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Conserved domains on  [gi|8923911|ref|NP_061167|]
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lanC-like protein 2 [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 ...
103-440 7.68e-158

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: 450.24  E-value: 7.68e-158
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923911  103 YTGWTGIALLYLQLYRVTCD-----QTYLLRSLDYVKRTLRNLNGR---RVTFLCGDAGPLAVGAVIYHKLRSDCESQEC 174
Cdd:cd04794   2 YTGAAGIAYMFLRLSEQGPDlkalsEDYLELALEYIEASLTELARKgssRISFLCGDAGILALAAVIYHALGDSERDEEF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923911  175 VTKLLQLQRSVvCQESDLPDELLYGRAGYLYALLYLNTEIGPGTVC-ESAIKEVVNAIIESGKTLSREERktERCPLLYQ 253
Cdd:cd04794  82 LEQLLELAKEA-LPLDDGPDELLYGRAGYLYALLFLRKHLGESLEIsDAVIKKLVDAILESGRQGAKDYR--SPPPLMYE 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923911  254 WHRKQYVGAAHGMAGIYYMLMQPAAKVDQETLTEMVKPSIDYVRHKKFRSGNYPSSLSNE--TDRLVHWCHGAPGVIHML 331
Cdd:cd04794 159 WHGKEYLGAAHGLAGILYMLLQAPPLLQIPSLAPLIKETLDYLLSLQFPSGNWPSSLGERsrSDRLVQWCHGAPGVVYLL 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923911  332 MQAYKVFKEEKYLKEAMECSDVIWQRGLLRKGYGICHGTAGNGYSFLSLYRLTQDKKYLYRACKFAEWCLDYGAH-GCRI 410
Cdd:cd04794 239 AKAYKVFLDPKYLEAAIRAGELVWERGLLRKGPGLCHGIAGNAYAFLLLYRLTGDEKYLYRALKFAEFALDYGFLtGART 318
                       330       340       350
                ....*....|....*....|....*....|.
gi 8923911  411 PDRPYSLFEGMAGAIHFLSDVL-GPETSRFP 440
Cdd:cd04794 319 PDRPYSLFEGLAGTACFLADLLqGPRKARFP 349
 
Name Accession Description Interval E-value
euk_LANCL cd04794
Eukaryotic Lanthionine synthetase C-like protein; This family contains the lanthionine ...
103-440 7.68e-158

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: 450.24  E-value: 7.68e-158
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923911  103 YTGWTGIALLYLQLYRVTCD-----QTYLLRSLDYVKRTLRNLNGR---RVTFLCGDAGPLAVGAVIYHKLRSDCESQEC 174
Cdd:cd04794   2 YTGAAGIAYMFLRLSEQGPDlkalsEDYLELALEYIEASLTELARKgssRISFLCGDAGILALAAVIYHALGDSERDEEF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923911  175 VTKLLQLQRSVvCQESDLPDELLYGRAGYLYALLYLNTEIGPGTVC-ESAIKEVVNAIIESGKTLSREERktERCPLLYQ 253
Cdd:cd04794  82 LEQLLELAKEA-LPLDDGPDELLYGRAGYLYALLFLRKHLGESLEIsDAVIKKLVDAILESGRQGAKDYR--SPPPLMYE 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923911  254 WHRKQYVGAAHGMAGIYYMLMQPAAKVDQETLTEMVKPSIDYVRHKKFRSGNYPSSLSNE--TDRLVHWCHGAPGVIHML 331
Cdd:cd04794 159 WHGKEYLGAAHGLAGILYMLLQAPPLLQIPSLAPLIKETLDYLLSLQFPSGNWPSSLGERsrSDRLVQWCHGAPGVVYLL 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923911  332 MQAYKVFKEEKYLKEAMECSDVIWQRGLLRKGYGICHGTAGNGYSFLSLYRLTQDKKYLYRACKFAEWCLDYGAH-GCRI 410
Cdd:cd04794 239 AKAYKVFLDPKYLEAAIRAGELVWERGLLRKGPGLCHGIAGNAYAFLLLYRLTGDEKYLYRALKFAEFALDYGFLtGART 318
                       330       340       350
                ....*....|....*....|....*....|.
gi 8923911  411 PDRPYSLFEGMAGAIHFLSDVL-GPETSRFP 440
Cdd:cd04794 319 PDRPYSLFEGLAGTACFLADLLqGPRKARFP 349
LANC_like pfam05147
Lanthionine synthetase C-like protein; Lanthionines are thioether bridges that are putatively ...
96-444 5.65e-124

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: 364.01  E-value: 5.65e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923911     96 DPHDCSAYTGWTGIALLYLQLYRVTCDQTYLLRSLDYVKRTLRNLNG---RRVTFLCGDAGPLAVGAVIYHKLRSDCESQ 172
Cdd:pfam05147   1 SPLDDSLYTGLAGIALFLLELYKVTGNEKYLKLAHKYLEKIARALSEkglPDISFFCGAAGIAYALAVASKLLGDYQLLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923911    173 ECVTKLLQLQRSVVcqESDLPDELLYGRAGYLYALLYLNTEIGPGtvcESAIKEVVNAIIESGktlSREERKTERCPLLY 252
Cdd:pfam05147  81 NYLDSALELIESNK--LPDEKYDLISGRAGILSYLLLLNEEFGIE---EDYLKLILKYLLRLG---IRSENQFSWCPLMY 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923911    253 QWHRKQYVGAAHGMAGIYYMLMQPAAKVDQETLTEMVKPSIDYVRHKKFR-SGNYPSSLSNETDRLVHWCHGAPGVIHML 331
Cdd:pfam05147 153 EPYGNFNLGFAHGLSGIAYALLALYKGTKSEKLLELIKKALNYEKSLKFKsEGNWPDSRGDKNDYLVAWCHGAPGILLAL 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923911    332 MQAYKVFKEEKYLKEAMECSDVIWQRGLLRKGYGICHGTAGNGYSFLSLYRLTQDKKYLYRACKFAEWCLDYGAHGCRI- 410
Cdd:pfam05147 233 LLAYKALNDEEFLEEAIEALEVVWKRGLLLKNPSLCHGLSGNLYILLLLYRLTNDPKYLERAKKFIISLLDYGKKNGFKc 312
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 8923911    411 ----PDRPYSLFEGMAGAIHFLSDVLGPETSRFPAFEL 444
Cdd:pfam05147 313 glprGDESFGLMEGIAGIAYFLLDLLNPDESLFPSALL 350
LcnDR2 COG4403
Lantibiotic modifying enzyme [Defense mechanisms];
103-440 1.42e-33

Lantibiotic modifying enzyme [Defense mechanisms];


Pssm-ID: 443528 [Multi-domain]  Cd Length: 405  Bit Score: 130.24  E-value: 1.42e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923911  103 YTGWTGIALLYLQLYRVTCDQTYL---LRSLDYVKRTLRNLNGRR--VTFLCGDAGpLAVGAVIYHKLRSDcesQECVTK 177
Cdd:COG4403  64 YDGAAGIALFLAELARLTGDERYRelaRAALRPLRRLLREELAGAmgPGLFTGLGG-IAYALAHLGELLGD---PRLLED 139
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923911  178 LLQL-QRSVVCQESDLPDELLYGRAGYLYALLYLNTEIGPGTVCESAIkEVVNAIIEsgktlSREERKTERCPLLYQWHR 256
Cdd:COG4403 140 ALALaALLEELIAADESLDVISGAAGAILALLALYRATGDPAALDLAI-RCGDRLLA-----AAVRDDGGRAWPTPEPAG 213
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923911  257 KQYVGAAHGMAGIYYMLMQPAAKVDQETLTEMVKPSIDYVR-HKKFRSGNYP--SSLSNETDRLVHWCHGAPGVIHMLMQ 333
Cdd:COG4403 214 RPLTGFAHGAAGIAYALLRLAAATGDERYLEAAREALAYERsLFDPEGGNWPdlREPDDGPRFRTAWCHGAAGIGLARLA 293
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923911  334 AYKVFKEEKYLKEAMECSDVIWQRGLLRkGYGICHGTAGNGYSFLSLYRLTQDKKYLYRACKFAEWCLDYG--AHGCRIP 411
Cdd:COG4403 294 LLRALGDPELREDLERALETTLRRGFGR-NDSLCHGDAGNLELLLRAARATGDPELLEAARRLAALLLARAerAGPLGLP 372
                       330       340       350
                ....*....|....*....|....*....|....
gi 8923911  412 DRP-----YSLFEGMAGAIHFLSDVLGPEtsRFP 440
Cdd:COG4403 373 GLPrgvesPGLMTGLAGIGYGLLRLAAPE--RLP 404
lanti_2_LanM TIGR03897
type 2 lantibiotic biosynthesis protein LanM; Members of this family are known generally as ...
97-423 7.97e-21

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


Pssm-ID: 274840 [Multi-domain]  Cd Length: 931  Bit Score: 95.79  E-value: 7.97e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923911     97 PHDCSAYTGWTGIALLYLQLYRVTCDQTYL------LRSL-DYVKRTLRNLNGRRVTFLCGDAGPLAVGAVIYhKLRSDC 169
Cdd:TIGR03897 589 PLGNDLYDGLAGIALFLAYLAALTGDKRYRdlarkaLQPLrKYLETLVELARSMGLGAFSGLGSIIYALAHLG-QLLNDP 667
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923911    170 ESQECVTKLLQLQRSVVCQESDLPDeLLYGRAGYLYAL--LYLNTEIgpgtvcesaiKEVVNAIIESGKTLSREERKTER 247
Cdd:TIGR03897 668 ELLNDAKKILNRLEELIIKDEEFLD-LIGGAAGAILVLlnLYEVTGD----------PEVLELAIACGEHLLKQAVEQEG 736
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923911    248 cplLYQWHRKQ----YVGAAHGMAGIYYMLMQPAAKVDQETLTEMVKPSIDYVRHkKFRS--GNYPSSLSNETDRL-VHW 320
Cdd:TIGR03897 737 ---GAAWKTSQsnkpLTGFSHGAAGIAWALLRLYKVTGDQRYLEAAKEALAYERS-LFDPeeGNWPDLREDGGPQFpVAW 812
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923911    321 CHGAPGVI---HMLMQAYKVFKEEKYLKEAMEcsdviwqrGLLRKGYG----ICHGTAGNGYSFLSLYRLTQDKKYLYRA 393
Cdd:TIGR03897 813 CHGAPGILlsrLGLLEILDDDEIREDIEIALE--------TTLKYGFGdndsLCHGDLGNLEILLEAAKVLDDEELQELA 884
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 8923911    394 CKFAEWCLD----YGAHGCRIPDRPYS--LFEGMAG 423
Cdd:TIGR03897 885 RRIASQVLArltkNGRYRLGLPRGVESpgLMTGLAG 920
 
Name Accession Description Interval E-value
euk_LANCL cd04794
Eukaryotic Lanthionine synthetase C-like protein; This family contains the lanthionine ...
103-440 7.68e-158

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: 450.24  E-value: 7.68e-158
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923911  103 YTGWTGIALLYLQLYRVTCD-----QTYLLRSLDYVKRTLRNLNGR---RVTFLCGDAGPLAVGAVIYHKLRSDCESQEC 174
Cdd:cd04794   2 YTGAAGIAYMFLRLSEQGPDlkalsEDYLELALEYIEASLTELARKgssRISFLCGDAGILALAAVIYHALGDSERDEEF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923911  175 VTKLLQLQRSVvCQESDLPDELLYGRAGYLYALLYLNTEIGPGTVC-ESAIKEVVNAIIESGKTLSREERktERCPLLYQ 253
Cdd:cd04794  82 LEQLLELAKEA-LPLDDGPDELLYGRAGYLYALLFLRKHLGESLEIsDAVIKKLVDAILESGRQGAKDYR--SPPPLMYE 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923911  254 WHRKQYVGAAHGMAGIYYMLMQPAAKVDQETLTEMVKPSIDYVRHKKFRSGNYPSSLSNE--TDRLVHWCHGAPGVIHML 331
Cdd:cd04794 159 WHGKEYLGAAHGLAGILYMLLQAPPLLQIPSLAPLIKETLDYLLSLQFPSGNWPSSLGERsrSDRLVQWCHGAPGVVYLL 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923911  332 MQAYKVFKEEKYLKEAMECSDVIWQRGLLRKGYGICHGTAGNGYSFLSLYRLTQDKKYLYRACKFAEWCLDYGAH-GCRI 410
Cdd:cd04794 239 AKAYKVFLDPKYLEAAIRAGELVWERGLLRKGPGLCHGIAGNAYAFLLLYRLTGDEKYLYRALKFAEFALDYGFLtGART 318
                       330       340       350
                ....*....|....*....|....*....|.
gi 8923911  411 PDRPYSLFEGMAGAIHFLSDVL-GPETSRFP 440
Cdd:cd04794 319 PDRPYSLFEGLAGTACFLADLLqGPRKARFP 349
LANC_like pfam05147
Lanthionine synthetase C-like protein; Lanthionines are thioether bridges that are putatively ...
96-444 5.65e-124

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: 364.01  E-value: 5.65e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923911     96 DPHDCSAYTGWTGIALLYLQLYRVTCDQTYLLRSLDYVKRTLRNLNG---RRVTFLCGDAGPLAVGAVIYHKLRSDCESQ 172
Cdd:pfam05147   1 SPLDDSLYTGLAGIALFLLELYKVTGNEKYLKLAHKYLEKIARALSEkglPDISFFCGAAGIAYALAVASKLLGDYQLLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923911    173 ECVTKLLQLQRSVVcqESDLPDELLYGRAGYLYALLYLNTEIGPGtvcESAIKEVVNAIIESGktlSREERKTERCPLLY 252
Cdd:pfam05147  81 NYLDSALELIESNK--LPDEKYDLISGRAGILSYLLLLNEEFGIE---EDYLKLILKYLLRLG---IRSENQFSWCPLMY 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923911    253 QWHRKQYVGAAHGMAGIYYMLMQPAAKVDQETLTEMVKPSIDYVRHKKFR-SGNYPSSLSNETDRLVHWCHGAPGVIHML 331
Cdd:pfam05147 153 EPYGNFNLGFAHGLSGIAYALLALYKGTKSEKLLELIKKALNYEKSLKFKsEGNWPDSRGDKNDYLVAWCHGAPGILLAL 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923911    332 MQAYKVFKEEKYLKEAMECSDVIWQRGLLRKGYGICHGTAGNGYSFLSLYRLTQDKKYLYRACKFAEWCLDYGAHGCRI- 410
Cdd:pfam05147 233 LLAYKALNDEEFLEEAIEALEVVWKRGLLLKNPSLCHGLSGNLYILLLLYRLTNDPKYLERAKKFIISLLDYGKKNGFKc 312
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 8923911    411 ----PDRPYSLFEGMAGAIHFLSDVLGPETSRFPAFEL 444
Cdd:pfam05147 313 glprGDESFGLMEGIAGIAYFLLDLLNPDESLFPSALL 350
LanC_like cd04434
Cyclases involved in the biosynthesis of lantibiotics, and similar proteins; LanC is the ...
103-441 3.57e-54

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: 184.24  E-value: 3.57e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923911  103 YTGWTGIALLYLQLYRVTCDQTYLLRSLDYVKRTLRNLNGR-----RVTFLCGDAGPLAVGAVIYHKLRSDCESQECVTK 177
Cdd:cd04434   1 YHGAAGIALFLLELYRATGDKEYLDEAKEGADYLLARLEGLgeplsGASLYSGLSGLLWALLELYEDLGDEKLLDALLDL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923911  178 LLQLQRSVVcQESDLPDELLYGRAGYLYALLYLNTEIGPGTVCESAIKeVVNAIIESGKTLSREERKtercpllYQWHRK 257
Cdd:cd04434  81 LDDIALEAK-EVWWSGNDLILGDAGIILYLLYAAEKTGDEKYKELAAK-IGDFLLQAAEELDNGGNW-------GLPKGS 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923911  258 QYVGAAHGMAGIYYMLMQPAAKVDQETLTEMVKPSIDYVRHKKFRSGNYPSSLS--NETDRLVHWCHGAPGVIHMLMQAY 335
Cdd:cd04434 152 IYPGFAHGTAGIAYALARLYEETGDEDFLDAAKEGAEYLEAIAVGDEDGFLIPLpdEKDLFYLGWCHGPAGTALLFYELY 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923911  336 KVFKE-EKYLKEAMECSDVIWQRGLLR---KGYGICHGTAGNGYSFLSLYRLTQDK----KYLYRACKFAEWCLDYGAHG 407
Cdd:cd04434 232 KATGDlDLADELLEGIIKTGAPEKLSPgfwNNLCLCHGTAGVLEHLLYVYRLTGDEreyaKRLADKLLGRATRNGEGLRW 311
                       330       340       350       360
                ....*....|....*....|....*....|....*....|
gi 8923911  408 CRIP------DRPYSLFEGMAGAIHFLSDVLGPETSRFPA 441
Cdd:cd04434 312 YQAWtgpgrvDASLGLMVGAAGIASALLKLLRAETKARPL 351
LcnDR2 COG4403
Lantibiotic modifying enzyme [Defense mechanisms];
103-440 1.42e-33

Lantibiotic modifying enzyme [Defense mechanisms];


Pssm-ID: 443528 [Multi-domain]  Cd Length: 405  Bit Score: 130.24  E-value: 1.42e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923911  103 YTGWTGIALLYLQLYRVTCDQTYL---LRSLDYVKRTLRNLNGRR--VTFLCGDAGpLAVGAVIYHKLRSDcesQECVTK 177
Cdd:COG4403  64 YDGAAGIALFLAELARLTGDERYRelaRAALRPLRRLLREELAGAmgPGLFTGLGG-IAYALAHLGELLGD---PRLLED 139
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923911  178 LLQL-QRSVVCQESDLPDELLYGRAGYLYALLYLNTEIGPGTVCESAIkEVVNAIIEsgktlSREERKTERCPLLYQWHR 256
Cdd:COG4403 140 ALALaALLEELIAADESLDVISGAAGAILALLALYRATGDPAALDLAI-RCGDRLLA-----AAVRDDGGRAWPTPEPAG 213
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923911  257 KQYVGAAHGMAGIYYMLMQPAAKVDQETLTEMVKPSIDYVR-HKKFRSGNYP--SSLSNETDRLVHWCHGAPGVIHMLMQ 333
Cdd:COG4403 214 RPLTGFAHGAAGIAYALLRLAAATGDERYLEAAREALAYERsLFDPEGGNWPdlREPDDGPRFRTAWCHGAAGIGLARLA 293
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923911  334 AYKVFKEEKYLKEAMECSDVIWQRGLLRkGYGICHGTAGNGYSFLSLYRLTQDKKYLYRACKFAEWCLDYG--AHGCRIP 411
Cdd:COG4403 294 LLRALGDPELREDLERALETTLRRGFGR-NDSLCHGDAGNLELLLRAARATGDPELLEAARRLAALLLARAerAGPLGLP 372
                       330       340       350
                ....*....|....*....|....*....|....
gi 8923911  412 DRP-----YSLFEGMAGAIHFLSDVLGPEtsRFP 440
Cdd:COG4403 373 GLPrgvesPGLMTGLAGIGYGLLRLAAPE--RLP 404
LanM-like cd04792
Cyclases involved in the biosynthesis of class II lantibiotics, and similar proteins; ...
66-423 2.23e-26

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: 112.41  E-value: 2.23e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923911   66 DGKIIHNFIR-----RIQTKI-----KDLLQQME---------EGLKTADPH-------DCSAYTGWTGIALLYLQLYRV 119
Cdd:cd04792 430 DGRVIPDFFEksgldRVIERLrnlseEDLERQLWliraslanwIGLDLSDDGewelsplGADLYDGLSGIALFLAALAAL 509
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923911  120 TCDQTYL---LRSLDYVKRTLRNLNGRRVTFLCGdaGPLAVGAVIY-----HKLRSDCESQECVTKLLQLQRSVVCQESD 191
Cdd:cd04792 510 TGDEKYRdlaRKALRPLRKLLRDLAADPRSLGIG--GFTGLGSILYalshlARLLGDPELLEDALELADLLTEAIIEDEE 587
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923911  192 LpdELLYGRAGYLYALLYLNTEIGPGTVCESAIKeVVNAIIesgKTLSREERKTERCPllyQWHRKQYVGAAHGMAGIYY 271
Cdd:cd04792 588 L--DIIGGSAGAILVLLALYERTGDERALELAIA-CGDHLL---KNAVENDGGARWKT---PASSRPLTGFAHGAAGIAW 658
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923911  272 MLMQPAAKVDQETLTEMVKPSIDYVRHKKFRS-GNYPSSLSNETDRLVHWCHGAPGVI--HMLMqaYKVFKEEKYLKEAM 348
Cdd:cd04792 659 ALLRLAAVTGDERYLEAAKEALAYERSLFDPEeGNWPDRRKRNNSFSAAWCHGAAGIGlaRLGL--LKILNDDEIEEEIE 736
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923911  349 ECSDVIwQRGLLRKGYGICHGTAGNGYSFLSLYRLTQDKKYLYRACKFAEWCLDYG--AHGCR----IPDRPYSLFEGMA 422
Cdd:cd04792 737 KALETT-LKYGFGNNDSLCHGDLGNLELLLVAAKLLGDPELQEEAEELAAIVLNRAeeAGGWLcglpTGVESPGLMTGLS 815

                .
gi 8923911  423 G 423
Cdd:cd04792 816 G 816
lanti_2_LanM TIGR03897
type 2 lantibiotic biosynthesis protein LanM; Members of this family are known generally as ...
97-423 7.97e-21

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


Pssm-ID: 274840 [Multi-domain]  Cd Length: 931  Bit Score: 95.79  E-value: 7.97e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923911     97 PHDCSAYTGWTGIALLYLQLYRVTCDQTYL------LRSL-DYVKRTLRNLNGRRVTFLCGDAGPLAVGAVIYhKLRSDC 169
Cdd:TIGR03897 589 PLGNDLYDGLAGIALFLAYLAALTGDKRYRdlarkaLQPLrKYLETLVELARSMGLGAFSGLGSIIYALAHLG-QLLNDP 667
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923911    170 ESQECVTKLLQLQRSVVCQESDLPDeLLYGRAGYLYAL--LYLNTEIgpgtvcesaiKEVVNAIIESGKTLSREERKTER 247
Cdd:TIGR03897 668 ELLNDAKKILNRLEELIIKDEEFLD-LIGGAAGAILVLlnLYEVTGD----------PEVLELAIACGEHLLKQAVEQEG 736
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923911    248 cplLYQWHRKQ----YVGAAHGMAGIYYMLMQPAAKVDQETLTEMVKPSIDYVRHkKFRS--GNYPSSLSNETDRL-VHW 320
Cdd:TIGR03897 737 ---GAAWKTSQsnkpLTGFSHGAAGIAWALLRLYKVTGDQRYLEAAKEALAYERS-LFDPeeGNWPDLREDGGPQFpVAW 812
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923911    321 CHGAPGVI---HMLMQAYKVFKEEKYLKEAMEcsdviwqrGLLRKGYG----ICHGTAGNGYSFLSLYRLTQDKKYLYRA 393
Cdd:TIGR03897 813 CHGAPGILlsrLGLLEILDDDEIREDIEIALE--------TTLKYGFGdndsLCHGDLGNLEILLEAAKVLDDEELQELA 884
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 8923911    394 CKFAEWCLD----YGAHGCRIPDRPYS--LFEGMAG 423
Cdd:TIGR03897 885 RRIASQVLArltkNGRYRLGLPRGVESpgLMTGLAG 920
LanC cd04793
Cyclases involved in the biosynthesis of lantibiotics; LanC is the cyclase enzyme of the ...
104-438 2.55e-17

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


Pssm-ID: 271201  Cd Length: 377  Bit Score: 83.17  E-value: 2.55e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923911  104 TGWTGIALLYLQLYRVTCDQTYLLRSLDYVKRTLRNLNGRRVTF-LCGdaGPLAVGAVIYHKLRSDCESQECVTKLLQLQ 182
Cdd:cd04793   4 SGLPGIALLLSELARLTPDEGWDEKAHQYLEAAIEELNSAGLSLsLFS--GLAGLAFALLALSRNGGRYQNLLSELNEYI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923911  183 RSVVCQESDLPD----------ELLYGRAGYL-YALLYLnteigpgTVCESAIKEVVNAIIEsgKTLSREERKTERCPLL 251
Cdd:cd04793  82 DELAEDRLAEAIaregispgeyDVISGLSGIGrYLLERP-------PPADDLLEEILDYLVD--LTEPIIEGGEKVPWPE 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923911  252 YQWHRKQYV---------GAAHGMAGIYYMLMQPAAK-VDQETLTEMVKPSIDYVRHKKF--RSGNYPSSLS-NETDRLV 318
Cdd:cd04793 153 LQPSESEKKaypsghfnlGLAHGIAGPLALLALALRRgIEVPGQREAIERIADWLLKWRQddDEGWWPTIVFpEELSNGR 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923911  319 H--------WCHGAPGVIHMLMQAYKVFKEEKYLKEAMECSDVIWQRGLLRKG---YGICHGTAGNGYSFLSLYRLTQDK 387
Cdd:cd04793 233 PppvpsrdaWCYGDPGIARALLLAGKALGDPELQELAEEALLAALRRPDELTGlisPTLCHGYAGLLQIARRMYRDTGEP 312
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 8923911  388 KYLYRACKFAEWCLDYGAHGCR----------IPDRPYSLFEGMAGAIHFLSDVLGPETSR 438
Cdd:cd04793 313 ALLAAAEELIDKLLDLYDPDLPfgfydtggsiTPLDDPGLLEGAAGIALALLSAITDKEPD 373
LanC_SerThrkinase cd04791
Lanthionine synthetase C-like domain associated with serine/threonine kinases; Some members of ...
98-440 6.64e-13

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: 69.22  E-value: 6.64e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923911   98 HDCSAYTGWTGIALLYLQLYRVTCDqtyllRSLDYVKRTLRNLNGRRVTFLCGDAGplaVGAVIYHK-LRSDCEsqecvt 176
Cdd:cd04791   1 GGLNVAYGAAGVLLALHRAGGAVPE-----ELEDWLVRRALRDLSLPPGLYDGLAG---IAWVLYELgRREEAE------ 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923911  177 KLLQLqrsvvCQESDLPDE---LLYGRAGYLYALLYLNTEIGPGTVcESAIKEVVNAIIESGKTLSReerktercPLLYQ 253
Cdd:cd04791  67 RLLDR-----ALALPLDSLdpsLYSGLAGIGLALLHLARATGDPEF-LERAARIAERLAARLREDDP--------GVYWN 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923911  254 WHRKQYVGAAHGMAGIYYMLMQpAAKV--DQETLTEMVKpSIDY-VRHKKFRSGNYPSSLSNETDRLVHWCHGAPGVIHM 330
Cdd:cd04791 133 DAGAVRAGLLHGWSGIALFLLR-LYEAtgDPAYLDLAER-ALRKdLARCVEDDDGALLQVDEGNRLLPYLCSGSAGIGLV 210
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923911  331 LMQAYKVFKEEKYLKEAMECSdviwqRGLLRKGY---GICHGTAGNGYSFLSLYRLTQDKKYLYRACKFAEwCLdyGAHG 407
Cdd:cd04791 211 LLRYLRHRGDDRYRELLEGIA-----RAVRSRFTvqpGLFHGLAGLGLALLDLAAALGDPRYRAAAERHAR-LL--NLHA 282
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
gi 8923911  408 CRIPDRPY-----------SLFEGMAGAIHFLSDVLGPETSRFP 440
Cdd:cd04791 283 LPRDGGIAfpgdqllrlstDLATGSAGVLLALLRLLHGGRSWLP 326
LanC_SerThrkinase cd04791
Lanthionine synthetase C-like domain associated with serine/threonine kinases; Some members of ...
75-231 9.42e-06

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: 47.27  E-value: 9.42e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923911   75 RRIQTKIKDLLQQMEEGLKTADPHDCSAY-------------TGWTGIALLYLQLYRVTCDQTYL---LRSLDY-VKRTL 137
Cdd:cd04791 101 ATGDPEFLERAARIAERLAARLREDDPGVywndagavragllHGWSGIALFLLRLYEATGDPAYLdlaERALRKdLARCV 180
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923911  138 RNLNG---------RRVTFLC-GDAGplaVGAVI--YHKLRSDcesQECVTKLLQLQRSVVCQESDLPDeLLYGRAGYLY 205
Cdd:cd04791 181 EDDDGallqvdegnRLLPYLCsGSAG---IGLVLlrYLRHRGD---DRYRELLEGIARAVRSRFTVQPG-LFHGLAGLGL 253
                       170       180
                ....*....|....*....|....*.
gi 8923911  206 ALLYLNtEIGPGTVCESAIKEVVNAI 231
Cdd:cd04791 254 ALLDLA-AALGDPRYRAAAERHARLL 278
YyaL COG1331
Uncharacterized conserved protein YyaL, SSP411 family, contains thoiredoxin and six-hairpin ...
328-402 2.98e-05

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: 46.38  E-value: 2.98e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923911  328 IHMLMQAYKVFKEEKYLKEAMECSDVIWQRgLLRKGYGICH----GTAG-NGYS---------FLSLYRLTQDKKYLYRA 393
Cdd:COG1331 419 IAALAEAGRVLGDPEYLEAAERAADFILDN-LWDPDGRLLRsyrdGEAGiPGFLedyaflieaLLALYEATGDPRWLERA 497

                ....*....
gi 8923911  394 CKFAEWCLD 402
Cdd:COG1331 498 LELADEALE 506
 
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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