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Conserved domains on  [gi|1126222082|ref|XP_019645296|]
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PREDICTED: histone-lysine N-methyltransferase, H3 lysine-79 specific-like, partial [Branchiostoma belcheri]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AdoMet_MTases super family cl17173
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 118-320 1.18e-91

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


The actual alignment was detected with superfamily member pfam08123:

Pssm-ID: 473071  Cd Length: 205  Bit Score: 295.37  E-value: 1.18e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126222082  118 YNHSID-NPDKLNNYEPFSPEVYGETSFDLIAQMTDEITITEDDTFMDLGSGVGQVVLQVAASTPCRFCYGVEKSDVPAI 196
Cdd:pfam08123    1 YSRSVSpDANKLNHYKAFSNEVYGELLPEFLSDVLDKCNLGPQDVFVDLGSGVGNCVLQAALEFGCKLSFGCEIMDNASN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126222082  197 YSQRMDVNFKKWMKWYGKTYGEYKLEKGDFLTPTFKDKI-ANTSIVFVNNFAFGPAVDHQLKERFANMKEGAKVVSSKAF 275
Cdd:pfam08123   81 LAELQDEEFKKRCKLFGKKLGKIEFIRGSFLDNERVEEIiPEADVILVNNFAFDPELNLQLKEMLQDLKDGCKIISLKSF 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1126222082  276 CPLNFRITDRNLNDIGTIMRVSELSPLRGSVSWTGKPVSYYLHVI 320
Cdd:pfam08123  161 VPLNYRINFRNLSDIFNILKVEELKLPEGSVSWTSRGVEYYISTV 205
CC_DOT1L cd20902
coiled coil domain of disruptor of telomeric-silencing 1-like (DOT1L) and similar proteins; ...
 555-619 3.44e-21

coiled coil domain of disruptor of telomeric-silencing 1-like (DOT1L) and similar proteins; This family contains DOT1L (disruptor of telomeric-silencing 1-like), a non-SET domain histone lysine methyltransferase (HKMT) that catalyzes monomethylation, dimethylation, and trimethylation of nucleosomal H3K79. DOT1L is recruited to the homeobox A by AF10 (ALL1-Fused gene from chromosome 10 protein), one of the mixed-lineage leukemia 1 (MLL1)-fusion partners that function in acute myeloid leukemia (ALL). Aberration of the MLL gene is implicated in acute leukemia; chromosomal translocations of MLL1 generate oncogenic chimeric proteins, containing the non-catalytic N-terminal portion of MLL1 fused with many partners such as AF10. The aberrant recruitment of DOT1L by MLL fusions and the resulting H3K79 methylation are thought to affect gene expression by altering chromatin accessibility. AF10 and DOT1L interact through their coiled coil domains.


:

Pssm-ID: 411016 [Multi-domain]  Cd Length: 65  Bit Score: 88.52  E-value: 3.44e-21
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1126222082  555 ALQRLLETFKMQYLQFLAYMRTPDYKQQLQQEIQQEKARQEQLTAKAGQLSQQIEQLLGEGKKLL 619
Cdd:cd20902      1 ALQKLLESFKIQYLQFLAYMKTPQYKASLQQQIEQEKEKNKQLTGKAQQLEKQIQALQKEGVRLL 65
SH3_and_anchor super family cl25512
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved ...
 591-667 4.34e-05

SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved SH3 domain, a variable region, and then a C-terminal hydrophobic transmembrane alpha helix region.


The actual alignment was detected with superfamily member TIGR04211:

Pssm-ID: 275056 [Multi-domain]  Cd Length: 198  Bit Score: 46.15  E-value: 4.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126222082  591 KARQEQLTAKAGQLSQQIEQLLGEGKKL------LSTRLQELGiKSAADILTLSQkevvRNRELHQKAQQLQQDIDKLEA 664
Cdd:TIGR04211   79 QEELAELQEQLAELRQENQELKQQLSTLeaeleeLQKELERIK-QISANAIELDE----ENRELREELAELKQENEALEA 153


                   ...
gi 1126222082  665 DNN 667
Cdd:TIGR04211  154 ENE 156
EnvC super family cl34844
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 591-765 1.26e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


The actual alignment was detected with superfamily member COG4942:

Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.21  E-value: 1.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126222082  591 KARQEQLTAKAGQLSQQIEQLLGEGKKLLSTrLQELGIKSAADILTLSQ--KEVVRNRELHQK-AQQLQQDIDKLEADnn 667
Cdd:COG4942     82 EAELAELEKEIAELRAELEAQKEELAELLRA-LYRLGRQPPLALLLSPEdfLDAVRRLQYLKYlAPARREQAEELRAD-- 158

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126222082  668 kkdpngvtREAVMQEIMAAMAERKRLKKLTNQLETEVATLQKGGSEKDSAEHA-----GKGQEETADGEQDIKRLTNDVS 742
Cdd:COG4942    159 --------LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARlekelAELAAELAELQQEAEELEALIA 230

                          170       180
                   ....*....|....*....|....*...
gi 1126222082  743 -----TTASVAMATSKPTSPMTGGLESP 765
Cdd:COG4942    231 rleaeAAAAAERTPAAGFAALKGKLPWP 258
 
Name Accession Description Interval E-value
DOT1 pfam08123
Histone methylation protein DOT1; The DOT1 domain regulates gene expression by methylating ...
 118-320 1.18e-91

Histone methylation protein DOT1; The DOT1 domain regulates gene expression by methylating histone H3. H3 methylation by DOT1 has been shown to be required for the DNA damage checkpoint in yeast.


Pssm-ID: 149273  Cd Length: 205  Bit Score: 295.37  E-value: 1.18e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126222082  118 YNHSID-NPDKLNNYEPFSPEVYGETSFDLIAQMTDEITITEDDTFMDLGSGVGQVVLQVAASTPCRFCYGVEKSDVPAI 196
Cdd:pfam08123    1 YSRSVSpDANKLNHYKAFSNEVYGELLPEFLSDVLDKCNLGPQDVFVDLGSGVGNCVLQAALEFGCKLSFGCEIMDNASN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126222082  197 YSQRMDVNFKKWMKWYGKTYGEYKLEKGDFLTPTFKDKI-ANTSIVFVNNFAFGPAVDHQLKERFANMKEGAKVVSSKAF 275
Cdd:pfam08123   81 LAELQDEEFKKRCKLFGKKLGKIEFIRGSFLDNERVEEIiPEADVILVNNFAFDPELNLQLKEMLQDLKDGCKIISLKSF 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1126222082  276 CPLNFRITDRNLNDIGTIMRVSELSPLRGSVSWTGKPVSYYLHVI 320
Cdd:pfam08123  161 VPLNYRINFRNLSDIFNILKVEELKLPEGSVSWTSRGVEYYISTV 205
CC_DOT1L cd20902
coiled coil domain of disruptor of telomeric-silencing 1-like (DOT1L) and similar proteins; ...
 555-619 3.44e-21

coiled coil domain of disruptor of telomeric-silencing 1-like (DOT1L) and similar proteins; This family contains DOT1L (disruptor of telomeric-silencing 1-like), a non-SET domain histone lysine methyltransferase (HKMT) that catalyzes monomethylation, dimethylation, and trimethylation of nucleosomal H3K79. DOT1L is recruited to the homeobox A by AF10 (ALL1-Fused gene from chromosome 10 protein), one of the mixed-lineage leukemia 1 (MLL1)-fusion partners that function in acute myeloid leukemia (ALL). Aberration of the MLL gene is implicated in acute leukemia; chromosomal translocations of MLL1 generate oncogenic chimeric proteins, containing the non-catalytic N-terminal portion of MLL1 fused with many partners such as AF10. The aberrant recruitment of DOT1L by MLL fusions and the resulting H3K79 methylation are thought to affect gene expression by altering chromatin accessibility. AF10 and DOT1L interact through their coiled coil domains.


Pssm-ID: 411016 [Multi-domain]  Cd Length: 65  Bit Score: 88.52  E-value: 3.44e-21
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1126222082  555 ALQRLLETFKMQYLQFLAYMRTPDYKQQLQQEIQQEKARQEQLTAKAGQLSQQIEQLLGEGKKLL 619
Cdd:cd20902      1 ALQKLLESFKIQYLQFLAYMKTPQYKASLQQQIEQEKEKNKQLTGKAQQLEKQIQALQKEGVRLL 65
SH3_and_anchor TIGR04211
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved ...
 591-667 4.34e-05

SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved SH3 domain, a variable region, and then a C-terminal hydrophobic transmembrane alpha helix region.


Pssm-ID: 275056 [Multi-domain]  Cd Length: 198  Bit Score: 46.15  E-value: 4.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126222082  591 KARQEQLTAKAGQLSQQIEQLLGEGKKL------LSTRLQELGiKSAADILTLSQkevvRNRELHQKAQQLQQDIDKLEA 664
Cdd:TIGR04211   79 QEELAELQEQLAELRQENQELKQQLSTLeaeleeLQKELERIK-QISANAIELDE----ENRELREELAELKQENEALEA 153


                   ...
gi 1126222082  665 DNN 667
Cdd:TIGR04211  154 ENE 156
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 591-689 9.58e-04

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 41.03  E-value: 9.58e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126222082   591 KARQEQLTAKAGQLSQQIEQLLGEGKKLLSTRLQELGIKSAADILTLSQKEVVRNRELHQKAQQLQQDIDKLEADNNKKd 670
Cdd:smart00935   17 KAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQQEELQK- 95

                            90
                    ....*....|....*....
gi 1126222082   671 pngvtreaVMQEIMAAMAE 689
Cdd:smart00935   96 --------ILDKINKAIKE 106
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 591-765 1.26e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.21  E-value: 1.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126222082  591 KARQEQLTAKAGQLSQQIEQLLGEGKKLLSTrLQELGIKSAADILTLSQ--KEVVRNRELHQK-AQQLQQDIDKLEADnn 667
Cdd:COG4942     82 EAELAELEKEIAELRAELEAQKEELAELLRA-LYRLGRQPPLALLLSPEdfLDAVRRLQYLKYlAPARREQAEELRAD-- 158

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126222082  668 kkdpngvtREAVMQEIMAAMAERKRLKKLTNQLETEVATLQKGGSEKDSAEHA-----GKGQEETADGEQDIKRLTNDVS 742
Cdd:COG4942    159 --------LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARlekelAELAAELAELQQEAEELEALIA 230

                          170       180
                   ....*....|....*....|....*...
gi 1126222082  743 -----TTASVAMATSKPTSPMTGGLESP 765
Cdd:COG4942    231 rleaeAAAAAERTPAAGFAALKGKLPWP 258
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
 591-684 3.83e-03

Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442073 [Multi-domain]  Cd Length: 171  Bit Score: 39.82  E-value: 3.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126222082  591 KARQEQLTAKAGQLSQQIEQLLGEGKKLLStRLQelgiksaADILTLSQKEVV-RNRELHQKAQQLQQDIDKLEADNNKK 669
Cdd:COG2825     42 KAAQKKLEKEFKKRQAELQKLEKELQALQE-KLQ-------KEAATLSEEERQkKERELQKKQQELQRKQQEAQQDLQKR 113

                           90
                   ....*....|....*
gi 1126222082  670 dpngvtREAVMQEIM 684
Cdd:COG2825    114 ------QQELLQPIL 122
 
Name Accession Description Interval E-value
DOT1 pfam08123
Histone methylation protein DOT1; The DOT1 domain regulates gene expression by methylating ...
 118-320 1.18e-91

Histone methylation protein DOT1; The DOT1 domain regulates gene expression by methylating histone H3. H3 methylation by DOT1 has been shown to be required for the DNA damage checkpoint in yeast.


Pssm-ID: 149273  Cd Length: 205  Bit Score: 295.37  E-value: 1.18e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126222082  118 YNHSID-NPDKLNNYEPFSPEVYGETSFDLIAQMTDEITITEDDTFMDLGSGVGQVVLQVAASTPCRFCYGVEKSDVPAI 196
Cdd:pfam08123    1 YSRSVSpDANKLNHYKAFSNEVYGELLPEFLSDVLDKCNLGPQDVFVDLGSGVGNCVLQAALEFGCKLSFGCEIMDNASN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126222082  197 YSQRMDVNFKKWMKWYGKTYGEYKLEKGDFLTPTFKDKI-ANTSIVFVNNFAFGPAVDHQLKERFANMKEGAKVVSSKAF 275
Cdd:pfam08123   81 LAELQDEEFKKRCKLFGKKLGKIEFIRGSFLDNERVEEIiPEADVILVNNFAFDPELNLQLKEMLQDLKDGCKIISLKSF 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1126222082  276 CPLNFRITDRNLNDIGTIMRVSELSPLRGSVSWTGKPVSYYLHVI 320
Cdd:pfam08123  161 VPLNYRINFRNLSDIFNILKVEELKLPEGSVSWTSRGVEYYISTV 205
CC_DOT1L cd20902
coiled coil domain of disruptor of telomeric-silencing 1-like (DOT1L) and similar proteins; ...
 555-619 3.44e-21

coiled coil domain of disruptor of telomeric-silencing 1-like (DOT1L) and similar proteins; This family contains DOT1L (disruptor of telomeric-silencing 1-like), a non-SET domain histone lysine methyltransferase (HKMT) that catalyzes monomethylation, dimethylation, and trimethylation of nucleosomal H3K79. DOT1L is recruited to the homeobox A by AF10 (ALL1-Fused gene from chromosome 10 protein), one of the mixed-lineage leukemia 1 (MLL1)-fusion partners that function in acute myeloid leukemia (ALL). Aberration of the MLL gene is implicated in acute leukemia; chromosomal translocations of MLL1 generate oncogenic chimeric proteins, containing the non-catalytic N-terminal portion of MLL1 fused with many partners such as AF10. The aberrant recruitment of DOT1L by MLL fusions and the resulting H3K79 methylation are thought to affect gene expression by altering chromatin accessibility. AF10 and DOT1L interact through their coiled coil domains.


Pssm-ID: 411016 [Multi-domain]  Cd Length: 65  Bit Score: 88.52  E-value: 3.44e-21
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1126222082  555 ALQRLLETFKMQYLQFLAYMRTPDYKQQLQQEIQQEKARQEQLTAKAGQLSQQIEQLLGEGKKLL 619
Cdd:cd20902      1 ALQKLLESFKIQYLQFLAYMKTPQYKASLQQQIEQEKEKNKQLTGKAQQLEKQIQALQKEGVRLL 65
SH3_and_anchor TIGR04211
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved ...
 591-667 4.34e-05

SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved SH3 domain, a variable region, and then a C-terminal hydrophobic transmembrane alpha helix region.


Pssm-ID: 275056 [Multi-domain]  Cd Length: 198  Bit Score: 46.15  E-value: 4.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126222082  591 KARQEQLTAKAGQLSQQIEQLLGEGKKL------LSTRLQELGiKSAADILTLSQkevvRNRELHQKAQQLQQDIDKLEA 664
Cdd:TIGR04211   79 QEELAELQEQLAELRQENQELKQQLSTLeaeleeLQKELERIK-QISANAIELDE----ENRELREELAELKQENEALEA 153


                   ...
gi 1126222082  665 DNN 667
Cdd:TIGR04211  154 ENE 156
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 591-689 9.58e-04

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 41.03  E-value: 9.58e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126222082   591 KARQEQLTAKAGQLSQQIEQLLGEGKKLLSTRLQELGIKSAADILTLSQKEVVRNRELHQKAQQLQQDIDKLEADNNKKd 670
Cdd:smart00935   17 KAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQQEELQK- 95

                            90
                    ....*....|....*....
gi 1126222082   671 pngvtreaVMQEIMAAMAE 689
Cdd:smart00935   96 --------ILDKINKAIKE 106
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 591-765 1.26e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.21  E-value: 1.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126222082  591 KARQEQLTAKAGQLSQQIEQLLGEGKKLLSTrLQELGIKSAADILTLSQ--KEVVRNRELHQK-AQQLQQDIDKLEADnn 667
Cdd:COG4942     82 EAELAELEKEIAELRAELEAQKEELAELLRA-LYRLGRQPPLALLLSPEdfLDAVRRLQYLKYlAPARREQAEELRAD-- 158

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126222082  668 kkdpngvtREAVMQEIMAAMAERKRLKKLTNQLETEVATLQKGGSEKDSAEHA-----GKGQEETADGEQDIKRLTNDVS 742
Cdd:COG4942    159 --------LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARlekelAELAAELAELQQEAEELEALIA 230

                          170       180
                   ....*....|....*....|....*...
gi 1126222082  743 -----TTASVAMATSKPTSPMTGGLESP 765
Cdd:COG4942    231 rleaeAAAAAERTPAAGFAALKGKLPWP 258
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
594-742 3.33e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.81  E-value: 3.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126222082  594 QEQLTAKAGQLSQQIEQLlgegkkllsTRLQElgiksaadilTLSQkevvRNRELHQKAQQLQQDIDKLEADNNKkdpng 673
Cdd:COG4372     44 QEELEQLREELEQAREEL---------EQLEE----------ELEQ----ARSELEQLEEELEELNEQLQAAQAE----- 95

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1126222082  674 vtREAVMQEIMAAMAERKRLKKLTNQLETEVATLQKggSEKDSAEHAGKGQEETADGEQDIKRLTNDVS 742
Cdd:COG4372     96 --LAQAQEELESLQEEAEELQEELEELQKERQDLEQ--QRKQLEAQIAELQSEIAEREEELKELEEQLE 160
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
 591-684 3.83e-03

Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442073 [Multi-domain]  Cd Length: 171  Bit Score: 39.82  E-value: 3.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126222082  591 KARQEQLTAKAGQLSQQIEQLLGEGKKLLStRLQelgiksaADILTLSQKEVV-RNRELHQKAQQLQQDIDKLEADNNKK 669
Cdd:COG2825     42 KAAQKKLEKEFKKRQAELQKLEKELQALQE-KLQ-------KEAATLSEEERQkKERELQKKQQELQRKQQEAQQDLQKR 113

                           90
                   ....*....|....*
gi 1126222082  670 dpngvtREAVMQEIM 684
Cdd:COG2825    114 ------QQELLQPIL 122
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
590-745 4.09e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 4.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126222082  590 EKARQEQLTAKAGQLSQQIEQLLGEGKKLLST--RLQEL--GIKSAADILTLSQKEVvrnRELHQKAQQLQQDIDKLEAD 665
Cdd:COG4372     47 LEQLREELEQAREELEQLEEELEQARSELEQLeeELEELneQLQAAQAELAQAQEEL---ESLQEEAEELQEELEELQKE 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126222082  666 NNKKDpngVTREAVMQEIMAAMAERKRLKKLTNQLETEVATLQkggsEKDSAEHAGKGQEETADGEQDIKRLTNDVSTTA 745
Cdd:COG4372    124 RQDLE---QQRKQLEAQIAELQSEIAEREEELKELEEQLESLQ----EELAALEQELQALSEAEAEQALDELLKEANRNA 196
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 594-788 5.67e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.97  E-value: 5.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126222082  594 QEQLTAKAGQLSQQIEQLlgegKKLLSTrLQE-----------LGIKSAADIL---TLSQKEVVRNRELHQKAQQLQQDI 659
Cdd:COG3883     71 QAEIAEAEAEIEERREEL----GERARA-LYRsggsvsyldvlLGSESFSDFLdrlSALSKIADADADLLEELKADKAEL 145

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126222082  660 DKLEADNNKKDPNGVTREAVMQEIMAAM-AERKRLKKLTNQLETEVATLQKggsEKDSAEHAGKGQEETADGEQDIKRLT 738
Cdd:COG3883    146 EAKKAELEAKLAELEALKAELEAAKAELeAQQAEQEALLAQLSAEEAAAEA---QLAELEAELAAAEAAAAAAAAAAAAA 222

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1126222082  739 NDVSTTASVAMATSKPTSPMTGGLESPSPERSGGVVGKQLSPHPARQGSP 788
Cdd:COG3883    223 AAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAA 272
 
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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