|
Name |
Accession |
Description |
Interval |
E-value |
| Glyco_hydro_47 |
pfam01532 |
Glycosyl hydrolase family 47; Members of this family are alpha-mannosidases that catalyze the ... |
658-1097 |
0e+00 |
|
Glycosyl hydrolase family 47; Members of this family are alpha-mannosidases that catalyze the hydrolysis of the terminal 1,2-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man(9)(GlcNAc)(2).
Pssm-ID: 460241 Cd Length: 453 Bit Score: 676.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 658 AFRHAWKGYKDFAWGHDELKPLSKSYSEWF-GLGLTLIDALDTLWILGLKEEFEEARKWVANDLIFDKNV-DVNLFESTI 735
Cdd:pfam01532 1 AFLHAWDGYKKYAWGHDELRPISGGGNDTFgGWGATIVDSLDTLIIMGLTDEFEEAVDWVEKTLDFDKDStEVSVFETTI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 736 RILGGLLSTYHLS--GDSLFLEKAKDIGNRLMPAFKTPSKIPYSDVNIGRGTAHP-PRWTSDSTVAEVTSIQLEFRELSR 812
Cdd:pfam01532 81 RYLGGLLSAYDLSgdGDDVLLEKAVDLADRLLPAFDTPTGIPYPRVNLKTGKGGNgHVAGGASSLAEAGTLQLEFTRLSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 813 LTGDEKFQKAVDEVMKHVH--TLSGKNDGLVPMFINTNSGQFTHlGVYTLGARADSYYEYLLKQWIQGGKKENELLEDYM 890
Cdd:pfam01532 161 LTGDPKYEDLAQKIMDVLWknQSRTPLPGLVPIYIDPDTGKFVG-SNIGLGARGDSYYEYLLKQYLLTGGTDPEYRDMYE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 891 RAIEGVKKHLLQR-SEPKKLTFVGEL---AHGHFSAKMDHLVCFLPGTLALGAHNGLP-ADHMKLAETLIETCYQMYAQV 965
Cdd:pfam01532 240 EAMDAIKKHLLFRpSTPSDLLFIGELdsgGGGKLSPKMDHLSCFAGGMLALGATLGLPrEGDLELAEKLTEGCYKTYDST 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 966 ETGLSPEIVHFNLHAQKGH-----RDVEIKPADRHNLLRPETVESLFYMYRFTGDKKYQDWGWEILQNFNRYTRVPtGGY 1040
Cdd:pfam01532 320 PTGLGPEIFYFDPCDEDCPwdedkWDFYVKIEDPHYLLRPETIESLFYLYRATGDPKYREWGWEIFQAIEKYTRTE-CGY 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1832439758 1041 TSINNVQNPsNPEPRDKMESFFLGETLKYMFLLFSDDiDLINLDKYIFNTEAHPLPI 1097
Cdd:pfam01532 399 SGLQDVTSP-PGEKEDNMESFWLAETLKYLYLLFSDD-DLLSLDEWVFNTEAHPLPV 453
|
|
| PTZ00470 |
PTZ00470 |
glycoside hydrolase family 47 protein; Provisional |
619-1097 |
0e+00 |
|
glycoside hydrolase family 47 protein; Provisional
Pssm-ID: 240427 Cd Length: 522 Bit Score: 614.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 619 QSTEPPSSKITEPEKHSSVEAEYQKEAVPINERQLAVIEAFRHAWKGYKDFAWGHDELKPLSKSYSEWFGLGLTLIDALD 698
Cdd:PTZ00470 40 QASKLPRGKKKQENPFNKIDEVYYQNEKLNIKRRESVREAMKHAWEGYKEYAWGHDELRPLTKRHHEWFGLGLTIIDSLD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 699 TLWILGLKEEFEEARKWVANDLIFDKNVD--VNLFESTIRILGGLLSTYHLSGDSLFLEKAKDIGNRLMPAFKTPSKIPY 776
Cdd:PTZ00470 120 TLKIMGLKKEYKEGRDWVANNLKQSKDTGlgVSVFETTIRVLGGLLSAYDLTGDEMYLEKAREIADRLLPAFNEDTGFPA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 777 SDVNIGRGTAHPPRWT-SDSTVAEVTSIQLEFRELSRLTGDEKFQKAVDEVMKHVHTLSGKNDGLVPMFINTNSGQFTHl 855
Cdd:PTZ00470 200 SEINLATGRKSYPGWAgGCSILSEVGTLQLEFNYLSEITGDPKYAEYVDKVMDALFSMKPAINGLYPIFLNPDAGRFCG- 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 856 GVYTLGARADSYYEYLLKQWIQGGKKENELLEDYMRAIEGVKKHLLQRSePKKLTFVGELAHGHFSAKMDHLVCFLPGTL 935
Cdd:PTZ00470 279 NHISLGALGDSYYEYLLKQWLYTNGREERYRRLFVESAKGIIEHLYKRS-PKGLTYIAEMDGGSLTNKMEHLACFAGGMF 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 936 ALGAHNGLPAD------HMKLAETLIETCYQMYAQVETGLSPEIVHFNlhaqKGHRDVEIKPADRHNLLRPETVESLFYM 1009
Cdd:PTZ00470 358 ALGAAINITPDdeksarYMEVGEEVTKTCYETYATSPTGLGPEIFHFD----PNSGDISPNVHDSHYILRPETVESIFIL 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 1010 YRFTGDKKYQDWGWEILQNFNRYTRVPTgGYTSINNVQNpSNPEPRDKMESFFLGETLKYMFLLFSDDiDLINLDKYIFN 1089
Cdd:PTZ00470 434 YRLTGDPKYREWAWKIFQAIEKHCKTEN-GYSGLKNVLT-VHPQQDDFQESFFLAETLKYLYLLFQPD-HVIPLDKYVFN 510
|
....*...
gi 1832439758 1090 TEAHPLPI 1097
Cdd:PTZ00470 511 TEAHPIPI 518
|
|
| UDPGlcNAc_PPase |
cd04193 |
UDPGlcNAc pyrophosphorylase catalayzes the synthesis of UDPGlcNAc; UDP-N-acetylglucosamine ... |
87-409 |
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: 574.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 87 QRWEAEGLHQISQNKVAVLLLAGGQGTRLGVSYPKGMYNVGLPSGKNLYQIQAERIRKVEQLAGKRHHCKCAIPWYIMTS 166
Cdd:cd04193 1 KEWEEAGLKAIAEGKVAVLLLAGGQGTRLGFDGPKGMFPVGLPSKKSLFQLQAERILKLQELAGEASGKKVPIPWYIMTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 167 EFTLGPTEEFFVQHNYFNLDRCNVVMFEQRMLPAVTFDGKAILEEKGKIAMAPDGNGGLYRALMDNKILDDMKQRGIQYV 246
Cdd:cd04193 81 EATHEETRKFFKENNYFGLDPEQVHFFQQGMLPCVDFDGKILLEEKGKIAMAPNGNGGLYKALQTAGILEDMKKRGIKYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 247 HVYCVDNILVKMADPVFIGFCISKGADCGAKVVEKAYPTEPVGVVCCVDGVYQVVEYSEISLETAQQQRPEGGLMFSAGN 326
Cdd:cd04193 161 HVYSVDNILVKVADPVFIGFCISKGADVGAKVVRKRYPTEKVGVVVLVDGKPQVVEYSEISDELAEKRDADGELQYNAGN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 327 ICNHFFTVEFLELVAQKWESQLKHHVAIKKVPYIDKEGNLVKPLKPNGIKLEKFVFDVFQFSKNFVAFEVLREEEFSPLK 406
Cdd:cd04193 241 IANHFFSLDFLEKAAEMEEPSLPYHIAKKKIPYVDLEGGLVKPDEPNGIKLELFIFDVFPFAKNFVCLEVDREEEFSPLK 320
|
...
gi 1832439758 407 NAD 409
Cdd:cd04193 321 NAD 323
|
|
| PLN02435 |
PLN02435 |
probable UDP-N-acetylglucosamine pyrophosphorylase |
1-480 |
1.54e-120 |
|
probable UDP-N-acetylglucosamine pyrophosphorylase
Pssm-ID: 215238 Cd Length: 493 Bit Score: 379.99 E-value: 1.54e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 1 MDPPEEVRARLERCGQGHLLRFWAELDPAQRRALLAALPP-GLGEHCRLAAAAGARQRGPperlDGRMEPLPAELLGSAR 79
Cdd:PLN02435 19 AAPPQALLERLKDYGQEDAFALWDELSPEERDLLVRDIESlDLPRIDRIIRCSLRSQGLP----VPAIEPVPENSVSTVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 80 RSGPAALQRWEAEGLHQISQNKVAVLLLAGGQGTRLGVSYPKGMYNVGLPSGKNLYQIQAERIRKVEQLAGKRHHCK--- 156
Cdd:PLN02435 95 ERTPEDRERWWKMGLKAISEGKLAVVLLSGGQGTRLGSSDPKGCFNIGLPSGKSLFQLQAERILCVQRLAAQASSEGpgr 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 157 -CAIPWYIMTSEFTLGPTEEFFVQHNYFNLDRCNVVMFEQRMLPAVTFDGKAILEEKGKIAMAPDGNGGLYRALMDNKIL 235
Cdd:PLN02435 175 pVTIHWYIMTSPFTDEATRKFFESHKYFGLEADQVTFFQQGTLPCVSKDGKFIMETPFKVAKAPDGNGGVYAALKSSRLL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 236 DDMKQRGIQYVHVYCVDNILVKMADPVFIGFCISKGADCGAKVVEKAYPTEPVGVVCCVDGV--YQVVEYSEI--SLETA 311
Cdd:PLN02435 255 EDMASRGIKYVDCYGVDNALVRVADPTFLGYFIDKGVASAAKVVRKAYPQEKVGVFVRRGKGgpLTVVEYSELdqAMASA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 312 QQQRpEGGLMFSAGNICNHFFTVEFLELVAQKWESQLKHHVAIKKVPYIDkeGNLVkplkpnGIKLEKFVFDVFQFSKNF 391
Cdd:PLN02435 335 INQQ-TGRLRYCWSNVCLHMFTLDFLNQVANGLEKDSIYHLAEKKIPSIH--GYTM------GLKLEQFIFDAFPYAPST 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 392 VAFEVLREEEFSPLKNADTADKDTPTTARQALLAQHYRWALKAGAkFVDENgcrIPekLSLSGTedppavcEISPLVSYF 471
Cdd:PLN02435 406 ALFEVLREEEFAPVKNANGSNFDTPESARLLVLRLHTRWVVAAGG-FLTHS---VP--LYATGV-------EVSPLCSYA 472
|
....*....
gi 1832439758 472 GEKWKQLSR 480
Cdd:PLN02435 473 GENLEAICR 481
|
|
| QRI1 |
COG4284 |
UDP-N-acetylglucosamine pyrophosphorylase [Carbohydrate transport and metabolism]; |
10-416 |
4.89e-113 |
|
UDP-N-acetylglucosamine pyrophosphorylase [Carbohydrate transport and metabolism];
Pssm-ID: 443425 Cd Length: 402 Bit Score: 356.50 E-value: 4.89e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 10 RLERCGQGHLLRFWAELDPAQRRALLAALPP---GLGEHC-RLAAAAGARQRGPPERldgRMEPLPAELLgSARRSGPAA 85
Cdd:COG4284 4 KLEPHGQEHLLRFWDELSEAQQKMLEAQIEEidiDVFQHLyRQLVLAEGATGLIPES---DIEPAPVTDL-PLTDLDEVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 86 LQRWEAEGLHQISQNKVAVLLLAGGQGTRLGVSYPKGMYNVGLPSGKNLYQIQAERIRKVEQLAGKRhhckcaIPWYIMT 165
Cdd:COG4284 80 RDRAEEAGEEALRAGKVAVILLAGGQGTRLGFDGPKGLLPVRPVKGKSLFDLIAEQVLAARRRYGVP------LPLYIMT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 166 SEFTLGPTEEFFVQHNYFNLDRCNVVMFEQRMLPAV-TFDGKAILEEKGKIAMAPDGNGGLYRALMDNKILDDMKQRGIQ 244
Cdd:COG4284 154 SFRTHEDTLAFLEEHDYFGLDGLPVHFFLQGMEPALdADLGPVLLPADPELELCPPGHGGIYTALLASGLLDKLLERGIR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 245 YVHVYCVDNILVKMADPVFIGFCISKGADCGAKVVEKAYPTEPVGVVCCVDGVYQVVEYSEISLETAQQQRpeGGLMFSA 324
Cdd:COG4284 234 YLFVSNVDNPLGAVPDPAFAGWHAASGAPFTAKVVRRTPPDEKVGHLARVDGRLILREYSQLPDEEAEAFT--GELRHPY 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 325 GNICNHFFTVEFLELVAQKWESQLKHHVAIKKVPYIDKEGnlvKPLKPNGIKLEKFVFDVFQFSKNFVAFEVLREEEFSP 404
Cdd:COG4284 312 GNINNHWFDLDFLKRLLDERGLGLPLHRAEKKVDPLDESG---KPTSPNVIKFETFMFDAIPLFDGAVAIEVDREERFAP 388
|
410
....*....|..
gi 1832439758 405 LKNadTADKDTP 416
Cdd:COG4284 389 VKN--TNGSDSP 398
|
|
| UDPGP |
pfam01704 |
UTP--glucose-1-phosphate uridylyltransferase; This family consists of UTP--glucose-1-phosphate ... |
55-447 |
1.28e-63 |
|
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: 222.00 E-value: 1.28e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 55 RQRGPPERLD-GRMEPLPAELLGSARRsgpaaLQR--WEAEGLhqisQNKVAVLLLAGGQGTRLGVSYPKGMYNVGlpSG 131
Cdd:pfam01704 13 SEKGKQEKIDwDKIKPPPEEEIVDYED-----LQEpeEEIKEL----LNKLAVLKLNGGLGTSMGCVGPKSLIEVR--DG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 132 KNLYQIQaerirkVEQLAGKRHHCKCAIPWYIMTSEFTLGPTEEFFvqHNYFNlDRCNVVMFEQRMLPAVTFDGKAILEE 211
Cdd:pfam01704 82 LTFLDLI------VQQIEHLNKKYNVDVPLVLMNSFNTDEDTKKII--RKYKG-HKVDILTFNQSRYPRIDKDTLLPVPK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 212 KGKI---AMAPDGNGGLYRALMDNKILDDMKQRGIQYVHVYCVDNiLVKMADPVFIGFCISKGADCGAKVVEKAYPTEPV 288
Cdd:pfam01704 153 SADSdeeEWYPPGHGDLYESLYNSGLLDKLLAEGKEYLFVSNIDN-LGATVDLNILNYMVDNGAEFLMEVTDKTRADVKG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 289 GVVCCVDGVYQVVEYSEI-SLETAQQQRPEGGLMFSAGNIcnhFFTVEFLELVAQkwESQLKHHVAIKKvPYIDKEGNLV 367
Cdd:pfam01704 232 GTLIEYDGKLRLLEIAQVpKEHVDEFKSIKKFKIFNTNNI---WINLKALKRVVE--EGELQLEIIVNK-KTLDNGENVI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 368 KPLKPNGIKLEKFvfdvfqfsKNFVAFEVLReEEFSPLKNADtadkdtpttarQALLAQHYRWALKAGA----------- 436
Cdd:pfam01704 306 QLETAVGAAIKNF--------KNAIGINVPR-SRFLPVKTTS-----------DLLLVMSDLYVLNHGSlimnpkrmfgt 365
|
410 420
....*....|....*....|.
gi 1832439758 437 ----------KFVDENGCRIP 447
Cdd:pfam01704 366 ppvvllgdhfKKVDEFLKRFP 386
|
|
| LanC_SerThrkinase |
cd04791 |
Lanthionine synthetase C-like domain associated with serine/threonine kinases; Some members of ... |
699-829 |
6.83e-03 |
|
Lanthionine synthetase C-like domain associated with serine/threonine kinases; Some members of this subgroup lack the zinc binding site and the active site residues, and therefore are most likely inactive. The function of this domain is unknown.
Pssm-ID: 271199 [Multi-domain] Cd Length: 327 Bit Score: 39.95 E-value: 6.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 699 TLWILGLKEEFEEARKWVANDLIFDKNVDvnlfestirILGGL-------LSTYHLSGDSLFLEKAKDIGNRLMPAFK-- 769
Cdd:cd04791 55 VLYELGRREEAERLLDRALALPLDSLDPS---------LYSGLagiglalLHLARATGDPEFLERAARIAERLAARLRed 125
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 770 TPSKIPYSDVNIGRGTAHpprwtSDSTVAevtsiqLEFRELSRLTGDEKFQKAVDEVMKH 829
Cdd:cd04791 126 DPGVYWNDAGAVRAGLLH-----GWSGIA------LFLLRLYEATGDPAYLDLAERALRK 174
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Glyco_hydro_47 |
pfam01532 |
Glycosyl hydrolase family 47; Members of this family are alpha-mannosidases that catalyze the ... |
658-1097 |
0e+00 |
|
Glycosyl hydrolase family 47; Members of this family are alpha-mannosidases that catalyze the hydrolysis of the terminal 1,2-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man(9)(GlcNAc)(2).
Pssm-ID: 460241 Cd Length: 453 Bit Score: 676.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 658 AFRHAWKGYKDFAWGHDELKPLSKSYSEWF-GLGLTLIDALDTLWILGLKEEFEEARKWVANDLIFDKNV-DVNLFESTI 735
Cdd:pfam01532 1 AFLHAWDGYKKYAWGHDELRPISGGGNDTFgGWGATIVDSLDTLIIMGLTDEFEEAVDWVEKTLDFDKDStEVSVFETTI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 736 RILGGLLSTYHLS--GDSLFLEKAKDIGNRLMPAFKTPSKIPYSDVNIGRGTAHP-PRWTSDSTVAEVTSIQLEFRELSR 812
Cdd:pfam01532 81 RYLGGLLSAYDLSgdGDDVLLEKAVDLADRLLPAFDTPTGIPYPRVNLKTGKGGNgHVAGGASSLAEAGTLQLEFTRLSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 813 LTGDEKFQKAVDEVMKHVH--TLSGKNDGLVPMFINTNSGQFTHlGVYTLGARADSYYEYLLKQWIQGGKKENELLEDYM 890
Cdd:pfam01532 161 LTGDPKYEDLAQKIMDVLWknQSRTPLPGLVPIYIDPDTGKFVG-SNIGLGARGDSYYEYLLKQYLLTGGTDPEYRDMYE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 891 RAIEGVKKHLLQR-SEPKKLTFVGEL---AHGHFSAKMDHLVCFLPGTLALGAHNGLP-ADHMKLAETLIETCYQMYAQV 965
Cdd:pfam01532 240 EAMDAIKKHLLFRpSTPSDLLFIGELdsgGGGKLSPKMDHLSCFAGGMLALGATLGLPrEGDLELAEKLTEGCYKTYDST 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 966 ETGLSPEIVHFNLHAQKGH-----RDVEIKPADRHNLLRPETVESLFYMYRFTGDKKYQDWGWEILQNFNRYTRVPtGGY 1040
Cdd:pfam01532 320 PTGLGPEIFYFDPCDEDCPwdedkWDFYVKIEDPHYLLRPETIESLFYLYRATGDPKYREWGWEIFQAIEKYTRTE-CGY 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1832439758 1041 TSINNVQNPsNPEPRDKMESFFLGETLKYMFLLFSDDiDLINLDKYIFNTEAHPLPI 1097
Cdd:pfam01532 399 SGLQDVTSP-PGEKEDNMESFWLAETLKYLYLLFSDD-DLLSLDEWVFNTEAHPLPV 453
|
|
| PTZ00470 |
PTZ00470 |
glycoside hydrolase family 47 protein; Provisional |
619-1097 |
0e+00 |
|
glycoside hydrolase family 47 protein; Provisional
Pssm-ID: 240427 Cd Length: 522 Bit Score: 614.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 619 QSTEPPSSKITEPEKHSSVEAEYQKEAVPINERQLAVIEAFRHAWKGYKDFAWGHDELKPLSKSYSEWFGLGLTLIDALD 698
Cdd:PTZ00470 40 QASKLPRGKKKQENPFNKIDEVYYQNEKLNIKRRESVREAMKHAWEGYKEYAWGHDELRPLTKRHHEWFGLGLTIIDSLD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 699 TLWILGLKEEFEEARKWVANDLIFDKNVD--VNLFESTIRILGGLLSTYHLSGDSLFLEKAKDIGNRLMPAFKTPSKIPY 776
Cdd:PTZ00470 120 TLKIMGLKKEYKEGRDWVANNLKQSKDTGlgVSVFETTIRVLGGLLSAYDLTGDEMYLEKAREIADRLLPAFNEDTGFPA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 777 SDVNIGRGTAHPPRWT-SDSTVAEVTSIQLEFRELSRLTGDEKFQKAVDEVMKHVHTLSGKNDGLVPMFINTNSGQFTHl 855
Cdd:PTZ00470 200 SEINLATGRKSYPGWAgGCSILSEVGTLQLEFNYLSEITGDPKYAEYVDKVMDALFSMKPAINGLYPIFLNPDAGRFCG- 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 856 GVYTLGARADSYYEYLLKQWIQGGKKENELLEDYMRAIEGVKKHLLQRSePKKLTFVGELAHGHFSAKMDHLVCFLPGTL 935
Cdd:PTZ00470 279 NHISLGALGDSYYEYLLKQWLYTNGREERYRRLFVESAKGIIEHLYKRS-PKGLTYIAEMDGGSLTNKMEHLACFAGGMF 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 936 ALGAHNGLPAD------HMKLAETLIETCYQMYAQVETGLSPEIVHFNlhaqKGHRDVEIKPADRHNLLRPETVESLFYM 1009
Cdd:PTZ00470 358 ALGAAINITPDdeksarYMEVGEEVTKTCYETYATSPTGLGPEIFHFD----PNSGDISPNVHDSHYILRPETVESIFIL 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 1010 YRFTGDKKYQDWGWEILQNFNRYTRVPTgGYTSINNVQNpSNPEPRDKMESFFLGETLKYMFLLFSDDiDLINLDKYIFN 1089
Cdd:PTZ00470 434 YRLTGDPKYREWAWKIFQAIEKHCKTEN-GYSGLKNVLT-VHPQQDDFQESFFLAETLKYLYLLFQPD-HVIPLDKYVFN 510
|
....*...
gi 1832439758 1090 TEAHPLPI 1097
Cdd:PTZ00470 511 TEAHPIPI 518
|
|
| UDPGlcNAc_PPase |
cd04193 |
UDPGlcNAc pyrophosphorylase catalayzes the synthesis of UDPGlcNAc; UDP-N-acetylglucosamine ... |
87-409 |
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: 574.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 87 QRWEAEGLHQISQNKVAVLLLAGGQGTRLGVSYPKGMYNVGLPSGKNLYQIQAERIRKVEQLAGKRHHCKCAIPWYIMTS 166
Cdd:cd04193 1 KEWEEAGLKAIAEGKVAVLLLAGGQGTRLGFDGPKGMFPVGLPSKKSLFQLQAERILKLQELAGEASGKKVPIPWYIMTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 167 EFTLGPTEEFFVQHNYFNLDRCNVVMFEQRMLPAVTFDGKAILEEKGKIAMAPDGNGGLYRALMDNKILDDMKQRGIQYV 246
Cdd:cd04193 81 EATHEETRKFFKENNYFGLDPEQVHFFQQGMLPCVDFDGKILLEEKGKIAMAPNGNGGLYKALQTAGILEDMKKRGIKYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 247 HVYCVDNILVKMADPVFIGFCISKGADCGAKVVEKAYPTEPVGVVCCVDGVYQVVEYSEISLETAQQQRPEGGLMFSAGN 326
Cdd:cd04193 161 HVYSVDNILVKVADPVFIGFCISKGADVGAKVVRKRYPTEKVGVVVLVDGKPQVVEYSEISDELAEKRDADGELQYNAGN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 327 ICNHFFTVEFLELVAQKWESQLKHHVAIKKVPYIDKEGNLVKPLKPNGIKLEKFVFDVFQFSKNFVAFEVLREEEFSPLK 406
Cdd:cd04193 241 IANHFFSLDFLEKAAEMEEPSLPYHIAKKKIPYVDLEGGLVKPDEPNGIKLELFIFDVFPFAKNFVCLEVDREEEFSPLK 320
|
...
gi 1832439758 407 NAD 409
Cdd:cd04193 321 NAD 323
|
|
| PLN02435 |
PLN02435 |
probable UDP-N-acetylglucosamine pyrophosphorylase |
1-480 |
1.54e-120 |
|
probable UDP-N-acetylglucosamine pyrophosphorylase
Pssm-ID: 215238 Cd Length: 493 Bit Score: 379.99 E-value: 1.54e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 1 MDPPEEVRARLERCGQGHLLRFWAELDPAQRRALLAALPP-GLGEHCRLAAAAGARQRGPperlDGRMEPLPAELLGSAR 79
Cdd:PLN02435 19 AAPPQALLERLKDYGQEDAFALWDELSPEERDLLVRDIESlDLPRIDRIIRCSLRSQGLP----VPAIEPVPENSVSTVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 80 RSGPAALQRWEAEGLHQISQNKVAVLLLAGGQGTRLGVSYPKGMYNVGLPSGKNLYQIQAERIRKVEQLAGKRHHCK--- 156
Cdd:PLN02435 95 ERTPEDRERWWKMGLKAISEGKLAVVLLSGGQGTRLGSSDPKGCFNIGLPSGKSLFQLQAERILCVQRLAAQASSEGpgr 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 157 -CAIPWYIMTSEFTLGPTEEFFVQHNYFNLDRCNVVMFEQRMLPAVTFDGKAILEEKGKIAMAPDGNGGLYRALMDNKIL 235
Cdd:PLN02435 175 pVTIHWYIMTSPFTDEATRKFFESHKYFGLEADQVTFFQQGTLPCVSKDGKFIMETPFKVAKAPDGNGGVYAALKSSRLL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 236 DDMKQRGIQYVHVYCVDNILVKMADPVFIGFCISKGADCGAKVVEKAYPTEPVGVVCCVDGV--YQVVEYSEI--SLETA 311
Cdd:PLN02435 255 EDMASRGIKYVDCYGVDNALVRVADPTFLGYFIDKGVASAAKVVRKAYPQEKVGVFVRRGKGgpLTVVEYSELdqAMASA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 312 QQQRpEGGLMFSAGNICNHFFTVEFLELVAQKWESQLKHHVAIKKVPYIDkeGNLVkplkpnGIKLEKFVFDVFQFSKNF 391
Cdd:PLN02435 335 INQQ-TGRLRYCWSNVCLHMFTLDFLNQVANGLEKDSIYHLAEKKIPSIH--GYTM------GLKLEQFIFDAFPYAPST 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 392 VAFEVLREEEFSPLKNADTADKDTPTTARQALLAQHYRWALKAGAkFVDENgcrIPekLSLSGTedppavcEISPLVSYF 471
Cdd:PLN02435 406 ALFEVLREEEFAPVKNANGSNFDTPESARLLVLRLHTRWVVAAGG-FLTHS---VP--LYATGV-------EVSPLCSYA 472
|
....*....
gi 1832439758 472 GEKWKQLSR 480
Cdd:PLN02435 473 GENLEAICR 481
|
|
| QRI1 |
COG4284 |
UDP-N-acetylglucosamine pyrophosphorylase [Carbohydrate transport and metabolism]; |
10-416 |
4.89e-113 |
|
UDP-N-acetylglucosamine pyrophosphorylase [Carbohydrate transport and metabolism];
Pssm-ID: 443425 Cd Length: 402 Bit Score: 356.50 E-value: 4.89e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 10 RLERCGQGHLLRFWAELDPAQRRALLAALPP---GLGEHC-RLAAAAGARQRGPPERldgRMEPLPAELLgSARRSGPAA 85
Cdd:COG4284 4 KLEPHGQEHLLRFWDELSEAQQKMLEAQIEEidiDVFQHLyRQLVLAEGATGLIPES---DIEPAPVTDL-PLTDLDEVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 86 LQRWEAEGLHQISQNKVAVLLLAGGQGTRLGVSYPKGMYNVGLPSGKNLYQIQAERIRKVEQLAGKRhhckcaIPWYIMT 165
Cdd:COG4284 80 RDRAEEAGEEALRAGKVAVILLAGGQGTRLGFDGPKGLLPVRPVKGKSLFDLIAEQVLAARRRYGVP------LPLYIMT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 166 SEFTLGPTEEFFVQHNYFNLDRCNVVMFEQRMLPAV-TFDGKAILEEKGKIAMAPDGNGGLYRALMDNKILDDMKQRGIQ 244
Cdd:COG4284 154 SFRTHEDTLAFLEEHDYFGLDGLPVHFFLQGMEPALdADLGPVLLPADPELELCPPGHGGIYTALLASGLLDKLLERGIR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 245 YVHVYCVDNILVKMADPVFIGFCISKGADCGAKVVEKAYPTEPVGVVCCVDGVYQVVEYSEISLETAQQQRpeGGLMFSA 324
Cdd:COG4284 234 YLFVSNVDNPLGAVPDPAFAGWHAASGAPFTAKVVRRTPPDEKVGHLARVDGRLILREYSQLPDEEAEAFT--GELRHPY 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 325 GNICNHFFTVEFLELVAQKWESQLKHHVAIKKVPYIDKEGnlvKPLKPNGIKLEKFVFDVFQFSKNFVAFEVLREEEFSP 404
Cdd:COG4284 312 GNINNHWFDLDFLKRLLDERGLGLPLHRAEKKVDPLDESG---KPTSPNVIKFETFMFDAIPLFDGAVAIEVDREERFAP 388
|
410
....*....|..
gi 1832439758 405 LKNadTADKDTP 416
Cdd:COG4284 389 VKN--TNGSDSP 398
|
|
| PTZ00339 |
PTZ00339 |
UDP-N-acetylglucosamine pyrophosphorylase; Provisional |
90-480 |
1.61e-94 |
|
UDP-N-acetylglucosamine pyrophosphorylase; Provisional
Pssm-ID: 240368 Cd Length: 482 Bit Score: 310.13 E-value: 1.61e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 90 EAEGLHQISQNKVAVLLLAGGQGTRLGVSYPKGMYNVGLPSGKNLYQIQAERIRKVEQLAGKRH--HCKCAIPWYIMTSE 167
Cdd:PTZ00339 95 KESGLEIIKKGEVAVLILAGGLGTRLGSDKPKGLLECTPVKKKTLFQFHCEKVRRLEEMAVAVSggGDDPTIYILVLTSS 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 168 FTLGPTEEFFVQHNYFNLDRCNVVMFEQRMLPAVT-FDGKAILEEKGKIAMAPDGNGGLYRALMDNKILDDMKQRGIQYV 246
Cdd:PTZ00339 175 FNHDQTRQFLEENNFFGLDKEQVIFFKQSSLPCYDeNTGRFIMSSQGSLCTAPGGNGDVFKALAKCSELMDIVRKGIKYV 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 247 HVYCVDNILVKMADPVFIGFCISKGADCGAKVVEKAYPTEPVGVVCCVDGVYQVVEYSEIS-LETAQQQRPEGGLMFSAG 325
Cdd:PTZ00339 255 QVISIDNILAKVLDPEFIGLASSFPAHDVLNKCVKREDDESVGVFCLKDYEWQVVEYTEINeRILNNDELLTGELAFNYG 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 326 NICNHFFTVEFL-ELVAQKWESQLKHHVAIKKVPYIDKEGNlvkplKPNGIKLEKFVFDVFQFSKNFVAFEVLREEEFSP 404
Cdd:PTZ00339 335 NICSHIFSLDFLkKVAANRLYESTPYHAARKKIPYINGPTD-----KTMGIKLEAFIFDIFRYAKNVLILEVDREDEFAP 409
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1832439758 405 LKNADTADKDTPTTARQALLAQHYRWALKAGAKFVDenGCRIPEKLslsgtedppavCEISPLVSYFGEKWKQLSR 480
Cdd:PTZ00339 410 IKNADGAAADTILNAQKLLLSLHTRWLEAALETVAG--NPREGLNL-----------CEISPLVSYGGEGLFQYPG 472
|
|
| UGPase_euk_like |
cd04180 |
Eukaryotic UGPase-like includes UDPase and UDPGlcNAc pyrophosphorylase enzymes; This family ... |
102-407 |
4.45e-80 |
|
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: 262.88 E-value: 4.45e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 102 VAVLLLAGGQGTRLGVSYPKGMYNVGLPSGKNLYQIQAERIRKVEQLAGKrhhcKCAIPWYIMTSEFTLGPTEEFFVQHN 181
Cdd:cd04180 1 VAVVLLAGGLGTRLGKDGPKSSTDVGLPSGQCFLQLIGEKILTLQEIDLY----SCKIPEQLMNSKYTHEKTQCYFEKIN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 182 yfnLDRCNVVMFEQRMLPAVTFDGKAILEEKGKIAMAPDGNGGLYRALMDNKILDDMKQRGIQYVHVYCVDNILVKMADP 261
Cdd:cd04180 77 ---QKNSYVITFMQGKLPLKNDDDARDPHNKTKCHLFPCGHGDVVLALIHSGHLNKLLEKGYRYIHFIGVDNLLVKVADP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 262 VFIGFCISKGADCGAKVVEKAYPTEPVGVVCCVDG-VYQVVEYSEISLETAQQQRP------EGGLMFSAGNICNHFFTV 334
Cdd:cd04180 154 LFIGIAIQNRKAINQKVVPKTRNEESGGYRIANINgRVQLLEYDQIKKLLKQKMVNnqipkdIDDAPFFLFNTNNLINFL 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1832439758 335 eflelvaqkwesqlkhhVAIKKVpyidkegnlvkplkpngiklekfVFDVFQFSKNFVAFEVLREEEFSPLKN 407
Cdd:cd04180 234 -----------------VEFKDR-----------------------VDDIIEFTDDIVGVMVHRAEEFAPVKN 266
|
|
| UDPGP |
pfam01704 |
UTP--glucose-1-phosphate uridylyltransferase; This family consists of UTP--glucose-1-phosphate ... |
55-447 |
1.28e-63 |
|
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: 222.00 E-value: 1.28e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 55 RQRGPPERLD-GRMEPLPAELLGSARRsgpaaLQR--WEAEGLhqisQNKVAVLLLAGGQGTRLGVSYPKGMYNVGlpSG 131
Cdd:pfam01704 13 SEKGKQEKIDwDKIKPPPEEEIVDYED-----LQEpeEEIKEL----LNKLAVLKLNGGLGTSMGCVGPKSLIEVR--DG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 132 KNLYQIQaerirkVEQLAGKRHHCKCAIPWYIMTSEFTLGPTEEFFvqHNYFNlDRCNVVMFEQRMLPAVTFDGKAILEE 211
Cdd:pfam01704 82 LTFLDLI------VQQIEHLNKKYNVDVPLVLMNSFNTDEDTKKII--RKYKG-HKVDILTFNQSRYPRIDKDTLLPVPK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 212 KGKI---AMAPDGNGGLYRALMDNKILDDMKQRGIQYVHVYCVDNiLVKMADPVFIGFCISKGADCGAKVVEKAYPTEPV 288
Cdd:pfam01704 153 SADSdeeEWYPPGHGDLYESLYNSGLLDKLLAEGKEYLFVSNIDN-LGATVDLNILNYMVDNGAEFLMEVTDKTRADVKG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 289 GVVCCVDGVYQVVEYSEI-SLETAQQQRPEGGLMFSAGNIcnhFFTVEFLELVAQkwESQLKHHVAIKKvPYIDKEGNLV 367
Cdd:pfam01704 232 GTLIEYDGKLRLLEIAQVpKEHVDEFKSIKKFKIFNTNNI---WINLKALKRVVE--EGELQLEIIVNK-KTLDNGENVI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 368 KPLKPNGIKLEKFvfdvfqfsKNFVAFEVLReEEFSPLKNADtadkdtpttarQALLAQHYRWALKAGA----------- 436
Cdd:pfam01704 306 QLETAVGAAIKNF--------KNAIGINVPR-SRFLPVKTTS-----------DLLLVMSDLYVLNHGSlimnpkrmfgt 365
|
410 420
....*....|....*....|.
gi 1832439758 437 ----------KFVDENGCRIP 447
Cdd:pfam01704 366 ppvvllgdhfKKVDEFLKRFP 386
|
|
| PLN02830 |
PLN02830 |
UDP-sugar pyrophosphorylase |
9-273 |
3.03e-14 |
|
UDP-sugar pyrophosphorylase
Pssm-ID: 215444 Cd Length: 615 Bit Score: 77.03 E-value: 3.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 9 ARLERCGQGHLLRFWAE--LDPAQRRALLAAL-------PPGLGEHCRLAAAAGARQRGPPERLDGRMEPLPAellGSAR 79
Cdd:PLN02830 32 RRLLELGQSHLFEHWPEpgVDDDDKRRLLEQVarldesyPGGLAAYVSNAKELLADSKEGVNPFEGWTPSVPE---GEVL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 80 RSGPAALQRWEAEGLHQIsqNKVAVLLLAGGQGTRLGVSYPKgmynVGLPS----GKNLYQIQAERIRKVEQLA-GKRHH 154
Cdd:PLN02830 109 EYGSEEFVELEEAGLREA--GNAAFVLVAGGLGERLGYSGIK----VALPTetatGTCYLQLYIESILALQERAkKRKAK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 155 CKCAIPWYIMTSEFTLGPTEEFFVQHNYFNLDRCNVVMFEQRMLPAVTfDGKAIL----EEKGKIAMAPDGNGGLYRALM 230
Cdd:PLN02830 183 KGRKIPLVIMTSDDTHARTLKLLERNDYFGMDPDQVTLLKQEKVACLM-DNDARLaldpNDPYKIQTKPHGHGDVHALLY 261
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1832439758 231 DNKILDDMKQRGIQYVHVYCVDNILVKMADPVFIGFCISKGAD 273
Cdd:PLN02830 262 SSGLLDKWLSAGKKWVVFFQDTNGLVFKAIPAALGVSATKGFD 304
|
|
| UGGPase |
cd06424 |
UGGPase catalyzes the synthesis of UDP-Glucose/UDP-Galactose; UGGPase: UDP-Galactose/Glucose ... |
102-270 |
5.10e-11 |
|
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: 65.17 E-value: 5.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 102 VAVLLLAGGQGTRLGVSYPKgmynVGLP----SGKNLYQIQAERIRKVEQLAGKrhHCKCAIPWYIMTSEFTLGPTEEFF 177
Cdd:cd06424 1 AVFVLVAGGLGERLGYSGIK----IGLPveltTNTTYLQYYLNYIRAFQEASKK--GEKMEIPFVIMTSDDTHSKTLKLL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 178 VQHNYFNLDRCNVVMFEQRMLPAVTfDGKAIL----EEKGKIAMAPDGNGGLYRALMDNKILDDMKQRGIQYVHVYCVDN 253
Cdd:cd06424 75 EENNYFGLEKDQVHILKQEKVFCLI-DNDAHLaldpDNTYSILTKPHGHGDVHTLLYNSGLLKKWIEAGYKWLVFFQDTN 153
|
170
....*....|....*..
gi 1832439758 254 ILVKMADPVFIGFCISK 270
Cdd:cd06424 154 ALAFKAIPAVLGVSATK 170
|
|
| UGPase_euk |
cd00897 |
Eukaryotic UGPase catalyses the synthesis of UDP-Glucose; UGPase (UDP-Glucose ... |
100-261 |
1.41e-09 |
|
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: 60.72 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 100 NKVAVLLLAGGQGTRLGVSYPKGMYNVglPSGKNLYQIQaerIRKVEQLagkRHHCKCAIPWYIMTSEFTLGPTEEFFVQ 179
Cdd:cd00897 2 NKLVVLKLNGGLGTSMGCTGPKSLIEV--RDGKTFLDLT---VQQIEHL---NKTYGVDVPLVLMNSFNTDEDTKKILKK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 180 HNYFNldrCNVVMFEQRMLPAVTFDGK---AILEEKGKIAMAPDGNGGLYRALMDNKILDDMKQRGIQYVHVYCVDN--- 253
Cdd:cd00897 74 YAGVN---VDIHTFNQSRYPRISKETLlpvPSWADSPDEEWYPPGHGDIFESLYNSGLLDTLLAQGKEYLFVSNIDNlga 150
|
170
....*....|...
gi 1832439758 254 -----ILVKMADP 261
Cdd:cd00897 151 tvdlrILNHMVDN 163
|
|
| PLN02474 |
PLN02474 |
UTP--glucose-1-phosphate uridylyltransferase |
100-254 |
2.91e-06 |
|
UTP--glucose-1-phosphate uridylyltransferase
Pssm-ID: 178092 Cd Length: 469 Bit Score: 51.03 E-value: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 100 NKVAVLLLAGGQGTRLGVSYPKGMYNV--GLpSGKNLYQIQAERIRKveqlagkrhHCKCAIPWYIMTSEFTLGPTEEFF 177
Cdd:PLN02474 78 DKLVVLKLNGGLGTTMGCTGPKSVIEVrnGL-TFLDLIVIQIENLNK---------KYGCNVPLLLMNSFNTHDDTQKIV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 178 VQHNYFNLDrcnVVMFEQRMLPAVTFDGKAILEEKGKIAMA---PDGNGGLYRALMDNKILDDMKQRGIQYVHVYCVDNI 254
Cdd:PLN02474 148 EKYTNSNIE---IHTFNQSQYPRVVADDFVPWPSKGKTDKDgwyPPGHGDVFPSLMNSGKLDALLSQGKEYVFIANSDNL 224
|
|
| MobA |
COG0746 |
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ... |
100-145 |
1.44e-03 |
|
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; Molybdopterin-guanine dinucleotide biosynthesis protein A is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 440509 [Multi-domain] Cd Length: 188 Bit Score: 40.95 E-value: 1.44e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1832439758 100 NKVAVLLLAGGQGTRLGVsyPKGMYNVGlpsGKNLYQIQAERIRKV 145
Cdd:COG0746 3 MPITGVILAGGRSRRMGQ--DKALLPLG---GRPLLERVLERLRPQ 43
|
|
| LanC_SerThrkinase |
cd04791 |
Lanthionine synthetase C-like domain associated with serine/threonine kinases; Some members of ... |
699-829 |
6.83e-03 |
|
Lanthionine synthetase C-like domain associated with serine/threonine kinases; Some members of this subgroup lack the zinc binding site and the active site residues, and therefore are most likely inactive. The function of this domain is unknown.
Pssm-ID: 271199 [Multi-domain] Cd Length: 327 Bit Score: 39.95 E-value: 6.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 699 TLWILGLKEEFEEARKWVANDLIFDKNVDvnlfestirILGGL-------LSTYHLSGDSLFLEKAKDIGNRLMPAFK-- 769
Cdd:cd04791 55 VLYELGRREEAERLLDRALALPLDSLDPS---------LYSGLagiglalLHLARATGDPEFLERAARIAERLAARLRed 125
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832439758 770 TPSKIPYSDVNIGRGTAHpprwtSDSTVAevtsiqLEFRELSRLTGDEKFQKAVDEVMKH 829
Cdd:cd04791 126 DPGVYWNDAGAVRAGLLH-----GWSGIA------LFLLRLYEATGDPAYLDLAERALRK 174
|
|
| |
