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Conserved domains on  [gi|12232389|ref|NP_073571|]
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ribosome assembly protein METTL17, mitochondrial isoform 2 precursor [Homo sapiens]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 106779)

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

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; ...
155-438 1.23e-59

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 pfam09243:

Pssm-ID: 473071  Cd Length: 275  Bit Score: 196.61  E-value: 1.23e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232389   155 SLVYMAARLDGGFAAVSRAFHEIRARNPAFQPQTLMDFGSGTGSVTWAAHSIWGQsLREYMCVDRSAAMLVLAEKLLKGG 234
Cdd:pfam09243   4 SLAYAAARMPATYAAVRRALTEFAERVPQFRPRSHLDIGGGPGTATWAASETWRG-IRPVTVIDASEPALAIGEEIARHG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232389   235 SESGEPYIPG---VFFRQFLPVspkvqfDVVVSAFSLSELpSKADRTEVVQTLWRKTGHFLVLVENGTKAGHSLLMDARD 311
Cdd:pfam09243  83 PALKQAAWRRsriGAALQFESA------DLVTISYVLFEL-TNEDREDVIDNLWAKAAQAVVIVEPGTPAGYRRVNEARE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232389   312 LvlkgkekspLDPRPGFVFAPCPHELPCPQLTNLA-CSFSQAYHPIPF-----SWNKKPKEEKFSMVILARGSPEEAhrW 385
Cdd:pfam09243 156 R---------LIAAGFHIAAPCPHSLACPLVAGLDwCHFSQRVARSSLhrqvkSGSLPYEDEKFSYLAAGRQPVAPA--W 224
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 12232389   386 PRITQPVLKRPRHVHCHLCCPDGHMQHAVLTaRRHGrDLYRCARVSSWGDLLP 438
Cdd:pfam09243 225 PRVVRPPQVRKGHVLIDLCTEDGTLQRVTVT-KRHG-SLYKAARDARWGDRWP 275
 
Name Accession Description Interval E-value
Rsm22 pfam09243
Mitochondrial small ribosomal subunit Rsm22; Rsm22 has been identified as a mitochondrial ...
155-438 1.23e-59

Mitochondrial small ribosomal subunit Rsm22; Rsm22 has been identified as a mitochondrial small ribosomal subunit and is a methyltransferase. In Schizosaccharomyces pombe, Rsm22 is tandemly fused to Cox11 (a factor required for copper insertion into cytochrome oxidase) and the two proteins are proteolytically cleaved after import into the mitochondria.


Pssm-ID: 401254  Cd Length: 275  Bit Score: 196.61  E-value: 1.23e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232389   155 SLVYMAARLDGGFAAVSRAFHEIRARNPAFQPQTLMDFGSGTGSVTWAAHSIWGQsLREYMCVDRSAAMLVLAEKLLKGG 234
Cdd:pfam09243   4 SLAYAAARMPATYAAVRRALTEFAERVPQFRPRSHLDIGGGPGTATWAASETWRG-IRPVTVIDASEPALAIGEEIARHG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232389   235 SESGEPYIPG---VFFRQFLPVspkvqfDVVVSAFSLSELpSKADRTEVVQTLWRKTGHFLVLVENGTKAGHSLLMDARD 311
Cdd:pfam09243  83 PALKQAAWRRsriGAALQFESA------DLVTISYVLFEL-TNEDREDVIDNLWAKAAQAVVIVEPGTPAGYRRVNEARE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232389   312 LvlkgkekspLDPRPGFVFAPCPHELPCPQLTNLA-CSFSQAYHPIPF-----SWNKKPKEEKFSMVILARGSPEEAhrW 385
Cdd:pfam09243 156 R---------LIAAGFHIAAPCPHSLACPLVAGLDwCHFSQRVARSSLhrqvkSGSLPYEDEKFSYLAAGRQPVAPA--W 224
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 12232389   386 PRITQPVLKRPRHVHCHLCCPDGHMQHAVLTaRRHGrDLYRCARVSSWGDLLP 438
Cdd:pfam09243 225 PRVVRPPQVRKGHVLIDLCTEDGTLQRVTVT-KRHG-SLYKAARDARWGDRWP 275
Rsm22 COG5459
Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal ...
127-419 2.48e-49

Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal structure and biogenesis]; Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) is part of the Pathway/BioSystem: Archaeal ribosomal proteins


Pssm-ID: 444210 [Multi-domain]  Cd Length: 306  Bit Score: 170.52  E-value: 2.48e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232389 127 EEKLRGAVLHALRKTTyhwQELS--YTEGLS------------LVYMAARLDGGFAAVSRAFHEIRARNPAFQPQTLMDF 192
Cdd:COG5459  11 EDLLEGRSGARLRAAI---RRLSerYRAERGsrrpyladeadaLAYAAYRLPATYAAVRAALAELAEAGPDFAPLTVLDV 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232389 193 GSGTGSVTWAAHSIWgQSLREYMCVDRSAAMLVLAEKLLKGGSESGEPYIPGVFFRqFLPVSPKVQFDVVVSAFSLSELP 272
Cdd:COG5459  88 GAGPGTAAWAAADAW-PSLLDATLLERSAAALALGRRLARAAANPALETAEWRLAD-LAAALPAPPADLVVASYVLNELA 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232389 273 sKADRTEVVQTLWRKTGHFLVLVENGTKAGHSLLMDARDLVLKGKekspldprpGFVFAPCPHELPCPQLTNLACSFSQa 352
Cdd:COG5459 166 -DAARAALVDRLWLAPDGALLIVEPGTPAGSRRLLAARDRLIAAG---------AHVAAPCPHAGACPLAEPDWCHFSR- 234
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 12232389 353 YHPIPfSWNKKPKE-------EKFSMVILARGSPEEAhrWPRITQPVLKRPRHVHCHLCCPDGHMQHAVLTARR 419
Cdd:COG5459 235 RLARP-RLHRRLKGaalpnedEKFSYLALRRDPARRP--AARVLRHPLSRKGGVELKLCTPDGGVRERLVSKRD 305
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
181-268 6.76e-03

malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin biosynthetic gene clusters in proteobacteria, firmicutes, green-sulfur bacteria, fusobacterium and bacteroides, carries out an enzymatic step prior to the formation of pimeloyl-CoA, namely O-methylation of the malonyl group preferentially while on acyl carrier protein. The enzyme is recognizable as a methyltransferase by homology. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 38.04  E-value: 6.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232389   181 NPAFQPQTLMDFGSGTGSVTWAAHSIWGQSlrEYMCVDRSAAMLVLAEKLLKGGSEsgepYIPGVFFRqfLPVSPKvQFD 260
Cdd:TIGR02072  30 KGIFIPASVLDIGCGTGYLTRALLKRFPQA--EFIALDISAGMLAQAKTKLSENVQ----FICGDAEK--LPLEDS-SFD 100

                  ....*...
gi 12232389   261 VVVSAFSL 268
Cdd:TIGR02072 101 LIVSNLAL 108
 
Name Accession Description Interval E-value
Rsm22 pfam09243
Mitochondrial small ribosomal subunit Rsm22; Rsm22 has been identified as a mitochondrial ...
155-438 1.23e-59

Mitochondrial small ribosomal subunit Rsm22; Rsm22 has been identified as a mitochondrial small ribosomal subunit and is a methyltransferase. In Schizosaccharomyces pombe, Rsm22 is tandemly fused to Cox11 (a factor required for copper insertion into cytochrome oxidase) and the two proteins are proteolytically cleaved after import into the mitochondria.


Pssm-ID: 401254  Cd Length: 275  Bit Score: 196.61  E-value: 1.23e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232389   155 SLVYMAARLDGGFAAVSRAFHEIRARNPAFQPQTLMDFGSGTGSVTWAAHSIWGQsLREYMCVDRSAAMLVLAEKLLKGG 234
Cdd:pfam09243   4 SLAYAAARMPATYAAVRRALTEFAERVPQFRPRSHLDIGGGPGTATWAASETWRG-IRPVTVIDASEPALAIGEEIARHG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232389   235 SESGEPYIPG---VFFRQFLPVspkvqfDVVVSAFSLSELpSKADRTEVVQTLWRKTGHFLVLVENGTKAGHSLLMDARD 311
Cdd:pfam09243  83 PALKQAAWRRsriGAALQFESA------DLVTISYVLFEL-TNEDREDVIDNLWAKAAQAVVIVEPGTPAGYRRVNEARE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232389   312 LvlkgkekspLDPRPGFVFAPCPHELPCPQLTNLA-CSFSQAYHPIPF-----SWNKKPKEEKFSMVILARGSPEEAhrW 385
Cdd:pfam09243 156 R---------LIAAGFHIAAPCPHSLACPLVAGLDwCHFSQRVARSSLhrqvkSGSLPYEDEKFSYLAAGRQPVAPA--W 224
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 12232389   386 PRITQPVLKRPRHVHCHLCCPDGHMQHAVLTaRRHGrDLYRCARVSSWGDLLP 438
Cdd:pfam09243 225 PRVVRPPQVRKGHVLIDLCTEDGTLQRVTVT-KRHG-SLYKAARDARWGDRWP 275
Rsm22 COG5459
Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal ...
127-419 2.48e-49

Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal structure and biogenesis]; Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) is part of the Pathway/BioSystem: Archaeal ribosomal proteins


Pssm-ID: 444210 [Multi-domain]  Cd Length: 306  Bit Score: 170.52  E-value: 2.48e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232389 127 EEKLRGAVLHALRKTTyhwQELS--YTEGLS------------LVYMAARLDGGFAAVSRAFHEIRARNPAFQPQTLMDF 192
Cdd:COG5459  11 EDLLEGRSGARLRAAI---RRLSerYRAERGsrrpyladeadaLAYAAYRLPATYAAVRAALAELAEAGPDFAPLTVLDV 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232389 193 GSGTGSVTWAAHSIWgQSLREYMCVDRSAAMLVLAEKLLKGGSESGEPYIPGVFFRqFLPVSPKVQFDVVVSAFSLSELP 272
Cdd:COG5459  88 GAGPGTAAWAAADAW-PSLLDATLLERSAAALALGRRLARAAANPALETAEWRLAD-LAAALPAPPADLVVASYVLNELA 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232389 273 sKADRTEVVQTLWRKTGHFLVLVENGTKAGHSLLMDARDLVLKGKekspldprpGFVFAPCPHELPCPQLTNLACSFSQa 352
Cdd:COG5459 166 -DAARAALVDRLWLAPDGALLIVEPGTPAGSRRLLAARDRLIAAG---------AHVAAPCPHAGACPLAEPDWCHFSR- 234
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 12232389 353 YHPIPfSWNKKPKE-------EKFSMVILARGSPEEAhrWPRITQPVLKRPRHVHCHLCCPDGHMQHAVLTARR 419
Cdd:COG5459 235 RLARP-RLHRRLKGaalpnedEKFSYLALRRDPARRP--AARVLRHPLSRKGGVELKLCTPDGGVRERLVSKRD 305
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
185-286 7.75e-07

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 47.13  E-value: 7.75e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232389 185 QPQTLMDFGSGTGSVTWAAHSIWGQslREYMCVDRSAAMLVLAEKLLkggsesgepyiPGVFFRQ--FLPVSPKVQFDVV 262
Cdd:COG4106   1 PPRRVLDLGCGTGRLTALLAERFPG--ARVTGVDLSPEMLARARARL-----------PNVRFVVadLRDLDPPEPFDLV 67
                        90       100
                ....*....|....*....|....
gi 12232389 263 VSAFSLSELPskaDRTEVVQTLWR 286
Cdd:COG4106  68 VSNAALHWLP---DHAALLARLAA 88
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
191-298 2.24e-06

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 45.63  E-value: 2.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232389   191 DFGSGTGSVTWAAHSIWGqslREYMCVDRSAAMLVLAEKLLKGgsesgepYIPGVFFRQ----FLPVSPKvQFDVVVSAF 266
Cdd:pfam13649   3 DLGCGTGRLTLALARRGG---ARVTGVDLSPEMLERARERAAE-------AGLNVEFVQgdaeDLPFPDG-SFDLVVSSG 71
                          90       100       110
                  ....*....|....*....|....*....|..
gi 12232389   267 SLSELPsKADRTEVVQTLWRktghflVLVENG 298
Cdd:pfam13649  72 VLHHLP-DPDLEAALREIAR------VLKPGG 96
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
190-286 2.02e-05

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 43.13  E-value: 2.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232389   190 MDFGSGTGSVTWAahsiWGQSLR--EYMCVDRSAAMLVLAEKLLKGgsESGEPYIPGVFFRQFLPVSPKVQFDVVVSAFS 267
Cdd:pfam08242   1 LEIGCGTGTLLRA----LLEALPglEYTGLDISPAALEAARERLAA--LGLLNAVRVELFQLDLGELDPGSFDVVVASNV 74
                          90
                  ....*....|....*....
gi 12232389   268 LSELPskaDRTEVVQTLWR 286
Cdd:pfam08242  75 LHHLA---DPRAVLRNIRR 90
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
186-294 1.30e-04

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: 41.90  E-value: 1.30e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232389 186 PQTLMDFGSGTGSVTWAahsiWGQSLREYMCVDRSAAMLVLAEKLLKGGSESGEpYIPGVFFRqfLPVSPKvQFDVVVSA 265
Cdd:COG2226  23 GARVLDLGCGTGRLALA----LAERGARVTGVDISPEMLELARERAAEAGLNVE-FVVGDAED--LPFPDG-SFDLVISS 94
                        90       100       110
                ....*....|....*....|....*....|..
gi 12232389 266 FSLSELPskaDRTEVVQTLWR---KTGHFLVL 294
Cdd:COG2226  95 FVLHHLP---DPERALAEIARvlkPGGRLVVV 123
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
191-293 4.49e-04

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 39.19  E-value: 4.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232389   191 DFGSGTGSVTwaahSIWGQSLREYMCVDRSAAMLVLAEKLLKggsESGEPYIPGVFFRqfLPVSPKvQFDVVVSAFSLSE 270
Cdd:pfam08241   2 DVGCGTGLLT----ELLARLGARVTGVDISPEMLELAREKAP---REGLTFVVGDAED--LPFPDN-SFDLVLSSEVLHH 71
                          90       100
                  ....*....|....*....|....*.
gi 12232389   271 LPskaDRTEVVQTLWR---KTGHFLV 293
Cdd:pfam08241  72 VE---DPERALREIARvlkPGGILII 94
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
185-293 1.49e-03

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: 38.46  E-value: 1.49e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232389 185 QPQTLMDFGSGTGSVTWAA----HSIWGqslreymcVDRSAAMLVLAEKLLKggsESGEPYIPGVFFRqfLPVSPKvQFD 260
Cdd:COG2227  24 AGGRVLDVGCGTGRLALALarrgADVTG--------VDISPEALEIARERAA---ELNVDFVQGDLED--LPLEDG-SFD 89
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 12232389 261 VVVSAFSLSELPskaDRTEVVQTLW---RKTGHFLV 293
Cdd:COG2227  90 LVICSEVLEHLP---DPAALLRELArllKPGGLLLL 122
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
166-303 2.65e-03

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 38.83  E-value: 2.65e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232389 166 GFAAVSRAFHEIRARNPAFQPQTLMDFGSGTGsvtwaahsIWGQSLREY----MCVDRSAAMLVLAEKllKGGsesgepY 241
Cdd:COG4976  27 GYEAPALLAEELLARLPPGPFGRVLDLGCGTG--------LLGEALRPRgyrlTGVDLSEEMLAKARE--KGV------Y 90
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 12232389 242 IPgvFFRQFLP--VSPKVQFDVVVSAFSLSELpskADRTEVVQTLWRKT---GHFLVLVENGTKAGH 303
Cdd:COG4976  91 DR--LLVADLAdlAEPDGRFDLIVAADVLTYL---GDLAAVFAGVARALkpgGLFIFSVEDADGSGR 152
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
185-311 5.39e-03

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 37.97  E-value: 5.39e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232389 185 QPQTLMDFGSGTGSVTWAAHSIWGqslREYMCVDRSAAMLVLAEKLLKggsesgEPYIPGVFFRQ-----FLPVSPKvQF 259
Cdd:COG0500  26 KGGRVLDLGCGTGRNLLALAARFG---GRVIGIDLSPEAIALARARAA------KAGLGNVEFLVadlaeLDPLPAE-SF 95
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 12232389 260 DVVVSAFSLSELPsKADRTEVVQTLWR--KTGHFLVLVENGTKAGHSLLMDARD 311
Cdd:COG0500  96 DLVVAFGVLHHLP-PEEREALLRELARalKPGGVLLLSASDAAAALSLARLLLL 148
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
181-268 6.76e-03

malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin biosynthetic gene clusters in proteobacteria, firmicutes, green-sulfur bacteria, fusobacterium and bacteroides, carries out an enzymatic step prior to the formation of pimeloyl-CoA, namely O-methylation of the malonyl group preferentially while on acyl carrier protein. The enzyme is recognizable as a methyltransferase by homology. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 38.04  E-value: 6.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12232389   181 NPAFQPQTLMDFGSGTGSVTWAAHSIWGQSlrEYMCVDRSAAMLVLAEKLLKGGSEsgepYIPGVFFRqfLPVSPKvQFD 260
Cdd:TIGR02072  30 KGIFIPASVLDIGCGTGYLTRALLKRFPQA--EFIALDISAGMLAQAKTKLSENVQ----FICGDAEK--LPLEDS-SFD 100

                  ....*...
gi 12232389   261 VVVSAFSL 268
Cdd:TIGR02072 101 LIVSNLAL 108
 
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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