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Conserved domains on  [gi|19113624|ref|NP_596832|]
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UDP-N-acetylglucosamine diphosphorylase Uap1/Qri1(predicted) [Schizosaccharomyces pombe]

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
PubMed:  12691742|9445404|10521532
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 ...
 84-412 2.28e-179

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: 504.83  E-value: 2.28e-179
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113624  84 SWWRTGLREIARGHVAALVLAGGQGTRLGFAGPKGCFRLGLPNNPSIFELQAQKIKKSLALARAAFpdqEASISIPWYIM 163
Cdd:cd04193   2 EWEEAGLKAIAEGKVAVLLLAGGQGTRLGFDGPKGMFPVGLPSKKSLFQLQAERILKLQELAGEAS---GKKVPIPWYIM 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113624 164 VSECTSEETISFFKENDFFGIDKKDVFFFQQGVLPCLDISGRVLFESDSSLAWAPNGNGGIYEALLSSGALNDMNRRGIL 243
Cdd:cd04193  79 TSEATHEETRKFFKENNYFGLDPEQVHFFQQGMLPCVDFDGKILLEEKGKIAMAPNGNGGLYKALQTAGILEDMKKRGIK 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113624 244 HITAYSVDNVLVLPVDPVFIGMATTKKLEVATKTVEKIDPAEKVGLLVSSHNHPCVVEYSEISDEackATENVDGHKHLL 323
Cdd:cd04193 159 YIHVYSVDNILVKVADPVFIGFCISKGADVGAKVVRKRYPTEKVGVVVLVDGKPQVVEYSEISDE---LAEKRDADGELQ 235

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113624 324 LRAANIAYHYFSFDFLQKAS-LHSSTLPIHLACKKIPFYDVTShHYTTPLNPNGYKLESFIFDLFPsvSVENFGCFQVPR 402
Cdd:cd04193 236 YNAGNIANHFFSLDFLEKAAeMEEPSLPYHIAKKKIPYVDLEG-GLVKPDEPNGIKLELFIFDVFP--FAKNFVCLEVDR 312

                       330
                ....*....|
gi 19113624 403 RTSFSPLKNS 412
Cdd:cd04193 313 EEEFSPLKNA 322
 
Name Accession Description Interval E-value
UDPGlcNAc_PPase cd04193
UDPGlcNAc pyrophosphorylase catalayzes the synthesis of UDPGlcNAc; UDP-N-acetylglucosamine ...
 84-412 2.28e-179

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: 504.83  E-value: 2.28e-179
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113624  84 SWWRTGLREIARGHVAALVLAGGQGTRLGFAGPKGCFRLGLPNNPSIFELQAQKIKKSLALARAAFpdqEASISIPWYIM 163
Cdd:cd04193   2 EWEEAGLKAIAEGKVAVLLLAGGQGTRLGFDGPKGMFPVGLPSKKSLFQLQAERILKLQELAGEAS---GKKVPIPWYIM 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113624 164 VSECTSEETISFFKENDFFGIDKKDVFFFQQGVLPCLDISGRVLFESDSSLAWAPNGNGGIYEALLSSGALNDMNRRGIL 243
Cdd:cd04193  79 TSEATHEETRKFFKENNYFGLDPEQVHFFQQGMLPCVDFDGKILLEEKGKIAMAPNGNGGLYKALQTAGILEDMKKRGIK 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113624 244 HITAYSVDNVLVLPVDPVFIGMATTKKLEVATKTVEKIDPAEKVGLLVSSHNHPCVVEYSEISDEackATENVDGHKHLL 323
Cdd:cd04193 159 YIHVYSVDNILVKVADPVFIGFCISKGADVGAKVVRKRYPTEKVGVVVLVDGKPQVVEYSEISDE---LAEKRDADGELQ 235

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113624 324 LRAANIAYHYFSFDFLQKAS-LHSSTLPIHLACKKIPFYDVTShHYTTPLNPNGYKLESFIFDLFPsvSVENFGCFQVPR 402
Cdd:cd04193 236 YNAGNIANHFFSLDFLEKAAeMEEPSLPYHIAKKKIPYVDLEG-GLVKPDEPNGIKLELFIFDVFP--FAKNFVCLEVDR 312

                       330
                ....*....|
gi 19113624 403 RTSFSPLKNS 412
Cdd:cd04193 313 EEEFSPLKNA 322
QRI1 COG4284
UDP-N-acetylglucosamine pyrophosphorylase [Carbohydrate transport and metabolism];
6-411 1.90e-112

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


Pssm-ID: 443425  Cd Length: 402  Bit Score: 337.63  E-value: 1.90e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113624   6 LFDRsiFEETNQLHLydqLNYLKKNDLQKFRKLLNQVQQLDLRSLWLKYRNAKATSQENRKLSPSEVGPLSIV-----DT 80
Cdd:COG4284   1 LIEK--LEPHGQEHL---LRFWDELSEAQQKMLEAQIEEIDIDVFQHLYRQLVLAEGATGLIPESDIEPAPVTdlpltDL 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113624  81 SDSSWWR---TGLREIARGHVAALVLAGGQGTRLGFAGPKGCFRLGLPNNPSIFELQAQKIkksLALARaafpdqEASIS 157
Cdd:COG4284  76 DEVDRDRaeeAGEEALRAGKVAVILLAGGQGTRLGFDGPKGLLPVRPVKGKSLFDLIAEQV---LAARR------RYGVP 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113624 158 IPWYIMVSECTSEETISFFKENDFFGIDKKDVFFFQQGVLPCLDI-SGRVLFESDSSLAWAPNGNGGIYEALLSSGALND 236
Cdd:COG4284 147 LPLYIMTSFRTHEDTLAFLEEHDYFGLDGLPVHFFLQGMEPALDAdLGPVLLPADPELELCPPGHGGIYTALLASGLLDK 226

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113624 237 MNRRGILHITAYSVDNVLVLPVDPVFIGMATTKKLEVATKTVEKIDPAEKVGLLVSSHNHPCVVEYSEISDEAckATENV 316
Cdd:COG4284 227 LLERGIRYLFVSNVDNPLGAVPDPAFAGWHAASGAPFTAKVVRRTPPDEKVGHLARVDGRLILREYSQLPDEE--AEAFT 304

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113624 317 DGHKHlllRAANIAYHYFSFDFLQK-ASLHSSTLPIHLACKKIPFYDVTShhytTPLNPNGYKLESFIFDLFPsvSVENF 395
Cdd:COG4284 305 GELRH---PYGNINNHWFDLDFLKRlLDERGLGLPLHRAEKKVDPLDESG----KPTSPNVIKFETFMFDAIP--LFDGA 375

                       410
                ....*....|....*.
gi 19113624 396 GCFQVPRRTSFSPLKN 411
Cdd:COG4284 376 VAIEVDREERFAPVKN 391
PLN02435 PLN02435
probable UDP-N-acetylglucosamine pyrophosphorylase
 85-464 8.57e-95

probable UDP-N-acetylglucosamine pyrophosphorylase


Pssm-ID: 215238  Cd Length: 493  Bit Score: 295.24  E-value: 8.57e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113624   85 WWRTGLREIARGHVAALVLAGGQGTRLGFAGPKGCFRLGLPNNPSIFELQAQKIKKSLALA-RAAFPDQEASISIPWYIM 163
Cdd:PLN02435 104 WWKMGLKAISEGKLAVVLLSGGQGTRLGSSDPKGCFNIGLPSGKSLFQLQAERILCVQRLAaQASSEGPGRPVTIHWYIM 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113624  164 VSECTSEETISFFKENDFFGIDKKDVFFFQQGVLPCLDISGRVLFESDSSLAWAPNGNGGIYEALLSSGALNDMNRRGIL 243
Cdd:PLN02435 184 TSPFTDEATRKFFESHKYFGLEADQVTFFQQGTLPCVSKDGKFIMETPFKVAKAPDGNGGVYAALKSSRLLEDMASRGIK 263

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113624  244 HITAYSVDNVLVLPVDPVFIGMATTKKLEVATKTVEKIDPAEKVGLLVS-SHNHP-CVVEYSEIsdEACKATENVDGHKH 321
Cdd:PLN02435 264 YVDCYGVDNALVRVADPTFLGYFIDKGVASAAKVVRKAYPQEKVGVFVRrGKGGPlTVVEYSEL--DQAMASAINQQTGR 341

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113624  322 LLLRAANIAYHYFSFDFLQKA--SLHSSTLpIHLACKKIPfydvTSHHYTTplnpnGYKLESFIFDLF---PSVSVenfg 396
Cdd:PLN02435 342 LRYCWSNVCLHMFTLDFLNQVanGLEKDSI-YHLAEKKIP----SIHGYTM-----GLKLEQFIFDAFpyaPSTAL---- 407

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19113624  397 cFQVPRRTSFSPLKNSSKSPNDNHETCVNDILSLGKSWILKNGGILSPSDCTY-----VSPECSLQGESLEWI 464
Cdd:PLN02435 408 -FEVLREEEFAPVKNANGSNFDTPESARLLVLRLHTRWVVAAGGFLTHSVPLYatgveVSPLCSYAGENLEAI 479
UDPGP pfam01704
UTP--glucose-1-phosphate uridylyltransferase; This family consists of UTP--glucose-1-phosphate ...
 66-445 7.05e-31

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: 123.39  E-value: 7.05e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113624    66 KLSPSEVGPLS---IVDTSD---SSWWRTGLREiargHVAALVLAGGQGTRLGFAGPKGCFRLGlpNNPSIFELQAQKIK 139
Cdd:pfam01704  20 KIDWDKIKPPPeeeIVDYEDlqePEEEIKELLN----KLAVLKLNGGLGTSMGCVGPKSLIEVR--DGLTFLDLIVQQIE 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113624   140 KSlalaraafpDQEASISIPWYIMVSECTSEETISFFKenDFFGiDKKDVFFFQQGVLPcldisgRVLFES--------- 210
Cdd:pfam01704  94 HL---------NKKYNVDVPLVLMNSFNTDEDTKKIIR--KYKG-HKVDILTFNQSRYP------RIDKDTllpvpksad 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113624   211 DSSLAWAPNGNGGIYEALLSSGALNDMNRRGILHITAYSVDNvLVLPVDPVFIGMATTKKLEVATKTVEKIDPAEKVGLL 290
Cdd:pfam01704 156 SDEEEWYPPGHGDLYESLYNSGLLDKLLAEGKEYLFVSNIDN-LGATVDLNILNYMVDNGAEFLMEVTDKTRADVKGGTL 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113624   291 VSSHNHPCVVEYSEISDEACKATENVDGHKhlLLRAANIayhYFSFDFLQKAsLHSSTLPIHLackkIPFYDVTSHHYTT 370
Cdd:pfam01704 235 IEYDGKLRLLEIAQVPKEHVDEFKSIKKFK--IFNTNNI---WINLKALKRV-VEEGELQLEI----IVNKKTLDNGENV 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113624   371 --PLNPNGYKLESFifdlfpsvsvENFGCFQVPRrTSFSPLKNSSkspndnhetcvnDILSLgKS--WILKNGG-ILSPS 445
Cdd:pfam01704 305 iqLETAVGAAIKNF----------KNAIGINVPR-SRFLPVKTTS------------DLLLV-MSdlYVLNHGSlIMNPK 360
 
Name Accession Description Interval E-value
UDPGlcNAc_PPase cd04193
UDPGlcNAc pyrophosphorylase catalayzes the synthesis of UDPGlcNAc; UDP-N-acetylglucosamine ...
 84-412 2.28e-179

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: 504.83  E-value: 2.28e-179
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113624  84 SWWRTGLREIARGHVAALVLAGGQGTRLGFAGPKGCFRLGLPNNPSIFELQAQKIKKSLALARAAFpdqEASISIPWYIM 163
Cdd:cd04193   2 EWEEAGLKAIAEGKVAVLLLAGGQGTRLGFDGPKGMFPVGLPSKKSLFQLQAERILKLQELAGEAS---GKKVPIPWYIM 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113624 164 VSECTSEETISFFKENDFFGIDKKDVFFFQQGVLPCLDISGRVLFESDSSLAWAPNGNGGIYEALLSSGALNDMNRRGIL 243
Cdd:cd04193  79 TSEATHEETRKFFKENNYFGLDPEQVHFFQQGMLPCVDFDGKILLEEKGKIAMAPNGNGGLYKALQTAGILEDMKKRGIK 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113624 244 HITAYSVDNVLVLPVDPVFIGMATTKKLEVATKTVEKIDPAEKVGLLVSSHNHPCVVEYSEISDEackATENVDGHKHLL 323
Cdd:cd04193 159 YIHVYSVDNILVKVADPVFIGFCISKGADVGAKVVRKRYPTEKVGVVVLVDGKPQVVEYSEISDE---LAEKRDADGELQ 235

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113624 324 LRAANIAYHYFSFDFLQKAS-LHSSTLPIHLACKKIPFYDVTShHYTTPLNPNGYKLESFIFDLFPsvSVENFGCFQVPR 402
Cdd:cd04193 236 YNAGNIANHFFSLDFLEKAAeMEEPSLPYHIAKKKIPYVDLEG-GLVKPDEPNGIKLELFIFDVFP--FAKNFVCLEVDR 312

                       330
                ....*....|
gi 19113624 403 RTSFSPLKNS 412
Cdd:cd04193 313 EEEFSPLKNA 322
QRI1 COG4284
UDP-N-acetylglucosamine pyrophosphorylase [Carbohydrate transport and metabolism];
6-411 1.90e-112

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


Pssm-ID: 443425  Cd Length: 402  Bit Score: 337.63  E-value: 1.90e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113624   6 LFDRsiFEETNQLHLydqLNYLKKNDLQKFRKLLNQVQQLDLRSLWLKYRNAKATSQENRKLSPSEVGPLSIV-----DT 80
Cdd:COG4284   1 LIEK--LEPHGQEHL---LRFWDELSEAQQKMLEAQIEEIDIDVFQHLYRQLVLAEGATGLIPESDIEPAPVTdlpltDL 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113624  81 SDSSWWR---TGLREIARGHVAALVLAGGQGTRLGFAGPKGCFRLGLPNNPSIFELQAQKIkksLALARaafpdqEASIS 157
Cdd:COG4284  76 DEVDRDRaeeAGEEALRAGKVAVILLAGGQGTRLGFDGPKGLLPVRPVKGKSLFDLIAEQV---LAARR------RYGVP 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113624 158 IPWYIMVSECTSEETISFFKENDFFGIDKKDVFFFQQGVLPCLDI-SGRVLFESDSSLAWAPNGNGGIYEALLSSGALND 236
Cdd:COG4284 147 LPLYIMTSFRTHEDTLAFLEEHDYFGLDGLPVHFFLQGMEPALDAdLGPVLLPADPELELCPPGHGGIYTALLASGLLDK 226

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113624 237 MNRRGILHITAYSVDNVLVLPVDPVFIGMATTKKLEVATKTVEKIDPAEKVGLLVSSHNHPCVVEYSEISDEAckATENV 316
Cdd:COG4284 227 LLERGIRYLFVSNVDNPLGAVPDPAFAGWHAASGAPFTAKVVRRTPPDEKVGHLARVDGRLILREYSQLPDEE--AEAFT 304

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113624 317 DGHKHlllRAANIAYHYFSFDFLQK-ASLHSSTLPIHLACKKIPFYDVTShhytTPLNPNGYKLESFIFDLFPsvSVENF 395
Cdd:COG4284 305 GELRH---PYGNINNHWFDLDFLKRlLDERGLGLPLHRAEKKVDPLDESG----KPTSPNVIKFETFMFDAIP--LFDGA 375

                       410
                ....*....|....*.
gi 19113624 396 GCFQVPRRTSFSPLKN 411
Cdd:COG4284 376 VAIEVDREERFAPVKN 391
PLN02435 PLN02435
probable UDP-N-acetylglucosamine pyrophosphorylase
 85-464 8.57e-95

probable UDP-N-acetylglucosamine pyrophosphorylase


Pssm-ID: 215238  Cd Length: 493  Bit Score: 295.24  E-value: 8.57e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113624   85 WWRTGLREIARGHVAALVLAGGQGTRLGFAGPKGCFRLGLPNNPSIFELQAQKIKKSLALA-RAAFPDQEASISIPWYIM 163
Cdd:PLN02435 104 WWKMGLKAISEGKLAVVLLSGGQGTRLGSSDPKGCFNIGLPSGKSLFQLQAERILCVQRLAaQASSEGPGRPVTIHWYIM 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113624  164 VSECTSEETISFFKENDFFGIDKKDVFFFQQGVLPCLDISGRVLFESDSSLAWAPNGNGGIYEALLSSGALNDMNRRGIL 243
Cdd:PLN02435 184 TSPFTDEATRKFFESHKYFGLEADQVTFFQQGTLPCVSKDGKFIMETPFKVAKAPDGNGGVYAALKSSRLLEDMASRGIK 263

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113624  244 HITAYSVDNVLVLPVDPVFIGMATTKKLEVATKTVEKIDPAEKVGLLVS-SHNHP-CVVEYSEIsdEACKATENVDGHKH 321
Cdd:PLN02435 264 YVDCYGVDNALVRVADPTFLGYFIDKGVASAAKVVRKAYPQEKVGVFVRrGKGGPlTVVEYSEL--DQAMASAINQQTGR 341

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113624  322 LLLRAANIAYHYFSFDFLQKA--SLHSSTLpIHLACKKIPfydvTSHHYTTplnpnGYKLESFIFDLF---PSVSVenfg 396
Cdd:PLN02435 342 LRYCWSNVCLHMFTLDFLNQVanGLEKDSI-YHLAEKKIP----SIHGYTM-----GLKLEQFIFDAFpyaPSTAL---- 407

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19113624  397 cFQVPRRTSFSPLKNSSKSPNDNHETCVNDILSLGKSWILKNGGILSPSDCTY-----VSPECSLQGESLEWI 464
Cdd:PLN02435 408 -FEVLREEEFAPVKNANGSNFDTPESARLLVLRLHTRWVVAAGGFLTHSVPLYatgveVSPLCSYAGENLEAI 479
PTZ00339 PTZ00339
UDP-N-acetylglucosamine pyrophosphorylase; Provisional
 13-469 1.49e-79

UDP-N-acetylglucosamine pyrophosphorylase; Provisional


Pssm-ID: 240368  Cd Length: 482  Bit Score: 255.44  E-value: 1.49e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113624   13 EETNQLHLYDQLNY--------LKKNDLQKFRKLLNQVQQLDLRSLWLKYRNAKATSQENRKLSPSEVGPL---SIVDTS 81
Cdd:PTZ00339   6 TGDGQDHLREALKRrsegeftpLATQILSSLTNVDFKHRNAVLEPKLEEYNAEAPVGIDIDSIHNCNIEPPnnnTFIDIY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113624   82 D-----SSWWRTGLREIARGHVAALVLAGGQGTRLGFAGPKGCFRLGLPNNPSIFELQAQKIKKSLALArAAFPDQEASI 156
Cdd:PTZ00339  86 EkekerKELKESGLEIIKKGEVAVLILAGGLGTRLGSDKPKGLLECTPVKKKTLFQFHCEKVRRLEEMA-VAVSGGGDDP 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113624  157 SIPWYIMVSECTSEETISFFKENDFFGIDKKDVFFFQQGVLPCLD-ISGRVLFESDSSLAWAPNGNGGIYEALLSSGALN 235
Cdd:PTZ00339 165 TIYILVLTSSFNHDQTRQFLEENNFFGLDKEQVIFFKQSSLPCYDeNTGRFIMSSQGSLCTAPGGNGDVFKALAKCSELM 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113624  236 DMNRRGILHITAYSVDNVLVLPVDPVFIGMATTKKLEVATKTVEKIDPAEKVGLLVSSHNHPCVVEYSEISDeaCKATEN 315
Cdd:PTZ00339 245 DIVRKGIKYVQVISIDNILAKVLDPEFIGLASSFPAHDVLNKCVKREDDESVGVFCLKDYEWQVVEYTEINE--RILNND 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113624  316 VDGHKHLLLRAANIAYHYFSFDFLQKAS---LHSSTlPIHLACKKIPFYDVTSHHyttplnPNGYKLESFIFDLFPsvSV 392
Cdd:PTZ00339 323 ELLTGELAFNYGNICSHIFSLDFLKKVAanrLYEST-PYHAARKKIPYINGPTDK------TMGIKLEAFIFDIFR--YA 393

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113624  393 ENFGCFQVPRRTSFSPLKNSSKSPNDNHETCVNDILSLGKSWILKNGGILSPSD-----CTYVSPECSLQGESLEWIKGK 467
Cdd:PTZ00339 394 KNVLILEVDREDEFAPIKNADGAAADTILNAQKLLLSLHTRWLEAALETVAGNPreglnLCEISPLVSYGGEGLFQYPGK 473


                 ..
gi 19113624  468 QV 469
Cdd:PTZ00339 474 KI 475
UGPase_euk_like cd04180
Eukaryotic UGPase-like includes UDPase and UDPGlcNAc pyrophosphorylase enzymes; This family ...
 98-411 7.29e-48

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: 165.81  E-value: 7.29e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113624  98 VAALVLAGGQGTRLGFAGPKGCFRLGLPNNPSIFELQAQKIkksLALARAAfpdqEASISIPWYIMVSECTSEETISFFK 177
Cdd:cd04180   1 VAVVLLAGGLGTRLGKDGPKSSTDVGLPSGQCFLQLIGEKI---LTLQEID----LYSCKIPEQLMNSKYTHEKTQCYFE 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113624 178 ENDffgIDKKDVFFFQQGVLPCLDISGRVLFESDSSLAWAPNGNGGIYEALLSSGALNDMNRRGILHITAYSVDNVLVLP 257
Cdd:cd04180  74 KIN---QKNSYVITFMQGKLPLKNDDDARDPHNKTKCHLFPCGHGDVVLALIHSGHLNKLLEKGYRYIHFIGVDNLLVKV 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113624 258 VDPVFIGMATTKKLEVATKTVEKIDPAEKVGLLVSSHNHPC-VVEYSEISDEACKATENVDGHK---HLLLRAANIAYHY 333
Cdd:cd04180 151 ADPLFIGIAIQNRKAINQKVVPKTRNEESGGYRIANINGRVqLLEYDQIKKLLKQKMVNNQIPKdidDAPFFLFNTNNLI 230

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19113624 334 FSFDFLQkaslhsstlpiHLACKKIPFYDvtshhyttplnpngyklesfifdlfpsvsveNFGCFQVPRRTSFSPLKN 411
Cdd:cd04180 231 NFLVEFK-----------DRVDDIIEFTD-------------------------------DIVGVMVHRAEEFAPVKN 266
UDPGP pfam01704
UTP--glucose-1-phosphate uridylyltransferase; This family consists of UTP--glucose-1-phosphate ...
 66-445 7.05e-31

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: 123.39  E-value: 7.05e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113624    66 KLSPSEVGPLS---IVDTSD---SSWWRTGLREiargHVAALVLAGGQGTRLGFAGPKGCFRLGlpNNPSIFELQAQKIK 139
Cdd:pfam01704  20 KIDWDKIKPPPeeeIVDYEDlqePEEEIKELLN----KLAVLKLNGGLGTSMGCVGPKSLIEVR--DGLTFLDLIVQQIE 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113624   140 KSlalaraafpDQEASISIPWYIMVSECTSEETISFFKenDFFGiDKKDVFFFQQGVLPcldisgRVLFES--------- 210
Cdd:pfam01704  94 HL---------NKKYNVDVPLVLMNSFNTDEDTKKIIR--KYKG-HKVDILTFNQSRYP------RIDKDTllpvpksad 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113624   211 DSSLAWAPNGNGGIYEALLSSGALNDMNRRGILHITAYSVDNvLVLPVDPVFIGMATTKKLEVATKTVEKIDPAEKVGLL 290
Cdd:pfam01704 156 SDEEEWYPPGHGDLYESLYNSGLLDKLLAEGKEYLFVSNIDN-LGATVDLNILNYMVDNGAEFLMEVTDKTRADVKGGTL 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113624   291 VSSHNHPCVVEYSEISDEACKATENVDGHKhlLLRAANIayhYFSFDFLQKAsLHSSTLPIHLackkIPFYDVTSHHYTT 370
Cdd:pfam01704 235 IEYDGKLRLLEIAQVPKEHVDEFKSIKKFK--IFNTNNI---WINLKALKRV-VEEGELQLEI----IVNKKTLDNGENV 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113624   371 --PLNPNGYKLESFifdlfpsvsvENFGCFQVPRrTSFSPLKNSSkspndnhetcvnDILSLgKS--WILKNGG-ILSPS 445
Cdd:pfam01704 305 iqLETAVGAAIKNF----------KNAIGINVPR-SRFLPVKTTS------------DLLLV-MSdlYVLNHGSlIMNPK 360
UGGPase cd06424
UGGPase catalyzes the synthesis of UDP-Glucose/UDP-Galactose; UGGPase: UDP-Galactose/Glucose ...
 98-290 5.22e-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: 84.82  E-value: 5.22e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113624  98 VAALVLAGGQGTRLGFAGPKGCFRLGLPNNPSIFELQAQKIkksLALARAAFPDQEasISIPWYIMVSECTSEETISFFK 177
Cdd:cd06424   1 AVFVLVAGGLGERLGYSGIKIGLPVELTTNTTYLQYYLNYI---RAFQEASKKGEK--MEIPFVIMTSDDTHSKTLKLLE 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113624 178 ENDFFGIDKKDVFFFQQGVLPCLDISGR--VLFESDS-SLAWAPNGNGGIYEALLSSGALNDMNRRGILHITAYSVDNVL 254
Cdd:cd06424  76 ENNYFGLEKDQVHILKQEKVFCLIDNDAhlALDPDNTySILTKPHGHGDVHTLLYNSGLLKKWIEAGYKWLVFFQDTNAL 155

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 19113624 255 VLPVDPVFIGMATTKKLEVATKTVEKIdPAEKVGLL 290
Cdd:cd06424 156 AFKAIPAVLGVSATKSLDMNSLTVPRK-PKEAIGAL 190
PLN02830 PLN02830
UDP-sugar pyrophosphorylase
 2-273 1.57e-17

UDP-sugar pyrophosphorylase


Pssm-ID: 215444  Cd Length: 615  Bit Score: 85.12  E-value: 1.57e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113624    2 DDKELFDRSIfeETNQLHLYDQLNYLKKNDLQKfRKLLNQVQQLDLR---SLWLKYRNAK---ATSQENRK----LSPS- 70
Cdd:PLN02830  26 DQRALVRRLL--ELGQSHLFEHWPEPGVDDDDK-RRLLEQVARLDESypgGLAAYVSNAKellADSKEGVNpfegWTPSv 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113624   71 ---EVgpLSIVDTSDSSWWRTGLREIARghvAALVL-AGGQGTRLGFAGPKgcfrLGLP----NNPSIFELQAQKIkksL 142
Cdd:PLN02830 103 pegEV--LEYGSEEFVELEEAGLREAGN---AAFVLvAGGLGERLGYSGIK----VALPtetaTGTCYLQLYIESI---L 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113624  143 ALARAAFPDQEAS-ISIPWYIMVSECTSEETISFFKENDFFGIDKKDVFFFQQGVLPCL-DISGRVLFESDS--SLAWAP 218
Cdd:PLN02830 171 ALQERAKKRKAKKgRKIPLVIMTSDDTHARTLKLLERNDYFGMDPDQVTLLKQEKVACLmDNDARLALDPNDpyKIQTKP 250

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 19113624  219 NGNGGIYEALLSSGALNDMNRRGILHITAYSVDNVLVLPVDPVFIGMATTKKLEV 273
Cdd:PLN02830 251 HGHGDVHALLYSSGLLDKWLSAGKKWVVFFQDTNGLVFKAIPAALGVSATKGFDM 305
UGPase_euk cd00897
Eukaryotic UGPase catalyses the synthesis of UDP-Glucose; UGPase (UDP-Glucose ...
 99-252 2.15e-06

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: 49.17  E-value: 2.15e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113624  99 AALVLAGGQGTRLGFAGPKGCfrLGLPNNPSIFELQAQKIKKSlalaraafpDQEASISIPWYIMVSECTSEETISFFKE 178
Cdd:cd00897   5 VVLKLNGGLGTSMGCTGPKSL--IEVRDGKTFLDLTVQQIEHL---------NKTYGVDVPLVLMNSFNTDEDTKKILKK 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113624 179 ndfFGIDKKDVFFFQQGVLPcldisgRVLFES---------DSSLAWAPNGNGGIYEALLSSGALNDMNRRGILHITAYS 249
Cdd:cd00897  74 ---YAGVNVDIHTFNQSRYP------RISKETllpvpswadSPDEEWYPPGHGDIFESLYNSGLLDTLLAQGKEYLFVSN 144


                ...
gi 19113624 250 VDN 252
Cdd:cd00897 145 IDN 147
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 98-117 5.51e-03

CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; 4-diphosphocytidyl-2-methyl-D-erythritol synthase (CDP-ME), also called 2C-methyl-d-erythritol 4-phosphate cytidylyltransferase catalyzes the third step in the alternative (non-mevalonate) pathway of Isopentenyl diphosphate (IPP) biosynthesis: the formation of 4-diphosphocytidyl-2C-methyl-D-erythritol from CTP and 2C-methyl-D-erythritol 4-phosphate. This mevalonate independent pathway that utilizes pyruvate and glyceraldehydes 3-phosphate as starting materials for production of IPP occurs in a variety of bacteria, archaea and plant cells, but is absent in mammals. Thus, CDP-ME synthetase is an attractive targets for the structure-based design of selective antibacterial, herbicidal and antimalarial drugs.


Pssm-ID: 133009 [Multi-domain]  Cd Length: 218  Bit Score: 38.27  E-value: 5.51e-03
                        10        20
                ....*....|....*....|
gi 19113624  98 VAALVLAGGQGTRLGFAGPK 117
Cdd:cd02516   1 VAAIILAAGSGSRMGADIPK 20
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 98-123 7.51e-03

MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme molybdopterin-guanine dinucleotide biosynthesis protein A (MobA). All mononuclear molybdoenzymes bind molybdenum in complex with an organic cofactor termed molybdopterin (MPT). In many bacteria, including Escherichia coli, molybdopterin can be further modified by attachment of a GMP group to the terminal phosphate of molybdopterin to form molybdopterin guanine dinucleotide (MGD). This GMP attachment step is catalyzed by MobA, by linking a guanosine 5'-phosphate to MPT forming molybdopterin guanine dinucleotide. This reaction requires GTP, MgCl2, and the MPT form of the cofactor. It is a reaction unique to prokaryotes, and therefore may represent a potential drug target.


Pssm-ID: 133000 [Multi-domain]  Cd Length: 181  Bit Score: 37.56  E-value: 7.51e-03
                        10        20
                ....*....|....*....|....*.
gi 19113624  98 VAALVLAGGQGTRLGfaGPKGCFRLG 123
Cdd:cd02503   1 ITGVILAGGKSRRMG--GDKALLELG 24
 
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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