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Conserved domains on  [gi|504683335|ref|WP_014870437|]
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DUF3524 domain-containing protein [Marinobacter sp. BSs20148]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DUF3524 pfam12038
Domain of unknown function (DUF3524); This presumed domain is functionally uncharacterized. ...
 11-175 2.12e-77

Domain of unknown function (DUF3524); This presumed domain is functionally uncharacterized. This domain is found in bacteria and eukaryotes. This domain is about 170 amino acids in length. This domain is found associated with pfam00534. This domain has two conserved sequence motifs: HENQ and FNS. This domain has a single completely conserved residue S that may be functionally important.


:

Pssm-ID: 432280  Cd Length: 165  Bit Score: 236.30  E-value: 2.12e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504683335   11 RILLLSAYDAGSHRRWREQLVLSQPEfEWHVLALSPRFFRWRIRGNALTWLSE-PLLKEHWDLLLVTSMVDLASVRGFHP 89
Cdd:pfam12038   1 KILLLEPFYGGSHKQLADGLAEHSPH-EVDLLTLPARKWKWRMRGSALYFAQEiPDLSAYGDLLFATSMLDLAELRALRP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504683335   90 NLAHTPALLYMHENQFAYPASDGQHNSIDPQMVNLYSAIAADTVLFNSDWNRRSFLEGVEQLFRRLPDGIPEGTLELISA 169
Cdd:pfam12038  80 DLANCPKLLYFHENQLTYPVRPGQERDFQYGFNNILSALAADRVLFNSRFNRDSFLEAIPALLKKMPDARPKGLVEKIRA 159


                  ....*.
gi 504683335  170 KSRVLP 175
Cdd:pfam12038 160 KSRVLY 165
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 215-317 1.08e-10

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: 61.27  E-value: 1.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504683335 215 VWAARWEYDKGPDRLLAILQELERRALSFQVCVLGESFRKVPEAMTTIQQQFAHRLVQFGYASSRSEYYEWLGSADVILS 294
Cdd:cd01635  114 VSVGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAALGLLERVVIIGGLVDDEVLELLLAAADVFVL 193

                         90       100
                 ....*....|....*....|...
gi 504683335 295 TALHEFQGLAVLEAVAVGCVPIV 317
Cdd:cd01635  194 PSRSEGFGLVLLEAMAAGKPVIA 216
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 285-388 7.41e-04

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


:

Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 39.20  E-value: 7.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504683335 285 WLGSADVILSTALHEFQGLAVLEAVAVGCVPIVPAREVYPELFAPE----YLYPDCGDDIPAEAAHAATLIEKQAVDGHG 360
Cdd:COG0438   17 LLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGetglLVPPGDPEALAEAILRLLEDPELRRRLGEA 96

                         90       100
                 ....*....|....*....|....*...
gi 504683335 361 DRLTVpgVQRFSLGALKPKYEALLLEAL 388
Cdd:COG0438   97 ARERA--EERFSWEAIAERLLALYEELL 122
 
Name Accession Description Interval E-value
DUF3524 pfam12038
Domain of unknown function (DUF3524); This presumed domain is functionally uncharacterized. ...
 11-175 2.12e-77

Domain of unknown function (DUF3524); This presumed domain is functionally uncharacterized. This domain is found in bacteria and eukaryotes. This domain is about 170 amino acids in length. This domain is found associated with pfam00534. This domain has two conserved sequence motifs: HENQ and FNS. This domain has a single completely conserved residue S that may be functionally important.


Pssm-ID: 432280  Cd Length: 165  Bit Score: 236.30  E-value: 2.12e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504683335   11 RILLLSAYDAGSHRRWREQLVLSQPEfEWHVLALSPRFFRWRIRGNALTWLSE-PLLKEHWDLLLVTSMVDLASVRGFHP 89
Cdd:pfam12038   1 KILLLEPFYGGSHKQLADGLAEHSPH-EVDLLTLPARKWKWRMRGSALYFAQEiPDLSAYGDLLFATSMLDLAELRALRP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504683335   90 NLAHTPALLYMHENQFAYPASDGQHNSIDPQMVNLYSAIAADTVLFNSDWNRRSFLEGVEQLFRRLPDGIPEGTLELISA 169
Cdd:pfam12038  80 DLANCPKLLYFHENQLTYPVRPGQERDFQYGFNNILSALAADRVLFNSRFNRDSFLEAIPALLKKMPDARPKGLVEKIRA 159


                  ....*.
gi 504683335  170 KSRVLP 175
Cdd:pfam12038 160 KSRVLY 165
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 215-317 1.08e-10

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: 61.27  E-value: 1.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504683335 215 VWAARWEYDKGPDRLLAILQELERRALSFQVCVLGESFRKVPEAMTTIQQQFAHRLVQFGYASSRSEYYEWLGSADVILS 294
Cdd:cd01635  114 VSVGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAALGLLERVVIIGGLVDDEVLELLLAAADVFVL 193

                         90       100
                 ....*....|....*....|...
gi 504683335 295 TALHEFQGLAVLEAVAVGCVPIV 317
Cdd:cd01635  194 PSRSEGFGLVLLEAMAAGKPVIA 216
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 214-331 2.66e-05

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: 44.19  E-value: 2.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504683335  214 IVWAARWEYDKGPDRLLAILQELERRALSFQVCVLGE-SFRKVPEAMttIQQQFAHRLVQFGYASSRSEYYEWLGSADVI 292
Cdd:pfam00534   5 ILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDgEEEKRLKKL--AEKLGLGDNVIFLGFVSDEDLPELLKIADVF 82

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 504683335  293 LSTALHEFQGLAVLEAVAVGCVPIVPAREVYPELFAPEY 331
Cdd:pfam00534  83 VLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGE 121
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 285-388 7.41e-04

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 39.20  E-value: 7.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504683335 285 WLGSADVILSTALHEFQGLAVLEAVAVGCVPIVPAREVYPELFAPE----YLYPDCGDDIPAEAAHAATLIEKQAVDGHG 360
Cdd:COG0438   17 LLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGetglLVPPGDPEALAEAILRLLEDPELRRRLGEA 96

                         90       100
                 ....*....|....*....|....*...
gi 504683335 361 DRLTVpgVQRFSLGALKPKYEALLLEAL 388
Cdd:COG0438   97 ARERA--EERFSWEAIAERLLALYEELL 122
 
Name Accession Description Interval E-value
DUF3524 pfam12038
Domain of unknown function (DUF3524); This presumed domain is functionally uncharacterized. ...
 11-175 2.12e-77

Domain of unknown function (DUF3524); This presumed domain is functionally uncharacterized. This domain is found in bacteria and eukaryotes. This domain is about 170 amino acids in length. This domain is found associated with pfam00534. This domain has two conserved sequence motifs: HENQ and FNS. This domain has a single completely conserved residue S that may be functionally important.


Pssm-ID: 432280  Cd Length: 165  Bit Score: 236.30  E-value: 2.12e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504683335   11 RILLLSAYDAGSHRRWREQLVLSQPEfEWHVLALSPRFFRWRIRGNALTWLSE-PLLKEHWDLLLVTSMVDLASVRGFHP 89
Cdd:pfam12038   1 KILLLEPFYGGSHKQLADGLAEHSPH-EVDLLTLPARKWKWRMRGSALYFAQEiPDLSAYGDLLFATSMLDLAELRALRP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504683335   90 NLAHTPALLYMHENQFAYPASDGQHNSIDPQMVNLYSAIAADTVLFNSDWNRRSFLEGVEQLFRRLPDGIPEGTLELISA 169
Cdd:pfam12038  80 DLANCPKLLYFHENQLTYPVRPGQERDFQYGFNNILSALAADRVLFNSRFNRDSFLEAIPALLKKMPDARPKGLVEKIRA 159


                  ....*.
gi 504683335  170 KSRVLP 175
Cdd:pfam12038 160 KSRVLY 165
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 215-317 1.08e-10

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: 61.27  E-value: 1.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504683335 215 VWAARWEYDKGPDRLLAILQELERRALSFQVCVLGESFRKVPEAMTTIQQQFAHRLVQFGYASSRSEYYEWLGSADVILS 294
Cdd:cd01635  114 VSVGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAALGLLERVVIIGGLVDDEVLELLLAAADVFVL 193

                         90       100
                 ....*....|....*....|...
gi 504683335 295 TALHEFQGLAVLEAVAVGCVPIV 317
Cdd:cd01635  194 PSRSEGFGLVLLEAMAAGKPVIA 216
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 5-384 5.58e-10

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: 60.24  E-value: 5.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504683335   5 LALRQPRILLLSAYDAGSHRRWREQLVLSQPEFEWHVLALSPRFFRwRIRGnaltwlsePLLKEHWDLLLVTSMVDLASV 84
Cdd:cd03801   27 LAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRLLR-ELRP--------LLRLRKFDVVHAHGLLAALLA 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504683335  85 RgFHPNLAHTPALLYMHENQFAYPASDG-QHNSIDPQMVNLYSAiaADTVLFNSDWNRRSFLEgveqlfrrlpdgipegT 163
Cdd:cd03801   98 A-LLALLLGAPLVVTLHGAEPGRLLLLLaAERRLLARAEALLRR--ADAVIAVSEALRDELRA----------------L 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504683335 164 LELISAKSRVLPVPIDDPVFLSEAERqsleagerlwrndlEPEPGALPLRIVWAARWEYDKGPDRLLAILQELERRALSF 243
Cdd:cd03801  159 GGIPPEKIVVIPNGVDLERFSPPLRR--------------KLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDV 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504683335 244 QVCVLGESFRKVPEAmttiqQQFAHRL---VQFGYASSRSEYYEWLGSADVILSTALHEFQGLAVLEAVAVGCVPIVPAR 320
Cdd:cd03801  225 RLVIVGGDGPLRAEL-----EELELGLgdrVRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDV 299

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504683335 321 EVYPELFAPEYLYPDCGDDIPAEAAHA--ATLIEKQAVDGHGDRLTVPGVQRFSLGALKPKYEALL 384
Cdd:cd03801  300 GGLPEVVEDGEGGLVVPPDDVEALADAllRLLADPELRARLGRAARERVAERFSWERVAERLLDLY 365
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 11-363 1.17e-09

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: 59.29  E-value: 1.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504683335  11 RILLLSAYDAGSHRRWREQLVLSQPeFEWHVLALSPRFFRWRIRGNAltwlsePLLKEH-WDLLLvtSMVDLASVRGFHP 89
Cdd:cd03811   31 DVTLVLLRDEGDLDKQLNGDVKLIR-LLIRVLKLIKLGLLKAILKLK------RILKRAkPDVVI--SFLGFATYIVAKL 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504683335  90 NLAHTPALLYMHenqFAYPASDGQHNSIDPQMVNLYSAiaaDTVLFNSDWNRRSFlegvEQLFRRLPDgipegtlelisa 169
Cdd:cd03811  102 AAARSKVIAWIH---SSLSKLYYLKKKLLLKLKLYKKA---DKIVCVSKGIKEDL----IRLGPSPPE------------ 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504683335 170 KSRVLPVPIDdpvfLSEAERQSLEAgerlwrNDLEPEPGalpLRIVWAARWEYDKGPDRLLAILQELERRALSFQVCVLG 249
Cdd:cd03811  160 KIEVIYNPID----IDRIRALAKEP------ILNEPEDG---PVILAVGRLDPQKGHDLLIEAFAKLRKKYPDVKLVILG 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504683335 250 E-SFRKvpeamttIQQQFAHRL-----VQF-GYassRSEYYEWLGSADVILSTALHEFQGLAVLEAVAVGcVPIVPAREV 322
Cdd:cd03811  227 DgPLRE-------ELEKLAKELglaerVIFlGF---QSNPYPYLKKADLFVLSSRYEGFPNVLLEAMALG-TPVVSTDCP 295

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 504683335 323 YP-ELFAPE---YLYPDcgDDIPAEAAHAATLIEKQAVDGHGDRL 363
Cdd:cd03811  296 GPrEILDDGengLLVPD--GDAAALAGILAALLQKKLDAALRERL 338
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 169-350 1.77e-05

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: 46.19  E-value: 1.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504683335 169 AKSRVLPVPIDDPVFLSEAERQSLEAGErlwrndlepEPGALPLrIVWAARWEYDKGPDRLLAILQELERRaLSFQVCVL 248
Cdd:cd03819  150 ERIRVIPNGVDTDRFPPEAEAEERAQLG---------LPEGKPV-VGYVGRLSPEKGWLLLVDAAAELKDE-PDFRLLVA 218

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504683335 249 G-----ESFRKVPEAMTtiqqqFAHRLVQFGYassRSEYYEWLGSADVILSTALHEFQGLAVLEAVAVGCvPIVP----- 318
Cdd:cd03819  219 GdgperDEIRRLVERLG-----LRDRVTFTGF---REDVPAALAASDVVVLPSLHEEFGRVALEAMACGT-PVVAtdvgg 289

                        170       180       190
                 ....*....|....*....|....*....|..
gi 504683335 319 AREVYPElFAPEYLYPDCGDDIPAEAAHAATL 350
Cdd:cd03819  290 AREIVVH-GRTGLLVPPGDAEALADAIRAAKL 320
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 214-331 2.66e-05

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: 44.19  E-value: 2.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504683335  214 IVWAARWEYDKGPDRLLAILQELERRALSFQVCVLGE-SFRKVPEAMttIQQQFAHRLVQFGYASSRSEYYEWLGSADVI 292
Cdd:pfam00534   5 ILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDgEEEKRLKKL--AEKLGLGDNVIFLGFVSDEDLPELLKIADVF 82

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 504683335  293 LSTALHEFQGLAVLEAVAVGCVPIVPAREVYPELFAPEY 331
Cdd:pfam00534  83 VLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGE 121
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
211-317 3.24e-05

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 43.27  E-value: 3.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504683335  211 PLRIVWAAR-WEYDKGPDRLLAILQELERRALSFQVCVLGESfrkVPEAMTTIQQQFAHRLVQFGYassRSEYYEWLGSA 289
Cdd:pfam13692   1 RPVILFVGRlHPNVKGVDYLLEAVPLLRKRDNDVRLVIVGDG---PEEELEELAAGLEDRVIFTGF---VEDLAELLAAA 74

                          90       100
                  ....*....|....*....|....*...
gi 504683335  290 DVILSTALHEFQGLAVLEAVAVGcVPIV 317
Cdd:pfam13692  75 DVFVLPSLYEGFGLKLLEAMAAG-LPVV 101
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 199-317 1.50e-04

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: 43.35  E-value: 1.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504683335 199 WRNDLEPEPGAlPLRIVWAARWEYDKGPDRLLAILQELERRALSFQVCVLGESFRKVPEAMTTIQQQFAHRLVQFGYass 278
Cdd:cd03808  178 FQYSPESLPSE-KVVFLFVARLLKDKGIDELIEAAKILKKKGPNVRFLLVGDGELENPSEILIEKLGLEGRIEFLGF--- 253

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 504683335 279 RSEYYEWLGSADVILSTALHEFQGLAVLEAVAVGcVPIV 317
Cdd:cd03808  254 RSDVPELLAESDVFVLPSYREGLPRSLLEAMAAG-RPVI 291
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
 167-328 2.21e-04

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: 43.04  E-value: 2.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504683335 167 ISAKSRVLPVPIDDPVFLSEaerqsLEAGERLWRNDLEPEPgalplRIVWAARWEYDKGPDRLLAILQELeRRALSFQVC 246
Cdd:cd03817  167 VKGPIEVIPNGIDLDKFEKP-----LNTEERRKLGLPPDEP-----ILLYVGRLAKEKNIDFLLRAFAEL-KKEPNIKLV 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504683335 247 VLGESFRKvPEAmttiqQQFAHRL-----VQF-GYASsRSEYYEWLGSADVILSTALHEFQGLAVLEAVAVGCvPIVPAR 320
Cdd:cd03817  236 IVGDGPER-EEL-----KELARELgladkVIFtGFVP-REELPEYYKAADLFVFASTTETQGLVYLEAMAAGL-PVVAAK 307


                 ....*....
gi 504683335 321 E-VYPELFA 328
Cdd:cd03817  308 DpAASELVE 316
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 213-320 5.97e-04

sucrose-phosphate synthase and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. The sucrose-phosphate synthases in this family may be unique to plants and photosynthetic bacteria. This enzyme catalyzes the synthesis of sucrose 6-phosphate from fructose 6-phosphate and uridine 5'-diphosphate-glucose, a key regulatory step of sucrose metabolism. The activity of this enzyme is regulated by phosphorylation and moderated by the concentration of various metabolites and light.


Pssm-ID: 340830 [Multi-domain]  Cd Length: 398  Bit Score: 41.46  E-value: 5.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504683335 213 RIVWAARWEYDKGPD---RLLAILQELERRALsfQVCVLGESFRkvPEAMTTIQ-QQFAHRL-----VQFGYASSRSEYY 283
Cdd:cd03800  222 VVLALGRLDPRKGIDtlvRAFAQLPELRELAN--LVLVGGPSDD--PLSMDREElAELAEELglidrVRFPGRVSRDDLP 297

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 504683335 284 EWLGSADVILSTALHEFQGLAVLEAVAVGcVPIVPAR 320
Cdd:cd03800  298 ELYRAADVFVVPSLYEPFGLTAIEAMACG-TPVVATA 333
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 285-388 7.41e-04

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 39.20  E-value: 7.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504683335 285 WLGSADVILSTALHEFQGLAVLEAVAVGCVPIVPAREVYPELFAPE----YLYPDCGDDIPAEAAHAATLIEKQAVDGHG 360
Cdd:COG0438   17 LLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGetglLVPPGDPEALAEAILRLLEDPELRRRLGEA 96

                         90       100
                 ....*....|....*....|....*...
gi 504683335 361 DRLTVpgVQRFSLGALKPKYEALLLEAL 388
Cdd:COG0438   97 ARERA--EERFSWEAIAERLLALYEELL 122
 
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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