGETIERENELVHWCHGAPGIAYLFAKA 125
Cdd:COG4403  216 LTGFAHGAAGIAYALLRLAAATGdERYLEAAREALAYERSLfdPEGGNWPD-LREPDDGPRFRTAWCHGAAGIGLARLAL 294

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033141 126 YLVSKKPQYLDTCIRCGELTWQKGLLkKGPGICHGVAGSAYVFLLLYRLTGNSKYIYRAQRFAQFLFTEEFKAGSRVLES 205
Cdd:COG4403  295 LRALGDPELREDLERALETTLRRGFG-RNDSLCHGDAGNLELLLRAARATGDPELLEAARRLAALLLARAERAGPLGLPG 373

                        170       180
                 ....*....|....*....|....*....
gi 768033141 206 I------YSLYEGFSGTVCFLIDLLQPNQ 228
Cdd:COG4403  374 LprgvesPGLMTGLAGIGYGLLRLAAPER 402
lanti_2_LanM TIGR03897
type 2 lantibiotic biosynthesis protein LanM; Members of this family are known generally as ...
 49-192 6.45e-12

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: 64.59  E-value: 6.45e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033141   49 YLGAAHGLSSILQMLLSYHEHLKPSD-RELVWQsvdfLMEQEQNC------NWPpELGETIErENELVHWCHGAPGIayl 121
Cdd:TIGR03897 749 LTGFSHGAAGIAWALLRLYKVTGDQRyLEAAKE----ALAYERSLfdpeegNWP-DLREDGG-PQFPVAWCHGAPGI--- 819

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768033141  122 fAKAYLVSKKPQYLDTC---IRCGELTWQKGLLKKGPGICHGVAGSAYVFLLLYRLTGNSKYIYRAQRFAQFLF 192
Cdd:TIGR03897 820 -LLSRLGLLEILDDDEIredIEIALETTLKYGFGDNDSLCHGDLGNLEILLEAAKVLDDEELQELARRIASQVL 892
 
Name Accession Description Interval E-value
euk_LANCL cd04794
Eukaryotic Lanthionine synthetase C-like protein; This family contains the lanthionine ...
 7-232 3.52e-114

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: 330.44  E-value: 3.52e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033141   7 DVEVLTPAQIKSICQAILDSGKQYAIKKRKPFPLMYSYYGTEYLGAAHGLSSILQMLLSYHEHL-KPSDRELVWQSVDFL 85
Cdd:cd04794  122 ESLEISDAVIKKLVDAILESGRQGAKDYRSPPPLMYEWHGKEYLGAAHGLAGILYMLLQAPPLLqIPSLAPLIKETLDYL 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033141  86 ME-QEQNCNWPPELGEtIERENELVHWCHGAPGIAYLFAKAYLVSKKPQYLDTCIRCGELTWQKGLLKKGPGICHGVAGS 164
Cdd:cd04794  202 LSlQFPSGNWPSSLGE-RSRSDRLVQWCHGAPGVVYLLAKAYKVFLDPKYLEAAIRAGELVWERGLLRKGPGLCHGIAGN 280

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768033141 165 AYVFLLLYRLTGNSKYIYRAQRFAQFLFTEEFKAGSRVLESIYSLYEGFSGTVCFLIDLLQ-PNQAEFP 232
Cdd:cd04794  281 AYAFLLLYRLTGDEKYLYRALKFAEFALDYGFLTGARTPDRPYSLFEGLAGTACFLADLLQgPRKARFP 349
LANC_like pfam05147
Lanthionine synthetase C-like protein; Lanthionines are thioether bridges that are putatively ...
 16-232 5.13e-63

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: 200.30  E-value: 5.13e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033141   16 IKSICQAILDSGKQYAiKKRKPFPLMYSYYGTEYLGAAHGLSSILQMLLSYHEHLK-PSDRELVWQSVDFLME--QEQNC 92
Cdd:pfam05147 127 LKLILKYLLRLGIRSE-NQFSWCPLMYEPYGNFNLGFAHGLSGIAYALLALYKGTKsEKLLELIKKALNYEKSlkFKSEG 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033141   93 NWPPELGEtieRENELVHWCHGAPGIAYLFAKAYLVSKKPQYLDTCIRCGELTWQKGLLKKGPGICHGVAGSAYVFLLLY 172
Cdd:pfam05147 206 NWPDSRGD---KNDYLVAWCHGAPGILLALLLAYKALNDEEFLEEAIEALEVVWKRGLLLKNPSLCHGLSGNLYILLLLY 282

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768033141  173 RLTGNSKYIYRAQRFAQFLFTEEFKAGSRVLESI----YSLYEGFSGTVCFLIDLLQPNQAEFP 232
Cdd:pfam05147 283 RLTNDPKYLERAKKFIISLLDYGKKNGFKCGLPRgdesFGLMEGIAGIAYFLLDLLNPDESLFP 346
LanC_like cd04434
Cyclases involved in the biosynthesis of lantibiotics, and similar proteins; LanC is the ...
 16-233 1.67e-19

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: 85.63  E-value: 1.67e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033141  16 IKSICQAILDSGKQYAIKKRKPFPLMYSYYGteylgAAHGLSSILQMLLSYHEHLKPSDR-ELVWQSVDFLMEQE-QNCN 93
Cdd:cd04434  125 AAKIGDFLLQAAEELDNGGNWGLPKGSIYPG-----FAHGTAGIAYALARLYEETGDEDFlDAAKEGAEYLEAIAvGDED 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033141  94 WPPELGETiERENELVHWCHGAPGIAYLFAKAYLVSKKPQYLD----TCIRCGELTWQKGLLKKGPGICHGVAGSAYVFL 169
Cdd:cd04434  200 GFLIPLPD-EKDLFYLGWCHGPAGTALLFYELYKATGDLDLADelleGIIKTGAPEKLSPGFWNNLCLCHGTAGVLEHLL 278

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768033141 170 LLYRLTGNSKY---------IYRAQRFAQFLFTEEFKAGSRVLESIYSLYEGFSGTVCFLIDLLQPNQAEFPL 233
Cdd:cd04434  279 YVYRLTGDEREyakrladklLGRATRNGEGLRWYQAWTGPGRVDASLGLMVGAAGIASALLKLLRAETKARPL 351
LcnDR2 COG4403
Lantibiotic modifying enzyme [Defense mechanisms];
49-228 2.46e-19

Lantibiotic modifying enzyme [Defense mechanisms];


Pssm-ID: 443528 [Multi-domain]  Cd Length: 405  Bit Score: 85.56  E-value: 2.46e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033141  49 YLGAAHGLSSILQMLLSYHEHLK-PSDRELVWQSVDFLMEQ--EQNCNWPPeLGETIERENELVHWCHGAPGIAYLFAKA 125
Cdd:COG4403  216 LTGFAHGAAGIAYALLRLAAATGdERYLEAAREALAYERSLfdPEGGNWPD-LREPDDGPRFRTAWCHGAAGIGLARLAL 294

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033141 126 YLVSKKPQYLDTCIRCGELTWQKGLLkKGPGICHGVAGSAYVFLLLYRLTGNSKYIYRAQRFAQFLFTEEFKAGSRVLES 205
Cdd:COG4403  295 LRALGDPELREDLERALETTLRRGFG-RNDSLCHGDAGNLELLLRAARATGDPELLEAARRLAALLLARAERAGPLGLPG 373

                        170       180
                 ....*....|....*....|....*....
gi 768033141 206 I------YSLYEGFSGTVCFLIDLLQPNQ 228
Cdd:COG4403  374 LprgvesPGLMTGLAGIGYGLLRLAAPER 402
LanC cd04793
Cyclases involved in the biosynthesis of lantibiotics; LanC is the cyclase enzyme of the ...
 9-227 3.21e-16

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: 76.62  E-value: 3.21e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033141   9 EVLTpaQIKSICQAILDSGKQYAIKKRKPFPLMYSYYGTEY--LGAAHGLSSILQMLLSYHEH--LKPSDRELVWQSVDF 84
Cdd:cd04793  129 EILD--YLVDLTEPIIEGGEKVPWPELQPSESEKKAYPSGHfnLGLAHGIAGPLALLALALRRgiEVPGQREAIERIADW 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033141  85 LMEQEQ--NCNWPPELG--ETIERENELVH-----WCHGAPGIAYLFAKAYLVSKKPQYLDTCIRCGELTWQKGLLKKG- 154
Cdd:cd04793  207 LLKWRQddDEGWWPTIVfpEELSNGRPPPVpsrdaWCYGDPGIARALLLAGKALGDPELQELAEEALLAALRRPDELTGl 286

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033141 155 --PGICHGVAGSAYVFLLLYRLTGNSKYIYRAQRFA----QFLFTEEFKAGSRVLESI-----YSLYEGFSGTVCFLIDL 223
Cdd:cd04793  287 isPTLCHGYAGLLQIARRMYRDTGEPALLAAAEELIdkllDLYDPDLPFGFYDTGGSItplddPGLLEGAAGIALALLSA 366


                 ....
gi 768033141 224 LQPN 227
Cdd:cd04793  367 ITDK 370
lanti_2_LanM TIGR03897
type 2 lantibiotic biosynthesis protein LanM; Members of this family are known generally as ...
 49-192 6.45e-12

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: 64.59  E-value: 6.45e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033141   49 YLGAAHGLSSILQMLLSYHEHLKPSD-RELVWQsvdfLMEQEQNC------NWPpELGETIErENELVHWCHGAPGIayl 121
Cdd:TIGR03897 749 LTGFSHGAAGIAWALLRLYKVTGDQRyLEAAKE----ALAYERSLfdpeegNWP-DLREDGG-PQFPVAWCHGAPGI--- 819

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768033141  122 fAKAYLVSKKPQYLDTC---IRCGELTWQKGLLKKGPGICHGVAGSAYVFLLLYRLTGNSKYIYRAQRFAQFLF 192
Cdd:TIGR03897 820 -LLSRLGLLEILDDDEIredIEIALETTLKYGFGDNDSLCHGDLGNLEILLEAAKVLDDEELQELARRIASQVL 892
LanM-like cd04792
Cyclases involved in the biosynthesis of class II lantibiotics, and similar proteins; ...
 15-228 2.54e-10

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: 60.02  E-value: 2.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033141  15 QIKSICQAILDSGKQYAIKKRKPFPLMYSYYGTEYLGAAHGLSSILQMLLSYHEHLKPSD-RELVWQSVDFlmEQ----E 89
Cdd:cd04792  612 RALELAIACGDHLLKNAVENDGGARWKTPASSRPLTGFAHGAAGIAWALLRLAAVTGDERyLEAAKEALAY--ERslfdP 689

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033141  90 QNCNWPpelGETIERENELVHWCHGAPGIA---YLFAKAYLVSKKPQYLDTCIRCgeltwqkgLLKKGPG----ICHGVA 162
Cdd:cd04792  690 EEGNWP---DRRKRNNSFSAAWCHGAAGIGlarLGLLKILNDDEIEEEIEKALET--------TLKYGFGnndsLCHGDL 758

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768033141 163 GSAYVFLLLYRLTGNSKYIYRAQRFAQFLFtEEFKAGSRVLESI------YSLYEGFSGTVCFLIDLLQPNQ 228
Cdd:cd04792  759 GNLELLLVAAKLLGDPELQEEAEELAAIVL-NRAEEAGGWLCGLptgvesPGLMTGLSGIGYGLLRLAAPDK 829
LanC_SerThrkinase cd04791
Lanthionine synthetase C-like domain associated with serine/threonine kinases; Some members of ...
 14-233 1.44e-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: 54.20  E-value: 1.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033141  14 AQIKSICQAILDSGKQYaikkrkPFPLMYSYYGTEYLGAAHGLSSILQMLLSYHEHLK-PSDRELVWQSVDFLMEQeqnC 92
Cdd:cd04791  109 ERAARIAERLAARLRED------DPGVYWNDAGAVRAGLLHGWSGIALFLLRLYEATGdPAYLDLAERALRKDLAR---C 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033141  93 NWPPELGETIERENE--LVHWCHGAPGIAYLFAKAYLVSKKPQY---LDTCIRC--GELTWQkgllkkgPGICHGVAGSA 165
Cdd:cd04791  180 VEDDDGALLQVDEGNrlLPYLCSGSAGIGLVLLRYLRHRGDDRYrelLEGIARAvrSRFTVQ-------PGLFHGLAGLG 252

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768033141 166 YVFLLLYRLTGNSKYIYRAQRFAQ--FLFTEEFKAGSRVL-ESIY----SLYEGFSGTVCFLIDLLQPNQAEFPL 233
Cdd:cd04791  253 LALLDLAAALGDPRYRAAAERHARllNLHALPRDGGIAFPgDQLLrlstDLATGSAGVLLALLRLLHGGRSWLPL 327
LcnDR2 COG4403
Lantibiotic modifying enzyme [Defense mechanisms];
46-191 8.67e-08

Lantibiotic modifying enzyme [Defense mechanisms];


Pssm-ID: 443528 [Multi-domain]  Cd Length: 405  Bit Score: 52.05  E-value: 8.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033141  46 GTEYLGAAHGLSSILQMLLSYHEHLKpsDRELVWQSVDFLmeqeqncnwppELGETIERENELVHWCHGAPGIAYLFAKA 125
Cdd:COG4403  107 GAMGPGLFTGLGGIAYALAHLGELLG--DPRLLEDALALA-----------ALLEELIAADESLDVISGAAGAILALLAL 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033141 126 YLVSKKPQYLDTCIRCGE------------LTWQKGLLKKGP--GICHGVAGSAYVFLLLYRLTGNSKYIYRAQRFAQFL 191
Cdd:COG4403  174 YRATGDPAALDLAIRCGDrllaaavrddggRAWPTPEPAGRPltGFAHGAAGIAYALLRLAAATGDERYLEAAREALAYE 253
LanC_SerThrkinase cd04791
Lanthionine synthetase C-like domain associated with serine/threonine kinases; Some members of ...
 111-225 1.26e-07

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


Pssm-ID: 271199 [Multi-domain]  Cd Length: 327  Bit Score: 51.50  E-value: 1.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033141 111 WCHGAPGIAYLFAKAYLVSKKPQYLDTCIRCGEL---TWQKGLL--------KKGPGICHGVAGSAYVFLLLYRLTGNSK 179
Cdd:cd04791   84 LYSGLAGIGLALLHLARATGDPEFLERAARIAERlaaRLREDDPgvywndagAVRAGLLHGWSGIALFLLRLYEATGDPA 163

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 768033141 180 YIYRAQRFAQFLFTE----------EFKAGSRVLesiYSLYEGFSGTVCFLIDLLQ 225
Cdd:cd04791  164 YLDLAERALRKDLARcvedddgallQVDEGNRLL---PYLCSGSAGIGLVLLRYLR 216
LanM-like cd04792
Cyclases involved in the biosynthesis of class II lantibiotics, and similar proteins; ...
 50-181 1.61e-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: 51.55  E-value: 1.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033141  50 LGAAHGLSSILQMLLSYHEHLK-PSDRELVWQSVDflmeqeqncnwppELGETIERENELvHWCHGAPG-IAYLFAkAYL 127
Cdd:cd04792  542 IGGFTGLGSILYALSHLARLLGdPELLEDALELAD-------------LLTEAIIEDEEL-DIIGGSAGaILVLLA-LYE 606

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768033141 128 VSKKPQYLDTCIRCGE------------LTWQKGLLKKG-PGICHGVAGSAYVFLLLYRLTGNSKYI 181
Cdd:cd04792  607 RTGDERALELAIACGDhllknavendggARWKTPASSRPlTGFAHGAAGIAWALLRLAAVTGDERYL 673
LanC_like cd04434
Cyclases involved in the biosynthesis of lantibiotics, and similar proteins; LanC is the ...
 114-225 3.38e-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: 50.19  E-value: 3.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033141 114 GAPGIAYLFAKAYLVSKKPQYLDTCIRCGEL---------TWQKGLLKKG---PGICHGVAGSAYVFLLLYRLTGNSKYI 181
Cdd:cd04434  101 GDAGIILYLLYAAEKTGDEKYKELAAKIGDFllqaaeeldNGGNWGLPKGsiyPGFAHGTAGIAYALARLYEETGDEDFL 180

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 768033141 182 YRAQRFAQFLFTEEFKAGSRVL------ESIYSLY--EGFSGTVCFLIDLLQ 225
Cdd:cd04434  181 DAAKEGAEYLEAIAVGDEDGFLiplpdeKDLFYLGwcHGPAGTALLFYELYK 232
LcnDR2 COG4403
Lantibiotic modifying enzyme [Defense mechanisms];
113-191 3.07e-06

Lantibiotic modifying enzyme [Defense mechanisms];


Pssm-ID: 443528 [Multi-domain]  Cd Length: 405  Bit Score: 47.43  E-value: 3.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033141 113 HGAPGIAYLFAKAYLVSKKPQYLDTCIRCgeLTWQKGLLK------KGPGICHGVAGSAYVFLLLYRLTGNSKYIYRAQR 186
Cdd:COG4403   65 DGAAGIALFLAELARLTGDERYRELARAA--LRPLRRLLReelagaMGPGLFTGLGGIAYALAHLGELLGDPRLLEDALA 142


                 ....*
gi 768033141 187 FAQFL 191
Cdd:COG4403  143 LAALL 147
LanC_like cd04434
Cyclases involved in the biosynthesis of lantibiotics, and similar proteins; LanC is the ...
 113-188 7.12e-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: 7.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033141 113 HGAPGIAYLFAKAYLVSKKPQYLDTCIRCGEL---TW-QKGLLKKGPGICHGVAGSAYVFLLLYRLTGNSKYIYRAQRFA 188
Cdd:cd04434    2 HGAAGIALFLLELYRATGDKEYLDEAKEGADYllaRLeGLGEPLSGASLYSGLSGLLWALLELYEDLGDEKLLDALLDLL 81
LanM-like cd04792
Cyclases involved in the biosynthesis of class II lantibiotics, and similar proteins; ...
 113-191 1.44e-04

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: 1.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033141 113 HGAPGIAYLFAKAYLVSKKPQYLDTCIRCGELT------WQKGLLKKGPGICHGVAGSAYVFLLLYRLTGNSKYIYRAQR 186
Cdd:cd04792  494 DGLSGIALFLAALAALTGDEKYRDLARKALRPLrkllrdLAADPRSLGIGGFTGLGSILYALSHLARLLGDPELLEDALE 573


                 ....*
gi 768033141 187 FAQFL 191
Cdd:cd04792  574 LADLL 578
LANC_like pfam05147
Lanthionine synthetase C-like protein; Lanthionines are thioether bridges that are putatively ...
 113-197 1.53e-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: 41.98  E-value: 1.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033141  113 HGAPGIAYLFAKAYLVSKKPQYLDTC---IRCGELTWQKGLLKKGPGIChGVAGSAYVFLLLYRLTGNS----KYIYRAQ 185
Cdd:pfam05147   9 TGLAGIALFLLELYKVTGNEKYLKLAhkyLEKIARALSEKGLPDISFFC-GAAGIAYALAVASKLLGDYqlllNYLDSAL 87

                          90
                  ....*....|..
gi 768033141  186 RFAQFLFTEEFK 197
Cdd:pfam05147  88 ELIESNKLPDEK 99
LanC_like cd04434
Cyclases involved in the biosynthesis of lantibiotics, and similar proteins; LanC is the ...
 159-224 3.58e-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: 40.95  E-value: 3.58e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768033141 159 HGVAGSAYVFLLLYRLTGNSKYIYRAQRFAQFLfTEEFKaGSRVLESIYSLYEGFSGtVCFLIDLL 224
Cdd:cd04434    2 HGAAGIALFLLELYRATGDKEYLDEAKEGADYL-LARLE-GLGEPLSGASLYSGLSG-LLWALLEL 64
YyaL COG1331
Uncharacterized conserved protein YyaL, SSP411 family, contains thoiredoxin and six-hairpin ...
 122-196 1.77e-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: 39.06  E-value: 1.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033141 122 FAKAYLVSKKPQYLDTCIRCGELTWQKgLLKKGPGICH----GVAGSA-----YVFLL-----LYRLTGNSKYIYRAQRF 187
Cdd:COG1331  422 LAEAGRVLGDPEYLEAAERAADFILDN-LWDPDGRLLRsyrdGEAGIPgfledYAFLIeallaLYEATGDPRWLERALEL 500


                 ....*....
gi 768033141 188 AQFLFtEEF 196
Cdd:COG1331  501 ADEAL-EHF 508
LanC_SerThrkinase cd04791
Lanthionine synthetase C-like domain associated with serine/threonine kinases; Some members of ...
 114-191 2.91e-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: 38.02  E-value: 2.91e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768033141 114 GAPGIAYLFAKAYLVSKKPQYLDTCIRCGeltwqkgLLKKGPGICHGVAGSAYVFLLLYRLTGNSKYIYRAQRFAQFL 191
Cdd:cd04791   48 GLAGIAWVLYELGRREEAERLLDRALALP-------LDSLDPSLYSGLAGIGLALLHLARATGDPEFLERAARIAERL 118
YesR COG4225
Rhamnogalacturonyl hydrolase YesR [Carbohydrate transport and metabolism];
110-197 4.34e-03

Rhamnogalacturonyl hydrolase YesR [Carbohydrate transport and metabolism];


Pssm-ID: 443369  Cd Length: 336  Bit Score: 37.48  E-value: 4.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768033141 110 HWCHGApgIAYLFAKAYLVSKKPQYLDTCIRCGELTWQKGLLKKGPGIC--HGVAGSAYvfLLLYRLTGNSKYIYRAQRF 187
Cdd:COG4225   21 DYTQGV--TLYGLLKLAEATGDKKYLDYIKRWFDFFIDEGNTYKLPPYNldDIAPGLAL--LELYEQTGDPKYLKAADTL 96

                         90
                 ....*....|
gi 768033141 188 AQFLFTEEFK 197
Cdd:COG4225   97 ADWQLNTQPR 106
 
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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