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Conserved domains on  [gi|1002245207|ref|XP_015626786|]
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L-arabinokinase [Oryza sativa Japonica Group]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GalK super family cl33780
Galactokinase [Carbohydrate transport and metabolism];
499-986 2.02e-40

Galactokinase [Carbohydrate transport and metabolism];


The actual alignment was detected with superfamily member COG0153:

Pssm-ID: 439923 [Multi-domain]  Cd Length: 380  Bit Score: 153.77  E-value: 2.02e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 499 EEEIYVARAPGRLDVMGGIADYSGSLVLQMPIREACHVAIQRsnpmkqklwkhtqarqlangRAVPLLQIVSFGSElsnr 578
Cdd:COG0153    15 EEPEGVFSAPGRVNLIGEHTDYNGGFVLPAAIDRGTYAAARP--------------------RDDRKVRVYSADFD---- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 579 aPTFDMDLSDFmdgdkpisydkakeyfSQDPSQKWAAYVAGTILVLMtELGVVFTdSMSILVSSSVPEGKGvsssasvev 658
Cdd:COG0153    71 -EEVEFDLDDL----------------EPGEEDGWANYVRGVAWALQ-ERGYKLG-GFDLVIDGDVPLGAG--------- 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 659 asMS-----------AIAAAYGLNIPPRDLAILCQKVENRIVGAPCGVMDQMTSACGEANKLLAMICQPAEVkELVSIPT 727
Cdd:COG0153   123 --LSssaalevavalALNDLFGLGLDPVELAKIGQRAENEFVGVPCGIMDQFASALGKKGHALLLDCRSLEY-EYVPLPL 199

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 728 H-IRFWGLDSGIRHSVGGTDYGSVRVgtymgrkmikcaasdllseslpSCppiqsgntnsdeyeEHGVDLLkseaSLEYL 806
Cdd:COG0153   200 EgYALVIVDTNVKHSLADSEYNERRA----------------------EC--------------EAAAAIL----GVKSL 239

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 807 CNLPPHRYEAVYARDIPEIITgdaflekygdhndavttvdpKRsycvkapTRHPIYENFRVEAFKALLTAaktvEQLSAL 886
Cdd:COG0153   240 RDVTLEDLEAARARLGDEVLR--------------------RR-------ARHVVTENQRVLEAVEALRA----GDLEAF 288

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 887 GELMYQCHYSY-NACGLGSDGTDRLVNMVQEVqhrktsqdggPSLFGAKITgggsggsvCVIgknCL--KSSEEIF--EI 961
Cdd:COG0153   289 GKLMNASHASLrDDYEVSCPELDTLVELALAE----------AGVLGARMTggg--fggCTI---ALvpKDAVDEFieAV 353

                         490       500
                  ....*....|....*....|....*.
gi 1002245207 962 QKRYKAATGYLPIVFEGS-SPGAGKF 986
Cdd:COG0153   354 AEAYAEKTGLEPDFYVVKpSDGARRL 379
Glycosyltransferase_GTB-type super family cl10013
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 26-345 7.78e-10

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: 62.18  E-value: 7.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207  26 LVFAYyitgHGFGHATRALEVVRHLIAAGHDVHVVTgaPEFVFTTEISSPNLHIRKVLLDCGAVQADALTVDRLASLEKY 105
Cdd:cd03784     4 LFVPF----PGQGHVNPMLPLAKALAARGHEVTVAT--PPFNFADLVEAAGLTFVPVGDDPDELELDSETNLGPDSLLEL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 106 HQTAVMPRESILRTEVE-WLNTIKADLVVSDVVPVACRAAADA-GIRSVCVTNFSWDFIYAEYVVVAGHHHRSIVWQIAE 183
Cdd:cd03784    78 LRRLLKAADELLDDLLAaLRSSWKPDLVIADPFAYAGPLVAEElGIPSVRLFTGPATLLSAYLHPFGVLNLLLSSLLEPE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 184 DYSH--CEFLLRL------------------------PGYCPMPAFRDVIDVPLVVRRLH------KSRSEVRKELGIKD 231
Cdd:cd03784   158 LFLDplLEVLDRLrerlglppfslvllllrlvpplyvIGPTFPSLPPDRPRLPSVLGGLRivpkngPLPDELWEWLDKQP 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 232 DVKVVIFNFG---------------------GQPAGWKLkkEWLPDGWLclvcgasetQELPPNfIKLAKDAytP--DLM 288
Cdd:cd03784   238 PRSVVYVSFGsmvrdlpeelleliaealaslGQRFLWVV--GPDPLGGL---------ERLPDN-VLVVKWV--PqdELL 303

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002245207 289 A--ASDCML--GkiGYGTVSEALAYKLPFVFVrrDYFNEEPFLRNMLEHYQCGVEMVRRDL 345
Cdd:cd03784   304 AhpAVGAFVthG--GWNSTLEALYAGVPMVVV--PLFADQPNNAARVEELGAGVELDKDEL 360
 
Name Accession Description Interval E-value
GalK COG0153
Galactokinase [Carbohydrate transport and metabolism];
499-986 2.02e-40

Galactokinase [Carbohydrate transport and metabolism];


Pssm-ID: 439923 [Multi-domain]  Cd Length: 380  Bit Score: 153.77  E-value: 2.02e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 499 EEEIYVARAPGRLDVMGGIADYSGSLVLQMPIREACHVAIQRsnpmkqklwkhtqarqlangRAVPLLQIVSFGSElsnr 578
Cdd:COG0153    15 EEPEGVFSAPGRVNLIGEHTDYNGGFVLPAAIDRGTYAAARP--------------------RDDRKVRVYSADFD---- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 579 aPTFDMDLSDFmdgdkpisydkakeyfSQDPSQKWAAYVAGTILVLMtELGVVFTdSMSILVSSSVPEGKGvsssasvev 658
Cdd:COG0153    71 -EEVEFDLDDL----------------EPGEEDGWANYVRGVAWALQ-ERGYKLG-GFDLVIDGDVPLGAG--------- 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 659 asMS-----------AIAAAYGLNIPPRDLAILCQKVENRIVGAPCGVMDQMTSACGEANKLLAMICQPAEVkELVSIPT 727
Cdd:COG0153   123 --LSssaalevavalALNDLFGLGLDPVELAKIGQRAENEFVGVPCGIMDQFASALGKKGHALLLDCRSLEY-EYVPLPL 199

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 728 H-IRFWGLDSGIRHSVGGTDYGSVRVgtymgrkmikcaasdllseslpSCppiqsgntnsdeyeEHGVDLLkseaSLEYL 806
Cdd:COG0153   200 EgYALVIVDTNVKHSLADSEYNERRA----------------------EC--------------EAAAAIL----GVKSL 239

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 807 CNLPPHRYEAVYARDIPEIITgdaflekygdhndavttvdpKRsycvkapTRHPIYENFRVEAFKALLTAaktvEQLSAL 886
Cdd:COG0153   240 RDVTLEDLEAARARLGDEVLR--------------------RR-------ARHVVTENQRVLEAVEALRA----GDLEAF 288

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 887 GELMYQCHYSY-NACGLGSDGTDRLVNMVQEVqhrktsqdggPSLFGAKITgggsggsvCVIgknCL--KSSEEIF--EI 961
Cdd:COG0153   289 GKLMNASHASLrDDYEVSCPELDTLVELALAE----------AGVLGARMTggg--fggCTI---ALvpKDAVDEFieAV 353

                         490       500
                  ....*....|....*....|....*.
gi 1002245207 962 QKRYKAATGYLPIVFEGS-SPGAGKF 986
Cdd:COG0153   354 AEAYAEKTGLEPDFYVVKpSDGARRL 379
PRK03817 PRK03817
galactokinase; Provisional
 503-747 4.59e-21

galactokinase; Provisional


Pssm-ID: 235163 [Multi-domain]  Cd Length: 351  Bit Score: 95.83  E-value: 4.59e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 503 YVARAPGRLDVMGGIADYSGSLVLQMPIREACHVAIQRSNPmkqklwkhtqarqlangravpllqiVSFGSELSNRAPTF 582
Cdd:PRK03817    1 MKVKSPGRVNLIGEHTDYNDGYVLPFAINLYTFLEIEKSEK-------------------------FIFYSENFNEEKTF 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 583 DMDlsdfmdgdkpisydkakeyfSQDPSQKWAAYVAGTILVLMTELGVVftDSMSILVSSSVPEGKGVSSSASVEVASMS 662
Cdd:PRK03817   56 ELD--------------------KLEKLNSWADYIKGVIWVLEKRGYEV--GGVKGKVSSNLPIGAGLSSSASLEVAVAY 113

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 663 AIAAAYGLNIPPRDLAILCQKVENRIVGAPCGVMDQMTSACGEANKLLAMICQPAEVkELVSIPTHIRFWGLDSGIRHSV 742
Cdd:PRK03817  114 ALNEAYNLNLSKLELALLAREAENEFVGVPCGIMDQFAVAFGKKDHAIFLDTMTLEY-EYVPFPEDYEILVFDTGVKREL 192


                  ....*
gi 1002245207 743 GGTDY 747
Cdd:PRK03817  193 ASSEY 197
GT1_Gtf-like cd03784
UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of ...
 26-345 7.78e-10

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: 62.18  E-value: 7.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207  26 LVFAYyitgHGFGHATRALEVVRHLIAAGHDVHVVTgaPEFVFTTEISSPNLHIRKVLLDCGAVQADALTVDRLASLEKY 105
Cdd:cd03784     4 LFVPF----PGQGHVNPMLPLAKALAARGHEVTVAT--PPFNFADLVEAAGLTFVPVGDDPDELELDSETNLGPDSLLEL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 106 HQTAVMPRESILRTEVE-WLNTIKADLVVSDVVPVACRAAADA-GIRSVCVTNFSWDFIYAEYVVVAGHHHRSIVWQIAE 183
Cdd:cd03784    78 LRRLLKAADELLDDLLAaLRSSWKPDLVIADPFAYAGPLVAEElGIPSVRLFTGPATLLSAYLHPFGVLNLLLSSLLEPE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 184 DYSH--CEFLLRL------------------------PGYCPMPAFRDVIDVPLVVRRLH------KSRSEVRKELGIKD 231
Cdd:cd03784   158 LFLDplLEVLDRLrerlglppfslvllllrlvpplyvIGPTFPSLPPDRPRLPSVLGGLRivpkngPLPDELWEWLDKQP 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 232 DVKVVIFNFG---------------------GQPAGWKLkkEWLPDGWLclvcgasetQELPPNfIKLAKDAytP--DLM 288
Cdd:cd03784   238 PRSVVYVSFGsmvrdlpeelleliaealaslGQRFLWVV--GPDPLGGL---------ERLPDN-VLVVKWV--PqdELL 303

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002245207 289 A--ASDCML--GkiGYGTVSEALAYKLPFVFVrrDYFNEEPFLRNMLEHYQCGVEMVRRDL 345
Cdd:cd03784   304 AhpAVGAFVthG--GWNSTLEALYAGVPMVVV--PLFADQPNNAARVEELGAGVELDKDEL 360
GalKase_gal_bdg pfam10509
Galactokinase galactose-binding signature; This is the highly conserved galactokinase ...
 499-540 2.02e-05

Galactokinase galactose-binding signature; This is the highly conserved galactokinase signature sequence which appears to be present in all galactokinases irrespective of how many other ATP binding sites, etc that they carry. The function of this domain appears to be to bind galactose, and the domain is normally at the N-terminus of the enzymes, EC:2.7.1.6. This domain is associated with the families GHMP_kinases_C, pfam08544 and GHMP_kinases_N, pfam00288.


Pssm-ID: 463125 [Multi-domain]  Cd Length: 50  Bit Score: 42.82  E-value: 2.02e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1002245207 499 EEEIYVARAPGRLDVMGGIADYSGSLVLQMPIREACHVAIQR 540
Cdd:pfam10509   9 KEPVGVASAPGRVNLIGEHTDYNGGFVLPAAINLDTYVAVSP 50
YjiC COG1819
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism];
31-347 1.73e-04

UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism];


Pssm-ID: 441424 [Multi-domain]  Cd Length: 268  Bit Score: 44.46  E-value: 1.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207  31 YITGHGFGHATRALEVVRHLIAAGHDVHVVTGaPEFVftteisspnlhirkvlldcGAVQADALTVdrlaslekyhqtav 110
Cdd:COG1819     4 FVTLGGRGHVNPLLALARALRARGHEVTFATG-PDFA-------------------DLVEAAGLEF-------------- 49

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 111 mpresilrteVEWlntiKADLVVSDVVPVACRAAADA-GIRSVCVTnfswdfiyaeyvvvaghhhrsivwqiaedyshce 189
Cdd:COG1819    50 ----------VDW----RPDLVVSDPLALAAALAAEAlGIPVVSLT---------------------------------- 81

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 190 fllrlPGYCPMPAFRDVIDVPLVVRRLHKSRSEVRKELGIKDDVKVVIFNFGGQPAGWK---------LKKEwlpdGWLC 260
Cdd:COG1819    82 -----PPELEYPRPPDPANVRFVGPLLPDGPAELPPWLEEDAGRPLVYVTLGTSANDRAdllravleaLADL----GVRV 152

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 261 LVC----GASETQELPPNFIKLakdAYTP--DLMAASDCML--GkiGYGTVSEALAYKLPFVFVrrDYFNEEPFLRNMLE 332
Cdd:COG1819   153 VVTtgglDPAELGPLPDNVRVV---DYVPqdALLPRADAVVhhG--GAGTTAEALRAGVPQVVV--PFGGDQPLNAARVE 225

                         330
                  ....*....|....*
gi 1002245207 333 HYQCGVeMVRRDLLT 347
Cdd:COG1819   226 RLGAGL-ALPPRRLT 239
Glyco_trans_1_3 pfam13528
Glycosyl transferase family 1;
30-61 8.77e-04

Glycosyl transferase family 1;


Pssm-ID: 404422  Cd Length: 321  Bit Score: 42.48  E-value: 8.77e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1002245207  30 YYITGHGFGHATRALEVVRHLiAAGHDVHVVT 61
Cdd:pfam13528   5 YGVVGEGMGHATRSRVVLEHL-VRGHEVHVVV 35
PLN02605 PLN02605
monogalactosyldiacylglycerol synthase
 218-312 1.40e-03

monogalactosyldiacylglycerol synthase


Pssm-ID: 215325 [Multi-domain]  Cd Length: 382  Bit Score: 42.26  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 218 KSRSEVRKELGIKDDVKVVIFNFGGQPAG----------WKLKKEWL--PDGWLCLVCGASET-QElppnfiKLAKDAYT 284
Cdd:PLN02605  191 RPKDELRRELGMDEDLPAVLLMGGGEGMGpleetaralgDSLYDKNLgkPIGQVVVICGRNKKlQS------KLESRDWK 264

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1002245207 285 PDL------------MAASDCMLGKIGYGTVSEALAYKLP 312
Cdd:PLN02605  265 IPVkvrgfvtnmeewMGACDCIITKAGPGTIAEALIRGLP 304
 
Name Accession Description Interval E-value
GalK COG0153
Galactokinase [Carbohydrate transport and metabolism];
499-986 2.02e-40

Galactokinase [Carbohydrate transport and metabolism];


Pssm-ID: 439923 [Multi-domain]  Cd Length: 380  Bit Score: 153.77  E-value: 2.02e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 499 EEEIYVARAPGRLDVMGGIADYSGSLVLQMPIREACHVAIQRsnpmkqklwkhtqarqlangRAVPLLQIVSFGSElsnr 578
Cdd:COG0153    15 EEPEGVFSAPGRVNLIGEHTDYNGGFVLPAAIDRGTYAAARP--------------------RDDRKVRVYSADFD---- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 579 aPTFDMDLSDFmdgdkpisydkakeyfSQDPSQKWAAYVAGTILVLMtELGVVFTdSMSILVSSSVPEGKGvsssasvev 658
Cdd:COG0153    71 -EEVEFDLDDL----------------EPGEEDGWANYVRGVAWALQ-ERGYKLG-GFDLVIDGDVPLGAG--------- 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 659 asMS-----------AIAAAYGLNIPPRDLAILCQKVENRIVGAPCGVMDQMTSACGEANKLLAMICQPAEVkELVSIPT 727
Cdd:COG0153   123 --LSssaalevavalALNDLFGLGLDPVELAKIGQRAENEFVGVPCGIMDQFASALGKKGHALLLDCRSLEY-EYVPLPL 199

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 728 H-IRFWGLDSGIRHSVGGTDYGSVRVgtymgrkmikcaasdllseslpSCppiqsgntnsdeyeEHGVDLLkseaSLEYL 806
Cdd:COG0153   200 EgYALVIVDTNVKHSLADSEYNERRA----------------------EC--------------EAAAAIL----GVKSL 239

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 807 CNLPPHRYEAVYARDIPEIITgdaflekygdhndavttvdpKRsycvkapTRHPIYENFRVEAFKALLTAaktvEQLSAL 886
Cdd:COG0153   240 RDVTLEDLEAARARLGDEVLR--------------------RR-------ARHVVTENQRVLEAVEALRA----GDLEAF 288

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 887 GELMYQCHYSY-NACGLGSDGTDRLVNMVQEVqhrktsqdggPSLFGAKITgggsggsvCVIgknCL--KSSEEIF--EI 961
Cdd:COG0153   289 GKLMNASHASLrDDYEVSCPELDTLVELALAE----------AGVLGARMTggg--fggCTI---ALvpKDAVDEFieAV 353

                         490       500
                  ....*....|....*....|....*.
gi 1002245207 962 QKRYKAATGYLPIVFEGS-SPGAGKF 986
Cdd:COG0153   354 AEAYAEKTGLEPDFYVVKpSDGARRL 379
PRK03817 PRK03817
galactokinase; Provisional
 503-747 4.59e-21

galactokinase; Provisional


Pssm-ID: 235163 [Multi-domain]  Cd Length: 351  Bit Score: 95.83  E-value: 4.59e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 503 YVARAPGRLDVMGGIADYSGSLVLQMPIREACHVAIQRSNPmkqklwkhtqarqlangravpllqiVSFGSELSNRAPTF 582
Cdd:PRK03817    1 MKVKSPGRVNLIGEHTDYNDGYVLPFAINLYTFLEIEKSEK-------------------------FIFYSENFNEEKTF 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 583 DMDlsdfmdgdkpisydkakeyfSQDPSQKWAAYVAGTILVLMTELGVVftDSMSILVSSSVPEGKGVSSSASVEVASMS 662
Cdd:PRK03817   56 ELD--------------------KLEKLNSWADYIKGVIWVLEKRGYEV--GGVKGKVSSNLPIGAGLSSSASLEVAVAY 113

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 663 AIAAAYGLNIPPRDLAILCQKVENRIVGAPCGVMDQMTSACGEANKLLAMICQPAEVkELVSIPTHIRFWGLDSGIRHSV 742
Cdd:PRK03817  114 ALNEAYNLNLSKLELALLAREAENEFVGVPCGIMDQFAVAFGKKDHAIFLDTMTLEY-EYVPFPEDYEILVFDTGVKREL 192


                  ....*
gi 1002245207 743 GGTDY 747
Cdd:PRK03817  193 ASSEY 197
PRK05101 PRK05101
galactokinase; Provisional
 485-751 3.79e-18

galactokinase; Provisional


Pssm-ID: 179937 [Multi-domain]  Cd Length: 382  Bit Score: 87.67  E-value: 3.79e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 485 QSRERVAASVF---FDWEEEIYVaRAPGRLDVMGGIADYSGSLVLQMPIREACHVAIQRsnpmkqklwkhtqarqlangR 561
Cdd:PRK05101    1 MSLKQKTQSLFaqqFGYPPTHTI-QAPGRVNLIGEHTDYNDGFVLPCAIDYQTVISCAK--------------------R 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 562 AVPLLQIVSfgSELSNRAPTFDMDlsdfmdgdKPISYDkakeyfsqdPSQKWAAYVAGTILVLMtELGVVFTdSMSILVS 641
Cdd:PRK05101   60 DDRIVRVIA--ADYDNQQDEFSLD--------APIVPH---------PEQQWANYVRGVVKHLQ-ERNPDFG-GADLVIS 118

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 642 SSVPEGKGVSSSASVEVASMSAIAAAYGLNIPPRDLAILCQKVENRIVGAPCGVMDQMTSACGEANKLLAMICQPAEVkE 721
Cdd:PRK05101  119 GNVPQGAGLSSSASLEVAVGQTFQQLYHLPLSGAEIALNGQEAENQFVGCNCGIMDQLISALGKKDHALLIDCRSLET-K 197

                         250       260       270
                  ....*....|....*....|....*....|
gi 1002245207 722 LVSIPTHIRFWGLDSGIRHSVGGTDYGSVR 751
Cdd:PRK05101  198 AVPMPEGVAVVIINSNVKRGLVDSEYNTRR 227
PRK00555 PRK00555
galactokinase; Provisional
 507-773 9.68e-13

galactokinase; Provisional


Pssm-ID: 179063 [Multi-domain]  Cd Length: 363  Bit Score: 71.04  E-value: 9.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 507 APGRLDVMGGIADYSgsLVLQMPIreachvaiqrsnpmkqklwkhtqarqlangrAVPLLQIVSFGSELSNrAPTFDmdl 586
Cdd:PRK00555    7 APGRINLIGEHTDYN--LGFALPI-------------------------------ALPQRTVVTFTPEHTD-AITAS--- 49

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 587 SDFMDGDKPISYDKAkeyfsqdPSQ--KWAAYVAGTILVLMTELGVVFTDSMSIlvSSSVPEGKGVSSSASVEVASMSAI 664
Cdd:PRK00555   50 SDRADGSARIPLDTT-------PGQvtGWAAYAAGVIWALRGAGHPVPGGAMSI--TSDVEIGSGLSSSAALECAVLGAV 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 665 AAAYGLNIPPRDLAILCQKVENRIVGAPCGVMDQMTSACGEANKLLAMICQPAEVKELVSIP--THIRFWGLDSGIRHSV 742
Cdd:PRK00555  121 GAATGTRIDRLEQARLAQRAENEYVGAPTGLLDQLAALFGAPKTALLIDFRDLTVRPVAFDPdaAGVVLLLMDSRARHRH 200

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1002245207 743 GGTDYGSVRVGTymgrkmiKCAASDLLSESL 773
Cdd:PRK00555  201 AGGEYAARRASC-------ERAAADLGVSSL 224
GT1_Gtf-like cd03784
UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of ...
 26-345 7.78e-10

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: 62.18  E-value: 7.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207  26 LVFAYyitgHGFGHATRALEVVRHLIAAGHDVHVVTgaPEFVFTTEISSPNLHIRKVLLDCGAVQADALTVDRLASLEKY 105
Cdd:cd03784     4 LFVPF----PGQGHVNPMLPLAKALAARGHEVTVAT--PPFNFADLVEAAGLTFVPVGDDPDELELDSETNLGPDSLLEL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 106 HQTAVMPRESILRTEVE-WLNTIKADLVVSDVVPVACRAAADA-GIRSVCVTNFSWDFIYAEYVVVAGHHHRSIVWQIAE 183
Cdd:cd03784    78 LRRLLKAADELLDDLLAaLRSSWKPDLVIADPFAYAGPLVAEElGIPSVRLFTGPATLLSAYLHPFGVLNLLLSSLLEPE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 184 DYSH--CEFLLRL------------------------PGYCPMPAFRDVIDVPLVVRRLH------KSRSEVRKELGIKD 231
Cdd:cd03784   158 LFLDplLEVLDRLrerlglppfslvllllrlvpplyvIGPTFPSLPPDRPRLPSVLGGLRivpkngPLPDELWEWLDKQP 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 232 DVKVVIFNFG---------------------GQPAGWKLkkEWLPDGWLclvcgasetQELPPNfIKLAKDAytP--DLM 288
Cdd:cd03784   238 PRSVVYVSFGsmvrdlpeelleliaealaslGQRFLWVV--GPDPLGGL---------ERLPDN-VLVVKWV--PqdELL 303

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002245207 289 A--ASDCML--GkiGYGTVSEALAYKLPFVFVrrDYFNEEPFLRNMLEHYQCGVEMVRRDL 345
Cdd:cd03784   304 AhpAVGAFVthG--GWNSTLEALYAGVPMVVV--PLFADQPNNAARVEELGAGVELDKDEL 360
PRK05322 PRK05322
galactokinase; Provisional
 492-708 1.66e-09

galactokinase; Provisional


Pssm-ID: 235407 [Multi-domain]  Cd Length: 387  Bit Score: 61.03  E-value: 1.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 492 ASVFFDWEEEIYVAraPGRLDVMGGIADYSGSLVLQMPIREACHVAIQRSNPMKQKLWKhtqarqlANgraVPLLQIVSF 571
Cdd:PRK05322   11 AEVFGEEAEDVFFS--PGRINLIGEHTDYNGGHVFPAAITLGTYGAARKRDDKKVRLYS-------AN---FEDLGIIEF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 572 gselsnraptfdmDLSDfmdgdkpISYDKAKeyfsqdpsqKWAAYVAGTILVLMtELGVVFTDSMSILVSSSVPEGKGVS 651
Cdd:PRK05322   79 -------------DLDD-------LSFDKED---------DWANYPKGVLKFLQ-EAGYKIDHGFDILIYGNIPNGAGLS 128

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1002245207 652 SSASVEVASMSAIAAAYGLNIPPRDLAILCQKVENRIVGAPCGVMDQMTSACGEANK 708
Cdd:PRK05322  129 SSASIELLTGVILKDLFNLDLDRLELVKLGQKTENEFIGVNSGIMDQFAIGMGKKDH 185
GT28_MurG cd03785
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4. ...
 25-316 2.66e-08

undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4.1.227) is an N-acetylglucosaminyltransferase, the last enzyme involved in the intracellular phase of peptidoglycan biosynthesis. It transfers N-acetyl-D-glucosamine (GlcNAc) from UDP-GlcNAc to the C4 hydroxyl of a lipid-linked N-acetylmuramoyl pentapeptide (NAM). The resulting disaccharide is then transported across the cell membrane, where it is polymerized into NAG-NAM cell-wall repeat structure. MurG belongs to the GT-B structural superfamily of glycoslytransferases, which have characteristic N- and C-terminal domains, each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


Pssm-ID: 340818 [Multi-domain]  Cd Length: 350  Bit Score: 56.84  E-value: 2.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207  25 HLVFAyyiTGHGFGHATRALEVVRHLIAAGHDVHVVTGAPEFVFTTeISSPNLHIRKVlldcgavqaDALTVDRLASLEK 104
Cdd:cd03785     1 KILIA---GGGTGGHIFPALALAEELRKRGAEILFIGTKRGLEAKL-VPEAGIPFHTI---------PISGLRRKGSLKN 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 105 YhqTAVMPRESILRTEVEWLNTIKADLVVSDV----VPVaCRAAADAGIRSvcvtnfswdFIYAEYVV--VAGHHHRSIV 178
Cdd:cd03785    68 L--KAPFKLLKGLRQARKILRKFKPDVVIGFGgyvsGPV-VLAARLLGIPL---------IIHEQNAVpgLANRLLSRFA 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 179 WQIAEDYSHCEfllrlpgycPMPAFRDVIDVPLVVRRLHKSRSEVRKELGIKDDVKVVIFnFGG-QPAGW------KLKK 251
Cdd:cd03785   136 DKVAVSFPETK---------KYFPAAKVVVTGNPVREEILNLRKELKRFGLPPDKPTLLV-FGGsQGARAinravpKALP 205

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002245207 252 EWLPDGW-LCLVCGASETQELPPNFIKLAKDA----YT---PDLMAASDCMLGKIGYGTVSEALAYKLPFVFV 316
Cdd:cd03785   206 KLLERGIqVIHQTGKGDYDEVKKLYEDLGINVkvfpFIddmAAAYAAADLVISRAGASTIAELTAAGKPAILI 278
PLN02521 PLN02521
galactokinase
 469-896 4.12e-08

galactokinase


Pssm-ID: 215285 [Multi-domain]  Cd Length: 497  Bit Score: 57.02  E-value: 4.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 469 TSLSGLVGNDPRSPEKQSRERVAASVFfdweEEIY------VARAPGRLDVMGGIADYSGSLVLQMPIREACHVAIQRSN 542
Cdd:PLN02521   13 SSLEPVYGDGSLLEEARLRYARLKAAF----VEVYgakpdlFARSPGRVNLIGEHIDYEGYSVLPMAIRQDTIVAIRRAE 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 543 pmkqklwkhtqarqlangrAVPLLQIvsfgselSNRAPTFdmdlsdfmdgdkpisydKAKEyFSQDPSQ-------KWAA 615
Cdd:PLN02521   89 -------------------GSKKLRI-------ANVNDKY-----------------TTCT-FPADPDQevdlanhKWGN 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 616 YV----AGTILVLMTE-LGVVFTDSMSILVSSSVPEGKGVSSSASVEVASMSAIAAAYGLNIPPRDLAILCQKVEnRIVG 690
Cdd:PLN02521  125 YFicgyKGVFEFLKSKgVDVGPPVGLDVVVDGTVPTGSGLSSSAALVCSAAIAIMAALGLNFTKKEVAQFTCKCE-RHIG 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 691 APCGVMDQMTSACGEANkllamicqpaeVKELVSI-PTHIRFWGLDSG----IRHSVGGTDYGSVRVGTYMGRkMIKCA- 764
Cdd:PLN02521  204 TQSGGMDQAISIMAQQG-----------VAKLIDFnPVRATDVQLPAGgtfvIANSLAESNKAVTAATNYNNR-VVECRl 271

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 765 ASDLLSESL--PSCPPIQSGNTNSDeYEEHGVDLLKSEASLEYLCNLPPHRYEAVYARDIPEIITGDAFLEKYGDHNDAV 842
Cdd:PLN02521  272 AAIVLAVKLgmSAEEAISKVKTLSD-VEGLCVSFAGSHGSSDPAVAVKELLHEGPYTAEEIEEILGESLTSIFKNSPTSL 350

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1002245207 843 TTVDPKRSYCVKAPTRHPIYENFRVEAFKALLTAAKTVEQ-LSALGELMYQCHYS 896
Cdd:PLN02521  351 AVLKAAKHFKLHQRAVHVYSEAKRVHAFRDTVSSSLSEEEkLKKLGDLMNESHYS 405
GT28_Beta-DGS-like cd17507
beta-diglucosyldiacylglycerol synthase and similar proteins; beta-diglucosyldiacylglycerol ...
 201-317 1.09e-07

beta-diglucosyldiacylglycerol synthase and similar proteins; beta-diglucosyldiacylglycerol synthase (processive diacylglycerol beta-glucosyltransferase EC 2.4.1.315) is involved in the biosynthesis of both the bilayer- and non-bilayer-forming membrane glucolipids. This family of glycosyltransferases also contains plant major galactolipid synthase (chloroplastic monogalactosyldiacylglycerol synthase 1 EC 2.4.1.46). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


Pssm-ID: 340861 [Multi-domain]  Cd Length: 364  Bit Score: 55.02  E-value: 1.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 201 PAFRDVIDVPlvvrrlhksrsEVRKELGIKDDVKVVIFnFGGQPAGWKLKK------EWLPDGWLCLVCGASET-----Q 269
Cdd:cd17507   176 PSFAEVRDKD-----------EARNELNLSPDKPTVLL-MGGGGGMGPVKEtveallDSLRAGQVLVVCGKNKKlyeklS 243

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1002245207 270 ELPPNFIKLAKDAYT---PDLMAASDCMLGKIGYGTVSEALAYKLPFVFVR 317
Cdd:cd17507   244 GLEEDYINVRVLGYVddmNELMAASDLVITKPGGLTISEALARGLPVIIYD 294
PTZ00290 PTZ00290
galactokinase; Provisional
 500-751 4.64e-06

galactokinase; Provisional


Pssm-ID: 240347 [Multi-domain]  Cd Length: 468  Bit Score: 50.21  E-value: 4.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 500 EEIYVARAPGRLDVMGGIADYSGSLVLQMPIREACHVAIQRSnpmkqklwKHTQARQLangravpllqivSFGSElsnRA 579
Cdd:PTZ00290   35 EWLLFTFAPGRVNFIGEHVDYMGGYVCPAAVLEGCHILVGRV--------KHFCDHKL------------RFATE---TD 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 580 PTFDMDlsdFMDGDKpisYDKAkeyfsqdpsqkWAAYVAGTILVLMTELGVVFTDS----MSILVSSSVPEGKGVSSSAS 655
Cdd:PTZ00290   92 EHFVLD---HLGGAK---HNKA-----------WTTFVRGAATLRLNRLGVAIDAPslqgVCMVVHGTLPMGAGMSASAS 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 656 VEVASMSAIAAAYGLN------IPPRDLAIL--------------CQKVENRIVGAPCGVMDQMTSACGEANKLLAMICQ 715
Cdd:PTZ00290  155 FGVALLNAINTVVTRRykgcptSPGRRYSILppmskeelielakqARRIETEFCGVNVGIMDQFISAFAEEDKFMFLDCK 234

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1002245207 716 PA--EVKELVSIPTHIRFWGL-DSGIRHSV-GGTD--YGSVR 751
Cdd:PTZ00290  235 SLtfESHDMTPLLGDGACFLLiDSMIKHDLlGGTAgmYNTVR 276
GalKase_gal_bdg pfam10509
Galactokinase galactose-binding signature; This is the highly conserved galactokinase ...
 499-540 2.02e-05

Galactokinase galactose-binding signature; This is the highly conserved galactokinase signature sequence which appears to be present in all galactokinases irrespective of how many other ATP binding sites, etc that they carry. The function of this domain appears to be to bind galactose, and the domain is normally at the N-terminus of the enzymes, EC:2.7.1.6. This domain is associated with the families GHMP_kinases_C, pfam08544 and GHMP_kinases_N, pfam00288.


Pssm-ID: 463125 [Multi-domain]  Cd Length: 50  Bit Score: 42.82  E-value: 2.02e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1002245207 499 EEEIYVARAPGRLDVMGGIADYSGSLVLQMPIREACHVAIQR 540
Cdd:pfam10509   9 KEPVGVASAPGRVNLIGEHTDYNGGFVLPAAINLDTYVAVSP 50
YjiC COG1819
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism];
31-347 1.73e-04

UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism];


Pssm-ID: 441424 [Multi-domain]  Cd Length: 268  Bit Score: 44.46  E-value: 1.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207  31 YITGHGFGHATRALEVVRHLIAAGHDVHVVTGaPEFVftteisspnlhirkvlldcGAVQADALTVdrlaslekyhqtav 110
Cdd:COG1819     4 FVTLGGRGHVNPLLALARALRARGHEVTFATG-PDFA-------------------DLVEAAGLEF-------------- 49

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 111 mpresilrteVEWlntiKADLVVSDVVPVACRAAADA-GIRSVCVTnfswdfiyaeyvvvaghhhrsivwqiaedyshce 189
Cdd:COG1819    50 ----------VDW----RPDLVVSDPLALAAALAAEAlGIPVVSLT---------------------------------- 81

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 190 fllrlPGYCPMPAFRDVIDVPLVVRRLHKSRSEVRKELGIKDDVKVVIFNFGGQPAGWK---------LKKEwlpdGWLC 260
Cdd:COG1819    82 -----PPELEYPRPPDPANVRFVGPLLPDGPAELPPWLEEDAGRPLVYVTLGTSANDRAdllravleaLADL----GVRV 152

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 261 LVC----GASETQELPPNFIKLakdAYTP--DLMAASDCML--GkiGYGTVSEALAYKLPFVFVrrDYFNEEPFLRNMLE 332
Cdd:COG1819   153 VVTtgglDPAELGPLPDNVRVV---DYVPqdALLPRADAVVhhG--GAGTTAEALRAGVPQVVV--PFGGDQPLNAARVE 225

                         330
                  ....*....|....*
gi 1002245207 333 HYQCGVeMVRRDLLT 347
Cdd:COG1819   226 RLGAGL-ALPPRRLT 239
COG4671 COG4671
Predicted glycosyl transferase [General function prediction only];
36-65 2.50e-04

Predicted glycosyl transferase [General function prediction only];


Pssm-ID: 443708 [Multi-domain]  Cd Length: 391  Bit Score: 44.46  E-value: 2.50e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1002245207  36 GFGHATRALEVVRHLIAAGHDVHVVTGAPE 65
Cdd:COG4671    14 GLGHLRRSLAIARALVADGFSVLLISGGPP 43
Glyco_trans_1_3 pfam13528
Glycosyl transferase family 1;
30-61 8.77e-04

Glycosyl transferase family 1;


Pssm-ID: 404422  Cd Length: 321  Bit Score: 42.48  E-value: 8.77e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1002245207  30 YYITGHGFGHATRALEVVRHLiAAGHDVHVVT 61
Cdd:pfam13528   5 YGVVGEGMGHATRSRVVLEHL-VRGHEVHVVV 35
PLN02605 PLN02605
monogalactosyldiacylglycerol synthase
 218-312 1.40e-03

monogalactosyldiacylglycerol synthase


Pssm-ID: 215325 [Multi-domain]  Cd Length: 382  Bit Score: 42.26  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 218 KSRSEVRKELGIKDDVKVVIFNFGGQPAG----------WKLKKEWL--PDGWLCLVCGASET-QElppnfiKLAKDAYT 284
Cdd:PLN02605  191 RPKDELRRELGMDEDLPAVLLMGGGEGMGpleetaralgDSLYDKNLgkPIGQVVVICGRNKKlQS------KLESRDWK 264

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1002245207 285 PDL------------MAASDCMLGKIGYGTVSEALAYKLP 312
Cdd:PLN02605  265 IPVkvrgfvtnmeewMGACDCIITKAGPGTIAEALIRGLP 304
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 26-323 5.95e-03

phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.


Pssm-ID: 340831 [Multi-domain]  Cd Length: 366  Bit Score: 40.21  E-value: 5.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207  26 LVFAYYITGHGfGHATRALEVVRHLIAAGHDVHVVTGAPEFVFTTEISSPNLHIRKVLLDCGAVqadaltvdrlasleky 105
Cdd:cd03801     4 LLSPELPPPVG-GAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLR---------------- 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 106 hqtavmpRESILRTEVEWLNTIKADLVVS---DVVPVACRAAADAGIRSVCVTNfswDFIYAEYVVVAGHHHRSI--VWQ 180
Cdd:cd03801    67 -------ARRLLRELRPLLRLRKFDVVHAhglLAALLAALLALLLGAPLVVTLH---GAEPGRLLLLLAAERRLLarAEA 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 181 IAEDYSHC--------EFLLRLPGycpmPAFRDVIDVPLVVrRLHKSRSEVRKELGIKDDVKVVIFnFG------GQPAG 246
Cdd:cd03801   137 LLRRADAViavsealrDELRALGG----IPPEKIVVIPNGV-DLERFSPPLRRKLGIPPDRPVLLF-VGrlsprkGVDLL 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 247 ----WKLKKEWlpDGWLCLVCGASEtqELPPNFIKLAKDAY-------------TPDLMAASDCML-----GKIGYgTVS 304
Cdd:cd03801   211 lealAKLLRRG--PDVRLVIVGGDG--PLRAELEELELGLGdrvrflgfvpdeeLPALYAAADVFVlpsryEGFGL-VVL 285

                         330
                  ....*....|....*....
gi 1002245207 305 EALAYKLPFVFVRRDYFNE 323
Cdd:cd03801   286 EAMAAGLPVVATDVGGLPE 304
MurG COG0707
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope ...
 213-316 7.34e-03

UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440471 [Multi-domain]  Cd Length: 363  Bit Score: 39.73  E-value: 7.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245207 213 VRR--LHKSRSEVRKELGIKDDVKVVIFnFGG-QPAG------WKLKKEWLPDGW-LCLVCGASETQELPPNFIKLAKDA 282
Cdd:COG0707   164 VRKeiLELDRPEARAKLGLDPDKPTLLV-FGGsQGARalneavPAALAALLEARLqVVHQTGKGDYEEVRAAYAAAIRPN 242

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1002245207 283 YT--------PDLMAASDCMLGKIGYGTVSEALAYKLPFVFV 316
Cdd:COG0707   243 AEvfpfiddmADAYAAADLVISRAGASTVAELAALGKPAILV 284
 
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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