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Conserved domains on  [gi|1031820596|ref|WP_064148380|]
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MULTISPECIES: cyclopropane-fatty-acyl-phospholipid synthase family protein [Klebsiella]

Protein Classification

SAM-dependent methyltransferase( domain architecture ID 11454891)

SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor

CATH:  2.20.25.110
EC:  2.1.-.-
Gene Ontology:  GO:0032259|GO:0008757|GO:1904047|GO:0008168
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CMAS super family cl47167
Mycolic acid cyclopropane synthetase; This family consist of ...
 132-401 2.56e-96

Mycolic acid cyclopropane synthetase; This family consist of Cyclopropane-fatty-acyl-phospholipid synthase or CFA synthase EC:2.1.1.79 this enzyme catalyze the reaction: S-adenosyl-L-methionine + phospholipid olefinic fatty acid <=> S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid.


The actual alignment was detected with superfamily member pfam02353:

Pssm-ID: 481507 [Multi-domain]  Cd Length: 272  Bit Score: 289.23  E-value: 2.56e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820596 132 QARENIAAHYDLGNEFYAHFLDDDLLYSSALFTDDQQDLTQAQRAKMARLCDQLALTPGDHLLEIGTGWGALAEYAARHY 211
Cdd:pfam02353   4 RDAENIQAHYDLSNDFFALFLDPTMTYSCAYFERPDMTLEEAQQAKLDLILDKLGLKPGMTLLDIGCGWGGLMRRAAERY 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820596 212 GCRVTTTTLSREQHRWATERMARAGLQDRVEVLLCDYRDLRGEYDKLVSVEMIEAVGQRYLPAFFRTCQARLRPGGRMAL 291
Cdd:pfam02353  84 DVNVVGLTLSKNQYKLARKRVAAEGLARKVEVLLQDYRDFDEPFDRIVSVGMFEHVGHENYDTFFKKLYNLLPPGGLMLL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820596 292 QAITIQDQRYR-DYSKSVDFIQRYIFPGGFLPSITAMSELMtRHTDFVVRNLFDMGPDYARTLAHWRQRFTHAWQDIEKL 370
Cdd:pfam02353 164 HTITGLHPDETsERGLPLKFIDKYIFPGGELPSISMIVESS-SEAGFTVEDVESLRPHYAKTLDLWAENLQANKDEAIAL 242

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1031820596 371 gFDERFRRMWLYYFGYCEAGFNARTISVVQL 401
Cdd:pfam02353 243 -QSEEFYRMWMLYLTGCAVAFRIGYIDVHQF 272
 
Name Accession Description Interval E-value
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
 132-401 2.56e-96

Mycolic acid cyclopropane synthetase; This family consist of Cyclopropane-fatty-acyl-phospholipid synthase or CFA synthase EC:2.1.1.79 this enzyme catalyze the reaction: S-adenosyl-L-methionine + phospholipid olefinic fatty acid <=> S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid.


Pssm-ID: 396777 [Multi-domain]  Cd Length: 272  Bit Score: 289.23  E-value: 2.56e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820596 132 QARENIAAHYDLGNEFYAHFLDDDLLYSSALFTDDQQDLTQAQRAKMARLCDQLALTPGDHLLEIGTGWGALAEYAARHY 211
Cdd:pfam02353   4 RDAENIQAHYDLSNDFFALFLDPTMTYSCAYFERPDMTLEEAQQAKLDLILDKLGLKPGMTLLDIGCGWGGLMRRAAERY 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820596 212 GCRVTTTTLSREQHRWATERMARAGLQDRVEVLLCDYRDLRGEYDKLVSVEMIEAVGQRYLPAFFRTCQARLRPGGRMAL 291
Cdd:pfam02353  84 DVNVVGLTLSKNQYKLARKRVAAEGLARKVEVLLQDYRDFDEPFDRIVSVGMFEHVGHENYDTFFKKLYNLLPPGGLMLL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820596 292 QAITIQDQRYR-DYSKSVDFIQRYIFPGGFLPSITAMSELMtRHTDFVVRNLFDMGPDYARTLAHWRQRFTHAWQDIEKL 370
Cdd:pfam02353 164 HTITGLHPDETsERGLPLKFIDKYIFPGGELPSISMIVESS-SEAGFTVEDVESLRPHYAKTLDLWAENLQANKDEAIAL 242

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1031820596 371 gFDERFRRMWLYYFGYCEAGFNARTISVVQL 401
Cdd:pfam02353 243 -QSEEFYRMWMLYLTGCAVAFRIGYIDVHQF 272
PRK11705 PRK11705
cyclopropane fatty acyl phospholipid synthase;
58-401 1.84e-89

cyclopropane fatty acyl phospholipid synthase;


Pssm-ID: 183282  Cd Length: 383  Bit Score: 275.57  E-value: 1.84e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820596  58 RVCTPEVYWRLLTGGSLAAAEAWMDGDWESHQLTALLQILARNG---EVLGRLERGFRLLGkpvARLRHwtrRNTRAQAR 134
Cdd:PRK11705   40 QVHNPRFFKRVLQEGSLGLGESYMDGWWDCDRLDEFFSRVLRAGldeKLPHHLKDTLRILR---ARLFN---LQSKKRAW 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820596 135 ENIAAHYDLGNEFYAHFLDDDLLYSSALFtDDQQDLTQAQRAKMARLCDQLALTPGDHLLEIGTGWGALAEYAARHYGCR 214
Cdd:PRK11705  114 IVGKEHYDLGNDLFEAMLDPRMQYSCGYW-KDADTLEEAQEAKLDLICRKLQLKPGMRVLDIGCGWGGLARYAAEHYGVS 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820596 215 VTTTTLSREQHRWATERMarAGLQdrVEVLLCDYRDLRGEYDKLVSVEMIEAVGQRYLPAFFRTCQARLRPGGRMALQAI 294
Cdd:PRK11705  193 VVGVTISAEQQKLAQERC--AGLP--VEIRLQDYRDLNGQFDRIVSVGMFEHVGPKNYRTYFEVVRRCLKPDGLFLLHTI 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820596 295 TiqdqRYRDYSKSVDFIQRYIFPGGFLPSITAMSELMTRHtdFVVRNLFDMGPDYARTLAHWRQRFTHAWQDIEKlGFDE 374
Cdd:PRK11705  269 G----SNKTDTNVDPWINKYIFPNGCLPSVRQIAQASEGL--FVMEDWHNFGADYDRTLMAWHENFEAAWPELAD-NYSE 341

                         330       340
                  ....*....|....*....|....*..
gi 1031820596 375 RFRRMWLYYFGYCEAGFNARTISVVQL 401
Cdd:PRK11705  342 RFYRMWRYYLLSCAGAFRARDIQLWQV 368
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 139-293 1.63e-72

Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 224.04  E-value: 1.63e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820596 139 AHYDLGNEFYAHFLDDDLLYSSALFTDDQQDLTQAQRAKMARLCDQLALTPGDHLLEIGTGWGALAEYAARHYGCRVTTT 218
Cdd:COG2230     1 HHYDLGNDFYRLFLDPTMTYSCAYFEDPDDTLEEAQEAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTGV 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1031820596 219 TLSREQHRWATERMARAGLQDRVEVLLCDYRDLR--GEYDKLVSVEMIEAVGQRYLPAFFRTCQARLRPGGRMALQA 293
Cdd:COG2230    81 TLSPEQLEYARERAAEAGLADRVEVRLADYRDLPadGQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLLHT 157
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 193-292 2.18e-10

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.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 57.44  E-value: 2.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820596 193 LLEIGTGWGALAEYAARHYGCRVTTTTLSREQHRWAtERMARAGLQDRVEVLLCDYRDLR----GEYDKLVSVEMIEAVG 268
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVTGVDISPVALELA-RKAAAALLADNVEVLKGDAEELPpeadESFDVIISDPPLHHLV 80

                          90       100
                  ....*....|....*....|....
gi 1031820596 269 QRYlPAFFRTCQARLRPGGRMALQ 292
Cdd:cd02440    81 EDL-ARFLEEARRLLKPGGVLVLT 103
rADc smart00650
Ribosomal RNA adenine dimethylases;
180-260 2.01e-04

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 41.73  E-value: 2.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820596  180 RLCDQLALTPGDHLLEIGTGWGALAEYAARHyGCRVTTTTLSReqhRWATERMARAGLQDRVEVLLCDYRDLR---GEYD 256
Cdd:smart00650   4 KIVRAANLRPGDTVLEIGPGKGALTEELLER-AKRVTAIEIDP---RLAPRLREKFAAADNLTVIHGDALKFDlpkLQPY 79


                   ....
gi 1031820596  257 KLVS 260
Cdd:smart00650  80 KVVG 83
 
Name Accession Description Interval E-value
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
 132-401 2.56e-96

Mycolic acid cyclopropane synthetase; This family consist of Cyclopropane-fatty-acyl-phospholipid synthase or CFA synthase EC:2.1.1.79 this enzyme catalyze the reaction: S-adenosyl-L-methionine + phospholipid olefinic fatty acid <=> S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid.


Pssm-ID: 396777 [Multi-domain]  Cd Length: 272  Bit Score: 289.23  E-value: 2.56e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820596 132 QARENIAAHYDLGNEFYAHFLDDDLLYSSALFTDDQQDLTQAQRAKMARLCDQLALTPGDHLLEIGTGWGALAEYAARHY 211
Cdd:pfam02353   4 RDAENIQAHYDLSNDFFALFLDPTMTYSCAYFERPDMTLEEAQQAKLDLILDKLGLKPGMTLLDIGCGWGGLMRRAAERY 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820596 212 GCRVTTTTLSREQHRWATERMARAGLQDRVEVLLCDYRDLRGEYDKLVSVEMIEAVGQRYLPAFFRTCQARLRPGGRMAL 291
Cdd:pfam02353  84 DVNVVGLTLSKNQYKLARKRVAAEGLARKVEVLLQDYRDFDEPFDRIVSVGMFEHVGHENYDTFFKKLYNLLPPGGLMLL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820596 292 QAITIQDQRYR-DYSKSVDFIQRYIFPGGFLPSITAMSELMtRHTDFVVRNLFDMGPDYARTLAHWRQRFTHAWQDIEKL 370
Cdd:pfam02353 164 HTITGLHPDETsERGLPLKFIDKYIFPGGELPSISMIVESS-SEAGFTVEDVESLRPHYAKTLDLWAENLQANKDEAIAL 242

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1031820596 371 gFDERFRRMWLYYFGYCEAGFNARTISVVQL 401
Cdd:pfam02353 243 -QSEEFYRMWMLYLTGCAVAFRIGYIDVHQF 272
PRK11705 PRK11705
cyclopropane fatty acyl phospholipid synthase;
58-401 1.84e-89

cyclopropane fatty acyl phospholipid synthase;


Pssm-ID: 183282  Cd Length: 383  Bit Score: 275.57  E-value: 1.84e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820596  58 RVCTPEVYWRLLTGGSLAAAEAWMDGDWESHQLTALLQILARNG---EVLGRLERGFRLLGkpvARLRHwtrRNTRAQAR 134
Cdd:PRK11705   40 QVHNPRFFKRVLQEGSLGLGESYMDGWWDCDRLDEFFSRVLRAGldeKLPHHLKDTLRILR---ARLFN---LQSKKRAW 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820596 135 ENIAAHYDLGNEFYAHFLDDDLLYSSALFtDDQQDLTQAQRAKMARLCDQLALTPGDHLLEIGTGWGALAEYAARHYGCR 214
Cdd:PRK11705  114 IVGKEHYDLGNDLFEAMLDPRMQYSCGYW-KDADTLEEAQEAKLDLICRKLQLKPGMRVLDIGCGWGGLARYAAEHYGVS 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820596 215 VTTTTLSREQHRWATERMarAGLQdrVEVLLCDYRDLRGEYDKLVSVEMIEAVGQRYLPAFFRTCQARLRPGGRMALQAI 294
Cdd:PRK11705  193 VVGVTISAEQQKLAQERC--AGLP--VEIRLQDYRDLNGQFDRIVSVGMFEHVGPKNYRTYFEVVRRCLKPDGLFLLHTI 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820596 295 TiqdqRYRDYSKSVDFIQRYIFPGGFLPSITAMSELMTRHtdFVVRNLFDMGPDYARTLAHWRQRFTHAWQDIEKlGFDE 374
Cdd:PRK11705  269 G----SNKTDTNVDPWINKYIFPNGCLPSVRQIAQASEGL--FVMEDWHNFGADYDRTLMAWHENFEAAWPELAD-NYSE 341

                         330       340
                  ....*....|....*....|....*..
gi 1031820596 375 RFRRMWLYYFGYCEAGFNARTISVVQL 401
Cdd:PRK11705  342 RFYRMWRYYLLSCAGAFRARDIQLWQV 368
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 139-293 1.63e-72

Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 224.04  E-value: 1.63e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820596 139 AHYDLGNEFYAHFLDDDLLYSSALFTDDQQDLTQAQRAKMARLCDQLALTPGDHLLEIGTGWGALAEYAARHYGCRVTTT 218
Cdd:COG2230     1 HHYDLGNDFYRLFLDPTMTYSCAYFEDPDDTLEEAQEAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTGV 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1031820596 219 TLSREQHRWATERMARAGLQDRVEVLLCDYRDLR--GEYDKLVSVEMIEAVGQRYLPAFFRTCQARLRPGGRMALQA 293
Cdd:COG2230    81 TLSPEQLEYARERAAEAGLADRVEVRLADYRDLPadGQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLLHT 157
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 194-287 2.00e-16

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 74.14  E-value: 2.00e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820596 194 LEIGTGWGALAEYAARHYGCRVTTTTLSREQHRWATERMARAGLqdRVEVLLCDYRDLR---GEYDKLVSVEMIEAVGQR 270
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGL--NVEFVQGDAEDLPfpdGSFDLVVSSGVLHHLPDP 79

                          90
                  ....*....|....*..
gi 1031820596 271 YLPAFFRTCQARLRPGG 287
Cdd:pfam13649  80 DLEAALREIARVLKPGG 96
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 179-291 1.82e-13

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 67.33  E-value: 1.82e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820596 179 ARLCDQLALTPGDHLLEIGTGWGALAEYAARHyGCRVTTTTLSREQHRWATERMARAGLqdRVEVLLCDYRDL---RGEY 255
Cdd:COG2226    12 EALLAALGLRPGARVLDLGCGTGRLALALAER-GARVTGVDISPEMLELARERAAEAGL--NVEFVVGDAEDLpfpDGSF 88

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1031820596 256 DKLVSVEMIEAVgqRYLPAFFRTCQARLRPGGRMAL 291
Cdd:COG2226    89 DLVISSFVLHHL--PDPERALAEIARVLKPGGRLVV 122
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 175-291 2.64e-11

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 60.42  E-value: 2.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820596 175 RAKMARLCDQLALtPGDHLLEIGTGWGALAEYAARHyGCRVTTTTLSREQHRWATERMARAglqdRVEVLLCDYRDL--- 251
Cdd:COG2227    11 DRRLAALLARLLP-AGGRVLDVGCGTGRLALALARR-GADVTGVDISPEALEIARERAAEL----NVDFVQGDLEDLple 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1031820596 252 RGEYDKLVSVEMIEAVgqRYLPAFFRTCQARLRPGGRMAL 291
Cdd:COG2227    85 DGSFDLVICSEVLEHL--PDPAALLRELARLLKPGGLLLL 122
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 193-292 2.18e-10

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.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 57.44  E-value: 2.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820596 193 LLEIGTGWGALAEYAARHYGCRVTTTTLSREQHRWAtERMARAGLQDRVEVLLCDYRDLR----GEYDKLVSVEMIEAVG 268
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVTGVDISPVALELA-RKAAAALLADNVEVLKGDAEELPpeadESFDVIISDPPLHHLV 80

                          90       100
                  ....*....|....*....|....
gi 1031820596 269 QRYlPAFFRTCQARLRPGGRMALQ 292
Cdd:cd02440    81 EDL-ARFLEEARRLLKPGGVLVLT 103
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 185-287 9.30e-09

tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; tRNA 5-hydroxyU34 O-methylase TrmR/YrrM is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443298  Cd Length: 173  Bit Score: 54.42  E-value: 9.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820596 185 LALTPGDHLLEIGTGWG----ALAEYAARhyGCRVTTTTLSREQHRWATERMARAGLQDRVEVLLCDYRD-----LRGEY 255
Cdd:COG4122    12 ARLLGAKRILEIGTGTGystlWLARALPD--DGRLTTIEIDPERAAIARENFARAGLADRIRLILGDALEvlprlADGPF 89

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1031820596 256 DkLVsveMIEAVGQRYlPAFFRTCQARLRPGG 287
Cdd:COG4122    90 D-LV---FIDADKSNY-PDYLELALPLLRPGG 116
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 178-302 2.73e-08

SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 53.77  E-value: 2.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820596 178 MARLCDQLALTPGDHLLEIGTGWGALAEYAARHYGCRVTTTTLSREQHRWATERMARAGLqDRVEVLLCDYRDL----RG 253
Cdd:COG0500    15 AALLALLERLPKGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAAKAGL-GNVEFLVADLAELdplpAE 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1031820596 254 EYDKLVSVEMIEAVGQRYLPAFFRTCQARLRPGGRMALQAITIQDQRYR 302
Cdd:COG0500    94 SFDLVVAFGVLHHLPPEEREALLRELARALKPGGVLLLSASDAAAALSL 142
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
189-292 1.35e-07

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 49.05  E-value: 1.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820596 189 PGDHLLEIGTGWGALAEY-AARHYGCRVTTTTLSREqhrwATERmARAGLqDRVEVLLCDYRDLR--GEYDKLVSVEMIE 265
Cdd:COG4106     1 PPRRVLDLGCGTGRLTALlAERFPGARVTGVDLSPE----MLAR-ARARL-PNVRFVVADLRDLDppEPFDLVVSNAALH 74

                          90       100
                  ....*....|....*....|....*..
gi 1031820596 266 AVGQRylPAFFRTCQARLRPGGRMALQ 292
Cdd:COG4106    75 WLPDH--AALLARLAAALAPGGVLAVQ 99
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
 178-289 3.04e-07

Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 50.47  E-value: 3.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820596 178 MARLCDQLALTPGDHLLEIGTGWG---A-LAEYAArhygcRVTTTTLSREQHRWATERMARAGLqDRVEVLLCD-YRDL- 251
Cdd:COG2518    55 VARMLEALDLKPGDRVLEIGTGSGyqaAvLARLAG-----RVYSVERDPELAERARERLAALGY-DNVTVRVGDgALGWp 128

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1031820596 252 -RGEYDKLVsvemIEAVGQRYLPAFFrtcqARLRPGGRM 289
Cdd:COG2518   129 eHAPFDRII----VTAAAPEVPEALL----EQLAPGGRL 159
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
189-296 8.61e-07

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 49.65  E-value: 8.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820596 189 PGDHLLEIGTGWGALAEYAARHYGCRVTTTTLSREQHRWATERMARAGLQDRVEVLLCDYRDLR--GEYDKLVSvEMIE- 265
Cdd:COG4076    35 PGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNPDIAAVARRIIAANGLSDRITVINADATDLDlpEKADVIIS-EMLDt 113

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1031820596 266 -AVGQRYLPAFFRTCQARLRPGGRMALQAITI 296
Cdd:COG4076   114 aLLDEGQVPILNHARKRLLKPGGRIIPERITN 145
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 194-291 1.11e-06

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 46.50  E-value: 1.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820596 194 LEIGTGWGALAEYAARhYGCRVTTTTLSREQHRWATERMARAGLQDRVevllCDYRDLR---GEYDKLVSVEMIEAVgqR 270
Cdd:pfam08241   1 LDVGCGTGLLTELLAR-LGARVTGVDISPEMLELAREKAPREGLTFVV----GDAEDLPfpdNSFDLVLSSEVLHHV--E 73

                          90       100
                  ....*....|....*....|.
gi 1031820596 271 YLPAFFRTCQARLRPGGRMAL 291
Cdd:pfam08241  74 DPERALREIARVLKPGGILII 94
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
132-305 1.98e-05

Predicted methyltransferase, contains TPR repeat [General function prediction only];


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 44.99  E-value: 1.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820596 132 QARENIAAHYDLGNEFYAHFLDDDLLYssalftddqqdltQAQRAKMARLCDQLALTPGDHLLEIGTGWGALAEYAARHY 211
Cdd:COG4976     2 ALDAYVEALFDQYADSYDAALVEDLGY-------------EAPALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRG 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820596 212 GcRVTTTTLSREqhrwATERMARAGLQDRVEVL-LCDYRDLRGEYDKLVSVEMIEAVGQryLPAFFRTCQARLRPGGRMA 290
Cdd:COG4976    69 Y-RLTGVDLSEE----MLAKAREKGVYDRLLVAdLADLAEPDGRFDLIVAADVLTYLGD--LAAVFAGVARALKPGGLFI 141

                         170
                  ....*....|....*
gi 1031820596 291 LQAITIQDQRYRDYS 305
Cdd:COG4976   142 FSVEDADGSGRYAHS 156
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 194-288 6.93e-05

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 41.58  E-value: 6.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820596 194 LEIGTGWGALAEYAARHY-GCRVTTTTLSREQHRWATERMARAGLQD--RVEVLLCDYRDLRGE-YDKLVSVEMIEAVgq 269
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALpGLEYTGLDISPAALEAARERLAALGLLNavRVELFQLDLGELDPGsFDVVVASNVLHHL-- 78

                          90
                  ....*....|....*....
gi 1031820596 270 RYLPAFFRTCQARLRPGGR 288
Cdd:pfam08242  79 ADPRAVLRNIRRLLKPGGV 97
rADc smart00650
Ribosomal RNA adenine dimethylases;
180-260 2.01e-04

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 41.73  E-value: 2.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820596  180 RLCDQLALTPGDHLLEIGTGWGALAEYAARHyGCRVTTTTLSReqhRWATERMARAGLQDRVEVLLCDYRDLR---GEYD 256
Cdd:smart00650   4 KIVRAANLRPGDTVLEIGPGKGALTEELLER-AKRVTAIEIDP---RLAPRLREKFAAADNLTVIHGDALKFDlpkLQPY 79


                   ....
gi 1031820596  257 KLVS 260
Cdd:smart00650  80 KVVG 83
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 189-291 2.50e-04

tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443299 [Multi-domain]  Cd Length: 238  Bit Score: 42.05  E-value: 2.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820596 189 PGDHLLEIGTGWGALAEY-AARHYGCRVTTTTLSREQHRWATERMARAGLQDRVEVLLCDYRDLRgEYDKLVSVEMI--- 264
Cdd:COG4123    37 KGGRVLDLGTGTGVIALMlAQRSPGARITGVEIQPEAAELARRNVALNGLEDRITVIHGDLKEFA-AELPPGSFDLVvsn 115

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1031820596 265 -----EAVGQ----------RY-----LPAFFRTCQARLRPGGRMAL 291
Cdd:COG4123   116 ppyfkAGSGRkspdearaiaRHedaltLEDLIRAAARLLKPGGRFAL 162
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 181-289 2.69e-04

16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA G1207 methylase RsmC is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 442062 [Multi-domain]  Cd Length: 191  Bit Score: 41.71  E-value: 2.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820596 181 LCDQLALTPGDHLLEIGTGWGALAEYAARHYGcrVTTTTLSREQHR--WATERMARAGLQDRVEVLLCD-YRDLRGE-YD 256
Cdd:COG2813    41 LLEHLPEPLGGRVLDLGCGYGVIGLALAKRNP--EARVTLVDVNARavELARANAAANGLENVEVLWSDgLSGVPDGsFD 118

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1031820596 257 KLVS-------VEMIEAVGQRylpaFFRTCQARLRPGGRM 289
Cdd:COG2813   119 LILSnppfhagRAVDKEVAHA----LIADAARHLRPGGEL 154
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 175-292 3.97e-04

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 40.87  E-value: 3.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820596 175 RAKMARLCDQLALTPGDH--LLEIGTGWGALAEYAaRHYGCRVTTTTLSREQHRWATERMARAGLQDRVEvllcdyRDLR 252
Cdd:pfam13489   6 ERLLADLLLRLLPKLPSPgrVLDFGCGTGIFLRLL-RAQGFSVTGVDPSPIAIERALLNVRFDQFDEQEA------AVPA 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1031820596 253 GEYDKLVSVEMIEAVgqRYLPAFFRTCQARLRPGGRMALQ 292
Cdd:pfam13489  79 GKFDVIVAREVLEHV--PDPPALLRQIAALLKPGGLLLLS 116
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
149-249 4.39e-04

Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 41.20  E-value: 4.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820596 149 AHFLDDDllYSSALFTDD----QQDLTQAQRAKMARLCDQLALTPGDHLLEIGTGWGALAEYAARHYG--CRVTTTTLSR 222
Cdd:pfam01135  31 EEFVPES--FKSYAYEDIplsiGYGQTISAPHMHAMMLELLELKPGMRVLEIGSGSGYLTACFARMVGevGRVVSIEHIP 108

                          90       100
                  ....*....|....*....|....*..
gi 1031820596 223 EQHRWATERMARAGLqDRVEVLLCDYR 249
Cdd:pfam01135 109 ELVEIARRNLEKLGL-ENVIVVVGDGR 134
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 183-260 1.20e-03

N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 40.53  E-value: 1.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820596 183 DQLALTPGDHLLEIGTGWGALAEYAARHY-GCRVTTTTLSREQHRWAtERMARAGLQDRVEVLLCDYRD--LRGEYDKLV 259
Cdd:PRK09328  102 EALLLKEPLRVLDLGTGSGAIALALAKERpDAEVTAVDISPEALAVA-RRNAKHGLGARVEFLQGDWFEplPGGRFDLIV 180


                  .
gi 1031820596 260 S 260
Cdd:PRK09328  181 S 181
PLN02244 PLN02244
tocopherol O-methyltransferase
 194-291 1.36e-03

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 40.50  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820596 194 LEIGTGWGALAEYAARHYGCRVTTTTLSREQHRWATERMARAGLQDRVEVLLCDYRDL---RGEYDKLVSVEMIEAV--G 268
Cdd:PLN02244  123 VDVGCGIGGSSRYLARKYGANVKGITLSPVQAARANALAAAQGLSDKVSFQVADALNQpfeDGQFDLVWSMESGEHMpdK 202

                          90       100
                  ....*....|....*....|...
gi 1031820596 269 QRYLPAFFRTCqarlRPGGRMAL 291
Cdd:PLN02244  203 RKFVQELARVA----APGGRIII 221
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
192-291 1.51e-03

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 39.71  E-value: 1.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820596  192 HLLEIGTGWGA-LAEYAARHYGCRVTTTTLSREQHRWATERMARAGLQDRVEVLlcdYRDLR-----GEYDKLVSVEMIE 265
Cdd:smart00828   2 RVLDFGCGYGSdLIDLAERHPHLQLHGYTISPEQAEVGRERIRALGLQGRIRIF---YRDSAkdpfpDTYDLVFGFEVIH 78

                           90       100
                   ....*....|....*....|....*.
gi 1031820596  266 AVGQRYlpAFFRTCQARLRPGGRMAL 291
Cdd:smart00828  79 HIKDKM--DLFSNISRHLKDGGHLVL 102
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 187-291 2.44e-03

Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


Pssm-ID: 176178 [Multi-domain]  Cd Length: 271  Bit Score: 39.61  E-value: 2.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820596 187 LTPGDHLLEIGTG-WGALAEYAARHYGCRVTTTTLSREQHRWATERMARAGLQDRVEVLLcdyRDLRGEYDKLVSVEmIE 265
Cdd:cd05188   132 LKPGDTVLVLGAGgVGLLAAQLAKAAGARVIVTDRSDEKLELAKELGADHVIDYKEEDLE---EELRLTGGGGADVV-ID 207

                          90       100
                  ....*....|....*....|....*.
gi 1031820596 266 AVGqryLPAFFRTCQARLRPGGRMAL 291
Cdd:cd05188   208 AVG---GPETLAQALRLLRPGGRIVV 230
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 189-290 3.73e-03

tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 N-methylase Trm61 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442009 [Multi-domain]  Cd Length: 249  Bit Score: 38.60  E-value: 3.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820596 189 PGDHLLEIGTGWGALAEYAARH---YGcRVTTTTLSREQHRWATERMARAGLQDRVEVLLCDYRD--LRGEYDKLV---- 259
Cdd:COG2519    91 PGARVLEAGTGSGALTLALARAvgpEG-KVYSYERREDFAEIARKNLERFGLPDNVELKLGDIREgiDEGDVDAVFldmp 169

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1031820596 260 -SVEMIEAVGQrylpaffrtcqaRLRPGGRMA 290
Cdd:COG2519   170 dPWEALEAVAK------------ALKPGGVLV 189
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
 181-291 4.13e-03

NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and conversion, General function prediction only];


Pssm-ID: 440369 [Multi-domain]  Cd Length: 322  Bit Score: 38.98  E-value: 4.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820596 181 LCDQLALTPGDHLLEIGTGwGALAEYA---ARHYGCRVTTTTLSREQHRWATERMARAGLQDRVEVLLCDYRDLRGE--Y 255
Cdd:COG0604   131 LFDRGRLKPGETVLVHGAA-GGVGSAAvqlAKALGARVIATASSPEKAELLRALGADHVIDYREEDFAERVRALTGGrgV 209

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1031820596 256 DkLVsvemIEAVGQRYLPAFFRTcqarLRPGGRMAL 291
Cdd:COG0604   210 D-VV----LDTVGGDTLARSLRA----LAPGGRLVS 236
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
192-294 6.59e-03

Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 37.50  E-value: 6.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031820596 192 HLLEIGTGWGALAEYAARHYG-CRVTT-------TTLSREQhrwaTERMARAGLQDRVEVLLCD---Y-RDLRGEYDkLV 259
Cdd:COG0421    40 RVLIIGGGDGGLARELLKHPPvERVDVveidpevVELAREY----FPLLAPAFDDPRLRVVIGDgraFlREAEESYD-VI 114

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1031820596 260 SVEMIEAVG---QRYLPAFFRTCQARLRPGGRMALQAI 294
Cdd:COG0421   115 IVDLTDPVGpaeGLFTREFYEDCRRALKPGGVLVVNLG 152
 
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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