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Conserved domains on  [gi|1063734715|ref|NP_198534|]
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sucrose synthase 5 [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN00142 super family cl30293
sucrose synthase
1-614 0e+00

sucrose synthase


The actual alignment was detected with superfamily member PLN00142:

Pssm-ID: 215073 [Multi-domain]  Cd Length: 815  Bit Score: 1315.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715   1 MMNETLNTARKLEMSLILADVFLSELPKDTPFQAFELRFKECGFEKGWGESAGRVKETMRILSEILQAPDPQNIDRFFAR 80
Cdd:PLN00142  196 MLNDRIQTLSKLQSALRKAEEYLSKLPKDTPYSEFEHRFQELGLEKGWGDTAERVLETIHLLLDLLQAPDPSTLEKFLGR 275
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715  81 VPRIFNVVIFSVHGYFGQTDVLGLPDTGGQVVYILDQVKALEDELLQRINSQGLNFKPQILVVTRLIPDAKKTKCNQELE 160
Cdd:PLN00142  276 IPMVFNVVIFSPHGYFGQANVLGLPDTGGQVVYILDQVRALENEMLLRIKQQGLDIKPQILIVTRLIPDAKGTTCNQRLE 355
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 161 PIFGTKYSNILRIPFVTENGILRRWVSRFDIYPYLERFTKDATTKILDILEGKPDLIIGNYTDGNLVASLMANKLGITQA 240
Cdd:PLN00142  356 KVSGTEHSHILRVPFRTEKGILRKWISRFDVWPYLETFAEDAASEILAELQGKPDLIIGNYSDGNLVASLLAHKLGVTQC 435
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 241 TIAHALEKTKYEDSDIKWKEFDPKYHFSSQFTADLISMNSADFIIASTYQEIAGSKERAGQYESHMSFTVPGLYRVVSGI 320
Cdd:PLN00142  436 TIAHALEKTKYPDSDIYWKKFDDKYHFSCQFTADLIAMNHADFIITSTYQEIAGSKDTVGQYESHTAFTLPGLYRVVHGI 515
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 321 NVFDPRFNIAAPGADDSIYFPFTAQDRRFTKFYTSIDELLYSQSENDEHIGYLVDKKKPIIFSMARLDVVKNLTGLTEWY 400
Cdd:PLN00142  516 DVFDPKFNIVSPGADMSIYFPYTEKQKRLTSLHPSIEELLYSPEQNDEHIGYLKDRKKPIIFSMARLDRVKNLTGLVEWY 595
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 401 AKNKRLRDLVNLVIVGGFFDASKSKDREEISEIKKMHSLIEKYQLKGQFRWITAQTDRTRNGELYRSIADTRGAFVQPAH 480
Cdd:PLN00142  596 GKNKRLRELVNLVVVGGFIDPSKSKDREEIAEIKKMHSLIEKYNLKGQFRWIAAQTNRVRNGELYRYIADTKGAFVQPAL 675
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 481 YEAFGLTVIEAMSCGLVTFATNQGGPAEIIVDGVSGFHIDPSNGEESSDKIADFFEKSGMDPDYWNMFSNEGLQRINECY 560
Cdd:PLN00142  676 YEAFGLTVVEAMTCGLPTFATCQGGPAEIIVDGVSGFHIDPYHGDEAANKIADFFEKCKEDPSYWNKISDAGLQRIYECY 755
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1063734715 561 TWKIYANKVINMGSTYSYWRHLNKDQKLAKQRYIHSFYNLQYRNLVKTIPILSD 614
Cdd:PLN00142  756 TWKIYAERLLTLGGVYGFWKYVSKLERRETRRYLEMFYNLKFRELAKTVPLAVD 809
 
Name Accession Description Interval E-value
PLN00142 PLN00142
sucrose synthase
1-614 0e+00

sucrose synthase


Pssm-ID: 215073 [Multi-domain]  Cd Length: 815  Bit Score: 1315.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715   1 MMNETLNTARKLEMSLILADVFLSELPKDTPFQAFELRFKECGFEKGWGESAGRVKETMRILSEILQAPDPQNIDRFFAR 80
Cdd:PLN00142  196 MLNDRIQTLSKLQSALRKAEEYLSKLPKDTPYSEFEHRFQELGLEKGWGDTAERVLETIHLLLDLLQAPDPSTLEKFLGR 275
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715  81 VPRIFNVVIFSVHGYFGQTDVLGLPDTGGQVVYILDQVKALEDELLQRINSQGLNFKPQILVVTRLIPDAKKTKCNQELE 160
Cdd:PLN00142  276 IPMVFNVVIFSPHGYFGQANVLGLPDTGGQVVYILDQVRALENEMLLRIKQQGLDIKPQILIVTRLIPDAKGTTCNQRLE 355
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 161 PIFGTKYSNILRIPFVTENGILRRWVSRFDIYPYLERFTKDATTKILDILEGKPDLIIGNYTDGNLVASLMANKLGITQA 240
Cdd:PLN00142  356 KVSGTEHSHILRVPFRTEKGILRKWISRFDVWPYLETFAEDAASEILAELQGKPDLIIGNYSDGNLVASLLAHKLGVTQC 435
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 241 TIAHALEKTKYEDSDIKWKEFDPKYHFSSQFTADLISMNSADFIIASTYQEIAGSKERAGQYESHMSFTVPGLYRVVSGI 320
Cdd:PLN00142  436 TIAHALEKTKYPDSDIYWKKFDDKYHFSCQFTADLIAMNHADFIITSTYQEIAGSKDTVGQYESHTAFTLPGLYRVVHGI 515
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 321 NVFDPRFNIAAPGADDSIYFPFTAQDRRFTKFYTSIDELLYSQSENDEHIGYLVDKKKPIIFSMARLDVVKNLTGLTEWY 400
Cdd:PLN00142  516 DVFDPKFNIVSPGADMSIYFPYTEKQKRLTSLHPSIEELLYSPEQNDEHIGYLKDRKKPIIFSMARLDRVKNLTGLVEWY 595
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 401 AKNKRLRDLVNLVIVGGFFDASKSKDREEISEIKKMHSLIEKYQLKGQFRWITAQTDRTRNGELYRSIADTRGAFVQPAH 480
Cdd:PLN00142  596 GKNKRLRELVNLVVVGGFIDPSKSKDREEIAEIKKMHSLIEKYNLKGQFRWIAAQTNRVRNGELYRYIADTKGAFVQPAL 675
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 481 YEAFGLTVIEAMSCGLVTFATNQGGPAEIIVDGVSGFHIDPSNGEESSDKIADFFEKSGMDPDYWNMFSNEGLQRINECY 560
Cdd:PLN00142  676 YEAFGLTVVEAMTCGLPTFATCQGGPAEIIVDGVSGFHIDPYHGDEAANKIADFFEKCKEDPSYWNKISDAGLQRIYECY 755
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1063734715 561 TWKIYANKVINMGSTYSYWRHLNKDQKLAKQRYIHSFYNLQYRNLVKTIPILSD 614
Cdd:PLN00142  756 TWKIYAERLLTLGGVYGFWKYVSKLERRETRRYLEMFYNLKFRELAKTVPLAVD 809
sucr_synth TIGR02470
sucrose synthase; This model represents sucrose synthase, an enzyme that, despite its name, ...
1-610 0e+00

sucrose synthase; This model represents sucrose synthase, an enzyme that, despite its name, generally uses rather produces sucrose. Sucrose plus UDP (or ADP) becomes D-fructose plus UDP-glucose (or ADP-glucose), which is then available for cell wall (or starch) biosynthesis. The enzyme is homologous to sucrose phosphate synthase, which catalyzes the penultimate step in sucrose synthesis. Sucrose synthase is found, so far, exclusively in plants and cyanobacteria. [Energy metabolism, Biosynthesis and degradation of polysaccharides]


Pssm-ID: 274149 [Multi-domain]  Cd Length: 784  Bit Score: 1051.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715   1 MMNETLNTARKLEMSLILADVFLSELPKDTPFQAFELRFKECGFEKGWGESAGRVKETMRILSEILQAPDPQNIDRFFAR 80
Cdd:TIGR02470 172 MINDRIQSVSHLQSQLRKAEEFLSALPPDTPYSEFEFELQELGFEPGWGDTAQRVLETLHLLDDLLEAPDPSVLEAFLGR 251
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715  81 VPRIFNVVIFSVHGYFGQTDVLGLPDTGGQVVYILDQVKALEDELLQRINSQGLNFKPQILVVTRLIPDAKKTKCNQELE 160
Cdd:TIGR02470 252 IPMVFNVVILSPHGYFGQENVLGLPDTGGQVVYILDQVRALENEMLQRIKLQGLEITPKILIVTRLIPDAEGTTCNQRLE 331
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 161 PIFGTKYSNILRIPFVTENGI-LRRWVSRFDIYPYLERFTKDATTKILDILEGKPDLIIGNYTDGNLVASLMANKLGITQ 239
Cdd:TIGR02470 332 KVYGTEHAWILRVPFRTENGIiLRNWISRFEIWPYLETFAEDAEKEILAELQGKPDLIIGNYSDGNLVASLLARKLGVTQ 411
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 240 ATIAHALEKTKYEDSDIKWKEFDPKYHFSSQFTADLISMNSADFIIASTYQEIAGSKERAGQYESHMSFTVPGLYRVVSG 319
Cdd:TIGR02470 412 CTIAHALEKTKYPDSDIYWQEFEDKYHFSCQFTADLIAMNAADFIITSTYQEIAGTKDSVGQYESHQAFTMPGLYRVVHG 491
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 320 INVFDPRFNIAAPGADDSIYFPFTAQDRRFTKFYTSIDELLYSQSENDEHIGYLVDKKKPIIFSMARLDVVKNLTGLTEW 399
Cdd:TIGR02470 492 IDVFDPKFNIVSPGADESIYFPYSDKEKRLTNLHPEIEELLFSLEDNDEHYGYLKDPNKPIIFSMARLDRVKNLTGLVEC 571
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 400 YAKNKRLRDLVNLVIVGGFFDASKSKDREEISEIKKMHSLIEKYQLKGQFRWITAQTDRTRNGELYRSIADTRGAFVQPA 479
Cdd:TIGR02470 572 YGRSPKLRELVNLVVVAGKLDAKESKDREEQAEIEKMHNLIDQYQLHGQIRWIGAQLNRVRNGELYRYIADTKGIFVQPA 651
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 480 HYEAFGLTVIEAMSCGLVTFATNQGGPAEIIVDGVSGFHIDPSNGEESSDKIADFFEKSGMDPDYWNMFSNEGLQRINEC 559
Cdd:TIGR02470 652 LYEAFGLTVLEAMTCGLPTFATRFGGPLEIIQDGVSGFHIDPYHGEEAAEKIVDFFEKCDEDPSYWQKISQGGLQRIYEK 731
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1063734715 560 YTWKIYANKVINMGSTYSYWRHLNKDQKLAKQRYIHSFYNLQYRNLVKTIP 610
Cdd:TIGR02470 732 YTWKIYSERLLTLAGIYGFWKFVSKLEREETRRYLEMFYHLKYRPLAEAVP 782
Sucrose_synth pfam00862
Sucrose synthase; Sucrose synthases catalyze the synthesis of sucrose from UDP-glucose and ...
1-361 0e+00

Sucrose synthase; Sucrose synthases catalyze the synthesis of sucrose from UDP-glucose and fructose. This family includes the bulk of the sucrose synthase protein. However the carboxyl terminal region of the sucrose synthases belongs to the glycosyl transferase family pfam00534.


Pssm-ID: 395692  Cd Length: 540  Bit Score: 761.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715   1 MMNETLNTARKLEMSLILADVFLSELPKDTPFQAFELRFKECGFEKGWGESAGRVKETMRILSEILQAPDPQNIDRFFAR 80
Cdd:pfam00862 180 MINDRINSVSKLQSALIKAEEFLSKLPKDTPYEEFEYRLQELGFEKGWGDTAERVKETMHLLSELLQAPDPSTLEKFLGR 259
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715  81 VPRIFNVVIFSVHGYFGQTDVLGLPDTGGQVVYILDQVKALEDELLQRINSQGLNFKPQILVVTRLIPDAKKTKCNQELE 160
Cdd:pfam00862 260 IPMVFNVVILSPHGYFGQANVLGLPDTGGQVVYILDQVRALENELLLRIKQQGLDIKPQILVVTRLIPEARGTTCNQELE 339
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 161 PIFGTKYSNILRIPFVTENGILRRWVSRFDIYPYLERFTKDATTKILDILEGKPDLIIGNYTDGNLVASLMANKLGITQA 240
Cdd:pfam00862 340 KISGTKHSHILRVPFRTENGILRQWISRFDIWPYLERFTQDAAKEILAELEGKPDLIIGNYSDGNLVASLLAHKLGVTQC 419
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 241 TIAHALEKTKYEDSDIKWKEFDPKYHFSSQFTADLISMNSADFIIASTYQEIAGSKERAGQYESHMSFTVPGLYRVVSGI 320
Cdd:pfam00862 420 TIAHALEKTKYEDSDIYWKELEPKYHFSCQFTADLIAMNAADFIITSTYQEIAGSKDRVGQYESHTAFTLPGLYRVVSGI 499
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1063734715 321 NVFDPRFNIAAPGADDSIYFPFTAQDRRFTKFYTSIDELLY 361
Cdd:pfam00862 500 DVFDPKFNIVSPGADQSIYFPYTEKERRLTSLHPSIEELLY 540
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
86-566 1.91e-130

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: 389.68  E-value: 1.91e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715  86 NVVIFSVHGYFGQtdVLGLPDTGGQVVYILDQVKALedelLQRInsqglnfkPQILVVTRLIPDAKktkcnqeLEPIFGT 165
Cdd:cd03800     1 RIALISVHGSPLA--QPGGADTGGQNVYVLELARAL----AELG--------YQVDIFTRRISPAD-------PEVVEIA 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 166 KYSNILRIPFVTENGILRRWVsrfdiYPYLERFTKDATTKILDILeGKPDLIIGNYTDGNLVASLMANKLGITQATIAHA 245
Cdd:cd03800    60 PGARVIRVPAGPPEYLPKEEL-----WPYLEEFADGLLRFIAREG-GRYDLIHSHYWDSGLVGALLARRLGVPLVHTFHS 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 246 LEKTKYEDSDIKWKefdpkYHFSSQFTADLISMNSADFIIASTYQEIAGSKERAGQYESHMsftvpglyRVVSginvfdp 325
Cdd:cd03800   134 LGRVKYRHLGAQDT-----YHPSLRITAEEQILEAADRVIASTPQEADELISLYGADPSRI--------NVVP------- 193
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 326 rfniaaPGADDSIYFPFTAQDRRFTKFytsidellysqsendehigyLVDKKKPIIFSMARLDVVKNLTGLTEWYAKNKR 405
Cdd:cd03800   194 ------PGVDLERFFPVDRAEARRARL--------------------LLPPDKPVVLALGRLDPRKGIDTLVRAFAQLPE 247
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 406 LRDLVNLVIVGGFFDASKSKDREEISEIKKMHSLIEKYQLKGQFRwitaqtdRTRNGELYRSiadtRGAFVQPAHYEAFG 485
Cdd:cd03800   248 LRELANLVLVGGPSDDPLSMDREELAELAEELGLIDRVRFPGRVS-------RDDLPELYRA----ADVFVVPSLYEPFG 316
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 486 LTVIEAMSCGLVTFATNQGGPAEIIVDGVSGFHIDPSNGEESSDKIADFFEksgmDPDYWNMFSNEGLQRINECYTWKIY 565
Cdd:cd03800   317 LTAIEAMACGTPVVATAVGGLQDIVRDGRTGLLVDPHDPEALAAALRRLLD----DPALWQRLSRAGLERARAHYTWESV 392

                  .
gi 1063734715 566 A 566
Cdd:cd03800   393 A 393
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
464-572 3.73e-21

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 89.28  E-value: 3.73e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 464 LYRSiADtrgAFVQPAHYEAFGLTVIEAMSCGLVTFATNQGGPAEIIVDGVSGFHIDPSNGEESSDKIADFFEksgmDPD 543
Cdd:COG0438    17 LLAA-AD---VFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLE----DPE 88
                          90       100
                  ....*....|....*....|....*....
gi 1063734715 544 YWNMFSNEGLQRINECYTWKIYANKVINM 572
Cdd:COG0438    89 LRRRLGEAARERAEERFSWEAIAERLLAL 117
 
Name Accession Description Interval E-value
PLN00142 PLN00142
sucrose synthase
1-614 0e+00

sucrose synthase


Pssm-ID: 215073 [Multi-domain]  Cd Length: 815  Bit Score: 1315.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715   1 MMNETLNTARKLEMSLILADVFLSELPKDTPFQAFELRFKECGFEKGWGESAGRVKETMRILSEILQAPDPQNIDRFFAR 80
Cdd:PLN00142  196 MLNDRIQTLSKLQSALRKAEEYLSKLPKDTPYSEFEHRFQELGLEKGWGDTAERVLETIHLLLDLLQAPDPSTLEKFLGR 275
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715  81 VPRIFNVVIFSVHGYFGQTDVLGLPDTGGQVVYILDQVKALEDELLQRINSQGLNFKPQILVVTRLIPDAKKTKCNQELE 160
Cdd:PLN00142  276 IPMVFNVVIFSPHGYFGQANVLGLPDTGGQVVYILDQVRALENEMLLRIKQQGLDIKPQILIVTRLIPDAKGTTCNQRLE 355
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 161 PIFGTKYSNILRIPFVTENGILRRWVSRFDIYPYLERFTKDATTKILDILEGKPDLIIGNYTDGNLVASLMANKLGITQA 240
Cdd:PLN00142  356 KVSGTEHSHILRVPFRTEKGILRKWISRFDVWPYLETFAEDAASEILAELQGKPDLIIGNYSDGNLVASLLAHKLGVTQC 435
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 241 TIAHALEKTKYEDSDIKWKEFDPKYHFSSQFTADLISMNSADFIIASTYQEIAGSKERAGQYESHMSFTVPGLYRVVSGI 320
Cdd:PLN00142  436 TIAHALEKTKYPDSDIYWKKFDDKYHFSCQFTADLIAMNHADFIITSTYQEIAGSKDTVGQYESHTAFTLPGLYRVVHGI 515
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 321 NVFDPRFNIAAPGADDSIYFPFTAQDRRFTKFYTSIDELLYSQSENDEHIGYLVDKKKPIIFSMARLDVVKNLTGLTEWY 400
Cdd:PLN00142  516 DVFDPKFNIVSPGADMSIYFPYTEKQKRLTSLHPSIEELLYSPEQNDEHIGYLKDRKKPIIFSMARLDRVKNLTGLVEWY 595
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 401 AKNKRLRDLVNLVIVGGFFDASKSKDREEISEIKKMHSLIEKYQLKGQFRWITAQTDRTRNGELYRSIADTRGAFVQPAH 480
Cdd:PLN00142  596 GKNKRLRELVNLVVVGGFIDPSKSKDREEIAEIKKMHSLIEKYNLKGQFRWIAAQTNRVRNGELYRYIADTKGAFVQPAL 675
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 481 YEAFGLTVIEAMSCGLVTFATNQGGPAEIIVDGVSGFHIDPSNGEESSDKIADFFEKSGMDPDYWNMFSNEGLQRINECY 560
Cdd:PLN00142  676 YEAFGLTVVEAMTCGLPTFATCQGGPAEIIVDGVSGFHIDPYHGDEAANKIADFFEKCKEDPSYWNKISDAGLQRIYECY 755
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1063734715 561 TWKIYANKVINMGSTYSYWRHLNKDQKLAKQRYIHSFYNLQYRNLVKTIPILSD 614
Cdd:PLN00142  756 TWKIYAERLLTLGGVYGFWKYVSKLERRETRRYLEMFYNLKFRELAKTVPLAVD 809
sucr_synth TIGR02470
sucrose synthase; This model represents sucrose synthase, an enzyme that, despite its name, ...
1-610 0e+00

sucrose synthase; This model represents sucrose synthase, an enzyme that, despite its name, generally uses rather produces sucrose. Sucrose plus UDP (or ADP) becomes D-fructose plus UDP-glucose (or ADP-glucose), which is then available for cell wall (or starch) biosynthesis. The enzyme is homologous to sucrose phosphate synthase, which catalyzes the penultimate step in sucrose synthesis. Sucrose synthase is found, so far, exclusively in plants and cyanobacteria. [Energy metabolism, Biosynthesis and degradation of polysaccharides]


Pssm-ID: 274149 [Multi-domain]  Cd Length: 784  Bit Score: 1051.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715   1 MMNETLNTARKLEMSLILADVFLSELPKDTPFQAFELRFKECGFEKGWGESAGRVKETMRILSEILQAPDPQNIDRFFAR 80
Cdd:TIGR02470 172 MINDRIQSVSHLQSQLRKAEEFLSALPPDTPYSEFEFELQELGFEPGWGDTAQRVLETLHLLDDLLEAPDPSVLEAFLGR 251
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715  81 VPRIFNVVIFSVHGYFGQTDVLGLPDTGGQVVYILDQVKALEDELLQRINSQGLNFKPQILVVTRLIPDAKKTKCNQELE 160
Cdd:TIGR02470 252 IPMVFNVVILSPHGYFGQENVLGLPDTGGQVVYILDQVRALENEMLQRIKLQGLEITPKILIVTRLIPDAEGTTCNQRLE 331
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 161 PIFGTKYSNILRIPFVTENGI-LRRWVSRFDIYPYLERFTKDATTKILDILEGKPDLIIGNYTDGNLVASLMANKLGITQ 239
Cdd:TIGR02470 332 KVYGTEHAWILRVPFRTENGIiLRNWISRFEIWPYLETFAEDAEKEILAELQGKPDLIIGNYSDGNLVASLLARKLGVTQ 411
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 240 ATIAHALEKTKYEDSDIKWKEFDPKYHFSSQFTADLISMNSADFIIASTYQEIAGSKERAGQYESHMSFTVPGLYRVVSG 319
Cdd:TIGR02470 412 CTIAHALEKTKYPDSDIYWQEFEDKYHFSCQFTADLIAMNAADFIITSTYQEIAGTKDSVGQYESHQAFTMPGLYRVVHG 491
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 320 INVFDPRFNIAAPGADDSIYFPFTAQDRRFTKFYTSIDELLYSQSENDEHIGYLVDKKKPIIFSMARLDVVKNLTGLTEW 399
Cdd:TIGR02470 492 IDVFDPKFNIVSPGADESIYFPYSDKEKRLTNLHPEIEELLFSLEDNDEHYGYLKDPNKPIIFSMARLDRVKNLTGLVEC 571
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 400 YAKNKRLRDLVNLVIVGGFFDASKSKDREEISEIKKMHSLIEKYQLKGQFRWITAQTDRTRNGELYRSIADTRGAFVQPA 479
Cdd:TIGR02470 572 YGRSPKLRELVNLVVVAGKLDAKESKDREEQAEIEKMHNLIDQYQLHGQIRWIGAQLNRVRNGELYRYIADTKGIFVQPA 651
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 480 HYEAFGLTVIEAMSCGLVTFATNQGGPAEIIVDGVSGFHIDPSNGEESSDKIADFFEKSGMDPDYWNMFSNEGLQRINEC 559
Cdd:TIGR02470 652 LYEAFGLTVLEAMTCGLPTFATRFGGPLEIIQDGVSGFHIDPYHGEEAAEKIVDFFEKCDEDPSYWQKISQGGLQRIYEK 731
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1063734715 560 YTWKIYANKVINMGSTYSYWRHLNKDQKLAKQRYIHSFYNLQYRNLVKTIP 610
Cdd:TIGR02470 732 YTWKIYSERLLTLAGIYGFWKFVSKLEREETRRYLEMFYHLKYRPLAEAVP 782
Sucrose_synth pfam00862
Sucrose synthase; Sucrose synthases catalyze the synthesis of sucrose from UDP-glucose and ...
1-361 0e+00

Sucrose synthase; Sucrose synthases catalyze the synthesis of sucrose from UDP-glucose and fructose. This family includes the bulk of the sucrose synthase protein. However the carboxyl terminal region of the sucrose synthases belongs to the glycosyl transferase family pfam00534.


Pssm-ID: 395692  Cd Length: 540  Bit Score: 761.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715   1 MMNETLNTARKLEMSLILADVFLSELPKDTPFQAFELRFKECGFEKGWGESAGRVKETMRILSEILQAPDPQNIDRFFAR 80
Cdd:pfam00862 180 MINDRINSVSKLQSALIKAEEFLSKLPKDTPYEEFEYRLQELGFEKGWGDTAERVKETMHLLSELLQAPDPSTLEKFLGR 259
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715  81 VPRIFNVVIFSVHGYFGQTDVLGLPDTGGQVVYILDQVKALEDELLQRINSQGLNFKPQILVVTRLIPDAKKTKCNQELE 160
Cdd:pfam00862 260 IPMVFNVVILSPHGYFGQANVLGLPDTGGQVVYILDQVRALENELLLRIKQQGLDIKPQILVVTRLIPEARGTTCNQELE 339
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 161 PIFGTKYSNILRIPFVTENGILRRWVSRFDIYPYLERFTKDATTKILDILEGKPDLIIGNYTDGNLVASLMANKLGITQA 240
Cdd:pfam00862 340 KISGTKHSHILRVPFRTENGILRQWISRFDIWPYLERFTQDAAKEILAELEGKPDLIIGNYSDGNLVASLLAHKLGVTQC 419
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 241 TIAHALEKTKYEDSDIKWKEFDPKYHFSSQFTADLISMNSADFIIASTYQEIAGSKERAGQYESHMSFTVPGLYRVVSGI 320
Cdd:pfam00862 420 TIAHALEKTKYEDSDIYWKELEPKYHFSCQFTADLIAMNAADFIITSTYQEIAGSKDRVGQYESHTAFTLPGLYRVVSGI 499
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1063734715 321 NVFDPRFNIAAPGADDSIYFPFTAQDRRFTKFYTSIDELLY 361
Cdd:pfam00862 500 DVFDPKFNIVSPGADQSIYFPYTEKERRLTSLHPSIEELLY 540
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
86-566 1.91e-130

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: 389.68  E-value: 1.91e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715  86 NVVIFSVHGYFGQtdVLGLPDTGGQVVYILDQVKALedelLQRInsqglnfkPQILVVTRLIPDAKktkcnqeLEPIFGT 165
Cdd:cd03800     1 RIALISVHGSPLA--QPGGADTGGQNVYVLELARAL----AELG--------YQVDIFTRRISPAD-------PEVVEIA 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 166 KYSNILRIPFVTENGILRRWVsrfdiYPYLERFTKDATTKILDILeGKPDLIIGNYTDGNLVASLMANKLGITQATIAHA 245
Cdd:cd03800    60 PGARVIRVPAGPPEYLPKEEL-----WPYLEEFADGLLRFIAREG-GRYDLIHSHYWDSGLVGALLARRLGVPLVHTFHS 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 246 LEKTKYEDSDIKWKefdpkYHFSSQFTADLISMNSADFIIASTYQEIAGSKERAGQYESHMsftvpglyRVVSginvfdp 325
Cdd:cd03800   134 LGRVKYRHLGAQDT-----YHPSLRITAEEQILEAADRVIASTPQEADELISLYGADPSRI--------NVVP------- 193
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 326 rfniaaPGADDSIYFPFTAQDRRFTKFytsidellysqsendehigyLVDKKKPIIFSMARLDVVKNLTGLTEWYAKNKR 405
Cdd:cd03800   194 ------PGVDLERFFPVDRAEARRARL--------------------LLPPDKPVVLALGRLDPRKGIDTLVRAFAQLPE 247
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 406 LRDLVNLVIVGGFFDASKSKDREEISEIKKMHSLIEKYQLKGQFRwitaqtdRTRNGELYRSiadtRGAFVQPAHYEAFG 485
Cdd:cd03800   248 LRELANLVLVGGPSDDPLSMDREELAELAEELGLIDRVRFPGRVS-------RDDLPELYRA----ADVFVVPSLYEPFG 316
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 486 LTVIEAMSCGLVTFATNQGGPAEIIVDGVSGFHIDPSNGEESSDKIADFFEksgmDPDYWNMFSNEGLQRINECYTWKIY 565
Cdd:cd03800   317 LTAIEAMACGTPVVATAVGGLQDIVRDGRTGLLVDPHDPEALAAALRRLLD----DPALWQRLSRAGLERARAHYTWESV 392

                  .
gi 1063734715 566 A 566
Cdd:cd03800   393 A 393
sucrsPsyn_pln TIGR02468
sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this ...
61-579 1.20e-35

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: 144.15  E-value: 1.20e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715   61 ILSEILQAPDPqniDRFFARVPRIFN-----------------VVIFSVHGYF-GQTDVLGL-PDTGGQVVYILDQVKAL 121
Cdd:TIGR02468  132 VAGDISVAGGE---PSTKGRLPRISSnlemetwsdqqkekklyIVLISLHGLVrGENMELGRdSDTGGQVKYVVELARAL 208
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715  122 E--------DELLQRINSQGLNF---KPQILVVTRlipdakKTKCNQELEPIFGTKYsnILRIPFvtenGILRRWVSRFD 190
Cdd:TIGR02468  209 GsmpgvyrvDLLTRQVSSPDVDWsygEPTEMLTPR------SSENDGDEMGESSGAY--IIRIPF----GPRDKYIPKEE 276
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715  191 IYPYLERFTKDATTKILD--------ILEGK---PDLIIGNYTDGNLVASLMANKLGITQATIAHALEKTKYED----SD 255
Cdd:TIGR02468  277 LWPYIPEFVDGALSHIVNmskvlgeqIGSGHpvwPYVIHGHYADAGDSAALLSGALNVPMVLTGHSLGRDKLEQllkqGR 356
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715  256 IKWKEFDPKYHFSSQFTADLISMNSADFIIASTYQEIagsKERAGQYEShmsFTvPGLYRV--------VSGINVFDPRF 327
Cdd:TIGR02468  357 MSKEEINSTYKIMRRIEAEELSLDASEIVITSTRQEI---EEQWGLYDG---FD-VILERKlrararrgVSCYGRFMPRM 429
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715  328 NIAAPGADdsiyfpFTAQDRRFTKFYTSIDELLYSQSEND-----EHIGYLVDKKKPIIFSMARLDVVKNLTGLTEWYAK 402
Cdd:TIGR02468  430 AVIPPGME------FSHIVPHDGDMDGETEGNEEHPAKPDppiwsEIMRFFTNPRKPMILALARPDPKKNITTLVKAFGE 503
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715  403 NKRLRDLVNLVIVGGffdaskskDREEISEIKKMHS--------LIEKYQLKGQFRWIT--AQTDRTrngELYRSIADTR 472
Cdd:TIGR02468  504 CRPLRELANLTLIMG--------NRDDIDEMSSGSSsvltsvlkLIDKYDLYGQVAYPKhhKQSDVP---DIYRLAAKTK 572
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715  473 GAFVQPAHYEAFGLTVIEAMSCGLVTFATNQGGPAEIIVDGVSGFHIDPsngeESSDKIADFFEKSGMDPDYWNMFSNEG 552
Cdd:TIGR02468  573 GVFINPAFIEPFGLTLIEAAAHGLPMVATKNGGPVDIHRVLDNGLLVDP----HDQQAIADALLKLVADKQLWAECRQNG 648
                          570       580       590
                   ....*....|....*....|....*....|.
gi 1063734715  553 LQRINEcYTW----KIYANKVINMGSTYSYW 579
Cdd:TIGR02468  649 LKNIHL-FSWpehcKTYLSRIASCRPRHPQW 678
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
377-555 7.57e-32

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: 120.84  E-value: 7.57e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 377 KKPIIFSMARLDVVKNLTGLTEWYAKNKRLRDLVNLVIVGgffdaskskdreEISEIKKMHSLIEKYQLKGQFRWITAQt 456
Cdd:pfam00534   1 KKKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAG------------DGEEEKRLKKLAEKLGLGDNVIFLGFV- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 457 DRTRNGELYRsIADtrgAFVQPAHYEAFGLTVIEAMSCGLVTFATNQGGPAEIIVDGVSGFHIDPSNGEESSDKIADFFE 536
Cdd:pfam00534  68 SDEDLPELLK-IAD---VFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKLLE 143
                         170
                  ....*....|....*....
gi 1063734715 537 ksgmDPDYWNMFSNEGLQR 555
Cdd:pfam00534 144 ----DEELRERLGENARKR 158
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
346-572 2.88e-23

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: 101.85  E-value: 2.88e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 346 DRRFTKFYTSIDELLYSQSENDEhigYLVDKKKPIIFSMARLDVVKNLTGLTEWYAKNKRLRDLVNLVIVGGffdasksk 425
Cdd:cd03801   163 PEKIVVIPNGVDLERFSPPLRRK---LGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVGG-------- 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 426 DREEISEIKKMhslieKYQLKGQFRWITAQTDRTRNgELYRSiADtrgAFVQPAHYEAFGLTVIEAMSCGLVTFATNQGG 505
Cdd:cd03801   232 DGPLRAELEEL-----ELGLGDRVRFLGFVPDEELP-ALYAA-AD---VFVLPSRYEGFGLVVLEAMAAGLPVVATDVGG 301
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063734715 506 PAEIIVDGVSGFHIDPSNGEESSDKIADFFEksgmDPDYWNMFSNEGLQRINECYTWKIYANKVINM 572
Cdd:cd03801   302 LPEVVEDGEGGLVVPPDDVEALADALLRLLA----DPELRARLGRAARERVAERFSWERVAERLLDL 364
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
464-572 3.73e-21

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 89.28  E-value: 3.73e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 464 LYRSiADtrgAFVQPAHYEAFGLTVIEAMSCGLVTFATNQGGPAEIIVDGVSGFHIDPSNGEESSDKIADFFEksgmDPD 543
Cdd:COG0438    17 LLAA-AD---VFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLE----DPE 88
                          90       100
                  ....*....|....*....|....*....
gi 1063734715 544 YWNMFSNEGLQRINECYTWKIYANKVINM 572
Cdd:COG0438    89 LRRRLGEAARERAEERFSWEAIAERLLAL 117
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
376-561 3.52e-16

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: 80.33  E-value: 3.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 376 KKKPIIFSMARLDVVKNLTGLTEwYAKNKRLRDL-VNLVIVGGFfdaskskDREEISEIkkmhsLIEKYQLKGQFRWita 454
Cdd:cd03808   187 SEKVVFLFVARLLKDKGIDELIE-AAKILKKKGPnVRFLLVGDG-------ELENPSEI-----LIEKLGLEGRIEF--- 250
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 455 qTDRTRNGELYRSIADtrgAFVQPAHYEAFGLTVIEAMSCGLVTFATNQGGPAEIIVDGVSGFHIDPSNGEESSDKIADF 534
Cdd:cd03808   251 -LGFRSDVPELLAESD---VFVLPSYREGLPRSLLEAMAAGRPVITTDVPGCRELVIDGVNGFLVPPGDVEALADAIEKL 326
                         170       180
                  ....*....|....*....|....*..
gi 1063734715 535 FEksgmDPDYWNMFSNEGLQRINECYT 561
Cdd:cd03808   327 IE----DPELRKEMGEAARKRVEEKFD 349
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
342-571 3.00e-15

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: 77.79  E-value: 3.00e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 342 FTAQD---------RRFTKFYTSIDELLYSQSENDEHIGYLVDKKkPIIFSMARLDVVKNLTGLTEWYAKNKRLRDLVNL 412
Cdd:cd03809   148 ATRDDiikfygvppEKIVVIPLGVDPSFFPPESAAVLIAKYLLPE-PYFLYVGTLEPRKNHERLLKAFALLKKQGGDLKL 226
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 413 VIVGGffdasKSKDREEIseikkmHSLIEKYQLKGQFRWitaqTDRTRNGEL---YRSiADtrgAFVQPAHYEAFGLTVI 489
Cdd:cd03809   227 VIVGG-----KGWEDEEL------LDLVKKLGLGGRVRF----LGYVSDEDLpalYRG-AR---AFVFPSLYEGFGLPVL 287
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 490 EAMSCGLVTFATNqgGPA--EIIvdGVSGFHIDPSNGEEssdkIADFFEKSGMDPDYWNMFSNEGLQRInECYTWKIYAN 567
Cdd:cd03809   288 EAMACGTPVIASN--ISVlpEVA--GDAALYFDPLDPES----IADAILRLLEDPSLREELIRKGLERA-KKFSWEKTAE 358

                  ....
gi 1063734715 568 KVIN 571
Cdd:cd03809   359 KTLE 362
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
375-537 6.90e-15

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: 76.63  E-value: 6.90e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 375 DKKKPIIFSMARLDVVKNLTGLTEWYAKNKRLRDLVNLVIVGgffdasKSKDREEIseikkmHSLIEKYQLKGQFRWITA 454
Cdd:cd03811   185 PEDGPVILAVGRLDPQKGHDLLIEAFAKLRKKYPDVKLVILG------DGPLREEL------EKLAKELGLAERVIFLGF 252
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 455 QTDrtrngeLYRSIADTRgAFVQPAHYEAFGLTVIEAMSCGLVTFATNQGGPAEIIVDGVSGFHIDPSNGEESSDKIADF 534
Cdd:cd03811   253 QSN------PYPYLKKAD-LFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPREILDDGENGLLVPDGDAAALAGILAAL 325

                  ...
gi 1063734715 535 FEK 537
Cdd:cd03811   326 LQK 328
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
432-558 2.64e-13

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: 72.00  E-value: 2.64e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 432 EIKKMHSLIEKYQLKGQFRWITAQTDRtrngELYRSIADTrgaFVQPAHYEAFGLTVIEAMSCGLVTFATNQGGPAEIIV 511
Cdd:cd04962   237 ERVPAEELARELGVEDRVLFLGKQDDV----EELLSIADL---FLLPSEKESFGLAALEAMACGVPVVSSNAGGIPEVVK 309
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1063734715 512 DGVSGFHIDPSNGEESSDKIADFFEksgmDPDYWNMFSNEGLQRINE 558
Cdd:cd04962   310 HGETGFLSDVGDVDAMAKSALSILE----DDELYNRMGRAARKRAAE 352
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
355-570 8.84e-13

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: 70.49  E-value: 8.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 355 SIDELLYSQSENDEHIGylvdKKKPIIFSMARLDVVKNLTGLTEWYAK-NKRLRDLVnLVIVGGFfdaskskdreeiSEI 433
Cdd:cd03798   181 GVDPARFQPEDRGLGLP----LDAFVILFVGRLIPRKGIDLLLEAFARlAKARPDVV-LLIVGDG------------PLR 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 434 KKMHSLIEKYQLKGQFRwITAQTDRTRNGELYRSiADtrgAFVQPAHYEAFGLTVIEAMSCGLVTFATNQGGPAEIIVDG 513
Cdd:cd03798   244 EALRALAEDLGLGDRVT-FTGRLPHEQVPAYYRA-CD---VFVLPSRHEGFGLVLLEAMACGLPVVATDVGGIPEVVGDP 318
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1063734715 514 VSGFHIDPSNGEESSDKIADFfeksgMDPDYWNMFSNEGLQRINECYTWKIYANKVI 570
Cdd:cd03798   319 ETGLLVPPGDADALAAALRRA-----LAEPYLRELGEAARARVAERFSWVKAADRIA 370
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
378-536 1.34e-12

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 65.23  E-value: 1.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 378 KPIIFSMARLDV-VKNLtgltEWYAKN-KRLR---DLVNLVIVGgffdaskSKDREEISEIKKmhsliekyQLKGQFRWI 452
Cdd:pfam13692   1 RPVILFVGRLHPnVKGV----DYLLEAvPLLRkrdNDVRLVIVG-------DGPEEELEELAA--------GLEDRVIFT 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 453 TAQTDRtrnGELYRSiADtrgAFVQPAHYEAFGLTVIEAMSCGLVTFATNQGGPAEIIvDGVSGFHIDPSNGEESSDKIA 532
Cdd:pfam13692  62 GFVEDL---AELLAA-AD---VFVLPSLYEGFGLKLLEAMAAGLPVVATDVGGIPELV-DGENGLLVPPGDPEALAEAIL 133

                  ....
gi 1063734715 533 DFFE 536
Cdd:pfam13692 134 RLLE 137
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
374-558 8.18e-12

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: 67.34  E-value: 8.18e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 374 VDKKKPIIFSMARLDVVKNLTGLTEWYAK-NKRLRDLVnLVIVGgffdasKSKDREEISEIKKMHSLIEKYQLKGQfrwi 452
Cdd:cd03807   186 LAEDRRVIGIVGRLHPVKDHSDLLRAAALlVETHPDLR-LLLVG------RGPERPNLERLLLELGLEDRVHLLGE---- 254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 453 taqtdRTRNGELYRsIADtrgAFVQPAHYEAFGLTVIEAMSCGLVTFATNQGGPAEIIVDGvSGFHIDPsngeESSDKIA 532
Cdd:cd03807   255 -----RSDVPALLP-AMD---IFVLSSRTEGFPNALLEAMACGLPVVATDVGGAAELVDDG-TGFLVPA----GDPQALA 320
                         170       180
                  ....*....|....*....|....*.
gi 1063734715 533 DFFEKSGMDPDYWNMFSNEGLQRINE 558
Cdd:cd03807   321 DAIRALLEDPEKRARLGRAARERIAN 346
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
430-542 1.42e-11

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: 66.58  E-value: 1.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 430 ISEIKKMHSLIEKYQLKGQFRWITAQTDRTRNGELYRSIADTR----GAFVQ---PAHY-------------EAFGLTVI 489
Cdd:cd03823   200 LTEEKGIDLLVEAFKRLPREDIELVIAGHGPLSDERQIEGGRRiaflGRVPTddiKDFYekidvlvvpsiwpEPFGLVVR 279
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1063734715 490 EAMSCGLVTFATNQGGPAEIIVDGVSGFHIDPSNGEESSDKIADFFEKSGMDP 542
Cdd:cd03823   280 EAIAAGLPVIASDLGGIAELIQPGVNGLLFAPGDAEDLAAAMRRLLTDPALLE 332
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
227-563 5.71e-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: 64.57  E-value: 5.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 227 VASLMANKLG-----ITQATIAHALEKTKYE-DSDIKWKE--------FDPKYHFSSQFTA--DLISMNSADFIIAS--- 287
Cdd:cd03820    18 VAINLANHLAkkgydVTIISLDSAEKPPFYElDDNIKIKNlgdrkyshFKLLLKYFKKVRRlrKYLKNNKPDVVISFrts 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 288 --TYQEIAGSKERAGQYEsHMSftvpglYRVVSGINVFDPRFNIAAPGADDsiyfpFTAQdrrftkfyTSIDELLYSQSE 365
Cdd:cd03820    98 llTFLALIGLKSKLIVWE-HNN------YEAYNKGLRRLLLRRLLYKRADK-----IVVL--------TEADKLKKYKQP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 366 N-----------DEHIGYLVDKKKPIIFSMARLDVVKNLTGLTEWYAKNKRLRDLVNLVIVGgffdaskskDREEISEIK 434
Cdd:cd03820   158 NsnvvvipnplsFPSEEPSTNLKSKRILAVGRLTYQKGFDLLIEAWALIAKKHPDWKLRIYG---------DGPEREELE 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 435 KmhsLIEKYQLKGQFRWITaqtdRTRN-GELYRSIAdtrgAFVQPAHYEAFGLTVIEAMSCGL--VTFATNqGGPAEIIV 511
Cdd:cd03820   229 K---LIDKLGLEDRVKLLG----PTKNiAEEYANSS----IFVLSSRYEGFPMVLLEAMAYGLpiISFDCP-TGPSEIIE 296
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1063734715 512 DGVSGFHIDPSNGEESSDKIADFFEksgmDPDYWNMFSNEGLQRInECYTWK 563
Cdd:cd03820   297 DGENGLLVPNGDVDALAEALLRLME----DEELRKKMGKNARKNA-ERFSIE 343
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
383-519 8.27e-11

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: 62.42  E-value: 8.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 383 SMARLDVVKNLTGLTEWYAKNKRLRDLVNLVIVGGffdaskSKDREEISEikkmhsLIEKYQLKGQFRWITAQTDRTRNg 462
Cdd:cd01635   115 SVGRLVPEKGIDLLLEALALLKARLPDLVLVLVGG------GGEREEEEA------LAAALGLLERVVIIGGLVDDEVL- 181
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1063734715 463 ELYRSIADtrgAFVQPAHYEAFGLTVIEAMSCGLVTFATNQGGPAEIIVDGVSGFHI 519
Cdd:cd01635   182 ELLLAAAD---VFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
GT4_ALG2-like cd03805
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ...
342-558 1.05e-10

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: 64.15  E-value: 1.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 342 FTAQ--DRRFTKFYTSIDELLY---------SQSENDEHIGYLVDKKKPIIFSMARLDVVKNLTGLTEWYAK---NKRLR 407
Cdd:cd03805   164 FTAGvfKKTFPSLAKNPPEVLYpcvdtdsfdSTSEDPDPGDLIAKSNKKFFLSINRFERKKNIALAIEAFAKlkqKLPEF 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 408 DLVNLVIVGGFfDASKSKDREEISEIKkmhSLIEKYQ-LKGQFRWITAQTDRTRNgELYRSiadTRGAFVQPAHyEAFGL 486
Cdd:cd03805   244 ENVRLVIAGGY-DPRVAENVEYLEELQ---RLAEELLnVEDQVLFLRSISDSQKE-QLLSS---ALALLYTPSN-EHFGI 314
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063734715 487 TVIEAMSCGLVTFATNQGGPAEIIVDGVSGFHIDPsNGEESSDKIADFFEksgmDPDYWNMFSNEGLQRINE 558
Cdd:cd03805   315 VPLEAMYAGKPVIACNSGGPLETVVEGVTGFLCEP-TPEAFAEAMLKLAN----DPDLADRMGAAGRKRVKE 381
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
375-555 6.88e-10

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: 61.14  E-value: 6.88e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 375 DKKKPIIFSMARLDVVKNLTGLTEWYAKNKRLRDlVNLVIVGgffdasKSKDREEISEIKKMHSLIEKYQLKGqfrWIta 454
Cdd:cd03817   198 PPDEPILLYVGRLAKEKNIDFLLRAFAELKKEPN-IKLVIVG------DGPEREELKELARELGLADKVIFTG---FV-- 265
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 455 qtDRTRNGELYRsIADtrgAFVQPAHYEAFGLTVIEAMSCGLVTFATNQGGPAEIIVDGVSGFHIDPSNGEessdkIADF 534
Cdd:cd03817   266 --PREELPEYYK-AAD---LFVFASTTETQGLVYLEAMAAGLPVVAAKDPAASELVEDGENGFLFEPNDET-----LAEK 334
                         170       180
                  ....*....|....*....|.
gi 1063734715 535 FEKSGMDPDYWNMFSNEGLQR 555
Cdd:cd03817   335 LLHLRENLELLRKLSKNAEIS 355
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
481-521 8.32e-10

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: 60.76  E-value: 8.32e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1063734715 481 YEAFGLTVIEAMSCGLVTFATNQGGPAEIIVDGVSGFHIDP 521
Cdd:cd03802   250 DEPFGLVMIEAMACGTPVIAYRRGGLPEVIQHGETGFLVDS 290
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
373-536 3.23e-09

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: 59.23  E-value: 3.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 373 LVDKKKPIIFSMARLDVVKNLTGLTEWYAKNKRLRDlVNLVIVGGffdaskSKDREEISEIK-KMHSLIEKyqlkgqfrw 451
Cdd:cd03814   193 LGPPGRPLLLYVGRLAPEKNLEALLDADLPLAASPP-VRLVVVGD------GPARAELEARGpDVIFTGFL--------- 256
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 452 itaqtDRTRNGELYRSiADtrgAFVQPAHYEAFGLTVIEAMSCGLVTFATNQGGPAEIIVDGVSGFHIDPSNGEESSDKI 531
Cdd:cd03814   257 -----TGEELARAYAS-AD---VFVFPSRTETFGLVVLEAMASGLPVVAADAGGPRDIVRPGGTGALVEPGDAAAFAAAL 327

                  ....*
gi 1063734715 532 ADFFE 536
Cdd:cd03814   328 RALLE 332
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
363-531 7.97e-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: 57.75  E-value: 7.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 363 QSENDEHIGYLVDKKKPIIFSMARLDVVKNLTGLTEWYAKNKRLRDLVnLVIVGgffDASkskDREEiseikkMHSLIEK 442
Cdd:cd03819   167 EAEAEERAQLGLPEGKPVVGYVGRLSPEKGWLLLVDAAAELKDEPDFR-LLVAG---DGP---ERDE------IRRLVER 233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 443 YQLKGQFRwITAQTDRTRNgelYRSIADTrgaFVQPAHYEAFGLTVIEAMSCGLVTFATNQGGPAEIIVDGVSGFHIDPS 522
Cdd:cd03819   234 LGLRDRVT-FTGFREDVPA---ALAASDV---VVLPSLHEEFGRVALEAMACGTPVVATDVGGAREIVVHGRTGLLVPPG 306

                  ....*....
gi 1063734715 523 NGEESSDKI 531
Cdd:cd03819   307 DAEALADAI 315
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
463-571 1.60e-08

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: 56.96  E-value: 1.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 463 ELYRSiADtrgAFVQPAHYEAFGLTVIEAMSCGLVTFATNQGGPAEIIVDGVSGFHIDPSNGEESSDKIADFFeksgMDP 542
Cdd:cd03825   259 DIYSA-AD---LFVHPSLADNLPNTLLEAMACGTPVVAFDTGGSPEIVQHGVTGYLVPPGDVQALAEAIEWLL----ANP 330
                          90       100
                  ....*....|....*....|....*....
gi 1063734715 543 DYWNMFSNEGLQRINECYTWKIYANKVIN 571
Cdd:cd03825   331 KERESLGERARALAENHFDQRVQAQRYLE 359
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
380-550 1.84e-08

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: 56.68  E-value: 1.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 380 IIFSMARLDVVKNLTGLTEWYAKNKRLRDLVNLVIVGgffdasKSKDREEISEIKKMHSLIEKYQLKGQFRwitaqtdrt 459
Cdd:cd04951   190 VILNVGRLTEAKDYPNLLLAISELILSKNDFKLLIAG------DGPLRNELERLICNLNLVDRVILLGQIS--------- 254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 460 rNGELYRSIADTrgaFVQPAHYEAFGLTVIEAMSCGLVTFATNQGGPAEIIVDgvSGFHIDPSNGEESSDKIADFFEksg 539
Cdd:cd04951   255 -NISEYYNAADL---FVLSSEWEGFGLVVAEAMACERPVVATDAGGVAEVVGD--HNYVVPVSDPQLLAEKIKEIFD--- 325
                         170
                  ....*....|.
gi 1063734715 540 MDPDYWNMFSN 550
Cdd:cd04951   326 MSDEERDILGN 336
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
374-568 2.45e-08

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 56.34  E-value: 2.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 374 VDKKKPIIFSMARLDVVKNLTGLTEWYAKNKRLRDLVNLVIVGGFFDASKSkdrEEISEIKKMHSLIEkyQLKGQFRWIT 453
Cdd:PRK15484  189 ISPDETVLLYAGRISPDKGILLLMQAFEKLATAHSNLKLVVVGDPTASSKG---EKAAYQKKVLEAAK--RIGDRCIMLG 263
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 454 AQT-DRTRNgelYRSIADTrgaFVQPAHY-EAFGLTVIEAMSCGLVTFATNQGGPAEIIVDGVSGFHI-DPSngeeSSDK 530
Cdd:PRK15484  264 GQPpEKMHN---YYPLADL---VVVPSQVeEAFCMVAVEAMAAGKPVLASTKGGITEFVLEGITGYHLaEPM----TSDS 333
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1063734715 531 IADFFEKSGMDPDYWNMfSNEGLQRINECYTWKIYANK 568
Cdd:PRK15484  334 IISDINRTLADPELTQI-AEQAKDFVFSKYSWEGVTQR 370
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
378-571 9.19e-08

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: 54.68  E-value: 9.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 378 KPIIFSMARLDVVKNLTGLTEWYAKNKRLRDLVNLVIVGgffdaskskdREEISEIKKMHsLIEKYQLKGQFRWITAQTD 457
Cdd:cd03821   204 RRIILFLGRIHPKKGLDLLIRAARKLAEQGRDWHLVIAG----------PDDGAYPAFLQ-LQSSLGLGDRVTFTGPLYG 272
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 458 RTRnGELYRSiADtrgAFVQPAHYEAFGLTVIEAMSCGLVTFATNQGGPAEIIVDGvSGFHIDPsNGEESSDKIADFFEK 537
Cdd:cd03821   273 EAK-WALYAS-AD---LFVLPSYSENFGNVVAEALACGLPVVITDKCGLSELVEAG-CGVVVDP-NVSSLAEALAEALRD 345
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1063734715 538 SGmDPDYWNMfSNEGLQRINECYTWKIYANKVIN 571
Cdd:cd03821   346 PA-DRKRLGE-MARRARQVEENFSWEAVAGQLGE 377
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
355-561 1.03e-07

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: 54.20  E-value: 1.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 355 SIDELLYSQSENDEHIGYLVDKKKPIIFSMARLDVVKNLTGLTEWYAKNKrlrdlVNLVIVGgffdaskskdreEISEIK 434
Cdd:cd03795   168 GIDKNVYNIPRVDFENIKREKKGKKIFLFIGRLVYYKGLDYLIEAAQYLN-----YPIVIGG------------EGPLKP 230
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 435 KMHSLIEKyQLKGQFRWITAQTDRTRNgeLYRSIADtrgAFVQPAHY--EAFGLTVIEAMSCGLVTFATNQGGPAEIIV- 511
Cdd:cd03795   231 DLEAQIEL-NLLDNVKFLGRVDDEEKV--IYLHLCD---VFVFPSVLrsEAFGIVLLEAMMCGKPVISTNIGTGVPYVNn 304
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1063734715 512 DGVSGFHIDPSNGEESSDKIaDFFEKsgmDPDYWNMFSNEGLQRINECYT 561
Cdd:cd03795   305 NGETGLVVPPKDPDALAEAI-DKLLS---DEELRESYGENAKKRFEELFT 350
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
342-551 1.27e-07

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: 53.84  E-value: 1.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 342 FTAQDRRFTKFYTSIDELLYSQSENDehigylvdKKKPIIFSMARLDVVKNLTGLTEWYAKNKRLRDLVNLVIVGgfFDA 421
Cdd:cd04949   132 FNKYPPIFTIPVGYVDQLDTAESNHE--------RKSNKIITISRLAPEKQLDHLIEAVAKAVKKVPEITLDIYG--YGE 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 422 SKSKDREEISEIKkmhslIEKY-QLKGQfrwitaqtdrTRNgelYRSIADTRGAFVQPAHYEAFGLTVIEAMS--CGLVT 498
Cdd:cd04949   202 EREKLKKLIEELH-----LEDNvFLKGY----------HSN---LDQEYQDAYLSLLTSQMEGFGLTLMEAIGhgLPVVS 263
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1063734715 499 FATNQgGPAEIIVDGVSGFHIDPSNGEESSDKIADFFEksgmDPDYWNMFSNE 551
Cdd:cd04949   264 YDVKY-GPSELIEDGENGYLIEKNNIDALADKIIELLN----DPEKLQQFSEE 311
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
478-570 3.21e-06

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: 50.03  E-value: 3.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 478 PAHYEAFGLTVIEAMSCGLVTFATNQGGPAEIIVDGVSGFHIDPSNGEEssdkIADFFEKSGMDPDYWNMFSNEGLQRIN 557
Cdd:cd03794   303 PANRGSSPSKLFEYMAAGKPILASDDGGSDLAVEINGCGLVVEPGDPEA----LADAILELLDDPELRRAMGENGRELAE 378
                          90
                  ....*....|...
gi 1063734715 558 ECYTWKIYANKVI 570
Cdd:cd03794   379 EKFSREKLADRLL 391
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
482-561 3.93e-06

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: 49.64  E-value: 3.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 482 EAFGLTVIEAMSCGLVTFATNQGGPAEIIVD-----GVSGFHIDPSNGEessdKIADFFEKSGMDPDYWNMFSNEGLQRI 556
Cdd:cd03813   381 EGQPLVILEAMASGVPVVATDVGSCRELIYGaddalGQAGLVVPPADPE----ALAEALIKLLRDPELRQAFGEAGRKRV 456

                  ....*
gi 1063734715 557 NECYT 561
Cdd:cd03813   457 EKYYT 461
PRK09922 PRK09922
lipopolysaccharide 1,6-galactosyltransferase;
474-538 4.41e-06

lipopolysaccharide 1,6-galactosyltransferase;


Pssm-ID: 182148 [Multi-domain]  Cd Length: 359  Bit Score: 49.32  E-value: 4.41e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063734715 474 AFVQPAHYEAFGLTVIEAMSCGLVTFATN-QGGPAEIIVDGVSGFHIDPSNGEESSDKIADFFEKS 538
Cdd:PRK09922  260 ALLLTSKFEGFPMTLLEAMSYGIPCISSDcMSGPRDIIKPGLNGELYTPGNIDEFVGKLNKVISGE 325
GT4_PIG-A-like cd03796
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ...
410-562 2.01e-04

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: 44.15  E-value: 2.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 410 VNLVIVGgffDASKSKDREEIseikkmhslIEKYQLKGQFRWITA-QTDRTRN----GELYRSIADTrgafvqpahyEAF 484
Cdd:cd03796   225 VRFIIGG---DGPKRIELEEM---------REKYQLQDRVELLGAvPHEEVRDvlvqGHIFLNTSLT----------EAF 282
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063734715 485 GLTVIEAMSCGLVTFATNQGGPAEIIVDGVSGF-HIDPSNGEESSDKIADFFEKSGMDPdyWNMFsneglQRINECYTW 562
Cdd:cd03796   283 CIAIVEAASCGLLVVSTRVGGIPEVLPPDMILLaEPDPEDIVRKLEEAISILRTGKHDP--WSFH-----NRVKKMYSW 354
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
378-590 2.05e-04

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 44.32  E-value: 2.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 378 KPIIFSMARLDVVKNLTGLTEWYAKNKRlrdlVNLVIVGgffdaskskDREEISEIKKMhsliekyqLKGQFRWITAQTD 457
Cdd:PLN02871  263 KPLIVYVGRLGAEKNLDFLKRVMERLPG----ARLAFVG---------DGPYREELEKM--------FAGTPTVFTGMLQ 321
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 458 RTRNGELYRSiADTrgaFVQPAHYEAFGLTVIEAMSCGLVTFATNQGGPAEIIVD---GVSGFHIDPSNGEESSDKIADF 534
Cdd:PLN02871  322 GDELSQAYAS-GDV---FVMPSESETLGFVVLEAMASGVPVVAARAGGIPDIIPPdqeGKTGFLYTPGDVDDCVEKLETL 397
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063734715 535 FEksgmdpdywnmfSNEGLQRIN-------ECYTWKIYANKVINMGSTYSYWRHLNKDQKLAK 590
Cdd:PLN02871  398 LA------------DPELRERMGaaareevEKWDWRAATRKLRNEQYSAAIWFWRKKRAQLLG 448
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
356-605 6.80e-04

capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. capH in Staphylococcus aureus has been shown to be required for the biosynthesis of the type 1 capsular polysaccharide (CP1).


Pssm-ID: 340840 [Multi-domain]  Cd Length: 357  Bit Score: 42.28  E-value: 6.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 356 IDELLYSQSENDEHIGYLVDKKKPIIFSMARLDVVKNLTGLTEWYAKNKRLRDLVNLVIVGgffdasKSKDREEISEIKK 435
Cdd:cd03812   169 IEKYKFNKEKRRKRRKLLILEDKLVLGHVGRFNEQKNHSFLIDIFEELKKKNPNVKLVLVG------EGELKEKIKEKVK 242
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 436 MHSLIEKYQLKGQfrwitaqtdRTRNGELYrSIADTrgaFVQPAHYEAFGLTVIEAMSCGLVTFATNQGGPAEIIVDGVS 515
Cdd:cd03812   243 ELGLEDKVIFLGF---------RNDVSEIL-SAMDV---FLFPSLYEGLPLVAVEAQASGLPCLLSDTITKECDITNNVE 309
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734715 516 GFHIDPSngeessdkiadffeksgmdPDYWnmfsneglqrinecytwkiyANKVINMgstYSYWRHLNKDQKLAKQRYIH 595
Cdd:cd03812   310 FLPLNET-------------------PSTW--------------------AEKILKL---IKRKRRINKEINKEKKELGY 347
                         250
                  ....*....|
gi 1063734715 596 SFYNLQYRNL 605
Cdd:cd03812   348 DDESLELTLL 357
GT4_ALG11-like cd03806
alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related ...
480-536 7.73e-04

alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ALG11 in yeast is involved in adding the final 1,2-linked Man to the Man5GlcNAc2-PP-Dol synthesized on the cytosolic face of the ER. The deletion analysis of ALG11 was shown to block the early steps of core biosynthesis that takes place on the cytoplasmic face of the ER and lead to a defect in the assembly of lipid-linked oligosaccharides.


Pssm-ID: 340835 [Multi-domain]  Cd Length: 419  Bit Score: 42.21  E-value: 7.73e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063734715 480 HYEAFGLTVIEAMSCGLVTFATNQGGPAEIIV----DGVSGFHidPSNGEESSDKIADFFE 536
Cdd:cd03806   333 WNEHFGIGVVEYMAAGLIPLAHASAGPLLDIVvpwdGGPTGFL--ASTPEEYAEAIEKILT 391
GT4_WbaZ-like cd03804
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ...
474-537 8.39e-04

mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbaZ in Salmonella enterica has been shown to possess mannosyltransferase activity.


Pssm-ID: 340833 [Multi-domain]  Cd Length: 356  Bit Score: 41.89  E-value: 8.39e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063734715 474 AFVQPAHyEAFGLTVIEAMSCGLVTFATNQGGPAEIIVDGVSGFHIDPSNgEESSDKIADFFEK 537
Cdd:cd03804   268 AFVFAAE-EDFGIVPVEAQACGTPVIAFGKGGALETVRPGPTGILFGEQT-VESLKAAVEEFEQ 329
GT4_AmsK-like cd03799
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ...
482-560 9.89e-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: 38.59  E-value: 9.89e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063734715 482 EAFGLTVIEAMSCGLVTFATNQGGPAEIIVDGVSGFHIDPSNGEESSDKIADFFEksgmDPDYWNMFSNEGLQRINECY 560
Cdd:cd03799   267 DGPPNTLKEAMAMGLPVISTEHGGIPELVEDGVSGFLVPERDAEAIAEKLTYLIE----HPAIWPEMGKAGRARVEEEY 341
 
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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