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Conserved domains on  [gi|15241313|ref|NP_197528|]
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sucrose phosphate synthase 1F [Arabidopsis thaliana]

Protein Classification

sucrsPsyn_pln family protein( domain architecture ID 11494298)

sucrsPsyn_pln family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
sucrsPsyn_pln TIGR02468
sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this ...
1-1039 0e+00

sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this family are sucrose-phosphate synthases of plants. This enzyme is known to exist in multigene families in several species of both monocots and dicots. The N-terminal domain is the glucosyltransferase domain. Members of this family also have a variable linker region and a C-terminal domain that resembles sucrose phosphate phosphatase (SPP) (EC 3.1.3.24) (see TIGR01485), the next and final enzyme of sucrose biosynthesis. The SPP-like domain likely serves a binding and not a catalytic function, as the reported SPP is always encoded by a distinct protein.


:

Pssm-ID: 274147 [Multi-domain]  Cd Length: 1050  Bit Score: 2117.92  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313      1 MAGNDWVNSYLEAILDVGQGLDDARSSPSLLLRERGRFTPSRYFVEEVITGYDETDLHRSWVKAVATRSPQERNTRLENM 80
Cdd:TIGR02468    1 MAGNDWINSYLEAILDVGPGLDDAKSSALLLLRERGRFSPTRYFVEEVITGFDETDLHRTWVKAVATRSPQERNTRLENM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313     81 CWRIWNLARQKKQHEEKEAQRLAKRRLEREKGRREATADMSEEFSEGEKGDIISDISTHG--ESTKPRLPRINSAESMEL 158
Cdd:TIGR02468   81 CWRIWNLARKKKQLEWEEAQRLAKRRLERERGRREATADMSEDLSEGEKGDVAGDISVAGgePSTKGRLPRISSNLEMET 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313    159 WASQQKGNKLYLVLISLHGLIRGENMELGRDSDTGGQVKYVVELARALGSMPGVYRVDLLTRQVSSPDVDYSYGEPTEML 238
Cdd:TIGR02468  161 WSDQQKEKKLYIVLISLHGLVRGENMELGRDSDTGGQVKYVVELARALGSMPGVYRVDLLTRQVSSPDVDWSYGEPTEML 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313    239 TPRDSEDFSDEMGESSGAYIVRIPFGPKDKYIPKELLWPHIPEFVDGAMSHIMQMSNVLGEQVGVGKPIWPSAIHGHYAD 318
Cdd:TIGR02468  241 TPRSSENDGDEMGESSGAYIIRIPFGPRDKYIPKEELWPYIPEFVDGALSHIVNMSKVLGEQIGSGHPVWPYVIHGHYAD 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313    319 AGDATALLSGALNVPMLLTGHSLGRDKLEQLLRQGRLSKEEINSTYKIMRRIEGEELSLDVSEMVITSTRQEIDEQWRLY 398
Cdd:TIGR02468  321 AGDSAALLSGALNVPMVLTGHSLGRDKLEQLLKQGRMSKEEINSTYKIMRRIEAEELSLDASEIVITSTRQEIEEQWGLY 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313    399 DGFDPILERKLRARIKRNVSCYGRFMPRMVKIPPGMEFNHIVPHGGDME-DTDGNEEHPTSPDPPIWAEIMRFFSNSRKP 477
Cdd:TIGR02468  401 DGFDVILERKLRARARRGVSCYGRFMPRMAVIPPGMEFSHIVPHDGDMDgETEGNEEHPAKPDPPIWSEIMRFFTNPRKP 480
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313    478 MILALARPDPKKNITTLVKAFGECRPLRELANLALIMGNRDGIDEMSSTSSSVLLSVLKLIDKYDLYGQVAYPKHHKQSD 557
Cdd:TIGR02468  481 MILALARPDPKKNITTLVKAFGECRPLRELANLTLIMGNRDDIDEMSSGSSSVLTSVLKLIDKYDLYGQVAYPKHHKQSD 560
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313    558 VPDIYRLAAKSKGVFINPAIIEPFGLTLIEAAAHGLPMVATKNGGPVDIHRVLDNGLLVDPHDQQSISEALLKLVADKHL 637
Cdd:TIGR02468  561 VPDIYRLAAKTKGVFINPAFIEPFGLTLIEAAAHGLPMVATKNGGPVDIHRVLDNGLLVDPHDQQAIADALLKLVADKQL 640
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313    638 WAKCRQNGLKNIHQFSWPEHCKTYLSRITSFKPRHPQWQSD--DGGDNSEPESPSDSLRDIQDISLNLKFSFDGSGNDNY 715
Cdd:TIGR02468  641 WAECRQNGLKNIHLFSWPEHCKTYLSRIASCRPRHPQWQRDtdDGEEASEDESPGDSLRDIQDISLNLSVDGDKESNNGS 720
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313    716 MNQEGS--SMDRKSKIEAAVQNWSKGKDsrkmGSLERSEVNSG--KFPAVRRRKFIVVIALDFDGEEDTLEATKRILDAV 791
Cdd:TIGR02468  721 SNVEGSgpPADRVAKIENAVRSWSKSPK----GSSAKAQQGSGagKYPALRRRKRLFVIAVDCYDDKDLLQIIKNIFEAV 796
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313    792 EKERAEGSVGFILSTSLTISEVQSFLVSGGLNPNDFDAFICNSGSDLHYTSLN-NEDGPFVVDFYYHSHIEYRWGGEGLR 870
Cdd:TIGR02468  797 RKERMEGSSGFILSTSMTISEIQSFLKSGGLNPTDFDALICNSGSELYYPSLNgSEEGKLVADQDYHSHIEYRWGGEGLR 876
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313    871 KTLIRWASSLNEKKADNDEQIVTLAEHLSTDYCYTFTVKKPAAVPPVRELRKLLRIQALRCHVVYSQNGTRINVIPVLAS 950
Cdd:TIGR02468  877 KTLVKWAASINEKKGENEEQIVEEDEESSTDHCYAFKVKDPSKVPPVKELRKLLRIQGLRCHAVYCRNGTRLNVIPLLAS 956
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313    951 RIQALRYLFVRWGIDMAKMAVFVGESGDTDYEGLLGGLHKSVVLKGVS--CSACLHANRSYPLTDVISFESNNVVHAS-- 1026
Cdd:TIGR02468  957 RSQALRYLFVRWGIELANMAVFVGESGDTDYEGLLGGLHKTVILKGVVsrGSEQLHANRSYPLDDVVPLDSPNIVQATgg 1036
                         1050
                   ....*....|....
gi 15241313   1027 -PDSDVRDALKKLE 1039
Cdd:TIGR02468 1037 sSSDDISDALKKLS 1050
 
Name Accession Description Interval E-value
sucrsPsyn_pln TIGR02468
sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this ...
1-1039 0e+00

sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this family are sucrose-phosphate synthases of plants. This enzyme is known to exist in multigene families in several species of both monocots and dicots. The N-terminal domain is the glucosyltransferase domain. Members of this family also have a variable linker region and a C-terminal domain that resembles sucrose phosphate phosphatase (SPP) (EC 3.1.3.24) (see TIGR01485), the next and final enzyme of sucrose biosynthesis. The SPP-like domain likely serves a binding and not a catalytic function, as the reported SPP is always encoded by a distinct protein.


Pssm-ID: 274147 [Multi-domain]  Cd Length: 1050  Bit Score: 2117.92  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313      1 MAGNDWVNSYLEAILDVGQGLDDARSSPSLLLRERGRFTPSRYFVEEVITGYDETDLHRSWVKAVATRSPQERNTRLENM 80
Cdd:TIGR02468    1 MAGNDWINSYLEAILDVGPGLDDAKSSALLLLRERGRFSPTRYFVEEVITGFDETDLHRTWVKAVATRSPQERNTRLENM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313     81 CWRIWNLARQKKQHEEKEAQRLAKRRLEREKGRREATADMSEEFSEGEKGDIISDISTHG--ESTKPRLPRINSAESMEL 158
Cdd:TIGR02468   81 CWRIWNLARKKKQLEWEEAQRLAKRRLERERGRREATADMSEDLSEGEKGDVAGDISVAGgePSTKGRLPRISSNLEMET 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313    159 WASQQKGNKLYLVLISLHGLIRGENMELGRDSDTGGQVKYVVELARALGSMPGVYRVDLLTRQVSSPDVDYSYGEPTEML 238
Cdd:TIGR02468  161 WSDQQKEKKLYIVLISLHGLVRGENMELGRDSDTGGQVKYVVELARALGSMPGVYRVDLLTRQVSSPDVDWSYGEPTEML 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313    239 TPRDSEDFSDEMGESSGAYIVRIPFGPKDKYIPKELLWPHIPEFVDGAMSHIMQMSNVLGEQVGVGKPIWPSAIHGHYAD 318
Cdd:TIGR02468  241 TPRSSENDGDEMGESSGAYIIRIPFGPRDKYIPKEELWPYIPEFVDGALSHIVNMSKVLGEQIGSGHPVWPYVIHGHYAD 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313    319 AGDATALLSGALNVPMLLTGHSLGRDKLEQLLRQGRLSKEEINSTYKIMRRIEGEELSLDVSEMVITSTRQEIDEQWRLY 398
Cdd:TIGR02468  321 AGDSAALLSGALNVPMVLTGHSLGRDKLEQLLKQGRMSKEEINSTYKIMRRIEAEELSLDASEIVITSTRQEIEEQWGLY 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313    399 DGFDPILERKLRARIKRNVSCYGRFMPRMVKIPPGMEFNHIVPHGGDME-DTDGNEEHPTSPDPPIWAEIMRFFSNSRKP 477
Cdd:TIGR02468  401 DGFDVILERKLRARARRGVSCYGRFMPRMAVIPPGMEFSHIVPHDGDMDgETEGNEEHPAKPDPPIWSEIMRFFTNPRKP 480
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313    478 MILALARPDPKKNITTLVKAFGECRPLRELANLALIMGNRDGIDEMSSTSSSVLLSVLKLIDKYDLYGQVAYPKHHKQSD 557
Cdd:TIGR02468  481 MILALARPDPKKNITTLVKAFGECRPLRELANLTLIMGNRDDIDEMSSGSSSVLTSVLKLIDKYDLYGQVAYPKHHKQSD 560
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313    558 VPDIYRLAAKSKGVFINPAIIEPFGLTLIEAAAHGLPMVATKNGGPVDIHRVLDNGLLVDPHDQQSISEALLKLVADKHL 637
Cdd:TIGR02468  561 VPDIYRLAAKTKGVFINPAFIEPFGLTLIEAAAHGLPMVATKNGGPVDIHRVLDNGLLVDPHDQQAIADALLKLVADKQL 640
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313    638 WAKCRQNGLKNIHQFSWPEHCKTYLSRITSFKPRHPQWQSD--DGGDNSEPESPSDSLRDIQDISLNLKFSFDGSGNDNY 715
Cdd:TIGR02468  641 WAECRQNGLKNIHLFSWPEHCKTYLSRIASCRPRHPQWQRDtdDGEEASEDESPGDSLRDIQDISLNLSVDGDKESNNGS 720
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313    716 MNQEGS--SMDRKSKIEAAVQNWSKGKDsrkmGSLERSEVNSG--KFPAVRRRKFIVVIALDFDGEEDTLEATKRILDAV 791
Cdd:TIGR02468  721 SNVEGSgpPADRVAKIENAVRSWSKSPK----GSSAKAQQGSGagKYPALRRRKRLFVIAVDCYDDKDLLQIIKNIFEAV 796
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313    792 EKERAEGSVGFILSTSLTISEVQSFLVSGGLNPNDFDAFICNSGSDLHYTSLN-NEDGPFVVDFYYHSHIEYRWGGEGLR 870
Cdd:TIGR02468  797 RKERMEGSSGFILSTSMTISEIQSFLKSGGLNPTDFDALICNSGSELYYPSLNgSEEGKLVADQDYHSHIEYRWGGEGLR 876
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313    871 KTLIRWASSLNEKKADNDEQIVTLAEHLSTDYCYTFTVKKPAAVPPVRELRKLLRIQALRCHVVYSQNGTRINVIPVLAS 950
Cdd:TIGR02468  877 KTLVKWAASINEKKGENEEQIVEEDEESSTDHCYAFKVKDPSKVPPVKELRKLLRIQGLRCHAVYCRNGTRLNVIPLLAS 956
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313    951 RIQALRYLFVRWGIDMAKMAVFVGESGDTDYEGLLGGLHKSVVLKGVS--CSACLHANRSYPLTDVISFESNNVVHAS-- 1026
Cdd:TIGR02468  957 RSQALRYLFVRWGIELANMAVFVGESGDTDYEGLLGGLHKTVILKGVVsrGSEQLHANRSYPLDDVVPLDSPNIVQATgg 1036
                         1050
                   ....*....|....
gi 15241313   1027 -PDSDVRDALKKLE 1039
Cdd:TIGR02468 1037 sSSDDISDALKKLS 1050
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
169-663 1.98e-149

sucrose-phosphate synthase and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. The sucrose-phosphate synthases in this family may be unique to plants and photosynthetic bacteria. This enzyme catalyzes the synthesis of sucrose 6-phosphate from fructose 6-phosphate and uridine 5'-diphosphate-glucose, a key regulatory step of sucrose metabolism. The activity of this enzyme is regulated by phosphorylation and moderated by the concentration of various metabolites and light.


Pssm-ID: 340830 [Multi-domain]  Cd Length: 398  Bit Score: 450.54  E-value: 1.98e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  169 YLVLISLHGLIRGENMElgrdSDTGGQVKYVVELARALgsMPGVYRVDLLTRQVSSPDVDysygeptemltprdsedfsd 248
Cdd:cd03800    1 RIALISVHGSPLAQPGG----ADTGGQNVYVLELARAL--AELGYQVDIFTRRISPADPE-------------------- 54
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  249 EMGESSGAYIVRIPFGPKDkYIPKELLWPHIPEFVDGAMSHIMQMsnvlgeqvgvgkPIWPSAIHGHYADAGDATALLSG 328
Cdd:cd03800   55 VVEIAPGARVIRVPAGPPE-YLPKEELWPYLEEFADGLLRFIARE------------GGRYDLIHSHYWDSGLVGALLAR 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  329 ALNVPMLLTGHSLGRDKLEQLLRQGrlskeeinsTYKIMRRIEGEELSLDVSEMVITSTRQEIDEQWRLYDGFDPilerk 408
Cdd:cd03800  122 RLGVPLVHTFHSLGRVKYRHLGAQD---------TYHPSLRITAEEQILEAADRVIASTPQEADELISLYGADPS----- 187
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  409 lrarikrnvscygrfmpRMVKIPPGMEFNHIVPHGGDMedtdgneehptspdppiwAEIMRFFSNSRKPMILALARPDPK 488
Cdd:cd03800  188 -----------------RINVVPPGVDLERFFPVDRAE------------------ARRARLLLPPDKPVVLALGRLDPR 232
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  489 KNITTLVKAFGECRPLRELANLALIMGNRDGIDEMSSTSSSVLLSVLKLIDKYDlygqvaYPKHHKQSDVPDIYRLAaks 568
Cdd:cd03800  233 KGIDTLVRAFAQLPELRELANLVLVGGPSDDPLSMDREELAELAEELGLIDRVR------FPGRVSRDDLPELYRAA--- 303
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  569 kGVFINPAIIEPFGLTLIEAAAHGLPMVATKNGGPVDIHRVLDNGLLVDPHDQQSISEALLKLVADKHLWAKCRQNGLKN 648
Cdd:cd03800  304 -DVFVVPSLYEPFGLTAIEAMACGTPVVATAVGGLQDIVRDGRTGLLVDPHDPEALAAALRRLLDDPALWQRLSRAGLER 382
                        490
                 ....*....|....*.
gi 15241313  649 IHQ-FSWPEHCKTYLS 663
Cdd:cd03800  383 ARAhYTWESVADQLLT 398
PLN00142 PLN00142
sucrose synthase
171-665 1.75e-29

sucrose synthase


Pssm-ID: 215073 [Multi-domain]  Cd Length: 815  Bit Score: 126.63  E-value: 1.75e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313   171 VLISLHGLIRGENMeLGRdSDTGGQVKYVVELARALGSmpgvyrvDLLTR-QVSSPDVDYSYGEPTEMLTPRDSEDFSDE 249
Cdd:PLN00142  283 VIFSPHGYFGQANV-LGL-PDTGGQVVYILDQVRALEN-------EMLLRiKQQGLDIKPQILIVTRLIPDAKGTTCNQR 353
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313   250 MGESSG---AYIVRIPFGPKDKYIPKEL----LWPHIPEFVDGAMSHImqmsnvLGEQVGVgkpiwPSAIHGHYADAGDA 322
Cdd:PLN00142  354 LEKVSGtehSHILRVPFRTEKGILRKWIsrfdVWPYLETFAEDAASEI------LAELQGK-----PDLIIGNYSDGNLV 422
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313   323 TALLSGALNVPMLLTGHSLGRDKLEQllrqGRLSKEEINSTYKIMRRIEGEELSLDVSEMVITSTRQEIdeqwrlydgfd 402
Cdd:PLN00142  423 ASLLAHKLGVTQCTIAHALEKTKYPD----SDIYWKKFDDKYHFSCQFTADLIAMNHADFIITSTYQEI----------- 487
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313   403 pilerklrARIKRNVSCY---GRF-MPRMVKIPPGME-----FNhIVPHGGDME------------------------DT 449
Cdd:PLN00142  488 --------AGSKDTVGQYeshTAFtLPGLYRVVHGIDvfdpkFN-IVSPGADMSiyfpytekqkrltslhpsieellySP 558
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313   450 DGNEEHptspdppiwaeiMRFFSNSRKPMILALARPDPKKNITTLVKAFGECRPLRELANLALIMGNRDG---------- 519
Cdd:PLN00142  559 EQNDEH------------IGYLKDRKKPIIFSMARLDRVKNLTGLVEWYGKNKRLRELVNLVVVGGFIDPskskdreeia 626
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313   520 -IDEMSSTsssvllsvlklIDKYDLYGQVAYPKhhKQSDVP---DIYRLAAKSKGVFINPAIIEPFGLTLIEAAAHGLPM 595
Cdd:PLN00142  627 eIKKMHSL-----------IEKYNLKGQFRWIA--AQTNRVrngELYRYIADTKGAFVQPALYEAFGLTVVEAMTCGLPT 693
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15241313   596 VATKNGGPVDI--HRVldNGLLVDPHDQQSISEALL----KLVADKHLWAKCRQNGLKNIHQ-FSWpehcKTYLSRI 665
Cdd:PLN00142  694 FATCQGGPAEIivDGV--SGFHIDPYHGDEAANKIAdffeKCKEDPSYWNKISDAGLQRIYEcYTW----KIYAERL 764
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
476-647 3.85e-22

Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.


Pssm-ID: 425737 [Multi-domain]  Cd Length: 158  Bit Score: 93.88  E-value: 3.85e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313    476 KPMILALARPDPKKNITTLVKAFGECRPLRELANLaLIMGNRDGIDEMSSTsssvllsvlklIDKYDLYGQVAYPKHHKQ 555
Cdd:pfam00534    2 KKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKL-VIAGDGEEEKRLKKL-----------AEKLGLGDNVIFLGFVSD 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313    556 SDVPDIYRLAakskGVFINPAIIEPFGLTLIEAAAHGLPMVATKNGGPVDIHRVLDNGLLVDPHDQQSISEALLKLVADK 635
Cdd:pfam00534   70 EDLPELLKIA----DVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKLLEDE 145
                          170
                   ....*....|..
gi 15241313    636 HLWAKCRQNGLK 647
Cdd:pfam00534  146 ELRERLGENARK 157
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
561-663 1.36e-21

Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 91.21  E-value: 1.36e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  561 IYRLAakskGVFINPAIIEPFGLTLIEAAAHGLPMVATKNGGPVDIHRVLDNGLLVDPHDQQSISEALLKLVADKHLWAK 640
Cdd:COG0438   17 LLAAA----DVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLEDPELRRR 92
                         90       100
                 ....*....|....*....|....
gi 15241313  641 CRQNGLKNI-HQFSWPEHCKTYLS 663
Cdd:COG0438   93 LGEAARERAeERFSWEAIAERLLA 116
 
Name Accession Description Interval E-value
sucrsPsyn_pln TIGR02468
sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this ...
1-1039 0e+00

sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this family are sucrose-phosphate synthases of plants. This enzyme is known to exist in multigene families in several species of both monocots and dicots. The N-terminal domain is the glucosyltransferase domain. Members of this family also have a variable linker region and a C-terminal domain that resembles sucrose phosphate phosphatase (SPP) (EC 3.1.3.24) (see TIGR01485), the next and final enzyme of sucrose biosynthesis. The SPP-like domain likely serves a binding and not a catalytic function, as the reported SPP is always encoded by a distinct protein.


Pssm-ID: 274147 [Multi-domain]  Cd Length: 1050  Bit Score: 2117.92  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313      1 MAGNDWVNSYLEAILDVGQGLDDARSSPSLLLRERGRFTPSRYFVEEVITGYDETDLHRSWVKAVATRSPQERNTRLENM 80
Cdd:TIGR02468    1 MAGNDWINSYLEAILDVGPGLDDAKSSALLLLRERGRFSPTRYFVEEVITGFDETDLHRTWVKAVATRSPQERNTRLENM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313     81 CWRIWNLARQKKQHEEKEAQRLAKRRLEREKGRREATADMSEEFSEGEKGDIISDISTHG--ESTKPRLPRINSAESMEL 158
Cdd:TIGR02468   81 CWRIWNLARKKKQLEWEEAQRLAKRRLERERGRREATADMSEDLSEGEKGDVAGDISVAGgePSTKGRLPRISSNLEMET 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313    159 WASQQKGNKLYLVLISLHGLIRGENMELGRDSDTGGQVKYVVELARALGSMPGVYRVDLLTRQVSSPDVDYSYGEPTEML 238
Cdd:TIGR02468  161 WSDQQKEKKLYIVLISLHGLVRGENMELGRDSDTGGQVKYVVELARALGSMPGVYRVDLLTRQVSSPDVDWSYGEPTEML 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313    239 TPRDSEDFSDEMGESSGAYIVRIPFGPKDKYIPKELLWPHIPEFVDGAMSHIMQMSNVLGEQVGVGKPIWPSAIHGHYAD 318
Cdd:TIGR02468  241 TPRSSENDGDEMGESSGAYIIRIPFGPRDKYIPKEELWPYIPEFVDGALSHIVNMSKVLGEQIGSGHPVWPYVIHGHYAD 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313    319 AGDATALLSGALNVPMLLTGHSLGRDKLEQLLRQGRLSKEEINSTYKIMRRIEGEELSLDVSEMVITSTRQEIDEQWRLY 398
Cdd:TIGR02468  321 AGDSAALLSGALNVPMVLTGHSLGRDKLEQLLKQGRMSKEEINSTYKIMRRIEAEELSLDASEIVITSTRQEIEEQWGLY 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313    399 DGFDPILERKLRARIKRNVSCYGRFMPRMVKIPPGMEFNHIVPHGGDME-DTDGNEEHPTSPDPPIWAEIMRFFSNSRKP 477
Cdd:TIGR02468  401 DGFDVILERKLRARARRGVSCYGRFMPRMAVIPPGMEFSHIVPHDGDMDgETEGNEEHPAKPDPPIWSEIMRFFTNPRKP 480
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313    478 MILALARPDPKKNITTLVKAFGECRPLRELANLALIMGNRDGIDEMSSTSSSVLLSVLKLIDKYDLYGQVAYPKHHKQSD 557
Cdd:TIGR02468  481 MILALARPDPKKNITTLVKAFGECRPLRELANLTLIMGNRDDIDEMSSGSSSVLTSVLKLIDKYDLYGQVAYPKHHKQSD 560
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313    558 VPDIYRLAAKSKGVFINPAIIEPFGLTLIEAAAHGLPMVATKNGGPVDIHRVLDNGLLVDPHDQQSISEALLKLVADKHL 637
Cdd:TIGR02468  561 VPDIYRLAAKTKGVFINPAFIEPFGLTLIEAAAHGLPMVATKNGGPVDIHRVLDNGLLVDPHDQQAIADALLKLVADKQL 640
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313    638 WAKCRQNGLKNIHQFSWPEHCKTYLSRITSFKPRHPQWQSD--DGGDNSEPESPSDSLRDIQDISLNLKFSFDGSGNDNY 715
Cdd:TIGR02468  641 WAECRQNGLKNIHLFSWPEHCKTYLSRIASCRPRHPQWQRDtdDGEEASEDESPGDSLRDIQDISLNLSVDGDKESNNGS 720
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313    716 MNQEGS--SMDRKSKIEAAVQNWSKGKDsrkmGSLERSEVNSG--KFPAVRRRKFIVVIALDFDGEEDTLEATKRILDAV 791
Cdd:TIGR02468  721 SNVEGSgpPADRVAKIENAVRSWSKSPK----GSSAKAQQGSGagKYPALRRRKRLFVIAVDCYDDKDLLQIIKNIFEAV 796
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313    792 EKERAEGSVGFILSTSLTISEVQSFLVSGGLNPNDFDAFICNSGSDLHYTSLN-NEDGPFVVDFYYHSHIEYRWGGEGLR 870
Cdd:TIGR02468  797 RKERMEGSSGFILSTSMTISEIQSFLKSGGLNPTDFDALICNSGSELYYPSLNgSEEGKLVADQDYHSHIEYRWGGEGLR 876
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313    871 KTLIRWASSLNEKKADNDEQIVTLAEHLSTDYCYTFTVKKPAAVPPVRELRKLLRIQALRCHVVYSQNGTRINVIPVLAS 950
Cdd:TIGR02468  877 KTLVKWAASINEKKGENEEQIVEEDEESSTDHCYAFKVKDPSKVPPVKELRKLLRIQGLRCHAVYCRNGTRLNVIPLLAS 956
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313    951 RIQALRYLFVRWGIDMAKMAVFVGESGDTDYEGLLGGLHKSVVLKGVS--CSACLHANRSYPLTDVISFESNNVVHAS-- 1026
Cdd:TIGR02468  957 RSQALRYLFVRWGIELANMAVFVGESGDTDYEGLLGGLHKTVILKGVVsrGSEQLHANRSYPLDDVVPLDSPNIVQATgg 1036
                         1050
                   ....*....|....
gi 15241313   1027 -PDSDVRDALKKLE 1039
Cdd:TIGR02468 1037 sSSDDISDALKKLS 1050
sucr_P_syn_N TIGR02472
sucrose-phosphate synthase, putative, glycosyltransferase domain; This family consists of the ...
168-666 1.74e-178

sucrose-phosphate synthase, putative, glycosyltransferase domain; This family consists of the N-terminal regions, or in some cases the entirety, of bacterial proteins closely related to plant sucrose-phosphate synthases (SPS). The C-terminal domain (TIGR02471), found with most members of this family, resembles both bona fide plant sucrose-phosphate phosphatases (SPP) and the SPP-like domain of plant SPS. At least two members of this family lack the SPP-like domain, which may have binding or regulatory rather than enzymatic activity by analogy to plant SPS. This enzyme produces sucrose 6-phosphate and UDP from UDP-glucose and D-fructose 6-phosphate, and may be encoded near the gene for fructokinase.


Pssm-ID: 131525 [Multi-domain]  Cd Length: 439  Bit Score: 527.37  E-value: 1.74e-178
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313    168 LYLVLISLHGLIRGENMELGRDSDTGGQVKYVVELARALGSMPGVYRVDLLTRQVSSPDVDYSYGEPTEMLTPrdsedfs 247
Cdd:TIGR02472    1 LYLLLLSLHGLIRGHDLELGRDADTGGQTKYVLELARALARRSEVEQVDLVTRLIKDAKVSPDYAQPIERIAP------- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313    248 demgessGAYIVRIPFGPKdKYIPKELLWPHIPEFVDGAMSHIMQMSNVlgeqvgvgkpiwPSAIHGHYADAGDATALLS 327
Cdd:TIGR02472   74 -------GARIVRLPFGPR-RYLRKELLWPYLDELADNLLQHLRQQGHL------------PDLIHAHYADAGYVGARLS 133
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313    328 GALNVPMLLTGHSLGRDKLEQLLRQGrLSKEEINSTYKIMRRIEGEELSLDVSEMVITSTRQEIDEQWRLYDGFDPiler 407
Cdd:TIGR02472  134 RLLGVPLIFTGHSLGREKRRRLLAAG-LKPQQIEKQYNISRRIEAEEETLAHASLVITSTHQEIEEQYALYDSYQP---- 208
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313    408 klrarikrnvscygrfmPRMVKIPPGMEFNHIVPhggdmedtdgneEHPTSPDPPIWAEIMRFFSNSRKPMILALARPDP 487
Cdd:TIGR02472  209 -----------------ERMQVIPPGVDLSRFYP------------PQSSEETSEIDNLLAPFLKDPEKPPILAISRPDR 259
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313    488 KKNITTLVKAFGECRPLRELANLALIMGNRDGIDEMSSTSSSVLLSVLKLIDKYDLYGQVAYPKHHKQSDVPDIYRLAAK 567
Cdd:TIGR02472  260 RKNIPSLVEAYGRSPKLQEMANLVLVLGCRDDIRKMESQQREVLQKVLLLIDRYDLYGKVAYPKHHRPDDVPELYRLAAR 339
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313    568 SKGVFINPAIIEPFGLTLIEAAAHGLPMVATKNGGPVDIHRVLDNGLLVDPHDQQSISEALLKLVADKHLWAKCRQNGLK 647
Cdd:TIGR02472  340 SRGIFVNPALTEPFGLTLLEAAACGLPIVATDDGGPRDIIANCRNGLLVDVLDLEAIASALEDALSDSSQWQLWSRNGIE 419
                          490       500
                   ....*....|....*....|
gi 15241313    648 NIH-QFSWPEHCKTYLSRIT 666
Cdd:TIGR02472  420 GVRrHYSWDAHVEKYLRILQ 439
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
169-663 1.98e-149

sucrose-phosphate synthase and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. The sucrose-phosphate synthases in this family may be unique to plants and photosynthetic bacteria. This enzyme catalyzes the synthesis of sucrose 6-phosphate from fructose 6-phosphate and uridine 5'-diphosphate-glucose, a key regulatory step of sucrose metabolism. The activity of this enzyme is regulated by phosphorylation and moderated by the concentration of various metabolites and light.


Pssm-ID: 340830 [Multi-domain]  Cd Length: 398  Bit Score: 450.54  E-value: 1.98e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  169 YLVLISLHGLIRGENMElgrdSDTGGQVKYVVELARALgsMPGVYRVDLLTRQVSSPDVDysygeptemltprdsedfsd 248
Cdd:cd03800    1 RIALISVHGSPLAQPGG----ADTGGQNVYVLELARAL--AELGYQVDIFTRRISPADPE-------------------- 54
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  249 EMGESSGAYIVRIPFGPKDkYIPKELLWPHIPEFVDGAMSHIMQMsnvlgeqvgvgkPIWPSAIHGHYADAGDATALLSG 328
Cdd:cd03800   55 VVEIAPGARVIRVPAGPPE-YLPKEELWPYLEEFADGLLRFIARE------------GGRYDLIHSHYWDSGLVGALLAR 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  329 ALNVPMLLTGHSLGRDKLEQLLRQGrlskeeinsTYKIMRRIEGEELSLDVSEMVITSTRQEIDEQWRLYDGFDPilerk 408
Cdd:cd03800  122 RLGVPLVHTFHSLGRVKYRHLGAQD---------TYHPSLRITAEEQILEAADRVIASTPQEADELISLYGADPS----- 187
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  409 lrarikrnvscygrfmpRMVKIPPGMEFNHIVPHGGDMedtdgneehptspdppiwAEIMRFFSNSRKPMILALARPDPK 488
Cdd:cd03800  188 -----------------RINVVPPGVDLERFFPVDRAE------------------ARRARLLLPPDKPVVLALGRLDPR 232
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  489 KNITTLVKAFGECRPLRELANLALIMGNRDGIDEMSSTSSSVLLSVLKLIDKYDlygqvaYPKHHKQSDVPDIYRLAaks 568
Cdd:cd03800  233 KGIDTLVRAFAQLPELRELANLVLVGGPSDDPLSMDREELAELAEELGLIDRVR------FPGRVSRDDLPELYRAA--- 303
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  569 kGVFINPAIIEPFGLTLIEAAAHGLPMVATKNGGPVDIHRVLDNGLLVDPHDQQSISEALLKLVADKHLWAKCRQNGLKN 648
Cdd:cd03800  304 -DVFVVPSLYEPFGLTAIEAMACGTPVVATAVGGLQDIVRDGRTGLLVDPHDPEALAAALRRLLDDPALWQRLSRAGLER 382
                        490
                 ....*....|....*.
gi 15241313  649 IHQ-FSWPEHCKTYLS 663
Cdd:cd03800  383 ARAhYTWESVADQLLT 398
HAD_SPS cd16419
sucrose-phosphate synthase; belongs to the haloalcanoic acid dehalogenase (HAD) superfamily; ...
767-997 2.03e-81

sucrose-phosphate synthase; belongs to the haloalcanoic acid dehalogenase (HAD) superfamily; Sucrose phosphate synthase (SPS; EC 2.4.1.14) also known as UDP-glucose-fructose-phosphate glucosyltransferase, catalyzes the transfer of a hexosyl group from UDP-glucose to D-fructose 6-phosphate to form UDP and D-sucrose-6-phosphate, this is the rate limiting step of sucrose synthesis. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319856  Cd Length: 174  Bit Score: 261.79  E-value: 2.03e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  767 IVVIALDFDGEED--TLEATKRILDAVEKERAEGSVGFILSTSLTISEVQSFLVSGGLNPNDFDAFICNSGSDLHYTSLN 844
Cdd:cd16419    1 LFVIAVDCYDSSGlpALRVIKNILKAVRSDSGGGSTGFVLSTSLTLSETVSLLKSAGISVTDFDALICNSGSELYYPSPS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  845 NEDGPFVVDFYYhshieyrwggeglrktlirwasslnekkadndeqivtlaehlstdycytftvkkpaavpPVRELRKLL 924
Cdd:cd16419   81 GDDDSDYELIPD-----------------------------------------------------------PVKELRKLL 101
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15241313  925 RIQALRCHVVYSQNGTRINVIPVLASRIQALRYLFVRWGIDMAKMAVFVGESGDTDYEGLLGGLHKSVVLKGV 997
Cdd:cd16419  102 RMRGLRCHLVYCRNGTRLHVLPLLASRSQALRYLFVRWGIDLSNMVVFVGESGDTDYEELLGGLHKTVILKGV 174
PLN00142 PLN00142
sucrose synthase
171-665 1.75e-29

sucrose synthase


Pssm-ID: 215073 [Multi-domain]  Cd Length: 815  Bit Score: 126.63  E-value: 1.75e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313   171 VLISLHGLIRGENMeLGRdSDTGGQVKYVVELARALGSmpgvyrvDLLTR-QVSSPDVDYSYGEPTEMLTPRDSEDFSDE 249
Cdd:PLN00142  283 VIFSPHGYFGQANV-LGL-PDTGGQVVYILDQVRALEN-------EMLLRiKQQGLDIKPQILIVTRLIPDAKGTTCNQR 353
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313   250 MGESSG---AYIVRIPFGPKDKYIPKEL----LWPHIPEFVDGAMSHImqmsnvLGEQVGVgkpiwPSAIHGHYADAGDA 322
Cdd:PLN00142  354 LEKVSGtehSHILRVPFRTEKGILRKWIsrfdVWPYLETFAEDAASEI------LAELQGK-----PDLIIGNYSDGNLV 422
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313   323 TALLSGALNVPMLLTGHSLGRDKLEQllrqGRLSKEEINSTYKIMRRIEGEELSLDVSEMVITSTRQEIdeqwrlydgfd 402
Cdd:PLN00142  423 ASLLAHKLGVTQCTIAHALEKTKYPD----SDIYWKKFDDKYHFSCQFTADLIAMNHADFIITSTYQEI----------- 487
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313   403 pilerklrARIKRNVSCY---GRF-MPRMVKIPPGME-----FNhIVPHGGDME------------------------DT 449
Cdd:PLN00142  488 --------AGSKDTVGQYeshTAFtLPGLYRVVHGIDvfdpkFN-IVSPGADMSiyfpytekqkrltslhpsieellySP 558
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313   450 DGNEEHptspdppiwaeiMRFFSNSRKPMILALARPDPKKNITTLVKAFGECRPLRELANLALIMGNRDG---------- 519
Cdd:PLN00142  559 EQNDEH------------IGYLKDRKKPIIFSMARLDRVKNLTGLVEWYGKNKRLRELVNLVVVGGFIDPskskdreeia 626
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313   520 -IDEMSSTsssvllsvlklIDKYDLYGQVAYPKhhKQSDVP---DIYRLAAKSKGVFINPAIIEPFGLTLIEAAAHGLPM 595
Cdd:PLN00142  627 eIKKMHSL-----------IEKYNLKGQFRWIA--AQTNRVrngELYRYIADTKGAFVQPALYEAFGLTVVEAMTCGLPT 693
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15241313   596 VATKNGGPVDI--HRVldNGLLVDPHDQQSISEALL----KLVADKHLWAKCRQNGLKNIHQ-FSWpehcKTYLSRI 665
Cdd:PLN00142  694 FATCQGGPAEIivDGV--SGFHIDPYHGDEAANKIAdffeKCKEDPSYWNKISDAGLQRIYEcYTW----KIYAERL 764
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
308-663 4.27e-26

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: 111.48  E-value: 4.27e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  308 WPSAIHGHYADAGDATALLSGALNVPMLLTGHSLGRDKLEQLLRQGRlskeeinstyKIMRRIEGEELSLDVsemVITst 387
Cdd:cd03801   82 KFDVVHAHGLLAALLAALLALLLGAPLVVTLHGAEPGRLLLLLAAER----------RLLARAEALLRRADA---VIA-- 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  388 rqeideqwrlydgFDPILERKLRARikrnvscYGRFMPRMVKIPPGMEFNHIVPhggdmedtDGNEEHPTSPDPPIwaei 467
Cdd:cd03801  147 -------------VSEALRDELRAL-------GGIPPEKIVVIPNGVDLERFSP--------PLRRKLGIPPDRPV---- 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  468 mrffsnsrkpmILALARPDPKKNITTLVKAFGECRplRELANLALIMGNRDG--IDEMSSTsssvllsvlklidKYDLYG 545
Cdd:cd03801  195 -----------LLFVGRLSPRKGVDLLLEALAKLL--RRGPDVRLVIVGGDGplRAELEEL-------------ELGLGD 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  546 QVAYPKHHKQSDVPDIYRLAAkskgVFINPAIIEPFGLTLIEAAAHGLPMVATKNGGPVDIHRVLDNGLLVDPHDQQSIS 625
Cdd:cd03801  249 RVRFLGFVPDEELPALYAAAD----VFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVVPPDDVEALA 324
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 15241313  626 EALLKLVADKHLWAKCRQNGLKNIHQ-FSWPEHCKTYLS 663
Cdd:cd03801  325 DALLRLLADPELRARLGRAARERVAErFSWERVAERLLD 363
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
458-662 8.25e-23

glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. MtfB (mannosyltransferase B) in E. coli has been shown to direct the growth of the O9-specific polysaccharide chain. It transfers two mannoses into the position 3 of the previously synthesized polysaccharide.


Pssm-ID: 340838 [Multi-domain]  Cd Length: 362  Bit Score: 101.29  E-value: 8.25e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  458 SPDPPIWAEIMRFFSNSRKPMILALARPDPKKNITTLVKAFGECRPLRELANLaLIMGNRDGIDEmsstsssvllSVLKL 537
Cdd:cd03809  174 SFFPPESAAVLIAKYLLPEPYFLYVGTLEPRKNHERLLKAFALLKKQGGDLKL-VIVGGKGWEDE----------ELLDL 242
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  538 IDKYDLYGQVAYPKHHKQSDVPDIYRLAAkskgVFINPAIIEPFGLTLIEAAAHGLPMVATkNGGPvdiHR--VLDNGLL 615
Cdd:cd03809  243 VKKLGLGGRVRFLGYVSDEDLPALYRGAR----AFVFPSLYEGFGLPVLEAMACGTPVIAS-NISV---LPevAGDAALY 314
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 15241313  616 VDPHDQQSISEALLKLVADKHLWAKCRQNGLKNIHQFSWPEHCKTYL 662
Cdd:cd03809  315 FDPLDPESIADAILRLLEDPSLREELIRKGLERAKKFSWEKTAEKTL 361
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
476-647 3.85e-22

Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.


Pssm-ID: 425737 [Multi-domain]  Cd Length: 158  Bit Score: 93.88  E-value: 3.85e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313    476 KPMILALARPDPKKNITTLVKAFGECRPLRELANLaLIMGNRDGIDEMSSTsssvllsvlklIDKYDLYGQVAYPKHHKQ 555
Cdd:pfam00534    2 KKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKL-VIAGDGEEEKRLKKL-----------AEKLGLGDNVIFLGFVSD 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313    556 SDVPDIYRLAakskGVFINPAIIEPFGLTLIEAAAHGLPMVATKNGGPVDIHRVLDNGLLVDPHDQQSISEALLKLVADK 635
Cdd:pfam00534   70 EDLPELLKIA----DVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKLLEDE 145
                          170
                   ....*....|..
gi 15241313    636 HLWAKCRQNGLK 647
Cdd:pfam00534  146 ELRERLGENARK 157
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
561-663 1.36e-21

Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 91.21  E-value: 1.36e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  561 IYRLAakskGVFINPAIIEPFGLTLIEAAAHGLPMVATKNGGPVDIHRVLDNGLLVDPHDQQSISEALLKLVADKHLWAK 640
Cdd:COG0438   17 LLAAA----DVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLEDPELRRR 92
                         90       100
                 ....*....|....*....|....
gi 15241313  641 CRQNGLKNI-HQFSWPEHCKTYLS 663
Cdd:COG0438   93 LGEAARERAeERFSWEAIAERLLA 116
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
476-634 9.31e-17

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 77.94  E-value: 9.31e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313    476 KPMILALAR-PDPKKNITTLVKAFGECRPLRELANLALI-MGNRDGIDEMSSTSSsvllsvlkliDKYDLYGQVAypkhh 553
Cdd:pfam13692    1 RPVILFVGRlHPNVKGVDYLLEAVPLLRKRDNDVRLVIVgDGPEEELEELAAGLE----------DRVIFTGFVE----- 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313    554 kqsDVPDIYRLAAkskgVFINPAIIEPFGLTLIEAAAHGLPMVATKNGGPVDIHRVlDNGLLVDPHDQQSISEALLKLVA 633
Cdd:pfam13692   66 ---DLAELLAAAD----VFVLPSLYEGFGLKLLEAMAAGLPVVATDVGGIPELVDG-ENGLLVPPGDPEALAEAILRLLE 137

                   .
gi 15241313    634 D 634
Cdd:pfam13692  138 D 138
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
457-616 1.42e-14

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.


Pssm-ID: 340816 [Multi-domain]  Cd Length: 235  Bit Score: 74.36  E-value: 1.42e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  457 TSPDPPIWAEIMRFFSNSRKPMILA----LARPDPKKNITTLVKAFGECRPLRELANLALIMGNRDGIDEMSSTSSSVLL 532
Cdd:cd01635   87 GPDSLESTRSELLALARLLVSLPLAdkvsVGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAALGLL 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  533 SVLKLIDKYDlygqvaypkhhkQSDVPDIYRLAAKskgVFINPAIIEPFGLTLIEAAAHGLPMVATKNGGPVDIHRVLDN 612
Cdd:cd01635  167 ERVVIIGGLV------------DDEVLELLLAAAD---VFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGEN 231

                 ....
gi 15241313  613 GLLV 616
Cdd:cd01635  232 GLLV 235
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
308-654 7.76e-14

Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Staphylococcus aureus CapJ may be involved in capsule polysaccharide biosynthesis. WlbH in Bordetella parapertussis has been shown to be required for the biosynthesis of a trisaccharide that, when attached to the B. pertussis lipopolysaccharide (LPS) core (band B), generates band A LPS.


Pssm-ID: 340828 [Multi-domain]  Cd Length: 376  Bit Score: 74.34  E-value: 7.76e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  308 WPSAIHGHYA-DAGDATALLSGALNVPMLLTGHslGRDKLEqllrqgrlskeeiNSTYKIMRRIEGEELSLdvSEMVITS 386
Cdd:cd03798   95 PPDLIHAHFAyPAGFAAALLARLYGVPYVVTEH--GSDINV-------------FPPRSLLRKLLRWALRR--AARVIAV 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  387 TRQEIDEQWRLydgfdpilerklrARIKRNVscygrfmprmvkippgmefnHIVPHGgdmedTDGNEEHPtSPDPPIWAE 466
Cdd:cd03798  158 SKALAEELVAL-------------GVPRDRV--------------------DVIPNG-----VDPARFQP-EDRGLGLPL 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  467 imrffsnsRKPMILALARPDPKKNITTLVKAFGECRPLRELANLaLIMGnrDGIDEMSSTSSSVLLSVLKLIDkydLYGQ 546
Cdd:cd03798  199 --------DAFVILFVGRLIPRKGIDLLLEAFARLAKARPDVVL-LIVG--DGPLREALRALAEDLGLGDRVT---FTGR 264
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  547 VayPKHhkqsDVPDIYRLAakskGVFINPAIIEPFGLTLIEAAAHGLPMVATKNGGPVDIHRVLDNGLLVDPHDQQSISE 626
Cdd:cd03798  265 L--PHE----QVPAYYRAC----DVFVLPSRHEGFGLVLLEAMACGLPVVATDVGGIPEVVGDPETGLLVPPGDADALAA 334
                        330       340       350
                 ....*....|....*....|....*....|.
gi 15241313  627 ALLKLVAD---KHLWAKCRQNGLKNihqFSW 654
Cdd:cd03798  335 ALRRALAEpylRELGEAARARVAER---FSW 362
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
473-649 8.83e-14

capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. CapM in Staphylococcus aureus is required for the synthesis of type 1 capsular polysaccharides.


Pssm-ID: 340837 [Multi-domain]  Cd Length: 358  Bit Score: 74.17  E-value: 8.83e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  473 NSRKPMILALARPDPKKNITTLVKAFgecrplRELANLA-----LIMGNRDGIDEMSSTsssvllsvlklIDKYDLYGQV 547
Cdd:cd03808  186 PSEKVVFLFVARLLKDKGIDELIEAA------KILKKKGpnvrfLLVGDGELENPSEIL-----------IEKLGLEGRI 248
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  548 AYPKHhkQSDVPDIYRLAakskGVFINPAIIEPFGLTLIEAAAHGLPMVATKNGGPVDIhrVLD--NGLLVDPHDQQSIS 625
Cdd:cd03808  249 EFLGF--RSDVPELLAES----DVFVLPSYREGLPRSLLEAMAAGRPVITTDVPGCREL--VIDgvNGFLVPPGDVEALA 320
                        170       180
                 ....*....|....*....|....
gi 15241313  626 EALLKLVADKHLWAKCRQNGLKNI 649
Cdd:cd03808  321 DAIEKLIEDPELRKEMGEAARKRV 344
sucr_syn_bact_C TIGR02471
sucrose-phosphate synthase, sucrose phosphatase-like domain, bacterial; Sucrose phosphate ...
769-994 5.50e-13

sucrose-phosphate synthase, sucrose phosphatase-like domain, bacterial; Sucrose phosphate synthase (SPS) and sucrose phosphate phosphatase (SPP) are the last two enzymes of sucrose biosynthesis. In cyanobacteria and plants, the C-terminal region of most or all versions of SPS has a domain homologous to the known SPP. This domain may serve a binding or regulatory rather than catalytic function. Sequences in this family are bacterial C-terminal regions found in all but two of the putative bacterial sucrose phosphate synthases described by TIGR02472.


Pssm-ID: 131524  Cd Length: 236  Bit Score: 69.79  E-value: 5.50e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313    769 VIALDFD----GEEDTLEATKRILdavekERAEGSVGFILSTSLTISEVQSFLVSggLNPNDFDAFICNSGSDLHYTSln 844
Cdd:TIGR02471    1 LIITDLDntllGDDEGLASFVELL-----RGSGDAVGFGIATGRSVESAKSRYAK--LNLPSPDVLIARVGTEIYYGP-- 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313    845 nEDGPfvvDFYYHSHIEYRWGGEGLRKTLIRWAS-SLNEKKADNDEQIVTLAehlstdycytftvkKPAAVPPVRELRKL 923
Cdd:TIGR02471   72 -ELQP---DRFWQKHIDHDWRRQAVVEALADIPGlTLQDDQEQGPFKISYLL--------------DPEGEPILPQIRQR 133
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15241313    924 LRIQALRCHVVYSQnGTRINVIPVLASRIQALRYLFVRWGIDMAKMAVFVGESGDtdyEGLLGGLHKSVVL 994
Cdd:TIGR02471  134 LRQQSQAAKVILSC-GWFLDVLPLRASKGLALRYLSYRWGLPLEQILVAGDSGND---EEMLRGLTLGVVV 200
S6PP pfam05116
Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate ...
764-993 1.61e-12

Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate phosphohydrolase proteins found in plants and cyanobacteria. Sucrose-6(F)-phosphate phosphohydrolase catalyzes the final step in the pathway of sucrose biosynthesis.


Pssm-ID: 428314 [Multi-domain]  Cd Length: 246  Bit Score: 68.45  E-value: 1.61e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313    764 RKFIVVIALD---FDGEEDTLEATKRILDAVEKEraegsVGFILSTSLTISEVQSFLVSGGL-NPndfDAFICNSGSDLH 839
Cdd:pfam05116    1 PPLLLVSDLDntlVDGDNEALARLNQLLEAYRPD-----VGLVFATGRSLDSAKELLKEKPLpTP---DYLITSVGTEIY 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313    840 YtslNNEDGPfvvDFYYHSHIEYRWGGEGLRKTLIRWAS-SLNEKKadndEQivtlaehlsTDYCYTFTVKKPAAVPPVR 918
Cdd:pfam05116   73 Y---GPSLVP---DQSWQEHLDYHWDRQAVVEALAKFPGlTLQPEE----EQ---------RPHKVSYFLDPEAAAAVLA 133
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15241313    919 ELRKLLRIQALRCHVVYSqNGTRINVIPVLASRIQALRYLFVRWGIDMAKMaVFVGESGDtDYEGLLGGLHKSVV 993
Cdd:pfam05116  134 ELEQLLRKRGLDVKVIYS-SGRDLDILPLRASKGEALRYLALKLGLPLENT-LVCGDSGN-DEELFIGGTRGVVV 205
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
400-653 2.54e-12

family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most closely related to the GT1 family of glycosyltransferases. WabH in Klebsiella pneumoniae has been shown to transfer a GlcNAc residue from UDP-GlcNAc onto the acceptor GalUA residue in the cellular outer core.


Pssm-ID: 340839 [Multi-domain]  Cd Length: 351  Bit Score: 69.69  E-value: 2.54e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  400 GFDPILERKLRARIKRNVSCYgRFMPRMVKIPPGMEfnhivphgGDMEDTDGNEEHPTS--------PDPPIWAEIMRFF 471
Cdd:cd03811  113 HSSLSKLYYLKKKLLLKLKLY-KKADKIVCVSKGIK--------EDLIRLGPSPPEKIEviynpidiDRIRALAKEPILN 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  472 SNSRKPMILALARPDPKKNITTLVKAFGECRPLRELANLALImGnrDGIDEmsstsssvlLSVLKLIDKYDLYGQVAYPK 551
Cdd:cd03811  184 EPEDGPVILAVGRLDPQKGHDLLIEAFAKLRKKYPDVKLVIL-G--DGPLR---------EELEKLAKELGLAERVIFLG 251
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  552 HhkqsdVPDIYRLAAKSKgVFINPAIIEPFGLTLIEAAAHGLPMVATKNGGPVDI--HRvlDNGLLVDPHDqQSISEALL 629
Cdd:cd03811  252 F-----QSNPYPYLKKAD-LFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPREIldDG--ENGLLVPDGD-AAALAGIL 322
                        250       260
                 ....*....|....*....|....
gi 15241313  630 KLVADKHLWAKCRQNGLKNIHQFS 653
Cdd:cd03811  323 AALLQKKLDAALRERLAKAQEAVF 346
HAD_SPP cd02605
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ...
769-993 3.41e-12

sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3.1.3.24) catalyzes the dephosphorylation of sucrose-6(F)-phosphate (Suc6P)-the final step in the pathway of sucrose biosynthesis in plants and cyanobacteria. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319792 [Multi-domain]  Cd Length: 245  Bit Score: 67.37  E-value: 3.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  769 VIALDFD----GEEDTLEATKRILDAVEKERAEGSVGFILSTSLTISEVQSFLVSGGL-NPndfDAFICNSGSDLHYTsl 843
Cdd:cd02605    1 LLVSDLDetlvGHDTNLQALERLQDLLEQLTADNDVILVYATGRSPESVLELIKEVMLpKP---DFIISDVGTEIYYG-- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  844 nnEDGPFVVDFYYHSHIEYRWGGEglrktlirwassLNEKKADNDEQIVTLAEHLSTDYCYTFTVKKPAAVPPVRELRKL 923
Cdd:cd02605   76 --ESGYLEPDTYWNEVLSEGWERF------------LFEAIADLFKQLKPQSELEQNPHKISFYLDPQNDAAVIEQLEEM 141
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15241313  924 LRIQALRCHVVYSQNGTR-INVIPVLASRIQALRYLFVRWGIDmAKMAVFVGESGDtDYEGLLGGLHKSVV 993
Cdd:cd02605  142 LLKAGLTVRIIYSSGLAYdLDILPLGAGKGEALRYLQEKWNFP-PERTLVCGDSGN-DIALLSTGTRGVIV 210
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
459-665 1.55e-11

UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. UDP-glucose-diacylglycerol glucosyltransferase (EC 2.4.1.337, UGDG; also known as 1,2-diacylglycerol 3-glucosyltransferase) catalyzes the transfer of glucose from UDP-glucose to 1,2-diacylglycerol forming 3-D-glucosyl-1,2-diacylglycerol.


Pssm-ID: 340844 [Multi-domain]  Cd Length: 372  Bit Score: 67.30  E-value: 1.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  459 PDPPIWAEIMRFFSNSRKPMILALARPDPKKNITTLVKAFgecRPLRELANLALIM-GnrDGIDEmsstsssvlLSVLKL 537
Cdd:cd03817  184 EKPLNTEERRKLGLPPDEPILLYVGRLAKEKNIDFLLRAF---AELKKEPNIKLVIvG--DGPER---------EELKEL 249
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  538 IDKYDLYGQVAYPKHHKQSDVPDIYRLAakskGVFINPAIIEPFGLTLIEAAAHGLPMVATKNGGPVDIHRVLDNGLLVD 617
Cdd:cd03817  250 ARELGLADKVIFTGFVPREELPEYYKAA----DLFVFASTTETQGLVYLEAMAAGLPVVAAKDPAASELVEDGENGFLFE 325
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 15241313  618 PhDQQSISEALLKLVADKHLWAKCRQNGLKNIHQFSWPEHCKTYLSRI 665
Cdd:cd03817  326 P-NDETLAEKLLHLRENLELLRKLSKNAEISAREFAFAKSVEKLYEEV 372
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
473-658 2.30e-11

accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases and is named after gtfA in Streptococcus gordonii, where it plays a role in the O-linked glycosylation of GspB, a cell surface glycoprotein involved in platelet binding. In general 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 in bacteria.


Pssm-ID: 340855 [Multi-domain]  Cd Length: 328  Bit Score: 66.17  E-value: 2.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  473 NSRKP-MILALARPDPKKNITTLVKAFGECRplRELANLALIM---GNRDGIDEMSstsssvllsvlklIDKYDLYGQVA 548
Cdd:cd04949  156 HERKSnKIITISRLAPEKQLDHLIEAVAKAV--KKVPEITLDIygyGEEREKLKKL-------------IEELHLEDNVF 220
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  549 YPKHHKQSDvpDIYRLAakskGVFINPAIIEPFGLTLIEAAAHGLPMVATK-NGGPVDIhrVLD--NGLLVDPHDQQSIS 625
Cdd:cd04949  221 LKGYHSNLD--QEYQDA----YLSLLTSQMEGFGLTLMEAIGHGLPVVSYDvKYGPSEL--IEDgeNGYLIEKNNIDALA 292
                        170       180       190
                 ....*....|....*....|....*....|...
gi 15241313  626 EALLKLVADKHLWAKCRQNGLKNIHQFSwPEHC 658
Cdd:cd04949  293 DKIIELLNDPEKLQQFSEESYKIAEKYS-TENV 324
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
538-655 2.88e-11

amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. AmSD in Erwinia amylovora has been shown to be involved in the biosynthesis of amylovoran, the acidic exopolysaccharide acting as a virulence factor. This enzyme may be responsible for the formation of galactose alpha-1,6 linkages in amylovoran.


Pssm-ID: 340847 [Multi-domain]  Cd Length: 351  Bit Score: 66.11  E-value: 2.88e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  538 IDKYDLYGQVAYPkhHKQSDVPDIYRLAAkskgVFINPAIIEPFGLTLIEAAAHGLPMVATK-NGGPVDIhrVLD--NGL 614
Cdd:cd03820  231 IDKLGLEDRVKLL--GPTKNIAEEYANSS----IFVLSSRYEGFPMVLLEAMAYGLPIISFDcPTGPSEI--IEDgeNGL 302
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 15241313  615 LVDPHDQQSISEALLKLVADKHLWAKCRQNGLKNIHQFSWP 655
Cdd:cd03820  303 LVPNGDVDALAEALLRLMEDEELRKKMGKNARKNAERFSIE 343
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
395-656 5.31e-11

glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family of glycosyltransferases and includes a sequence annotated as alpha-D-mannose-alpha(1-6)phosphatidyl myo-inositol monomannoside transferase from Bacillus halodurans. 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 bacteria and eukaryotes.


Pssm-ID: 340842 [Multi-domain]  Cd Length: 365  Bit Score: 65.39  E-value: 5.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  395 WRLYDGFDPIL------ERKLRARIKRNVscygrfmprmvkippgmefnHIVPHGGDMEDTdgneeHPTSPDPPIWAEim 468
Cdd:cd03814  140 RWFHNPFDTTLvpspsiARELEGHGFERV--------------------RLWPRGVDTELF-----HPSRRDAALRRR-- 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  469 rfFSNSRKPMILALARPDPKKNITTLVKAFgecRPLRELANLALIM-GnrDGIDemsstsssvllsvlklidKYDLygQV 547
Cdd:cd03814  193 --LGPPGRPLLLYVGRLAPEKNLEALLDAD---LPLAASPPVRLVVvG--DGPA------------------RAEL--EA 245
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  548 AYPKHH-----KQSDVPDIYrlaaKSKGVFINPAIIEPFGLTLIEAAAHGLPMVATKNGGPVDIHRVLDNGLLVDPHDQQ 622
Cdd:cd03814  246 RGPDVIftgflTGEELARAY----ASADVFVFPSRTETFGLVVLEAMASGLPVVAADAGGPRDIVRPGGTGALVEPGDAA 321
                        250       260       270
                 ....*....|....*....|....*....|....
gi 15241313  623 SISEALLKLVADKHLWAKCRQNGLKNIHQFSWPE 656
Cdd:cd03814  322 AFAAALRALLEDPELRRRMAARARAEAERYSWEA 355
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
560-644 2.18e-10

putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Escherichia coli WcaC has been predicted to function in colanic acid biosynthesis. WcfI in Bacteroides fragilis has been shown to be involved in the capsular polysaccharide biosynthesis.


Pssm-ID: 340851 [Multi-domain]  Cd Length: 364  Bit Score: 63.50  E-value: 2.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  560 DIYRLAakskGVFINPAIIEPFGLTLIEAAAHGLPMVATKNGGPVDIHRVLDNGLLVDPHDQQSISEALLKLVADKHLWA 639
Cdd:cd03825  259 DIYSAA----DLFVHPSLADNLPNTLLEAMACGTPVVAFDTGGSPEIVQHGVTGYLVPPGDVQALAEAIEWLLANPKERE 334

                 ....*
gi 15241313  640 KCRQN 644
Cdd:cd03825  335 SLGER 339
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
458-649 6.73e-10

Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbnK in Shigella dysenteriae has been shown to be involved in the type 7 O-antigen biosynthesis.


Pssm-ID: 340836 [Multi-domain]  Cd Length: 362  Bit Score: 61.95  E-value: 6.73e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  458 SPDPPIWAEIMRFFSNSRK-PMILALARPDPKKNITTLVKAFGECRPLRELANLALIM--GNRDGIDEMSSTSSSVllsv 534
Cdd:cd03807  171 SPDDASRARARRRLGLAEDrRVIGIVGRLHPVKDHSDLLRAAALLVETHPDLRLLLVGrgPERPNLERLLLELGLE---- 246
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  535 lkliDKYDLYGQvaypkhhkQSDVP------DIYRLAAKSKGvfinpaiiepFGLTLIEAAAHGLPMVATKNGGPVDIhr 608
Cdd:cd03807  247 ----DRVHLLGE--------RSDVPallpamDIFVLSSRTEG----------FPNALLEAMACGLPVVATDVGGAAEL-- 302
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 15241313  609 VLDN-GLLVDPHDQQSISEALLKLVADKHLWAKCRQNGLKNI 649
Cdd:cd03807  303 VDDGtGFLVPAGDPQALADAIRALLEDPEKRARLGRAARERI 344
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
438-640 1.03e-09

Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 family of glycosyltransferases. WavL in Vibrio cholerae has been shown to be involved in the biosynthesis of the lipopolysaccharide core.


Pssm-ID: 340846 [Multi-domain]  Cd Length: 345  Bit Score: 61.60  E-value: 1.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  438 HIVPHGGDMedtdgneeHPTSPDPPiWAEIMRFFSNSRKPMILALARPDPKKNITTLVKAFGEcrpLRELANLALIM--- 514
Cdd:cd03819  153 RVIPNGVDT--------DRFPPEAE-AEERAQLGLPEGKPVVGYVGRLSPEKGWLLLVDAAAE---LKDEPDFRLLVagd 220
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  515 GNRDgiDEMSSTsssvllsvlklIDKYDLYGQVAYPKHHkqSDVPDIYRLAAkskgVFINPAIIEPFGLTLIEAAAHGLP 594
Cdd:cd03819  221 GPER--DEIRRL-----------VERLGLRDRVTFTGFR--EDVPAALAASD----VVVLPSLHEEFGRVALEAMACGTP 281
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 15241313  595 MVATKNGGPVDIhrVLDN--GLLVDPHDQQSISEALLKLVADKHLWAK 640
Cdd:cd03819  282 VVATDVGGAREI--VVHGrtGLLVPPGDAEALADAIRAAKLLPEAREK 327
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
421-640 1.33e-09

glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ExpE7 in Sinorhizobium meliloti has been shown to be involved in the biosynthesis of galactoglucans (exopolysaccharide II).


Pssm-ID: 340850 [Multi-domain]  Cd Length: 357  Bit Score: 61.19  E-value: 1.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  421 GRFMPRMVKIPPGMEFNHIVPhggdmedtdgneEHPTSPDPPIwaeimRFfsnsrkpmiLALARPDPKKNITTLVKAFGE 500
Cdd:cd03823  162 GLFSARISVIPNAVEPDLAPP------------PRRRPGTERL-----RF---------GYIGRLTEEKGIDLLVEAFKR 215
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  501 CRPLR-ELanlaLIMGNRDGIDEmsstsssvllSVLKLIDKYDLYGQVaypkhhKQSDVPDIYRLAAkskgVFINPAI-I 578
Cdd:cd03823  216 LPREDiEL----VIAGHGPLSDE----------RQIEGGRRIAFLGRV------PTDDIKDFYEKID----VLVVPSIwP 271
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15241313  579 EPFGLTLIEAAAHGLPMVATKNGGPVDIHRVLDNGLLVDPHDQQSISEALLKLVADKHLWAK 640
Cdd:cd03823  272 EPFGLVVREAIAAGLPVIASDLGGIAELIQPGVNGLLFAPGDAEDLAAAMRRLLTDPALLER 333
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
460-658 4.53e-09

glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family of glycosyltransferases. 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 bacteria, while some of them are also found in Archaea and eukaryotes.


Pssm-ID: 340841 [Multi-domain]  Cd Length: 474  Bit Score: 60.04  E-value: 4.53e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  460 DPPIWAEIMRFFSNSRKPMILALARPDPKKNITTLVKAFGECRPLRELANLALImGNRDGiDEMSSTSSSVLLSVLKLID 539
Cdd:cd03813  277 DIQRFAPAREERPEKEPPVVGLVGRVVPIKDVKTFIRAFKLVRRAMPDAEGWLI-GPEDE-DPEYAQECKRLVASLGLEN 354
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  540 KYDLYGQVaypkhhkqsDVPDIYRlaakSKGVFINPAIIEPFGLTLIEAAAHGLPMVATKNGGPVD-IHRVLDN----GL 614
Cdd:cd03813  355 KVKFLGFQ---------NIKEYYP----KLGLLVLTSISEGQPLVILEAMASGVPVVATDVGSCRElIYGADDAlgqaGL 421
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 15241313  615 LVDPHDQQSISEALLKLVADKHLWAKCRQNGLKNIHQFSWPEHC 658
Cdd:cd03813  422 VVPPADPEALAEALIKLLRDPELRQAFGEAGRKRVEKYYTLEGM 465
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
571-634 9.91e-09

Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. 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 bacteria and eukaryotes.


Pssm-ID: 340826 [Multi-domain]  Cd Length: 355  Bit Score: 58.44  E-value: 9.91e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15241313  571 VFINPAII--EPFGLTLIEAAAHGLPMVATKNGG---PVDIHRVldNGLLVDPHDQQSISEALLKLVAD 634
Cdd:cd03795  264 VFVFPSVLrsEAFGIVLLEAMMCGKPVISTNIGTgvpYVNNNGE--TGLVVPPKDPDALAEAIDKLLSD 330
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
487-649 1.49e-08

N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. 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 bacteria, while some of them are also found in Archaea and eukaryotes.


Pssm-ID: 340859 [Multi-domain]  Cd Length: 370  Bit Score: 58.13  E-value: 1.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  487 PKKNITTLVKAFGECRplRELANLALIMGnrDGIDemsstsssvLLSVLKLIDKYDLYGQVAYpkHHKQSDVPDIYRLAa 566
Cdd:cd04962  207 PVKRIDDVVRVFARVR--RKIPAKLLLVG--DGPE---------RVPAEELARELGVEDRVLF--LGKQDDVEELLSIA- 270
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  567 kskGVFINPAIIEPFGLTLIEAAAHGLPMVATKNGGPVDIHRVLDNGLLVDPHDQQSISEALLKLVADKHLWAKCRQNGL 646
Cdd:cd04962  271 ---DLFLLPSEKESFGLAALEAMACGVPVVSSNAGGIPEVVKHGETGFLSDVGDVDAMAKSALSILEDDELYNRMGRAAR 347

                 ...
gi 15241313  647 KNI 649
Cdd:cd04962  348 KRA 350
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
475-655 2.68e-07

Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Bme6 in Brucella melitensis has been shown to be involved in the biosynthesis of a polysaccharide.


Pssm-ID: 340848 [Multi-domain]  Cd Length: 377  Bit Score: 53.91  E-value: 2.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  475 RKPMILALARPDPKKNITTLVKAFgecRPLRELANLA--LIMGNRDGidemsstsssVLLSVLKLIDKYDLYGQVAYPKH 552
Cdd:cd03821  203 DRRIILFLGRIHPKKGLDLLIRAA---RKLAEQGRDWhlVIAGPDDG----------AYPAFLQLQSSLGLGDRVTFTGP 269
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  553 HKQSDVPDIYrlaaKSKGVFINPAIIEPFGLTLIEAAAHGLPMVATKNggpVDIHRVL--DNGLLVDPHDqQSISEALLK 630
Cdd:cd03821  270 LYGEAKWALY----ASADLFVLPSYSENFGNVVAEALACGLPVVITDK---CGLSELVeaGCGVVVDPNV-SSLAEALAE 341
                        170       180
                 ....*....|....*....|....*...
gi 15241313  631 LVADKHLWAKCRQNGLKNIHQ---FSWP 655
Cdd:cd03821  342 ALRDPADRKRLGEMARRARQVeenFSWE 369
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
462-654 1.56e-05

Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. WbuB in E. coli is involved in the biosynthesis of the O26 O-antigen. It has been proposed to function as an N-acetyl-L-fucosamine (L-FucNAc) transferase.


Pssm-ID: 340825 [Multi-domain]  Cd Length: 391  Bit Score: 48.49  E-value: 1.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  462 PIWAEIMRFFSNSRKPMILALARPDPKK-----NIttlvkafGECRPLRELANLALIMGNRDGI--------DEmssTSS 528
Cdd:cd03794  192 PNWADLEEFKPPPKDELRKKLGLDDKFVvvyagNI-------GKAQGLETLLEAAERLKRRPDIrflfvgdgDE---KER 261
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  529 SVLLSVLKLIDKYDLYGQV---AYPKHHKQSDV---P----DIYRLAAKSKgvfinpaiiepfgltLIEAAAHGLPMVAT 598
Cdd:cd03794  262 LKELAKARGLDNVTFLGRVpkeEVPELLSAADVglvPlkdnPANRGSSPSK---------------LFEYMAAGKPILAS 326
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15241313  599 KNGGPVDIHRVLDNGLLVDPHDQQSISEALLKLVADKHLWAKCRQNGLKNI-HQFSW 654
Cdd:cd03794  327 DDGGSDLAVEINGCGLVVEPGDPEALADAILELLDDPELRRAMGENGRELAeEKFSR 383
GT4_PIG-A-like cd03796
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ...
538-630 2.57e-05

phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Phosphatidylinositol glycan-class A (PIG-A), an X-linked gene in humans, is necessary for the synthesis of N-acetylglucosaminyl-phosphatidylinositol, a very early intermediate in glycosyl phosphatidylinositol (GPI)-anchor biosynthesis. The GPI-anchor is an important cellular structure that facilitates the attachment of many proteins to cell surfaces. Somatic mutations in PIG-A have been associated with Paroxysmal Nocturnal Hemoglobinuria (PNH), an acquired hematological disorder.


Pssm-ID: 340827 [Multi-domain]  Cd Length: 398  Bit Score: 48.00  E-value: 2.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  538 IDKYDLYGQV---AYPKHHkqsDVPDIYRlaaksKG-VFINPAIIEPFGLTLIEAAAHGLPMVATKNGGpvdIHRVLDNG 613
Cdd:cd03796  243 REKYQLQDRVellGAVPHE---EVRDVLV-----QGhIFLNTSLTEAFCIAIVEAASCGLLVVSTRVGG---IPEVLPPD 311
                         90
                 ....*....|....*....
gi 15241313  614 LLV--DPhDQQSISEALLK 630
Cdd:cd03796  312 MILlaEP-DPEDIVRKLEE 329
GT4_trehalose_phosphorylase cd03792
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ...
476-662 5.15e-05

trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly catalyzes trehalose synthesis and degradation from alpha-glucose-1-phosphate (alpha-Glc-1-P) and glucose. The catalyzing activity includes the phosphorolysis of trehalose, which produce alpha-Glc-1-P and glucose, and the subsequent synthesis of trehalose. This family is most closely related to the GT4 family of glycosyltransferases.


Pssm-ID: 340823 [Multi-domain]  Cd Length: 378  Bit Score: 46.93  E-value: 5.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  476 KPMILALARPDPKKNITTLVKAFGECRPLRELANLaLIMGNrDGIDemsstsssvllsvlklidkyDLYGQVAYPK-HHK 554
Cdd:cd03792  197 RPYILQVARFDPSKDPLGVIDAYKLFKRRAEEPQL-VICGH-GAVD--------------------DPEGSVVYEEvMEY 254
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  555 QSDVPDIYRLAAKSKGVFINP-----------AIIEPFGLTLIEAAAHGLPMVATKNGG-PVdihRVLD--NGLLVDPHD 620
Cdd:cd03792  255 AGDDHDIHVLRLPPSDQEINAlqraatvvlqlSTREGFGLTVSEALWKGKPVIATPAGGiPL---QVIDgeTGFLVNSVE 331
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 15241313  621 QQSISeaLLKLVADKHLWAKCRQNGLKNI-HQFSWPEHCKTYL 662
Cdd:cd03792  332 GAAVR--ILRLLTDPELRRKMGLAAREHVrDNFLITGNLRAWL 372
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
579-643 2.41e-04

UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. aviGT4 in Streptomyces viridochromogenes has been shown to be involved in biosynthesis of oligosaccharide antibiotic avilamycin A. Inactivation of aviGT4 resulted in a mutant that accumulated a novel avilamycin derivative lacking the terminal eurekanate residue.


Pssm-ID: 340832 [Multi-domain]  Cd Length: 333  Bit Score: 44.59  E-value: 2.41e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15241313  579 EPFGLTLIEAAAHGLPMVATKNGGPVDIHRVLDNGLLVDPhdQQSISEALLKLvaDKHLWAKCRQ 643
Cdd:cd03802  251 EPFGLVMIEAMACGTPVIAYRRGGLPEVIQHGETGFLVDS--VEEMAEAIANI--DRIDRAACRR 311
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
478-634 6.22e-04

LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases and is named after WbdM in Escherichia coli. In general 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 in bacteria.


Pssm-ID: 340857 [Multi-domain]  Cd Length: 360  Bit Score: 43.20  E-value: 6.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  478 MILALARPDPKKNITTLVKAFGECrPLRELANLALIMGN---RDGIDEMsstsssvllsvlklIDKYDLYGQVAYPKHHk 554
Cdd:cd04951  190 VILNVGRLTEAKDYPNLLLAISEL-ILSKNDFKLLIAGDgplRNELERL--------------ICNLNLVDRVILLGQI- 253
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  555 qSDVPDIYRLAakskGVFINPAIIEPFGLTLIEAAAHGLPMVATKNGGPVDIhrVLDNGLLVDPHDQQSISEALLKLVAD 634
Cdd:cd04951  254 -SNISEYYNAA----DLFVLSSEWEGFGLVVAEAMACERPVVATDAGGVAEV--VGDHNYVVPVSDPQLLAEKIKEIFDM 326
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
565-654 1.38e-03

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 42.39  E-value: 1.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313   565 AAKSKGVFINPAIIEPFGLTLIEAAAHGLPMVATKNGGPVDI---HRVLDNGLLVDPHDQQSISEALLKLVADKHLWAKC 641
Cdd:PLN02871  328 AYASGDVFVMPSESETLGFVVLEAMASGVPVVAARAGGIPDIippDQEGKTGFLYTPGDVDDCVEKLETLLADPELRERM 407
                          90
                  ....*....|...
gi 15241313   642 RQNGLKNIHQFSW 654
Cdd:PLN02871  408 GAAAREEVEKWDW 420
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
475-637 1.49e-03

glycosyltransferase family 4 proteins; 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 glycosyltransferase family 4 (GT4). 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.


Pssm-ID: 340860 [Multi-domain]  Cd Length: 365  Bit Score: 42.05  E-value: 1.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  475 RKPMILALARPDPKKNITTLVKAFGECRPLRELANLaLIMGnrDGidemssTSSSVLLSVLKLIDKYDLYGqvAYPkhhk 554
Cdd:cd05844  188 RAPTILFVGRLVEKKGCDVLIEAFRRLAARHPTARL-VIAG--DG------PLRPALQALAAALGRVRFLG--ALP---- 252
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  555 QSDVPDIYRLAAkskgVFINPAII------EPFGLTLIEAAAHGLPMVATKNGGPVDihRVLD--NGLLVDPHDQQSISE 626
Cdd:cd05844  253 HAEVQDWMRRAE----IFCLPSVTaasgdsEGLGIVLLEAAACGVPVVSSRHGGIPE--AILDgeTGFLVPEGDVDALAD 326
                        170
                 ....*....|.
gi 15241313  627 ALLKLVADKHL 637
Cdd:cd05844  327 ALQALLADRAL 337
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
439-654 1.56e-03

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 42.08  E-value: 1.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313   439 IVPHGGDMEDTDGNEEHPTSPDPPIwaeimrffsNSRKPMILALARPDPKKNITTLVKAFGECRPLRElaNLALI----- 513
Cdd:PRK15484  165 IVPNGFCLETYQSNPQPNLRQQLNI---------SPDETVLLYAGRISPDKGILLLMQAFEKLATAHS--NLKLVvvgdp 233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313   514 MGNRDGidEMSSTSSSVLLSVLKLIDKYDLYGQVAYPKHHKqsdvpdIYRLAAKskgVFINPAIIEPFGLTLIEAAAHGL 593
Cdd:PRK15484  234 TASSKG--EKAAYQKKVLEAAKRIGDRCIMLGGQPPEKMHN------YYPLADL---VVVPSQVEEAFCMVAVEAMAAGK 302
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15241313   594 PMVATKNGGPVDIhrVLDNGL---LVDPHDQQSISEALLKLVADKHLwAKCRQNGLKNI-HQFSW 654
Cdd:PRK15484  303 PVLASTKGGITEF--VLEGITgyhLAEPMTSDSIISDINRTLADPEL-TQIAEQAKDFVfSKYSW 364
GT4_AmsK-like cd03799
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ...
571-638 2.32e-03

Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases found specifically in certain bacteria. AmsK in Erwinia amylovora, has been reported to be involved in the biosynthesis of amylovoran, a exopolysaccharide acting as a virulence factor.


Pssm-ID: 340829 [Multi-domain]  Cd Length: 350  Bit Score: 41.28  E-value: 2.32e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15241313  571 VFINPAIIEPFG------LTLIEAAAHGLPMVATKNGGPVDIhrVLDN--GLLVDPHDQQSISEALLKLVADKHLW 638
Cdd:cd03799  253 IFIAPSVTAADGdqdgppNTLKEAMAMGLPVISTEHGGIPEL--VEDGvsGFLVPERDAEAIAEKLTYLIEHPAIW 326
GT4_ALG2-like cd03805
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ...
579-653 2.64e-03

alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ALG2, a 1,3-mannosyltransferase, in yeast catalyzes the mannosylation of Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate. A deficiency of this enzyme causes an abnormal accumulation of Man1GlcNAc2-PP-dolichol and Man2GlcNAc2-PP-dolichol, which is associated with a type of congenital disorders of glycosylation (CDG), designated CDG-Ii, in humans.


Pssm-ID: 340834 [Multi-domain]  Cd Length: 392  Bit Score: 41.42  E-value: 2.64e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15241313  579 EPFGLTLIEAAAHGLPMVATKNGGPVDihRVLDN--GLLVDPhDQQSISEALLKLVADKHLWAKCRQNGLKNIHQ-FS 653
Cdd:cd03805  310 EHFGIVPLEAMYAGKPVIACNSGGPLE--TVVEGvtGFLCEP-TPEAFAEAMLKLANDPDLADRMGAAGRKRVKEkFS 384
GT5_Glycogen_synthase_DULL1-like cd03791
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ...
572-654 3.94e-03

Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 family of glycosyltransferases. Glycogen synthase (EC:2.4.1.21) catalyzes the formation and elongation of the alpha-1,4-glucose backbone using ADP-glucose, the second and key step of glycogen biosynthesis. This family includes starch synthases of plants, such as DULL1 in Zea mays and glycogen synthases of various organisms.


Pssm-ID: 340822 [Multi-domain]  Cd Length: 474  Bit Score: 41.01  E-value: 3.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  572 FINPAIIEPFGLTLIEAAAHGLPMVATKNGGPVDIhrVLD--------NGLLVDPHDQQSISEAL---LKLVADKHLWAK 640
Cdd:cd03791  372 FLMPSRFEPCGLVQMYAMRYGTLPIVRRTGGLADT--VFDydpetgegTGFVFEDYDAEALLAALrraLALYRNPELWRK 449
                         90
                 ....*....|....*
gi 15241313  641 CRQNGLKnihQ-FSW 654
Cdd:cd03791  450 LQKNAMK---QdFSW 461
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
769-978 5.94e-03

Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport and metabolism, General function prediction only];


Pssm-ID: 440327 [Multi-domain]  Cd Length: 192  Bit Score: 38.96  E-value: 5.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  769 VIALDFDGeedTL-----EATKRILDAVEKERAEGsVGFILSTSLTISEVQSFLVSGGLNpndfDAFICNSGSDLHYTSl 843
Cdd:COG0561    4 LIALDLDG---TLlnddgEISPRTKEALRRLREKG-IKVVIATGRPLRSALPLLEELGLD----DPLITSNGALIYDPD- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241313  844 nnedgpfvvdfyyhshieyrwgGEGLRKTLIrwasslnekkaDNDEqivtlaehlstdycytftvkkpaavppVRELRKL 923
Cdd:COG0561   75 ----------------------GEVLYERPL-----------DPED---------------------------VREILEL 94
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 15241313  924 LRIQALRCHVVYSQNGTRINVIPVLASRIQALRYLFVRWGIDMAKMAVFvgesGD 978
Cdd:COG0561   95 LREHGLHLQVVVRSGPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAF----GD 145
 
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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