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Conserved domains on  [gi|19114944|ref|NP_594032|]
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spore wall 1,3-beta-glucan synthase catalytic subunit Bgs2 [Schizosaccharomyces pombe]

Protein Classification

1,3-beta-glucan synthase( domain architecture ID 10626219)

1,3-beta-glucan synthase is a glycosyltransferase family 48 protein that catalyzes the addition of glucose to a ((1->3)-beta-D-glucosyl) chain

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Glucan_synthase pfam02364
1,3-beta-glucan synthase component; This family consists of various 1,3-beta-glucan synthase ...
844-1666 0e+00

1,3-beta-glucan synthase component; This family consists of various 1,3-beta-glucan synthase components including Gls1, Gls2 and Gls3 from yeast. 1,3-beta-glucan synthase EC:2.4.1.34 also known as callose synthase catalyzes the formation of a beta-1,3-glucan polymer that is a major component of the fungal cell wall. The reaction catalyzed is:- UDP-glucose + {(1,3)-beta-D-glucosyl}(N) <=> UDP + {(1,3)-beta-D-glucosyl}(N+1).


:

Pssm-ID: 426739  Cd Length: 818  Bit Score: 1563.32  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114944    844 YFPAHSEAERRLSFFAQSLATPIPEPIPVDAMPTFTVLVPHYGEKILLSLKEIIREQDKLSRVTLLEYLKQLHANEWKCF 923
Cdd:pfam02364    1 FFPKNSEAERRISFFAQSLSTPMPEPPPVEKMPTFTVLIPHYSEKILLSLREIIREEEDGSRVTLLEYLKQLHPDEWKNF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114944    924 VRDTKILAEEDAlsnqDLNSQDESMKAEQLHKKFDDLPFYCIGFKNATPEYTLRTRIWASLRSQTLYRTVSGFMNYSRAI 1003
Cdd:pfam02364   81 VEDTKLLAEEDD----ADDSNSEKDEEDLVKEKIDDLPFYCIGFKSSTPEYTLRTRIWASLRGQTLYRTVSGFMNYSRAI 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114944   1004 KLLYRVENPDVAQLFEGQMDVLEYELDRMASRKFKMCVSMQRYAKFTADEIENTEFILRAYPDLLIAYLDEDPPKEGETt 1083
Cdd:pfam02364  157 KLLYRVENPSLVQLYSGNSEKLERELESMALRKFRLVVSMQRYAKFKAEEDENAEFLLRAYPDLQIAYLDEEPDEEGGE- 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114944   1084 PQLYAALIDGYSELD-ENKKRKPKYRIKLSGNPILGDGKSDNQNLSLPFYRGEYIQLIDANQDNYLEECLKIRSILAEFE 1162
Cdd:pfam02364  236 PEYYSVLIDGHCEIDqENGKRKPKYRIRLSGNPILGDGKSDNQNHAIIFYRGEYIQVIDANQDNYLEECLKIRSVLAEFE 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114944   1163 AFDLKTNDPYAETNALYQNNPVAIMGAREYIFSENIGILGDVAAGKEQTFGTLFARTMAQIGGKLHYGHPDFLNAIYMTT 1242
Cdd:pfam02364  316 EMNLGIRSPYIPGIYDEEKNPVAILGAREYIFSENIGVLGDIAAGKEQTFGTLFARTLAEIGGKLHYGHPDFLNAIFMTT 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114944   1243 RGGVSKAQKGLHVNEDIYAGMTALQRGGRIKHCEYYQCGKGRDLGFGSILNFTTKIGTGMGEQMVSREYYYLGTQLPFDR 1322
Cdd:pfam02364  396 RGGVSKAQKGLHLNEDIYAGMNATLRGGRIKHCEYYQCGKGRDLGFGSILNFTTKIGAGMGEQMLSREYYYLGTQLPLDR 475
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114944   1323 FLSFYYAHPGFHINNIFIMLSVQLFMVVLVNLGGMYHVVTVCDYDHDQKLTVPMRPEGCYQLNPVVNWLKRCIISIFIVF 1402
Cdd:pfam02364  476 FLSFYYAHPGFHLNNMFIMLSVQLFMLLLLNLGALNHESIICEYDKDNPITDPERPIGCYNLQPVLNWVSRFVLSIFIVF 555
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114944   1403 FISFVPLTVQELTERGAWRALTRLGKHFASFSPMFEVFACQTYAQSVIANLSFGGARYIGTGRGFATARLSFSLLFSRFA 1482
Cdd:pfam02364  556 FISFLPLIVQELLERGFLKAVSRFFKHFLSLSPLFEVFVCQIYAHSLLRNLTFGGARYIATGRGFATTRIPFAELYSRFA 635
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114944   1483 GPSIYLGSRTLLMLLFGTMTVWIPHLIYFWISTLAMCISPFIFNPHQFSWTDFFVDYREFIRWLSRGNSRSHINSWIGYC 1562
Cdd:pfam02364  636 RSSIYKGIELFLMLLFATTTMWIPALLWFWITVVSLCLAPFLFNPHQFSWLDFFIDYRDFIRWLSRGNSKTHENSWIGYE 715
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114944   1563 RLTRTRITGYKRRLLGVPVSKGVIDTSRAHFTNMFFTEIFIPLMLVPLTLVSYFFIDSQPGNPDPsKVTNPILRILILAF 1642
Cdd:pfam02364  716 RQSRLRITGYKRKLLGDPSEKLSGDVPRASFTNLFFSEIILPLIVALLIFIAYRFINSQYGVRGP-KPTNSVYRLAIVSI 794
                          810       820
                   ....*....|....*....|....
gi 19114944   1643 LPIIVAAVVSMTFAGMACMMGPLL 1666
Cdd:pfam02364  795 LPILLNWIVLLVLFGISCLLGPAL 818
FKS1_dom1 pfam14288
1,3-beta-glucan synthase subunit FKS1, domain-1; The FKS1_dom1 domain is likely to be the ...
335-441 7.06e-47

1,3-beta-glucan synthase subunit FKS1, domain-1; The FKS1_dom1 domain is likely to be the 'Class I' region just N-terminal to the first set of transmembrane helices that is involved in 1,3-beta-glucan synthesis itself. This family is found on proteins with family Glucan_synthase, pfam02364.


:

Pssm-ID: 464126  Cd Length: 112  Bit Score: 163.93  E-value: 7.06e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114944    335 QVRQLALYLLCWGEANNIRFCPECLCFIFKLANDFM------QSEDYAKSEPIEDDCFYLDNVITPLYEFIRDQQFELLD 408
Cdd:pfam14288    2 KLLQIALYLLIWGEAANVRFMPECLCYIFHCMAYELngildgNVSPMTYSPYSGPEGSFLDNVITPIYRFIRDQEYEISK 81
                           90       100       110
                   ....*....|....*....|....*....|...
gi 19114944    409 GKlvrrERDHAQIIGYDDINQLFWYPEGIARIV 441
Cdd:pfam14288   82 NG----EADHSAWIGYDDINQLFWSPECIERLG 110
GarD super family cl48851
bacterial effector GarD (gamma resistance determinant); GarD shields Chlamydia trachomatis ...
1628-1762 3.29e-03

bacterial effector GarD (gamma resistance determinant); GarD shields Chlamydia trachomatis inclusions from RNF213-mediated ubiquitylation and destruction, thereby providing protection from cell-autonomous immunity.


The actual alignment was detected with superfamily member cd23942:

Pssm-ID: 467933  Cd Length: 284  Bit Score: 41.71  E-value: 3.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114944 1628 SKVTNPILRILI-LAFLPIIVAAVVSMTFAG-------MACMMGplldlCCkkfGAVLAALAHGITVFMFIIVFEVSWYL 1699
Cdd:cd23942  135 AMIGSFVANLIItIALCALLAGTVLALFFLGpgasavlTAAMIG-----CC---AAGGGALLISVLGFIISSVCQAKKQQ 206
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114944 1700 E-AWCLAKTVLSMLCIIAIQRF---FFK--IIQVLFLTRELKH-DGTNLAWWTGKWYSRGLGFHALSQPS 1762
Cdd:cd23942  207 EaVRHLQRATLYALVSEQIQRFpkdFLTngVAKSLAQIQAGEQlDEGMLSWEEMPSLTQLGGREGQDAQA 276
 
Name Accession Description Interval E-value
Glucan_synthase pfam02364
1,3-beta-glucan synthase component; This family consists of various 1,3-beta-glucan synthase ...
844-1666 0e+00

1,3-beta-glucan synthase component; This family consists of various 1,3-beta-glucan synthase components including Gls1, Gls2 and Gls3 from yeast. 1,3-beta-glucan synthase EC:2.4.1.34 also known as callose synthase catalyzes the formation of a beta-1,3-glucan polymer that is a major component of the fungal cell wall. The reaction catalyzed is:- UDP-glucose + {(1,3)-beta-D-glucosyl}(N) <=> UDP + {(1,3)-beta-D-glucosyl}(N+1).


Pssm-ID: 426739  Cd Length: 818  Bit Score: 1563.32  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114944    844 YFPAHSEAERRLSFFAQSLATPIPEPIPVDAMPTFTVLVPHYGEKILLSLKEIIREQDKLSRVTLLEYLKQLHANEWKCF 923
Cdd:pfam02364    1 FFPKNSEAERRISFFAQSLSTPMPEPPPVEKMPTFTVLIPHYSEKILLSLREIIREEEDGSRVTLLEYLKQLHPDEWKNF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114944    924 VRDTKILAEEDAlsnqDLNSQDESMKAEQLHKKFDDLPFYCIGFKNATPEYTLRTRIWASLRSQTLYRTVSGFMNYSRAI 1003
Cdd:pfam02364   81 VEDTKLLAEEDD----ADDSNSEKDEEDLVKEKIDDLPFYCIGFKSSTPEYTLRTRIWASLRGQTLYRTVSGFMNYSRAI 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114944   1004 KLLYRVENPDVAQLFEGQMDVLEYELDRMASRKFKMCVSMQRYAKFTADEIENTEFILRAYPDLLIAYLDEDPPKEGETt 1083
Cdd:pfam02364  157 KLLYRVENPSLVQLYSGNSEKLERELESMALRKFRLVVSMQRYAKFKAEEDENAEFLLRAYPDLQIAYLDEEPDEEGGE- 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114944   1084 PQLYAALIDGYSELD-ENKKRKPKYRIKLSGNPILGDGKSDNQNLSLPFYRGEYIQLIDANQDNYLEECLKIRSILAEFE 1162
Cdd:pfam02364  236 PEYYSVLIDGHCEIDqENGKRKPKYRIRLSGNPILGDGKSDNQNHAIIFYRGEYIQVIDANQDNYLEECLKIRSVLAEFE 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114944   1163 AFDLKTNDPYAETNALYQNNPVAIMGAREYIFSENIGILGDVAAGKEQTFGTLFARTMAQIGGKLHYGHPDFLNAIYMTT 1242
Cdd:pfam02364  316 EMNLGIRSPYIPGIYDEEKNPVAILGAREYIFSENIGVLGDIAAGKEQTFGTLFARTLAEIGGKLHYGHPDFLNAIFMTT 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114944   1243 RGGVSKAQKGLHVNEDIYAGMTALQRGGRIKHCEYYQCGKGRDLGFGSILNFTTKIGTGMGEQMVSREYYYLGTQLPFDR 1322
Cdd:pfam02364  396 RGGVSKAQKGLHLNEDIYAGMNATLRGGRIKHCEYYQCGKGRDLGFGSILNFTTKIGAGMGEQMLSREYYYLGTQLPLDR 475
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114944   1323 FLSFYYAHPGFHINNIFIMLSVQLFMVVLVNLGGMYHVVTVCDYDHDQKLTVPMRPEGCYQLNPVVNWLKRCIISIFIVF 1402
Cdd:pfam02364  476 FLSFYYAHPGFHLNNMFIMLSVQLFMLLLLNLGALNHESIICEYDKDNPITDPERPIGCYNLQPVLNWVSRFVLSIFIVF 555
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114944   1403 FISFVPLTVQELTERGAWRALTRLGKHFASFSPMFEVFACQTYAQSVIANLSFGGARYIGTGRGFATARLSFSLLFSRFA 1482
Cdd:pfam02364  556 FISFLPLIVQELLERGFLKAVSRFFKHFLSLSPLFEVFVCQIYAHSLLRNLTFGGARYIATGRGFATTRIPFAELYSRFA 635
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114944   1483 GPSIYLGSRTLLMLLFGTMTVWIPHLIYFWISTLAMCISPFIFNPHQFSWTDFFVDYREFIRWLSRGNSRSHINSWIGYC 1562
Cdd:pfam02364  636 RSSIYKGIELFLMLLFATTTMWIPALLWFWITVVSLCLAPFLFNPHQFSWLDFFIDYRDFIRWLSRGNSKTHENSWIGYE 715
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114944   1563 RLTRTRITGYKRRLLGVPVSKGVIDTSRAHFTNMFFTEIFIPLMLVPLTLVSYFFIDSQPGNPDPsKVTNPILRILILAF 1642
Cdd:pfam02364  716 RQSRLRITGYKRKLLGDPSEKLSGDVPRASFTNLFFSEIILPLIVALLIFIAYRFINSQYGVRGP-KPTNSVYRLAIVSI 794
                          810       820
                   ....*....|....*....|....
gi 19114944   1643 LPIIVAAVVSMTFAGMACMMGPLL 1666
Cdd:pfam02364  795 LPILLNWIVLLVLFGISCLLGPAL 818
FKS1_dom1 pfam14288
1,3-beta-glucan synthase subunit FKS1, domain-1; The FKS1_dom1 domain is likely to be the ...
335-441 7.06e-47

1,3-beta-glucan synthase subunit FKS1, domain-1; The FKS1_dom1 domain is likely to be the 'Class I' region just N-terminal to the first set of transmembrane helices that is involved in 1,3-beta-glucan synthesis itself. This family is found on proteins with family Glucan_synthase, pfam02364.


Pssm-ID: 464126  Cd Length: 112  Bit Score: 163.93  E-value: 7.06e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114944    335 QVRQLALYLLCWGEANNIRFCPECLCFIFKLANDFM------QSEDYAKSEPIEDDCFYLDNVITPLYEFIRDQQFELLD 408
Cdd:pfam14288    2 KLLQIALYLLIWGEAANVRFMPECLCYIFHCMAYELngildgNVSPMTYSPYSGPEGSFLDNVITPIYRFIRDQEYEISK 81
                           90       100       110
                   ....*....|....*....|....*....|...
gi 19114944    409 GKlvrrERDHAQIIGYDDINQLFWYPEGIARIV 441
Cdd:pfam14288   82 NG----EADHSAWIGYDDINQLFWSPECIERLG 110
GarD cd23942
bacterial effector GarD (gamma resistance determinant); GarD shields Chlamydia trachomatis ...
1628-1762 3.29e-03

bacterial effector GarD (gamma resistance determinant); GarD shields Chlamydia trachomatis inclusions from RNF213-mediated ubiquitylation and destruction, thereby providing protection from cell-autonomous immunity.


Pssm-ID: 467933  Cd Length: 284  Bit Score: 41.71  E-value: 3.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114944 1628 SKVTNPILRILI-LAFLPIIVAAVVSMTFAG-------MACMMGplldlCCkkfGAVLAALAHGITVFMFIIVFEVSWYL 1699
Cdd:cd23942  135 AMIGSFVANLIItIALCALLAGTVLALFFLGpgasavlTAAMIG-----CC---AAGGGALLISVLGFIISSVCQAKKQQ 206
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114944 1700 E-AWCLAKTVLSMLCIIAIQRF---FFK--IIQVLFLTRELKH-DGTNLAWWTGKWYSRGLGFHALSQPS 1762
Cdd:cd23942  207 EaVRHLQRATLYALVSEQIQRFpkdFLTngVAKSLAQIQAGEQlDEGMLSWEEMPSLTQLGGREGQDAQA 276
 
Name Accession Description Interval E-value
Glucan_synthase pfam02364
1,3-beta-glucan synthase component; This family consists of various 1,3-beta-glucan synthase ...
844-1666 0e+00

1,3-beta-glucan synthase component; This family consists of various 1,3-beta-glucan synthase components including Gls1, Gls2 and Gls3 from yeast. 1,3-beta-glucan synthase EC:2.4.1.34 also known as callose synthase catalyzes the formation of a beta-1,3-glucan polymer that is a major component of the fungal cell wall. The reaction catalyzed is:- UDP-glucose + {(1,3)-beta-D-glucosyl}(N) <=> UDP + {(1,3)-beta-D-glucosyl}(N+1).


Pssm-ID: 426739  Cd Length: 818  Bit Score: 1563.32  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114944    844 YFPAHSEAERRLSFFAQSLATPIPEPIPVDAMPTFTVLVPHYGEKILLSLKEIIREQDKLSRVTLLEYLKQLHANEWKCF 923
Cdd:pfam02364    1 FFPKNSEAERRISFFAQSLSTPMPEPPPVEKMPTFTVLIPHYSEKILLSLREIIREEEDGSRVTLLEYLKQLHPDEWKNF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114944    924 VRDTKILAEEDAlsnqDLNSQDESMKAEQLHKKFDDLPFYCIGFKNATPEYTLRTRIWASLRSQTLYRTVSGFMNYSRAI 1003
Cdd:pfam02364   81 VEDTKLLAEEDD----ADDSNSEKDEEDLVKEKIDDLPFYCIGFKSSTPEYTLRTRIWASLRGQTLYRTVSGFMNYSRAI 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114944   1004 KLLYRVENPDVAQLFEGQMDVLEYELDRMASRKFKMCVSMQRYAKFTADEIENTEFILRAYPDLLIAYLDEDPPKEGETt 1083
Cdd:pfam02364  157 KLLYRVENPSLVQLYSGNSEKLERELESMALRKFRLVVSMQRYAKFKAEEDENAEFLLRAYPDLQIAYLDEEPDEEGGE- 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114944   1084 PQLYAALIDGYSELD-ENKKRKPKYRIKLSGNPILGDGKSDNQNLSLPFYRGEYIQLIDANQDNYLEECLKIRSILAEFE 1162
Cdd:pfam02364  236 PEYYSVLIDGHCEIDqENGKRKPKYRIRLSGNPILGDGKSDNQNHAIIFYRGEYIQVIDANQDNYLEECLKIRSVLAEFE 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114944   1163 AFDLKTNDPYAETNALYQNNPVAIMGAREYIFSENIGILGDVAAGKEQTFGTLFARTMAQIGGKLHYGHPDFLNAIYMTT 1242
Cdd:pfam02364  316 EMNLGIRSPYIPGIYDEEKNPVAILGAREYIFSENIGVLGDIAAGKEQTFGTLFARTLAEIGGKLHYGHPDFLNAIFMTT 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114944   1243 RGGVSKAQKGLHVNEDIYAGMTALQRGGRIKHCEYYQCGKGRDLGFGSILNFTTKIGTGMGEQMVSREYYYLGTQLPFDR 1322
Cdd:pfam02364  396 RGGVSKAQKGLHLNEDIYAGMNATLRGGRIKHCEYYQCGKGRDLGFGSILNFTTKIGAGMGEQMLSREYYYLGTQLPLDR 475
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114944   1323 FLSFYYAHPGFHINNIFIMLSVQLFMVVLVNLGGMYHVVTVCDYDHDQKLTVPMRPEGCYQLNPVVNWLKRCIISIFIVF 1402
Cdd:pfam02364  476 FLSFYYAHPGFHLNNMFIMLSVQLFMLLLLNLGALNHESIICEYDKDNPITDPERPIGCYNLQPVLNWVSRFVLSIFIVF 555
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114944   1403 FISFVPLTVQELTERGAWRALTRLGKHFASFSPMFEVFACQTYAQSVIANLSFGGARYIGTGRGFATARLSFSLLFSRFA 1482
Cdd:pfam02364  556 FISFLPLIVQELLERGFLKAVSRFFKHFLSLSPLFEVFVCQIYAHSLLRNLTFGGARYIATGRGFATTRIPFAELYSRFA 635
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114944   1483 GPSIYLGSRTLLMLLFGTMTVWIPHLIYFWISTLAMCISPFIFNPHQFSWTDFFVDYREFIRWLSRGNSRSHINSWIGYC 1562
Cdd:pfam02364  636 RSSIYKGIELFLMLLFATTTMWIPALLWFWITVVSLCLAPFLFNPHQFSWLDFFIDYRDFIRWLSRGNSKTHENSWIGYE 715
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114944   1563 RLTRTRITGYKRRLLGVPVSKGVIDTSRAHFTNMFFTEIFIPLMLVPLTLVSYFFIDSQPGNPDPsKVTNPILRILILAF 1642
Cdd:pfam02364  716 RQSRLRITGYKRKLLGDPSEKLSGDVPRASFTNLFFSEIILPLIVALLIFIAYRFINSQYGVRGP-KPTNSVYRLAIVSI 794
                          810       820
                   ....*....|....*....|....
gi 19114944   1643 LPIIVAAVVSMTFAGMACMMGPLL 1666
Cdd:pfam02364  795 LPILLNWIVLLVLFGISCLLGPAL 818
FKS1_dom1 pfam14288
1,3-beta-glucan synthase subunit FKS1, domain-1; The FKS1_dom1 domain is likely to be the ...
335-441 7.06e-47

1,3-beta-glucan synthase subunit FKS1, domain-1; The FKS1_dom1 domain is likely to be the 'Class I' region just N-terminal to the first set of transmembrane helices that is involved in 1,3-beta-glucan synthesis itself. This family is found on proteins with family Glucan_synthase, pfam02364.


Pssm-ID: 464126  Cd Length: 112  Bit Score: 163.93  E-value: 7.06e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114944    335 QVRQLALYLLCWGEANNIRFCPECLCFIFKLANDFM------QSEDYAKSEPIEDDCFYLDNVITPLYEFIRDQQFELLD 408
Cdd:pfam14288    2 KLLQIALYLLIWGEAANVRFMPECLCYIFHCMAYELngildgNVSPMTYSPYSGPEGSFLDNVITPIYRFIRDQEYEISK 81
                           90       100       110
                   ....*....|....*....|....*....|...
gi 19114944    409 GKlvrrERDHAQIIGYDDINQLFWYPEGIARIV 441
Cdd:pfam14288   82 NG----EADHSAWIGYDDINQLFWSPECIERLG 110
GarD cd23942
bacterial effector GarD (gamma resistance determinant); GarD shields Chlamydia trachomatis ...
1628-1762 3.29e-03

bacterial effector GarD (gamma resistance determinant); GarD shields Chlamydia trachomatis inclusions from RNF213-mediated ubiquitylation and destruction, thereby providing protection from cell-autonomous immunity.


Pssm-ID: 467933  Cd Length: 284  Bit Score: 41.71  E-value: 3.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114944 1628 SKVTNPILRILI-LAFLPIIVAAVVSMTFAG-------MACMMGplldlCCkkfGAVLAALAHGITVFMFIIVFEVSWYL 1699
Cdd:cd23942  135 AMIGSFVANLIItIALCALLAGTVLALFFLGpgasavlTAAMIG-----CC---AAGGGALLISVLGFIISSVCQAKKQQ 206
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114944 1700 E-AWCLAKTVLSMLCIIAIQRF---FFK--IIQVLFLTRELKH-DGTNLAWWTGKWYSRGLGFHALSQPS 1762
Cdd:cd23942  207 EaVRHLQRATLYALVSEQIQRFpkdFLTngVAKSLAQIQAGEQlDEGMLSWEEMPSLTQLGGREGQDAQA 276
 
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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