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Conserved domains on  [gi|345104489|gb|AEN71066|]
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sucrose synthase Sus1 [Gossypium darwinii]

Protein Classification

sucrose synthase( domain architecture ID 11476401)

sucrose synthase is a sucrose-cleaving enzyme that provides UDP-glucose and fructose for various metabolic pathways

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN00142 PLN00142
sucrose synthase
1-805 0e+00

sucrose synthase


:

Pssm-ID: 215073 [Multi-domain]  Cd Length: 815  Bit Score: 1739.08  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489   1 MANPVITRVHSLRERLDETLLAHGNEILALLSRIEGKGKGILQHHQIILEFEAI--PEENRKKLADGAFFEVLKASQEAI 78
Cdd:PLN00142   2 AAAPVLTRSHSIRERVPDALSQHRNELKALLSRYVAQGKGILQPHQLIDELEAVidDDEERKKLLDGPFGDILRSTQEAI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489  79 VLPPWVALAVRPRPGVWEYIRVNVHALVVEELTVAEYLHFKEELVDGSSNGNFVLELDFEPFNSSFPRPTLSKSIGNGVE 158
Cdd:PLN00142  82 VLPPFVALAVRPRPGVWEYVRVNVSELSVEELTVSEYLKFKEELVDGSWNDNFVLELDFEPFNASFPRPTLSSSIGNGVQ 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 159 FLNRHLSAKLFHDKESMHPLLEFLRVHCHKGKNMMLNDRIQNLNALQHVLRKAEEYLGTLPPETPCAEFEHRFQEIGLER 238
Cdd:PLN00142 162 FLNRHLSSKLFRDKESLEPLLDFLRAHNHKGETLMLNDRIQTLSKLQSALRKAEEYLSKLPKDTPYSEFEHRFQELGLEK 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 239 GWGDTAQRVLEMIQLLLDLLEAPDPCTLEKFFGRIPMVFNVVILTPHGHFAQDNVLGYPDTGGQVVYILDQVRALENEML 318
Cdd:PLN00142 242 GWGDTAERVLETIHLLLDLLQAPDPSTLEKFLGRIPMVFNVVIFSPHGYFGQANVLGLPDTGGQVVYILDQVRALENEML 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 319 LRIKQQGLNITPRILIITRLLPDAVGTTCGQRLEKVYGTEYSDILRVPFRTEKGIVRKWISRFEVWPYLETYTEDVAHEI 398
Cdd:PLN00142 322 LRIKQQGLDIKPQILIVTRLIPDAKGTTCNQRLEKVSGTEHSHILRVPFRTEKGILRKWISRFDVWPYLETFAEDAASEI 401
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 399 SKELQGKPDLIIGNYSDGNIVASLLAHKLGVTQCTIAHALEKTKYPDSDIYWKKLEDKYHFSCQFTADLFAMNHTDFIIT 478
Cdd:PLN00142 402 LAELQGKPDLIIGNYSDGNLVASLLAHKLGVTQCTIAHALEKTKYPDSDIYWKKFDDKYHFSCQFTADLIAMNHADFIIT 481
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 479 STFQEIAGSKDTVGQYESHTAFTLPGLYRVVHGIDVFDPKFNIVSPGADMEIYFPYTEEKRRLKHFHTEIEDLLYSKVEN 558
Cdd:PLN00142 482 STYQEIAGSKDTVGQYESHTAFTLPGLYRVVHGIDVFDPKFNIVSPGADMSIYFPYTEKQKRLTSLHPSIEELLYSPEQN 561
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 559 EEHLCVLNDRNKPILFTMARLDRVKNLTGLVEWYGKNAKLRELANLVVVGGD-RRKESKDLEEKAEMKKMFELIEKYNLN 637
Cdd:PLN00142 562 DEHIGYLKDRKKPIIFSMARLDRVKNLTGLVEWYGKNKRLRELVNLVVVGGFiDPSKSKDREEIAEIKKMHSLIEKYNLK 641
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 638 GQFRWISSQMNRIRNGELYRYICDTKGAFVQPALYEAFGLTVVEAMTCGLPTFATCNGGPAEIIVHGKSGFNIDPYHGDQ 717
Cdd:PLN00142 642 GQFRWIAAQTNRVRNGELYRYIADTKGAFVQPALYEAFGLTVVEAMTCGLPTFATCQGGPAEIIVDGVSGFHIDPYHGDE 721
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 718 AADILVDFFEKCKKDPSHWDKISQGGLKRIEEKYTWKIYSERLLTLTGVYGFWKHVSNLERRESRRYLEMFYALKYRKLA 797
Cdd:PLN00142 722 AANKIADFFEKCKEDPSYWNKISDAGLQRIYECYTWKIYAERLLTLGGVYGFWKYVSKLERRETRRYLEMFYNLKFRELA 801

                 ....*...
gi 345104489 798 ESVPLAEE 805
Cdd:PLN00142 802 KTVPLAVD 809
 
Name Accession Description Interval E-value
PLN00142 PLN00142
sucrose synthase
1-805 0e+00

sucrose synthase


Pssm-ID: 215073 [Multi-domain]  Cd Length: 815  Bit Score: 1739.08  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489   1 MANPVITRVHSLRERLDETLLAHGNEILALLSRIEGKGKGILQHHQIILEFEAI--PEENRKKLADGAFFEVLKASQEAI 78
Cdd:PLN00142   2 AAAPVLTRSHSIRERVPDALSQHRNELKALLSRYVAQGKGILQPHQLIDELEAVidDDEERKKLLDGPFGDILRSTQEAI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489  79 VLPPWVALAVRPRPGVWEYIRVNVHALVVEELTVAEYLHFKEELVDGSSNGNFVLELDFEPFNSSFPRPTLSKSIGNGVE 158
Cdd:PLN00142  82 VLPPFVALAVRPRPGVWEYVRVNVSELSVEELTVSEYLKFKEELVDGSWNDNFVLELDFEPFNASFPRPTLSSSIGNGVQ 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 159 FLNRHLSAKLFHDKESMHPLLEFLRVHCHKGKNMMLNDRIQNLNALQHVLRKAEEYLGTLPPETPCAEFEHRFQEIGLER 238
Cdd:PLN00142 162 FLNRHLSSKLFRDKESLEPLLDFLRAHNHKGETLMLNDRIQTLSKLQSALRKAEEYLSKLPKDTPYSEFEHRFQELGLEK 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 239 GWGDTAQRVLEMIQLLLDLLEAPDPCTLEKFFGRIPMVFNVVILTPHGHFAQDNVLGYPDTGGQVVYILDQVRALENEML 318
Cdd:PLN00142 242 GWGDTAERVLETIHLLLDLLQAPDPSTLEKFLGRIPMVFNVVIFSPHGYFGQANVLGLPDTGGQVVYILDQVRALENEML 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 319 LRIKQQGLNITPRILIITRLLPDAVGTTCGQRLEKVYGTEYSDILRVPFRTEKGIVRKWISRFEVWPYLETYTEDVAHEI 398
Cdd:PLN00142 322 LRIKQQGLDIKPQILIVTRLIPDAKGTTCNQRLEKVSGTEHSHILRVPFRTEKGILRKWISRFDVWPYLETFAEDAASEI 401
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 399 SKELQGKPDLIIGNYSDGNIVASLLAHKLGVTQCTIAHALEKTKYPDSDIYWKKLEDKYHFSCQFTADLFAMNHTDFIIT 478
Cdd:PLN00142 402 LAELQGKPDLIIGNYSDGNLVASLLAHKLGVTQCTIAHALEKTKYPDSDIYWKKFDDKYHFSCQFTADLIAMNHADFIIT 481
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 479 STFQEIAGSKDTVGQYESHTAFTLPGLYRVVHGIDVFDPKFNIVSPGADMEIYFPYTEEKRRLKHFHTEIEDLLYSKVEN 558
Cdd:PLN00142 482 STYQEIAGSKDTVGQYESHTAFTLPGLYRVVHGIDVFDPKFNIVSPGADMSIYFPYTEKQKRLTSLHPSIEELLYSPEQN 561
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 559 EEHLCVLNDRNKPILFTMARLDRVKNLTGLVEWYGKNAKLRELANLVVVGGD-RRKESKDLEEKAEMKKMFELIEKYNLN 637
Cdd:PLN00142 562 DEHIGYLKDRKKPIIFSMARLDRVKNLTGLVEWYGKNKRLRELVNLVVVGGFiDPSKSKDREEIAEIKKMHSLIEKYNLK 641
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 638 GQFRWISSQMNRIRNGELYRYICDTKGAFVQPALYEAFGLTVVEAMTCGLPTFATCNGGPAEIIVHGKSGFNIDPYHGDQ 717
Cdd:PLN00142 642 GQFRWIAAQTNRVRNGELYRYIADTKGAFVQPALYEAFGLTVVEAMTCGLPTFATCQGGPAEIIVDGVSGFHIDPYHGDE 721
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 718 AADILVDFFEKCKKDPSHWDKISQGGLKRIEEKYTWKIYSERLLTLTGVYGFWKHVSNLERRESRRYLEMFYALKYRKLA 797
Cdd:PLN00142 722 AANKIADFFEKCKEDPSYWNKISDAGLQRIYECYTWKIYAERLLTLGGVYGFWKYVSKLERRETRRYLEMFYNLKFRELA 801

                 ....*...
gi 345104489 798 ESVPLAEE 805
Cdd:PLN00142 802 KTVPLAVD 809
sucr_synth TIGR02470
sucrose synthase; This model represents sucrose synthase, an enzyme that, despite its name, ...
25-803 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: 1507.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489   25 NEILALLSRIEGKGKGILQHHQIILEFE-AIPEENR-KKLADGAFFEVLKASQEAIVLPPWVALAVRPRPGVWEYIRVNV 102
Cdd:TIGR02470   2 AELRQLLSRYVSQGKRYLLRHQLLDEFEqYCSDADKeKKLSESPLGKLIFSTQEAIVLPPWVALAVRPRIGVWEYVRVNV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489  103 HALVVEELTVAEYLHFKEELVDGSSNGNFVLELDFEPFNSSFPRPTLSKSIGNGVEFLNRHLSAKLFHDKESMHPLLEFL 182
Cdd:TIGR02470  82 EELSVEELTISEYLDFKEQLVNGHANDPNVLELDFEPFNASFPRPSDSKSIGNGVQFLNRHLSSKLFQDPESMEPLLNFL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489  183 RVHCHKGKNMMLNDRIQNLNALQHVLRKAEEYLGTLPPETPCAEFEHRFQEIGLERGWGDTAQRVLEMIQLLLDLLEAPD 262
Cdd:TIGR02470 162 RVHNYNGIQLMINDRIQSVSHLQSQLRKAEEFLSALPPDTPYSEFEFELQELGFEPGWGDTAQRVLETLHLLDDLLEAPD 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489  263 PCTLEKFFGRIPMVFNVVILTPHGHFAQDNVLGYPDTGGQVVYILDQVRALENEMLLRIKQQGLNITPRILIITRLLPDA 342
Cdd:TIGR02470 242 PSVLEAFLGRIPMVFNVVILSPHGYFGQENVLGLPDTGGQVVYILDQVRALENEMLQRIKLQGLEITPKILIVTRLIPDA 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489  343 VGTTCGQRLEKVYGTEYSDILRVPFRTEKGIV-RKWISRFEVWPYLETYTEDVAHEISKELQGKPDLIIGNYSDGNIVAS 421
Cdd:TIGR02470 322 EGTTCNQRLEKVYGTEHAWILRVPFRTENGIIlRNWISRFEIWPYLETFAEDAEKEILAELQGKPDLIIGNYSDGNLVAS 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489  422 LLAHKLGVTQCTIAHALEKTKYPDSDIYWKKLEDKYHFSCQFTADLFAMNHTDFIITSTFQEIAGSKDTVGQYESHTAFT 501
Cdd:TIGR02470 402 LLARKLGVTQCTIAHALEKTKYPDSDIYWQEFEDKYHFSCQFTADLIAMNAADFIITSTYQEIAGTKDSVGQYESHQAFT 481
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489  502 LPGLYRVVHGIDVFDPKFNIVSPGADMEIYFPYTEEKRRLKHFHTEIEDLLYSKVENEEHLCVLNDRNKPILFTMARLDR 581
Cdd:TIGR02470 482 MPGLYRVVHGIDVFDPKFNIVSPGADESIYFPYSDKEKRLTNLHPEIEELLFSLEDNDEHYGYLKDPNKPIIFSMARLDR 561
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489  582 VKNLTGLVEWYGKNAKLRELANLVVVGGDRR-KESKDLEEKAEMKKMFELIEKYNLNGQFRWISSQMNRIRNGELYRYIC 660
Cdd:TIGR02470 562 VKNLTGLVECYGRSPKLRELVNLVVVAGKLDaKESKDREEQAEIEKMHNLIDQYQLHGQIRWIGAQLNRVRNGELYRYIA 641
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489  661 DTKGAFVQPALYEAFGLTVVEAMTCGLPTFATCNGGPAEIIVHGKSGFNIDPYHGDQAADILVDFFEKCKKDPSHWDKIS 740
Cdd:TIGR02470 642 DTKGIFVQPALYEAFGLTVLEAMTCGLPTFATRFGGPLEIIQDGVSGFHIDPYHGEEAAEKIVDFFEKCDEDPSYWQKIS 721
                         730       740       750       760       770       780
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 345104489  741 QGGLKRIEEKYTWKIYSERLLTLTGVYGFWKHVSNLERRESRRYLEMFYALKYRKLAESVPLA 803
Cdd:TIGR02470 722 QGGLQRIYEKYTWKIYSERLLTLAGIYGFWKFVSKLEREETRRYLEMFYHLKYRPLAEAVPLA 784
Sucrose_synth pfam00862
Sucrose synthase; Sucrose synthases catalyze the synthesis of sucrose from UDP-glucose and ...
16-553 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: 1054.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489   16 LDETLLAHGNEILALLSRIEGKGKGILQHHQIILEFEAIPEEN--RKKLADGAFFEVLKASQEAIVLPPWVALAVRPRPG 93
Cdd:pfam00862   1 VPDALSQSRNELKRLLSRYVAQGKRLMKRHELLDEFEKVIEDKkeRSKLMEGLLGKILHSTQEAIVLPPWVAFAVRPRPG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489   94 VWEYIRVNVHALVVEELTVAEYLHFKEELVDGSSNGNFVLELDFEPFNSSFPRPTLSKSIGNGVEFLNRHLSAKLFHDKE 173
Cdd:pfam00862  81 VWEYVRVNADELSVEELTVSEYLKFKERLVDESWNDENALELDFGPFNASFPRLTLPSSIGNGVQFLNRHLSSKLFRDSE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489  174 SMHPLLEFLRVHCHKGKNMMLNDRIQNLNALQHVLRKAEEYLGTLPPETPCAEFEHRFQEIGLERGWGDTAQRVLEMIQL 253
Cdd:pfam00862 161 SLEPLLDFLRSHNYDGESLMINDRINSVSKLQSALIKAEEFLSKLPKDTPYEEFEYRLQELGFEKGWGDTAERVKETMHL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489  254 LLDLLEAPDPCTLEKFFGRIPMVFNVVILTPHGHFAQDNVLGYPDTGGQVVYILDQVRALENEMLLRIKQQGLNITPRIL 333
Cdd:pfam00862 241 LSELLQAPDPSTLEKFLGRIPMVFNVVILSPHGYFGQANVLGLPDTGGQVVYILDQVRALENELLLRIKQQGLDIKPQIL 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489  334 IITRLLPDAVGTTCGQRLEKVYGTEYSDILRVPFRTEKGIVRKWISRFEVWPYLETYTEDVAHEISKELQGKPDLIIGNY 413
Cdd:pfam00862 321 VVTRLIPEARGTTCNQELEKISGTKHSHILRVPFRTENGILRQWISRFDIWPYLERFTQDAAKEILAELEGKPDLIIGNY 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489  414 SDGNIVASLLAHKLGVTQCTIAHALEKTKYPDSDIYWKKLEDKYHFSCQFTADLFAMNHTDFIITSTFQEIAGSKDTVGQ 493
Cdd:pfam00862 401 SDGNLVASLLAHKLGVTQCTIAHALEKTKYEDSDIYWKELEPKYHFSCQFTADLIAMNAADFIITSTYQEIAGSKDRVGQ 480
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489  494 YESHTAFTLPGLYRVVHGIDVFDPKFNIVSPGADMEIYFPYTEEKRRLKHFHTEIEDLLY 553
Cdd:pfam00862 481 YESHTAFTLPGLYRVVSGIDVFDPKFNIVSPGADQSIYFPYTEKERRLTSLHPSIEELLY 540
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
278-762 5.01e-147

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: 437.06  E-value: 5.01e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 278 NVVILTPHGHFAQDNVLGypDTGGQVVYILDQVRALenemllrikqqgLNITPRILIITRLLPDAVGTTcgqrlekVYGT 357
Cdd:cd03800    1 RIALISVHGSPLAQPGGA--DTGGQNVYVLELARAL------------AELGYQVDIFTRRISPADPEV-------VEIA 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 358 EYSDILRVPFRTEKGIVRKwisrfEVWPYLETYTEDVAHEISKELqGKPDLIIGNYSDGNIVASLLAHKLGVTQCTIAHA 437
Cdd:cd03800   60 PGARVIRVPAGPPEYLPKE-----ELWPYLEEFADGLLRFIAREG-GRYDLIHSHYWDSGLVGALLARRLGVPLVHTFHS 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 438 LEKTKYPDSDIYWKkledkYHFSCQFTADLFAMNHTDFIITSTFQEIAGSKDTVGQYESHtaftlpglyrvvhgidvfdp 517
Cdd:cd03800  134 LGRVKYRHLGAQDT-----YHPSLRITAEEQILEAADRVIASTPQEADELISLYGADPSR-------------------- 188
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 518 kFNIVSPGADMEIYFPYTEEKRRlkhfhteiedllyskveneeHLCVLNDRNKPILFTMARLDRVKNLTGLVEWYGKNAK 597
Cdd:cd03800  189 -INVVPPGVDLERFFPVDRAEAR--------------------RARLLLPPDKPVVLALGRLDPRKGIDTLVRAFAQLPE 247
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 598 LRELANLVVVGGDRR-KESKDLEEKAEMKKMFELIEKYNLNGQfrwissqMNRIRNGELYRYicdtKGAFVQPALYEAFG 676
Cdd:cd03800  248 LRELANLVLVGGPSDdPLSMDREELAELAEELGLIDRVRFPGR-------VSRDDLPELYRA----ADVFVVPSLYEPFG 316
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 677 LTVVEAMTCGLPTFATCNGGPAEIIVHGKSGFNIDPYHGDQAADILVDFFEkckkDPSHWDKISQGGLKRIEEKYTWKIY 756
Cdd:cd03800  317 LTAIEAMACGTPVVATAVGGLQDIVRDGRTGLLVDPHDPEALAAALRRLLD----DPALWQRLSRAGLERARAHYTWESV 392

                 ....*.
gi 345104489 757 SERLLT 762
Cdd:cd03800  393 ADQLLT 398
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
665-763 1.00e-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: 1.00e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 665 AFVQPALYEAFGLTVVEAMTCGLPTFATCNGGPAEIIVHGKSGFNIDPYHGDQAADILVDFFEkckkDPSHWDKISQGGL 744
Cdd:COG0438   23 VFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLE----DPELRRRLGEAAR 98
                         90
                 ....*....|....*....
gi 345104489 745 KRIEEKYTWKIYSERLLTL 763
Cdd:COG0438   99 ERAEERFSWEAIAERLLAL 117
 
Name Accession Description Interval E-value
PLN00142 PLN00142
sucrose synthase
1-805 0e+00

sucrose synthase


Pssm-ID: 215073 [Multi-domain]  Cd Length: 815  Bit Score: 1739.08  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489   1 MANPVITRVHSLRERLDETLLAHGNEILALLSRIEGKGKGILQHHQIILEFEAI--PEENRKKLADGAFFEVLKASQEAI 78
Cdd:PLN00142   2 AAAPVLTRSHSIRERVPDALSQHRNELKALLSRYVAQGKGILQPHQLIDELEAVidDDEERKKLLDGPFGDILRSTQEAI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489  79 VLPPWVALAVRPRPGVWEYIRVNVHALVVEELTVAEYLHFKEELVDGSSNGNFVLELDFEPFNSSFPRPTLSKSIGNGVE 158
Cdd:PLN00142  82 VLPPFVALAVRPRPGVWEYVRVNVSELSVEELTVSEYLKFKEELVDGSWNDNFVLELDFEPFNASFPRPTLSSSIGNGVQ 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 159 FLNRHLSAKLFHDKESMHPLLEFLRVHCHKGKNMMLNDRIQNLNALQHVLRKAEEYLGTLPPETPCAEFEHRFQEIGLER 238
Cdd:PLN00142 162 FLNRHLSSKLFRDKESLEPLLDFLRAHNHKGETLMLNDRIQTLSKLQSALRKAEEYLSKLPKDTPYSEFEHRFQELGLEK 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 239 GWGDTAQRVLEMIQLLLDLLEAPDPCTLEKFFGRIPMVFNVVILTPHGHFAQDNVLGYPDTGGQVVYILDQVRALENEML 318
Cdd:PLN00142 242 GWGDTAERVLETIHLLLDLLQAPDPSTLEKFLGRIPMVFNVVIFSPHGYFGQANVLGLPDTGGQVVYILDQVRALENEML 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 319 LRIKQQGLNITPRILIITRLLPDAVGTTCGQRLEKVYGTEYSDILRVPFRTEKGIVRKWISRFEVWPYLETYTEDVAHEI 398
Cdd:PLN00142 322 LRIKQQGLDIKPQILIVTRLIPDAKGTTCNQRLEKVSGTEHSHILRVPFRTEKGILRKWISRFDVWPYLETFAEDAASEI 401
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 399 SKELQGKPDLIIGNYSDGNIVASLLAHKLGVTQCTIAHALEKTKYPDSDIYWKKLEDKYHFSCQFTADLFAMNHTDFIIT 478
Cdd:PLN00142 402 LAELQGKPDLIIGNYSDGNLVASLLAHKLGVTQCTIAHALEKTKYPDSDIYWKKFDDKYHFSCQFTADLIAMNHADFIIT 481
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 479 STFQEIAGSKDTVGQYESHTAFTLPGLYRVVHGIDVFDPKFNIVSPGADMEIYFPYTEEKRRLKHFHTEIEDLLYSKVEN 558
Cdd:PLN00142 482 STYQEIAGSKDTVGQYESHTAFTLPGLYRVVHGIDVFDPKFNIVSPGADMSIYFPYTEKQKRLTSLHPSIEELLYSPEQN 561
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 559 EEHLCVLNDRNKPILFTMARLDRVKNLTGLVEWYGKNAKLRELANLVVVGGD-RRKESKDLEEKAEMKKMFELIEKYNLN 637
Cdd:PLN00142 562 DEHIGYLKDRKKPIIFSMARLDRVKNLTGLVEWYGKNKRLRELVNLVVVGGFiDPSKSKDREEIAEIKKMHSLIEKYNLK 641
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 638 GQFRWISSQMNRIRNGELYRYICDTKGAFVQPALYEAFGLTVVEAMTCGLPTFATCNGGPAEIIVHGKSGFNIDPYHGDQ 717
Cdd:PLN00142 642 GQFRWIAAQTNRVRNGELYRYIADTKGAFVQPALYEAFGLTVVEAMTCGLPTFATCQGGPAEIIVDGVSGFHIDPYHGDE 721
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 718 AADILVDFFEKCKKDPSHWDKISQGGLKRIEEKYTWKIYSERLLTLTGVYGFWKHVSNLERRESRRYLEMFYALKYRKLA 797
Cdd:PLN00142 722 AANKIADFFEKCKEDPSYWNKISDAGLQRIYECYTWKIYAERLLTLGGVYGFWKYVSKLERRETRRYLEMFYNLKFRELA 801

                 ....*...
gi 345104489 798 ESVPLAEE 805
Cdd:PLN00142 802 KTVPLAVD 809
sucr_synth TIGR02470
sucrose synthase; This model represents sucrose synthase, an enzyme that, despite its name, ...
25-803 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: 1507.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489   25 NEILALLSRIEGKGKGILQHHQIILEFE-AIPEENR-KKLADGAFFEVLKASQEAIVLPPWVALAVRPRPGVWEYIRVNV 102
Cdd:TIGR02470   2 AELRQLLSRYVSQGKRYLLRHQLLDEFEqYCSDADKeKKLSESPLGKLIFSTQEAIVLPPWVALAVRPRIGVWEYVRVNV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489  103 HALVVEELTVAEYLHFKEELVDGSSNGNFVLELDFEPFNSSFPRPTLSKSIGNGVEFLNRHLSAKLFHDKESMHPLLEFL 182
Cdd:TIGR02470  82 EELSVEELTISEYLDFKEQLVNGHANDPNVLELDFEPFNASFPRPSDSKSIGNGVQFLNRHLSSKLFQDPESMEPLLNFL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489  183 RVHCHKGKNMMLNDRIQNLNALQHVLRKAEEYLGTLPPETPCAEFEHRFQEIGLERGWGDTAQRVLEMIQLLLDLLEAPD 262
Cdd:TIGR02470 162 RVHNYNGIQLMINDRIQSVSHLQSQLRKAEEFLSALPPDTPYSEFEFELQELGFEPGWGDTAQRVLETLHLLDDLLEAPD 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489  263 PCTLEKFFGRIPMVFNVVILTPHGHFAQDNVLGYPDTGGQVVYILDQVRALENEMLLRIKQQGLNITPRILIITRLLPDA 342
Cdd:TIGR02470 242 PSVLEAFLGRIPMVFNVVILSPHGYFGQENVLGLPDTGGQVVYILDQVRALENEMLQRIKLQGLEITPKILIVTRLIPDA 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489  343 VGTTCGQRLEKVYGTEYSDILRVPFRTEKGIV-RKWISRFEVWPYLETYTEDVAHEISKELQGKPDLIIGNYSDGNIVAS 421
Cdd:TIGR02470 322 EGTTCNQRLEKVYGTEHAWILRVPFRTENGIIlRNWISRFEIWPYLETFAEDAEKEILAELQGKPDLIIGNYSDGNLVAS 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489  422 LLAHKLGVTQCTIAHALEKTKYPDSDIYWKKLEDKYHFSCQFTADLFAMNHTDFIITSTFQEIAGSKDTVGQYESHTAFT 501
Cdd:TIGR02470 402 LLARKLGVTQCTIAHALEKTKYPDSDIYWQEFEDKYHFSCQFTADLIAMNAADFIITSTYQEIAGTKDSVGQYESHQAFT 481
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489  502 LPGLYRVVHGIDVFDPKFNIVSPGADMEIYFPYTEEKRRLKHFHTEIEDLLYSKVENEEHLCVLNDRNKPILFTMARLDR 581
Cdd:TIGR02470 482 MPGLYRVVHGIDVFDPKFNIVSPGADESIYFPYSDKEKRLTNLHPEIEELLFSLEDNDEHYGYLKDPNKPIIFSMARLDR 561
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489  582 VKNLTGLVEWYGKNAKLRELANLVVVGGDRR-KESKDLEEKAEMKKMFELIEKYNLNGQFRWISSQMNRIRNGELYRYIC 660
Cdd:TIGR02470 562 VKNLTGLVECYGRSPKLRELVNLVVVAGKLDaKESKDREEQAEIEKMHNLIDQYQLHGQIRWIGAQLNRVRNGELYRYIA 641
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489  661 DTKGAFVQPALYEAFGLTVVEAMTCGLPTFATCNGGPAEIIVHGKSGFNIDPYHGDQAADILVDFFEKCKKDPSHWDKIS 740
Cdd:TIGR02470 642 DTKGIFVQPALYEAFGLTVLEAMTCGLPTFATRFGGPLEIIQDGVSGFHIDPYHGEEAAEKIVDFFEKCDEDPSYWQKIS 721
                         730       740       750       760       770       780
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 345104489  741 QGGLKRIEEKYTWKIYSERLLTLTGVYGFWKHVSNLERRESRRYLEMFYALKYRKLAESVPLA 803
Cdd:TIGR02470 722 QGGLQRIYEKYTWKIYSERLLTLAGIYGFWKFVSKLEREETRRYLEMFYHLKYRPLAEAVPLA 784
Sucrose_synth pfam00862
Sucrose synthase; Sucrose synthases catalyze the synthesis of sucrose from UDP-glucose and ...
16-553 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: 1054.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489   16 LDETLLAHGNEILALLSRIEGKGKGILQHHQIILEFEAIPEEN--RKKLADGAFFEVLKASQEAIVLPPWVALAVRPRPG 93
Cdd:pfam00862   1 VPDALSQSRNELKRLLSRYVAQGKRLMKRHELLDEFEKVIEDKkeRSKLMEGLLGKILHSTQEAIVLPPWVAFAVRPRPG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489   94 VWEYIRVNVHALVVEELTVAEYLHFKEELVDGSSNGNFVLELDFEPFNSSFPRPTLSKSIGNGVEFLNRHLSAKLFHDKE 173
Cdd:pfam00862  81 VWEYVRVNADELSVEELTVSEYLKFKERLVDESWNDENALELDFGPFNASFPRLTLPSSIGNGVQFLNRHLSSKLFRDSE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489  174 SMHPLLEFLRVHCHKGKNMMLNDRIQNLNALQHVLRKAEEYLGTLPPETPCAEFEHRFQEIGLERGWGDTAQRVLEMIQL 253
Cdd:pfam00862 161 SLEPLLDFLRSHNYDGESLMINDRINSVSKLQSALIKAEEFLSKLPKDTPYEEFEYRLQELGFEKGWGDTAERVKETMHL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489  254 LLDLLEAPDPCTLEKFFGRIPMVFNVVILTPHGHFAQDNVLGYPDTGGQVVYILDQVRALENEMLLRIKQQGLNITPRIL 333
Cdd:pfam00862 241 LSELLQAPDPSTLEKFLGRIPMVFNVVILSPHGYFGQANVLGLPDTGGQVVYILDQVRALENELLLRIKQQGLDIKPQIL 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489  334 IITRLLPDAVGTTCGQRLEKVYGTEYSDILRVPFRTEKGIVRKWISRFEVWPYLETYTEDVAHEISKELQGKPDLIIGNY 413
Cdd:pfam00862 321 VVTRLIPEARGTTCNQELEKISGTKHSHILRVPFRTENGILRQWISRFDIWPYLERFTQDAAKEILAELEGKPDLIIGNY 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489  414 SDGNIVASLLAHKLGVTQCTIAHALEKTKYPDSDIYWKKLEDKYHFSCQFTADLFAMNHTDFIITSTFQEIAGSKDTVGQ 493
Cdd:pfam00862 401 SDGNLVASLLAHKLGVTQCTIAHALEKTKYEDSDIYWKELEPKYHFSCQFTADLIAMNAADFIITSTYQEIAGSKDRVGQ 480
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489  494 YESHTAFTLPGLYRVVHGIDVFDPKFNIVSPGADMEIYFPYTEEKRRLKHFHTEIEDLLY 553
Cdd:pfam00862 481 YESHTAFTLPGLYRVVSGIDVFDPKFNIVSPGADQSIYFPYTEKERRLTSLHPSIEELLY 540
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
278-762 5.01e-147

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: 437.06  E-value: 5.01e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 278 NVVILTPHGHFAQDNVLGypDTGGQVVYILDQVRALenemllrikqqgLNITPRILIITRLLPDAVGTTcgqrlekVYGT 357
Cdd:cd03800    1 RIALISVHGSPLAQPGGA--DTGGQNVYVLELARAL------------AELGYQVDIFTRRISPADPEV-------VEIA 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 358 EYSDILRVPFRTEKGIVRKwisrfEVWPYLETYTEDVAHEISKELqGKPDLIIGNYSDGNIVASLLAHKLGVTQCTIAHA 437
Cdd:cd03800   60 PGARVIRVPAGPPEYLPKE-----ELWPYLEEFADGLLRFIAREG-GRYDLIHSHYWDSGLVGALLARRLGVPLVHTFHS 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 438 LEKTKYPDSDIYWKkledkYHFSCQFTADLFAMNHTDFIITSTFQEIAGSKDTVGQYESHtaftlpglyrvvhgidvfdp 517
Cdd:cd03800  134 LGRVKYRHLGAQDT-----YHPSLRITAEEQILEAADRVIASTPQEADELISLYGADPSR-------------------- 188
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 518 kFNIVSPGADMEIYFPYTEEKRRlkhfhteiedllyskveneeHLCVLNDRNKPILFTMARLDRVKNLTGLVEWYGKNAK 597
Cdd:cd03800  189 -INVVPPGVDLERFFPVDRAEAR--------------------RARLLLPPDKPVVLALGRLDPRKGIDTLVRAFAQLPE 247
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 598 LRELANLVVVGGDRR-KESKDLEEKAEMKKMFELIEKYNLNGQfrwissqMNRIRNGELYRYicdtKGAFVQPALYEAFG 676
Cdd:cd03800  248 LRELANLVLVGGPSDdPLSMDREELAELAEELGLIDRVRFPGR-------VSRDDLPELYRA----ADVFVVPSLYEPFG 316
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 677 LTVVEAMTCGLPTFATCNGGPAEIIVHGKSGFNIDPYHGDQAADILVDFFEkckkDPSHWDKISQGGLKRIEEKYTWKIY 756
Cdd:cd03800  317 LTAIEAMACGTPVVATAVGGLQDIVRDGRTGLLVDPHDPEALAAALRRLLD----DPALWQRLSRAGLERARAHYTWESV 392

                 ....*.
gi 345104489 757 SERLLT 762
Cdd:cd03800  393 ADQLLT 398
sucrsPsyn_pln TIGR02468
sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this ...
279-763 9.12e-39

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: 155.71  E-value: 9.12e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489   279 VVILTPHGHFAQDNV-LGY-PDTGGQVVYILDQVRALENemllrikqqglniTP---RILIITRLL--PDaVGTTCGQRL 351
Cdd:TIGR02468  172 IVLISLHGLVRGENMeLGRdSDTGGQVKYVVELARALGS-------------MPgvyRVDLLTRQVssPD-VDWSYGEPT 237
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489   352 EKVYGTEYSD------------ILRVPFrtekGIVRKWISRFEVWPYLETYTED-VAH--EISKEL-----QGK---PDL 408
Cdd:TIGR02468  238 EMLTPRSSENdgdemgessgayIIRIPF----GPRDKYIPKEELWPYIPEFVDGaLSHivNMSKVLgeqigSGHpvwPYV 313
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489   409 IIGNYSDGNIVASLLAHKLGVTQCTIAHALEKTK---------YPDSDIywkklEDKYHFSCQFTADLFAMNHTDFIITS 479
Cdd:TIGR02468  314 IHGHYADAGDSAALLSGALNVPMVLTGHSLGRDKleqllkqgrMSKEEI-----NSTYKIMRRIEAEELSLDASEIVITS 388
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489   480 TFQEIAGskdtvgQYESHTAFTlPGLYRVV----------HGidVFDPKFNIVSPGADmeiyfpyteekrrLKHFHTEIE 549
Cdd:TIGR02468  389 TRQEIEE------QWGLYDGFD-VILERKLrararrgvscYG--RFMPRMAVIPPGME-------------FSHIVPHDG 446
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489   550 DLLYSKVENEEH------------LCVLNDRNKPILFTMARLDRVKNLTGLVEWYGKNAKLRELANLVVVGGDRrkesKD 617
Cdd:TIGR02468  447 DMDGETEGNEEHpakpdppiwseiMRFFTNPRKPMILALARPDPKKNITTLVKAFGECRPLRELANLTLIMGNR----DD 522
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489   618 LEEKAEMK-----KMFELIEKYNLNGQFRWiSSQMNRIRNGELYRYICDTKGAFVQPALYEAFGLTVVEAMTCGLPTFAT 692
Cdd:TIGR02468  523 IDEMSSGSssvltSVLKLIDKYDLYGQVAY-PKHHKQSDVPDIYRLAAKTKGVFINPAFIEPFGLTLIEAAAHGLPMVAT 601
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 345104489   693 CNGGPAEIIVHGKSGFNIDPYHGDQAADILVdffeKCKKDPSHWDKISQGGLKRIeEKYTW----KIYSERLLTL 763
Cdd:TIGR02468  602 KNGGPVDIHRVLDNGLLVDPHDQQAIADALL----KLVADKQLWAECRQNGLKNI-HLFSWpehcKTYLSRIASC 671
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
569-738 1.04e-28

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: 112.37  E-value: 1.04e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489  569 NKPILFTMARLDRVKNLTGLVEWYGKNAKLRELANLVVVGgdrrkeskdleEKAEMKKMFELIEKYNLNGQFRWISsQMN 648
Cdd:pfam00534   1 KKKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAG-----------DGEEEKRLKKLAEKLGLGDNVIFLG-FVS 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489  649 RIRNGELYRyICDtkgAFVQPALYEAFGLTVVEAMTCGLPTFATCNGGPAEIIVHGKSGFNIDPYHGDQAADiLVDFFEK 728
Cdd:pfam00534  69 DEDLPELLK-IAD---VFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAE-AIDKLLE 143
                         170
                  ....*....|
gi 345104489  729 CKKDPSHWDK 738
Cdd:pfam00534 144 DEELRERLGE 153
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
665-763 1.00e-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: 1.00e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 665 AFVQPALYEAFGLTVVEAMTCGLPTFATCNGGPAEIIVHGKSGFNIDPYHGDQAADILVDFFEkckkDPSHWDKISQGGL 744
Cdd:COG0438   23 VFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLE----DPELRRRLGEAAR 98
                         90
                 ....*....|....*....
gi 345104489 745 KRIEEKYTWKIYSERLLTL 763
Cdd:COG0438   99 ERAEERFSWEAIAERLLAL 117
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
567-763 1.25e-20

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: 94.53  E-value: 1.25e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 567 DRNKPILFTMARLDRVKNLTGLVEWYGKNAKLRELANLVVVGGDRrkeskdlEEKAEMKKMfelieKYNLNGQFRWISSQ 646
Cdd:cd03801  189 PPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVGGDG-------PLRAELEEL-----ELGLGDRVRFLGFV 256
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 647 M-NRIRngELYRyICDtkgAFVQPALYEAFGLTVVEAMTCGLPTFATCNGGPAEIIVHGKSGFNIDPyhGDQAAdiLVDF 725
Cdd:cd03801  257 PdEELP--ALYA-AAD---VFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVVPP--DDVEA--LADA 326
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 345104489 726 FEKCKKDPSHWDKISQGGLKRIEEKYTWKIYSERLLTL 763
Cdd:cd03801  327 LLRLLADPELRARLGRAARERVAERFSWERVAERLLDL 364
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
522-728 1.13e-17

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: 85.49  E-value: 1.13e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 522 VSPGA--DMEIYFPYTEEKRRLKHFHTEIEDLLysKVENEEHLCvlNDRNKPILFTMARLDRVKNLTGLVEWYGKNAKLR 599
Cdd:cd03811  142 VSKGIkeDLIRLGPSPPEKIEVIYNPIDIDRIR--ALAKEPILN--EPEDGPVILAVGRLDPQKGHDLLIEAFAKLRKKY 217
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 600 ELANLVVVGgdrrkeskDLEEKAEMKKmfeLIEKYNLNGQFRWISSQMNrirngeLYRYI--CDtkgAFVQPALYEAFGL 677
Cdd:cd03811  218 PDVKLVILG--------DGPLREELEK---LAKELGLAERVIFLGFQSN------PYPYLkkAD---LFVLSSRYEGFPN 277
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 345104489 678 TVVEAMTCGLPTFATCNGGPAEIIVHGKSGFNIDPYHGDQAADILVDFFEK 728
Cdd:cd03811  278 VLLEAMALGTPVVSTDCPGPREILDDGENGLLVPDGDAAALAGILAALLQK 328
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
570-761 1.05e-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: 79.71  E-value: 1.05e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 570 KPILFTMARLDRVKNLTGLVEWYGKNAKLRELANLVVVGGdrrKESKDLEEkaemkkmFELIEKYNLNGQFRWISsqmnR 649
Cdd:cd03809  192 EPYFLYVGTLEPRKNHERLLKAFALLKKQGGDLKLVIVGG---KGWEDEEL-------LDLVKKLGLGGRVRFLG----Y 257
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 650 IRNGELYRYICDTKgAFVQPALYEAFGLTVVEAMTCGLPTFATcNGGP-AEIIvhGKSGFNIDPYHGDQAADILvdffEK 728
Cdd:cd03809  258 VSDEDLPALYRGAR-AFVFPSLYEGFGLPVLEAMACGTPVIAS-NISVlPEVA--GDAALYFDPLDPESIADAI----LR 329
                        170       180       190
                 ....*....|....*....|....*....|...
gi 345104489 729 CKKDPSHWDKISQGGLKRIeEKYTWKIYSERLL 761
Cdd:cd03809  330 LLEDPSLREELIRKGLERA-KKFSWEKTAEKTL 361
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
569-761 2.17e-15

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: 78.41  E-value: 2.17e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 569 NKPILFTMARLDRVKNLTGLVEWYGKNAKLRELANLVVVGgdrrkeskDLEEKAEMKkmfELIEKYNLNGQFRWISSQMN 648
Cdd:cd03808  188 EKVVFLFVARLLKDKGIDELIEAAKILKKKGPNVRFLLVG--------DGELENPSE---ILIEKLGLEGRIEFLGFRSD 256
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 649 rIRngELYRyICDtkgAFVQPALYEAFGLTVVEAMTCGLPTFATCNGGPAEIIVHGKSGFNIDPyhGDqaADILVDFFEK 728
Cdd:cd03808  257 -VP--ELLA-ESD---VFVLPSYREGLPRSLLEAMAAGRPVITTDVPGCRELVIDGVNGFLVPP--GD--VEALADAIEK 325
                        170       180       190
                 ....*....|....*....|....*....|...
gi 345104489 729 CKKDPSHWDKISQGGLKRIEEKYTWKIYSERLL 761
Cdd:cd03808  326 LIEDPELRKEMGEAARKRVEEKFDEEKVVNKLL 358
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
419-754 1.11e-12

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: 70.34  E-value: 1.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 419 VASLLAHKLG-----VTQCTIAHALEKTKYP-DSDIYWKKLEDKYHFSCQFTADLF----------AMNHTDFIITS--- 479
Cdd:cd03820   18 VAINLANHLAkkgydVTIISLDSAEKPPFYElDDNIKIKNLGDRKYSHFKLLLKYFkkvrrlrkylKNNKPDVVISFrts 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 480 --TFQEIAGSKD-TVGQYesHTaftlpglyrvvhgidvfdpkfnivSPGADMEIYFPYTEEKRRLKHFHTEI----EDLL 552
Cdd:cd03820   98 llTFLALIGLKSkLIVWE--HN------------------------NYEAYNKGLRRLLLRRLLYKRADKIVvlteADKL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 553 YSKVENEEHLCVLN------------DRNKPILFTMARLDRVKNLTGLVEWYGKNAKLRELANLVVVG-GDRRKESKDLe 619
Cdd:cd03820  152 KKYKQPNSNVVVIPnplsfpseepstNLKSKRILAVGRLTYQKGFDLLIEAWALIAKKHPDWKLRIYGdGPEREELEKL- 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 620 ekaemkkmfelIEKYNLNGQFRWISSQMNrIRngELYRyicdTKGAFVQPALYEAFGLTVVEAMTCGLP--TFAtCNGGP 697
Cdd:cd03820  231 -----------IDKLGLEDRVKLLGPTKN-IA--EEYA----NSSIFVLSSRYEGFPMVLLEAMAYGLPiiSFD-CPTGP 291
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 345104489 698 AEIIVHGKSGFNIDPYHGDQAADILVDFFEkckkDPSHWDKISQGGLKRIeEKYTWK 754
Cdd:cd03820  292 SEIIEDGENGLLVPNGDVDALAEALLRLME----DEELRKKMGKNARKNA-ERFSIE 343
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
572-763 1.15e-12

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: 1.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 572 ILFtMARLDRVKNLTGLVEWYGKNAKLRELANLVVVGGDRRKEskdleekaemkKMFELIEKYNLNGQFRWISsqmnRIR 651
Cdd:cd03798  203 ILF-VGRLIPRKGIDLLLEAFARLAKARPDVVLLIVGDGPLRE-----------ALRALAEDLGLGDRVTFTG----RLP 266
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 652 NGELYRYI--CDtkgAFVQPALYEAFGLTVVEAMTCGLPTFATCNGGPAEIIVHGKSGFNIDPYHGDQAADILVDFFEKc 729
Cdd:cd03798  267 HEQVPAYYraCD---VFVLPSRHEGFGLVLLEAMACGLPVVATDVGGIPEVVGDPETGLLVPPGDADALAAALRRALAE- 342
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 345104489 730 kkdpsHWDKIS-QGGLKRIEEKYTWKIYSERLLTL 763
Cdd:cd03798  343 -----PYLRELgEAARARVAERFSWVKAADRIAAA 372
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
581-751 3.97e-11

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: 65.45  E-value: 3.97e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 581 RVKNLTGLVEWYgknAKLREL--ANLVVVGgdrrkeskDLEEKAEMkkmFELIEKYNLNGQFRWISSQmNRIrngELYRY 658
Cdd:cd04962  207 PVKRIDDVVRVF---ARVRRKipAKLLLVG--------DGPERVPA---EELARELGVEDRVLFLGKQ-DDV---EELLS 268
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 659 ICDTkgaFVQPALYEAFGLTVVEAMTCGLPTFATCNGGPAEIIVHGKSGFNIDPYHGDQAADILVDFFEkckkDPSHWDK 738
Cdd:cd04962  269 IADL---FLLPSEKESFGLAALEAMACGVPVVSSNAGGIPEVVKHGETGFLSDVGDVDAMAKSALSILE----DDELYNR 341
                        170
                 ....*....|...
gi 345104489 739 ISQGGLKRIEEKY 751
Cdd:cd04962  342 MGRAARKRAAERF 354
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
567-749 4.92e-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: 65.38  E-value: 4.92e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 567 DRNKPILFTMARLDRVKNLTGLVEWYgknAKLRELAN--LVVVG-GDRRKEskdLEEKAEMKKmfeLIEKYNLNGqfrWI 643
Cdd:cd03817  198 PPDEPILLYVGRLAKEKNIDFLLRAF---AELKKEPNikLVIVGdGPEREE---LKELARELG---LADKVIFTG---FV 265
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 644 SSqmNRIrnGELYrYICDtkgAFVQPALYEAFGLTVVEAMTCGLPTFATCNGGPAEIIVHGKSGFNIDPYHGDqaadiLV 723
Cdd:cd03817  266 PR--EEL--PEYY-KAAD---LFVFASTTETQGLVYLEAMAAGLPVVAAKDPAASELVEDGENGFLFEPNDET-----LA 332
                        170       180
                 ....*....|....*....|....*.
gi 345104489 724 DFFEKCKKDPSHWDKISQGGLKRIEE 749
Cdd:cd03817  333 EKLLHLRENLELLRKLSKNAEISARE 358
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
576-708 1.55e-10

glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


Pssm-ID: 340816 [Multi-domain]  Cd Length: 235  Bit Score: 62.04  E-value: 1.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 576 MARLDRVKNLTGLVEWYGKNAKLRELANLVVVGGDRRKESKDLEEKAEMKKMFELIekynlngqFRWISSQMNRirngEL 655
Cdd:cd01635  116 VGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAALGLLERVVI--------IGGLVDDEVL----EL 183
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 345104489 656 YRYICDtkgAFVQPALYEAFGLTVVEAMTCGLPTFATCNGGPAEIIVHGKSGF 708
Cdd:cd01635  184 LLAAAD---VFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGL 233
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
672-713 2.11e-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: 63.08  E-value: 2.11e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 345104489 672 YEAFGLTVVEAMTCGLPTFATCNGGPAEIIVHGKSGFNIDPY 713
Cdd:cd03802  250 DEPFGLVMIEAMACGTPVIAYRRGGLPEVIQHGETGFLVDSV 291
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
570-727 2.19e-10

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 59.45  E-value: 2.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489  570 KPILFTMARLD-RVKNLTGLVE-WygknAKLRE---LANLVVVGGDRRKEskdLEEKAEmkkmfeliekyNLNGQFRWIS 644
Cdd:pfam13692   1 RPVILFVGRLHpNVKGVDYLLEaV----PLLRKrdnDVRLVIVGDGPEEE---LEELAA-----------GLEDRVIFTG 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489  645 SQmnrirnGELYRYICDTKgAFVQPALYEAFGLTVVEAMTCGLPTFATCNGGPAEIIvHGKSGFNIDPYHGDQAADILVD 724
Cdd:pfam13692  63 FV------EDLAELLAAAD-VFVLPSLYEGFGLKLLEAMAAGLPVVATDVGGIPELV-DGENGLLVPPGDPEALAEAILR 134

                  ...
gi 345104489  725 FFE 727
Cdd:pfam13692 135 LLE 137
GT4_ALG2-like cd03805
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ...
569-760 2.94e-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: 62.99  E-value: 2.94e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 569 NKPILFTMARLDRVKNLTGLVEWYGK-NAKLRELAN--LVVVGG--DRRKES----KDLEEKAEmkkmfeliEKYNLNGQ 639
Cdd:cd03805  210 NKKFFLSINRFERKKNIALAIEAFAKlKQKLPEFENvrLVIAGGydPRVAENveylEELQRLAE--------ELLNVEDQ 281
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 640 FRWISSQMNRIRNGELYRYICdtkgafvqpALY----EAFGLTVVEAMTCGLPTFATCNGGPAEIIVHGKSGFNIDPyHG 715
Cdd:cd03805  282 VLFLRSISDSQKEQLLSSALA---------LLYtpsnEHFGIVPLEAMYAGKPVIACNSGGPLETVVEGVTGFLCEP-TP 351
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 345104489 716 DQAADILVDFFekckKDPSHWDKISQGGLKRIEEKYTWKIYSERL 760
Cdd:cd03805  352 EAFAEAMLKLA----NDPDLADRMGAAGRKRVKEKFSREAFAERL 392
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
567-720 4.39e-10

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: 61.99  E-value: 4.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 567 DRNKPILFTMARLDRVKNLTGLVEWYGKNAKLRELAnLVVVGgdrrkeskDLEEKAEMKKmfeLIEKYNLNGQFRWISsq 646
Cdd:cd03819  179 PEGKPVVGYVGRLSPEKGWLLLVDAAAELKDEPDFR-LLVAG--------DGPERDEIRR---LVERLGLRDRVTFTG-- 244
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 345104489 647 mNRIRNGELYRyICDTkgaFVQPALYEAFGLTVVEAMTCGLPTFATCNGGPAEIIVHGKSGFNIDPYHGDQAAD 720
Cdd:cd03819  245 -FREDVPAALA-ASDV---VVLPSLHEEFGRVALEAMACGTPVVATDVGGAREIVVHGRTGLLVPPGDAEALAD 313
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
606-763 1.03e-09

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: 61.19  E-value: 1.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 606 VVGGDRRKESKDLEE---KAEMKKMFELIEKYNLNGQFRWISSQMNR---IRNGELYRYI---CDtkgAFVQPALYEAFG 676
Cdd:cd03825  201 ESVTKPRKGFDELIEalkLLATKDDLLLVVFGKNDPQIVILPFDIISlgyIDDDEQLVDIysaAD---LFVHPSLADNLP 277
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 677 LTVVEAMTCGLPTFATCNGGPAEIIVHGKSGFNIDPyhGDQAAdiLVDFFEKCKKDPSHWDKISQGGLKRIEEKYTWKIY 756
Cdd:cd03825  278 NTLLEAMACGTPVVAFDTGGSPEIVQHGVTGYLVPP--GDVQA--LAEAIEWLLANPKERESLGERARALAENHFDQRVQ 353

                 ....*..
gi 345104489 757 SERLLTL 763
Cdd:cd03825  354 AQRYLEL 360
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
569-755 1.04e-09

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: 61.23  E-value: 1.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 569 NKPILFTMARLDRVKNLTGLVEWYGKNAKLRELANLVVVGGDrrkeskDLEEKAEMKkmfeLIEKYNLNGQFRWI--SSQ 646
Cdd:cd03821  203 DRRIILFLGRIHPKKGLDLLIRAARKLAEQGRDWHLVIAGPD------DGAYPAFLQ----LQSSLGLGDRVTFTgpLYG 272
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 647 MNRirnGELYryicdtKGA--FVQPALYEAFGLTVVEAMTCGLPTFATCNGGPAEIIVHGkSGFNIDPyHGDQAADILVD 724
Cdd:cd03821  273 EAK---WALY------ASAdlFVLPSYSENFGNVVAEALACGLPVVITDKCGLSELVEAG-CGVVVDP-NVSSLAEALAE 341
                        170       180       190
                 ....*....|....*....|....*....|...
gi 345104489 725 FFekckKDPSHWDKISQGGLK--RIEEKYTWKI 755
Cdd:cd03821  342 AL----RDPADRKRLGEMARRarQVEENFSWEA 370
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
569-753 1.40e-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: 60.77  E-value: 1.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 569 NKPILFTMARLDRVKNLTGLVEWYGKNAKLRELAnLVVVGgdrrkeskDLEEKAEMKKMFeliekynLNGQFRwissqmn 648
Cdd:cd03814  197 GRPLLLYVGRLAPEKNLEALLDADLPLAASPPVR-LVVVG--------DGPARAELEARG-------PDVIFT------- 253
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 649 RIRNG-ELYRYI--CDtkgAFVQPALYEAFGLTVVEAMTCGLPTFATCNGGPAEIIVHGKSGFNIDPYHGDQAADILVDF 725
Cdd:cd03814  254 GFLTGeELARAYasAD---VFVFPSRTETFGLVVLEAMASGLPVVAADAGGPRDIVRPGGTGALVEPGDAAAFAAALRAL 330
                        170       180
                 ....*....|....*....|....*...
gi 345104489 726 FEkckkDPSHWDKISQGGLKRIEEkYTW 753
Cdd:cd03814  331 LE----DPELRRRMAARARAEAER-YSW 353
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
567-763 1.74e-09

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: 60.41  E-value: 1.74e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 567 DRNKPILFTMARLDRVKNLTGLVEWYGKNAKLRELANLVVVG-GDRRkeskdlEEKAEMKKMFELIEKYNLNGQfrwiSS 645
Cdd:cd03807  187 AEDRRVIGIVGRLHPVKDHSDLLRAAALLVETHPDLRLLLVGrGPER------PNLERLLLELGLEDRVHLLGE----RS 256
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 646 QMnrirnGELYRYIcDtkgAFVQPALYEAFGLTVVEAMTCGLPTFATCNGGPAEIIVhGKSGFNIDPYHGDQAADILVDF 725
Cdd:cd03807  257 DV-----PALLPAM-D---IFVLSSRTEGFPNALLEAMACGLPVVATDVGGAAELVD-DGTGFLVPAGDPQALADAIRAL 326
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 345104489 726 FEkckkDPSHWDKISQGGLKRIEEKYTWKIYSERLLTL 763
Cdd:cd03807  327 LE----DPEKRARLGRAARERIANEFSIDAMVRRYETL 360
stp2 TIGR03088
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match ...
666-753 3.50e-09

sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match to the pfam00534 Glycosyl transferases group 1 domain. Nearly all are found in species that encode the PEP-CTERM/exosortase system predicted to act in protein sorting in a number of Gram-negative bacteria. In particular, these transferases are found proximal to a particular variant of exosortase, EpsH1, which appears to travel with a conserved group of genes summarized by Genome Property GenProp0652. The nature of the sugar transferase reaction catalyzed by members of this clade is unknown and may conceivably be variable with respect to substrate by species, but we hypothesize a conserved substrate.


Pssm-ID: 132132 [Multi-domain]  Cd Length: 374  Bit Score: 59.35  E-value: 3.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489  666 FVQPALYEAFGLTVVEAMTCGLPTFATCNGGPAEIIVHGKSGFNIDPyhGDqaADILVDFFEKCKKDPSHWDKISQGGLK 745
Cdd:TIGR03088 276 FVLPSLAEGISNTILEAMASGLPVIATAVGGNPELVQHGVTGALVPP--GD--AVALARALQPYVSDPAARRAHGAAGRA 351

                  ....*...
gi 345104489  746 RIEEKYTW 753
Cdd:TIGR03088 352 RAEQQFSI 359
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
672-752 1.93e-08

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: 56.95  E-value: 1.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 672 YEAFGLTVVEAMTCGLPTFATCNGGPAEIIVHGKSGFNIDPyhgDQAADiLVDFFEKCKKDPSHWDKISQGGLKRIEEKY 751
Cdd:cd03823  271 PEPFGLVVREAIAAGLPVIASDLGGIAELIQPGVNGLLFAP---GDAED-LAAAMRRLLTDPALLERLRAGAEPPRSTES 346

                 .
gi 345104489 752 T 752
Cdd:cd03823  347 Q 347
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
623-759 1.10e-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: 54.61  E-value: 1.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 623 EMKKMFELIEKYNL--NGQFRWISSQMNRI-RNGELYryicdtkgafVQPALYEAFGLTVVEAMTCGLPTFA-TCNGGPA 698
Cdd:cd04949  202 EREKLKKLIEELHLedNVFLKGYHSNLDQEyQDAYLS----------LLTSQMEGFGLTLMEAIGHGLPVVSyDVKYGPS 271
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 345104489 699 EIIVHGKSGFNIDPYHGDQAADILVDFFekckKDPSHWDKISQGGLKrIEEKYTWKIYSER 759
Cdd:cd04949  272 ELIEDGENGYLIEKNNIDALADKIIELL----NDPEKLQQFSEESYK-IAEKYSTENVMEK 327
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
679-761 1.87e-07

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: 54.27  E-value: 1.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 679 VVEAMTCGLPTFATCNGGPAEIIVHGKSGFNIDPyhGDQAAdiLVDFFEKCKKDPSHWDKISQGGLKRIEEKYTWKIYSE 758
Cdd:cd03794  313 LFEYMAAGKPILASDDGGSDLAVEINGCGLVVEP--GDPEA--LADAILELLDDPELRRAMGENGRELAEEKFSREKLAD 388

                 ...
gi 345104489 759 RLL 761
Cdd:cd03794  389 RLL 391
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
569-701 2.52e-07

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: 53.60  E-value: 2.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 569 NKPILFTMARLDRVKNLTGLVEWYGKNAKLRELANLVVVG-GDRRKEskdLEEKAemkKMFELIEKYNLNGQFRWISSQM 647
Cdd:cd04951  187 DEFVILNVGRLTEAKDYPNLLLAISELILSKNDFKLLIAGdGPLRNE---LERLI---CNLNLVDRVILLGQISNISEYY 260
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 345104489 648 NrirngelyryICDTkgaFVQPALYEAFGLTVVEAMTCGLPTFATCNGGPAEII 701
Cdd:cd04951  261 N----------AADL---FVLSSEWEGFGLVVAEAMACERPVVATDAGGVAEVV 301
GT4_trehalose_phosphorylase cd03792
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ...
564-752 8.98e-07

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: 51.94  E-value: 8.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 564 VLNDRNKPILFTMARLDRVKNLTGLVEWYGKNAKLRELANLVVVGG---DRRKESKDLEEKAEMKKMFELIEKYNLNGQF 640
Cdd:cd03792  191 FVIDPERPYILQVARFDPSKDPLGVIDAYKLFKRRAEEPQLVICGHgavDDPEGSVVYEEVMEYAGDDHDIHVLRLPPSD 270
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 641 RWISSQMNRIRngelyryicdtkgAFVQPALYEAFGLTVVEAMTCGLPTFATCNGGPAEIIVHGKSGFNIDPyhGDQAAD 720
Cdd:cd03792  271 QEINALQRAAT-------------VVLQLSTREGFGLTVSEALWKGKPVIATPAGGIPLQVIDGETGFLVNS--VEGAAV 335
                        170       180       190
                 ....*....|....*....|....*....|..
gi 345104489 721 ILVDFFekckKDPSHWDKISQGGLKRIEEKYT 752
Cdd:cd03792  336 RILRLL----TDPELRRKMGLAAREHVRDNFL 363
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
570-752 1.46e-06

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: 51.12  E-value: 1.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 570 KPILFTMARLDRVKNLTGLVEwygknaKLRELANLVVVGGDRrKESKDLEEKAEMKKmfelIEKYNLNGqfrwissqmnR 649
Cdd:cd03795  191 KKIFLFIGRLVYYKGLDYLIE------AAQYLNYPIVIGGEG-PLKPDLEAQIELNL----LDNVKFLG----------R 249
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 650 IRNGELYRY--ICDtkgAFVQPALY--EAFGLTVVEAMTCGLPTFAT-CNGGPAEIIVHGKSGFNIDPyhGDQAAdiLVD 724
Cdd:cd03795  250 VDDEEKVIYlhLCD---VFVFPSVLrsEAFGIVLLEAMMCGKPVISTnIGTGVPYVNNNGETGLVVPP--KDPDA--LAE 322
                        170       180
                 ....*....|....*....|....*...
gi 345104489 725 FFEKCKKDPSHWDKISQGGLKRIEEKYT 752
Cdd:cd03795  323 AIDKLLSDEELRESYGENAKKRFEELFT 350
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
673-752 2.31e-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: 50.80  E-value: 2.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 673 EAFGLTVVEAMTCGLPTFATCNGGPAEII-----VHGKSGFNIDPYHGDQAADILVdffeKCKKDPSHWDKISQGGLKRI 747
Cdd:cd03813  381 EGQPLVILEAMASGVPVVATDVGSCRELIygaddALGQAGLVVPPADPEALAEALI----KLLRDPELRQAFGEAGRKRV 456

                 ....*
gi 345104489 748 EEKYT 752
Cdd:cd03813  457 EKYYT 461
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
570-775 2.56e-06

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 50.86  E-value: 2.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 570 KPILFTMARLDRVKNLTGLVEWYGKNAKlrelANLVVVGgdrrkeskDLEEKAEMKKMFEliekyNLNGQFrwissqMNR 649
Cdd:PLN02871 263 KPLIVYVGRLGAEKNLDFLKRVMERLPG----ARLAFVG--------DGPYREELEKMFA-----GTPTVF------TGM 319
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 650 IRNGEL---YRyicdTKGAFVQPALYEAFGLTVVEAMTCGLPTFATCNGGPAEII---VHGKSGFNIDPYHGDQAADILv 723
Cdd:PLN02871 320 LQGDELsqaYA----SGDVFVMPSESETLGFVVLEAMASGVPVVAARAGGIPDIIppdQEGKTGFLYTPGDVDDCVEKL- 394
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 345104489 724 dffEKCKKDPSHWDKISQGGlkRIE-EKYTWKIYSERLLTLTGVYGFWKHVSN 775
Cdd:PLN02871 395 ---ETLLADPELRERMGAAA--REEvEKWDWRAATRKLRNEQYSAAIWFWRKK 442
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
567-759 5.16e-06

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 49.40  E-value: 5.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 567 DRNKPILFTMARLDRVKNLTGLVEWYGKNAKLRELANLVVVgGDRRKESKDleEKAE-MKKMFELIEKYN-----LNGQf 640
Cdd:PRK15484 190 SPDETVLLYAGRISPDKGILLLMQAFEKLATAHSNLKLVVV-GDPTASSKG--EKAAyQKKVLEAAKRIGdrcimLGGQ- 265
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 641 rwISSQMNRirngelYRYICDTkgAFVQPALYEAFGLTVVEAMTCGLPTFATCNGGPAEIIVHGKSGFNI-DPYHGDQ-A 718
Cdd:PRK15484 266 --PPEKMHN------YYPLADL--VVVPSQVEEAFCMVAVEAMAAGKPVLASTKGGITEFVLEGITGYHLaEPMTSDSiI 335
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 345104489 719 ADIlvdffEKCKKDPSHwDKISQGGLKRIEEKYTWKIYSER 759
Cdd:PRK15484 336 SDI-----NRTLADPEL-TQIAEQAKDFVFSKYSWEGVTQR 370
GT4_WbaZ-like cd03804
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ...
665-728 3.67e-05

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: 46.89  E-value: 3.67e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 345104489 665 AFVQPAlYEAFGLTVVEAMTCGLPTFATCNGGPAEIIVHGKSGFnidpYHGDQAADIL---VDFFEK 728
Cdd:cd03804  268 AFVFAA-EEDFGIVPVEAQACGTPVIAFGKGGALETVRPGPTGI----LFGEQTVESLkaaVEEFEQ 329
GT4_AmsK-like cd03799
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ...
673-751 4.00e-05

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: 46.67  E-value: 4.00e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 345104489 673 EAFGLTVVEAMTCGLPTFATCNGGPAEIIVHGKSGFNIDPYHGDQAADILVDFFEkckkDPSHWDKISQGGLKRIEEKY 751
Cdd:cd03799  267 DGPPNTLKEAMAMGLPVISTEHGGIPELVEDGVSGFLVPERDAEAIAEKLTYLIE----HPAIWPEMGKAGRARVEEEY 341
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
673-760 1.07e-04

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: 45.14  E-value: 1.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 673 EAFGLTVVEAMTCGLPTFATCNGGPAEIIVHGKSGFNIDPyhGDQAAdiLVDFFEKCKKDPSHWDKISQGGLKRIEEKYT 752
Cdd:cd05844  279 EGLGIVLLEAAACGVPVVSSRHGGIPEAILDGETGFLVPE--GDVDA--LADALQALLADRALADRMGGAARAFVCEQFD 354

                 ....*...
gi 345104489 753 WKIYSERL 760
Cdd:cd05844  355 IRVQTAKL 362
GT4_AmsK-like cd04946
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ...
666-751 5.82e-04

amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. AmsK is involved in the biosynthesis of amylovoran, which functions as a virulence factor. It functions as a glycosyl transferase which transfers galactose from UDP-galactose to a lipid-linked amylovoran-subunit precursor. The members of this family are found mainly in bacteria and Archaea.


Pssm-ID: 340854 [Multi-domain]  Cd Length: 401  Bit Score: 43.22  E-value: 5.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 666 FVQPALYEAFGLTVVEAMTCGLPTFATCNGGPAEIIVHGKSGF--NIDPYHGDQAADILvdffeKCKKDPSHWDKISQGG 743
Cdd:cd04946  308 FVNVSESEGIPVSIMEAISFGIPVIATNVGGTREIVENETNGLllDKDPTPNEIVSSIM-----KFYLDGGDYKTMKISA 382

                 ....*...
gi 345104489 744 LKRIEEKY 751
Cdd:cd04946  383 RECWEERF 390
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
547-711 6.34e-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: 42.66  E-value: 6.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 547 EIEDLLYSKVENEEHLCVLNDRNKPILFTMARLDRVKNLTGLVEWYGKNAKLRELANLVVVG-GDRRKEskdLEEKAEMK 625
Cdd:cd03812  168 DIEKYKFNKEKRRKRRKLLILEDKLVLGHVGRFNEQKNHSFLIDIFEELKKKNPNVKLVLVGeGELKEK---IKEKVKEL 244
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 626 kmfELIEKYNLNGqfrwissqmNRIRNGELYRyicdTKGAFVQPALYEAFGLTVVEAMTCGLPTFATCNGGPAEIIVHGK 705
Cdd:cd03812  245 ---GLEDKVIFLG---------FRNDVSEILS----AMDVFLFPSLYEGLPLVAVEAQASGLPCLLSDTITKECDITNNV 308

                 ....*.
gi 345104489 706 SGFNID 711
Cdd:cd03812  309 EFLPLN 314
PRK09922 PRK09922
lipopolysaccharide 1,6-galactosyltransferase;
665-760 1.64e-03

lipopolysaccharide 1,6-galactosyltransferase;


Pssm-ID: 182148 [Multi-domain]  Cd Length: 359  Bit Score: 41.62  E-value: 1.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 665 AFVQPALYEAFGLTVVEAMTCGLPTFAT-CNGGPAEIIvhgKSGFNIDPYHG---DQAADILVDFFEKcKKDPSHwDKIS 740
Cdd:PRK09922 260 ALLLTSKFEGFPMTLLEAMSYGIPCISSdCMSGPRDII---KPGLNGELYTPgniDEFVGKLNKVISG-EVKYQH-DAIP 334
                         90       100
                 ....*....|....*....|
gi 345104489 741 QGglkrIEEKYTWKiYSERL 760
Cdd:PRK09922 335 NS----IERFYEVL-YFKNL 349
GT4_PIG-A-like cd03796
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ...
606-700 4.21e-03

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: 40.30  E-value: 4.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345104489 606 VVGGDRRKESkDLEEkaemkkmfeLIEKYNLNGQFRWISS-QMNRIRN----GELyryicdtkgaFVQPALYEAFGLTVV 680
Cdd:cd03796  228 IIGGDGPKRI-ELEE---------MREKYQLQDRVELLGAvPHEEVRDvlvqGHI----------FLNTSLTEAFCIAIV 287
                         90       100
                 ....*....|....*....|
gi 345104489 681 EAMTCGLPTFATCNGGPAEI 700
Cdd:cd03796  288 EAASCGLLVVSTRVGGIPEV 307
 
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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