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Conserved domains on  [gi|57226667|gb|AAW43127|]
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transferase, putative [Cryptococcus neoformans var. neoformans JEC21]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GT4_PIG-A-like cd03796
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ...
 347-743 0e+00

phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Phosphatidylinositol glycan-class A (PIG-A), an X-linked gene in humans, is necessary for the synthesis of N-acetylglucosaminyl-phosphatidylinositol, a very early intermediate in glycosyl phosphatidylinositol (GPI)-anchor biosynthesis. The GPI-anchor is an important cellular structure that facilitates the attachment of many proteins to cell surfaces. Somatic mutations in PIG-A have been associated with Paroxysmal Nocturnal Hemoglobinuria (PNH), an acquired hematological disorder.


:

Pssm-ID: 340827 [Multi-domain]  Cd Length: 398  Bit Score: 692.83  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 347 IAMVSDFFFPVIGGVEGHIYSLSVELMRRGHKVIVITHSHPDRLGIHYLEPSLKVYYLPYLPIASSASLPNFLLFLPYFR 426
Cdd:cd03796   2 ICMVSDFFYPNLGGVETHIYQLSQCLIKRGHKVIVITHAYGNRVGVRYLTNGLKVYYLPFKVFYNQSTLPTLFSTFPLLR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 427 HIILTENIQLVHGHGALSSLAHEAVIHAPLLGVKAVFTDHSLFGFGDAVGVLTNKLLGAALRCVDEVICVSNTGRENTVL 506
Cdd:cd03796  82 NILIRERIQIVHGHQAFSSLAHEALFHARTLGLKTVFTDHSLFGFADASSILTNKLLRFSLADIDHVICVSHTSKENTVL 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 507 RAQLDPSIVSVIPNALEAEHFKPDPFRADPDWITIVVISRLVHRKGIDLLISSAPQICALFPKVRFIVGGDGPKMVELEQ 586
Cdd:cd03796 162 RASLDPRIVSVIPNAVDSSDFTPDPSKPDPNKITIVVISRLVYRKGIDLLVGIIPRICKKHPNVRFIIGGDGPKRIELEE 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 587 MREKYELQGRVELLGRVNPGDVRDVLTKGQIYLSNSLTEAFGISIIEAASAGLFVVATKVGGVPEILPQDMIEFCRADED 666
Cdd:cd03796 242 MREKYQLQDRVELLGAVPHEEVRDVLVQGHIFLNTSLTEAFCIAIVEAASCGLLVVSTRVGGIPEVLPPDMILLAEPDPE 321

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 57226667 667 DVIRALTHAIHTIQSSRHSPWSAHIRVRDMYSWSHVSSRAEIVYLRAMSRPHREIGERMRRYLELGPVFGVVMCCIL 743
Cdd:cd03796 322 DIVRKLEEAISILRTGKHDPWSFHNRVKKMYSWEDVARRTEKVYDRILSTPNRPFLERLKRYYNCGPIAGKIFCLLA 398
PlsC COG0204
1-acyl-sn-glycerol-3-phosphate acyltransferase [Lipid transport and metabolism]; ...
 42-255 4.70e-53

1-acyl-sn-glycerol-3-phosphate acyltransferase [Lipid transport and metabolism]; 1-acyl-sn-glycerol-3-phosphate acyltransferase is part of the Pathway/BioSystem: Phospholipid biosynthesis


:

Pssm-ID: 439974 [Multi-domain]  Cd Length: 215  Bit Score: 183.29  E-value: 4.70e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667  42 YFVARTFYCIAGTILGWKFQVEGEQYLwelsgehgggkanEKGRSMVMVGNHQSFVDILYLGRIFPKHAAIMAKKSIQWI 121
Cdd:COG0204  13 YRLVRLWARLLLRLLGVRVRVEGLENL-------------PADGPVLIVANHQSWLDILLLLAALPRPVRFVAKKELFKI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 122 PGLGWFMMMSGTVFINRSNNKSAIASLQHAGEEMKRKRiSLWIFPEGTRhnTPEPELLNFKKGAFYLAVQAGVPIVPVVC 201
Cdd:COG0204  80 PLLGWLLRALGAIPVDRSKRRAALRALRQAVEALKAGE-SLVIFPEGTR--SPDGRLLPFKTGAARLALEAGVPIVPVAI 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 57226667 202 ENYNHLFNGKSHFRRGTLRIKVLPPISTTGLTAADVPGLIERTRNAMLETLQEI 255
Cdd:COG0204 157 DGTERALPKGFLPRPGKVTVRIGPPIDPSDLEGEDRRELAERLRAAIEALLAEL 210
 
Name Accession Description Interval E-value
GT4_PIG-A-like cd03796
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ...
 347-743 0e+00

phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Phosphatidylinositol glycan-class A (PIG-A), an X-linked gene in humans, is necessary for the synthesis of N-acetylglucosaminyl-phosphatidylinositol, a very early intermediate in glycosyl phosphatidylinositol (GPI)-anchor biosynthesis. The GPI-anchor is an important cellular structure that facilitates the attachment of many proteins to cell surfaces. Somatic mutations in PIG-A have been associated with Paroxysmal Nocturnal Hemoglobinuria (PNH), an acquired hematological disorder.


Pssm-ID: 340827 [Multi-domain]  Cd Length: 398  Bit Score: 692.83  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 347 IAMVSDFFFPVIGGVEGHIYSLSVELMRRGHKVIVITHSHPDRLGIHYLEPSLKVYYLPYLPIASSASLPNFLLFLPYFR 426
Cdd:cd03796   2 ICMVSDFFYPNLGGVETHIYQLSQCLIKRGHKVIVITHAYGNRVGVRYLTNGLKVYYLPFKVFYNQSTLPTLFSTFPLLR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 427 HIILTENIQLVHGHGALSSLAHEAVIHAPLLGVKAVFTDHSLFGFGDAVGVLTNKLLGAALRCVDEVICVSNTGRENTVL 506
Cdd:cd03796  82 NILIRERIQIVHGHQAFSSLAHEALFHARTLGLKTVFTDHSLFGFADASSILTNKLLRFSLADIDHVICVSHTSKENTVL 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 507 RAQLDPSIVSVIPNALEAEHFKPDPFRADPDWITIVVISRLVHRKGIDLLISSAPQICALFPKVRFIVGGDGPKMVELEQ 586
Cdd:cd03796 162 RASLDPRIVSVIPNAVDSSDFTPDPSKPDPNKITIVVISRLVYRKGIDLLVGIIPRICKKHPNVRFIIGGDGPKRIELEE 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 587 MREKYELQGRVELLGRVNPGDVRDVLTKGQIYLSNSLTEAFGISIIEAASAGLFVVATKVGGVPEILPQDMIEFCRADED 666
Cdd:cd03796 242 MREKYQLQDRVELLGAVPHEEVRDVLVQGHIFLNTSLTEAFCIAIVEAASCGLLVVSTRVGGIPEVLPPDMILLAEPDPE 321

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 57226667 667 DVIRALTHAIHTIQSSRHSPWSAHIRVRDMYSWSHVSSRAEIVYLRAMSRPHREIGERMRRYLELGPVFGVVMCCIL 743
Cdd:cd03796 322 DIVRKLEEAISILRTGKHDPWSFHNRVKKMYSWEDVARRTEKVYDRILSTPNRPFLERLKRYYNCGPIAGKIFCLLA 398
PlsC COG0204
1-acyl-sn-glycerol-3-phosphate acyltransferase [Lipid transport and metabolism]; ...
 42-255 4.70e-53

1-acyl-sn-glycerol-3-phosphate acyltransferase [Lipid transport and metabolism]; 1-acyl-sn-glycerol-3-phosphate acyltransferase is part of the Pathway/BioSystem: Phospholipid biosynthesis


Pssm-ID: 439974 [Multi-domain]  Cd Length: 215  Bit Score: 183.29  E-value: 4.70e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667  42 YFVARTFYCIAGTILGWKFQVEGEQYLwelsgehgggkanEKGRSMVMVGNHQSFVDILYLGRIFPKHAAIMAKKSIQWI 121
Cdd:COG0204  13 YRLVRLWARLLLRLLGVRVRVEGLENL-------------PADGPVLIVANHQSWLDILLLLAALPRPVRFVAKKELFKI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 122 PGLGWFMMMSGTVFINRSNNKSAIASLQHAGEEMKRKRiSLWIFPEGTRhnTPEPELLNFKKGAFYLAVQAGVPIVPVVC 201
Cdd:COG0204  80 PLLGWLLRALGAIPVDRSKRRAALRALRQAVEALKAGE-SLVIFPEGTR--SPDGRLLPFKTGAARLALEAGVPIVPVAI 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 57226667 202 ENYNHLFNGKSHFRRGTLRIKVLPPISTTGLTAADVPGLIERTRNAMLETLQEI 255
Cdd:COG0204 157 DGTERALPKGFLPRPGKVTVRIGPPIDPSDLEGEDRRELAERLRAAIEALLAEL 210
LPLAT_AGPAT-like cd07989
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: AGPAT-like; ...
 55-245 2.55e-46

Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: AGPAT-like; Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are such LPLATs as 1-acyl-sn-glycerol-3-phosphate acyltransferase (AGPAT, PlsC), Tafazzin (product of Barth syndrome gene), and similar proteins.


Pssm-ID: 153251 [Multi-domain]  Cd Length: 184  Bit Score: 163.21  E-value: 2.55e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667  55 ILGWKFQVEGEQYLwelsgehgggkanEKGRSMVMVGNHQSFVDILYLGRIFPKHAAIMAKKSIQWIPGLGWFMMMSGTV 134
Cdd:cd07989   7 LLGVRVRVEGLENL-------------PPKGPVIIVANHQSYLDPLVLGAALPRPIRFVAKKELFKIPFLGWLLRLLGAI 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 135 FINRSNNKSAIASLQHAGEEMKRKRiSLWIFPEGTRhnTPEPELLNFKKGAFYLAVQAGVPIVPVVCENYNH-LFNGKSH 213
Cdd:cd07989  74 PIDRGNGRSAREALREAIEALKEGE-SVVIFPEGTR--SRDGELLPFKSGAFRLAKEAGVPIVPVAISGTWGsLPKGKKL 150

                       170       180       190
                ....*....|....*....|....*....|....
gi 57226667 214 FRRGTLRIKVLPPISTTGL--TAADVPGLIERTR 245
Cdd:cd07989 151 PRPGRVTVRIGEPIPPEGLelAEEDRKELREKVR 184
PIGA pfam08288
PIGA (GPI anchor biosynthesis); This domain is found on phosphatidylinositol ...
 384-473 3.57e-45

PIGA (GPI anchor biosynthesis); This domain is found on phosphatidylinositol n-acetylglucosaminyltransferase proteins. These proteins are involved in GPI anchor biosynthesis and are associated with disease the paroxysmal nocturnal haemoglobinuria.


Pssm-ID: 400541  Cd Length: 90  Bit Score: 156.65  E-value: 3.57e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667   384 HSHPDRLGIHYLEPSLKVYYLPYLPIASSASLPNFLLFLPYFRHIILTENIQLVHGHGALSSLAHEAVIHAPLLGVKAVF 463
Cdd:pfam08288   1 HAYGDRTGVRYLTNGLKVYYVPFLVIYRQSTFPTVFGTFPLFRNILLRERIDIVHGHGSFSTLAHEAILHARTMGLKTVF 80

                          90
                  ....*....|
gi 57226667   464 TDHSLFGFGD 473
Cdd:pfam08288  81 TDHSLFGFAD 90
AGP_acyltrn TIGR00530
1-acyl-sn-glycerol-3-phosphate acyltransferases; This model describes the core homologous ...
 88-201 8.03e-37

1-acyl-sn-glycerol-3-phosphate acyltransferases; This model describes the core homologous region of a collection of related proteins, several of which are known to act as 1-acyl-sn-glycerol-3-phosphate acyltransferases (EC 2.3.1.51). Proteins scoring above the trusted cutoff are likely to have the same general activity. However, there is variation among characterized members as to whether the acyl group can be donated by acyl carrier protein or coenzyme A, and in the length and saturation of the donated acyl group. 1-acyl-sn-glycerol-3-phosphate acyltransferase is also called 1-AGP acyltransferase, lysophosphatidic acid acyltransferase, and LPA acyltransferase. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 129621 [Multi-domain]  Cd Length: 130  Bit Score: 134.40  E-value: 8.03e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667    88 VMVGNHQSFVDILYLGRIFPKHAAIMAKKSIQWIPGLGWFMMMSGTVFINRsNNKSAIASLQHAGEEMKRKRISLWIFPE 167
Cdd:TIGR00530  19 LVVANHQSNLDPLTLSAAFPPPIVFIAKKELKWIPFFGIMLWLTGAIFIDR-ENIRAIATALKAAIEVLKQGRSIGVFPE 97

                          90       100       110
                  ....*....|....*....|....*....|....
gi 57226667   168 GTRhnTPEPELLNFKKGAFYLAVQAGVPIVPVVC 201
Cdd:TIGR00530  98 GTR--SRGRDILPFKKGAFHIAIKAGVPILPVVL 129
Acyltransferase pfam01553
Acyltransferase; This family contains acyltransferases involved in phospholipid biosynthesis ...
 59-201 3.71e-35

Acyltransferase; This family contains acyltransferases involved in phospholipid biosynthesis and other proteins of unknown function. This family also includes tafazzin, the Barth syndrome gene.


Pssm-ID: 366704 [Multi-domain]  Cd Length: 131  Bit Score: 129.71  E-value: 3.71e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667    59 KFQVEGEQYLwelsgehgggkanEKGRSMVMVGNHQSFVDILYLGRIFPKHA---AIMAKKSIQWIPGLGWFMMMSGTVF 135
Cdd:pfam01553   1 RIEVHGLENL-------------PRGGPAIVVANHQSYLDVLLLSLALYKRGrplVFVAKKELFDIPLVGWLMRLLGCIF 67

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57226667   136 INRSNNKSAIASLQHAGEEMKRKRiSLWIFPEGTRhnTPEPELLNFKKGAFYLAVQAGVPIVPVVC 201
Cdd:pfam01553  68 IDRKNRKDAAGTLEYLVELLREGK-LVVIFPEGTR--SREGELLPFKKGAFRLAIEAGVPIVPVAI 130
PlsC smart00563
Phosphate acyltransferases; Function in phospholipid biosynthesis and have either ...
 87-201 4.96e-35

Phosphate acyltransferases; Function in phospholipid biosynthesis and have either glycerolphosphate, 1-acylglycerolphosphate, or 2-acylglycerolphosphoethanolamine acyltransferase activities. Tafazzin, the product of the gene mutated in patients with Barth syndrome, is a member of this family.


Pssm-ID: 214724 [Multi-domain]  Cd Length: 118  Bit Score: 129.01  E-value: 4.96e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667     87 MVMVGNHQSFVDILYLGRIFPKHAA---IMAKKSIQWIPGLGWFMMMSGTVFINRSNNKSAIASLQHAGeEMKRKRISLW 163
Cdd:smart00563   1 ALVVANHQSFLDPLVLSALLPRKLGrvrFVAKKELFYVPLLGWLLRLLGAIFIDRSNGRKARAALREAV-ELLKEGEWLL 79

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 57226667    164 IFPEGTRhnTPEPELLNFKKGAFYLAVQAGVPIVPVVC 201
Cdd:smart00563  80 IFPEGTR--SRPGKLLPFKKGAARLALEAGVPIVPVAI 115
PLN02901 PLN02901
1-acyl-sn-glycerol-3-phosphate acyltransferase
 88-253 8.33e-23

1-acyl-sn-glycerol-3-phosphate acyltransferase


Pssm-ID: 215488 [Multi-domain]  Cd Length: 214  Bit Score: 97.49  E-value: 8.33e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667   88 VMVGNHQSFVDI---LYLGRIFpkhaAIMAKKSIQWIPGLGWFMMMSGTVFINRSNNKSAIASLQHAgEEMKRKRISLWI 164
Cdd:PLN02901  53 VYVSNHQSFLDIytlFHLGRPF----KFISKTSIFLIPIIGWAMYMTGHIPLKRMDRRSQLECLKRC-MELLKKGASVFF 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667  165 FPEGTRhnTPEPELLNFKKGAFYLAVQAGVPIVPVVCENYNHLF-NGKSH-FRRGTLRIKVLPPISTTGltaADVpgLIE 242
Cdd:PLN02901 128 FPEGTR--SKDGKLAAFKKGAFSVAAKTGVPVVPITLVGTGKIMpNGKEGiLNPGSVKVVIHPPIEGSD---ADE--LCN 200

                        170
                 ....*....|.
gi 57226667  243 RTRNAMLETLQ 253
Cdd:PLN02901 201 EARKVIAESLV 211
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 617-715 9.13e-12

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 62.70  E-value: 9.13e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 617 IYLSNSLTEAFGISIIEAASAGLFVVATKVGGVPEILPQDMIEFC--RADEDDVIRALTHAIHTIQSSRHSPWSAHIRVR 694
Cdd:COG0438  23 VFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLvpPGDPEALAEAILRLLEDPELRRRLGEAARERAE 102

                        90       100
                ....*....|....*....|.
gi 57226667 695 DMYSWSHVSSRAEIVYLRAMS 715
Cdd:COG0438 103 ERFSWEAIAERLLALYEELLA 123
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
 536-656 2.51e-06

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 50.86  E-value: 2.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667  536 PDWITIVVISRLVHRKGIDLLISsapqICALFPKVRFIVGGDGPKMVELEQMrekyeLQG-RVELLGRVNPGDVRDVLTK 614
Cdd:PLN02871 261 PEKPLIVYVGRLGAEKNLDFLKR----VMERLPGARLAFVGDGPYREELEKM-----FAGtPTVFTGMLQGDELSQAYAS 331

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 57226667  615 GQIYLSNSLTEAFGISIIEAASAGLFVVATKVGGVPEILPQD 656
Cdd:PLN02871 332 GDVFVMPSESETLGFVVLEAMASGVPVVAARAGGIPDIIPPD 373
sucrsPsyn_pln TIGR02468
sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this ...
 589-653 1.51e-05

sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this family are sucrose-phosphate synthases of plants. This enzyme is known to exist in multigene families in several species of both monocots and dicots. The N-terminal domain is the glucosyltransferase domain. Members of this family also have a variable linker region and a C-terminal domain that resembles sucrose phosphate phosphatase (SPP) (EC 3.1.3.24) (see TIGR01485), the next and final enzyme of sucrose biosynthesis. The SPP-like domain likely serves a binding and not a catalytic function, as the reported SPP is always encoded by a distinct protein.


Pssm-ID: 274147 [Multi-domain]  Cd Length: 1050  Bit Score: 48.62  E-value: 1.51e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667    589 EKYELQGRVELLGRVNPGDVRDVL-----TKGqIYLSNSLTEAFGISIIEAASAGLFVVATKVGGVPEIL 653
Cdd:TIGR02468  542 DKYDLYGQVAYPKHHKQSDVPDIYrlaakTKG-VFINPAFIEPFGLTLIEAAAHGLPMVATKNGGPVDIH 610
 
Name Accession Description Interval E-value
GT4_PIG-A-like cd03796
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ...
 347-743 0e+00

phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Phosphatidylinositol glycan-class A (PIG-A), an X-linked gene in humans, is necessary for the synthesis of N-acetylglucosaminyl-phosphatidylinositol, a very early intermediate in glycosyl phosphatidylinositol (GPI)-anchor biosynthesis. The GPI-anchor is an important cellular structure that facilitates the attachment of many proteins to cell surfaces. Somatic mutations in PIG-A have been associated with Paroxysmal Nocturnal Hemoglobinuria (PNH), an acquired hematological disorder.


Pssm-ID: 340827 [Multi-domain]  Cd Length: 398  Bit Score: 692.83  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 347 IAMVSDFFFPVIGGVEGHIYSLSVELMRRGHKVIVITHSHPDRLGIHYLEPSLKVYYLPYLPIASSASLPNFLLFLPYFR 426
Cdd:cd03796   2 ICMVSDFFYPNLGGVETHIYQLSQCLIKRGHKVIVITHAYGNRVGVRYLTNGLKVYYLPFKVFYNQSTLPTLFSTFPLLR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 427 HIILTENIQLVHGHGALSSLAHEAVIHAPLLGVKAVFTDHSLFGFGDAVGVLTNKLLGAALRCVDEVICVSNTGRENTVL 506
Cdd:cd03796  82 NILIRERIQIVHGHQAFSSLAHEALFHARTLGLKTVFTDHSLFGFADASSILTNKLLRFSLADIDHVICVSHTSKENTVL 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 507 RAQLDPSIVSVIPNALEAEHFKPDPFRADPDWITIVVISRLVHRKGIDLLISSAPQICALFPKVRFIVGGDGPKMVELEQ 586
Cdd:cd03796 162 RASLDPRIVSVIPNAVDSSDFTPDPSKPDPNKITIVVISRLVYRKGIDLLVGIIPRICKKHPNVRFIIGGDGPKRIELEE 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 587 MREKYELQGRVELLGRVNPGDVRDVLTKGQIYLSNSLTEAFGISIIEAASAGLFVVATKVGGVPEILPQDMIEFCRADED 666
Cdd:cd03796 242 MREKYQLQDRVELLGAVPHEEVRDVLVQGHIFLNTSLTEAFCIAIVEAASCGLLVVSTRVGGIPEVLPPDMILLAEPDPE 321

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 57226667 667 DVIRALTHAIHTIQSSRHSPWSAHIRVRDMYSWSHVSSRAEIVYLRAMSRPHREIGERMRRYLELGPVFGVVMCCIL 743
Cdd:cd03796 322 DIVRKLEEAISILRTGKHDPWSFHNRVKKMYSWEDVARRTEKVYDRILSTPNRPFLERLKRYYNCGPIAGKIFCLLA 398
PlsC COG0204
1-acyl-sn-glycerol-3-phosphate acyltransferase [Lipid transport and metabolism]; ...
 42-255 4.70e-53

1-acyl-sn-glycerol-3-phosphate acyltransferase [Lipid transport and metabolism]; 1-acyl-sn-glycerol-3-phosphate acyltransferase is part of the Pathway/BioSystem: Phospholipid biosynthesis


Pssm-ID: 439974 [Multi-domain]  Cd Length: 215  Bit Score: 183.29  E-value: 4.70e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667  42 YFVARTFYCIAGTILGWKFQVEGEQYLwelsgehgggkanEKGRSMVMVGNHQSFVDILYLGRIFPKHAAIMAKKSIQWI 121
Cdd:COG0204  13 YRLVRLWARLLLRLLGVRVRVEGLENL-------------PADGPVLIVANHQSWLDILLLLAALPRPVRFVAKKELFKI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 122 PGLGWFMMMSGTVFINRSNNKSAIASLQHAGEEMKRKRiSLWIFPEGTRhnTPEPELLNFKKGAFYLAVQAGVPIVPVVC 201
Cdd:COG0204  80 PLLGWLLRALGAIPVDRSKRRAALRALRQAVEALKAGE-SLVIFPEGTR--SPDGRLLPFKTGAARLALEAGVPIVPVAI 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 57226667 202 ENYNHLFNGKSHFRRGTLRIKVLPPISTTGLTAADVPGLIERTRNAMLETLQEI 255
Cdd:COG0204 157 DGTERALPKGFLPRPGKVTVRIGPPIDPSDLEGEDRRELAERLRAAIEALLAEL 210
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 347-705 1.28e-52

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: 186.97  E-value: 1.28e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 347 IAMVSDFFFPVIGGVEGHIYSLSVELMRRGHKVIVITHSHPDRLgiHYLEPSLKVYYLPYLPIAssasLPNFLLFLPYFR 426
Cdd:cd03801   2 ILLLSPELPPPVGGAERHVRELARALAARGHDVTVLTPADPGEP--PEELEDGVIVPLLPSLAA----LLRARRLLRELR 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 427 HIILTENIQLVHGHGALSSLAheAVIHAPLLGVKAVFTDHSL-FGFGDAVGVLTNKLL---GAALRCVDEVICVSNTGRE 502
Cdd:cd03801  76 PLLRLRKFDVVHAHGLLAALL--AALLALLLGAPLVVTLHGAePGRLLLLLAAERRLLaraEALLRRADAVIAVSEALRD 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 503 NTVLRAQLDPSIVSVIPNALEAEHFKPDPFRA---DPDWITIVVISRLVHRKGIDLLISSAPQICALFPKVRF-IVGGDG 578
Cdd:cd03801 154 ELRALGGIPPEKIVVIPNGVDLERFSPPLRRKlgiPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLvIVGGDG 233

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 579 PKMVELEQMreKYELQGRVELLGRVNPGDVRDVLTKGQIYLSNSLTEAFGISIIEAASAGLFVVATKVGGVPEILpQDMI 658
Cdd:cd03801 234 PLRAELEEL--ELGLGDRVRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVV-EDGE 310

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 57226667 659 EFCRADEDDViRALTHAIHTI-----QSSRHSpWSAHIRVRDMYSWSHVSSR 705
Cdd:cd03801 311 GGLVVPPDDV-EALADALLRLladpeLRARLG-RAARERVAERFSWERVAER 360
LPLAT_AGPAT-like cd07989
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: AGPAT-like; ...
 55-245 2.55e-46

Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: AGPAT-like; Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are such LPLATs as 1-acyl-sn-glycerol-3-phosphate acyltransferase (AGPAT, PlsC), Tafazzin (product of Barth syndrome gene), and similar proteins.


Pssm-ID: 153251 [Multi-domain]  Cd Length: 184  Bit Score: 163.21  E-value: 2.55e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667  55 ILGWKFQVEGEQYLwelsgehgggkanEKGRSMVMVGNHQSFVDILYLGRIFPKHAAIMAKKSIQWIPGLGWFMMMSGTV 134
Cdd:cd07989   7 LLGVRVRVEGLENL-------------PPKGPVIIVANHQSYLDPLVLGAALPRPIRFVAKKELFKIPFLGWLLRLLGAI 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 135 FINRSNNKSAIASLQHAGEEMKRKRiSLWIFPEGTRhnTPEPELLNFKKGAFYLAVQAGVPIVPVVCENYNH-LFNGKSH 213
Cdd:cd07989  74 PIDRGNGRSAREALREAIEALKEGE-SVVIFPEGTR--SRDGELLPFKSGAFRLAKEAGVPIVPVAISGTWGsLPKGKKL 150

                       170       180       190
                ....*....|....*....|....*....|....
gi 57226667 214 FRRGTLRIKVLPPISTTGL--TAADVPGLIERTR 245
Cdd:cd07989 151 PRPGRVTVRIGEPIPPEGLelAEEDRKELREKVR 184
PIGA pfam08288
PIGA (GPI anchor biosynthesis); This domain is found on phosphatidylinositol ...
 384-473 3.57e-45

PIGA (GPI anchor biosynthesis); This domain is found on phosphatidylinositol n-acetylglucosaminyltransferase proteins. These proteins are involved in GPI anchor biosynthesis and are associated with disease the paroxysmal nocturnal haemoglobinuria.


Pssm-ID: 400541  Cd Length: 90  Bit Score: 156.65  E-value: 3.57e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667   384 HSHPDRLGIHYLEPSLKVYYLPYLPIASSASLPNFLLFLPYFRHIILTENIQLVHGHGALSSLAHEAVIHAPLLGVKAVF 463
Cdd:pfam08288   1 HAYGDRTGVRYLTNGLKVYYVPFLVIYRQSTFPTVFGTFPLFRNILLRERIDIVHGHGSFSTLAHEAILHARTMGLKTVF 80

                          90
                  ....*....|
gi 57226667   464 TDHSLFGFGD 473
Cdd:pfam08288  81 TDHSLFGFAD 90
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 353-655 5.72e-42

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: 156.36  E-value: 5.72e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 353 FFFPVIGGVEGHIYSLSVELMRRGHKVIVITHSHPdrlgihyLEPSLKVYYLPYlpiaSSASLPNFLLFLPYFRHIILT- 431
Cdd:cd03819   5 TPALEIGGAETYILDLARALAERGHRVLVVTAGGP-------LLPRLRQIGIGL----PGLKVPLLRALLGNVRLARLIr 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 432 -ENIQLVHGHGALSSLAheAVIHAPLLGVKAVFTDHSLfgfgDAVGVLTNKLLGAALRCVDEVICVSNTGRENTVLRAQL 510
Cdd:cd03819  74 rERIDLIHAHSRAPAWL--GWLASRLTGVPLVTTVHGS----YLATYHPKDFALAVRARGDRVIAVSELVRDHLIEALGV 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 511 DPSIVSVIPNALEAEHFKPDPFRADPDWI-------TIVVISRLVHRKGIDLLIssapQICALFPK---VRFIVGGDGPK 580
Cdd:cd03819 148 DPERIRVIPNGVDTDRFPPEAEAEERAQLglpegkpVVGYVGRLSPEKGWLLLV----DAAAELKDepdFRLLVAGDGPE 223

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57226667 581 MVELEQMREKYELQGRVELLGRVNpgDVRDVLTKGQIYLSNSLTEAFGISIIEAASAGLFVVATKVGGVPEILPQ 655
Cdd:cd03819 224 RDEIRRLVERLGLRDRVTFTGFRE--DVPAALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGAREIVVH 296
AGP_acyltrn TIGR00530
1-acyl-sn-glycerol-3-phosphate acyltransferases; This model describes the core homologous ...
 88-201 8.03e-37

1-acyl-sn-glycerol-3-phosphate acyltransferases; This model describes the core homologous region of a collection of related proteins, several of which are known to act as 1-acyl-sn-glycerol-3-phosphate acyltransferases (EC 2.3.1.51). Proteins scoring above the trusted cutoff are likely to have the same general activity. However, there is variation among characterized members as to whether the acyl group can be donated by acyl carrier protein or coenzyme A, and in the length and saturation of the donated acyl group. 1-acyl-sn-glycerol-3-phosphate acyltransferase is also called 1-AGP acyltransferase, lysophosphatidic acid acyltransferase, and LPA acyltransferase. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 129621 [Multi-domain]  Cd Length: 130  Bit Score: 134.40  E-value: 8.03e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667    88 VMVGNHQSFVDILYLGRIFPKHAAIMAKKSIQWIPGLGWFMMMSGTVFINRsNNKSAIASLQHAGEEMKRKRISLWIFPE 167
Cdd:TIGR00530  19 LVVANHQSNLDPLTLSAAFPPPIVFIAKKELKWIPFFGIMLWLTGAIFIDR-ENIRAIATALKAAIEVLKQGRSIGVFPE 97

                          90       100       110
                  ....*....|....*....|....*....|....
gi 57226667   168 GTRhnTPEPELLNFKKGAFYLAVQAGVPIVPVVC 201
Cdd:TIGR00530  98 GTR--SRGRDILPFKKGAFHIAIKAGVPILPVVL 129
Acyltransferase pfam01553
Acyltransferase; This family contains acyltransferases involved in phospholipid biosynthesis ...
 59-201 3.71e-35

Acyltransferase; This family contains acyltransferases involved in phospholipid biosynthesis and other proteins of unknown function. This family also includes tafazzin, the Barth syndrome gene.


Pssm-ID: 366704 [Multi-domain]  Cd Length: 131  Bit Score: 129.71  E-value: 3.71e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667    59 KFQVEGEQYLwelsgehgggkanEKGRSMVMVGNHQSFVDILYLGRIFPKHA---AIMAKKSIQWIPGLGWFMMMSGTVF 135
Cdd:pfam01553   1 RIEVHGLENL-------------PRGGPAIVVANHQSYLDVLLLSLALYKRGrplVFVAKKELFDIPLVGWLMRLLGCIF 67

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57226667   136 INRSNNKSAIASLQHAGEEMKRKRiSLWIFPEGTRhnTPEPELLNFKKGAFYLAVQAGVPIVPVVC 201
Cdd:pfam01553  68 IDRKNRKDAAGTLEYLVELLREGK-LVVIFPEGTR--SREGELLPFKKGAFRLAIEAGVPIVPVAI 130
PlsC smart00563
Phosphate acyltransferases; Function in phospholipid biosynthesis and have either ...
 87-201 4.96e-35

Phosphate acyltransferases; Function in phospholipid biosynthesis and have either glycerolphosphate, 1-acylglycerolphosphate, or 2-acylglycerolphosphoethanolamine acyltransferase activities. Tafazzin, the product of the gene mutated in patients with Barth syndrome, is a member of this family.


Pssm-ID: 214724 [Multi-domain]  Cd Length: 118  Bit Score: 129.01  E-value: 4.96e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667     87 MVMVGNHQSFVDILYLGRIFPKHAA---IMAKKSIQWIPGLGWFMMMSGTVFINRSNNKSAIASLQHAGeEMKRKRISLW 163
Cdd:smart00563   1 ALVVANHQSFLDPLVLSALLPRKLGrvrFVAKKELFYVPLLGWLLRLLGAIFIDRSNGRKARAALREAV-ELLKEGEWLL 79

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 57226667    164 IFPEGTRhnTPEPELLNFKKGAFYLAVQAGVPIVPVVC 201
Cdd:smart00563  80 IFPEGTR--SRPGKLLPFKKGAARLALEAGVPIVPVAI 115
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 359-653 4.76e-34

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: 133.64  E-value: 4.76e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 359 GGVEGHIYSLSVELMRRGHKVIVITHSHPdrlGIHYLEPSLKVYYLPYLPIASSASLPNFLLFLPYFRHIILTENIQLVH 438
Cdd:cd03811  12 GGAERVLLNLANALDKRGYDVTLVLLRDE---GDLDKQLNGDVKLIRLLIRVLKLIKLGLLKAILKLKRILKRAKPDVVI 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 439 GHGALSSLAheaVIHAPLLGVKAVFTDHSLFgFGDAVGVLTNKLLGAALRCVDEVICVSNTGRENTVLRAQLDPSIVSVI 518
Cdd:cd03811  89 SFLGFATYI---VAKLAAARSKVIAWIHSSL-SKLYYLKKKLLLKLKLYKKADKIVCVSKGIKEDLIRLGPSPPEKIEVI 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 519 PNALEAEHFKPDPFRADPDW----ITIVVISRLVHRKGIDLLISSAPQICALFPKVRFIVGGDGPKMVELEQMREKYELQ 594
Cdd:cd03811 165 YNPIDIDRIRALAKEPILNEpedgPVILAVGRLDPQKGHDLLIEAFAKLRKKYPDVKLVILGDGPLREELEKLAKELGLA 244

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 57226667 595 GRVELLGRVNpgDVRDVLTKGQIYLSNSLTEAFGISIIEAASAGLFVVATKVGGVPEIL 653
Cdd:cd03811 245 ERVIFLGFQS--NPYPYLKKADLFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPREIL 301
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 347-705 7.52e-32

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: 128.51  E-value: 7.52e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 347 IAMVS--DFFFPVIGGVEG-----HIYSLSVELMRRGHKVIVITHSHPDRLG-IHYLEPSLKVYYLPYLPiassaslPNF 418
Cdd:cd03800   2 IALISvhGSPLAQPGGADTggqnvYVLELARALAELGYQVDIFTRRISPADPeVVEIAPGARVIRVPAGP-------PEY 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 419 LL------FLPYF-----RHIiLTENIQ--LVHGHGALSSLAheAVIHAPLLGVKAVFTDHSLfgfgdavGVLTNKLLGA 485
Cdd:cd03800  75 LPkeelwpYLEEFadgllRFI-AREGGRydLIHSHYWDSGLV--GALLARRLGVPLVHTFHSL-------GRVKYRHLGA 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 486 ---------------ALRCVDEVIcvSNTGRENTVLRA--QLDPSIVSVIPNALEAEHFKPDP--------FRADPDWIT 540
Cdd:cd03800 145 qdtyhpslritaeeqILEAADRVI--ASTPQEADELISlyGADPSRINVVPPGVDLERFFPVDraearrarLLLPPDKPV 222

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 541 IVVISRLVHRKGIDLLISSAPQICALFPKVRF-IVGGDGPKM-----VELEQMREKYELQGRVELLGRVNPGDVRDVLTK 614
Cdd:cd03800 223 VLALGRLDPRKGIDTLVRAFAQLPELRELANLvLVGGPSDDPlsmdrEELAELAEELGLIDRVRFPGRVSRDDLPELYRA 302

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 615 GQIYLSNSLTEAFGISIIEAASAGLFVVATKVGGVPEIL----------PQDMIEFCRAdeddVIRALTHAIHTIQSSRh 684
Cdd:cd03800 303 ADVFVVPSLYEPFGLTAIEAMACGTPVVATAVGGLQDIVrdgrtgllvdPHDPEALAAA----LRRLLDDPALWQRLSR- 377

                       410       420
                ....*....|....*....|.
gi 57226667 685 spwSAHIRVRDMYSWSHVSSR 705
Cdd:cd03800 378 ---AGLERARAHYTWESVADQ 395
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
 359-674 7.68e-32

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: 127.82  E-value: 7.68e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 359 GGVEGHIYSLSVELMRRGHKVIVITHSHPDRLGIHYLEPSLKVYYLPylpiassASLPNFLLFLPYFRHIILTENIQLVH 438
Cdd:cd03807  12 GGAETMLLRLLEHMDKSRFEHVVISLTGDGVLGEELLAAGVPVVCLG-------LSSGKDPGVLLRLAKLIRKRNPDVVH 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 439 GHGALSSLAheAVIHAPLLGVKAVF-TDHSLFGFGDAVGVLtNKLLGAALRCVDEVICVSNTGREntVLRAQ-LDPSIVS 516
Cdd:cd03807  85 TWMYHADLI--GGLAAKLAGGVKVIwSVRSSNIPQRLTRLV-RKLCLLLSKFSPATVANSSAVAE--FHQEQgYAKNKIV 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 517 VIPNALEAEHFKPDPFRADP---------DWITIVVISRLVHRKGIDLLISSAPQICALFPKVRFIVGGDGPKMVELEQM 587
Cdd:cd03807 160 VIYNGIDLFKLSPDDASRARarrrlglaeDRRVIGIVGRLHPVKDHSDLLRAAALLVETHPDLRLLLVGRGPERPNLERL 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 588 REKYELQGRVELLGRVnpGDVRDVLTKGQIYLSNSLTEAFGISIIEAASAGLFVVATKVGGVPEILPqDMIEFCRADED- 666
Cdd:cd03807 240 LLELGLEDRVHLLGER--SDVPALLPAMDIFVLSSRTEGFPNALLEAMACGLPVVATDVGGAAELVD-DGTGFLVPAGDp 316

                       330
                ....*....|..
gi 57226667 667 ----DVIRALTH 674
Cdd:cd03807 317 qalaDAIRALLE 328
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 353-713 3.16e-31

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: 126.34  E-value: 3.16e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 353 FFFP--VIGGVEGHIYSLSVELMRRGHKVIVIT----HSHPDRLGIHYLEPSLKV---------YYLPYLPIASSASLPN 417
Cdd:cd03798   6 NIYPnaNSPGRGIFVRRQVRALSRRGVDVEVLApapwGPAAARLLRKLLGEAVPPrdgrrllplKPRLRLLAPLRAPSLA 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 418 FLLFlpYFRHiiltENIQLVHGHGALSSLAhEAVIHAPLLGVKAVFTDHSLFGFGDAVGVLTNKLLGAALRCVDEVICVS 497
Cdd:cd03798  86 KLLK--RRRR----GPPDLIHAHFAYPAGF-AAALLARLYGVPYVVTEHGSDINVFPPRSLLRKLLRWALRRAARVIAVS 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 498 nTGRENTVLRAQLDPSIVSVIPNALEAEHFKP--DPFRADPDWITIVVISRLVHRKGIDLLISSAPQICALFPKVRFIVG 575
Cdd:cd03798 159 -KALAEELVALGVPRDRVDVIPNGVDPARFQPedRGLGLPLDAFVILFVGRLIPRKGIDLLLEAFARLAKARPDVVLLIV 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 576 GDGPKMVELEQMREKYELQGRVELLGRVNPGDVRDVLTKGQIYLSNSLTEAFGISIIEAASAGLFVVATKVGGVPEIL-- 653
Cdd:cd03798 238 GDGPLREALRALAEDLGLGDRVTFTGRLPHEQVPAYYRACDVFVLPSRHEGFGLVLLEAMACGLPVVATDVGGIPEVVgd 317

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 654 PQDMIEFCRADEDDVIRALTHAIHTIQSSRhSPWSAHIRVRDMYSWSHVSSRAEIVYLRA 713
Cdd:cd03798 318 PETGLLVPPGDADALAAALRRALAEPYLRE-LGEAARARVAERFSWVKAADRIAAAYRDV 376
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 357-652 1.81e-29

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: 120.39  E-value: 1.81e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 357 VIGGVEGHIYSLSVELMRRGHKVIVITHSHPDRlgIHYLEpSLKVYYLPYlPIASSASLP-NFLLFLPYFRHIILTENIQ 435
Cdd:cd03808   8 VDGGFQSFRLPLIKALVKKGYEVHVIAPDGDKL--SDELK-ELGVKVIDI-PILRRGINPlKDLKALFKLYKLLKKEKPD 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 436 LVHGH----GALSSLAheavihAPLLGVKA-VFTDHSLfGFGDAVGVLTNKLLGA----ALRCVDEVICVSNTGRENTV- 505
Cdd:cd03808  84 IVHCHtpkpGILGRLA------ARLAGVPKvIYTVHGL-GFVFTEGKLLRLLYLLleklALLFTDKVIFVNEDDRDLAIk 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 506 LRAQLDPSIVSVIPNALEAEHFKPDPFRADPDWITIVVISRLVHRKGIDLLISSAPQICALFPKVRFIVGGDGPKMVELE 585
Cdd:cd03808 157 KGIIKKKKTVLIPGSGVDLDRFQYSPESLPSEKVVFLFVARLLKDKGIDELIEAAKILKKKGPNVRFLLVGDGELENPSE 236

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 57226667 586 QMREKYELQGRVELLGRVNpgDVRDVLTKGQIYLSNSLTEAFGISIIEAASAGLFVVATKVGGVPEI 652
Cdd:cd03808 237 ILIEKLGLEGRIEFLGFRS--DVPELLAESDVFVLPSYREGLPRSLLEAMAAGRPVITTDVPGCREL 301
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
 346-653 1.63e-28

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: 118.15  E-value: 1.63e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 346 VIAMVSDFFFPVIGGVEGHIYSLSVELMRRGHKVIVITHSHPDRlgihylEPSLKVYYLPYLPIASSASLPNFLLFLPYF 425
Cdd:cd03817   1 KIAIFTDTYLPQVNGVATSVRNLARALEKRGHEVYVITPSDPGA------EDEEEVVRYRSFSIPIRKYHRQHIPFPFKK 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 426 RHIILTE--NIQLVHGHGALSS------LAHEavIHAPLlgvkaVFTDHSL---------FGFGDAVGVLTnKLLGAALR 488
Cdd:cd03817  75 AVIDRIKelGPDIIHTHTPFSLgklglrIARK--LKIPI-----VHTYHTMyedylhyipKGKLLVKAVVR-KLVRRFYN 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 489 CVDEVICVSNTGREntVLRAQLDPSIVSVIPNALEAEHFKPDP-------FRADPDWITIVVISRLVHRKGIDLLISSAP 561
Cdd:cd03817 147 HTDAVIAPSEKIKD--TLREYGVKGPIEVIPNGIDLDKFEKPLnteerrkLGLPPDEPILLYVGRLAKEKNIDFLLRAFA 224

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 562 QICALfPKVRFIVGGDGPKMVELEQMREKYELQGRVELLGRVNPGDVRDVLTKGQIYLSNSLTEAFGISIIEAASAGLFV 641
Cdd:cd03817 225 ELKKE-PNIKLVIVGDGPEREELKELARELGLADKVIFTGFVPREELPEYYKAADLFVFASTTETQGLVYLEAMAAGLPV 303

                       330
                ....*....|..
gi 57226667 642 VATKVGGVPEIL 653
Cdd:cd03817 304 VAAKDPAASELV 315
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 539-653 1.18e-27

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: 109.29  E-value: 1.18e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667   539 ITIVVISRLVHRKGIDLLISSAPQICALFPKVRFIVGGDGPKMVELEQMREKYELQGRVELLGRVNPGDVRDVLTKGQIY 618
Cdd:pfam00534   3 KIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVSDEDLPELLKIADVF 82

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 57226667   619 LSNSLTEAFGISIIEAASAGLFVVATKVGGVPEIL 653
Cdd:pfam00534  83 VLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVV 117
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
 358-653 2.54e-25

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: 108.09  E-value: 2.54e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 358 IGGVEGHIYSLSVELMRRGHKVIVITHSHPDRLGIHYLEPSLKVYYLPYLPIASSASLPNFLLFLPYFRHIILTENIQLV 437
Cdd:cd03820  12 AGGAERVAINLANHLAKKGYDVTIISLDSAEKPPFYELDDNIKIKNLGDRKYSHFKLLLKYFKKVRRLRKYLKNNKPDVV 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 438 --HGHGALSSLAheaVIHaplLGVKAVFTDH-SLFGFGDAVGVLTNKLLgaALRCVDEVICVSNTGRENtvlRAQLDPSI 514
Cdd:cd03820  92 isFRTSLLTFLA---LIG---LKSKLIVWEHnNYEAYNKGLRRLLLRRL--LYKRADKIVVLTEADKLK---KYKQPNSN 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 515 VSVIPNALEaehfkPDPFRADPDWI--TIVVISRLVHRKGIDLLISSAPQICALFP--KVRfIVGgDGPKMVELEQMREK 590
Cdd:cd03820 161 VVVIPNPLS-----FPSEEPSTNLKskRILAVGRLTYQKGFDLLIEAWALIAKKHPdwKLR-IYG-DGPEREELEKLIDK 233

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57226667 591 YELQGRVELLGRVNpgDVRDVLTKGQIYLSNSLTEAFGISIIEAASAGLFVVATK-VGGVPEIL 653
Cdd:cd03820 234 LGLEDRVKLLGPTK--NIAEEYANSSIFVLSSRYEGFPMVLLEAMAYGLPIISFDcPTGPSEII 295
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
 347-654 8.51e-24

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: 103.95  E-value: 8.51e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 347 IAMVSDFFFP-VIGGVEGHIYSLSVELMRRGHKVIVIT-HSHP------DRLGIHYLEPSLKVYYLPYLPIASSASLP-N 417
Cdd:cd03823   2 ILLVNSLYPPqRVGGAEISVHDLAEALVAEGHEVAVLTaGVGPpgqatvARSVVRYRRAPDETLPLALKRRGYELFETyN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 418 FLLFlPYFRHIILTENIQLVHGHgALSSLAHEAVIHAPLLGVKAVFTDHSLFGFGDAVGVLTNKllgaalrcVDEVICVS 497
Cdd:cd03823  82 PGLR-RLLARLLEDFRPDVVHTH-NLSGLGASLLDAARDLGIPVVHTLHDYWLLCPRQFLFKKG--------GDAVLAPS 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 498 NTgRENTVLRAQLDPSIVSVIPNALEAEHFKPDPFRADPDWITIVVISRLVHRKGIDLLISSAPQIcaLFPKVRFIVGGD 577
Cdd:cd03823 152 RF-TANLHEANGLFSARISVIPNAVEPDLAPPPRRRPGTERLRFGYIGRLTEEKGIDLLVEAFKRL--PREDIELVIAGH 228

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 57226667 578 GPkmvelEQMREKYELQGRVELLGRVNPGDVRDVLTKGQIYLSNSL-TEAFGISIIEAASAGLFVVATKVGGVPEILP 654
Cdd:cd03823 229 GP-----LSDERQIEGGRRIAFLGRVPTDDIKDFYEKIDVLVVPSIwPEPFGLVVREAIAAGLPVIASDLGGIAELIQ 301
PLN02901 PLN02901
1-acyl-sn-glycerol-3-phosphate acyltransferase
 88-253 8.33e-23

1-acyl-sn-glycerol-3-phosphate acyltransferase


Pssm-ID: 215488 [Multi-domain]  Cd Length: 214  Bit Score: 97.49  E-value: 8.33e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667   88 VMVGNHQSFVDI---LYLGRIFpkhaAIMAKKSIQWIPGLGWFMMMSGTVFINRSNNKSAIASLQHAgEEMKRKRISLWI 164
Cdd:PLN02901  53 VYVSNHQSFLDIytlFHLGRPF----KFISKTSIFLIPIIGWAMYMTGHIPLKRMDRRSQLECLKRC-MELLKKGASVFF 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667  165 FPEGTRhnTPEPELLNFKKGAFYLAVQAGVPIVPVVCENYNHLF-NGKSH-FRRGTLRIKVLPPISTTGltaADVpgLIE 242
Cdd:PLN02901 128 FPEGTR--SKDGKLAAFKKGAFSVAAKTGVPVVPITLVGTGKIMpNGKEGiLNPGSVKVVIHPPIEGSD---ADE--LCN 200

                        170
                 ....*....|.
gi 57226667  243 RTRNAMLETLQ 253
Cdd:PLN02901 201 EARKVIAESLV 211
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
540-677 1.02e-22

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 94.50  E-value: 1.02e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667   540 TIVVISRLVHR-KGIDLLISSAPQICALFPKVRFIVGGDGPKMvELEQMREKyeLQGRVELLGRVNpgDVRDVLTKGQIY 618
Cdd:pfam13692   3 VILFVGRLHPNvKGVDYLLEAVPLLRKRDNDVRLVIVGDGPEE-ELEELAAG--LEDRVIFTGFVE--DLAELLAAADVF 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667   619 LSNSLTEAFGISIIEAASAGLFVVATKVGGVPEILP-QDMIEFCRADEDDVIRALTHAIH 677
Cdd:pfam13692  78 VLPSLYEGFGLKLLEAMAAGLPVVATDVGGIPELVDgENGLLVPPGDPEALAEAILRLLE 137
PRK15018 PRK15018
1-acyl-sn-glycerol-3-phosphate acyltransferase; Provisional
 88-266 8.00e-22

1-acyl-sn-glycerol-3-phosphate acyltransferase; Provisional


Pssm-ID: 184979  Cd Length: 245  Bit Score: 95.47  E-value: 8.00e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667   88 VMVGNHQSFVDILYLGRIFPKHAAIMAKKSIQWIPGLGWFMMMSGTVFINRSNNKSAIASLQHAGEEMKRKRISLWIFPE 167
Cdd:PRK15018  68 IYIANHQNNYDMVTASNIVQPPTVTVGKKSLLWIPFFGQLYWLTGNLLIDRNNRTKAHGTIAEVVNHFKKRRISIWMFPE 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667  168 GTRhnTPEPELLNFKKGAFYLAVQAGVPIVPVVCENYNHLFNgKSHFRRGTLRIKVLPPISTTGLTAADVPGLIERTRNA 247
Cdd:PRK15018 148 GTR--SRGRGLLPFKTGAFHAAIAAGVPIIPVCVSTTSNKIN-LNRLHNGLVIVEMLPPIDVSQYGKDQVRELAAHCRSI 224

                        170
                 ....*....|....*....
gi 57226667  248 MLETLQEISTPSQSTSQAG 266
Cdd:PRK15018 225 MEQKIAELDKEVAEREAAG 243
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
359-525 1.66e-21

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 92.21  E-value: 1.66e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667   359 GGVEGHIYSLSVELMRRGHKVIVITHSHPDRLGihylEPSLKVYYLPYLPIASSASLPNFLLFLPYFRHIILTENIQLVH 438
Cdd:pfam13439   1 GGVERYVLELARALARRGHEVTVVTPGGPGPLA----EEVVRVVRVPRVPLPLPPRLLRSLAFLRRLRRLLRRERPDVVH 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667   439 GHGALSSLAhEAVIHAPLLGVKAVFTDHSLFGFGDAVG-------VLTNKLLGAALRCVDEVICVSNTGRENTVLRAQLD 511
Cdd:pfam13439  77 AHSPFPLGL-AALAARLRLGIPLVVTYHGLFPDYKRLGarlsplrRLLRRLERRLLRRADRVIAVSEAVADELRRLYGVP 155

                         170
                  ....*....|....
gi 57226667   512 PSIVSVIPNALEAE 525
Cdd:pfam13439 156 PEKIRVIPNGVDLE 169
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 347-656 6.60e-21

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: 92.47  E-value: 6.60e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 347 IAMVSDFFFPVIGGVEGHIYSLSVELMRRGHKVIVIThshpdrlgihylepslkvyylpylpiassaslpNFLLFLPYFR 426
Cdd:cd01635   1 ILLVTGEYPPLRGGLELHVRALARALAALGHEVTVLA---------------------------------LLLLALRRIL 47

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 427 HIILTENIQLVHGHgALSSLAHEAVIHAPLLGVKAVFTDHSLFGFgdavgvlTNKLLGAALRCVDEVICvsntgrentvl 506
Cdd:cd01635  48 KKLLELKPDVVHAH-SPHAAALAALLAARLLGIPIVVTVHGPDSL-------ESTRSELLALARLLVSL----------- 108

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 507 raqldpsivsvipnaleaehfkpdpfradpDWITIVVISRLVHRKGIDLLISSAPQICALFPKVRFIVGGDGPKMVELEQ 586
Cdd:cd01635 109 ------------------------------PLADKVSVGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEA 158

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 57226667 587 MREKYELQGRVELLGRVNPGDVRDVLTKG-QIYLSNSLTEAFGISIIEAASAGLFVVATKVGGVPEILPQD 656
Cdd:cd01635 159 LAAALGLLERVVIIGGLVDDEVLELLLAAaDVFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDG 229
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 347-679 4.84e-20

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: 92.81  E-value: 4.84e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 347 IAMVSDFFFPVIGGVEGHIYSLSVELMRRGHKVIVITHSHPDRlgihYLEPSLKVYYLPYLPIASSASLPNFLLFLPYFR 426
Cdd:cd03809   2 ILIDGRSLAQRLTGIGRYTRELLKALAKNDPDESVLAVPPLPG----ELLRLLREYPELSLGVIKIKLWRELALLRWLQI 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 427 HIILTENIQLVHghgalsSLAHEAVIHapLLGVKAVFTDHSLF------GFGDAVGVLTNKLLGAALRCVDEVICVSNTG 500
Cdd:cd03809  78 LLPKKDKPDLLH------SPHNTAPLL--LKGCPQVVTIHDLIplrypeFFPKRFRLYYRLLLPISLRRADAIITVSEAT 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 501 RENTVLRAQLDPSIVSVIPNALEAEHFKPDP-------FRADPDWItiVVISRLVHRKGIDLLISSAPQICALFPKVR-F 572
Cdd:cd03809 150 RDDIIKFYGVPPEKIVVIPLGVDPSFFPPESaavliakYLLPEPYF--LYVGTLEPRKNHERLLKAFALLKKQGGDLKlV 227

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 573 IVGGDGPKMVELEQMREKYELQGRVELLGRVNPGDVRDVLTKGQIYLSNSLTEAFGISIIEAASAGLFVVATKVGGVPEI 652
Cdd:cd03809 228 IVGGKGWEDEELLDLVKKLGLGGRVRFLGYVSDEDLPALYRGARAFVFPSLYEGFGLPVLEAMACGTPVIASNISVLPEV 307

                       330       340
                ....*....|....*....|....*..
gi 57226667 653 LPQDMIEFcraDEDDVIrALTHAIHTI 679
Cdd:cd03809 308 AGDAALYF---DPLDPE-SIADAILRL 330
LPLAT cd06551
Lysophospholipid acyltransferases (LPLATs) of glycerophospholipid biosynthesis; ...
 54-243 7.65e-20

Lysophospholipid acyltransferases (LPLATs) of glycerophospholipid biosynthesis; Lysophospholipid acyltransferase (LPLAT) superfamily members are acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis. These proteins catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this superfamily are LPLATs such as glycerol-3-phosphate 1-acyltransferase (GPAT, PlsB), 1-acyl-sn-glycerol-3-phosphate acyltransferase (AGPAT, PlsC), lysophosphatidylcholine acyltransferase 1 (LPCAT-1), lysophosphatidylethanolamine acyltransferase (LPEAT, also known as, MBOAT2, membrane-bound O-acyltransferase domain-containing protein 2), lipid A biosynthesis lauroyl/myristoyl acyltransferase, 2-acylglycerol O-acyltransferase (MGAT), dihydroxyacetone phosphate acyltransferase (DHAPAT, also known as 1 glycerol-3-phosphate O-acyltransferase 1) and Tafazzin (the protein product of the Barth syndrome (TAZ) gene).


Pssm-ID: 153244 [Multi-domain]  Cd Length: 187  Bit Score: 87.85  E-value: 7.65e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667  54 TILGWKFQVEGEQylwelsgehgggkANEKGRSMVMVGNHQSFVDILYL----GRIFPK-HAAIMAKKSIQWIPGLGWfm 128
Cdd:cd06551   8 FFGFVRLEVKGPP-------------PPPGGGPVLFVSNHSSWWDGLILflllERGLRRdVYGLMDEELLERYPFFTR-- 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 129 mmSGTVFINRSNNKSAIASLQHAGEEMKRKRISLWIFPEGTRHNtPEPELLNFKKGAFYLAVQAGVPIVPVVcenynhLF 208
Cdd:cd06551  73 --LGAFSVDRDSPRSAAKSLKYVARLLSKPGSVVWIFPEGTRTR-RDKRPLQFKPGVAHLAEKAGVPIVPVA------LR 143

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 57226667 209 NGKSHF-RRGTLRIKVLPPISTT-----GLTAADVPGLIER 243
Cdd:cd06551 144 YTFELFeQFPEIFVRIGPPIPYAetalgEELAAELANRLTR 184
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
 355-676 8.60e-20

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: 92.03  E-value: 8.60e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 355 FPVIGGvEGHIYS-LSVELMRRGHKVIVITHSHPDRLG-----IHYLE---PSLKVYYLPYLPIASSASLPNfllflpyf 425
Cdd:cd04962   8 YPSYGG-SGVVATeLGLELAERGHEVHFISSAIPFRLNlysgnIFFHEvevPNYPLFEYPPYTLALASKIVE-------- 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 426 rhIILTENIQLVHGHGAL-----SSLAHEAVIHAP-----LLG--VKAVFTDHSlfgFGDAVGVLTNKllgaalrcVDEV 493
Cdd:cd04962  79 --VAKEHKLDVLHAHYAIphascAYLAREILGEKIpivttLHGtdITLVGYDPS---LQPAVRFSINK--------SDRV 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 494 ICVSNTGRENTVLRAQLDPSIvSVIPNALEAEHFKPDPFRAD-------PDWITIVVISRLVHRKGIDLLISSAPQICAL 566
Cdd:cd04962 146 TAVSSSLRQETYELFDVDKDI-EVIHNFIDEDVFKRKPAGALkrrllapPDEKVVIHVSNFRPVKRIDDVVRVFARVRRK 224

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 567 FPkVRFIVGGDGPKMVELEQMREKYELQGRVELLGRVNpgDVRDVLTKGQIYLSNSLTEAFGISIIEAASAGLFVVATKV 646
Cdd:cd04962 225 IP-AKLLLVGDGPERVPAEELARELGVEDRVLFLGKQD--DVEELLSIADLFLLPSEKESFGLAALEAMACGVPVVSSNA 301

                       330       340       350
                ....*....|....*....|....*....|
gi 57226667 647 GGVPEILPQDMIEFcRADEDDVIRALTHAI 676
Cdd:cd04962 302 GGIPEVVKHGETGF-LSDVGDVDAMAKSAL 330
LPLAT_LPCAT1-like cd07991
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LPCAT1-like; ...
 78-200 1.36e-18

Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LPCAT1-like; Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are such LPLATs as lysophosphatidylcholine acyltransferase 1 (LPCAT-1), glycerol-3-phosphate acyltransferase 3 (GPAT3), and similar sequences.


Pssm-ID: 153253 [Multi-domain]  Cd Length: 211  Bit Score: 84.97  E-value: 1.36e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667  78 GKANEKGRSMVMVGNHQSFVDILYLGRIFPkhAAIMAKKSIQWIPGLGWFMMMSGTVFINRSNNKSAiaslQHAGEEMKR 157
Cdd:cd07991  17 GKPDPPEAPRIIVANHTSFIDPLILFSDLF--PSIVAKKELGKLPFIGTILRALGCIFVDRSEPKDR----KKVVEEIKE 90

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 57226667 158 K-----RISLWIFPEGTRHNtpEPELLNFKKGAFYLavqaGVPIVPVV 200
Cdd:cd07991  91 RatdpnWPPILIFPEGTTTN--GKALIMFKKGAFEP----GVPVQPVA 132
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
 346-676 1.72e-17

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: 85.11  E-value: 1.72e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 346 VIAMVSDFFFPVIGGVEGHIYSLSVELMRRGHKVIVITHSHPDRLGIHYL--EPSLKVYYLPYLPIASSaslPNFLLFLP 423
Cdd:cd03821   1 KILHVTPSISPKAGGPVKVVLRLAAALAALGHEVTIVSTGDGYESLVVEEngRYIPPQDGFASIPLLRQ---GAGRTDFS 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 424 YFRHIILTENI---QLVHGHGALSSLAHEAVIHAPLLGVKAVFTDHslfgfGDAVG-----------VLTNKLLGAALRC 489
Cdd:cd03821  78 PGLPNWLRRNLreyDVVHIHGVWTYTSLAACKLARRRGIPYVVSPH-----GMLDPwalqqkhwkkrIALHLIERRNLNN 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 490 VDEVICVSNTGRENtvLRAQLDPSIVSVIPNALEAEHFKPDPFRADPDWIT-----IVVISRLVHRKGIDLLISSAPQIC 564
Cdd:cd03821 153 AALVHFTSEQEADE--LRRFGLEPPIAVIPNGVDIPEFDPGLRDRRKHNGLedrriILFLGRIHPKKGLDLLIRAARKLA 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 565 ALFPKVRFIVGGDGPKMVELE-QMREKYELQGRVELLGRVNPGDVRDVLTKGQIYLSNSLTEAFGISIIEAASAGLFVVA 643
Cdd:cd03821 231 EQGRDWHLVIAGPDDGAYPAFlQLQSSLGLGDRVTFTGPLYGEAKWALYASADLFVLPSYSENFGNVVAEALACGLPVVI 310

                       330       340       350
                ....*....|....*....|....*....|...
gi 57226667 644 TKVGGVPEILPQDMIEFCRADEDDVIRALTHAI 676
Cdd:cd03821 311 TDKCGLSELVEAGCGVVVDPNVSSLAEALAEAL 343
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
 350-648 3.26e-17

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: 83.86  E-value: 3.26e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 350 VSDFFFPVIGGVEGHIYSLSVELMRRGHKVIVITHSHpDRLGIHYLEPSLKVYYLPYlpIASSASLPNFLLFLPYFRhiI 429
Cdd:cd03795   5 VFKFYYPDIGGIEQVIYDLAEGLKKKGIEVDVLCFSK-EKETPEKEENGIRIHRVKS--FLNVASTPFSPSYIKRFK--K 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 430 LTENIQLVHGH--GALSSLAHEAV-IHAPLlgvkaVFTDHSlfgfgDavgVLTNK--------LLGAALRCVDEVICVS- 497
Cdd:cd03795  80 LAKEYDIIHYHfpNPLADLLLFFSgAKKPV-----VVHWHS-----D---IVKQKkllklykpLMTRFLRRADRIIATSp 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 498 NTGRENTVLRAQLDPsiVSVIPNALEAEhfKPDPFRADPDWIT--------IVVISRLVHRKGIDLLISSAPQI-CALFp 568
Cdd:cd03795 147 NYVETSPTLREFKNK--VRVIPLGIDKN--VYNIPRVDFENIKrekkgkkiFLFIGRLVYYKGLDYLIEAAQYLnYPIV- 221

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 569 kvrfiVGGDGPKMVELEQmREKYELQGRVELLGRVNPGDVRDVLTKGQIYL--SNSLTEAFGISIIEAASAGLFVVATKV 646
Cdd:cd03795 222 -----IGGEGPLKPDLEA-QIELNLLDNVKFLGRVDDEEKVIYLHLCDVFVfpSVLRSEAFGIVLLEAMMCGKPVISTNI 295


                ..
gi 57226667 647 GG 648
Cdd:cd03795 296 GT 297
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
 436-651 4.89e-17

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: 83.66  E-value: 4.89e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 436 LVHGH----GALS-SLAHEavIHAPLL----GVKAvFTDHSLFGFGDAVGVLTNKLLGAALRCVDEVICVSNTGREnTVL 506
Cdd:cd05844  84 LVHAHfgrdGVYAlPLARA--LGVPLVvtfhGFDI-TTSRAWLAASPGWPSQFQRHRRALQRPAALFVAVSGFIRD-RLL 159

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 507 RAQLDPSIVSVIPNALEAEHFKPDPFRADPDwiTIVVISRLVHRKGIDLLISSAPQICALFPKVRFIVGGDGPkmvELEQ 586
Cdd:cd05844 160 ARGLPAERIHVHYIGIDPAKFAPRDPAERAP--TILFVGRLVEKKGCDVLIEAFRRLAARHPTARLVIAGDGP---LRPA 234

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 57226667 587 MREKYELQGRVELLGRVNPGDVRDVLTKGQIYLSNSLT------EAFGISIIEAASAGLFVVATKVGGVPE 651
Cdd:cd05844 235 LQALAAALGRVRFLGALPHAEVQDWMRRAEIFCLPSVTaasgdsEGLGIVLLEAAACGVPVVSSRHGGIPE 305
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 347-654 6.09e-17

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: 83.11  E-value: 6.09e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 347 IAMVSDFFFPVIGGVEGHIYSLSVELMRRGHKVIVITHSHPDRlgihYLEPSLKVYYLPYLPIASSASLPNFLLFLPYFR 426
Cdd:cd03814   2 IALVTDTYHPQVNGVVRTLERLVDHLRRRGHEVRVVAPGPFDE----AESAEGRVVSVPSFPLPFYPEYRLALPLPRRVR 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 427 HIILTENIQLVHghgaLSS---LAHEAVIHAPLLGVKAVFTDHSLFG------FGDAVGVLTNKLLGAALRCVDEVICVS 497
Cdd:cd03814  78 RLIKEFQPDIIH----IATpgpLGLAALRAARRLGLPVVTSYHTDFPeylsyyTLGPLSWLAWAYLRWFHNPFDTTLVPS 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 498 NTGREntvLRAQLDPSIVSVIPNALEAEHFKPDpfRADPDW---------ITIVVISRLVHRKGIDLLISSAPQICALFP 568
Cdd:cd03814 154 PSIAR---ELEGHGFERVRLWPRGVDTELFHPS--RRDAALrrrlgppgrPLLLYVGRLAPEKNLEALLDADLPLAASPP 228

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 569 kVRFIVGGDGPkmvELEQMREKYeLQgrVELLGRVNPGDVRDVLTKGQIYLSNSLTEAFGISIIEAASAGLFVVATKVGG 648
Cdd:cd03814 229 -VRLVVVGDGP---ARAELEARG-PD--VIFTGFLTGEELARAYASADVFVFPSRTETFGLVVLEAMASGLPVVAADAGG 301


                ....*.
gi 57226667 649 VPEILP 654
Cdd:cd03814 302 PRDIVR 307
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
 347-676 2.35e-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: 2.35e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 347 IAMVSDFFFPVIGGVEGHIYSLSVELMRRGHKVIVITHSHPDRLGIHYLEPS-----LKVYYLPYLPIASSASLPNFLLF 421
Cdd:cd03794   2 ILLISQYYPPPKGAAAARVYELAKELVRRGHEVTVLTPSPNYPLGRIFAGATetkdgIRVIRVKLGPIKKNGLIRRLLNY 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 422 LPYFRHIIL-----TENIQLVHGHGALSSLAHEAVIHAPLLGVKAVFTDHSLFGFGD-AVGVLTNKLLGAALRC------ 489
Cdd:cd03794  82 LSFALAALLkllvrEERPDVIIAYSPPITLGLAALLLKKLRGAPFILDVRDLWPESLiALGVLKKGSLLKLLKKlerkly 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 490 --VDEVICVSNTGRENtVLRAQLDPSIVSVIPNALEAEHFKPDP------FRADPDWITIVVISRLVHRKGIDLLISSAP 561
Cdd:cd03794 162 rlADAIIVLSPGLKEY-LLRKGVPKEKIIVIPNWADLEEFKPPPkdelrkKLGLDDKFVVVYAGNIGKAQGLETLLEAAE 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 562 QIcALFPKVRFIVGGDGPKMVELEQMREKYELQGrVELLGRVNPGDVRDVLTKGQI-YLSNSLTEAFGISI----IEAAS 636
Cdd:cd03794 241 RL-KRRPDIRFLFVGDGDEKERLKELAKARGLDN-VTFLGRVPKEEVPELLSAADVgLVPLKDNPANRGSSpsklFEYMA 318

                       330       340       350       360
                ....*....|....*....|....*....|....*....|
gi 57226667 637 AGLFVVATKVGGVPEILPQDMIEFCRADEDDVirALTHAI 676
Cdd:cd03794 319 AGKPILASDDGGSDLAVEINGCGLVVEPGDPE--ALADAI 356
LPLAT_LCLAT1-like cd07990
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LCLAT1-like; ...
 75-170 6.16e-15

Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LCLAT1-like; Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are such LPLATs as Lysocardiolipin acyltransferase 1 (LCLAT1) or 1-acyl-sn-glycerol-3-phosphate acyltransferase and similar proteins.


Pssm-ID: 153252 [Multi-domain]  Cd Length: 193  Bit Score: 73.81  E-value: 6.16e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667  75 HGGGKANEKGRSMVMVgNHQSFVDILYLGRIFPK-----HAAIMAKKSIQWIPGLGWFMMMSGTVFINRSNNKSAIAsLQ 149
Cdd:cd07990  15 YGDEPKLPKERALIIS-NHRSEVDWLVLWMLADRfgrlgRLKIVLKDSLKYPPLGGWGWQLGEFIFLKRKWEKDEKT-IK 92

                        90       100
                ....*....|....*....|...
gi 57226667 150 HAGEEMKRKRISLW--IFPEGTR 170
Cdd:cd07990  93 RQLKRLKDSPEPFWllIFPEGTR 115
GT4_AmsK-like cd03799
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ...
 511-668 2.74e-13

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: 72.10  E-value: 2.74e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 511 DPSIVSVIPNALEAEHFKPDPFRADPDW-ITIVVISRLVHRKGIDLLISSAPQICALFPKVRFIVGGDGPKMVELEQMRE 589
Cdd:cd03799 146 DEKKIIVHRSGIDCNKFRFKPRYLPLDGkIRILTVGRLTEKKGLEYAIEAVAKLAQKYPNIEYQIIGDGDLKEQLQQLIQ 225

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 590 KYELQGRVELLGRVNPGDVRDVLTKGQIYLSNSLTEAFG------ISIIEAASAGLFVVATKVGGVPEiLPQDMIEFCRA 663
Cdd:cd03799 226 ELNIGDCVKLLGWKPQEEIIEILDEADIFIAPSVTAADGdqdgppNTLKEAMAMGLPVISTEHGGIPE-LVEDGVSGFLV 304


                ....*
gi 57226667 664 DEDDV 668
Cdd:cd03799 305 PERDA 309
LPLAT_ABO13168-like cd07988
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: Unknown ...
 55-236 5.55e-13

Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: Unknown ABO13168; Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are uncharacterized phospholipid/glycerol acyltransferases such as the Acinetobacter baumannii ATCC 17978 locus ABO13168 putative acyltransferase, and similar proteins.


Pssm-ID: 153250 [Multi-domain]  Cd Length: 163  Bit Score: 67.24  E-value: 5.55e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667  55 ILGWKFQvegeqylwelsgehggGKANEKGRSMVMVGNHQSFVDILYLgrIFPKHAA-----IMAKKSIQWIPgLGWFMM 129
Cdd:cd07988   7 LSGWRIE----------------GEPPNKPKFVVIGAPHTSNWDFVLG--LLAAFALglkisFLGKHSLFKPP-LGPFMR 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 130 MSGTVFINRSNNKSAIASLqhAGEEMKRKRISLWIFPEGTRHNTPepellNFKKGAFYLAVQAGVPIVPVvcenynhlfn 209
Cdd:cd07988  68 WLGGIPVDRSRAGGLVEQV--VEEFRRREEFVLAIAPEGTRSKVD-----KWKTGFYHIARGAGVPILLV---------- 130

                       170       180
                ....*....|....*....|....*..
gi 57226667 210 gKSHFRRGTLRIkvLPPISTTGLTAAD 236
Cdd:cd07988 131 -YLDYKRKTVGI--GPLFEPSGDIEAD 154
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 511-653 6.79e-13

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: 71.60  E-value: 6.79e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 511 DPSIVSVIPNALEAEHFKPDP-FRADPDWITIVVISRLVHRKGIDLLISSAPQICALFPKVRF-IVGG--DGPKMV-ELE 585
Cdd:cd03813 265 DPDKTRVIPNGIDIQRFAPAReERPEKEPPVVGLVGRVVPIKDVKTFIRAFKLVRRAMPDAEGwLIGPedEDPEYAqECK 344

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 57226667 586 QMREKYELQGRVELLGRVNpgdVRDVLTKGQIYLSNSLTEAFGISIIEAASAGLFVVATKVGGVPEIL 653
Cdd:cd03813 345 RLVASLGLENKVKFLGFQN---IKEYYPKLGLLVLTSISEGQPLVILEAMASGVPVVATDVGSCRELI 409
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
 347-712 1.27e-12

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: 69.62  E-value: 1.27e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 347 IAMVSDFFFPVI----GGVEGHIYSLSVELMRRGHKVIVIT--HSHPDRlgihylePSLKVYylPYLPIASSASLPNFLL 420
Cdd:cd03802   2 IAQVSPPRGPVPpgkyGGTELVVSALTEGLVRRGHEVTLFApgDSHTSA-------PLVAVI--PRALRLDPIPQESKLA 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 421 FLPYFRHIIL-TENIQLVHGHgalssLAHEAVIHAPLLGVKAVFTDHslfGFGDavgvLTNKLLGAALRCVDeVICVSNT 499
Cdd:cd03802  73 ELLEALEVQLrASDFDVIHNH-----SYDWLPPFAPLIGTPFVTTLH---GPSI----PPSLAIYAAEPPVN-YVSISDA 139

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 500 GRENTVLRAQLdpsivSVIPNALEAEHFKPDPFRADPdwitIVVISRLVHRKGIDLLISSAPQIcalfpKVR-FIVGGDG 578
Cdd:cd03802 140 QRAATPPIDYL-----TVVHNGLDPADYRFQPDPEDY----LAFLGRIAPEKGLEDAIRVARRA-----GLPlKIAGKVR 205

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 579 PKMVELEQmrEKYELQGRVELLGRVNPGDVRDVLTKGQIYLSNSL-TEAFGISIIEAASAGLFVVATKVGGVPEILPQDM 657
Cdd:cd03802 206 DEDYFYYL--QEPLPGPRIEFIGEVGHDEKQELLGGARALLFPINwDEPFGLVMIEAMACGTPVIAYRRGGLPEVIQHGE 283

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
gi 57226667 658 IEFCRADEDDVIRalthAIHTIqsSRHSPWSAHIRVRDMYSWSHVSSRAEIVYLR 712
Cdd:cd03802 284 TGFLVDSVEEMAE----AIANI--DRIDRAACRRYAEDRFSAARMADRYEALYRK 332
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
 358-653 5.72e-12

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: 67.86  E-value: 5.72e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 358 IGGVEGHIYSLSVELMRRGHKVIVITHShpdrlGIHYLEPSLKVYYLPYLPIASSASlpNFLLFLPYFRHIILTENIQLV 437
Cdd:cd04951  11 LGGAEKQTVLLADQMFIRGHDVNIVYLT-----GEVEVKPLNNNIIIYNLGMDKNPR--SLLKALLKLKKIISAFKPDVV 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 438 HGH----GALSSLAhEAVIHAPLLgvkaVFTDHslfgfgdavgvltNKLLGAALRCV---------DEVICVSNTGRENT 504
Cdd:cd04951  84 HSHmfhaNIFARFL-RMLYPIPLL----ICTAH-------------NKNEGGRIRMFiyrltdflcDITTNVSREALDEF 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 505 VLRAQLDPSIVSVIPNALEAEHFKPDP---------FRADPDWITIVVISRLVHRKGIDLLISSAPQICALFPKVRFIVG 575
Cdd:cd04951 146 IAKKAFSKNKSVPVYNGIDLNKFKKDInvrlkirnkLNLKNDEFVILNVGRLTEAKDYPNLLLAISELILSKNDFKLLIA 225

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 57226667 576 GDGPKMVELEQMREKYELQGRVELLGRVNpgDVRDVLTKGQIYLSNSLTEAFGISIIEAASAGLFVVATKVGGVPEIL 653
Cdd:cd04951 226 GDGPLRNELERLICNLNLVDRVILLGQIS--NISEYYNAADLFVLSSEWEGFGLVVAEAMACERPVVATDAGGVAEVV 301
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 617-715 9.13e-12

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 62.70  E-value: 9.13e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 617 IYLSNSLTEAFGISIIEAASAGLFVVATKVGGVPEILPQDMIEFC--RADEDDVIRALTHAIHTIQSSRHSPWSAHIRVR 694
Cdd:COG0438  23 VFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLvpPGDPEALAEAILRLLEDPELRRRLGEAARERAE 102

                        90       100
                ....*....|....*....|.
gi 57226667 695 DMYSWSHVSSRAEIVYLRAMS 715
Cdd:COG0438 103 ERFSWEAIAERLLALYEELLA 123
Glyco_trans_4_4 pfam13579
Glycosyl transferase 4-like domain;
359-521 7.00e-11

Glycosyl transferase 4-like domain;


Pssm-ID: 433325 [Multi-domain]  Cd Length: 158  Bit Score: 61.26  E-value: 7.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667   359 GGVEGHIYSLSVELMRRGHKVIVITHsHPDRLGIHYLEPSLKVYYLPYLPiasSASLPNFLLFLPYFRHIILTENIQLVH 438
Cdd:pfam13579   1 GGIGVYVLELARALAALGHEVRVVTP-GGPPGRPELVGDGVRVHRLPVPP---RPSPLADLAALRRLRRLLRAERPDVVH 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667   439 GHGALSSLAheAVIHAPLLGVKAVFTDHSLFGFGD--AVGVLTNKLLGAALRCVDEVICVSNTGREnTVLRAQLDPSIVS 516
Cdd:pfam13579  77 AHSPTAGLA--ARLARRRRGVPLVVTVHGLALDYGsgWKRRLARALERRLLRRADAVVVVSEAEAE-LLRALGVPAARVV 153


                  ....*
gi 57226667   517 VIPNA 521
Cdd:pfam13579 154 VVPNG 158
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
 358-642 3.15e-10

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: 62.69  E-value: 3.15e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 358 IGGVEGHIYSLSVELMRRGHKVIVITHSHPDrlgIHYLEP----SLKVYYLPYLPIassaslpNFLLFLPYFRHIILTEN 433
Cdd:cd03812  11 VGGIETFLMNLYRKLDKSKIEFDFLATSDDK---GEYDEEleelGGKIFYIPPKKK-------NIIKYFIKLLKLIKKEK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 434 IQLVHGHGALSSLAHEavIHAPLLGVKaVFTDHS-------LFGFGDAVGVLTNKLLgaalRCVDEVICVSNTGRENtvL 506
Cdd:cd03812  81 YDIVHVHGSSSNGIIL--LLAAKAGVP-VRIAHShntkdssIKLRKIRKNVLKKLIE----RLSTKYLACSEDAGEW--L 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 507 RAQLDPSIVSVIPNALEAEHFKPDPFRADP--------DWITIVVISRLVHRKGIDLLISSAPQICALFPKVRFIVGGDG 578
Cdd:cd03812 152 FGEVENGKFKVIPNGIDIEKYKFNKEKRRKrrkllileDKLVLGHVGRFNEQKNHSFLIDIFEELKKKNPNVKLVLVGEG 231

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57226667 579 PKMVELEQMREKYELQGRVELLGRVNpgDVRDVLTKGQIYLSNSLTEAFGISIIEAASAGLFVV 642
Cdd:cd03812 232 ELKEKIKEKVKELGLEDKVIFLGFRN--DVSEILSAMDVFLFPSLYEGLPLVAVEAQASGLPCL 293
LPLAT_AAK14816-like cd07992
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: Unknown ...
 90-254 8.15e-10

Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: Unknown AAK14816-like; Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are uncharacterized glycerol-3-phosphate acyltransferases such as the Plasmodium falciparum locus AAK14816 putative acyltransferase, and similar proteins.


Pssm-ID: 153254 [Multi-domain]  Cd Length: 203  Bit Score: 59.20  E-value: 8.15e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667  90 VGNHQ-SFVDILYLGRIFPKHAAIMAKKSIQWIPGLGWFMMMSGTVFINR-------SNNKSAIASLQHAGEEMKRKRIS 161
Cdd:cd07992  33 LGNHPnALIDPLLLAATLRRPVRFLAKADLFKNPLIGWLLESFGAIPVYRpkdlargGIGKISNAAVFDAVGEALKAGGA 112

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 162 LWIFPEGTRHNtpEPELLNFKKGAFYLAVQA------GVPIVPVVCeNYNHlfngKSHFrRGTLRIKVLPPISTTGLTAA 235
Cdd:cd07992 113 IGIFPEGGSHD--RPRLLPLKAGAARMALEAleagqkDVKIVPVGL-NYED----KSRF-RSRVLVEFGKPISVSAFEEA 184

                       170
                ....*....|....*....
gi 57226667 236 DVPGLIERTRnamLETLQE 254
Cdd:cd07992 185 EASRDVEKKL---INQLEA 200
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
 490-685 4.15e-09

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: 58.85  E-value: 4.15e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 490 VDEVIcVSnTGRENTVLRAQLDPSI-VSVIPNAlEAEHFKPDPFRADPDWITIVVISRLVHRKGIDLLISSAPQICALFP 568
Cdd:cd04949 114 YDAII-VS-TEQQKQDLSERFNKYPpIFTIPVG-YVDQLDTAESNHERKSNKIITISRLAPEKQLDHLIEAVAKAVKKVP 190

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 569 KVRF-IVGGDGPKMVeLEQMREKYELQGRVELLGRVNpgDVRDVLTKGQIYLSNSLTEAFGISIIEAASAGLFVVATKVG 647
Cdd:cd04949 191 EITLdIYGYGEEREK-LKKLIEELHLEDNVFLKGYHS--NLDQEYQDAYLSLLTSQMEGFGLTLMEAIGHGLPVVSYDVK 267

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 57226667 648 -GVPEILpQD-----MIEFCRADE--DDVIRALTHAIHTIQSSRHS 685
Cdd:cd04949 268 yGPSELI-EDgengyLIEKNNIDAlaDKIIELLNDPEKLQQFSEES 312
GT4_AmsK-like cd04946
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ...
 487-653 9.57e-09

amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. AmsK is involved in the biosynthesis of amylovoran, which functions as a virulence factor. It functions as a glycosyl transferase which transfers galactose from UDP-galactose to a lipid-linked amylovoran-subunit precursor. The members of this family are found mainly in bacteria and Archaea.


Pssm-ID: 340854 [Multi-domain]  Cd Length: 401  Bit Score: 58.24  E-value: 9.57e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 487 LRCVDEVICVSNTGRENTVLRAQLDPSIVSVIPNALEAEHFKPDPFRADPdwITIVVISRLVHRKGIDLLISSAPQICAL 566
Cdd:cd04946 175 VSYLDAVFLISKEGKDYLQKCYPAYKEKIFVSRLGVSDKEQYSKVKKEGD--LRLVSCSSIVPVKRIDLIIETLNSLCVA 252

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 567 FPKVRFI---VGGdGPKMVELEQMREKYELQGRVELLGRVNPGDVRdvltkgQIYLSN--------SLTEAFGISIIEAA 635
Cdd:cd04946 253 HPSICISwthIGG-GPLKERLEKLAENKLENVKVNFTGEVSNKEVK------QLYKENdvdvfvnvSESEGIPVSIMEAI 325

                       170
                ....*....|....*...
gi 57226667 636 SAGLFVVATKVGGVPEIL 653
Cdd:cd04946 326 SFGIPVIATNVGGTREIV 343
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
 515-653 3.69e-08

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: 56.19  E-value: 3.69e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 515 VSVIPNALEAEHFKPDP-------FRADPDWITIVVISRLVH--RKGIDLLISSapqiCALFPKVRFI----VGGDGPKM 581
Cdd:cd03825 163 VVVIPNGIDTEIFAPVDkakarkrLGIPQDKKVILFGAESVTkpRKGFDELIEA----LKLLATKDDLllvvFGKNDPQI 238

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 57226667 582 VELE-QMREKYELQGRVELlgrvnpgdvRDVLTKGQIYLSNSLTEAFGISIIEAASAGLFVVATKVGGVPEIL 653
Cdd:cd03825 239 VILPfDIISLGYIDDDEQL---------VDIYSAADLFVHPSLADNLPNTLLEAMACGTPVVAFDTGGSPEIV 302
GT4_WbaZ-like cd03804
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ...
 542-654 3.92e-08

mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbaZ in Salmonella enterica has been shown to possess mannosyltransferase activity.


Pssm-ID: 340833 [Multi-domain]  Cd Length: 356  Bit Score: 56.14  E-value: 3.92e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 542 VVISRLVHRKGIDLLIssapQICALFPKvRFIVGGDGPKMVELEQMrekyeLQGRVELLGRVNPGDVRDVLTKGQIYLSN 621
Cdd:cd03804 203 LTASRLVPYKRIDLAV----EAFNELPK-RLVVIGDGPDLDRLRAM-----ASPNVEFLGYQPDEVLKELLSKARAFVFA 272

                        90       100       110
                ....*....|....*....|....*....|...
gi 57226667 622 SlTEAFGISIIEAASAGLFVVATKVGGVPEILP 654
Cdd:cd03804 273 A-EEDFGIVPVEAQACGTPVIAFGKGGALETVR 304
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
 10-199 1.75e-07

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 54.93  E-value: 1.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667    10 LALYTILLISTSFLAVLIAIVcsltgrrlntnyfvARTFYciagtilgwKFQVEGEQYLwelsGEHGGgkanekgrsMVM 89
Cdd:PRK08633  402 GTLYTLLLLPDSLLRFLLLLL--------------MHTRY---------RLRVEGRENI----PAKGG---------ALL 445

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667    90 VGNHQSFVDILYLGRIFPKHAAIMAKKSIQWIPGLGWFMMMSGTVFINRSNNKSAIASLQHA---GEemkrkriSLWIFP 166
Cdd:PRK08633  446 LGNHVSWIDWALLQAASPRPIRFVMERSIYEKWYLKWFFKLFGVIPISSGGSKESLEFIRKAlddGE-------VVCIFP 518

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 57226667   167 EG--TRHNtpepELLNFKKGaFYLAVQ-AGVPIVPV 199
Cdd:PRK08633  519 EGaiTRNG----QLNEFKRG-FELIVKgTDVPIIPF 549
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
 536-656 2.51e-06

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 50.86  E-value: 2.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667  536 PDWITIVVISRLVHRKGIDLLISsapqICALFPKVRFIVGGDGPKMVELEQMrekyeLQG-RVELLGRVNPGDVRDVLTK 614
Cdd:PLN02871 261 PEKPLIVYVGRLGAEKNLDFLKR----VMERLPGARLAFVGDGPYREELEKM-----FAGtPTVFTGMLQGDELSQAYAS 331

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 57226667  615 GQIYLSNSLTEAFGISIIEAASAGLFVVATKVGGVPEILPQD 656
Cdd:PLN02871 332 GDVFVMPSESETLGFVVLEAMASGVPVVAARAGGIPDIIPPD 373
PRK14014 PRK14014
putative acyltransferase; Provisional
 4-190 2.88e-06

putative acyltransferase; Provisional


Pssm-ID: 237584 [Multi-domain]  Cd Length: 301  Bit Score: 49.85  E-value: 2.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667    4 VIYYLNLALYTILLISTSFLAVLIAIVCSLTG----RRLNTNY--FVARTFYCIAGTILGWKFQVEgeqylWELSGehgG 77
Cdd:PRK14014   9 LRGLLSILLLILNTLFWSVPIIILGLLKLLLPipaiRRACSRLlnFIAEAWISINNVILRLLPRTQ-----WDVEG---L 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667   78 GKANEKGRSMVmVGNHQSFVDILYLGRIFPKHAAIM---AKKSIQWIP--GLGW------FMMMSGTVFINRsNNKSA-- 144
Cdd:PRK14014  81 EGLSKKGWYLV-ISNHQSWVDILVLQYVFNRRIPMLkffLKQELIWVPflGLAWwaldfpFMKRYSKAYLAK-NPELKgk 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 57226667  145 -IASLQHAGEEMKRKRISLWIFPEGTR-----H---NTPEPELLNFKKG--AFYLAV 190
Cdd:PRK14014 159 dLETTRRACEKFKRMPTTIVNFVEGTRftpekHqqqQSPYQHLLKPKAGgiAFALNA 215
GT5_Glycogen_synthase_DULL1-like cd03791
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ...
 541-712 3.14e-06

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: 50.25  E-value: 3.14e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 541 IVVISRLVHRKGIDLLISSAPQICALfpKVRFIVGGDGPKmvELEQ-MRekyELQGRvellgrvNPGDVR-----DVLTK 614
Cdd:cd03791 297 FGFVGRLTEQKGVDLILDALPELLEE--GGQLVVLGSGDP--EYEQaFR---ELAER-------YPGKVAvvigfDEALA 362

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 615 GQIY------LSNSLTEAFGISIIEAASAGLFVVATKVGGVpeilpQDMIE-------------FCRADEDDVIRALTHA 675
Cdd:cd03791 363 HRIYagadffLMPSRFEPCGLVQMYAMRYGTLPIVRRTGGL-----ADTVFdydpetgegtgfvFEDYDAEALLAALRRA 437

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 57226667 676 IHtiqSSRHSPWSAHIRVRDM---YSWSHVSSRAEIVYLR 712
Cdd:cd03791 438 LA---LYRNPELWRKLQKNAMkqdFSWDKSAKEYLELYRS 474
LPLAT_DHAPAT-like cd07993
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: GPAT-like; ...
 79-170 6.65e-06

Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: GPAT-like; Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are such LPLATs as dihydroxyacetone phosphate acyltransferase (DHAPAT, also known as 1 glycerol-3-phosphate O-acyltransferase 1) and similar proteins.


Pssm-ID: 153255 [Multi-domain]  Cd Length: 205  Bit Score: 47.57  E-value: 6.65e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667  79 KANEKGRSMVMVGNHQSFVD------ILYLGRIFPKHAAimAKKSIQwIPGLGWFMMMSGTVFINRS--NNKSAIASLQH 150
Cdd:cd07993  16 KAAQEGHPVVLLPTHRSYLDflllsfILFSLGLPLPHIA--AGENLN-IPILGTLLRRLGAFFIRRSfgKDPLYRAVLQE 92

                        90       100
                ....*....|....*....|
gi 57226667 151 AGEEMKRKRISLWIFPEGTR 170
Cdd:cd07993  93 YVQELLKNGQPLEFFIEGTR 112
GT4_trehalose_phosphorylase cd03792
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ...
 531-650 1.05e-05

trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly catalyzes trehalose synthesis and degradation from alpha-glucose-1-phosphate (alpha-Glc-1-P) and glucose. The catalyzing activity includes the phosphorolysis of trehalose, which produce alpha-Glc-1-P and glucose, and the subsequent synthesis of trehalose. This family is most closely related to the GT4 family of glycosyltransferases.


Pssm-ID: 340823 [Multi-domain]  Cd Length: 378  Bit Score: 48.47  E-value: 1.05e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 531 PFRADPDWITIVVISRLVHRKGIDLLISSAPQICALFPKVRFIVGG----DGPK-MVELEQMREKYELQGRVELLgRVNP 605
Cdd:cd03792 190 PFVIDPERPYILQVARFDPSKDPLGVIDAYKLFKRRAEEPQLVICGhgavDDPEgSVVYEEVMEYAGDDHDIHVL-RLPP 268

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 57226667 606 GD--VRDVLTKGQIYLSNSLTEAFGISIIEAASAGLFVVATKVGGVP 650
Cdd:cd03792 269 SDqeINALQRAATVVLQLSTREGFGLTVSEALWKGKPVIATPAGGIP 315
sucrsPsyn_pln TIGR02468
sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this ...
 589-653 1.51e-05

sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this family are sucrose-phosphate synthases of plants. This enzyme is known to exist in multigene families in several species of both monocots and dicots. The N-terminal domain is the glucosyltransferase domain. Members of this family also have a variable linker region and a C-terminal domain that resembles sucrose phosphate phosphatase (SPP) (EC 3.1.3.24) (see TIGR01485), the next and final enzyme of sucrose biosynthesis. The SPP-like domain likely serves a binding and not a catalytic function, as the reported SPP is always encoded by a distinct protein.


Pssm-ID: 274147 [Multi-domain]  Cd Length: 1050  Bit Score: 48.62  E-value: 1.51e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667    589 EKYELQGRVELLGRVNPGDVRDVL-----TKGqIYLSNSLTEAFGISIIEAASAGLFVVATKVGGVPEIL 653
Cdd:TIGR02468  542 DKYDLYGQVAYPKHHKQSDVPDIYrlaakTKG-VFINPAFIEPFGLTLIEAAAHGLPMVATKNGGPVDIH 610
GT4_ExpC-like cd03818
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ...
 374-667 3.70e-05

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


Pssm-ID: 340845 [Multi-domain]  Cd Length: 396  Bit Score: 46.97  E-value: 3.70e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 374 RRGHKVIVITHSHPdrLGIHYLEPslkVYYLPYLPIASSASLPNFllflpyfrhiILTENIQLVHGHGALSSLAH----- 448
Cdd:cd03818  23 QPGNEVTFLTRRND--QGIPGVRP---VRYRPFRGVASPLEGHRY----------VRDFEEGVLRGQAVLRALLAlkreg 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 449 ---EAVI-HA---PLLGVKAVFTDHSLFGF--------GDAVGVLTNKLLG----AALRCVDEVIC----VSNTGRENTV 505
Cdd:cd03818  88 frpDVVVgHPgwgEALFVKDVFPDVPLIGYceyyyraeGADVGFDPEFPLDlmirCRLRNRNIALLlsleQADLGVTPTR 167

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 506 LRAQLDPSI----VSVIPNALEAEHFKPDPfRADP--DWITIV-----VISrLVHR-----KGIDLLISSAPQICALFPK 569
Cdd:cd03818 168 WQRSLFPAAyrdrISVIHDGVDTDRLAPDP-AARLrlLNGTELkagdpVIT-YVARnlepyRGFHVFMRALPRIQARRPD 245

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 570 VRF-IVGGD----GPKMVELEQMREKY--ELQG---RVELLGRVNPGDVRDVLTKGQIYLSnsLTEAFGIS--IIEAASA 637
Cdd:cd03818 246 ARVvVVGGDgvsyGSPPPDGGSWKQKMlaELGVdleRVHFVGKVPYDQYVRLLQLSDAHVY--LTYPFVLSwsLLEAMAC 323

                       330       340       350
                ....*....|....*....|....*....|
gi 57226667 638 GLFVVATKVGGVPEILpQDMIEFCRADEDD 667
Cdd:cd03818 324 GCPVIGSDTAPVREVI-RDGRNGLLVDFFD 352
PLN02833 PLN02833
glycerol acyltransferase family protein
 83-208 5.76e-05

glycerol acyltransferase family protein


Pssm-ID: 215447  Cd Length: 376  Bit Score: 46.30  E-value: 5.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667   83 KGRSMVMVGNHQSFVDILYLGRIFPkHAAIMAKKSiQWIPGLGWFMMMS-GTVFINR--SNNKSAIAS--LQHAGEEmkr 157
Cdd:PLN02833 161 RRPKQVFVANHTSMIDFIVLEQMTP-FAVIMQKHP-GWVGFLQNTILESvGCIWFNRteAKDREVVAKklRDHVQDP--- 235

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 57226667  158 KRISLWIFPEGTRHNTpePELLNFKKGAFYLavqaGVPIVPVVCEnYNHLF 208
Cdd:PLN02833 236 DRNPLLIFPEGTCVNN--EYTVMFKKGAFEL----GCTVCPIAIK-YNKIF 279
GlgA COG0297
Glycogen synthase [Carbohydrate transport and metabolism];
535-597 8.19e-05

Glycogen synthase [Carbohydrate transport and metabolism];


Pssm-ID: 440066 [Multi-domain]  Cd Length: 476  Bit Score: 45.85  E-value: 8.19e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57226667 535 DPDWITIVVISRLVHRKGIDLLISSAPQICALfpKVRFIVGGDGPKMVElEQMRE-KYELQGRV 597
Cdd:COG0297 292 DPDAPLIGMVSRLTEQKGLDLLLEALDELLEE--DVQLVVLGSGDPEYE-EAFRElAARYPGRV 352
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
4-255 1.17e-04

acyl-[ACP]--phospholipid O-acyltransferase;


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 45.73  E-value: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667     4 VIYYLNLALYTILListsFLAVLIAIVCSLTGRRLNTNYF------VARTFYciagtilgwKFQVEGEQYLWELsgehgg 77
Cdd:PRK06814  392 LLQALGFSIPWIIL----FIALANLIVAILILRLLPTNLLrdifsiLFRAFY---------RVEVKGLENLQKA------ 452

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667    78 gkanekGRSMVMVGNHQSFVDILYLGRIFPKHA--AI---MAKKsiQWI-PglgwFMMMSGTVFINRSN---NKSAIASL 148
Cdd:PRK06814  453 ------GKKAVIAANHVSFLDGPLLAAYLPEEPtfAIdtdIAKA--WWVkP----FLKLAKALPVDPTNpmaTRTLIKEV 520

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667   149 QhAGEemkrkriSLWIFPEGtrHNTPEPELLNFKKGAFYLAVQAGVPIVPVVCE--NYNHLFNGKSHFRRG---TLRIKV 223
Cdd:PRK06814  521 Q-KGE-------KLVIFPEG--RITVTGSLMKIYDGPGMIADKAGAMVVPVRIDglQFTHFSRLKNQVRRKwfpKVTVTI 590

                         250       260       270
                  ....*....|....*....|....*....|...
gi 57226667   224 LPPISTtgltaADVPGLIERT-RNAMLETLQEI 255
Cdd:PRK06814  591 LPPVKL-----AVDPELKGRErRSAAGAALYDI 618
PLN02380 PLN02380
1-acyl-sn-glycerol-3-phosphate acyltransferase
 15-170 1.68e-04

1-acyl-sn-glycerol-3-phosphate acyltransferase


Pssm-ID: 178006 [Multi-domain]  Cd Length: 376  Bit Score: 44.73  E-value: 1.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667   15 ILLISTSFLAVLIAIVCSLTGRRLN------TNYFVARTFYCIAGTILGWKFQVEGEQYLWELSGEHGGgkaneKGRSMV 88
Cdd:PLN02380  14 LLFLLSGLIVNLIQAVCFILVRPLSkslyrrINRAVAELLWLELIWLVDWWAGVKVQLYADEETFELMG-----KEHALV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667   89 MvGNHQSFVDILyLGRIFPKHA-------AIMaKKSIQWIPGLGWFMMMSGTVFINRSNNKSAiASLQHAGEEMKRKRIS 161
Cdd:PLN02380  89 I-SNHRSDIDWL-VGWILAQRSgclgsalAVM-KKSSKFLPVIGWSMWFSEYVFLERSWAKDE-NTLKSGFQRLKDFPRP 164

                        170
                 ....*....|.
gi 57226667  162 LW--IFPEGTR 170
Cdd:PLN02380 165 FWlaLFVEGTR 175
LPLAT_MGAT-like cd07987
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: MGAT-like; ...
 120-225 1.93e-04

Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: MGAT-like; Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this suubgroup are such LPLATs as 2-acylglycerol O-acyltransferase (MGAT), and similar proteins.


Pssm-ID: 153249 [Multi-domain]  Cd Length: 212  Bit Score: 43.43  E-value: 1.93e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667 120 WIPGLGWFMMMSGTVFINRSNnksaIASLQHAGEemkrkriSLWIFPEGTRHNT-PEPE----LLNFKKGAFYLAVQAGV 194
Cdd:cd07987  61 PLPGLRDLLRRLGAVPGSREN----CVRLLREGE-------LVLIFPGGAREALkSKREeyylLWKKRKGFARLALRAGA 129

                        90       100       110
                ....*....|....*....|....*....|...
gi 57226667 195 PIVPVVCENYNHLFN--GKSHFRRGTLRIKVLP 225
Cdd:cd07987 130 PIVPVFTFGEEELFRvlGDPDGPVGKRLFRLLP 162
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
515-707 3.77e-04

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 43.63  E-value: 3.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667  515 VSVIPNALEAEHFKPDP-------FRADPDWITIVVISRLVHRKGIDLLISSAPQICALFPKVRFIVGGD------GPKM 581
Cdd:PRK15484 163 ISIVPNGFCLETYQSNPqpnlrqqLNISPDETVLLYAGRISPDKGILLLMQAFEKLATAHSNLKLVVVGDptasskGEKA 242

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667  582 VELEQMREKYE-LQGRVELLGRVNPGDVRDVLTKGQIYLSNS-LTEAFGISIIEAASAGLFVVATKVGGVPEILPQDMIE 659
Cdd:PRK15484 243 AYQKKVLEAAKrIGDRCIMLGGQPPEKMHNYYPLADLVVVPSqVEEAFCMVAVEAMAAGKPVLASTKGGITEFVLEGITG 322

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 57226667  660 FCRADE-------DDVIRALThaihtiQSSRHS-PWSAHIRVRDMYSWSHVSSRAE 707
Cdd:PRK15484 323 YHLAEPmtsdsiiSDINRTLA------DPELTQiAEQAKDFVFSKYSWEGVTQRFE 372
PRK15179 PRK15179
Vi polysaccharide biosynthesis protein TviE; Provisional
 540-659 2.89e-03

Vi polysaccharide biosynthesis protein TviE; Provisional


Pssm-ID: 185101 [Multi-domain]  Cd Length: 694  Bit Score: 41.17  E-value: 2.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667  540 TIVVISRLVHRKGIDLLISSAPQICALFPKVRFIVGGDGPKMVELEQMREKYELQGRVELLGRVNpgDVRDVLTKGQIYL 619
Cdd:PRK15179 519 TVGTVMRVDDNKRPFLWVEAAQRFAASHPKVRFIMVGGGPLLESVREFAQRLGMGERILFTGLSR--RVGYWLTQFNAFL 596

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 57226667  620 SNSLTEAFGISIIEAASAGLFVVATKVGGVPE---------ILPQDMIE 659
Cdd:PRK15179 597 LLSRFEGLPNVLIEAQFSGVPVVTTLAGGAGEavqegvtglTLPADTVT 645
PLN00142 PLN00142
sucrose synthase
 573-653 6.53e-03

sucrose synthase


Pssm-ID: 215073 [Multi-domain]  Cd Length: 815  Bit Score: 39.96  E-value: 6.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57226667  573 IVGG--------DGPKMVELEQMR---EKYELQGRVELLG----RVNPGD----VRDvlTKGqIYLSNSLTEAFGISIIE 633
Cdd:PLN00142 609 VVGGfidpskskDREEIAEIKKMHsliEKYNLKGQFRWIAaqtnRVRNGElyryIAD--TKG-AFVQPALYEAFGLTVVE 685

                         90       100
                 ....*....|....*....|
gi 57226667  634 AASAGLFVVATKVGGVPEIL 653
Cdd:PLN00142 686 AMTCGLPTFATCQGGPAEII 705
 
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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