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Conserved domains on  [gi|68846235|sp|Q16222|]
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RecName: Full=UDP-N-acetylhexosamine pyrophosphorylase; AltName: Full=Antigen X; Short=AGX; AltName: Full=Protein-pyrophosphorylation enzyme; AltName: Full=Sperm-associated antigen 2; AltName: Full=UDP-N-acetylgalactosamine pyrophosphorylase; AltName: Full=UDP-N-acetylglucosamine pyrophosphorylase

Protein Classification

UDPGP type 1 family protein( domain architecture ID 10135883)

UDPGP type 1 family protein such as human UDP-N-acetylhexosamine pyrophosphorylase that catalyzes the last step in biosynthesis of uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc) by converting UTP and glucosamine 1-phosphate (GlcNAc-1-P) to the sugar nucleotide

EC:  2.7.-.-
Gene Ontology:  GO:0016772
SCOP:  4000691|3000077

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
UDPGlcNAc_PPase cd04193
UDPGlcNAc pyrophosphorylase catalayzes the synthesis of UDPGlcNAc; UDP-N-acetylglucosamine ...
88-410 0e+00

UDPGlcNAc pyrophosphorylase catalayzes the synthesis of UDPGlcNAc; UDP-N-acetylglucosamine (UDPGlcNAc) pyrophosphorylase (UAP) (also named GlcNAc1P uridyltransferase), catalyzes the reversible conversion of UTP and GlcNAc1 to PPi and UDPGlcNAc. UDP-N-acetylglucosamine (UDPGlcNAc), the activated form of GlcNAc, is a key precursor of N- and O-linked glycosylations. It is essential for the synthesis of chitin (a major component of the fungal cell wall) and of the glycosylphosphatidylinositol (GPI) linker which anchors a variety of cell surface proteins to the plasma membrane. In bacteria, UDPGlcNAc represents an essential precursor for both peptidoglycan and lipopolysaccharide biosynthesis. Human UAP has two isoforms, resulting from alternative splicing of a single gene and differing by the presence or absence of 17 amino acids. UDPGlcNAc pyrophosphorylase shares significant sequence and structure conservation with UDPglucose pyrophosphorylase.


:

Pssm-ID: 133036  Cd Length: 323  Bit Score: 596.51  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235  88 QAWESEGLFQISQNKVAVLLLAGGQGTRLGVAYPKGMYDVGLPSRKTLFQIQAERILKLQQVAEKYYGNKCIIPWYIMTS 167
Cdd:cd04193   1 KEWEEAGLKAIAEGKVAVLLLAGGQGTRLGFDGPKGMFPVGLPSKKSLFQLQAERILKLQELAGEASGKKVPIPWYIMTS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235 168 GRTMESTKEFFTKHKYFGLKKENVIFFQQGMLPAMSFDGKIILEEKNKVSMAPDGNGGLYRALAAQNIVEDMEQRGIWSI 247
Cdd:cd04193  81 EATHEETRKFFKENNYFGLDPEQVHFFQQGMLPCVDFDGKILLEEKGKIAMAPNGNGGLYKALQTAGILEDMKKRGIKYI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235 248 HVYCVDNILVKVADPRFIGFCIQKGADCGAKVVEKTNPTEPVGVVCRVDGVYQVVEYSEISLATAQKRSSDGRLLFNAGN 327
Cdd:cd04193 161 HVYSVDNILVKVADPVFIGFCISKGADVGAKVVRKRYPTEKVGVVVLVDGKPQVVEYSEISDELAEKRDADGELQYNAGN 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235 328 IANHFFTVPFLRDVVNVYEPQLQHHVAQKKIPYVDTQGQLIKPDKPNGIKMEKFVFDIFQFAKKFVVYEVLREDEFSPLK 407
Cdd:cd04193 241 IANHFFSLDFLEKAAEMEEPSLPYHIAKKKIPYVDLEGGLVKPDEPNGIKLELFIFDVFPFAKNFVCLEVDREEEFSPLK 320

                ...
gi 68846235 408 NAD 410
Cdd:cd04193 321 NAD 323
 
Name Accession Description Interval E-value
UDPGlcNAc_PPase cd04193
UDPGlcNAc pyrophosphorylase catalayzes the synthesis of UDPGlcNAc; UDP-N-acetylglucosamine ...
88-410 0e+00

UDPGlcNAc pyrophosphorylase catalayzes the synthesis of UDPGlcNAc; UDP-N-acetylglucosamine (UDPGlcNAc) pyrophosphorylase (UAP) (also named GlcNAc1P uridyltransferase), catalyzes the reversible conversion of UTP and GlcNAc1 to PPi and UDPGlcNAc. UDP-N-acetylglucosamine (UDPGlcNAc), the activated form of GlcNAc, is a key precursor of N- and O-linked glycosylations. It is essential for the synthesis of chitin (a major component of the fungal cell wall) and of the glycosylphosphatidylinositol (GPI) linker which anchors a variety of cell surface proteins to the plasma membrane. In bacteria, UDPGlcNAc represents an essential precursor for both peptidoglycan and lipopolysaccharide biosynthesis. Human UAP has two isoforms, resulting from alternative splicing of a single gene and differing by the presence or absence of 17 amino acids. UDPGlcNAc pyrophosphorylase shares significant sequence and structure conservation with UDPglucose pyrophosphorylase.


Pssm-ID: 133036  Cd Length: 323  Bit Score: 596.51  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235  88 QAWESEGLFQISQNKVAVLLLAGGQGTRLGVAYPKGMYDVGLPSRKTLFQIQAERILKLQQVAEKYYGNKCIIPWYIMTS 167
Cdd:cd04193   1 KEWEEAGLKAIAEGKVAVLLLAGGQGTRLGFDGPKGMFPVGLPSKKSLFQLQAERILKLQELAGEASGKKVPIPWYIMTS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235 168 GRTMESTKEFFTKHKYFGLKKENVIFFQQGMLPAMSFDGKIILEEKNKVSMAPDGNGGLYRALAAQNIVEDMEQRGIWSI 247
Cdd:cd04193  81 EATHEETRKFFKENNYFGLDPEQVHFFQQGMLPCVDFDGKILLEEKGKIAMAPNGNGGLYKALQTAGILEDMKKRGIKYI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235 248 HVYCVDNILVKVADPRFIGFCIQKGADCGAKVVEKTNPTEPVGVVCRVDGVYQVVEYSEISLATAQKRSSDGRLLFNAGN 327
Cdd:cd04193 161 HVYSVDNILVKVADPVFIGFCISKGADVGAKVVRKRYPTEKVGVVVLVDGKPQVVEYSEISDELAEKRDADGELQYNAGN 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235 328 IANHFFTVPFLRDVVNVYEPQLQHHVAQKKIPYVDTQGQLIKPDKPNGIKMEKFVFDIFQFAKKFVVYEVLREDEFSPLK 407
Cdd:cd04193 241 IANHFFSLDFLEKAAEMEEPSLPYHIAKKKIPYVDLEGGLVKPDEPNGIKLELFIFDVFPFAKNFVCLEVDREEEFSPLK 320

                ...
gi 68846235 408 NAD 410
Cdd:cd04193 321 NAD 323
PLN02435 PLN02435
probable UDP-N-acetylglucosamine pyrophosphorylase
10-506 2.59e-136

probable UDP-N-acetylglucosamine pyrophosphorylase


Pssm-ID: 215238  Cd Length: 493  Bit Score: 403.48  E-value: 2.59e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235   10 LSKAGQEHLLRFWNELEEAQQVELYAELQAMNFEELNFFFQKAIEGfnqsshQKNVDARMEPVPREVLGSAT-RDQDQLQ 88
Cdd:PLN02435  29 LKDYGQEDAFALWDELSPEERDLLVRDIESLDLPRIDRIIRCSLRS------QGLPVPAIEPVPENSVSTVEeRTPEDRE 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235   89 AWESEGLFQISQNKVAVLLLAGGQGTRLGVAYPKGMYDVGLPSRKTLFQIQAERILKLQ----QVAEKYYGNKCIIPWYI 164
Cdd:PLN02435 103 RWWKMGLKAISEGKLAVVLLSGGQGTRLGSSDPKGCFNIGLPSGKSLFQLQAERILCVQrlaaQASSEGPGRPVTIHWYI 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235  165 MTSGRTMESTKEFFTKHKYFGLKKENVIFFQQGMLPAMSFDGKIILEEKNKVSMAPDGNGGLYRALAAQNIVEDMEQRGI 244
Cdd:PLN02435 183 MTSPFTDEATRKFFESHKYFGLEADQVTFFQQGTLPCVSKDGKFIMETPFKVAKAPDGNGGVYAALKSSRLLEDMASRGI 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235  245 WSIHVYCVDNILVKVADPRFIGFCIQKGADCGAKVVEKTNPTEPVGVVCR--VDGVYQVVEYSEI--SLATAQKRSSdGR 320
Cdd:PLN02435 263 KYVDCYGVDNALVRVADPTFLGYFIDKGVASAAKVVRKAYPQEKVGVFVRrgKGGPLTVVEYSELdqAMASAINQQT-GR 341
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235  321 LLFNAGNIANHFFTVPFLRDVVNVYEPQLQHHVAQKKIPYVDTQGQlikpdkpnGIKMEKFVFDIFQFAKKFVVYEVLRE 400
Cdd:PLN02435 342 LRYCWSNVCLHMFTLDFLNQVANGLEKDSIYHLAEKKIPSIHGYTM--------GLKLEQFIFDAFPYAPSTALFEVLRE 413
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235  401 DEFSPLKNADSQNgKDNPTTARHALMSLHHCWVLNAGGhFIdengsrLPAIPRSATNgksetitadvnhnlkdandvpiq 480
Cdd:PLN02435 414 EEFAPVKNANGSN-FDTPESARLLVLRLHTRWVVAAGG-FL------THSVPLYATG----------------------- 462
                        490       500
                 ....*....|....*....|....*.
gi 68846235  481 CEISPLISYAGEGLESYVADKEFHAP 506
Cdd:PLN02435 463 VEVSPLCSYAGENLEAICRGRTFHAP 488
QRI1 COG4284
UDP-N-acetylglucosamine pyrophosphorylase [Carbohydrate transport and metabolism];
6-418 8.48e-136

UDP-N-acetylglucosamine pyrophosphorylase [Carbohydrate transport and metabolism];


Pssm-ID: 443425  Cd Length: 402  Bit Score: 398.87  E-value: 8.48e-136
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235   6 LKLTLSKAGQEHLLRFWNELEEAQQVELYAELQAMNFEELNFFFQKAIEGFNQSShqKNVDARMEPVPREVLGSATRDQD 85
Cdd:COG4284   1 LIEKLEPHGQEHLLRFWDELSEAQQKMLEAQIEEIDIDVFQHLYRQLVLAEGATG--LIPESDIEPAPVTDLPLTDLDEV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235  86 QLQAWESEGLFQISQNKVAVLLLAGGQGTRLGVAYPKGMYDVGLPSRKTLFQIQAERILKlqqvAEKYYGnkCIIPWYIM 165
Cdd:COG4284  79 DRDRAEEAGEEALRAGKVAVILLAGGQGTRLGFDGPKGLLPVRPVKGKSLFDLIAEQVLA----ARRRYG--VPLPLYIM 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235 166 TSGRTMESTKEFFTKHKYFGLKKENVIFFQQGMLPAM-SFDGKIILEEKNKVSMAPDGNGGLYRALAAQNIVEDMEQRGI 244
Cdd:COG4284 153 TSFRTHEDTLAFLEEHDYFGLDGLPVHFFLQGMEPALdADLGPVLLPADPELELCPPGHGGIYTALLASGLLDKLLERGI 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235 245 WSIHVYCVDNILVKVADPRFIGFCIQKGADCGAKVVEKTNPTEPVGVVCRVDGVYQVVEYSEisLATAQKRSSDGRLLFN 324
Cdd:COG4284 233 RYLFVSNVDNPLGAVPDPAFAGWHAASGAPFTAKVVRRTPPDEKVGHLARVDGRLILREYSQ--LPDEEAEAFTGELRHP 310
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235 325 AGNIANHFFTVPFLRDVVNVYEPQLQHHVAQKKIPYVDTQGqliKPDKPNGIKMEKFVFDIFQFAKKFVVYEVLREDEFS 404
Cdd:COG4284 311 YGNINNHWFDLDFLKRLLDERGLGLPLHRAEKKVDPLDESG---KPTSPNVIKFETFMFDAIPLFDGAVAIEVDREERFA 387
                       410
                ....*....|....
gi 68846235 405 PLKNAdsqNGKDNP 418
Cdd:COG4284 388 PVKNT---NGSDSP 398
UDPGP pfam01704
UTP--glucose-1-phosphate uridylyltransferase; This family consists of UTP--glucose-1-phosphate ...
45-472 2.14e-126

UTP--glucose-1-phosphate uridylyltransferase; This family consists of UTP--glucose-1-phosphate uridylyltransferases, EC:2.7.7.9. Also known as UDP-glucose pyrophosphorylase (UDPGP) and Glucose-1-phosphate uridylyltransferase. UTP--glucose-1-phosphate uridylyltransferase catalyzes the interconversion of MgUTP + glucose-1-phosphate and UDP-glucose + MgPPi. UDP-glucose is an important intermediate in mammalian carbohydrate interconversion involved in various metabolic roles depending on tissue type. In Dictyostelium (slime mold) mutants in this enzyme abort the development cycle. Also within the family is UDP-N-acetylglucosamine or AGX1 and two hypothetical proteins from Borrelia burgdorferi the lyme disease spirochaete Swiss:O51893 and Swiss:O51036.


Pssm-ID: 460300  Cd Length: 412  Bit Score: 375.31  E-value: 2.14e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235    45 LNFFFQKAIEGFNQSSHQKNVD-ARMEPVPREVLgsatRDQDQLQA--WESEGLFqisqNKVAVLLLAGGQGTRLGVAYP 121
Cdd:pfam01704   1 LDGFFKLFSRYLSEKGKQEKIDwDKIKPPPEEEI----VDYEDLQEpeEEIKELL----NKLAVLKLNGGLGTSMGCVGP 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235   122 KGMYDVGlpSRKTLFQIQAERILKLQQvaeKYygnKCIIPWYIMTSGRTMESTKEFFTKhkYFGlKKENVIFFQQGMLPA 201
Cdd:pfam01704  73 KSLIEVR--DGLTFLDLIVQQIEHLNK---KY---NVDVPLVLMNSFNTDEDTKKIIRK--YKG-HKVDILTFNQSRYPR 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235   202 MSFDGKIILEEK---NKVSMAPDGNGGLYRALAAQNIVEDMEQRGIWSIHVYCVDNiLVKVADPRFIGFCIQKGADCGAK 278
Cdd:pfam01704 142 IDKDTLLPVPKSadsDEEEWYPPGHGDLYESLYNSGLLDKLLAEGKEYLFVSNIDN-LGATVDLNILNYMVDNGAEFLME 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235   279 VVEKTNPTEPVGVVCRVDGVYQVVEYSEI-SLATAQKRSSDGRLLFNAGNIanhFFTVPFLRDVVNvyEPQLQHHVAQKK 357
Cdd:pfam01704 221 VTDKTRADVKGGTLIEYDGKLRLLEIAQVpKEHVDEFKSIKKFKIFNTNNI---WINLKALKRVVE--EGELQLEIIVNK 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235   358 iPYVDTQGQLIKPDKPNGIKMEKFvfdifqfaKKFVVYEVLReDEFSPLKNADSqngkdnpttarhALMSLHHCWVLNAG 437
Cdd:pfam01704 296 -KTLDNGENVIQLETAVGAAIKNF--------KNAIGINVPR-SRFLPVKTTSD------------LLLVMSDLYVLNHG 353
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235   438 -------------------GHF--IDENGSRLPAIPrSATNGKSETITADV----NHNLK 472
Cdd:pfam01704 354 slimnpkrmfgtppvvllgDHFkkVDEFLKRFPSIP-DLLELDHLTVSGDVtfgrNVTLK 412
 
Name Accession Description Interval E-value
UDPGlcNAc_PPase cd04193
UDPGlcNAc pyrophosphorylase catalayzes the synthesis of UDPGlcNAc; UDP-N-acetylglucosamine ...
88-410 0e+00

UDPGlcNAc pyrophosphorylase catalayzes the synthesis of UDPGlcNAc; UDP-N-acetylglucosamine (UDPGlcNAc) pyrophosphorylase (UAP) (also named GlcNAc1P uridyltransferase), catalyzes the reversible conversion of UTP and GlcNAc1 to PPi and UDPGlcNAc. UDP-N-acetylglucosamine (UDPGlcNAc), the activated form of GlcNAc, is a key precursor of N- and O-linked glycosylations. It is essential for the synthesis of chitin (a major component of the fungal cell wall) and of the glycosylphosphatidylinositol (GPI) linker which anchors a variety of cell surface proteins to the plasma membrane. In bacteria, UDPGlcNAc represents an essential precursor for both peptidoglycan and lipopolysaccharide biosynthesis. Human UAP has two isoforms, resulting from alternative splicing of a single gene and differing by the presence or absence of 17 amino acids. UDPGlcNAc pyrophosphorylase shares significant sequence and structure conservation with UDPglucose pyrophosphorylase.


Pssm-ID: 133036  Cd Length: 323  Bit Score: 596.51  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235  88 QAWESEGLFQISQNKVAVLLLAGGQGTRLGVAYPKGMYDVGLPSRKTLFQIQAERILKLQQVAEKYYGNKCIIPWYIMTS 167
Cdd:cd04193   1 KEWEEAGLKAIAEGKVAVLLLAGGQGTRLGFDGPKGMFPVGLPSKKSLFQLQAERILKLQELAGEASGKKVPIPWYIMTS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235 168 GRTMESTKEFFTKHKYFGLKKENVIFFQQGMLPAMSFDGKIILEEKNKVSMAPDGNGGLYRALAAQNIVEDMEQRGIWSI 247
Cdd:cd04193  81 EATHEETRKFFKENNYFGLDPEQVHFFQQGMLPCVDFDGKILLEEKGKIAMAPNGNGGLYKALQTAGILEDMKKRGIKYI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235 248 HVYCVDNILVKVADPRFIGFCIQKGADCGAKVVEKTNPTEPVGVVCRVDGVYQVVEYSEISLATAQKRSSDGRLLFNAGN 327
Cdd:cd04193 161 HVYSVDNILVKVADPVFIGFCISKGADVGAKVVRKRYPTEKVGVVVLVDGKPQVVEYSEISDELAEKRDADGELQYNAGN 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235 328 IANHFFTVPFLRDVVNVYEPQLQHHVAQKKIPYVDTQGQLIKPDKPNGIKMEKFVFDIFQFAKKFVVYEVLREDEFSPLK 407
Cdd:cd04193 241 IANHFFSLDFLEKAAEMEEPSLPYHIAKKKIPYVDLEGGLVKPDEPNGIKLELFIFDVFPFAKNFVCLEVDREEEFSPLK 320

                ...
gi 68846235 408 NAD 410
Cdd:cd04193 321 NAD 323
PLN02435 PLN02435
probable UDP-N-acetylglucosamine pyrophosphorylase
10-506 2.59e-136

probable UDP-N-acetylglucosamine pyrophosphorylase


Pssm-ID: 215238  Cd Length: 493  Bit Score: 403.48  E-value: 2.59e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235   10 LSKAGQEHLLRFWNELEEAQQVELYAELQAMNFEELNFFFQKAIEGfnqsshQKNVDARMEPVPREVLGSAT-RDQDQLQ 88
Cdd:PLN02435  29 LKDYGQEDAFALWDELSPEERDLLVRDIESLDLPRIDRIIRCSLRS------QGLPVPAIEPVPENSVSTVEeRTPEDRE 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235   89 AWESEGLFQISQNKVAVLLLAGGQGTRLGVAYPKGMYDVGLPSRKTLFQIQAERILKLQ----QVAEKYYGNKCIIPWYI 164
Cdd:PLN02435 103 RWWKMGLKAISEGKLAVVLLSGGQGTRLGSSDPKGCFNIGLPSGKSLFQLQAERILCVQrlaaQASSEGPGRPVTIHWYI 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235  165 MTSGRTMESTKEFFTKHKYFGLKKENVIFFQQGMLPAMSFDGKIILEEKNKVSMAPDGNGGLYRALAAQNIVEDMEQRGI 244
Cdd:PLN02435 183 MTSPFTDEATRKFFESHKYFGLEADQVTFFQQGTLPCVSKDGKFIMETPFKVAKAPDGNGGVYAALKSSRLLEDMASRGI 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235  245 WSIHVYCVDNILVKVADPRFIGFCIQKGADCGAKVVEKTNPTEPVGVVCR--VDGVYQVVEYSEI--SLATAQKRSSdGR 320
Cdd:PLN02435 263 KYVDCYGVDNALVRVADPTFLGYFIDKGVASAAKVVRKAYPQEKVGVFVRrgKGGPLTVVEYSELdqAMASAINQQT-GR 341
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235  321 LLFNAGNIANHFFTVPFLRDVVNVYEPQLQHHVAQKKIPYVDTQGQlikpdkpnGIKMEKFVFDIFQFAKKFVVYEVLRE 400
Cdd:PLN02435 342 LRYCWSNVCLHMFTLDFLNQVANGLEKDSIYHLAEKKIPSIHGYTM--------GLKLEQFIFDAFPYAPSTALFEVLRE 413
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235  401 DEFSPLKNADSQNgKDNPTTARHALMSLHHCWVLNAGGhFIdengsrLPAIPRSATNgksetitadvnhnlkdandvpiq 480
Cdd:PLN02435 414 EEFAPVKNANGSN-FDTPESARLLVLRLHTRWVVAAGG-FL------THSVPLYATG----------------------- 462
                        490       500
                 ....*....|....*....|....*.
gi 68846235  481 CEISPLISYAGEGLESYVADKEFHAP 506
Cdd:PLN02435 463 VEVSPLCSYAGENLEAICRGRTFHAP 488
QRI1 COG4284
UDP-N-acetylglucosamine pyrophosphorylase [Carbohydrate transport and metabolism];
6-418 8.48e-136

UDP-N-acetylglucosamine pyrophosphorylase [Carbohydrate transport and metabolism];


Pssm-ID: 443425  Cd Length: 402  Bit Score: 398.87  E-value: 8.48e-136
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235   6 LKLTLSKAGQEHLLRFWNELEEAQQVELYAELQAMNFEELNFFFQKAIEGFNQSShqKNVDARMEPVPREVLGSATRDQD 85
Cdd:COG4284   1 LIEKLEPHGQEHLLRFWDELSEAQQKMLEAQIEEIDIDVFQHLYRQLVLAEGATG--LIPESDIEPAPVTDLPLTDLDEV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235  86 QLQAWESEGLFQISQNKVAVLLLAGGQGTRLGVAYPKGMYDVGLPSRKTLFQIQAERILKlqqvAEKYYGnkCIIPWYIM 165
Cdd:COG4284  79 DRDRAEEAGEEALRAGKVAVILLAGGQGTRLGFDGPKGLLPVRPVKGKSLFDLIAEQVLA----ARRRYG--VPLPLYIM 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235 166 TSGRTMESTKEFFTKHKYFGLKKENVIFFQQGMLPAM-SFDGKIILEEKNKVSMAPDGNGGLYRALAAQNIVEDMEQRGI 244
Cdd:COG4284 153 TSFRTHEDTLAFLEEHDYFGLDGLPVHFFLQGMEPALdADLGPVLLPADPELELCPPGHGGIYTALLASGLLDKLLERGI 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235 245 WSIHVYCVDNILVKVADPRFIGFCIQKGADCGAKVVEKTNPTEPVGVVCRVDGVYQVVEYSEisLATAQKRSSDGRLLFN 324
Cdd:COG4284 233 RYLFVSNVDNPLGAVPDPAFAGWHAASGAPFTAKVVRRTPPDEKVGHLARVDGRLILREYSQ--LPDEEAEAFTGELRHP 310
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235 325 AGNIANHFFTVPFLRDVVNVYEPQLQHHVAQKKIPYVDTQGqliKPDKPNGIKMEKFVFDIFQFAKKFVVYEVLREDEFS 404
Cdd:COG4284 311 YGNINNHWFDLDFLKRLLDERGLGLPLHRAEKKVDPLDESG---KPTSPNVIKFETFMFDAIPLFDGAVAIEVDREERFA 387
                       410
                ....*....|....
gi 68846235 405 PLKNAdsqNGKDNP 418
Cdd:COG4284 388 PVKNT---NGSDSP 398
UDPGP pfam01704
UTP--glucose-1-phosphate uridylyltransferase; This family consists of UTP--glucose-1-phosphate ...
45-472 2.14e-126

UTP--glucose-1-phosphate uridylyltransferase; This family consists of UTP--glucose-1-phosphate uridylyltransferases, EC:2.7.7.9. Also known as UDP-glucose pyrophosphorylase (UDPGP) and Glucose-1-phosphate uridylyltransferase. UTP--glucose-1-phosphate uridylyltransferase catalyzes the interconversion of MgUTP + glucose-1-phosphate and UDP-glucose + MgPPi. UDP-glucose is an important intermediate in mammalian carbohydrate interconversion involved in various metabolic roles depending on tissue type. In Dictyostelium (slime mold) mutants in this enzyme abort the development cycle. Also within the family is UDP-N-acetylglucosamine or AGX1 and two hypothetical proteins from Borrelia burgdorferi the lyme disease spirochaete Swiss:O51893 and Swiss:O51036.


Pssm-ID: 460300  Cd Length: 412  Bit Score: 375.31  E-value: 2.14e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235    45 LNFFFQKAIEGFNQSSHQKNVD-ARMEPVPREVLgsatRDQDQLQA--WESEGLFqisqNKVAVLLLAGGQGTRLGVAYP 121
Cdd:pfam01704   1 LDGFFKLFSRYLSEKGKQEKIDwDKIKPPPEEEI----VDYEDLQEpeEEIKELL----NKLAVLKLNGGLGTSMGCVGP 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235   122 KGMYDVGlpSRKTLFQIQAERILKLQQvaeKYygnKCIIPWYIMTSGRTMESTKEFFTKhkYFGlKKENVIFFQQGMLPA 201
Cdd:pfam01704  73 KSLIEVR--DGLTFLDLIVQQIEHLNK---KY---NVDVPLVLMNSFNTDEDTKKIIRK--YKG-HKVDILTFNQSRYPR 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235   202 MSFDGKIILEEK---NKVSMAPDGNGGLYRALAAQNIVEDMEQRGIWSIHVYCVDNiLVKVADPRFIGFCIQKGADCGAK 278
Cdd:pfam01704 142 IDKDTLLPVPKSadsDEEEWYPPGHGDLYESLYNSGLLDKLLAEGKEYLFVSNIDN-LGATVDLNILNYMVDNGAEFLME 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235   279 VVEKTNPTEPVGVVCRVDGVYQVVEYSEI-SLATAQKRSSDGRLLFNAGNIanhFFTVPFLRDVVNvyEPQLQHHVAQKK 357
Cdd:pfam01704 221 VTDKTRADVKGGTLIEYDGKLRLLEIAQVpKEHVDEFKSIKKFKIFNTNNI---WINLKALKRVVE--EGELQLEIIVNK 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235   358 iPYVDTQGQLIKPDKPNGIKMEKFvfdifqfaKKFVVYEVLReDEFSPLKNADSqngkdnpttarhALMSLHHCWVLNAG 437
Cdd:pfam01704 296 -KTLDNGENVIQLETAVGAAIKNF--------KNAIGINVPR-SRFLPVKTTSD------------LLLVMSDLYVLNHG 353
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235   438 -------------------GHF--IDENGSRLPAIPrSATNGKSETITADV----NHNLK 472
Cdd:pfam01704 354 slimnpkrmfgtppvvllgDHFkkVDEFLKRFPSIP-DLLELDHLTVSGDVtfgrNVTLK 412
UGPase_euk_like cd04180
Eukaryotic UGPase-like includes UDPase and UDPGlcNAc pyrophosphorylase enzymes; This family ...
103-408 7.49e-123

Eukaryotic UGPase-like includes UDPase and UDPGlcNAc pyrophosphorylase enzymes; This family includes UDP-Glucose Pyrophosphorylase (UDPase) and UDPGlcNAc pyrophosphorylase enzymes. The two enzymes share significant sequence and structure similarity. UDP-Glucose Pyrophosphorylase catalyzes a reversible production of UDP-Glucose and pyrophosphate (PPi) from Glucose-1-phosphate and UTP. UDP-glucose plays pivotal roles in galactose utilization, in glycogen synthesis, and in the synthesis of the carbohydrate moieties of glycolipids , glycoproteins , and proteoglycans . UDP-N-acetylglucosamine (UDPGlcNAc) pyrophosphorylase (UAP) (also named GlcNAc1P uridyltransferase), catalyzes the reversible conversion of UTP and GlcNAc1P from PPi and UDPGlcNAc, which is a key precursor of N- and O-linked glycosylations and is essential for the synthesis of chitin (a major component of the fungal cell wall) and of the glycosylphosphatidylinositol (GPI) linker anchoring a variety of cell surface proteins to the plasma membrane. In bacteria, UDPGlcNAc represents an essential precursor for both peptidoglycan and lipopolysaccharide biosynthesis.


Pssm-ID: 133023  Cd Length: 266  Bit Score: 360.72  E-value: 7.49e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235 103 VAVLLLAGGQGTRLGVAYPKGMYDVGLPSRKTLFQIQAERILKLQQVAEkyygNKCIIPWYIMTSGRTMESTKEFFTKHK 182
Cdd:cd04180   1 VAVVLLAGGLGTRLGKDGPKSSTDVGLPSGQCFLQLIGEKILTLQEIDL----YSCKIPEQLMNSKYTHEKTQCYFEKIN 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235 183 yfgLKKENVIFFQQGMLPAMSFDGKIILEEKNKVSMAPDGNGGLYRALAAQNIVEDMEQRGIWSIHVYCVDNILVKVADP 262
Cdd:cd04180  77 ---QKNSYVITFMQGKLPLKNDDDARDPHNKTKCHLFPCGHGDVVLALIHSGHLNKLLEKGYRYIHFIGVDNLLVKVADP 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235 263 RFIGFCIQKGADCGAKVVEKTNPTEPVGVVCRVD-GVYQVVEYSEISLATAQKR------SSDGRLLFNAGNIANHFFTV 335
Cdd:cd04180 154 LFIGIAIQNRKAINQKVVPKTRNEESGGYRIANInGRVQLLEYDQIKKLLKQKMvnnqipKDIDDAPFFLFNTNNLINFL 233
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 68846235 336 PFLRDVVNvyepqlqhhvaqkkipyvdtqgqlikpdkpngikmekfvfDIFQFAKKFVVYEVLREDEFSPLKN 408
Cdd:cd04180 234 VEFKDRVD----------------------------------------DIIEFTDDIVGVMVHRAEEFAPVKN 266
PTZ00339 PTZ00339
UDP-N-acetylglucosamine pyrophosphorylase; Provisional
10-508 3.52e-114

UDP-N-acetylglucosamine pyrophosphorylase; Provisional


Pssm-ID: 240368  Cd Length: 482  Bit Score: 346.34  E-value: 3.52e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235   10 LSKAGQEHLLRFWNELEE-------AQQVELYAELQAMNFEE-----LNFFFQKAIEGFNQSSHQKNVdarMEPVPREVL 77
Cdd:PTZ00339   5 LTGDGQDHLREALKRRSEgeftplaTQILSSLTNVDFKHRNAvlepkLEEYNAEAPVGIDIDSIHNCN---IEPPNNNTF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235   78 GSATRDQDQLQAWESEGLFQISQNKVAVLLLAGGQGTRLGVAYPKGMYDVGLPSRKTLFQIQAERILKLQQVAEKYY--G 155
Cdd:PTZ00339  82 IDIYEKEKERKELKESGLEIIKKGEVAVLILAGGLGTRLGSDKPKGLLECTPVKKKTLFQFHCEKVRRLEEMAVAVSggG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235  156 NKCIIPWYIMTSGRTMESTKEFFTKHKYFGLKKENVIFFQQGMLPAMS-FDGKIILEEKNKVSMAPDGNGGLYRALAAQN 234
Cdd:PTZ00339 162 DDPTIYILVLTSSFNHDQTRQFLEENNFFGLDKEQVIFFKQSSLPCYDeNTGRFIMSSQGSLCTAPGGNGDVFKALAKCS 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235  235 IVEDMEQRGIWSIHVYCVDNILVKVADPRFIGFCIQKGADCGAKVVEKTNPTEPVGVVCRVDGVYQVVEYSEIS-LATAQ 313
Cdd:PTZ00339 242 ELMDIVRKGIKYVQVISIDNILAKVLDPEFIGLASSFPAHDVLNKCVKREDDESVGVFCLKDYEWQVVEYTEINeRILNN 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235  314 KRSSDGRLLFNAGNIANHFFTVPFLRDVVNVY-EPQLQHHVAQKKIPYVDtqgqlIKPDKPNGIKMEKFVFDIFQFAKKF 392
Cdd:PTZ00339 322 DELLTGELAFNYGNICSHIFSLDFLKKVAANRlYESTPYHAARKKIPYIN-----GPTDKTMGIKLEAFIFDIFRYAKNV 396
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235  393 VVYEVLREDEFSPLKNADSQNGkDNPTTARHALMSLHHCWVLNAgghfidenGSRLPAIPRSATNGksetitadvnhnlk 472
Cdd:PTZ00339 397 LILEVDREDEFAPIKNADGAAA-DTILNAQKLLLSLHTRWLEAA--------LETVAGNPREGLNL-------------- 453
                        490       500       510
                 ....*....|....*....|....*....|....*.
gi 68846235  473 dandvpiqCEISPLISYAGEGLESYVADKEFHAPLI 508
Cdd:PTZ00339 454 --------CEISPLVSYGGEGLFQYPGKKILGLPEI 481
UGGPase cd06424
UGGPase catalyzes the synthesis of UDP-Glucose/UDP-Galactose; UGGPase: UDP-Galactose/Glucose ...
103-294 8.39e-18

UGGPase catalyzes the synthesis of UDP-Glucose/UDP-Galactose; UGGPase: UDP-Galactose/Glucose Pyrophosphorylase catalyzes the reversible production of UDP-Glucose/UDP-Galactose and pyrophosphate (PPi) from Glucose-1-phosphate/Galactose-1-phosphate and UTP. Its dual substrate specificity distinguishes it from the single substrate enzyme UDP-glucose pyrophosphorylase. It may play a key role in the galactose metabolism in raffinose oligosaccharide (RFO) metabolizing plants. RFO raffinose is a major photoassimilate and is a galactosylderivative of sucrose (Suc) containing a galactose (Gal) moiety. Upon arriving at the sink tissue, the Gal moieties of the RFOs are initially removed by alpha-galactosidase and then are phosphorylated to Gal-1-P. Gal-1-P is converted to UDP-Gal. The UDP-Gal is further metabolized to UDP-Glc via an epimerase reaction. The UDP-Glc can be directly utilized in cell wall metabolism or in Suc synthesis. However, for the Suc synthesis UDP-Glc must be further metabolized to Glc-1-P. This can be carried out either by the UGPase in the reverse direction or by the dual substrate PPase itself operating in the reverse direction. According to the latter possibility, the three-step pathway of Gal-1-P to Glc-1-P could be carried out by a single PPase, functioning sequentially in reverse directions separated by the epimerase reaction.


Pssm-ID: 133046  Cd Length: 315  Bit Score: 84.43  E-value: 8.39e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235 103 VAVLLLAGGQGTRLGVAYPKGMYDVGLPSRKTLFQIQAERILKLQQVAEKYYGNKciIPWYIMTSGRTMESTKEFFTKHK 182
Cdd:cd06424   1 AVFVLVAGGLGERLGYSGIKIGLPVELTTNTTYLQYYLNYIRAFQEASKKGEKME--IPFVIMTSDDTHSKTLKLLEENN 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235 183 YFGLKKENVIFFQQGMLPAM-SFDGKIILEEKNKVSMA--PDGNGGLYRALAAQNIVEDMEQRGIWSIHVYCVDNILVKV 259
Cdd:cd06424  79 YFGLEKDQVHILKQEKVFCLiDNDAHLALDPDNTYSILtkPHGHGDVHTLLYNSGLLKKWIEAGYKWLVFFQDTNALAFK 158
                       170       180       190
                ....*....|....*....|....*....|....*
gi 68846235 260 ADPRFIGFCIQKGADCGAKVVEKTnPTEPVGVVCR 294
Cdd:cd06424 159 AIPAVLGVSATKSLDMNSLTVPRK-PKEAIGALCK 192
PLN02830 PLN02830
UDP-sugar pyrophosphorylase
91-224 1.07e-16

UDP-sugar pyrophosphorylase


Pssm-ID: 215444  Cd Length: 615  Bit Score: 83.20  E-value: 1.07e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235   91 ESEGLFQIsqNKVAVLLLAGGQGTRLGVAYPKgmydVGLPSRKT----LFQIQAERILKLQQVAEKYYGNKCI-IPWYIM 165
Cdd:PLN02830 119 EEAGLREA--GNAAFVLVAGGLGERLGYSGIK----VALPTETAtgtcYLQLYIESILALQERAKKRKAKKGRkIPLVIM 192
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 68846235  166 TSGRTMESTKEFFTKHKYFGLKKENVIFFQQGMLPAMS-FDGKIILEEKN--KVSMAPDGNG 224
Cdd:PLN02830 193 TSDDTHARTLKLLERNDYFGMDPDQVTLLKQEKVACLMdNDARLALDPNDpyKIQTKPHGHG 254
UGPase_euk cd00897
Eukaryotic UGPase catalyses the synthesis of UDP-Glucose; UGPase (UDP-Glucose ...
101-303 7.55e-08

Eukaryotic UGPase catalyses the synthesis of UDP-Glucose; UGPase (UDP-Glucose Pyrophosphorylase) catalyzes the reversible production of UDP-Glucose and pyrophosphate (PPi) from Glucose-1-phosphate and UTP. UDP-glucose plays pivotal roles in galactose utilization, in glycogen synthesis, and in the synthesis of the carbohydrate moieties of glycolipids, glycoproteins, and proteoglycans. UGPase is found in both prokaryotes and eukaryotes. Interestingly, while the prokaryotic and eukaryotic forms of UGPase catalyze the same reaction, they share low sequence similarity. This family consists of mainly eukaryotic UTP-glucose-1-phosphate uridylyltransferases.


Pssm-ID: 132998  Cd Length: 300  Bit Score: 54.17  E-value: 7.55e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235 101 NKVAVLLLAGGQGTRLGVAYPKGMYDVglPSRKTLFQIQAERILKLQQvaeKYYGNkciIPWYIMTSGRTMESTKEFFTK 180
Cdd:cd00897   2 NKLVVLKLNGGLGTSMGCTGPKSLIEV--RDGKTFLDLTVQQIEHLNK---TYGVD---VPLVLMNSFNTDEDTKKILKK 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235 181 HKYFglkKENVIFFQQGMLPAMSFDGKIILEEK---NKVSMAPDGNGGLYRALAAQNIVEDMEQRGIWSIHVYCVDNiLV 257
Cdd:cd00897  74 YAGV---NVDIHTFNQSRYPRISKETLLPVPSWadsPDEEWYPPGHGDIFESLYNSGLLDTLLAQGKEYLFVSNIDN-LG 149
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 68846235 258 KVADPRFIGFCIQKGADCGAKVVEKTNPTEPVGVVCRVDGVYQVVE 303
Cdd:cd00897 150 ATVDLRILNHMVDNKAEYIMEVTDKTRADVKGGTLIQYEGKLRLLE 195
PLN02474 PLN02474
UTP--glucose-1-phosphate uridylyltransferase
101-328 3.23e-04

UTP--glucose-1-phosphate uridylyltransferase


Pssm-ID: 178092  Cd Length: 469  Bit Score: 43.33  E-value: 3.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235  101 NKVAVLLLAGGQGTRLGVAYPKGMYDV--GLpSRKTLFQIQAERIlklqqvaEKYYGnkCIIPWYIMTSGRTMESTKEFF 178
Cdd:PLN02474  78 DKLVVLKLNGGLGTTMGCTGPKSVIEVrnGL-TFLDLIVIQIENL-------NKKYG--CNVPLLLMNSFNTHDDTQKIV 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68846235  179 TKHKYFGLKkenVIFFQQGMLPAMSFDGKIILEEKNKVSMA---PDGNGGLYRALAAQNIVEDMEQRGIWSIHVYCVDNi 255
Cdd:PLN02474 148 EKYTNSNIE---IHTFNQSQYPRVVADDFVPWPSKGKTDKDgwyPPGHGDVFPSLMNSGKLDALLSQGKEYVFIANSDN- 223
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 68846235  256 LVKVADPRFIGFCIQKGADCGAKVVEKTNPTEPVGVVCRVDGVYQVVEYSEISLATAQK-RSSDGRLLFNAGNI 328
Cdd:PLN02474 224 LGAIVDLKILNHLIQNKNEYCMEVTPKTLADVKGGTLISYEGKVQLLEIAQVPDEHVNEfKSIEKFKIFNTNNL 297
 
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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