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Conserved domains on  [gi|1705366836|ref|WP_142693959|]
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glycosyltransferase [Campylobacter troglodytis]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
3-396 1.02e-69

glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ExpE7 in Sinorhizobium meliloti has been shown to be involved in the biosynthesis of galactoglucans (exopolysaccharide II).


:

Pssm-ID: 340850 [Multi-domain]  Cd Length: 357  Bit Score: 232.22  E-value: 1.02e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836   3 KILKIIHGFPPDFMAGSEVYSHTLTKELSLNGHKVFVFTrIENdflQPYTIFDEIIEFKQKNVNPICIRRINKPKDYIYR 82
Cdd:cd03823     1 KILLVNSLYPPQRVGGAEISVHDLAEALVAEGHEVAVLT-AGV---GPPGQATVARSVVRYRRAPDETLPLALKRRGYEL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836  83 DKFFDENVEKAFKEYMMEINPDIVHFGHLCHLSINLVHIAKSLGKRIVFTLHDFWLFCvkgqlINQngeicqnpsiencq 162
Cdd:cd03823    77 FETYNPGLRRLLARLLEDFRPDVVHTHNLSGLGASLLDAARDLGIPVVHTLHDYWLLC-----PRQ-------------- 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 163 kcspykpkiqevkKMFnalkylRDKIDIFIAPSHTIRNFFIENGVSKSKIIYQKYGFdTKTIIYKRRIFTKNANIKFGFM 242
Cdd:cd03823   138 -------------FLF------KKGGDAVLAPSRFTANLHEANGLFSARISVIPNAV-EPDLAPPPRRRPGTERLRFGYI 197
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 243 GRIIPTKGIGVLLKAFKDLPNE--SLYIYGNISKTQMRFLQL-SNVKFMGAYNNADINKVLNSIDVLIVPSIWLENSPLV 319
Cdd:cd03823   198 GRLTEEKGIDLLVEAFKRLPREdiELVIAGHGPLSDERQIEGgRRIAFLGRVPTDDIKDFYEKIDVLVVPSIWPEPFGLV 277
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1705366836 320 IQEAFLSGVVVITSNIGGMNELI--GKNeGFLFKAGDSNDLIKVIKKIKQDCRILNTIKDNRHKVDSIQTDAKKILKIY 396
Cdd:cd03823   278 VREAIAAGLPVIASDLGGIAELIqpGVN-GLLFAPGDAEDLAAAMRRLLTDPALLERLRAGAEPPRSTESQAEEYLKLY 355
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
415-558 1.78e-17

Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, chromosome partitioning, Coenzyme transport and metabolism];


:

Pssm-ID: 440301 [Multi-domain]  Cd Length: 159  Bit Score: 79.95  E-value: 1.78e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 415 RITIDTNPdTCNFRCKMCdthsiYNKHFKKLRPDMSLDILNKTLLESKQMKVSEIIPTtMGEPMLYKYFDTIVDFCLQND 494
Cdd:COG0535     1 RLQIELTN-RCNLRCKHC-----YADAGPKRPGELSTEEAKRILDELAELGVKVVGLT-GGEPLLRPDLFELVEYAKELG 73
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1705366836 495 IKLNLTTNGSqLFNKKYnVKYIKNKllpALSDIKISFNSLDYAVNEEIMRNTNTRD-VLAKIERL 558
Cdd:COG0535    74 IRVNLSTNGT-LLTEEL-AERLAEA---GLDHVTISLDGVDPETHDKIRGVPGAFDkVLEAIKLL 133
AslB super family cl33987
Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, ...
425-723 4.11e-11

Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, protein turnover, chaperones];


The actual alignment was detected with superfamily member COG0641:

Pssm-ID: 440406 [Multi-domain]  Cd Length: 349  Bit Score: 65.01  E-value: 4.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 425 CNFRCKMCdthsIYNKHFKKLRPDMSLDILNKTL--LESKQMKVSEIiptTM----GEPML-YKYFDTIVDFCLQN---- 493
Cdd:COG0641    11 CNLRCSYC----YYSEGDEGSRRRMSEETAEKAIdfLIESSGPGKEL---TItffgGEPLLnFDFIKEIVEYARKYakkg 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 494 -DIKLNLTTNGSqLFNKKYnVKYIKNKllpalsDIKISFnSLDYavNEEI---MRNTNT-----RDVLAKIERLCSMRdk 564
Cdd:COG0641    84 kKIRFSIQTNGT-LLDDEW-IDFLKEN------GFSVGI-SLDG--PKEIhdrNRVTKNgkgsfDRVMRNIKLLKEHG-- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 565 ffprVSITLQMTFMKSNIDSIKPIIEYAIKHKINRIkghQLWITHKELENEAIYKDKEFIELWNELV-LSLERYKDDIRL 643
Cdd:COG0641   151 ----VEVNIRCTVTRENLDDPEELYDFLKELGFRSI---QFNPVVEEGEADYSLTPEDYGEFLIELFdEWLERDGGKIFV 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 644 ENFTPIQDS--TKAKGKCPFLGQELW-VNYRGDISVCcapdKQRASLGDF--GNITHISLDKVISSAKYRNLVKHYPK-- 716
Cdd:COG0641   224 REFDILLAGllPPCSSPCVGAGGNYLvVDPDGDIYPC----DEFVGDPEFrlGNVFDGSLAELLDSPKLRAFGREKNVll 299

                  ....*..
gi 1705366836 717 MEVCQKC 723
Cdd:COG0641   300 DEECRSC 306
 
Name Accession Description Interval E-value
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
3-396 1.02e-69

glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ExpE7 in Sinorhizobium meliloti has been shown to be involved in the biosynthesis of galactoglucans (exopolysaccharide II).


Pssm-ID: 340850 [Multi-domain]  Cd Length: 357  Bit Score: 232.22  E-value: 1.02e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836   3 KILKIIHGFPPDFMAGSEVYSHTLTKELSLNGHKVFVFTrIENdflQPYTIFDEIIEFKQKNVNPICIRRINKPKDYIYR 82
Cdd:cd03823     1 KILLVNSLYPPQRVGGAEISVHDLAEALVAEGHEVAVLT-AGV---GPPGQATVARSVVRYRRAPDETLPLALKRRGYEL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836  83 DKFFDENVEKAFKEYMMEINPDIVHFGHLCHLSINLVHIAKSLGKRIVFTLHDFWLFCvkgqlINQngeicqnpsiencq 162
Cdd:cd03823    77 FETYNPGLRRLLARLLEDFRPDVVHTHNLSGLGASLLDAARDLGIPVVHTLHDYWLLC-----PRQ-------------- 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 163 kcspykpkiqevkKMFnalkylRDKIDIFIAPSHTIRNFFIENGVSKSKIIYQKYGFdTKTIIYKRRIFTKNANIKFGFM 242
Cdd:cd03823   138 -------------FLF------KKGGDAVLAPSRFTANLHEANGLFSARISVIPNAV-EPDLAPPPRRRPGTERLRFGYI 197
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 243 GRIIPTKGIGVLLKAFKDLPNE--SLYIYGNISKTQMRFLQL-SNVKFMGAYNNADINKVLNSIDVLIVPSIWLENSPLV 319
Cdd:cd03823   198 GRLTEEKGIDLLVEAFKRLPREdiELVIAGHGPLSDERQIEGgRRIAFLGRVPTDDIKDFYEKIDVLVVPSIWPEPFGLV 277
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1705366836 320 IQEAFLSGVVVITSNIGGMNELI--GKNeGFLFKAGDSNDLIKVIKKIKQDCRILNTIKDNRHKVDSIQTDAKKILKIY 396
Cdd:cd03823   278 VREAIAAGLPVIASDLGGIAELIqpGVN-GLLFAPGDAEDLAAAMRRLLTDPALLERLRAGAEPPRSTESQAEEYLKLY 355
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
237-368 2.55e-20

Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.


Pssm-ID: 425737 [Multi-domain]  Cd Length: 158  Bit Score: 88.10  E-value: 2.55e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 237 IKFGFMGRIIPTKGIGVLLKAFKDL----PNESLYIYGNIS-----KTQMRFLQLS-NVKFMGAYNNADINKVLNSIDVL 306
Cdd:pfam00534   3 KIILFVGRLEPEKGLDLLIKAFALLkeknPNLKLVIAGDGEeekrlKKLAEKLGLGdNVIFLGFVSDEDLPELLKIADVF 82
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1705366836 307 IVPSIWlENSPLVIQEAFLSGVVVITSNIGGMNELIGKNE-GFLFKAGDSNDLIKVIKKIKQD 368
Cdd:pfam00534  83 VLPSRY-EGFGIVLLEAMACGLPVIASDVGGPPEVVKDGEtGFLVKPNNAEALAEAIDKLLED 144
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
415-558 1.78e-17

Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, chromosome partitioning, Coenzyme transport and metabolism];


Pssm-ID: 440301 [Multi-domain]  Cd Length: 159  Bit Score: 79.95  E-value: 1.78e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 415 RITIDTNPdTCNFRCKMCdthsiYNKHFKKLRPDMSLDILNKTLLESKQMKVSEIIPTtMGEPMLYKYFDTIVDFCLQND 494
Cdd:COG0535     1 RLQIELTN-RCNLRCKHC-----YADAGPKRPGELSTEEAKRILDELAELGVKVVGLT-GGEPLLRPDLFELVEYAKELG 73
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1705366836 495 IKLNLTTNGSqLFNKKYnVKYIKNKllpALSDIKISFNSLDYAVNEEIMRNTNTRD-VLAKIERL 558
Cdd:COG0535    74 IRVNLSTNGT-LLTEEL-AERLAEA---GLDHVTISLDGVDPETHDKIRGVPGAFDkVLEAIKLL 133
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
242-401 1.20e-16

Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 76.57  E-value: 1.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 242 MGRIIPTKGIGVLLKAFkdlpneslyiygnisktqmrflqlsnvkfmgaynnadinkvLNSIDVLIVPSIWlENSPLVIQ 321
Cdd:COG0438     1 MGRLVPRKGLDLLLEAL-----------------------------------------LAAADVFVLPSRS-EGFGLVLL 38
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 322 EAFLSGVVVITSNIGGMNELIGKNE-GFLFKAGDSNDLIKVIKKIKQDCRILNTIKDN-RHKVD---SIQTDAKKILKIY 396
Cdd:COG0438    39 EAMAAGLPVIATDVGGLPEVIEDGEtGLLVPPGDPEALAEAILRLLEDPELRRRLGEAaRERAEerfSWEAIAERLLALY 118

                  ....*
gi 1705366836 397 YSLIE 401
Cdd:COG0438   119 EELLA 123
AslB COG0641
Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, ...
425-723 4.11e-11

Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440406 [Multi-domain]  Cd Length: 349  Bit Score: 65.01  E-value: 4.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 425 CNFRCKMCdthsIYNKHFKKLRPDMSLDILNKTL--LESKQMKVSEIiptTM----GEPML-YKYFDTIVDFCLQN---- 493
Cdd:COG0641    11 CNLRCSYC----YYSEGDEGSRRRMSEETAEKAIdfLIESSGPGKEL---TItffgGEPLLnFDFIKEIVEYARKYakkg 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 494 -DIKLNLTTNGSqLFNKKYnVKYIKNKllpalsDIKISFnSLDYavNEEI---MRNTNT-----RDVLAKIERLCSMRdk 564
Cdd:COG0641    84 kKIRFSIQTNGT-LLDDEW-IDFLKEN------GFSVGI-SLDG--PKEIhdrNRVTKNgkgsfDRVMRNIKLLKEHG-- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 565 ffprVSITLQMTFMKSNIDSIKPIIEYAIKHKINRIkghQLWITHKELENEAIYKDKEFIELWNELV-LSLERYKDDIRL 643
Cdd:COG0641   151 ----VEVNIRCTVTRENLDDPEELYDFLKELGFRSI---QFNPVVEEGEADYSLTPEDYGEFLIELFdEWLERDGGKIFV 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 644 ENFTPIQDS--TKAKGKCPFLGQELW-VNYRGDISVCcapdKQRASLGDF--GNITHISLDKVISSAKYRNLVKHYPK-- 716
Cdd:COG0641   224 REFDILLAGllPPCSSPCVGAGGNYLvVDPDGDIYPC----DEFVGDPEFrlGNVFDGSLAELLDSPKLRAFGREKNVll 299

                  ....*..
gi 1705366836 717 MEVCQKC 723
Cdd:COG0641   300 DEECRSC 306
N_Twi_rSAM NF033640
twitch domain-containing radical SAM protein; Members of this family are unusual among radical ...
424-598 7.11e-11

twitch domain-containing radical SAM protein; Members of this family are unusual among radical SAM proteins in several ways. First, the N-terminal region consists of an iron-sulfur cluster-binding twitch domain (half of a SPASM domain), something usually found C-terminal to the radical SAM domain. Second, the radical SAM domains in many of the members of this family score poorly vs. the Pfam HMM, PF04055 (version 19), used to identify radical SAM. Lastly, the majority of members sequenced to date come from uncultured bacteria from marine or aquifer sources rather than from conventionally cultured bacterial isolates. The function is unknown.


Pssm-ID: 468123 [Multi-domain]  Cd Length: 396  Bit Score: 64.60  E-value: 7.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 424 TCNFRCKMCDTH--SIYNKHFKKLRPDMSLDILNKTLLESKQM--KVSEIIPTTM------GEPMLYKYFDTIVDFCLQN 493
Cdd:NF033640  119 LCNLKCRMCGPHssSSWAKEAKKLGGPKLGDKKKISWFEDEEFwkWLEELLPSLKeiyfagGEPLLIKEHYKLLEKLVEK 198
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 494 ----DIKLNLTTNGSQLFNKKYNVKyiknKLLPALSDIKISFnSLD--YAVNEEIMRNTNTRDVLAKIERLcsmrDKFFP 567
Cdd:NF033640  199 grakNIELRYNTNLTVLPDKLKDLL----DLWKKFKSVSISA-SIDgvGERNEYIRYGSKWDEIEKNLKKL----KEECP 269
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1705366836 568 RVSITLQMTFMKSNIDSIKPIIEYAIKHKIN 598
Cdd:NF033640  270 NVELRINPTVSALNVLHLPELLDWLLELGLG 300
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
422-590 7.64e-07

Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S cluster and S-adenosylmethionine (SAM) in close proximity. They are characterized by a conserved CxxxCxxC motif, which coordinates the conserved iron-sulfur cluster. Mechanistically, they share the transfer of a single electron from the iron-sulfur cluster to SAM, which leads to its reductive cleavage to methionine and a 5'-deoxyadenosyl radical, which, in turn, abstracts a hydrogen from the appropriately positioned carbon atom. Depending on the enzyme, SAM is consumed during this process or it is restored and reused. Radical SAM enzymes catalyze steps in metabolism, DNA repair, the biosynthesis of vitamins and coenzymes, and the biosynthesis of many antibiotics. Examples are biotin synthase (BioB), lipoyl synthase (LipA), pyruvate formate-lyase (PFL), coproporphyrinogen oxidase (HemN), lysine 2,3-aminomutase (LAM), anaerobic ribonucleotide reductase (ARR), and MoaA, an enzyme of the biosynthesis of molybdopterin.


Pssm-ID: 100105 [Multi-domain]  Cd Length: 204  Bit Score: 50.41  E-value: 7.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 422 PDTCNFRCKMCDTHSIYNKHFKKLRPDMSLDILnktLLESKQMKVSEIIpTTMGEPMLYKYF-DTIVDFC-LQNDIKLNL 499
Cdd:cd01335     4 TRGCNLNCGFCSNPASKGRGPESPPEIEEILDI---VLEAKERGVEVVI-LTGGEPLLYPELaELLRRLKkELPGFEISI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 500 TTNGSQLFNKkynvkyIKNKLLPALSDIK-ISFNSLDYAVNEEIMRNTNT-RDVLAKIERLCSMRDKFFPRVSITLQMTF 577
Cdd:cd01335    80 ETNGTLLTEE------LLKELKELGLDGVgVSLDSGDEEVADKIRGSGESfKERLEALKELREAGLGLSTTLLVGLGDED 153
                         170
                  ....*....|...
gi 1705366836 578 MKSNIDSIKPIIE 590
Cdd:cd01335   154 EEDDLEELELLAE 166
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
425-573 9.72e-07

Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual methylations, isomerization, sulphur insertion, ring formation, anaerobic oxidation and protein radical formation.


Pssm-ID: 427681 [Multi-domain]  Cd Length: 159  Bit Score: 49.06  E-value: 9.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 425 CNFRCKMCDTHSIynkHFKKLRPDMSLDILNKTLLESKQMKVSEIIpTTMGEPMLYKYFDTIVDFCLQ----NDIKLNLT 500
Cdd:pfam04055   5 CNLRCTYCAFPSI---RARGKGRELSPEEILEEAKELKRLGVEVVI-LGGGEPLLLPDLVELLERLLKlelaEGIRITLE 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1705366836 501 TNGSqLFNKKYnVKYIKNKLLPALSdikISFNSLDYAVNEEIMRNTNTRDVLAKIERLcsmRDKFFPRVSITL 573
Cdd:pfam04055  81 TNGT-LLDEEL-LELLKEAGLDRVS---IGLESGDDEVLKLINRGHTFEEVLEALELL---REAGIPVVTDNI 145
moaA PRK00164
GTP 3',8-cyclase MoaA;
415-597 3.34e-06

GTP 3',8-cyclase MoaA;


Pssm-ID: 234672 [Multi-domain]  Cd Length: 331  Bit Score: 49.75  E-value: 3.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 415 RITIdTnpDTCNFRCKMCdtHSiyNKHFKKLRPD--MSLDILNKTLLESKQMKVSEI-IptTMGEPMLYKYFDTIVDFC- 490
Cdd:PRK00164   20 RISV-T--DRCNFRCTYC--MP--EGYLPFLPKEelLSLEEIERLVRAFVALGVRKVrL--TGGEPLLRKDLEDIIAALa 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 491 -LQNDIKLNLTTNGSQLfnkkynVKYIKnKLLPA-LSDIKISFNSLDYAVNEEIMRNTNTRDVLAKIERLcsmRDKFFPR 568
Cdd:PRK00164   91 aLPGIRDLALTTNGYLL------ARRAA-ALKDAgLDRVNVSLDSLDPERFKAITGRDRLDQVLAGIDAA---LAAGLTP 160
                         170       180       190
                  ....*....|....*....|....*....|
gi 1705366836 569 VSItlQMTFMKS-NIDSIKPIIEYAIKHKI 597
Cdd:PRK00164  161 VKV--NAVLMKGvNDDEIPDLLEWAKDRGI 188
PelF NF038011
GT4 family glycosyltransferase PelF; Proteins of this family are components of the ...
240-348 7.03e-06

GT4 family glycosyltransferase PelF; Proteins of this family are components of the exopolysaccharide Pel transporter. It has been reported that PelF is a soluble glycosyltransferase that uses UDP-glucose as the substrate for the synthesis of exopolysaccharide Pel, whereas PelG is a Wzx-like and PST family exopolysaccharide transporter.


Pssm-ID: 411604 [Multi-domain]  Cd Length: 489  Bit Score: 49.16  E-value: 7.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 240 GFMGRIIPTKGIGVLLKAF----KDLPNESLYI---------YGNISKTQMRFLQL-SNVKFMGAYNnadINKVLNSIDV 305
Cdd:NF038011  310 GLIGRVVPIKDIKTFIRAMrtvvRAMPEAEGWIvgpeeedpaYAAECRSLVASLGLqDKVKFLGFQK---IDDLLPQVGL 386
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1705366836 306 LIVPSIwLENSPLVIQEAFLSGVVVITSNIGGMNELIgknEGF 348
Cdd:NF038011  387 MVLSSI-SEALPLVVLEAFAAGVPVVTTDVGSCRQLI---EGL 425
SPASM cd21109
Iron-sulfur cluster-binding SPASM domain; This iron-sulfur cluster-binding domain is named ...
659-723 1.01e-05

Iron-sulfur cluster-binding SPASM domain; This iron-sulfur cluster-binding domain is named SPASM after the biochemically characterized members, AlbA, PqqE, anSME, and MftC, which are involved in Subtilosin A, Pyrroloquinoline quinone, Anaerobic Sulfatase, and Mycofactocin maturation, respectively. SPASM occurs as an additional C-terminal domain in many peptide-modifying enzymes of the radical S-adenosylmethionine (SAM) superfamily. Radical SAM enzymes are characterized by a conserved CxxxCxxC motif, which coordinates the conserved iron-sulfur cluster that is involved in the reductive cleavage of SAM and generates a 5'-deoxyadenosyl radical, which in turn abstracts a hydrogen from the appropriately positioned carbon atom of the substrate. Radical SAM enzymes with a C-terminal SPASM domain contain at least one other iron-sulfur cluster.


Pssm-ID: 410609 [Multi-domain]  Cd Length: 65  Bit Score: 43.57  E-value: 1.01e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1705366836 659 CPFLGQELWVNYRGDISVCCAPDKQRASLgdfGNITHISLDKVISSAKYRNLVK--HYPKMEVCQKC 723
Cdd:cd21109     2 CPAPWTSLYITPDGDVYPCCFDVNEELKL---GNIREQSLKEIWNSEKYREFRKllLDGKIKLCKNC 65
SPASM pfam13186
Iron-sulfur cluster-binding domain; This domain occurs as an additional C-terminal iron-sulfur ...
659-723 6.48e-05

Iron-sulfur cluster-binding domain; This domain occurs as an additional C-terminal iron-sulfur cluster binding domain in many radical SAM domain, pfam04055 proteins. The domain occurs in a number of proteins that modify a protein to become an active enzyme, or a peptide to become a ribosomal natural product. The domain is named SPASM because it occurs in the maturases of Subilitosin, PQQ, Anaerobic Sulfatases, and Mycofactocin.


Pssm-ID: 433020 [Multi-domain]  Cd Length: 66  Bit Score: 41.31  E-value: 6.48e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1705366836 659 CPFLGQELWVNYRGDISVCcaPDKQRASLGDFGNITHISLDKVISSAKYRNL--VKHYPKMEVCQKC 723
Cdd:pfam13186   1 CFAGWTSLVILPDGDVYPC--FDDDFVGPIVLGNIREQSLAEIWNSPKYREFrkLGKFALIELCRDC 65
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
174-369 1.06e-04

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 45.47  E-value: 1.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 174 VKKMFNALKYLRDKIDIFIAPSHTIRNFFIENGVSKSKII--YQKyGFDTKTIIYK------RRIFTKNANIKF--GFMG 243
Cdd:PLN02871  192 VKPMWDIIRFLHRAADLTLVTSPALGKELEAAGVTAANRIrvWNK-GVDSESFHPRfrseemRARLSGGEPEKPliVYVG 270
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 244 RIIPTKGIGVLLKAFKDLPNESLYIYGN---ISKTQMRFLQLsNVKFMGAYNNADINKVLNSIDVLIVPSiwlENSPL-- 318
Cdd:PLN02871  271 RLGAEKNLDFLKRVMERLPGARLAFVGDgpyREELEKMFAGT-PTVFTGMLQGDELSQAYASGDVFVMPS---ESETLgf 346
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1705366836 319 VIQEAFLSGVVVITSNIGGMNELIGKNE----GFLFKAGDSNDLIKVIKKIKQDC 369
Cdd:PLN02871  347 VVLEAMASGVPVVAARAGGIPDIIPPDQegktGFLYTPGDVDDCVEKLETLLADP 401
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
425-626 2.26e-03

Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, coproporphyrinogen III oxidase, biotin synthase and MiaB families, and includes a representative in the eukaryotic elongator subunit, Elp-3. Some members of the family are methyltransferases.


Pssm-ID: 214792 [Multi-domain]  Cd Length: 216  Bit Score: 40.08  E-value: 2.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836  425 CNFRCKMCDTHSIYNKhFKKLRPDMSLDIL------NKTLLESKQMKVSEIIPTTMGEPMLYKYFDTIVD-FCLQNDIKL 497
Cdd:smart00729  11 CPRRCTFCSFPSLRGK-LRSRYLEALVREIellaekGEKEGLVGTVFIGGGTPTLLSPEQLEELLEAIREiLGLAKDVEI 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836  498 NLTTNGSQLFN------KKYNVKYiknkllpalsdIKISFNSLDYAVNEEIMRNTNTRDVLAKIERLcsmRDKFFPRVSI 571
Cdd:smart00729  90 TIETRPDTLTEellealKEAGVNR-----------VSLGVQSGDDEVLKAINRGHTVEDVLEAVELL---REAGPIKVST 155
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836  572 TLQMTFMKSNIDSIKPIIEYAIKHKINRIKGHQLWIT-----HKELENEAIYKDKEFIEL 626
Cdd:smart00729 156 DLIVGLPGETEEDFEETLKLLKELGPDRVSIFPLSPRpgtplAKMYKRLKPPTKEERAEL 215
 
Name Accession Description Interval E-value
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
3-396 1.02e-69

glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ExpE7 in Sinorhizobium meliloti has been shown to be involved in the biosynthesis of galactoglucans (exopolysaccharide II).


Pssm-ID: 340850 [Multi-domain]  Cd Length: 357  Bit Score: 232.22  E-value: 1.02e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836   3 KILKIIHGFPPDFMAGSEVYSHTLTKELSLNGHKVFVFTrIENdflQPYTIFDEIIEFKQKNVNPICIRRINKPKDYIYR 82
Cdd:cd03823     1 KILLVNSLYPPQRVGGAEISVHDLAEALVAEGHEVAVLT-AGV---GPPGQATVARSVVRYRRAPDETLPLALKRRGYEL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836  83 DKFFDENVEKAFKEYMMEINPDIVHFGHLCHLSINLVHIAKSLGKRIVFTLHDFWLFCvkgqlINQngeicqnpsiencq 162
Cdd:cd03823    77 FETYNPGLRRLLARLLEDFRPDVVHTHNLSGLGASLLDAARDLGIPVVHTLHDYWLLC-----PRQ-------------- 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 163 kcspykpkiqevkKMFnalkylRDKIDIFIAPSHTIRNFFIENGVSKSKIIYQKYGFdTKTIIYKRRIFTKNANIKFGFM 242
Cdd:cd03823   138 -------------FLF------KKGGDAVLAPSRFTANLHEANGLFSARISVIPNAV-EPDLAPPPRRRPGTERLRFGYI 197
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 243 GRIIPTKGIGVLLKAFKDLPNE--SLYIYGNISKTQMRFLQL-SNVKFMGAYNNADINKVLNSIDVLIVPSIWLENSPLV 319
Cdd:cd03823   198 GRLTEEKGIDLLVEAFKRLPREdiELVIAGHGPLSDERQIEGgRRIAFLGRVPTDDIKDFYEKIDVLVVPSIWPEPFGLV 277
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1705366836 320 IQEAFLSGVVVITSNIGGMNELI--GKNeGFLFKAGDSNDLIKVIKKIKQDCRILNTIKDNRHKVDSIQTDAKKILKIY 396
Cdd:cd03823   278 VREAIAAGLPVIASDLGGIAELIqpGVN-GLLFAPGDAEDLAAAMRRLLTDPALLERLRAGAEPPRSTESQAEEYLKLY 355
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
3-396 8.48e-35

phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.


Pssm-ID: 340831 [Multi-domain]  Cd Length: 366  Bit Score: 136.13  E-value: 8.48e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836   3 KILKIIHGFPPDFmAGSEVYSHTLTKELSLNGHKVFVFTriendFLQPYTIFDEIIEFKQKNVNPICIRRINKPKdyiyr 82
Cdd:cd03801     1 KILLLSPELPPPV-GGAERHVRELARALAARGHDVTVLT-----PADPGEPPEELEDGVIVPLLPSLAALLRARR----- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836  83 dkffdenVEKAFKEYMMEINPDIVHFgHLCHLSINLVHIAKSLGKRIVFTLHDFWLFcvkgqlinqngeicqnpsiENCQ 162
Cdd:cd03801    70 -------LLRELRPLLRLRKFDVVHA-HGLLAALLAALLALLLGAPLVVTLHGAEPG-------------------RLLL 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 163 KCSPYKPKIQEvkkmfnaLKYLRDKIDIFIAPSHTIRNFFIENGV---SKSKIIYqkYGFDTKTII--YKRRIFTKNANI 237
Cdd:cd03801   123 LLAAERRLLAR-------AEALLRRADAVIAVSEALRDELRALGGippEKIVVIP--NGVDLERFSppLRRKLGIPPDRP 193
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 238 KFGFMGRIIPTKGIGVLLKAFKDL----PNESLYIYGN----ISKTQMRFLQLS-NVKFMGAYNNADINKVLNSIDVLIV 308
Cdd:cd03801   194 VLLFVGRLSPRKGVDLLLEALAKLlrrgPDVRLVIVGGdgplRAELEELELGLGdRVRFLGFVPDEELPALYAAADVFVL 273
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 309 PSIWlENSPLVIQEAFLSGVVVITSNIGGMNELIGKNE-GFLFKAGDSNDLIKVIKKIKQD----CRILNTIKDNRHKVD 383
Cdd:cd03801   274 PSRY-EGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEgGLVVPPDDVEALADALLRLLADpelrARLGRAARERVAERF 352
                         410
                  ....*....|...
gi 1705366836 384 SIQTDAKKILKIY 396
Cdd:cd03801   353 SWERVAERLLDLY 365
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
21-365 4.00e-22

capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. CapM in Staphylococcus aureus is required for the synthesis of type 1 capsular polysaccharides.


Pssm-ID: 340837 [Multi-domain]  Cd Length: 358  Bit Score: 98.82  E-value: 4.00e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836  21 VYSHT--LTKELSLNGHKVFVFTRiENDFLQpytifdEIIEFKQKNV--NPICIRRINKPKDYiyrdkffdenveKAFKE 96
Cdd:cd03808    12 FQSFRlpLIKALVKKGYEVHVIAP-DGDKLS------DELKELGVKVidIPILRRGINPLKDL------------KALFK 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836  97 Y---MMEINPDIVHfghlCHLSINLVH--IAKSL--GKRIVFTLHDF-WLFCVKG--QLINQNGE----------ICQNP 156
Cdd:cd03808    73 LyklLKKEKPDIVH----CHTPKPGILgrLAARLagVPKVIYTVHGLgFVFTEGKllRLLYLLLEklallftdkvIFVNE 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 157 SIEncqkcspykpkiqevkkmfnalKYLRDKIDIFIAPSHTIRNffieNGVSKSKIIYQKYGFDTKTIiykrriftknan 236
Cdd:cd03808   149 DDR----------------------DLAIKKGIIKKKKTVLIPG----SGVDLDRFQYSPESLPSEKV------------ 190
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 237 iKFGFMGRIIPTKGIGVLLKAFKDL----PNESLYIYG-----NISKTQMRFLQLS-NVKFMGAYNnaDINKVLNSIDVL 306
Cdd:cd03808   191 -VFLFVARLLKDKGIDELIEAAKILkkkgPNVRFLLVGdgeleNPSEILIEKLGLEgRIEFLGFRS--DVPELLAESDVF 267
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1705366836 307 IVPSIWlENSPLVIQEAFLSGVVVITSNIGGMNELI--GKNeGFLFKAGDSNDLIKVIKKI 365
Cdd:cd03808   268 VLPSYR-EGLPRSLLEAMAAGRPVITTDVPGCRELVidGVN-GFLVPPGDVEALADAIEKL 326
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
237-368 2.55e-20

Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.


Pssm-ID: 425737 [Multi-domain]  Cd Length: 158  Bit Score: 88.10  E-value: 2.55e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 237 IKFGFMGRIIPTKGIGVLLKAFKDL----PNESLYIYGNIS-----KTQMRFLQLS-NVKFMGAYNNADINKVLNSIDVL 306
Cdd:pfam00534   3 KIILFVGRLEPEKGLDLLIKAFALLkeknPNLKLVIAGDGEeekrlKKLAEKLGLGdNVIFLGFVSDEDLPELLKIADVF 82
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1705366836 307 IVPSIWlENSPLVIQEAFLSGVVVITSNIGGMNELIGKNE-GFLFKAGDSNDLIKVIKKIKQD 368
Cdd:pfam00534  83 VLPSRY-EGFGIVLLEAMACGLPVIASDVGGPPEVVKDGEtGFLVKPNNAEALAEAIDKLLED 144
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
21-396 1.87e-19

UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. UDP-glucose-diacylglycerol glucosyltransferase (EC 2.4.1.337, UGDG; also known as 1,2-diacylglycerol 3-glucosyltransferase) catalyzes the transfer of glucose from UDP-glucose to 1,2-diacylglycerol forming 3-D-glucosyl-1,2-diacylglycerol.


Pssm-ID: 340844 [Multi-domain]  Cd Length: 372  Bit Score: 90.80  E-value: 1.87e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836  21 VYS-HTLTKELSLNGHKVFVFTriendflqpyTIFDEiiEFKQKNVNpicIRRINKPKDYIYRDKFFDENVEKAFKEYMM 99
Cdd:cd03817    17 ATSvRNLARALEKRGHEVYVIT----------PSDPG--AEDEEEVV---RYRSFSIPIRKYHRQHIPFPFKKAVIDRIK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 100 EINPDIVHFgHlCHLSINL--VHIAKSLGKRIVFTLHDFWlfcvkgqlinqngeicqnpsiencQKCSPY--KPKIQEVK 175
Cdd:cd03817    82 ELGPDIIHT-H-TPFSLGKlgLRIARKLKIPIVHTYHTMY------------------------EDYLHYipKGKLLVKA 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 176 KMFNALKYLRDKIDIFIAPSHTIRNFFIENGVSKS-KIIYQkyGFDTK-----TIIYKRRIFTKNAN-IKFGFMGRIIPT 248
Cdd:cd03817   136 VVRKLVRRFYNHTDAVIAPSEKIKDTLREYGVKGPiEVIPN--GIDLDkfekpLNTEERRKLGLPPDePILLYVGRLAKE 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 249 KGIGVLLKAFKDLPNES---LYIYGNIS-----KTQMRFLQLS-NVKFMGAYNNADINKVLNSIDVLIVPSIwLENSPLV 319
Cdd:cd03817   214 KNIDFLLRAFAELKKEPnikLVIVGDGPereelKELARELGLAdKVIFTGFVPREELPEYYKAADLFVFAST-TETQGLV 292
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1705366836 320 IQEAFLSGVVVITSNIGGMNELI--GKNeGFLFKAGDSNdLIKVIKKIKQDCRILNTIKDNRHKVDSIQTDAKKILKIY 396
Cdd:cd03817   293 YLEAMAAGLPVVAAKDPAASELVedGEN-GFLFEPNDET-LAEKLLHLRENLELLRKLSKNAEISAREFAFAKSVEKLY 369
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
100-368 3.37e-19

putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Escherichia coli WcaC has been predicted to function in colanic acid biosynthesis. WcfI in Bacteroides fragilis has been shown to be involved in the capsular polysaccharide biosynthesis.


Pssm-ID: 340851 [Multi-domain]  Cd Length: 364  Bit Score: 90.08  E-value: 3.37e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 100 EINPDIVHFgHLCHLSI-NLVHIAK-SLGKRIVFTLHDFWLF---CVKGQLINQNGEICQnpsieNCQKCSPYKP-KIQE 173
Cdd:cd03825    49 FIEADIIHL-HWIHGGYlSLKALFKlLRRKPVVWTLHDMWPFtggCHYPMECEGWKTGCG-----NCPNLNSYPPaKKDL 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 174 VKKMFNALKYLRDKIDIFI-APSHTIRNFFIENGV-SKSKIIYQKYGFDT-------KTIIYKRRIFTKNAN-IKFGFMG 243
Cdd:cd03825   123 SRQLFRRKREALAKKRLTIvAPSRWLADMVRRSPLlKGLPVVVIPNGIDTeifapvdKAKARKRLGIPQDKKvILFGAES 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 244 RIIPTKGIGVL---LKAFKDLPNESLYIYGNISKTqmRFLQLSNVKFMGAYNN----ADInkvLNSIDVLIVPSIwLENS 316
Cdd:cd03825   203 VTKPRKGFDELieaLKLLATKDDLLLVVFGKNDPQ--IVILPFDIISLGYIDDdeqlVDI---YSAADLFVHPSL-ADNL 276
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1705366836 317 PLVIQEAFLSGVVVITSNIGGMNELIGKNE-GFLFKAGDSNDLIKVIKKIKQD 368
Cdd:cd03825   277 PNTLLEAMACGTPVVAFDTGGSPEIVQHGVtGYLVPPGDVQALAEAIEWLLAN 329
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
238-368 3.56e-19

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 84.49  E-value: 3.56e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 238 KFGFMGRIIP-TKGIGVLLKAFKDLPNES----LYIYGNISKTQMRFLQL---SNVKFMGAYNnaDINKVLNSIDVLIVP 309
Cdd:pfam13692   3 VILFVGRLHPnVKGVDYLLEAVPLLRKRDndvrLVIVGDGPEEELEELAAgleDRVIFTGFVE--DLAELLAAADVFVLP 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1705366836 310 SIWlENSPLVIQEAFLSGVVVITSNIGGMNELIGKNEGFLFKAGDSNDLIKVIKKIKQD 368
Cdd:pfam13692  81 SLY-EGFGLKLLEAMAAGLPVVATDVGGIPELVDGENGLLVPPGDPEALAEAILRLLED 138
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
415-558 1.78e-17

Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, chromosome partitioning, Coenzyme transport and metabolism];


Pssm-ID: 440301 [Multi-domain]  Cd Length: 159  Bit Score: 79.95  E-value: 1.78e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 415 RITIDTNPdTCNFRCKMCdthsiYNKHFKKLRPDMSLDILNKTLLESKQMKVSEIIPTtMGEPMLYKYFDTIVDFCLQND 494
Cdd:COG0535     1 RLQIELTN-RCNLRCKHC-----YADAGPKRPGELSTEEAKRILDELAELGVKVVGLT-GGEPLLRPDLFELVEYAKELG 73
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1705366836 495 IKLNLTTNGSqLFNKKYnVKYIKNKllpALSDIKISFNSLDYAVNEEIMRNTNTRD-VLAKIERL 558
Cdd:COG0535    74 IRVNLSTNGT-LLTEEL-AERLAEA---GLDHVTISLDGVDPETHDKIRGVPGAFDkVLEAIKLL 133
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
4-355 1.97e-17

Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Staphylococcus aureus CapJ may be involved in capsule polysaccharide biosynthesis. WlbH in Bordetella parapertussis has been shown to be required for the biosynthesis of a trisaccharide that, when attached to the B. pertussis lipopolysaccharide (LPS) core (band B), generates band A LPS.


Pssm-ID: 340828 [Multi-domain]  Cd Length: 376  Bit Score: 84.74  E-value: 1.97e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836   4 ILKIIHGFPPDFMAGSEVYSHTLTKELSLNGHKVFVFTriendFLQPYTIFDEIIEFKQKNVNPICIRR---INKPKDYi 80
Cdd:cd03798     1 VLILTNIYPNANSPGRGIFVRRQVRALSRRGVDVEVLA-----PAPWGPAAARLLRKLLGEAVPPRDGRrllPLKPRLR- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836  81 YRDKFFDENVeKAFKEYMMEINPDIVHfGHLCHLSINLVHI-AKSLGKRIVFTLHdfwlfcvkGQLINQNgeicqnpsie 159
Cdd:cd03798    75 LLAPLRAPSL-AKLLKRRRRGPPDLIH-AHFAYPAGFAAALlARLYGVPYVVTEH--------GSDINVF---------- 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 160 ncqkcSPYK-PKIQEVKKMFNALKYlrdkidifIAPSHTIRNFFIENGVSKSKIIYQKYGFDTKTIIYKRRIFTKNAN-I 237
Cdd:cd03798   135 -----PPRSlLRKLLRWALRRAARV--------IAVSKALAEELVALGVPRDRVDVIPNGVDPARFQPEDRGLGLPLDaF 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 238 KFGFMGRIIPTKGIGVLLKAFKDL----PNESLYIYGNIS-----KTQMRFLQL-SNVKFMGAYNNADINKVLNSIDVLI 307
Cdd:cd03798   202 VILFVGRLIPRKGIDLLLEAFARLakarPDVVLLIVGDGPlrealRALAEDLGLgDRVTFTGRLPHEQVPAYYRACDVFV 281
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1705366836 308 VPSiWLENSPLVIQEAFLSGVVVITSNIGGMNELIGKNE-GFLFKAGDS 355
Cdd:cd03798   282 LPS-RHEGFGLVLLEAMACGLPVVATDVGGIPEVVGDPEtGLLVPPGDA 329
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
3-387 2.43e-17

family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most closely related to the GT1 family of glycosyltransferases. WabH in Klebsiella pneumoniae has been shown to transfer a GlcNAc residue from UDP-GlcNAc onto the acceptor GalUA residue in the cellular outer core.


Pssm-ID: 340839 [Multi-domain]  Cd Length: 351  Bit Score: 84.33  E-value: 2.43e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836   3 KILKIIHGFPpdfMAGSEVYSHTLTKELSLNGHKVFVFTRiendflqpytiFDEIIEFKQKNVNpicIRRINKPKDYIYR 82
Cdd:cd03811     1 KILFVIPSLS---GGGAERVLLNLANALDKRGYDVTLVLL-----------RDEGDLDKQLNGD---VKLIRLLIRVLKL 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836  83 DKFFDENVEKAFKEYMMEINPDIVHfgHLCHLSINLVHIAKSLGKRIVFTLHDfwlfcvkgqlinqngeicqnpsiencq 162
Cdd:cd03811    64 IKLGLLKAILKLKRILKRAKPDVVI--SFLGFATYIVAKLAAARSKVIAWIHS--------------------------- 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 163 kcspYKPKIQEVKKMFNALKYLRDKIDIFIAPSHTIRNFFIENGV---SKSKIIYQkyGFDTKTIIYKRRI---FTKNAN 236
Cdd:cd03811   115 ----SLSKLYYLKKKLLLKLKLYKKADKIVCVSKGIKEDLIRLGPsppEKIEVIYN--PIDIDRIRALAKEpilNEPEDG 188
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 237 IKFGFMGRIIPTKGIGVLLKAFKDL----PNESLYIYGNIS-----KTQMRFLQLSN-VKFMGAYNNadINKVLNSIDVL 306
Cdd:cd03811   189 PVILAVGRLDPQKGHDLLIEAFAKLrkkyPDVKLVILGDGPlreelEKLAKELGLAErVIFLGFQSN--PYPYLKKADLF 266
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 307 IVPSIWlENSPLVIQEAFLSGVVVITSNIGGMNELIGKNE-GFLFKAGDSNDLIKVIKKIKQDCRILNTIKDNRHKVDSI 385
Cdd:cd03811   267 VLSSRY-EGFPNVLLEAMALGTPVVSTDCPGPREILDDGEnGLLVPDGDAAALAGILAALLQKKLDAALRERLAKAQEAV 345

                  ..
gi 1705366836 386 QT 387
Cdd:cd03811   346 FR 347
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
242-401 1.20e-16

Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 76.57  E-value: 1.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 242 MGRIIPTKGIGVLLKAFkdlpneslyiygnisktqmrflqlsnvkfmgaynnadinkvLNSIDVLIVPSIWlENSPLVIQ 321
Cdd:COG0438     1 MGRLVPRKGLDLLLEAL-----------------------------------------LAAADVFVLPSRS-EGFGLVLL 38
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 322 EAFLSGVVVITSNIGGMNELIGKNE-GFLFKAGDSNDLIKVIKKIKQDCRILNTIKDN-RHKVD---SIQTDAKKILKIY 396
Cdd:COG0438    39 EAMAAGLPVIATDVGGLPEVIEDGEtGLLVPPGDPEALAEAILRLLEDPELRRRLGEAaRERAEerfSWEAIAERLLALY 118

                  ....*
gi 1705366836 397 YSLIE 401
Cdd:COG0438   119 EELLA 123
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
98-397 1.66e-16

Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbnK in Shigella dysenteriae has been shown to be involved in the type 7 O-antigen biosynthesis.


Pssm-ID: 340836 [Multi-domain]  Cd Length: 362  Bit Score: 81.98  E-value: 1.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836  98 MMEINPDIVH--FGHLCHLSInlvhIAKSL--GKRIVFTLHDFWlfcvkgqlinqngeicqnpsiencqkCSPYKPKIqe 173
Cdd:cd03807    75 IRKRNPDVVHtwMYHADLIGG----LAAKLagGVKVIWSVRSSN--------------------------IPQRLTRL-- 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 174 vkKMFNALKyLRDKIDIFIAPSHTIRNFFIENGVSKSKIIYQKYGFDT--------KTIIYKRRIFTKNANIKFGFMGRI 245
Cdd:cd03807   123 --VRKLCLL-LSKFSPATVANSSAVAEFHQEQGYAKNKIVVIYNGIDLfklspddaSRARARRRLGLAEDRRVIGIVGRL 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 246 IPTKGIGVLLKAFKDL----PNESLYIYGN-ISKTQMRFLQLS-----NVKFMGayNNADINKVLNSIDVLIVPSIWlEN 315
Cdd:cd03807   200 HPVKDHSDLLRAAALLvethPDLRLLLVGRgPERPNLERLLLElgledRVHLLG--ERSDVPALLPAMDIFVLSSRT-EG 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 316 SPLVIQEAFLSGVVVITSNIGGMNELIGKNEGFLFKAGDSNDLIKVIKKIKQDCRILNTIKDN-RHKVD---SIQTDAKK 391
Cdd:cd03807   277 FPNALLEAMACGLPVVATDVGGAAELVDDGTGFLVPAGDPQALADAIRALLEDPEKRARLGRAaRERIAnefSIDAMVRR 356

                  ....*.
gi 1705366836 392 ILKIYY 397
Cdd:cd03807   357 YETLYY 362
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
103-358 1.76e-15

glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to glycosyltransferase family 4 (GT4). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


Pssm-ID: 340860 [Multi-domain]  Cd Length: 365  Bit Score: 78.65  E-value: 1.76e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 103 PDIVHfGHLCHLSINLVHIAKSLGKRIVFTLHDFwlfcvkgqlinqngEICQNPSIENCQKCSPYKPKIQEvkkmfnalK 182
Cdd:cd05844    82 PALVH-AHFGRDGVYALPLARALGVPLVVTFHGF--------------DITTSRAWLAASPGWPSQFQRHR--------R 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 183 YLRDKIDIFIAPSHTIRNFFIENGVSKSKIIYQKYGFDTKTIIYKRRiftKNANIKFGFMGRIIPTKGIGVLLKAFKDL- 261
Cdd:cd05844   139 ALQRPAALFVAVSGFIRDRLLARGLPAERIHVHYIGIDPAKFAPRDP---AERAPTILFVGRLVEKKGCDVLIEAFRRLa 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 262 ---PNESLYIYGN---ISKTQMRFLQLSNVKFMGAYNNADINKVLNSIDVLIVPSIW-----LENSPLVIQEAFLSGVVV 330
Cdd:cd05844   216 arhPTARLVIAGDgplRPALQALAAALGRVRFLGALPHAEVQDWMRRAEIFCLPSVTaasgdSEGLGIVLLEAAACGVPV 295
                         250       260
                  ....*....|....*....|....*....
gi 1705366836 331 ITSNIGGMNELIGKNE-GFLFKAGDSNDL 358
Cdd:cd05844   296 VSSRHGGIPEAILDGEtGFLVPEGDVDAL 324
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
3-378 2.14e-15

Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. WbuB in E. coli is involved in the biosynthesis of the O26 O-antigen. It has been proposed to function as an N-acetyl-L-fucosamine (L-FucNAc) transferase.


Pssm-ID: 340825 [Multi-domain]  Cd Length: 391  Bit Score: 78.92  E-value: 2.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836   3 KILKIIHGFPPDfMAGSEVYSHTLTKELSLNGHKVFVFTRIENDFLQPytIFDEIIEFKQkNVNPICIRRInkpkdYIYR 82
Cdd:cd03794     1 KILLISQYYPPP-KGAAAARVYELAKELVRRGHEVTVLTPSPNYPLGR--IFAGATETKD-GIRVIRVKLG-----PIKK 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836  83 DKFFDENVE------KAFKEYMMEI-NPDIVHFGHLCHLSINLVH-IAKSLGKRIVFTLHDFWLFCVKGQLINQNGeicq 154
Cdd:cd03794    72 NGLIRRLLNylsfalAALLKLLVREeRPDVIIAYSPPITLGLAALlLKKLRGAPFILDVRDLWPESLIALGVLKKG---- 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 155 npsiencqkcSPYKpkiqevkkmfnALKYLRDKI----DIFIAPSHTIRNFFIENGVSKSKIIYQKYGFDTKTIIYKRRI 230
Cdd:cd03794   148 ----------SLLK-----------LLKKLERKLyrlaDAIIVLSPGLKEYLLRKGVPKEKIIVIPNWADLEEFKPPPKD 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 231 -----FTKNANIKFGFMGRIIPTKGIGVLLKAFKDLPNES-----LYIYGNISKTQMRF---LQLSNVKFMGAYNNADIN 297
Cdd:cd03794   207 elrkkLGLDDKFVVVYAGNIGKAQGLETLLEAAERLKRRPdirflFVGDGDEKERLKELakaRGLDNVTFLGRVPKEEVP 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 298 KVLNSIDVLIVP----SIWLENSPLVIQEAFLSGVVVITSNIGGMNELIGKNE-GFLFKAGDSNDLIKVIKKIKQDCRIL 372
Cdd:cd03794   287 ELLSAADVGLVPlkdnPANRGSSPSKLFEYMAAGKPILASDDGGSDLAVEINGcGLVVEPGDPEALADAILELLDDPELR 366

                  ....*.
gi 1705366836 373 NTIKDN 378
Cdd:cd03794   367 RAMGEN 372
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
4-366 1.50e-14

Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 family of glycosyltransferases. WavL in Vibrio cholerae has been shown to be involved in the biosynthesis of the lipopolysaccharide core.


Pssm-ID: 340846 [Multi-domain]  Cd Length: 345  Bit Score: 75.47  E-value: 1.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836   4 ILKIIHGFPpdfMAGSEVYSHTLTKELSLNGHKVFVFTrIENDFLQPYTIFDEIIEFKQKNvnpicIRRINKPKDYIYRd 83
Cdd:cd03819     1 ILMLTPALE---IGGAETYILDLARALAERGHRVLVVT-AGGPLLPRLRQIGIGLPGLKVP-----LLRALLGNVRLAR- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836  84 kffdenvekafkeYMMEINPDIVHfghlCH-----LSINLVhiAKSLGKRIVFTLHDFWLFcvkgqlinqngeicqnpsi 158
Cdd:cd03819    71 -------------LIRRERIDLIH----AHsrapaWLGWLA--SRLTGVPLVTTVHGSYLA------------------- 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 159 encqkcsPYKPKIQEVKKMFNAlkylrdkiDIFIAPSHTIRNFFIEN-GVSKSKIIYQKYGFDTK------TIIYKRRIF 231
Cdd:cd03819   113 -------TYHPKDFALAVRARG--------DRVIAVSELVRDHLIEAlGVDPERIRVIPNGVDTDrfppeaEAEERAQLG 177
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 232 TKNANIKFGFMGRIIPTKGIGVLLKA---FKDLPNESLYIYGNIS-----KTQMRFLQLSN-VKFMGayNNADINKVLNS 302
Cdd:cd03819   178 LPEGKPVVGYVGRLSPEKGWLLLVDAaaeLKDEPDFRLLVAGDGPerdeiRRLVERLGLRDrVTFTG--FREDVPAALAA 255
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1705366836 303 IDVLIVPSIWlENSPLVIQEAFLSGVVVITSNIGGMNELIGKNE-GFLFKAGDSNDLIKVIKKIK 366
Cdd:cd03819   256 SDVVVLPSLH-EEFGRVALEAMACGTPVVATDVGGAREIVVHGRtGLLVPPGDAEALADAIRAAK 319
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
18-212 3.65e-12

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 65.25  E-value: 3.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836  18 GSEVYSHTLTKELSLNGHKVFVFTRIENDFLqpytifdeiiEFKQKNVNPICIRRINKPKDYIYRDKFFdenveKAFKEY 97
Cdd:pfam13439   2 GVERYVLELARALARRGHEVTVVTPGGPGPL----------AEEVVRVVRVPRVPLPLPPRLLRSLAFL-----RRLRRL 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836  98 MMEINPDIVHFGHLCHLSINLVHIAKSLGKRIVFTLHDFWLFcvkgqlinqngeicqnpsiencqkCSPYKPKIQEVKKM 177
Cdd:pfam13439  67 LRRERPDVVHAHSPFPLGLAALAARLRLGIPLVVTYHGLFPD------------------------YKRLGARLSPLRRL 122
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1705366836 178 FNAL-KYLRDKIDIFIAPSHTIRNFFIEN-GVSKSKI 212
Cdd:pfam13439 123 LRRLeRRLLRRADRVIAVSEAVADELRRLyGVPPEKI 159
GT4_AmsK-like cd03799
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ...
171-360 5.04e-12

Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases found specifically in certain bacteria. AmsK in Erwinia amylovora, has been reported to be involved in the biosynthesis of amylovoran, a exopolysaccharide acting as a virulence factor.


Pssm-ID: 340829 [Multi-domain]  Cd Length: 350  Bit Score: 67.86  E-value: 5.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 171 IQEVKKMFNalkYLRDKIDIFIAPSHTIRNFFIENGVSKSKIIYQKYGFDTKTIIYKRRIFTKNANIKFGFMGRIIPTKG 250
Cdd:cd03799   112 ILEGNKVYP---QLFAQGDLFLPNCELFKHRLIALGCDEKKIIVHRSGIDCNKFRFKPRYLPLDGKIRILTVGRLTEKKG 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 251 IGVLLKAFKDLPNEslyiYGNIS-------------KTQMRFLQLSN-VKFMGAYNNADINKVLNSIDVLIVPSIW---- 312
Cdd:cd03799   189 LEYAIEAVAKLAQK----YPNIEyqiigdgdlkeqlQQLIQELNIGDcVKLLGWKPQEEIIEILDEADIFIAPSVTaadg 264
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1705366836 313 -LENSPLVIQEAFLSGVVVITSNIGGMNELIGKN-EGFLFKAGDSNDLIK 360
Cdd:cd03799   265 dQDGPPNTLKEAMAMGLPVISTEHGGIPELVEDGvSGFLVPERDAEAIAE 314
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
175-350 7.86e-12

glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


Pssm-ID: 340816 [Multi-domain]  Cd Length: 235  Bit Score: 65.89  E-value: 7.86e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 175 KKMFNALKYLRDKIDIFIAPSHtirNFFIENGVSKSKIIYQKYGF---DTKTIIYKRRIFTKNANIKFG-------FMGR 244
Cdd:cd01635    42 ALRRILKKLLELKPDVVHAHSP---HAAALAALLAARLLGIPIVVtvhGPDSLESTRSELLALARLLVSlpladkvSVGR 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 245 IIPTKGIGVLLKAFKDLPNE----SLYIYGN------ISKTQMRFLQLSNVKFMGAY-NNADINKVLNSIDVLIVPSIWl 313
Cdd:cd01635   119 LVPEKGIDLLLEALALLKARlpdlVLVLVGGggereeEEALAAALGLLERVVIIGGLvDDEVLELLLAAADVFVLPSRS- 197
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1705366836 314 ENSPLVIQEAFLSGVVVITSNIGGMNELIGKNE-GFLF 350
Cdd:cd01635   198 EGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGEnGLLV 235
AslB COG0641
Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, ...
425-723 4.11e-11

Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440406 [Multi-domain]  Cd Length: 349  Bit Score: 65.01  E-value: 4.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 425 CNFRCKMCdthsIYNKHFKKLRPDMSLDILNKTL--LESKQMKVSEIiptTM----GEPML-YKYFDTIVDFCLQN---- 493
Cdd:COG0641    11 CNLRCSYC----YYSEGDEGSRRRMSEETAEKAIdfLIESSGPGKEL---TItffgGEPLLnFDFIKEIVEYARKYakkg 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 494 -DIKLNLTTNGSqLFNKKYnVKYIKNKllpalsDIKISFnSLDYavNEEI---MRNTNT-----RDVLAKIERLCSMRdk 564
Cdd:COG0641    84 kKIRFSIQTNGT-LLDDEW-IDFLKEN------GFSVGI-SLDG--PKEIhdrNRVTKNgkgsfDRVMRNIKLLKEHG-- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 565 ffprVSITLQMTFMKSNIDSIKPIIEYAIKHKINRIkghQLWITHKELENEAIYKDKEFIELWNELV-LSLERYKDDIRL 643
Cdd:COG0641   151 ----VEVNIRCTVTRENLDDPEELYDFLKELGFRSI---QFNPVVEEGEADYSLTPEDYGEFLIELFdEWLERDGGKIFV 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 644 ENFTPIQDS--TKAKGKCPFLGQELW-VNYRGDISVCcapdKQRASLGDF--GNITHISLDKVISSAKYRNLVKHYPK-- 716
Cdd:COG0641   224 REFDILLAGllPPCSSPCVGAGGNYLvVDPDGDIYPC----DEFVGDPEFrlGNVFDGSLAELLDSPKLRAFGREKNVll 299

                  ....*..
gi 1705366836 717 MEVCQKC 723
Cdd:COG0641   300 DEECRSC 306
N_Twi_rSAM NF033640
twitch domain-containing radical SAM protein; Members of this family are unusual among radical ...
424-598 7.11e-11

twitch domain-containing radical SAM protein; Members of this family are unusual among radical SAM proteins in several ways. First, the N-terminal region consists of an iron-sulfur cluster-binding twitch domain (half of a SPASM domain), something usually found C-terminal to the radical SAM domain. Second, the radical SAM domains in many of the members of this family score poorly vs. the Pfam HMM, PF04055 (version 19), used to identify radical SAM. Lastly, the majority of members sequenced to date come from uncultured bacteria from marine or aquifer sources rather than from conventionally cultured bacterial isolates. The function is unknown.


Pssm-ID: 468123 [Multi-domain]  Cd Length: 396  Bit Score: 64.60  E-value: 7.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 424 TCNFRCKMCDTH--SIYNKHFKKLRPDMSLDILNKTLLESKQM--KVSEIIPTTM------GEPMLYKYFDTIVDFCLQN 493
Cdd:NF033640  119 LCNLKCRMCGPHssSSWAKEAKKLGGPKLGDKKKISWFEDEEFwkWLEELLPSLKeiyfagGEPLLIKEHYKLLEKLVEK 198
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 494 ----DIKLNLTTNGSQLFNKKYNVKyiknKLLPALSDIKISFnSLD--YAVNEEIMRNTNTRDVLAKIERLcsmrDKFFP 567
Cdd:NF033640  199 grakNIELRYNTNLTVLPDKLKDLL----DLWKKFKSVSISA-SIDgvGERNEYIRYGSKWDEIEKNLKKL----KEECP 269
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1705366836 568 RVSITLQMTFMKSNIDSIKPIIEYAIKHKIN 598
Cdd:NF033640  270 NVELRINPTVSALNVLHLPELLDWLLELGLG 300
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
240-412 7.46e-11

glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria, while some of them are also found in Archaea and eukaryotes.


Pssm-ID: 340841 [Multi-domain]  Cd Length: 474  Bit Score: 65.05  E-value: 7.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 240 GFMGRIIPTKGIGVLLKAFK----DLPNESLYI---------YGNISKTQMRFLQLSN-VKFMGAYNNADinkVLNSIDV 305
Cdd:cd03813   297 GLVGRVVPIKDVKTFIRAFKlvrrAMPDAEGWLigpededpeYAQECKRLVASLGLENkVKFLGFQNIKE---YYPKLGL 373
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 306 LIVPSIwLENSPLVIQEAFLSGVVVITSNIGGMNELIGKNEGFLFKAG------DSNDLIKVIKKIKQDcrilntiKDNR 379
Cdd:cd03813   374 LVLTSI-SEGQPLVILEAMASGVPVVATDVGSCRELIYGADDALGQAGlvvppaDPEALAEALIKLLRD-------PELR 445
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1705366836 380 HkvdSIQTDAKKILKIYYSLiekDKNIDlqQYK 412
Cdd:cd03813   446 Q---AFGEAGRKRVEKYYTL---EGMID--SYR 470
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
22-368 2.07e-10

glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. MtfB (mannosyltransferase B) in E. coli has been shown to direct the growth of the O9-specific polysaccharide chain. It transfers two mannoses into the position 3 of the previously synthesized polysaccharide.


Pssm-ID: 340838 [Multi-domain]  Cd Length: 362  Bit Score: 63.15  E-value: 2.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836  22 YSHTLTKELSLNGHKVFVFTriendfLQPYTIFDEIIEFKQKNVNPICIRRinKPKDYIYRDKFFDENVEKAFKeymmei 101
Cdd:cd03809    19 YTRELLKALAKNDPDESVLA------VPPLPGELLRLLREYPELSLGVIKI--KLWRELALLRWLQILLPKKDK------ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 102 nPDIVHfghlcHLSINLVHIAKslGKRIVFTLHDFWLFcvkgqlinqngeicqnpsiencqkcspYKPKIqevkKMFNAL 181
Cdd:cd03809    85 -PDLLH-----SPHNTAPLLLK--GCPQVVTIHDLIPL---------------------------RYPEF----FPKRFR 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 182 KYLRDKI-------DIFIAPSHTIRN----FFienGVSKSKI--IYQkyGFDT-KTIIYKRRIFTKNANIKFGFM---GR 244
Cdd:cd03809   126 LYYRLLLpislrraDAIITVSEATRDdiikFY---GVPPEKIvvIPL--GVDPsFFPPESAAVLIAKYLLPEPYFlyvGT 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 245 IIPTKGIGVLLKAFKDLPNES----LYIYG-------NISKTQMRFLQLSNVKFMGAYNNADINKVLNSIDVLIVPSIWl 313
Cdd:cd03809   201 LEPRKNHERLLKAFALLKKQGgdlkLVIVGgkgwedeELLDLVKKLGLGGRVRFLGYVSDEDLPALYRGARAFVFPSLY- 279
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1705366836 314 ENSPLVIQEAFLSGVVVITSNIGGMNElIGKNEGFLFKAGDSNDLIKVIKKIKQD 368
Cdd:cd03809   280 EGFGLPVLEAMACGTPVIASNISVLPE-VAGDAALYFDPLDPESIADAILRLLED 333
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
160-368 1.38e-09

amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. AmSD in Erwinia amylovora has been shown to be involved in the biosynthesis of amylovoran, the acidic exopolysaccharide acting as a virulence factor. This enzyme may be responsible for the formation of galactose alpha-1,6 linkages in amylovoran.


Pssm-ID: 340847 [Multi-domain]  Cd Length: 351  Bit Score: 60.33  E-value: 1.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 160 NCQKCSPYKPKIQEVKKMFNALKYLRD-KIDIFIAPSHTIRNFFIENGvSKSKII------YQKYGFDTKTIIYKRRIFT 232
Cdd:cd03820    59 GDRKYSHFKLLLKYFKKVRRLRKYLKNnKPDVVISFRTSLLTFLALIG-LKSKLIvwehnnYEAYNKGLRRLLLRRLLYK 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 233 K-------------------NANI---------------------KFGFMGRIIPTKGIGVLLKAFKDLPNE----SLYI 268
Cdd:cd03820   138 RadkivvlteadklkkykqpNSNVvvipnplsfpseepstnlkskRILAVGRLTYQKGFDLLIEAWALIAKKhpdwKLRI 217
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 269 YGN-----ISKTQMRFLQLSN-VKFMGAYNNadINKVLNSIDVLIVPSIWlENSPLVIQEAFLSGVVVITSNI-GGMNEL 341
Cdd:cd03820   218 YGDgpereELEKLIDKLGLEDrVKLLGPTKN--IAEEYANSSIFVLSSRY-EGFPMVLLEAMAYGLPIISFDCpTGPSEI 294
                         250       260
                  ....*....|....*....|....*...
gi 1705366836 342 IGKNE-GFLFKAGDSNDLIKVIKKIKQD 368
Cdd:cd03820   295 IEDGEnGLLVPNGDVDALAEALLRLMED 322
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
177-359 1.62e-08

glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family of glycosyltransferases and includes a sequence annotated as alpha-D-mannose-alpha(1-6)phosphatidyl myo-inositol monomannoside transferase from Bacillus halodurans. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes.


Pssm-ID: 340842 [Multi-domain]  Cd Length: 365  Bit Score: 57.30  E-value: 1.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 177 MFNALKYLRDKIDIFIAPSHTIRNFFIENGVSKskIIYQKYGFDTKTI------IYKRRIFTKNANIKFGFMGRIIPTKG 250
Cdd:cd03814   135 AWAYLRWFHNPFDTTLVPSPSIARELEGHGFER--VRLWPRGVDTELFhpsrrdAALRRRLGPPGRPLLLYVGRLAPEKN 212
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 251 IGVLLKAFKDLPNE---SLYIYG-NISKTQMRFlQLSNVKFMGAYNNADINKVLNSIDVLIVPSIwLENSPLVIQEAFLS 326
Cdd:cd03814   213 LEALLDADLPLAASppvRLVVVGdGPARAELEA-RGPDVIFTGFLTGEELARAYASADVFVFPSR-TETFGLVVLEAMAS 290
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1705366836 327 GVVVITSNIGGMNELIGKNE-GFLFKAGDSNDLI 359
Cdd:cd03814   291 GLPVVAADAGGPRDIVRPGGtGALVEPGDAAAFA 324
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
285-396 2.15e-08

N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria, while some of them are also found in Archaea and eukaryotes.


Pssm-ID: 340859 [Multi-domain]  Cd Length: 370  Bit Score: 56.98  E-value: 2.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 285 VKFMGayNNADINKVLNSIDVLIVPSiWLENSPLVIQEAFLSGVVVITSNIGGMNELIGKNE-GFLFKAGDSNDLIKVIK 363
Cdd:cd04962   254 VLFLG--KQDDVEELLSIADLFLLPS-EKESFGLAALEAMACGVPVVSSNAGGIPEVVKHGEtGFLSDVGDVDAMAKSAL 330
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1705366836 364 KIKQDCRILNTIKDNRHKVDSIQTDAKKILKIY 396
Cdd:cd04962   331 SILEDDELYNRMGRAARKRAAERFDPERIVPQY 363
Tyw1 COG0731
Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily [Translation, ribosomal ...
418-592 2.49e-08

Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily [Translation, ribosomal structure and biogenesis]; Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440495 [Multi-domain]  Cd Length: 248  Bit Score: 55.58  E-value: 2.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 418 IDTNPD-TCNFRCKMC---DTHSIYNKHFKKLRPDmslDILNKtlLESKQMKVSEIIPTTM-------GEPMLYKYFDTI 486
Cdd:COG0731    26 INLIPNkTCNFDCVYCqrgRTTDLTRERREFDDPE---EILEE--LIEFLRKLPEEAREPDhitfsgsGEPTLYPNLGEL 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 487 VDFCLQ-NDIKLNLTTNGSQLFNKKynvkyIKNKLLPAlsDIkISFnSLDyAVNEEIMR---NTNTRDVLAKI-ERLCSM 561
Cdd:COG0731   101 IEEIKKlRGIKTALLTNGSLLHRPE-----VREELLKA--DQ-VYP-SLD-AADEETFRkinRPHPGLSWERIiEGLELF 170
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1705366836 562 RDKFFPRvsITLQMTFMKSNIDSIKPIIEYA 592
Cdd:COG0731   171 RKLYKGR--TVIETMLVKGINDSEEELEAYA 199
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
239-370 3.96e-08

UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. aviGT4 in Streptomyces viridochromogenes has been shown to be involved in biosynthesis of oligosaccharide antibiotic avilamycin A. Inactivation of aviGT4 resulted in a mutant that accumulated a novel avilamycin derivative lacking the terminal eurekanate residue.


Pssm-ID: 340832 [Multi-domain]  Cd Length: 333  Bit Score: 55.76  E-value: 3.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 239 FGFMGRIIPTKGIGVLLKAFKDLpNESLYIYGNISKtQMRF------LQLSNVKFMGAYNNADINKVLNSIDVLIVPSIW 312
Cdd:cd03802   172 LAFLGRIAPEKGLEDAIRVARRA-GLPLKIAGKVRD-EDYFyylqepLPGPRIEFIGEVGHDEKQELLGGARALLFPINW 249
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1705366836 313 LENSPLVIQEAFLSGVVVITSNIGGMNELIGKNE-GFLfkAGDSNDLIKVIKKI----KQDCR 370
Cdd:cd03802   250 DEPFGLVMIEAMACGTPVIAYRRGGLPEVIQHGEtGFL--VDSVEEMAEAIANIdridRAACR 310
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
220-381 1.01e-07

Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP-linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes.


Pssm-ID: 340826 [Multi-domain]  Cd Length: 355  Bit Score: 54.59  E-value: 1.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 220 DTKTIIYKRRIFTKNANIK---FGFMGRIIPTKGIGVLLKAFKDLpNESLYIYG-----NISKTQMRFLQLSNVKFMGAY 291
Cdd:cd03795   172 NVYNIPRVDFENIKREKKGkkiFLFIGRLVYYKGLDYLIEAAQYL-NYPIVIGGegplkPDLEAQIELNLLDNVKFLGRV 250
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 292 NNADINKVLNSIDVLIVPSIW-LENSPLVIQEAFLSGVVVITSNIGGMNELIGKN--EGFLFKAGDSNDLIKVIKKIKQD 368
Cdd:cd03795   251 DDEEKVIYLHLCDVFVFPSVLrSEAFGIVLLEAMMCGKPVISTNIGTGVPYVNNNgeTGLVVPPKDPDALAEAIDKLLSD 330
                         170
                  ....*....|...
gi 1705366836 369 CRILNTIKDNRHK 381
Cdd:cd03795   331 EELRESYGENAKK 343
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
175-405 1.49e-07

capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. capH in Staphylococcus aureus has been shown to be required for the biosynthesis of the type 1 capsular polysaccharide (CP1).


Pssm-ID: 340840 [Multi-domain]  Cd Length: 357  Bit Score: 54.22  E-value: 1.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 175 KKMFNALKYLRDKI-DIFIAPSHTI-RNFFIENGVSKSKIIY-----QKYGFDTKTIIYKRRIFTKNANIKFGFMGRIIP 247
Cdd:cd03812   123 KIRKNVLKKLIERLsTKYLACSEDAgEWLFGEVENGKFKVIPngidiEKYKFNKEKRRKRRKLLILEDKLVLGHVGRFNE 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 248 TKGIGVLLKAFKDLPNES----LYIYGNIS-------KTQMRFLQlSNVKFMGAYNnaDINKVLNSIDVLIVPSIWlENS 316
Cdd:cd03812   203 QKNHSFLIDIFEELKKKNpnvkLVLVGEGElkekikeKVKELGLE-DKVIFLGFRN--DVSEILSAMDVFLFPSLY-EGL 278
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 317 PLVIQEAFLSGVVVITSNIGGMNELIGKNEGFLfkagDSNDLIKVIKKikqdcRILNTIKDNRHKVDSIQtDAKKILKIY 396
Cdd:cd03812   279 PLVAVEAQASGLPCLLSDTITKECDITNNVEFL----PLNETPSTWAE-----KILKLIKRKRRINKEIN-KEKKELGYD 348

                  ....*....
gi 1705366836 397 YSLIEKDKN 405
Cdd:cd03812   349 DESLELTLL 357
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
422-590 7.64e-07

Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S cluster and S-adenosylmethionine (SAM) in close proximity. They are characterized by a conserved CxxxCxxC motif, which coordinates the conserved iron-sulfur cluster. Mechanistically, they share the transfer of a single electron from the iron-sulfur cluster to SAM, which leads to its reductive cleavage to methionine and a 5'-deoxyadenosyl radical, which, in turn, abstracts a hydrogen from the appropriately positioned carbon atom. Depending on the enzyme, SAM is consumed during this process or it is restored and reused. Radical SAM enzymes catalyze steps in metabolism, DNA repair, the biosynthesis of vitamins and coenzymes, and the biosynthesis of many antibiotics. Examples are biotin synthase (BioB), lipoyl synthase (LipA), pyruvate formate-lyase (PFL), coproporphyrinogen oxidase (HemN), lysine 2,3-aminomutase (LAM), anaerobic ribonucleotide reductase (ARR), and MoaA, an enzyme of the biosynthesis of molybdopterin.


Pssm-ID: 100105 [Multi-domain]  Cd Length: 204  Bit Score: 50.41  E-value: 7.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 422 PDTCNFRCKMCDTHSIYNKHFKKLRPDMSLDILnktLLESKQMKVSEIIpTTMGEPMLYKYF-DTIVDFC-LQNDIKLNL 499
Cdd:cd01335     4 TRGCNLNCGFCSNPASKGRGPESPPEIEEILDI---VLEAKERGVEVVI-LTGGEPLLYPELaELLRRLKkELPGFEISI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 500 TTNGSQLFNKkynvkyIKNKLLPALSDIK-ISFNSLDYAVNEEIMRNTNT-RDVLAKIERLCSMRDKFFPRVSITLQMTF 577
Cdd:cd01335    80 ETNGTLLTEE------LLKELKELGLDGVgVSLDSGDEEVADKIRGSGESfKERLEALKELREAGLGLSTTLLVGLGDED 153
                         170
                  ....*....|...
gi 1705366836 578 MKSNIDSIKPIIE 590
Cdd:cd01335   154 EEDDLEELELLAE 166
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
425-573 9.72e-07

Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual methylations, isomerization, sulphur insertion, ring formation, anaerobic oxidation and protein radical formation.


Pssm-ID: 427681 [Multi-domain]  Cd Length: 159  Bit Score: 49.06  E-value: 9.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 425 CNFRCKMCDTHSIynkHFKKLRPDMSLDILNKTLLESKQMKVSEIIpTTMGEPMLYKYFDTIVDFCLQ----NDIKLNLT 500
Cdd:pfam04055   5 CNLRCTYCAFPSI---RARGKGRELSPEEILEEAKELKRLGVEVVI-LGGGEPLLLPDLVELLERLLKlelaEGIRITLE 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1705366836 501 TNGSqLFNKKYnVKYIKNKLLPALSdikISFNSLDYAVNEEIMRNTNTRDVLAKIERLcsmRDKFFPRVSITL 573
Cdd:pfam04055  81 TNGT-LLDEEL-LELLKEAGLDRVS---IGLESGDDEVLKLINRGHTFEEVLEALELL---REAGIPVVTDNI 145
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
64-398 1.65e-06

LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases and is named after WbdM in Escherichia coli. In general glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found in bacteria.


Pssm-ID: 340857 [Multi-domain]  Cd Length: 360  Bit Score: 50.91  E-value: 1.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836  64 NVNPICIRRINKPKDYIYRDKFFDENVEKAF----------KEYMMEINPDIVHfGHLCHLSInLVHIAKslgkrivftl 133
Cdd:cd04951    31 DVNIVYLTGEVEVKPLNNNIIIYNLGMDKNPrsllkallklKKIISAFKPDVVH-SHMFHANI-FARFLR---------- 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 134 hdfwLFCVKGQLInqngeicqnpsiencqkCSPYKPKIQEVKKMF--NALKYLRDK--------IDIFIAPSHTIRN--F 201
Cdd:cd04951    99 ----MLYPIPLLI-----------------CTAHNKNEGGRIRMFiyRLTDFLCDIttnvsreaLDEFIAKKAFSKNksV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 202 FIENGVSKSKIiyqKYGFDTKTIIyKRRIFTKNANIKFGFMGRIIPTKGIGVLLKAFKDL----PNESLYIYG------N 271
Cdd:cd04951   158 PVYNGIDLNKF---KKDINVRLKI-RNKLNLKNDEFVILNVGRLTEAKDYPNLLLAISELilskNDFKLLIAGdgplrnE 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 272 ISKTQMRFLQLSNVKFMGAYnnADINKVLNSIDVLIVPSIWlENSPLVIQEAFLSGVVVITSNIGGMNELIGkNEGFLFK 351
Cdd:cd04951   234 LERLICNLNLVDRVILLGQI--SNISEYYNAADLFVLSSEW-EGFGLVVAEAMACERPVVATDAGGVAEVVG-DHNYVVP 309
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1705366836 352 AGDSNDLIKVIKKIKQDC----RILNTIKDNRHKVDSIQTDAKKILKIYYS 398
Cdd:cd04951   310 VSDPQLLAEKIKEIFDMSdeerDILGNKNEYIAKNFSINTIVNEWERLYSG 360
moaA PRK00164
GTP 3',8-cyclase MoaA;
415-597 3.34e-06

GTP 3',8-cyclase MoaA;


Pssm-ID: 234672 [Multi-domain]  Cd Length: 331  Bit Score: 49.75  E-value: 3.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 415 RITIdTnpDTCNFRCKMCdtHSiyNKHFKKLRPD--MSLDILNKTLLESKQMKVSEI-IptTMGEPMLYKYFDTIVDFC- 490
Cdd:PRK00164   20 RISV-T--DRCNFRCTYC--MP--EGYLPFLPKEelLSLEEIERLVRAFVALGVRKVrL--TGGEPLLRKDLEDIIAALa 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 491 -LQNDIKLNLTTNGSQLfnkkynVKYIKnKLLPA-LSDIKISFNSLDYAVNEEIMRNTNTRDVLAKIERLcsmRDKFFPR 568
Cdd:PRK00164   91 aLPGIRDLALTTNGYLL------ARRAA-ALKDAgLDRVNVSLDSLDPERFKAITGRDRLDQVLAGIDAA---LAAGLTP 160
                         170       180       190
                  ....*....|....*....|....*....|
gi 1705366836 569 VSItlQMTFMKS-NIDSIKPIIEYAIKHKI 597
Cdd:PRK00164  161 VKV--NAVLMKGvNDDEIPDLLEWAKDRGI 188
PelF NF038011
GT4 family glycosyltransferase PelF; Proteins of this family are components of the ...
240-348 7.03e-06

GT4 family glycosyltransferase PelF; Proteins of this family are components of the exopolysaccharide Pel transporter. It has been reported that PelF is a soluble glycosyltransferase that uses UDP-glucose as the substrate for the synthesis of exopolysaccharide Pel, whereas PelG is a Wzx-like and PST family exopolysaccharide transporter.


Pssm-ID: 411604 [Multi-domain]  Cd Length: 489  Bit Score: 49.16  E-value: 7.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 240 GFMGRIIPTKGIGVLLKAF----KDLPNESLYI---------YGNISKTQMRFLQL-SNVKFMGAYNnadINKVLNSIDV 305
Cdd:NF038011  310 GLIGRVVPIKDIKTFIRAMrtvvRAMPEAEGWIvgpeeedpaYAAECRSLVASLGLqDKVKFLGFQK---IDDLLPQVGL 386
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1705366836 306 LIVPSIwLENSPLVIQEAFLSGVVVITSNIGGMNELIgknEGF 348
Cdd:NF038011  387 MVLSSI-SEALPLVVLEAFAAGVPVVTTDVGSCRQLI---EGL 425
SPASM cd21109
Iron-sulfur cluster-binding SPASM domain; This iron-sulfur cluster-binding domain is named ...
659-723 1.01e-05

Iron-sulfur cluster-binding SPASM domain; This iron-sulfur cluster-binding domain is named SPASM after the biochemically characterized members, AlbA, PqqE, anSME, and MftC, which are involved in Subtilosin A, Pyrroloquinoline quinone, Anaerobic Sulfatase, and Mycofactocin maturation, respectively. SPASM occurs as an additional C-terminal domain in many peptide-modifying enzymes of the radical S-adenosylmethionine (SAM) superfamily. Radical SAM enzymes are characterized by a conserved CxxxCxxC motif, which coordinates the conserved iron-sulfur cluster that is involved in the reductive cleavage of SAM and generates a 5'-deoxyadenosyl radical, which in turn abstracts a hydrogen from the appropriately positioned carbon atom of the substrate. Radical SAM enzymes with a C-terminal SPASM domain contain at least one other iron-sulfur cluster.


Pssm-ID: 410609 [Multi-domain]  Cd Length: 65  Bit Score: 43.57  E-value: 1.01e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1705366836 659 CPFLGQELWVNYRGDISVCCAPDKQRASLgdfGNITHISLDKVISSAKYRNLVK--HYPKMEVCQKC 723
Cdd:cd21109     2 CPAPWTSLYITPDGDVYPCCFDVNEELKL---GNIREQSLKEIWNSEKYREFRKllLDGKIKLCKNC 65
SPASM pfam13186
Iron-sulfur cluster-binding domain; This domain occurs as an additional C-terminal iron-sulfur ...
659-723 6.48e-05

Iron-sulfur cluster-binding domain; This domain occurs as an additional C-terminal iron-sulfur cluster binding domain in many radical SAM domain, pfam04055 proteins. The domain occurs in a number of proteins that modify a protein to become an active enzyme, or a peptide to become a ribosomal natural product. The domain is named SPASM because it occurs in the maturases of Subilitosin, PQQ, Anaerobic Sulfatases, and Mycofactocin.


Pssm-ID: 433020 [Multi-domain]  Cd Length: 66  Bit Score: 41.31  E-value: 6.48e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1705366836 659 CPFLGQELWVNYRGDISVCcaPDKQRASLGDFGNITHISLDKVISSAKYRNL--VKHYPKMEVCQKC 723
Cdd:pfam13186   1 CFAGWTSLVILPDGDVYPC--FDDDFVGPIVLGNIREQSLAEIWNSPKYREFrkLGKFALIELCRDC 65
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
199-337 9.31e-05

Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Bme6 in Brucella melitensis has been shown to be involved in the biosynthesis of a polysaccharide.


Pssm-ID: 340848 [Multi-domain]  Cd Length: 377  Bit Score: 45.44  E-value: 9.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 199 RNFFIENGVSKSKIIYQKYGFDTKTIIYKRRIFTknanikfgFMGRIIPTKGIGVLLKAFKDLPNES----LYIYGNISK 274
Cdd:cd03821   175 PIAVIPNGVDIPEFDPGLRDRRKHNGLEDRRIIL--------FLGRIHPKKGLDLLIRAARKLAEQGrdwhLVIAGPDDG 246
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1705366836 275 TQMRFLQL-------SNVKFMGAYNNADINKVLNSIDVLIVPSIWlENSPLVIQEAFLSGV-VVITSNIGG 337
Cdd:cd03821   247 AYPAFLQLqsslglgDRVTFTGPLYGEAKWALYASADLFVLPSYS-ENFGNVVAEALACGLpVVITDKCGL 316
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
174-369 1.06e-04

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 45.47  E-value: 1.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 174 VKKMFNALKYLRDKIDIFIAPSHTIRNFFIENGVSKSKII--YQKyGFDTKTIIYK------RRIFTKNANIKF--GFMG 243
Cdd:PLN02871  192 VKPMWDIIRFLHRAADLTLVTSPALGKELEAAGVTAANRIrvWNK-GVDSESFHPRfrseemRARLSGGEPEKPliVYVG 270
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 244 RIIPTKGIGVLLKAFKDLPNESLYIYGN---ISKTQMRFLQLsNVKFMGAYNNADINKVLNSIDVLIVPSiwlENSPL-- 318
Cdd:PLN02871  271 RLGAEKNLDFLKRVMERLPGARLAFVGDgpyREELEKMFAGT-PTVFTGMLQGDELSQAYASGDVFVMPS---ESETLgf 346
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1705366836 319 VIQEAFLSGVVVITSNIGGMNELIGKNE----GFLFKAGDSNDLIKVIKKIKQDC 369
Cdd:PLN02871  347 VVLEAMASGVPVVAARAGGIPDIIPPDQegktGFLYTPGDVDDCVEKLETLLADP 401
GT5_Glycogen_synthase_DULL1-like cd03791
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ...
239-364 2.28e-04

Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 family of glycosyltransferases. Glycogen synthase (EC:2.4.1.21) catalyzes the formation and elongation of the alpha-1,4-glucose backbone using ADP-glucose, the second and key step of glycogen biosynthesis. This family includes starch synthases of plants, such as DULL1 in Zea mays and glycogen synthases of various organisms.


Pssm-ID: 340822 [Multi-domain]  Cd Length: 474  Bit Score: 44.48  E-value: 2.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 239 FGFMGRIIPTKGIGVLLKAFKDLPNES--LYIYGN-ISKTQMRFLQLS-----NVKFMGAYNNADINKVLNSIDVLIVPS 310
Cdd:cd03791   297 FGFVGRLTEQKGVDLILDALPELLEEGgqLVVLGSgDPEYEQAFRELAerypgKVAVVIGFDEALAHRIYAGADFFLMPS 376
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1705366836 311 IWlENSPLVIQEAFLSGVVVITSNIGG-------MNELIGKNEGFLFKAGDSNDLIKVIKK 364
Cdd:cd03791   377 RF-EPCGLVQMYAMRYGTLPIVRRTGGladtvfdYDPETGEGTGFVFEDYDAEALLAALRR 436
MoaA COG2896
GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and ...
423-597 1.17e-03

GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and metabolism]; GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 442141 [Multi-domain]  Cd Length: 329  Bit Score: 41.58  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 423 DTCNFRCK--MCDTHSIYNKHFKKLRPDmslDILnkTLLE-SKQMKVSEI-IptTMGEPMLYKYFDTIVDFC--LQNDIK 496
Cdd:COG2896    22 DRCNFRCTycMPEEGYQFLPKEELLSFE---EIE--RLVRaFVELGVRKIrL--TGGEPLLRKDLPELIARLaaLPGIED 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 497 LNLTTNGSQLfnkkynVKYIKnKLLPA-LSDIKISFNSLDYAVNEEIMRNTNTRDVLAKIERLcsmRDKFFPRVSItlQM 575
Cdd:COG2896    95 LALTTNGSLL------ARYAE-ALKAAgLDRVNVSLDSLDPERFRRITRRDDLDKVLAGIDAA---LAAGLTPVKI--NA 162
                         170       180
                  ....*....|....*....|...
gi 1705366836 576 TFMKS-NIDSIKPIIEYAIKHKI 597
Cdd:COG2896   163 VVMRGvNDDEILDLLEFAKERGI 185
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
187-368 1.18e-03

accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases and is named after gtfA in Streptococcus gordonii, where it plays a role in the O-linked glycosylation of GspB, a cell surface glycoprotein involved in platelet binding. In general glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found in bacteria.


Pssm-ID: 340855 [Multi-domain]  Cd Length: 328  Bit Score: 41.52  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 187 KIDIFIAPSHTIRNFFIENGVSKSkiiyqkygfdtktiIYKRRIFTKNANIKFGFMGRIIPTKGIGVLLKAF----KDLP 262
Cdd:cd04949   125 KQDLSERFNKYPPIFTIPVGYVDQ--------------LDTAESNHERKSNKIITISRLAPEKQLDHLIEAVakavKKVP 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 263 NESLYIYG-----NISKTQMRFLQLSNVKFMGAYNNaDINKVLNSIDVLIVPSIwLENSPLVIQEAFLSGVVVITSNIG- 336
Cdd:cd04949   191 EITLDIYGygeerEKLKKLIEELHLEDNVFLKGYHS-NLDQEYQDAYLSLLTSQ-MEGFGLTLMEAIGHGLPVVSYDVKy 268
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1705366836 337 GMNELI--GKNeGFLFKAGDSNDLIKVIKKIKQD 368
Cdd:cd04949   269 GPSELIedGEN-GYLIEKNNIDALADKIIELLND 301
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
425-626 2.26e-03

Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, coproporphyrinogen III oxidase, biotin synthase and MiaB families, and includes a representative in the eukaryotic elongator subunit, Elp-3. Some members of the family are methyltransferases.


Pssm-ID: 214792 [Multi-domain]  Cd Length: 216  Bit Score: 40.08  E-value: 2.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836  425 CNFRCKMCDTHSIYNKhFKKLRPDMSLDIL------NKTLLESKQMKVSEIIPTTMGEPMLYKYFDTIVD-FCLQNDIKL 497
Cdd:smart00729  11 CPRRCTFCSFPSLRGK-LRSRYLEALVREIellaekGEKEGLVGTVFIGGGTPTLLSPEQLEELLEAIREiLGLAKDVEI 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836  498 NLTTNGSQLFN------KKYNVKYiknkllpalsdIKISFNSLDYAVNEEIMRNTNTRDVLAKIERLcsmRDKFFPRVSI 571
Cdd:smart00729  90 TIETRPDTLTEellealKEAGVNR-----------VSLGVQSGDDEVLKAINRGHTVEDVLEAVELL---REAGPIKVST 155
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836  572 TLQMTFMKSNIDSIKPIIEYAIKHKINRIKGHQLWIT-----HKELENEAIYKDKEFIEL 626
Cdd:smart00729 156 DLIVGLPGETEEDFEETLKLLKELGPDRVSIFPLSPRpgtplAKMYKRLKPPTKEERAEL 215
QueE COG0602
Organic radical activating enzyme NrdG/QueE [Coenzyme transport and metabolism]; Organic ...
425-504 3.94e-03

Organic radical activating enzyme NrdG/QueE [Coenzyme transport and metabolism]; Organic radical activating enzyme NrdG/QueE is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440367 [Multi-domain]  Cd Length: 205  Bit Score: 39.35  E-value: 3.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 425 CNFRCKMCDT-HSIYNKHFKKlrpdMSLDILNKTLLESKQMKVSeiIptTMGEPMLYKYFDTIVDFCLQNDIKLNLTTNG 503
Cdd:COG0602    30 CNLRCSWCDTkYAWDGEGGKR----MSAEEILEEVAALGARHVV--I--TGGEPLLQDDLAELLEALKDAGYEVALETNG 101

                  .
gi 1705366836 504 S 504
Cdd:COG0602   102 T 102
GT4_mannosyltransferase-like cd03822
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ...
22-377 9.02e-03

mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. ORF704 in E. coli has been shown to be involved in the biosynthesis of O-specific mannose homopolysaccharides.


Pssm-ID: 340849 [Multi-domain]  Cd Length: 370  Bit Score: 38.91  E-value: 9.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836  22 YSHTLTKELSLNGHKVFVftriendflqPYTIFDEIIEFKQKNVNPICIRRINkPKDYIYRDKFFDENvekafkeymmei 101
Cdd:cd03822    18 YTDDLVEGLRKGGPVVIV----------VIVSPQDEILKDDDFEVPNEIKSWN-SNEYFRLLDHLNFK------------ 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 102 NPDIVHFGHlcHLSI-------NLVHIAKSLGKRIVFTLHDFwlfcvkgqlinqngeicQNPSIENCQKCSPYK---PKI 171
Cdd:cd03822    75 KPDVVHIQH--EFGIfggkyglYALGLLLHLRIPVITTLHTV-----------------LDLSDPGKQALKVLFriaTLS 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 172 QEVKKMFNALKYL-RDKIDIFIAPSHTIRNFFIENGVSKSKIIYQKYGFDTKTIIykrriftknanIKFGFMGriiPTKG 250
Cdd:cd03822   136 ERVVVMAPISRFLlVRIKLIPAVNIEVIPHGVPEVPQDPTTALKRLLLPEGKKVI-----------LTFGFIG---PGKG 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705366836 251 IGVLLKAFKDL----------------PNESLYIYGNISKTQMRFLQLSNVKFMGAY--NNADINKVLNSIDVLIVP--S 310
Cdd:cd03822   202 LEILLEALPELkaefpdvrlviagelhPSLARYEGERYRKAAIEELGLQDHVDFHNNflPEEEVPRYISAADVVVLPylN 281
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1705366836 311 IWLENSPLVIQeAFLSGVVVITSNIGGMNELIGKNEGFLFKAGDSNDLIKVIKKIKQDCRILNTIKD 377
Cdd:cd03822   282 TEQSSSGTLSY-AIACGKPVISTPLRHAEELLADGRGVLVPFDDPSAIAEAILRLLEDDERRQAIAE 347
 
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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