NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1681437811|dbj|GEB87937|]
View 

dethiobiotin synthase [Zymomonas mobilis subsp. mobilis]

Protein Classification

AdoMet_MTases and DTBS domain-containing protein( domain architecture ID 13525819)

AdoMet_MTases and DTBS domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
AAA_26 pfam13500
AAA domain; This domain is found in a number of proteins involved in cofactor biosynthesis ...
 265-458 8.59e-81

AAA domain; This domain is found in a number of proteins involved in cofactor biosynthesis such as dethiobiotin synthase and cobyric acid synthase. This domain contains a P-loop motif.


:

Pssm-ID: 433259 [Multi-domain]  Cd Length: 198  Bit Score: 249.10  E-value: 8.59e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811 265 KGVFVTGTDTGIGKTLTAACLVRAW-----KSFYWKPFQTGLsEEEGDSAVVKRLAKISDDQLIPPAVTLAAPLSPEAAA 339
Cdd:pfam13500   1 RTLFVTGTDTGVGKTVVSLGLARALkrrgvKVGYWKPVQTGL-VEDGDSELVKRLLGLDQSYEDPEPFRLSAPLSPHLAA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811 340 KQENRIITKHDISFPSLKDNEILVIEGAGGLMVPISPDKMMIDFIQDCQLPVILVARSGLGTINHTLLSLEALRSRKIPI 419
Cdd:pfam13500  80 RQEGVTIDLEKIIYELPADADPVVVEGAGGLLVPINEDLLNADIAANLGLPVILVARGGLGTINHTLLTLEALRQRGIPV 159

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1681437811 420 AGAILSGTQNQENRQAIEKYGKVSILAEIPCLDQVNPEQ 458
Cdd:pfam13500 160 LGVILNGVPNPENVRTIFAFGGVPVLGAVPYLPDLTAPT 198
BioC super family cl37044
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 16-261 1.64e-49

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]


The actual alignment was detected with superfamily member TIGR02072:

Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 169.39  E-value: 1.64e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811  16 RFGKASA-YDQAAFVQKIVAKKLAEKIKltfPNSTFLPIKILEFGCGTGFLTEELTRLFPKAEITVSDISPAMLERAKTK 94
Cdd:TIGR02072   1 SFNKAAKtYDRHAKIQREMAKRLLALLK---EKGIFIPASVLDIGCGTGYLTRALLKRFPQAEFIALDISAGMLAQAKTK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811  95 fdpLRNALNFQVLDGENLP-QYPFYDLICSSLSLQWFTDRQKGLRRLIDQLNPDGQLWVSTLCENSFHEWRQLYHQRNLL 173
Cdd:TIGR02072  78 ---LSENVQFICGDAEKLPlEDSSFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFSTFGPGTLHELRQSFGQHGLR 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811 174 CPimecsSINELHSDWPTLG-QGEWTSEKIIDYPQNGFTFLRHFKKIGASlpQETIPPLSASKLRTLL----TLFDQGEK 248
Cdd:TIGR02072 155 YL-----SLDELKALLKNSFeLLTLEEELITLSFDDPLDVLRHLKKTGAN--GLSSGRTSRKQLKAFLeryeQEFQPDGL 227

                         250
                  ....*....|...
gi 1681437811 249 KITYHIGYGSFRK 261
Cdd:TIGR02072 228 PLTYHVVYGIAKK 240
 
Name Accession Description Interval E-value
AAA_26 pfam13500
AAA domain; This domain is found in a number of proteins involved in cofactor biosynthesis ...
 265-458 8.59e-81

AAA domain; This domain is found in a number of proteins involved in cofactor biosynthesis such as dethiobiotin synthase and cobyric acid synthase. This domain contains a P-loop motif.


Pssm-ID: 433259 [Multi-domain]  Cd Length: 198  Bit Score: 249.10  E-value: 8.59e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811 265 KGVFVTGTDTGIGKTLTAACLVRAW-----KSFYWKPFQTGLsEEEGDSAVVKRLAKISDDQLIPPAVTLAAPLSPEAAA 339
Cdd:pfam13500   1 RTLFVTGTDTGVGKTVVSLGLARALkrrgvKVGYWKPVQTGL-VEDGDSELVKRLLGLDQSYEDPEPFRLSAPLSPHLAA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811 340 KQENRIITKHDISFPSLKDNEILVIEGAGGLMVPISPDKMMIDFIQDCQLPVILVARSGLGTINHTLLSLEALRSRKIPI 419
Cdd:pfam13500  80 RQEGVTIDLEKIIYELPADADPVVVEGAGGLLVPINEDLLNADIAANLGLPVILVARGGLGTINHTLLTLEALRQRGIPV 159

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1681437811 420 AGAILSGTQNQENRQAIEKYGKVSILAEIPCLDQVNPEQ 458
Cdd:pfam13500 160 LGVILNGVPNPENVRTIFAFGGVPVLGAVPYLPDLTAPT 198
BioD COG0132
Dethiobiotin synthetase [Coenzyme transport and metabolism]; Dethiobiotin synthetase is part ...
 265-459 1.03e-80

Dethiobiotin synthetase [Coenzyme transport and metabolism]; Dethiobiotin synthetase is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 439902 [Multi-domain]  Cd Length: 222  Bit Score: 249.69  E-value: 1.03e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811 265 KGVFVTGTDTGIGKTLTAACLVRAWKS-----FYWKPFQTGLSEEEG-----DSAVVKRLAKISDDQLIPPAVTLAAPLS 334
Cdd:COG0132     2 KGLFVTGTDTDVGKTVVTAALAAALRAaglrvGYYKPVQTGCEETDGglrngDAELLRRLSGLPLSYELVNPYRFEEPLS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811 335 PEAAAKQENRIITKHDIS--FPSL-KDNEILVIEGAGGLMVPISPDKMMIDFIQDCQLPVILVARSGLGTINHTLLSLEA 411
Cdd:COG0132    82 PHLAARLEGVPIDLDKILaaLRALaARYDLVLVEGAGGLLVPLTEDLTLADLAKALGLPVILVVRARLGTINHTLLTVEA 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1681437811 412 LRSRKIPIAGAILSGTQ-----NQENRQAIEKYGKVSILAEIPCLDQVNPEQI 459
Cdd:COG0132   162 LRARGLPLAGIVLNGVPppdlaERDNLETLERLTGAPVLGVLPYLADLDPEAL 214
DTBS cd03109
dethiobiotin synthetase; Dethiobiotin synthetase (DTBS) is the penultimate enzyme in the ...
 265-439 1.04e-62

dethiobiotin synthetase; Dethiobiotin synthetase (DTBS) is the penultimate enzyme in the biotin biosynthesis pathway in Escherichia coli and other microorganisms. The enzyme catalyzes formation of the ureido ring of dethiobiotin from (7R,8S)-7,8-diaminononanoic acid (DAPA) and carbon dioxide. The enzyme utilizes carbon dioxide instead of hydrogen carbonate as substrate and is dependent on ATP and divalent metal ions as cofactors.


Pssm-ID: 349763 [Multi-domain]  Cd Length: 189  Bit Score: 202.03  E-value: 1.04e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811 265 KGVFVTGTDTGIGKTLTAACLVRAW-----KSFYWKPFQTGL-SEEEGDSAVVKRLAKISDDQLIPPAVTLAAPLSPEAA 338
Cdd:cd03109     1 KTLFVTGTDTDVGKTVVSAGLARALrkkgiKVGYLKPVQTGCpGLEDSDAELLRKLAGLLLDLELINPYRFEAPLSPHLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811 339 AKQENRIITKHDISFP---SLKDNEILVIEGAGGLMVPISPDKMMIDFIQDCQLPVILVARSGLGTINHTLLSLEALRSR 415
Cdd:cd03109    81 AELEGRDIDLEEIVRAleeLAKSYDVVLVEGAGGLLVPLTEGYLNADLARALGLPVILVARGGLGTINHTLLTLEALKSR 160

                         170       180
                  ....*....|....*....|....*....
gi 1681437811 416 KIPIAGAILSGTQ-----NQENRQAIEKY 439
Cdd:cd03109   161 GLDVAGVVLNGIPpepeaEADNAETLKEL 189
bioD TIGR00347
dethiobiotin synthase; Dethiobiotin synthase is involved in biotin biosynthesis and catalyses ...
 268-425 4.95e-50

dethiobiotin synthase; Dethiobiotin synthase is involved in biotin biosynthesis and catalyses the reaction (CO2 + 7,8-diaminononanoate + ATP = dethiobiotin + phosphate + ADP). The enzyme binds ATP (see motif in first 12 residues of the SEED alignment) and requires magnesium as a co-factor. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 129447 [Multi-domain]  Cd Length: 166  Bit Score: 168.31  E-value: 4.95e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811 268 FVTGTDTGIGKTLTAACLVRAWK-----SFYWKPFQTGLSEEEGDSAVVKRLAKISDD-QLIPPaVTLAAPLSPEAAAKQ 341
Cdd:TIGR00347   1 FVTGTDTGVGKTVASSALAAKLKkagysVGYYKPVQTGIEKTNSDALLLQNISGTALDwDEVNP-YAFALPLSPHIAADQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811 342 ENRIITKHDISF--PSLKDN-EILVIEGAGGLMVPISPDKMMIDFIQDCQLPVILVARSGLGTINHTLLSLEALRSRKIP 418
Cdd:TIGR00347  80 EGRPIDLEELSKhlRTLEQKyDFVLVEGAGGLCVPITEEYTTADLIKLLQLPVILVVRVKLGTINHTLLTVEHARQTGLT 159


                  ....*..
gi 1681437811 419 IAGAILS 425
Cdd:TIGR00347 160 LAGVILN 166
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 16-261 1.64e-49

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: 169.39  E-value: 1.64e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811  16 RFGKASA-YDQAAFVQKIVAKKLAEKIKltfPNSTFLPIKILEFGCGTGFLTEELTRLFPKAEITVSDISPAMLERAKTK 94
Cdd:TIGR02072   1 SFNKAAKtYDRHAKIQREMAKRLLALLK---EKGIFIPASVLDIGCGTGYLTRALLKRFPQAEFIALDISAGMLAQAKTK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811  95 fdpLRNALNFQVLDGENLP-QYPFYDLICSSLSLQWFTDRQKGLRRLIDQLNPDGQLWVSTLCENSFHEWRQLYHQRNLL 173
Cdd:TIGR02072  78 ---LSENVQFICGDAEKLPlEDSSFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFSTFGPGTLHELRQSFGQHGLR 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811 174 CPimecsSINELHSDWPTLG-QGEWTSEKIIDYPQNGFTFLRHFKKIGASlpQETIPPLSASKLRTLL----TLFDQGEK 248
Cdd:TIGR02072 155 YL-----SLDELKALLKNSFeLLTLEEELITLSFDDPLDVLRHLKKTGAN--GLSSGRTSRKQLKAFLeryeQEFQPDGL 227

                         250
                  ....*....|...
gi 1681437811 249 KITYHIGYGSFRK 261
Cdd:TIGR02072 228 PLTYHVVYGIAKK 240
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
52-150 4.71e-27

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 104.13  E-value: 4.71e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811  52 PIKILEFGCGTGFLTEELTRLFPKAEITVSDISPAMLERAKTKFDPLRnalnFQVLDGENLPQYPFYDLICSSLSLQWFT 131
Cdd:COG4106     2 PRRVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARARLPNVR----FVVADLRDLDPPEPFDLVVSNAALHWLP 77

                          90
                  ....*....|....*....
gi 1681437811 132 DRQKGLRRLIDQLNPDGQL 150
Cdd:COG4106    78 DHAALLARLAAALAPGGVL 96
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 55-148 7.50e-21

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 86.85  E-value: 7.50e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811  55 ILEFGCGTGFLTEELTRLFpKAEITVSDISPAMLERAKTKFDPLRNALNFQVLDGENLPQYP-FYDLICSSLSLQWFT-- 131
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRG-GARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLPFPDgSFDLVVSSGVLHHLPdp 79

                          90
                  ....*....|....*..
gi 1681437811 132 DRQKGLRRLIDQLNPDG 148
Cdd:pfam13649  80 DLEAALREIARVLKPGG 96
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 10-257 1.42e-12

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 67.48  E-value: 1.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811  10 KNQIIERFGKA-SAYDQAAFVQKIVAKKLAEKIkltfPNSTFlpIKILEFGCGTGflteELTRLFPKA--EITVSDISPA 86
Cdd:PRK10258    6 KQAIAAAFGRAaAHYEQHAELQRQSADALLAML----PQRKF--THVLDAGCGPG----WMSRYWRERgsQVTALDLSPP 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811  87 MLERAKTKfdplRNALNFQVLDGENLPqYP--FYDLICSSLSLQWFTDRQKGLRRLIDQLNPDGQLWVSTLCENSFHEWR 164
Cdd:PRK10258   76 MLAQARQK----DAADHYLAGDIESLP-LAtaTFDLAWSNLAVQWCGNLSTALRELYRVVRPGGVVAFTTLVQGSLPELH 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811 165 QLY-------HQRNLLCPIMECSSINELHSdwptlgqgEWTSEKIIDYPQNGFTFLRHFKKIGASLPQE--TIPPLSASK 235
Cdd:PRK10258  151 QAWqavderpHANRFLPPDAIEQALNGWRY--------QHHIQPITLWFDDALSAMRSLKGIGATHLHEgrDPRILTRSQ 222

                         250       260
                  ....*....|....*....|....
gi 1681437811 236 LRTLLTLF--DQGEKKITYHIGYG 257
Cdd:PRK10258  223 LQRLQLAWpqQQGRYPLTYHLFLG 246
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 54-153 1.97e-12

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: 63.60  E-value: 1.97e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811  54 KILEFGCGTGFLTEELtRLFPKAEITVSDISPAMLERAKtKFDPLRNALNFQVL--DGENLPQYPF--YDLICSSLSLQW 129
Cdd:cd02440     1 RVLDLGCGTGALALAL-ASGPGARVTGVDISPVALELAR-KAAAALLADNVEVLkgDAEELPPEADesFDVIISDPPLHH 78

                          90       100
                  ....*....|....*....|....*
gi 1681437811 130 F-TDRQKGLRRLIDQLNPDGQLWVS 153
Cdd:cd02440    79 LvEDLARFLEEARRLLKPGGVLVLT 103
PLN02974 PLN02974
adenosylmethionine-8-amino-7-oxononanoate transaminase
 269-439 7.24e-11

adenosylmethionine-8-amino-7-oxononanoate transaminase


Pssm-ID: 215526 [Multi-domain]  Cd Length: 817  Bit Score: 64.74  E-value: 7.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811 269 VTGTDTGIGKTLTAACLVRAWKS-----FYWKPFQTGLSEEEgDSAVVKR------------LAKISDDQLIPPAVTLAA 331
Cdd:PLN02974   32 VWGANTAVGKTLVSAGLAAAAASrrspvLYVKPVQTGFPDDS-DARFVFRkadslsrrseslFASNRTLFLSPPAAKSAL 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811 332 -----------------------------------PLSPEAAAKQENRIITKHDI------SFPSLKDNE------ILVI 364
Cdd:PLN02974  111 ggvssmgahaavnagaeagvtssalwchtlfawrrAVSPHLAARREGRGVSDDEVleavnrSLREVGANEsgggrvLALV 190

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1681437811 365 EGAGGLMVPISPDKMMIDFIQDCQLPVILVARSGLGTINHTLLSLEALRSRKIPIAGAILSGTqNQENRQAIEKY 439
Cdd:PLN02974  191 ETAGGVASPGPSGTLQCDLYRPLRLPAILVGDGRLGGISATLAAYESLLLRGYDVVAVVIEDH-GLSNEKALLSY 264
rADc smart00650
Ribosomal RNA adenine dimethylases;
33-113 6.70e-04

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 40.57  E-value: 6.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811   33 VAKKLAEKIKLTfPNSTflpikILEFGCGTGFLTEELTRLFpkAEITVSDISPAMLERAKTKFDPLRN-------ALNFQ 105
Cdd:smart00650   1 VIDKIVRAANLR-PGDT-----VLEIGPGKGALTEELLERA--KRVTAIEIDPRLAPRLREKFAAADNltvihgdALKFD 72

                           90
                   ....*....|....
gi 1681437811  106 VLDGE------NLP 113
Cdd:smart00650  73 LPKLQpykvvgNLP 86
 
Name Accession Description Interval E-value
AAA_26 pfam13500
AAA domain; This domain is found in a number of proteins involved in cofactor biosynthesis ...
 265-458 8.59e-81

AAA domain; This domain is found in a number of proteins involved in cofactor biosynthesis such as dethiobiotin synthase and cobyric acid synthase. This domain contains a P-loop motif.


Pssm-ID: 433259 [Multi-domain]  Cd Length: 198  Bit Score: 249.10  E-value: 8.59e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811 265 KGVFVTGTDTGIGKTLTAACLVRAW-----KSFYWKPFQTGLsEEEGDSAVVKRLAKISDDQLIPPAVTLAAPLSPEAAA 339
Cdd:pfam13500   1 RTLFVTGTDTGVGKTVVSLGLARALkrrgvKVGYWKPVQTGL-VEDGDSELVKRLLGLDQSYEDPEPFRLSAPLSPHLAA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811 340 KQENRIITKHDISFPSLKDNEILVIEGAGGLMVPISPDKMMIDFIQDCQLPVILVARSGLGTINHTLLSLEALRSRKIPI 419
Cdd:pfam13500  80 RQEGVTIDLEKIIYELPADADPVVVEGAGGLLVPINEDLLNADIAANLGLPVILVARGGLGTINHTLLTLEALRQRGIPV 159

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1681437811 420 AGAILSGTQNQENRQAIEKYGKVSILAEIPCLDQVNPEQ 458
Cdd:pfam13500 160 LGVILNGVPNPENVRTIFAFGGVPVLGAVPYLPDLTAPT 198
BioD COG0132
Dethiobiotin synthetase [Coenzyme transport and metabolism]; Dethiobiotin synthetase is part ...
 265-459 1.03e-80

Dethiobiotin synthetase [Coenzyme transport and metabolism]; Dethiobiotin synthetase is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 439902 [Multi-domain]  Cd Length: 222  Bit Score: 249.69  E-value: 1.03e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811 265 KGVFVTGTDTGIGKTLTAACLVRAWKS-----FYWKPFQTGLSEEEG-----DSAVVKRLAKISDDQLIPPAVTLAAPLS 334
Cdd:COG0132     2 KGLFVTGTDTDVGKTVVTAALAAALRAaglrvGYYKPVQTGCEETDGglrngDAELLRRLSGLPLSYELVNPYRFEEPLS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811 335 PEAAAKQENRIITKHDIS--FPSL-KDNEILVIEGAGGLMVPISPDKMMIDFIQDCQLPVILVARSGLGTINHTLLSLEA 411
Cdd:COG0132    82 PHLAARLEGVPIDLDKILaaLRALaARYDLVLVEGAGGLLVPLTEDLTLADLAKALGLPVILVVRARLGTINHTLLTVEA 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1681437811 412 LRSRKIPIAGAILSGTQ-----NQENRQAIEKYGKVSILAEIPCLDQVNPEQI 459
Cdd:COG0132   162 LRARGLPLAGIVLNGVPppdlaERDNLETLERLTGAPVLGVLPYLADLDPEAL 214
DTBS cd03109
dethiobiotin synthetase; Dethiobiotin synthetase (DTBS) is the penultimate enzyme in the ...
 265-439 1.04e-62

dethiobiotin synthetase; Dethiobiotin synthetase (DTBS) is the penultimate enzyme in the biotin biosynthesis pathway in Escherichia coli and other microorganisms. The enzyme catalyzes formation of the ureido ring of dethiobiotin from (7R,8S)-7,8-diaminononanoic acid (DAPA) and carbon dioxide. The enzyme utilizes carbon dioxide instead of hydrogen carbonate as substrate and is dependent on ATP and divalent metal ions as cofactors.


Pssm-ID: 349763 [Multi-domain]  Cd Length: 189  Bit Score: 202.03  E-value: 1.04e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811 265 KGVFVTGTDTGIGKTLTAACLVRAW-----KSFYWKPFQTGL-SEEEGDSAVVKRLAKISDDQLIPPAVTLAAPLSPEAA 338
Cdd:cd03109     1 KTLFVTGTDTDVGKTVVSAGLARALrkkgiKVGYLKPVQTGCpGLEDSDAELLRKLAGLLLDLELINPYRFEAPLSPHLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811 339 AKQENRIITKHDISFP---SLKDNEILVIEGAGGLMVPISPDKMMIDFIQDCQLPVILVARSGLGTINHTLLSLEALRSR 415
Cdd:cd03109    81 AELEGRDIDLEEIVRAleeLAKSYDVVLVEGAGGLLVPLTEGYLNADLARALGLPVILVARGGLGTINHTLLTLEALKSR 160

                         170       180
                  ....*....|....*....|....*....
gi 1681437811 416 KIPIAGAILSGTQ-----NQENRQAIEKY 439
Cdd:cd03109   161 GLDVAGVVLNGIPpepeaEADNAETLKEL 189
bioD TIGR00347
dethiobiotin synthase; Dethiobiotin synthase is involved in biotin biosynthesis and catalyses ...
 268-425 4.95e-50

dethiobiotin synthase; Dethiobiotin synthase is involved in biotin biosynthesis and catalyses the reaction (CO2 + 7,8-diaminononanoate + ATP = dethiobiotin + phosphate + ADP). The enzyme binds ATP (see motif in first 12 residues of the SEED alignment) and requires magnesium as a co-factor. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 129447 [Multi-domain]  Cd Length: 166  Bit Score: 168.31  E-value: 4.95e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811 268 FVTGTDTGIGKTLTAACLVRAWK-----SFYWKPFQTGLSEEEGDSAVVKRLAKISDD-QLIPPaVTLAAPLSPEAAAKQ 341
Cdd:TIGR00347   1 FVTGTDTGVGKTVASSALAAKLKkagysVGYYKPVQTGIEKTNSDALLLQNISGTALDwDEVNP-YAFALPLSPHIAADQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811 342 ENRIITKHDISF--PSLKDN-EILVIEGAGGLMVPISPDKMMIDFIQDCQLPVILVARSGLGTINHTLLSLEALRSRKIP 418
Cdd:TIGR00347  80 EGRPIDLEELSKhlRTLEQKyDFVLVEGAGGLCVPITEEYTTADLIKLLQLPVILVVRVKLGTINHTLLTVEHARQTGLT 159


                  ....*..
gi 1681437811 419 IAGAILS 425
Cdd:TIGR00347 160 LAGVILN 166
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 16-261 1.64e-49

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: 169.39  E-value: 1.64e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811  16 RFGKASA-YDQAAFVQKIVAKKLAEKIKltfPNSTFLPIKILEFGCGTGFLTEELTRLFPKAEITVSDISPAMLERAKTK 94
Cdd:TIGR02072   1 SFNKAAKtYDRHAKIQREMAKRLLALLK---EKGIFIPASVLDIGCGTGYLTRALLKRFPQAEFIALDISAGMLAQAKTK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811  95 fdpLRNALNFQVLDGENLP-QYPFYDLICSSLSLQWFTDRQKGLRRLIDQLNPDGQLWVSTLCENSFHEWRQLYHQRNLL 173
Cdd:TIGR02072  78 ---LSENVQFICGDAEKLPlEDSSFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFSTFGPGTLHELRQSFGQHGLR 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811 174 CPimecsSINELHSDWPTLG-QGEWTSEKIIDYPQNGFTFLRHFKKIGASlpQETIPPLSASKLRTLL----TLFDQGEK 248
Cdd:TIGR02072 155 YL-----SLDELKALLKNSFeLLTLEEELITLSFDDPLDVLRHLKKTGAN--GLSSGRTSRKQLKAFLeryeQEFQPDGL 227

                         250
                  ....*....|...
gi 1681437811 249 KITYHIGYGSFRK 261
Cdd:TIGR02072 228 PLTYHVVYGIAKK 240
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
52-150 4.71e-27

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 104.13  E-value: 4.71e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811  52 PIKILEFGCGTGFLTEELTRLFPKAEITVSDISPAMLERAKTKFDPLRnalnFQVLDGENLPQYPFYDLICSSLSLQWFT 131
Cdd:COG4106     2 PRRVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARARLPNVR----FVVADLRDLDPPEPFDLVVSNAALHWLP 77

                          90
                  ....*....|....*....
gi 1681437811 132 DRQKGLRRLIDQLNPDGQL 150
Cdd:COG4106    78 DHAALLARLAAALAPGGVL 96
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 54-166 3.09e-23

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: 95.06  E-value: 3.09e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811  54 KILEFGCGTGFLTEELTRLFpkAEITVSDISPAMLERAKTKFDPLRNALNFQVLDGENLPqYP--FYDLICSSLSLQWFT 131
Cdd:COG2226    25 RVLDLGCGTGRLALALAERG--ARVTGVDISPEMLELARERAAEAGLNVEFVVGDAEDLP-FPdgSFDLVISSFVLHHLP 101

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1681437811 132 DRQKGLRRLIDQLNPDGQLWVSTLCENSFHEWRQL 166
Cdd:COG2226   102 DPERALAEIARVLKPGGRLVVVDFSPPDLAELEEL 136
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 52-154 1.23e-21

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: 90.08  E-value: 1.23e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811  52 PIKILEFGCGTGFLTEELTRLFpkAEITVSDISPAMLERAKTKFDPLRnaLNFQVLDGENLPQYP-FYDLICSSLSLQWF 130
Cdd:COG2227    25 GGRVLDVGCGTGRLALALARRG--ADVTGVDISPEALEIARERAAELN--VDFVQGDLEDLPLEDgSFDLVICSEVLEHL 100

                          90       100
                  ....*....|....*....|....
gi 1681437811 131 TDRQKGLRRLIDQLNPDGQLWVST 154
Cdd:COG2227   101 PDPAALLRELARLLKPGGLLLLST 124
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 55-148 7.50e-21

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 86.85  E-value: 7.50e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811  55 ILEFGCGTGFLTEELTRLFpKAEITVSDISPAMLERAKTKFDPLRNALNFQVLDGENLPQYP-FYDLICSSLSLQWFT-- 131
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRG-GARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLPFPDgSFDLVVSSGVLHHLPdp 79

                          90
                  ....*....|....*..
gi 1681437811 132 DRQKGLRRLIDQLNPDG 148
Cdd:pfam13649  80 DLEAALREIARVLKPGG 96
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 56-150 9.91e-18

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 78.18  E-value: 9.91e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811  56 LEFGCGTGFLTEELTRLFPKAEITVSDISPAMLERAKTKFDPLR----NALNFQVLDGENLPQYPFyDLICSSLSLQWFT 131
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERLAALGllnaVRVELFQLDLGELDPGSF-DVVVASNVLHHLA 79

                          90
                  ....*....|....*....
gi 1681437811 132 DRQKGLRRLIDQLNPDGQL 150
Cdd:pfam08242  80 DPRAVLRNIRRLLKPGGVL 98
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 56-152 1.10e-17

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 78.09  E-value: 1.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811  56 LEFGCGTGFLTEELTRLFPkaEITVSDISPAMLERAKTKFDplRNALNFQVLDGENLPqYP--FYDLICSSLSLQWFTDR 133
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGA--RVTGVDISPEMLELAREKAP--REGLTFVVGDAEDLP-FPdnSFDLVLSSEVLHHVEDP 75

                          90
                  ....*....|....*....
gi 1681437811 134 QKGLRRLIDQLNPDGQLWV 152
Cdd:pfam08241  76 ERALREIARVLKPGGILII 94
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 52-153 2.14e-15

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 74.57  E-value: 2.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811  52 PIKILEFGCGTGFLTEELTRLFpKAEITVSDISPAMLERAKTKFDPLRNA-LNFQVLDGENLPQYPF--YDLICSSLSLQ 128
Cdd:COG0500    27 GGRVLDLGCGTGRNLLALAARF-GGRVIGIDLSPEAIALARARAAKAGLGnVEFLVADLAELDPLPAesFDLVVAFGVLH 105

                          90       100
                  ....*....|....*....|....*..
gi 1681437811 129 WF--TDRQKGLRRLIDQLNPDGQLWVS 153
Cdd:COG0500   106 HLppEEREALLRELARALKPGGVLLLS 132
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
20-148 1.03e-14

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 72.34  E-value: 1.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811  20 ASAYDQAAFVQKI--VAKKLAEKIKLTFPNSTFLPIkiLEFGCGTGFLTEELTRLFpkAEITVSDISPAMLERAKTKFDP 97
Cdd:COG4976    15 ADSYDAALVEDLGyeAPALLAEELLARLPPGPFGRV--LDLGCGTGLLGEALRPRG--YRLTGVDLSEEMLAKAREKGVY 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1681437811  98 LRnalnFQVLDGENLPQYPF-YDLICSSLSLQWFTDRQKGLRRLIDQLNPDG 148
Cdd:COG4976    91 DR----LLVADLADLAEPDGrFDLIVAADVLTYLGDLAAVFAGVARALKPGG 138
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 10-257 1.42e-12

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 67.48  E-value: 1.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811  10 KNQIIERFGKA-SAYDQAAFVQKIVAKKLAEKIkltfPNSTFlpIKILEFGCGTGflteELTRLFPKA--EITVSDISPA 86
Cdd:PRK10258    6 KQAIAAAFGRAaAHYEQHAELQRQSADALLAML----PQRKF--THVLDAGCGPG----WMSRYWRERgsQVTALDLSPP 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811  87 MLERAKTKfdplRNALNFQVLDGENLPqYP--FYDLICSSLSLQWFTDRQKGLRRLIDQLNPDGQLWVSTLCENSFHEWR 164
Cdd:PRK10258   76 MLAQARQK----DAADHYLAGDIESLP-LAtaTFDLAWSNLAVQWCGNLSTALRELYRVVRPGGVVAFTTLVQGSLPELH 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811 165 QLY-------HQRNLLCPIMECSSINELHSdwptlgqgEWTSEKIIDYPQNGFTFLRHFKKIGASLPQE--TIPPLSASK 235
Cdd:PRK10258  151 QAWqavderpHANRFLPPDAIEQALNGWRY--------QHHIQPITLWFDDALSAMRSLKGIGATHLHEgrDPRILTRSQ 222

                         250       260
                  ....*....|....*....|....
gi 1681437811 236 LRTLLTLF--DQGEKKITYHIGYG 257
Cdd:PRK10258  223 LQRLQLAWpqQQGRYPLTYHLFLG 246
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 54-153 1.97e-12

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: 63.60  E-value: 1.97e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811  54 KILEFGCGTGFLTEELtRLFPKAEITVSDISPAMLERAKtKFDPLRNALNFQVL--DGENLPQYPF--YDLICSSLSLQW 129
Cdd:cd02440     1 RVLDLGCGTGALALAL-ASGPGARVTGVDISPVALELAR-KAAAALLADNVEVLkgDAEELPPEADesFDVIISDPPLHH 78

                          90       100
                  ....*....|....*....|....*
gi 1681437811 130 F-TDRQKGLRRLIDQLNPDGQLWVS 153
Cdd:cd02440    79 LvEDLARFLEEARRLLKPGGVLVLT 103
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
 52-152 2.57e-12

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 234970  Cd Length: 258  Bit Score: 66.89  E-value: 2.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811  52 PIKILEFGCGTGFLTEELTRLFPKAEITVSDISPAMLERAKTKfdplrnalnfqvldgenLPQYPFY------------- 118
Cdd:PRK01683   32 PRYVVDLGCGPGNSTELLVERWPAARITGIDSSPAMLAEARSR-----------------LPDCQFVeadiaswqppqal 94

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1681437811 119 DLICSSLSLQWFTDRQKGLRRLIDQLNPDGQLWV 152
Cdd:PRK01683   95 DLIFANASLQWLPDHLELFPRLVSLLAPGGVLAV 128
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 53-156 4.14e-12

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 63.98  E-value: 4.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811  53 IKILEFGCGTGFLTEEL-TRLFPKAEITVSDISPAMLERAKTKFD--PLRNaLNFQVLDGENLPQYPF---YDLICSSLS 126
Cdd:pfam13847   5 MRVLDLGCGTGHLSFELaEELGPNAEVVGIDISEEAIEKARENAQklGFDN-VEFEQGDIEELPELLEddkFDVVISNCV 83

                          90       100       110
                  ....*....|....*....|....*....|
gi 1681437811 127 LQWFTDRQKGLRRLIDQLNPDGQLWVSTLC 156
Cdd:pfam13847  84 LNHIPDPDKVLQEILRVLKPGGRLIISDPD 113
PRK14103 PRK14103
trans-aconitate 2-methyltransferase; Provisional
 52-150 7.44e-12

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 184509  Cd Length: 255  Bit Score: 65.48  E-value: 7.44e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811  52 PIKILEFGCGTGFLTEELTRLFPKAEITVSDISPAMLERAKTKfdplrnALNFQVLDGENLPQYPFYDLICSSLSLQWFT 131
Cdd:PRK14103   30 ARRVVDLGCGPGNLTRYLARRWPGAVIEALDSSPEMVAAARER------GVDARTGDVRDWKPKPDTDVVVSNAALQWVP 103

                          90
                  ....*....|....*....
gi 1681437811 132 DRQKGLRRLIDQLNPDGQL 150
Cdd:PRK14103  104 EHADLLVRWVDELAPGSWI 122
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 29-169 1.65e-11

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 62.45  E-value: 1.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811  29 VQKIVAKKLAEKIKLTFPNsTFLPIKILEFGCGTGFLTEELTRLFPkaEITVSDISPAMLERAktkfdpLRNALNFQVLD 108
Cdd:pfam13489   1 YAHQRERLLADLLLRLLPK-LPSPGRVLDFGCGTGIFLRLLRAQGF--SVTGVDPSPIAIERA------LLNVRFDQFDE 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1681437811 109 GENLPQYPFYDLICSSLSLQWFTDRQKGLRRLIDQLNPDGQLWVSTLceNSFHEWRQLYHQ 169
Cdd:pfam13489  72 QEAAVPAGKFDVIVAREVLEHVPDPPALLRQIAALLKPGGLLLLSTP--LASDEADRLLLE 130
PLN02974 PLN02974
adenosylmethionine-8-amino-7-oxononanoate transaminase
 269-439 7.24e-11

adenosylmethionine-8-amino-7-oxononanoate transaminase


Pssm-ID: 215526 [Multi-domain]  Cd Length: 817  Bit Score: 64.74  E-value: 7.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811 269 VTGTDTGIGKTLTAACLVRAWKS-----FYWKPFQTGLSEEEgDSAVVKR------------LAKISDDQLIPPAVTLAA 331
Cdd:PLN02974   32 VWGANTAVGKTLVSAGLAAAAASrrspvLYVKPVQTGFPDDS-DARFVFRkadslsrrseslFASNRTLFLSPPAAKSAL 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811 332 -----------------------------------PLSPEAAAKQENRIITKHDI------SFPSLKDNE------ILVI 364
Cdd:PLN02974  111 ggvssmgahaavnagaeagvtssalwchtlfawrrAVSPHLAARREGRGVSDDEVleavnrSLREVGANEsgggrvLALV 190

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1681437811 365 EGAGGLMVPISPDKMMIDFIQDCQLPVILVARSGLGTINHTLLSLEALRSRKIPIAGAILSGTqNQENRQAIEKY 439
Cdd:PLN02974  191 ETAGGVASPGPSGTLQCDLYRPLRLPAILVGDGRLGGISATLAAYESLLLRGYDVVAVVIEDH-GLSNEKALLSY 264
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 1-167 1.47e-09

bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE;


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 58.24  E-value: 1.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811   1 MYKMKDKSRKNQIIERFGK-ASAYDQA----AFVQKIVAKKLAekIKLTFPnstFLPIKILEFGCGTGFLTEELTR-LFP 74
Cdd:PRK00216    1 FMTVAEEEKQEKVAEMFDSiAPKYDLMndllSFGLHRVWRRKT--IKWLGV---RPGDKVLDLACGTGDLAIALAKaVGK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811  75 KAEITVSDISPAMLERAKTKFDPLRNALNFQVL--DGENLPqYP--FYDLICSSLSLQWFTDRQKGLRRLIDQLNPDGQL 150
Cdd:PRK00216   76 TGEVVGLDFSEGMLAVGREKLRDLGLSGNVEFVqgDAEALP-FPdnSFDAVTIAFGLRNVPDIDKALREMYRVLKPGGRL 154

                         170       180
                  ....*....|....*....|..
gi 1681437811 151 WVstlCEnsFHE-----WRQLY 167
Cdd:PRK00216  155 VI---LE--FSKptnppLKKAY 171
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 54-154 1.49e-08

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 53.78  E-value: 1.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811  54 KILEFGCGTGFLTEELTRLFpKAEITVSDISPAMLERAKTKFD--PLRNALNFQVLDGENLPQYPFYDLICSSLSLQWFT 131
Cdd:COG2230    54 RVLDIGCGWGGLALYLARRY-GVRVTGVTLSPEQLEYARERAAeaGLADRVEVRLADYRDLPADGQFDAIVSIGMFEHVG 132

                          90       100
                  ....*....|....*....|....*
gi 1681437811 132 DRQKG--LRRLIDQLNPDGQLWVST 154
Cdd:COG2230   133 PENYPayFAKVARLLKPGGRLLLHT 157
PRK08317 PRK08317
hypothetical protein; Provisional
 54-150 4.39e-08

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 53.79  E-value: 4.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811  54 KILEFGCGTGFLTEELTRLF-PKAEITVSDISPAMLERAKTKFDPLRNALNFQVLDGENLPqYP--FYDLICSSLSLQWF 130
Cdd:PRK08317   22 RVLDVGCGPGNDARELARRVgPEGRVVGIDRSEAMLALAKERAAGLGPNVEFVRGDADGLP-FPdgSFDAVRSDRVLQHL 100

                          90       100
                  ....*....|....*....|
gi 1681437811 131 TDRQKGLRRLIDQLNPDGQL 150
Cdd:PRK08317  101 EDPARALAEIARVLRPGGRV 120
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
52-152 2.52e-07

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 51.67  E-value: 2.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811  52 PIKILEFGCGTGFLTEELTRLF-PKAEITVSDISPAMLERAKTKfdpLRNA----LNFQVLDGENLPqypF----YDLIC 122
Cdd:pfam01209  43 GNKFLDVAGGTGDWTFGLSDSAgSSGKVVGLDINENMLKEGEKK---AKEEgkynIEFLQGNAEELP---FeddsFDIVT 116

                          90       100       110
                  ....*....|....*....|....*....|
gi 1681437811 123 SSLSLQWFTDRQKGLRRLIDQLNPDGQLWV 152
Cdd:pfam01209 117 ISFGLRNFPDYLKVLKEAFRVLKPGGRVVC 146
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 55-112 6.43e-07

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 50.22  E-value: 6.43e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811  55 ILEFGCGTGFLTEELTRLfpKAEITVSDISPAMLERAK--TKFDPLRNALNFQVLDGENL 112
Cdd:PRK07580   67 ILDAGCGVGSLSIPLARR--GAKVVASDISPQMVEEARerAPEAGLAGNITFEVGDLESL 124
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 54-152 9.94e-06

Methyltransferase small domain; This domain is found in ribosomal RNA small subunit methyltransferase C as well as other methyltransferases.


Pssm-ID: 428349 [Multi-domain]  Cd Length: 170  Bit Score: 45.66  E-value: 9.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811  54 KILEFGCGTGFLTEELTRLFPKAEITVSDISPAMLERAKTKFdpLRNALN---FQVLDG-ENLPQYPFyDLICS------ 123
Cdd:pfam05175  34 KVLDLGCGAGVLGAALAKESPDAELTMVDINARALESARENL--AANGLEngeVVASDVySGVEDGKF-DLIISnppfha 110

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1681437811 124 ----SLSLQWftdrqkglrRLI----DQLNPDGQLWV 152
Cdd:pfam05175 111 glatTYNVAQ---------RFIadakRHLRPGGELWI 138
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 54-152 1.22e-05

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: 45.95  E-value: 1.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811  54 KILEFGCGTGFLTEELTRLFPKAEITVSDISPAMLERAKtkfdplRNAL-----NFQVL--DG-ENLPQYPFyDLICSS- 124
Cdd:COG2813    52 RVLDLGCGYGVIGLALAKRNPEARVTLVDVNARAVELAR------ANAAangleNVEVLwsDGlSGVPDGSF-DLILSNp 124

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1681437811 125 -LSLQWFTDRQkGLRRLIDQ----LNPDGQLWV 152
Cdd:COG2813   125 pFHAGRAVDKE-VAHALIADaarhLRPGGELWL 156
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 267-467 6.70e-05

CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid a,c-diamide synthases. These include CbiA and CbiP from S.typhimurium, and CobQ from R. capsulatus. These amidases catalyze amidations to various side chains of hydrogenobyrinic acid or cobyrinic acid a,c-diamide in the biosynthesis of cobalamin (vitamin B12) from uroporphyrinogen III. Vitamin B12 is an important cofactor and an essential nutrient for many plants and animals and is primarily produced by bacteria. The family also contains dethiobiotin synthetases as well as the plasmid partitioning proteins of the MinD/ParA family.


Pssm-ID: 426369 [Multi-domain]  Cd Length: 228  Bit Score: 44.26  E-value: 6.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811 267 VFVTGTDTGIGKTLTAACLVRAWKSFYWK--PF----QTGLSEEEG----------------------DSAVVKRLAKIS 318
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRvlLIdldpQSNNSSVEGlegdiapalqalaeglkgrvnlDPILLKEKSDEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811 319 DDQLIPPAVTLAAPLSPEAAAKQENRIITkhdiSFPSLKDN-EILVIEGAGGLMVP-----ISPDKMMIDFiqdcQLPVI 392
Cdd:pfam01656  81 GLDLIPGNIDLEKFEKELLGPRKEERLRE----ALEALKEDyDYVIIDGAPGLGELlrnalIAADYVIIPL----EPEVI 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811 393 LVA-RSGLGTINHTLlsLEALRSRKIPIAGAIL----SGTQNQENRQAIEKY-GKVSILAEIPCLDQVnpeqIEIVARNM 466
Cdd:pfam01656 153 LVEdAKRLGGVIAAL--VGGYALLGLKIIGVVLnkvdGDNHGKLLKEALEELlRGLPVLGVIPRDEAV----AEAPARGL 226


                  .
gi 1681437811 467 P 467
Cdd:pfam01656 227 P 227
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
 32-121 1.60e-04

Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members of this family are protein methyltransferases targetting Lys residues in specific proteins, including calmodulin, VCP, Kin17 and Hsp70 proteins.


Pssm-ID: 313513  Cd Length: 172  Bit Score: 42.32  E-value: 1.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811  32 IVAKKLAEKIKLTFPNSTFLPIKILEFGCGTGFLTEELTRLFPKAEITVSDISPaMLERAKTKFD--PLRNALNFQVLD- 108
Cdd:pfam10294  27 VLSKYLEMKIFKELGANNLSGLNVLELGSGTGLVGIAVALLLPGASVTITDLEE-ALELLKKNIElnALSSKVVVKVLDw 105

                          90
                  ....*....|....*..
gi 1681437811 109 GENLPQYPF----YDLI 121
Cdd:pfam10294 106 GENLPPDLFdghpVDLI 122
PLN02490 PLN02490
MPBQ/MSBQ methyltransferase
 53-138 2.11e-04

MPBQ/MSBQ methyltransferase


Pssm-ID: 215270 [Multi-domain]  Cd Length: 340  Bit Score: 43.34  E-value: 2.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811  53 IKILEFGCGTGFLTEELTRLFPKAEITVSDISPAMLERAKTKfDPLRNAlnfQVLDG--ENLPqYP--FYDLICSSLSLQ 128
Cdd:PLN02490  115 LKVVDVGGGTGFTTLGIVKHVDAKNVTILDQSPHQLAKAKQK-EPLKEC---KIIEGdaEDLP-FPtdYADRYVSAGSIE 189

                          90
                  ....*....|
gi 1681437811 129 WFTDRQKGLR 138
Cdd:PLN02490  190 YWPDPQRGIK 199
rsmC PRK09489
16S rRNA (guanine(1207)-N(2))-methyltransferase RsmC;
48-92 2.25e-04

16S rRNA (guanine(1207)-N(2))-methyltransferase RsmC;


Pssm-ID: 181902 [Multi-domain]  Cd Length: 342  Bit Score: 43.39  E-value: 2.25e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1681437811  48 STFLPI---KILEFGCGTGFLTEELTRLFPKAEITVSDISPAMLERAK 92
Cdd:PRK09489  190 STLTPHtkgKVLDVGCGAGVLSAVLARHSPKIRLTLSDVSAAALESSR 237
COG3963 COG3963
Phosphatidylethanolamine N-methyltransferase [Lipid transport and metabolism];
55-148 3.85e-04

Phosphatidylethanolamine N-methyltransferase [Lipid transport and metabolism];


Pssm-ID: 443163  Cd Length: 193  Bit Score: 41.35  E-value: 3.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811  55 ILEFGCGTGFLTEE-LTRLFPKAEITVSDISPAMLERAKTKFDplrnalNFQVLDG--ENLPQY------PFYDLICSSL 125
Cdd:COG3963    49 VVELGPGTGVFTRAiLARGVPDARLLAVEINPEFAEHLRRRFP------RVTVVNGdaEDLAELlaehgiGKVDAVVSGL 122

                          90       100
                  ....*....|....*....|....*..
gi 1681437811 126 SLQWFTDRQKglRRLIDQ----LNPDG 148
Cdd:COG3963   123 PLLSFPPELR--RAILDAafrvLAPGG 147
PTZ00338 PTZ00338
dimethyladenosine transferase-like protein; Provisional
 29-128 4.81e-04

dimethyladenosine transferase-like protein; Provisional


Pssm-ID: 240367 [Multi-domain]  Cd Length: 294  Bit Score: 41.91  E-value: 4.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811  29 VQKIVakkLAEKIKltfPNSTflpikILEFGCGTGFLTEeltRLFPKAEITVS-DISPAMLERAKTKFDPLRNALNFQVL 107
Cdd:PTZ00338   25 LDKIV---EKAAIK---PTDT-----VLEIGPGTGNLTE---KLLQLAKKVIAiEIDPRMVAELKKRFQNSPLASKLEVI 90

                          90       100
                  ....*....|....*....|..
gi 1681437811 108 DGENLPQ-YPFYDLICSSLSLQ 128
Cdd:PTZ00338   91 EGDALKTeFPYFDVCVANVPYQ 112
rADc smart00650
Ribosomal RNA adenine dimethylases;
33-113 6.70e-04

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 40.57  E-value: 6.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811   33 VAKKLAEKIKLTfPNSTflpikILEFGCGTGFLTEELTRLFpkAEITVSDISPAMLERAKTKFDPLRN-------ALNFQ 105
Cdd:smart00650   1 VIDKIVRAANLR-PGDT-----VLEIGPGKGALTEELLERA--KRVTAIEIDPRLAPRLREKFAAADNltvihgdALKFD 72

                           90
                   ....*....|....
gi 1681437811  106 VLDGE------NLP 113
Cdd:smart00650  73 LPKLQpykvvgNLP 86
NodS pfam05401
Nodulation protein S (NodS); This family consists of nodulation S (NodS) proteins. The ...
 24-150 2.43e-03

Nodulation protein S (NodS); This family consists of nodulation S (NodS) proteins. The products of the rhizobial nodulation genes are involved in the biosynthesis of lipochitin oligosaccharides (LCOs), which are host-specific signal molecules required for nodule formation. NodS is an S-adenosyl-L-methionine (SAM)-dependent methyltransferase involved in N methylation of LCOs. NodS uses N-deacetylated chitooligosaccharides, the products of the NodBC proteins, as its methyl acceptors.


Pssm-ID: 428457  Cd Length: 201  Bit Score: 39.22  E-value: 2.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811  24 DQAAFVQKivakKLAEKIKLTFPNSTFlpIKILEFGCGTGFLTEeltRLFPKAE-ITVSDISPAMLERAKTKFDPLRNaL 102
Cdd:pfam05401  22 DSCAFEQK----RLAAILELCLGDGDA--ADALEIGCAAGAFTE---MLAILCErLTVVDLMPEAIAKAQERTGKWSD-I 91

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1681437811 103 NFQVLDGENLPQYPFYDLICSSLSLQWFTDRQK---GLRRLIDQLNPDGQL 150
Cdd:pfam05401  92 IWHECDICQFDLNAKFDLIICAEVLYYIHDKEElhaAIENIVQLLAPDEQF 142
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 52-123 2.90e-03

Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 39.36  E-value: 2.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811  52 PIKILEFGCGTGFLTEELTRLFPKAEITVSDISPAMLERAKtkfdplRNALNFQVLDG---------ENLPQYPFYDLIC 122
Cdd:COG2890   113 PPRVLDLGTGSGAIALALAKERPDARVTAVDISPDALAVAR------RNAERLGLEDRvrflqgdlfEPLPGDGRFDLIV 186


                  .
gi 1681437811 123 S 123
Cdd:COG2890   187 S 187
PRK11036 PRK11036
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;
30-150 6.82e-03

tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;


Pssm-ID: 182918  Cd Length: 255  Bit Score: 38.41  E-value: 6.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681437811  30 QKIVAKKLaEKIKLTFPNStflPIKILEFGCGTGFLTEELTRLfpKAEITVSDISPAMLERAKtkfdplRNALNFQVLDG 109
Cdd:PRK11036   27 QAILWQDL-DRLLAELPPR---PLRVLDAGGGEGQTAIKLAEL--GHQVILCDLSAEMIQRAK------QAAEAKGVSDN 94

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1681437811 110 ENLPQYPF----------YDLICSSLSLQWFTDRQKGLRRLIDQLNPDGQL 150
Cdd:PRK11036   95 MQFIHCAAqdiaqhletpVDLILFHAVLEWVADPKSVLQTLWSVLRPGGAL 145
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH