|
Name |
Accession |
Description |
Interval |
E-value |
| Glycosyltransferase_GTB-type super family |
cl10013 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
500-860 |
1.67e-20 |
|
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.
The actual alignment was detected with superfamily member cd03784:
Pssm-ID: 471961 [Multi-domain] Cd Length: 404 Bit Score: 94.93 E-value: 1.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597322467 500 LKRLHDEIKPDITVVDDLFAPGLSFARNAKVnwialapnvikdfaipmqPYLAALWkYPAIGTGFKYPIPwnliPWNVFF 579
Cdd:cd03784 93 LAALRSSWKPDLVIADPFAYAGPLVAEELGI------------------PSVRLFT-GPATLLSAYLHPF----GVLNLL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597322467 580 TLVSAFAILTDKTRPRLAQHLRKTYGPDFTLTTMADLGLLTPapegikvLVANSPDIDLPLSVLPDHIIPCGPIiRAAPP 659
Cdd:cd03784 150 LSSLLEPELFLDPLLEVLDRLRERLGLPPFSLVLLLLRLVPP-------LYVIGPTFPSLPPDRPRLPSVLGGL-RIVPK 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597322467 660 ICVVDPGLTTWL---KRGPTIYMNLGTHMGFSLDDAKEVAYAFRALFDHassagsvrednfQILWKLPRELPEGQdandf 736
Cdd:cd03784 222 NGPLPDELWEWLdkqPPRSVVYVSFGSMVRDLPEELLELIAEALASLGQ------------RFLWVVGPDPLGGL----- 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597322467 737 tgewtdftdilrqEIEDDRARIMDWF--AAeaksILESGEIVCSINHGGANSFHEALCAGVPQVVLPRWADCYDFASRAE 814
Cdd:cd03784 285 -------------ERLPDNVLVVKWVpqDE----LLAHPAVGAFVTHGGWNSTLEALYAGVPMVVVPLFADQPNNAARVE 347
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1597322467 815 LLGIGKRAnhRKHPWHRSELGEALIAVIIGPEARAIQERAKSVAKR 860
Cdd:cd03784 348 ELGAGVEL--DKDELTAEELAKAVREVLEDESYRRAAELLAELREE 391
|
|
| Kelch_5 |
pfam13854 |
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ... |
297-342 |
2.71e-09 |
|
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.
:
Pssm-ID: 433528 [Multi-domain] Cd Length: 41 Bit Score: 53.34 E-value: 2.71e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1597322467 297 PTARRGFCYVGAEgkngtYEIFVFGGTNSDTGSSFDDVYVLSLPGF 342
Cdd:pfam13854 1 PVPRYGHCAVTVG-----DYIYLYGGYTGGEGQPSDDVYVLSLPTF 41
|
|
| NanM super family |
cl34543 |
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis]; |
231-380 |
3.51e-06 |
|
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
The actual alignment was detected with superfamily member COG3055:
Pssm-ID: 442289 [Multi-domain] Cd Length: 277 Bit Score: 49.77 E-value: 3.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597322467 231 HATMVGGGAVYiptfgdngltvVMGGSTWTLQPSQSSPDGWMdfgnltfYDPISKDWywqQTTGTAPTARRGFCYVGAEG 310
Cdd:COG3055 64 AAAVAQDGKLY-----------VFGGFTGANPSSTPLNDVYV-------YDPATNTW---TKLAPMPTPRGGATALLLDG 122
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597322467 311 KngtyeIFVFGGTNSDTGSSFDDVYVLSLPGfvWTQVPyESKITRRSHSCAVVGRRQMLSVGGTDGKTGW 380
Cdd:COG3055 123 K-----IYVVGGWDDGGNVAWVEVYDPATGT--WTQLA-PLPTPRDHLAAAVLPDGKILVIGGRNGSGFS 184
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GT1_Gtf-like |
cd03784 |
UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of ... |
500-860 |
1.67e-20 |
|
UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of homologous glycosyltransferases involved in the final stages of the biosynthesis of antibiotics vancomycin and related chloroeremomycin. Gtfs transfer sugar moieties from an activated NDP-sugar donor to the oxidatively cross-linked heptapeptide core of vancomycin group antibiotics. The core structure is important for the bioactivity of the antibiotics.
Pssm-ID: 340817 [Multi-domain] Cd Length: 404 Bit Score: 94.93 E-value: 1.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597322467 500 LKRLHDEIKPDITVVDDLFAPGLSFARNAKVnwialapnvikdfaipmqPYLAALWkYPAIGTGFKYPIPwnliPWNVFF 579
Cdd:cd03784 93 LAALRSSWKPDLVIADPFAYAGPLVAEELGI------------------PSVRLFT-GPATLLSAYLHPF----GVLNLL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597322467 580 TLVSAFAILTDKTRPRLAQHLRKTYGPDFTLTTMADLGLLTPapegikvLVANSPDIDLPLSVLPDHIIPCGPIiRAAPP 659
Cdd:cd03784 150 LSSLLEPELFLDPLLEVLDRLRERLGLPPFSLVLLLLRLVPP-------LYVIGPTFPSLPPDRPRLPSVLGGL-RIVPK 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597322467 660 ICVVDPGLTTWL---KRGPTIYMNLGTHMGFSLDDAKEVAYAFRALFDHassagsvrednfQILWKLPRELPEGQdandf 736
Cdd:cd03784 222 NGPLPDELWEWLdkqPPRSVVYVSFGSMVRDLPEELLELIAEALASLGQ------------RFLWVVGPDPLGGL----- 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597322467 737 tgewtdftdilrqEIEDDRARIMDWF--AAeaksILESGEIVCSINHGGANSFHEALCAGVPQVVLPRWADCYDFASRAE 814
Cdd:cd03784 285 -------------ERLPDNVLVVKWVpqDE----LLAHPAVGAFVTHGGWNSTLEALYAGVPMVVVPLFADQPNNAARVE 347
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1597322467 815 LLGIGKRAnhRKHPWHRSELGEALIAVIIGPEARAIQERAKSVAKR 860
Cdd:cd03784 348 ELGAGVEL--DKDELTAEELAKAVREVLEDESYRRAAELLAELREE 391
|
|
| YjiC |
COG1819 |
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism]; |
625-860 |
5.41e-19 |
|
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism];
Pssm-ID: 441424 [Multi-domain] Cd Length: 268 Bit Score: 87.99 E-value: 5.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597322467 625 GIKVLVANSPDIDLPLSVLPDHIIPCGPIIRAAPPicVVDPGLTTwLKRGPTIYMNLGTHMGFSLDDAKEVAYAFRALfD 704
Cdd:COG1819 74 GIPVVSLTPPELEYPRPPDPANVRFVGPLLPDGPA--ELPPWLEE-DAGRPLVYVTLGTSANDRADLLRAVLEALADL-G 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597322467 705 H---ASSAGSVREDnfqiLWKLPrelpegqdANDFTGEWTDFTDILRqeieddRARIMdwfaaeaksilesgeivcsINH 781
Cdd:COG1819 150 VrvvVTTGGLDPAE----LGPLP--------DNVRVVDYVPQDALLP------RADAV-------------------VHH 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1597322467 782 GGANSFHEALCAGVPQVVLPRWADCYDFASRAELLGIGKRANHRKhpWHRSELGEALIAVIIGPEARaiqERAKSVAKR 860
Cdd:COG1819 193 GGAGTTAEALRAGVPQVVVPFGGDQPLNAARVERLGAGLALPPRR--LTAEALRAALRRLLADPSYR---ERAARLAAE 266
|
|
| Kelch_5 |
pfam13854 |
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ... |
297-342 |
2.71e-09 |
|
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.
Pssm-ID: 433528 [Multi-domain] Cd Length: 41 Bit Score: 53.34 E-value: 2.71e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1597322467 297 PTARRGFCYVGAEgkngtYEIFVFGGTNSDTGSSFDDVYVLSLPGF 342
Cdd:pfam13854 1 PVPRYGHCAVTVG-----DYIYLYGGYTGGEGQPSDDVYVLSLPTF 41
|
|
| PLN02210 |
PLN02210 |
UDP-glucosyl transferase |
647-859 |
2.54e-07 |
|
UDP-glucosyl transferase
Pssm-ID: 215127 [Multi-domain] Cd Length: 456 Bit Score: 54.27 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597322467 647 IIPCGPIIraAP----------------PICVVDPGLTTWLK---RGPTIYMNLGTHMGFSLDDAKEVAYAFRAlfdhas 707
Cdd:PLN02210 225 VIPIGPLV--SPfllgddeeetldgknlDMCKSDDCCMEWLDkqaRSSVVYISFGSMLESLENQVETIAKALKN------ 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597322467 708 sagsvREDNFqiLWKL-PRElpEGQDandftgewtdfTDILRQEIEDDRARIMDWfaAEAKSILESGEIVCSINHGGANS 786
Cdd:PLN02210 297 -----RGVPF--LWVIrPKE--KAQN-----------VQVLQEMVKEGQGVVLEW--SPQEKILSHMAISCFVTHCGWNS 354
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1597322467 787 FHEALCAGVPQVVLPRWAD-CYDFASRAELLGIGKRANHRK--HPWHRSELGEALIAVIIGPEARAIQERA---KSVAK 859
Cdd:PLN02210 355 TIETVVAGVPVVAYPSWTDqPIDARLLVDVFGIGVRMRNDAvdGELKVEEVERCIEAVTEGPAAADIRRRAaelKHVAR 433
|
|
| NanM |
COG3055 |
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis]; |
231-380 |
3.51e-06 |
|
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442289 [Multi-domain] Cd Length: 277 Bit Score: 49.77 E-value: 3.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597322467 231 HATMVGGGAVYiptfgdngltvVMGGSTWTLQPSQSSPDGWMdfgnltfYDPISKDWywqQTTGTAPTARRGFCYVGAEG 310
Cdd:COG3055 64 AAAVAQDGKLY-----------VFGGFTGANPSSTPLNDVYV-------YDPATNTW---TKLAPMPTPRGGATALLLDG 122
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597322467 311 KngtyeIFVFGGTNSDTGSSFDDVYVLSLPGfvWTQVPyESKITRRSHSCAVVGRRQMLSVGGTDGKTGW 380
Cdd:COG3055 123 K-----IYVVGGWDDGGNVAWVEVYDPATGT--WTQLA-PLPTPRDHLAAAVLPDGKILVIGGRNGSGFS 184
|
|
| MGT |
TIGR01426 |
glycosyltransferase, MGT family; This model describes the MGT (macroside glycosyltransferase) ... |
665-875 |
1.01e-05 |
|
glycosyltransferase, MGT family; This model describes the MGT (macroside glycosyltransferase) subfamily of the UDP-glucuronosyltransferase family. Members include a number of glucosyl transferases for macrolide antibiotic inactivation, but also include transferases of glucose-related sugars for macrolide antibiotic production. [Cellular processes, Toxin production and resistance]
Pssm-ID: 273616 [Multi-domain] Cd Length: 392 Bit Score: 48.91 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597322467 665 PGLTTWL---KRGPTIYMNLGTHMGFSLDDAKEVAYAFRALFDHA--SSAGSVREDNFqilwklpRELPEgqdaNDFTGE 739
Cdd:TIGR01426 213 KEDGSWErpgDGRPVVLISLGTVFNNQPSFYRTCVEAFRDLDWHVvlSVGRGVDPADL-------GELPP----NVEVRQ 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597322467 740 WTDFTDILrqeiedDRARIMdwfaaeaksilesgeivcsINHGGANSFHEALCAGVPQVVLPRWADCYDFASRAELLGIG 819
Cdd:TIGR01426 282 WVPQLEIL------KKADAF-------------------ITHGGMNSTMEALFNGVPMVAVPQGADQPMTARRIAELGLG 336
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1597322467 820 KRANhrKHPWHRSELGEALIAVIIGPEaraIQERAKSVAKRHPETEGRVNAAKEIL 875
Cdd:TIGR01426 337 RHLP--PEEVTAEKLREAVLAVLSDPR---YAERLRKMRAEIREAGGARRAADEIE 387
|
|
| PLN02153 |
PLN02153 |
epithiospecifier protein |
185-379 |
7.02e-05 |
|
epithiospecifier protein
Pssm-ID: 177814 [Multi-domain] Cd Length: 341 Bit Score: 46.13 E-value: 7.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597322467 185 FVFGGIATGWTNANPasQPVPGVLSYNMTTTMWTNETTPGfSGFSKHatmvgGGAvyiptfgdnGLTVVMGgSTWTLQPS 264
Cdd:PLN02153 141 YVFGGVSKGGLMKTP--ERFRTIEAYNIADGKWVQLPDPG-ENFEKR-----GGA---------GFAVVQG-KIWVVYGF 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597322467 265 QSS--PDGWMDFGN--LTFYDPISKDWYWQQTTGTAPTARRGFcyvgAEGKNGTYeIFVFGGT-------NSDTGSSFDD 333
Cdd:PLN02153 203 ATSilPGGKSDYESnaVQFFDPASGKWTEVETTGAKPSARSVF----AHAVVGKY-IIIFGGEvwpdlkgHLGPGTLSNE 277
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1597322467 334 VYVLSLPGFVWTQVPY--ESKITR--RSHSCAVV-GRRQMLSVGG---TDGKTG 379
Cdd:PLN02153 278 GYALDTETLVWEKLGEcgEPAMPRgwTAYTTATVyGKNGLLMHGGklpTNERTD 331
|
|
| UDPGT |
pfam00201 |
UDP-glucoronosyl and UDP-glucosyl transferase; |
779-862 |
1.07e-04 |
|
UDP-glucoronosyl and UDP-glucosyl transferase;
Pssm-ID: 278624 [Multi-domain] Cd Length: 499 Bit Score: 45.86 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597322467 779 INHGGANSFHEALCAGVPQVVLPRWADCYDFASRAELLGIGKRANHRKHPwhRSELGEALIAVIIGPEARAIQERAKSVA 858
Cdd:pfam00201 345 ITHAGSNGVYEAICHGVPMVGMPLFGDQMDNAKHMEAKGAAVTLNVLTMT--SEDLLNALKEVINDPSYKENIMRLSSIH 422
|
....
gi 1597322467 859 KRHP 862
Cdd:pfam00201 423 HDQP 426
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GT1_Gtf-like |
cd03784 |
UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of ... |
500-860 |
1.67e-20 |
|
UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of homologous glycosyltransferases involved in the final stages of the biosynthesis of antibiotics vancomycin and related chloroeremomycin. Gtfs transfer sugar moieties from an activated NDP-sugar donor to the oxidatively cross-linked heptapeptide core of vancomycin group antibiotics. The core structure is important for the bioactivity of the antibiotics.
Pssm-ID: 340817 [Multi-domain] Cd Length: 404 Bit Score: 94.93 E-value: 1.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597322467 500 LKRLHDEIKPDITVVDDLFAPGLSFARNAKVnwialapnvikdfaipmqPYLAALWkYPAIGTGFKYPIPwnliPWNVFF 579
Cdd:cd03784 93 LAALRSSWKPDLVIADPFAYAGPLVAEELGI------------------PSVRLFT-GPATLLSAYLHPF----GVLNLL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597322467 580 TLVSAFAILTDKTRPRLAQHLRKTYGPDFTLTTMADLGLLTPapegikvLVANSPDIDLPLSVLPDHIIPCGPIiRAAPP 659
Cdd:cd03784 150 LSSLLEPELFLDPLLEVLDRLRERLGLPPFSLVLLLLRLVPP-------LYVIGPTFPSLPPDRPRLPSVLGGL-RIVPK 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597322467 660 ICVVDPGLTTWL---KRGPTIYMNLGTHMGFSLDDAKEVAYAFRALFDHassagsvrednfQILWKLPRELPEGQdandf 736
Cdd:cd03784 222 NGPLPDELWEWLdkqPPRSVVYVSFGSMVRDLPEELLELIAEALASLGQ------------RFLWVVGPDPLGGL----- 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597322467 737 tgewtdftdilrqEIEDDRARIMDWF--AAeaksILESGEIVCSINHGGANSFHEALCAGVPQVVLPRWADCYDFASRAE 814
Cdd:cd03784 285 -------------ERLPDNVLVVKWVpqDE----LLAHPAVGAFVTHGGWNSTLEALYAGVPMVVVPLFADQPNNAARVE 347
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1597322467 815 LLGIGKRAnhRKHPWHRSELGEALIAVIIGPEARAIQERAKSVAKR 860
Cdd:cd03784 348 ELGAGVEL--DKDELTAEELAKAVREVLEDESYRRAAELLAELREE 391
|
|
| YjiC |
COG1819 |
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism]; |
625-860 |
5.41e-19 |
|
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism];
Pssm-ID: 441424 [Multi-domain] Cd Length: 268 Bit Score: 87.99 E-value: 5.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597322467 625 GIKVLVANSPDIDLPLSVLPDHIIPCGPIIRAAPPicVVDPGLTTwLKRGPTIYMNLGTHMGFSLDDAKEVAYAFRALfD 704
Cdd:COG1819 74 GIPVVSLTPPELEYPRPPDPANVRFVGPLLPDGPA--ELPPWLEE-DAGRPLVYVTLGTSANDRADLLRAVLEALADL-G 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597322467 705 H---ASSAGSVREDnfqiLWKLPrelpegqdANDFTGEWTDFTDILRqeieddRARIMdwfaaeaksilesgeivcsINH 781
Cdd:COG1819 150 VrvvVTTGGLDPAE----LGPLP--------DNVRVVDYVPQDALLP------RADAV-------------------VHH 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1597322467 782 GGANSFHEALCAGVPQVVLPRWADCYDFASRAELLGIGKRANHRKhpWHRSELGEALIAVIIGPEARaiqERAKSVAKR 860
Cdd:COG1819 193 GGAGTTAEALRAGVPQVVVPFGGDQPLNAARVERLGAGLALPPRR--LTAEALRAALRRLLADPSYR---ERAARLAAE 266
|
|
| Kelch_5 |
pfam13854 |
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ... |
297-342 |
2.71e-09 |
|
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.
Pssm-ID: 433528 [Multi-domain] Cd Length: 41 Bit Score: 53.34 E-value: 2.71e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1597322467 297 PTARRGFCYVGAEgkngtYEIFVFGGTNSDTGSSFDDVYVLSLPGF 342
Cdd:pfam13854 1 PVPRYGHCAVTVG-----DYIYLYGGYTGGEGQPSDDVYVLSLPTF 41
|
|
| PLN02210 |
PLN02210 |
UDP-glucosyl transferase |
647-859 |
2.54e-07 |
|
UDP-glucosyl transferase
Pssm-ID: 215127 [Multi-domain] Cd Length: 456 Bit Score: 54.27 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597322467 647 IIPCGPIIraAP----------------PICVVDPGLTTWLK---RGPTIYMNLGTHMGFSLDDAKEVAYAFRAlfdhas 707
Cdd:PLN02210 225 VIPIGPLV--SPfllgddeeetldgknlDMCKSDDCCMEWLDkqaRSSVVYISFGSMLESLENQVETIAKALKN------ 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597322467 708 sagsvREDNFqiLWKL-PRElpEGQDandftgewtdfTDILRQEIEDDRARIMDWfaAEAKSILESGEIVCSINHGGANS 786
Cdd:PLN02210 297 -----RGVPF--LWVIrPKE--KAQN-----------VQVLQEMVKEGQGVVLEW--SPQEKILSHMAISCFVTHCGWNS 354
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1597322467 787 FHEALCAGVPQVVLPRWAD-CYDFASRAELLGIGKRANHRK--HPWHRSELGEALIAVIIGPEARAIQERA---KSVAK 859
Cdd:PLN02210 355 TIETVVAGVPVVAYPSWTDqPIDARLLVDVFGIGVRMRNDAvdGELKVEEVERCIEAVTEGPAAADIRRRAaelKHVAR 433
|
|
| PLN02555 |
PLN02555 |
limonoid glucosyltransferase |
746-854 |
9.96e-07 |
|
limonoid glucosyltransferase
Pssm-ID: 178170 [Multi-domain] Cd Length: 480 Bit Score: 52.11 E-value: 9.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597322467 746 ILRQEIED---DRARIMDWFAAEakSILESGEIVCSINHGGANSFHEALCAGVPQVVLPRWAD-CYDFASRAELLGIGKR 821
Cdd:PLN02555 326 VLPEEFLEkagDKGKIVQWCPQE--KVLAHPSVACFVTHCGWNSTMEALSSGVPVVCFPQWGDqVTDAVYLVDVFKTGVR 403
|
90 100 110
....*....|....*....|....*....|....*...
gi 1597322467 822 -----ANHRKHPwhRSELGEALIAVIIGPEARAIQERA 854
Cdd:PLN02555 404 lcrgeAENKLIT--REEVAECLLEATVGEKAAELKQNA 439
|
|
| NanM |
COG3055 |
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis]; |
231-380 |
3.51e-06 |
|
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442289 [Multi-domain] Cd Length: 277 Bit Score: 49.77 E-value: 3.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597322467 231 HATMVGGGAVYiptfgdngltvVMGGSTWTLQPSQSSPDGWMdfgnltfYDPISKDWywqQTTGTAPTARRGFCYVGAEG 310
Cdd:COG3055 64 AAAVAQDGKLY-----------VFGGFTGANPSSTPLNDVYV-------YDPATNTW---TKLAPMPTPRGGATALLLDG 122
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597322467 311 KngtyeIFVFGGTNSDTGSSFDDVYVLSLPGfvWTQVPyESKITRRSHSCAVVGRRQMLSVGGTDGKTGW 380
Cdd:COG3055 123 K-----IYVVGGWDDGGNVAWVEVYDPATGT--WTQLA-PLPTPRDHLAAAVLPDGKILVIGGRNGSGFS 184
|
|
| PLN02554 |
PLN02554 |
UDP-glycosyltransferase family protein |
670-805 |
4.14e-06 |
|
UDP-glycosyltransferase family protein
Pssm-ID: 215304 Cd Length: 481 Bit Score: 50.17 E-value: 4.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597322467 670 WLKRGPT---IYMNLGTHMGFSLDDAKEVAYAfralfdhassagsVREDNFQILWKLPRELPEGqdANDFTGEWTDFTDI 746
Cdd:PLN02554 267 WLDEQPPksvVFLCFGSMGGFSEEQAREIAIA-------------LERSGHRFLWSLRRASPNI--MKEPPGEFTNLEEI 331
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1597322467 747 LRQEIED---DRARIMDWfaAEAKSILESGEIVCSINHGGANSFHEALCAGVPQVVLPRWAD 805
Cdd:PLN02554 332 LPEGFLDrtkDIGKVIGW--APQVAVLAKPAIGGFVTHCGWNSILESLWFGVPMAAWPLYAE 391
|
|
| MGT |
TIGR01426 |
glycosyltransferase, MGT family; This model describes the MGT (macroside glycosyltransferase) ... |
665-875 |
1.01e-05 |
|
glycosyltransferase, MGT family; This model describes the MGT (macroside glycosyltransferase) subfamily of the UDP-glucuronosyltransferase family. Members include a number of glucosyl transferases for macrolide antibiotic inactivation, but also include transferases of glucose-related sugars for macrolide antibiotic production. [Cellular processes, Toxin production and resistance]
Pssm-ID: 273616 [Multi-domain] Cd Length: 392 Bit Score: 48.91 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597322467 665 PGLTTWL---KRGPTIYMNLGTHMGFSLDDAKEVAYAFRALFDHA--SSAGSVREDNFqilwklpRELPEgqdaNDFTGE 739
Cdd:TIGR01426 213 KEDGSWErpgDGRPVVLISLGTVFNNQPSFYRTCVEAFRDLDWHVvlSVGRGVDPADL-------GELPP----NVEVRQ 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597322467 740 WTDFTDILrqeiedDRARIMdwfaaeaksilesgeivcsINHGGANSFHEALCAGVPQVVLPRWADCYDFASRAELLGIG 819
Cdd:TIGR01426 282 WVPQLEIL------KKADAF-------------------ITHGGMNSTMEALFNGVPMVAVPQGADQPMTARRIAELGLG 336
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1597322467 820 KRANhrKHPWHRSELGEALIAVIIGPEaraIQERAKSVAKRHPETEGRVNAAKEIL 875
Cdd:TIGR01426 337 RHLP--PEEVTAEKLREAVLAVLSDPR---YAERLRKMRAEIREAGGARRAADEIE 387
|
|
| PLN02173 |
PLN02173 |
UDP-glucosyl transferase family protein |
668-805 |
1.33e-05 |
|
UDP-glucosyl transferase family protein
Pssm-ID: 177830 [Multi-domain] Cd Length: 449 Bit Score: 48.49 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597322467 668 TTWLKRGP---TIYMNLGTHMGFSLDDAKEVAYAFralfdhassagsvreDNFQILWKL----PRELPEGqdandftgew 740
Cdd:PLN02173 255 TDWLDKRPqgsVVYIAFGSMAKLSSEQMEEIASAI---------------SNFSYLWVVraseESKLPPG---------- 309
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1597322467 741 tdFTDIlrqeIEDDRARIMDWfaAEAKSILESGEIVCSINHGGANSFHEALCAGVPQVVLPRWAD 805
Cdd:PLN02173 310 --FLET----VDKDKSLVLKW--SPQLQVLSNKAIGCFMTHCGWNSTMEGLSLGVPMVAMPQWTD 366
|
|
| PLN02153 |
PLN02153 |
epithiospecifier protein |
185-379 |
7.02e-05 |
|
epithiospecifier protein
Pssm-ID: 177814 [Multi-domain] Cd Length: 341 Bit Score: 46.13 E-value: 7.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597322467 185 FVFGGIATGWTNANPasQPVPGVLSYNMTTTMWTNETTPGfSGFSKHatmvgGGAvyiptfgdnGLTVVMGgSTWTLQPS 264
Cdd:PLN02153 141 YVFGGVSKGGLMKTP--ERFRTIEAYNIADGKWVQLPDPG-ENFEKR-----GGA---------GFAVVQG-KIWVVYGF 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597322467 265 QSS--PDGWMDFGN--LTFYDPISKDWYWQQTTGTAPTARRGFcyvgAEGKNGTYeIFVFGGT-------NSDTGSSFDD 333
Cdd:PLN02153 203 ATSilPGGKSDYESnaVQFFDPASGKWTEVETTGAKPSARSVF----AHAVVGKY-IIIFGGEvwpdlkgHLGPGTLSNE 277
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1597322467 334 VYVLSLPGFVWTQVPY--ESKITR--RSHSCAVV-GRRQMLSVGG---TDGKTG 379
Cdd:PLN02153 278 GYALDTETLVWEKLGEcgEPAMPRgwTAYTTATVyGKNGLLMHGGklpTNERTD 331
|
|
| UDPGT |
pfam00201 |
UDP-glucoronosyl and UDP-glucosyl transferase; |
779-862 |
1.07e-04 |
|
UDP-glucoronosyl and UDP-glucosyl transferase;
Pssm-ID: 278624 [Multi-domain] Cd Length: 499 Bit Score: 45.86 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597322467 779 INHGGANSFHEALCAGVPQVVLPRWADCYDFASRAELLGIGKRANHRKHPwhRSELGEALIAVIIGPEARAIQERAKSVA 858
Cdd:pfam00201 345 ITHAGSNGVYEAICHGVPMVGMPLFGDQMDNAKHMEAKGAAVTLNVLTMT--SEDLLNALKEVINDPSYKENIMRLSSIH 422
|
....
gi 1597322467 859 KRHP 862
Cdd:pfam00201 423 HDQP 426
|
|
| NanM |
COG3055 |
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis]; |
185-376 |
3.25e-03 |
|
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442289 [Multi-domain] Cd Length: 277 Bit Score: 40.52 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597322467 185 FVFGGiatgWTNANPASQPVPGVLSYNMtTTMWTNETTPGFSGFSKHATMVGGGAVYiptfgdngltvVMGGSTWtlqps 264
Cdd:COG3055 74 YVFGG----FTGANPSSTPLNDVYVYDP-ATNTWTKLAPMPTPRGGATALLLDGKIY-----------VVGGWDD----- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1597322467 265 qSSPDGWMDfgnltFYDPISKDWywqQTTGTAPTARRGFCyvGAEGKNGtyEIFVFGGTNSDTGSSfddvyvlslpgfVW 344
Cdd:COG3055 133 -GGNVAWVE-----VYDPATGTW---TQLAPLPTPRDHLA--AAVLPDG--KILVIGGRNGSGFSN------------TW 187
|
170 180 190
....*....|....*....|....*....|..
gi 1597322467 345 TQVPyeSKITRRSHSCAVVGRRQMLSVGGTDG 376
Cdd:COG3055 188 TTLA--PLPTARAGHAAAVLGGKILVFGGESG 217
|
|
| |
