|
Name |
Accession |
Description |
Interval |
E-value |
| Glyco_transf_24 |
pfam18404 |
Glucosyltransferase 24; This is the catalytic domain found in UDP-glucose:glycoprotein ... |
1232-1498 |
0e+00 |
|
Glucosyltransferase 24; This is the catalytic domain found in UDP-glucose:glycoprotein glucosyltransferase (UGGT). This domain belongs to glucosyltransferase 24 family (GT24) A-type domain. The GT domain displays the expected glycosyltransferase type A (GT-A) fold.
:
Pssm-ID: 436473 Cd Length: 268 Bit Score: 583.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859593 1232 NIFSVASGHLYERFLRIMMLSVLRNTKTPVKFWLLKNYLSPTFKEVIPHMAKEYGFRYELVQYRWPRWLRQQTERQRIIW 1311
Cdd:pfam18404 2 NIFSVASGHLYERFLKIMMLSVRKNTKSPVKFWFIENFLSPSFKAFLPHLAKEYGFEYELVTYKWPSWLRKQTEKQRIIW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859593 1312 GYKILFLDVLFPLAVDKIIFVDADQIVRHDLKELRDFDLDGAPYGYTPFCDSRREMDGYRFWKTGYWASHLLRRKYHISA 1391
Cdd:pfam18404 82 GYKILFLDVLFPLDLDKVIFVDADQVVRTDLKELVDMDLEGAPYGYTPMCDSRKEMEGFRFWKQGYWKDHLRGRPYHISA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859593 1392 LYVVDLKKFRRIGAGDRLRSQYQALSQDPNSLSNLDQDLPNNMIYQVAIKSLPQDWLWCETWCDDESKQRAKTIDLCNNP 1471
Cdd:pfam18404 162 LYVVDLKRFRQMAAGDRLRSHYQQLSADPNSLANLDQDLPNNMQHQVPIFSLPQEWLWCETWCSDESLKKAKTIDLCNNP 241
|
250 260
....*....|....*....|....*..
gi 238859593 1472 KTKESKLKAAARIVPEWVEYDAEIRQL 1498
Cdd:pfam18404 242 LTKEPKLDRAKRIIPEWTDYDEEVAAL 268
|
|
| Thioredoxin_12 |
pfam18400 |
Thioredoxin-like domain; This is one of four TRXL(thioredoxin-like) domains found in ... |
45-226 |
1.76e-69 |
|
Thioredoxin-like domain; This is one of four TRXL(thioredoxin-like) domains found in UDP-glucose:glycoprotein glucosyltransferase (UGGT).
:
Pssm-ID: 465748 Cd Length: 187 Bit Score: 231.36 E-value: 1.76e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859593 45 ETPLLLEASEFMAEESNEKFWQFLETVQELAIY-KQTESDYSYYNLILKKAGQFLDNLHINLLKFAFSIRAYSPAIQMFQ 123
Cdd:pfam18400 1 ATPLLLEALETLAEENPDLFFPFLDALTNLDGEfADASTDEELYEAALKLASDHLSPLALSLFKLALSLRSASPRIEAFY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859593 124 QIAAD----EPPPDGCNAFVVIHKKHTCKINEIKKLLKKAA-SRTRPYLFKGDHKFPTNKEnLPVVILYAEMGTRTFSAF 198
Cdd:pfam18400 81 QIYAEsvsfEGAPPECDSWVDWGGEVYCDPEDLDALLKSEAsSRPQPELLPFDHVYPDSGS-SPVAILYADLGSPNFREF 159
|
170 180
....*....|....*....|....*...
gi 238859593 199 HKVLSEKAQNEEILYVLRHYIQKPSSRK 226
Cdd:pfam18400 160 HKYLSELAKDGKIRYVLRHVPPSGSESK 187
|
|
| Thioredoxin_14 |
pfam18402 |
Thioredoxin-like domain; This is the third out of four TRXL(thioredoxin-like) domains found in ... |
437-686 |
2.31e-63 |
|
Thioredoxin-like domain; This is the third out of four TRXL(thioredoxin-like) domains found in UDP-glucose:glycoprotein glucosyltransferase (UGGT).
:
Pssm-ID: 465750 Cd Length: 248 Bit Score: 216.38 E-value: 2.31e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859593 437 LDIRHS-----SIMWINDLENDDLYITWPTSCQKLLKPVFPGSVPSIRRNFHNLVLFIDPAQ-EYTLDFIKLADVFYSHE 510
Cdd:pfam18402 1 FDIRDRiegggVIIWLNDLEKDKRYSRWPSSLQELLRPTYPGQLPPIRKNLFNLVLVVDLSQpEDLLLLVETLQSFVQRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859593 511 VPLRIGFVFILNTDDEvdgandaGVALWRAFNYIAEEFDISEAFISIVHMYQKVKKDQNILTVDNVKSVLQNTFPHANIW 590
Cdd:pfam18402 81 IPVRFGLVPLVNSTED-------GLAQAKLFYYLLENYGLKAALSFLTASLYALAKKVLSPTKAIFSSALKERTLRPQAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859593 591 DILGI--HSKYDEERKAGASFYKMTGLGPL--PQALyNGEPFKHEEmNIKElkmAVLQRMMDASVYLQREVFLGTLNDRT 666
Cdd:pfam18402 154 SFDEVlkSEVYDERLKKAKEYLKRLGLDSLsgPVFV-NGVPLPRDE-NWLQ---ALSQRISEDLQLLQKAVYEGALTDDD 228
|
250 260
....*....|....*....|
gi 238859593 667 NAIDFLMDRNNVVPRINTLI 686
Cdd:pfam18402 229 DVPDFFYDLPNALPRRNPLI 248
|
|
| Thioredoxin_15 |
pfam18403 |
Thioredoxin-like domain; This is the fourth TRXL(thioredoxin-like) domain found in UDP-glucose: ... |
710-933 |
1.36e-57 |
|
Thioredoxin-like domain; This is the fourth TRXL(thioredoxin-like) domain found in UDP-glucose:glycoprotein glucosyltransferase (UGGT).
:
Pssm-ID: 465751 Cd Length: 205 Bit Score: 197.83 E-value: 1.36e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859593 710 TFFFLDSQdkSAVIAKNMYYLTqDDESIISAVTLWIIADFDKPSGRKLLFNALKHMKTSVHSRLGIIYNPTSKiNEENTA 789
Cdd:pfam18403 1 DLNKLYSE--HADLFDKMPYLE-ASSDKEDWATLWVVADLDSESGRKLLLSALEFRKSNPGVRLGIIHNPASP-SEASSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859593 790 ISRGILAAFLTQKNMFLRSFLGQLAKEEIATAIYSGdkiktfliegmdknafeKKYNTVGVNIFRTHQLFCQdVLKLRPG 869
Cdd:pfam18403 77 ISSALLAALLKLKNLDALEFLTKLLEEEEAAASESG-----------------KSSAEAAADYWKALQPFLR-VLGLKPG 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 238859593 870 EMGIVSNGRFLGPLDED--FYAEDFYLLEKITFSNLGEKIKGIVENMGINAN-NMSDFIMKVDALMS 933
Cdd:pfam18403 139 QNALVLNGRVVGPIPEDeeFSADDFELLLSYERSKRIEPVYKAIEELGLEDKiSDPDAVAKLTSLVA 205
|
|
| UDP-g_GGTase |
pfam06427 |
UDP-glucose:Glycoprotein Glucosyltransferase; This domain consists of 7 stranded ... |
1094-1199 |
5.26e-46 |
|
UDP-glucose:Glycoprotein Glucosyltransferase; This domain consists of 7 stranded beta-sandwiches found in UDP-glucose-glycoprotein glucosyltransferase-like proteins. UDP-g_GGTase is an important, central component of the QC system in the ER for checking that glycoproteins are folded correctly. This QC prevents incorrectly folded glycoproteins from leaving the ER.
:
Pssm-ID: 461910 Cd Length: 109 Bit Score: 160.73 E-value: 5.26e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859593 1094 GQCFDKVTEQPPRGLQFTLGTKNKPAVVDTIVMAHHGYFQLKANPGAWILRLHQGKSEDIYQIVGHEGTD-SQADLEDII 1172
Cdd:pfam06427 2 GHARDVTTGSPPRGLQLVLGTEKNPHVADTIVMANLGYFQLKANPGVWKLELREGRSSDIYEIESVGAEGwPSPGDEGTE 81
|
90 100
....*....|....*....|....*..
gi 238859593 1173 VVLNSFKSKILKVKVKKETDKIKEDIL 1199
Cdd:pfam06427 82 VALTSFEGLTLYPRLSRKPGMENEDVL 108
|
|
| Thioredoxin_13 |
pfam18401 |
Thioredoxin-like domain; This is the second out of four TRXL(thioredoxin-like) domains found ... |
296-424 |
1.10e-44 |
|
Thioredoxin-like domain; This is the second out of four TRXL(thioredoxin-like) domains found in UDP-glucose:glycoprotein glucosyltransferase (UGGT).
:
Pssm-ID: 465749 Cd Length: 136 Bit Score: 158.11 E-value: 1.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859593 296 ESNKQMMPLKVWELQDLSFQAASQIMSAPvyDSIKLMKDISQNFPIKARSLTRIAVNQHMREEIKENQKDLqvrfkIQPG 375
Cdd:pfam18401 1 EEVEDLKPLSVWELQDLGLQAAQFIMSSD--DPLDTLLKLSQDFPKYASSLARHNVSDELREEIEENQERL-----LPPG 73
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 238859593 376 DARLFINGLRVDMDVYDAFSILDMLKLEGKMMNGLRNLGINGEDMSKFL 424
Cdd:pfam18401 74 DNALWLNGLQLDERDIDPFSLLDILRRERKLINGLRKLGLSGSEAVDLL 122
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Glyco_transf_24 |
pfam18404 |
Glucosyltransferase 24; This is the catalytic domain found in UDP-glucose:glycoprotein ... |
1232-1498 |
0e+00 |
|
Glucosyltransferase 24; This is the catalytic domain found in UDP-glucose:glycoprotein glucosyltransferase (UGGT). This domain belongs to glucosyltransferase 24 family (GT24) A-type domain. The GT domain displays the expected glycosyltransferase type A (GT-A) fold.
Pssm-ID: 436473 Cd Length: 268 Bit Score: 583.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859593 1232 NIFSVASGHLYERFLRIMMLSVLRNTKTPVKFWLLKNYLSPTFKEVIPHMAKEYGFRYELVQYRWPRWLRQQTERQRIIW 1311
Cdd:pfam18404 2 NIFSVASGHLYERFLKIMMLSVRKNTKSPVKFWFIENFLSPSFKAFLPHLAKEYGFEYELVTYKWPSWLRKQTEKQRIIW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859593 1312 GYKILFLDVLFPLAVDKIIFVDADQIVRHDLKELRDFDLDGAPYGYTPFCDSRREMDGYRFWKTGYWASHLLRRKYHISA 1391
Cdd:pfam18404 82 GYKILFLDVLFPLDLDKVIFVDADQVVRTDLKELVDMDLEGAPYGYTPMCDSRKEMEGFRFWKQGYWKDHLRGRPYHISA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859593 1392 LYVVDLKKFRRIGAGDRLRSQYQALSQDPNSLSNLDQDLPNNMIYQVAIKSLPQDWLWCETWCDDESKQRAKTIDLCNNP 1471
Cdd:pfam18404 162 LYVVDLKRFRQMAAGDRLRSHYQQLSADPNSLANLDQDLPNNMQHQVPIFSLPQEWLWCETWCSDESLKKAKTIDLCNNP 241
|
250 260
....*....|....*....|....*..
gi 238859593 1472 KTKESKLKAAARIVPEWVEYDAEIRQL 1498
Cdd:pfam18404 242 LTKEPKLDRAKRIIPEWTDYDEEVAAL 268
|
|
| GT8_HUGT1_C_like |
cd06432 |
The C-terminal domain of HUGT1-like is highly homologous to the GT 8 family; C-terminal domain ... |
1231-1478 |
4.11e-180 |
|
The C-terminal domain of HUGT1-like is highly homologous to the GT 8 family; C-terminal domain of glycoprotein glucosyltransferase (UGT). UGT is a large glycoprotein whose C-terminus contains the catalytic activity. This catalytic C-terminal domain is highly homologous to Glycosyltransferase Family 8 (GT 8) and contains the DXD motif that coordinates donor sugar binding, characteristic for Family 8 glycosyltransferases. GT 8 proteins are retaining enzymes based on the relative anomeric stereochemistry of the substrate and product in the reaction catalyzed. The non-catalytic N-terminal portion of the human UTG1 (HUGT1) has been shown to monitor the protein folding status and activate its glucosyltransferase activity.
Pssm-ID: 133054 Cd Length: 248 Bit Score: 536.20 E-value: 4.11e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859593 1231 LNIFSVASGHLYERFLRIMMLSVLRNTKTPVKFWLLKNYLSPTFKEVIPHMAKEYGFRYELVQYRWPRWLRQQTERQRII 1310
Cdd:cd06432 1 INIFSVASGHLYERFLRIMMLSVMKNTKSPVKFWFIKNFLSPQFKEFLPEMAKEYGFEYELVTYKWPRWLHKQTEKQRII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859593 1311 WGYKILFLDVLFPLAVDKIIFVDADQIVRHDLKELRDFDLDGAPYGYTPFCDSRREMDGYRFWKTGYWASHLLRRKYHIS 1390
Cdd:cd06432 81 WGYKILFLDVLFPLNVDKVIFVDADQIVRTDLKELMDMDLKGAPYGYTPFCDSRKEMDGFRFWKQGYWKSHLRGRPYHIS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859593 1391 ALYVVDLKKFRRIGAGDRLRSQYQALSQDPNSLSNLDQDLPNNMIYQVAIKSLPQDWLWCETWCDDESKQRAKTIDLCNN 1470
Cdd:cd06432 161 ALYVVDLKRFRRIAAGDRLRGQYQQLSQDPNSLANLDQDLPNNMQHQVPIFSLPQEWLWCETWCSDESKKKAKTIDLCNN 240
|
....*...
gi 238859593 1471 PKTKESKL 1478
Cdd:cd06432 241 PLTKEPKL 248
|
|
| Thioredoxin_12 |
pfam18400 |
Thioredoxin-like domain; This is one of four TRXL(thioredoxin-like) domains found in ... |
45-226 |
1.76e-69 |
|
Thioredoxin-like domain; This is one of four TRXL(thioredoxin-like) domains found in UDP-glucose:glycoprotein glucosyltransferase (UGGT).
Pssm-ID: 465748 Cd Length: 187 Bit Score: 231.36 E-value: 1.76e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859593 45 ETPLLLEASEFMAEESNEKFWQFLETVQELAIY-KQTESDYSYYNLILKKAGQFLDNLHINLLKFAFSIRAYSPAIQMFQ 123
Cdd:pfam18400 1 ATPLLLEALETLAEENPDLFFPFLDALTNLDGEfADASTDEELYEAALKLASDHLSPLALSLFKLALSLRSASPRIEAFY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859593 124 QIAAD----EPPPDGCNAFVVIHKKHTCKINEIKKLLKKAA-SRTRPYLFKGDHKFPTNKEnLPVVILYAEMGTRTFSAF 198
Cdd:pfam18400 81 QIYAEsvsfEGAPPECDSWVDWGGEVYCDPEDLDALLKSEAsSRPQPELLPFDHVYPDSGS-SPVAILYADLGSPNFREF 159
|
170 180
....*....|....*....|....*...
gi 238859593 199 HKVLSEKAQNEEILYVLRHYIQKPSSRK 226
Cdd:pfam18400 160 HKYLSELAKDGKIRYVLRHVPPSGSESK 187
|
|
| Thioredoxin_14 |
pfam18402 |
Thioredoxin-like domain; This is the third out of four TRXL(thioredoxin-like) domains found in ... |
437-686 |
2.31e-63 |
|
Thioredoxin-like domain; This is the third out of four TRXL(thioredoxin-like) domains found in UDP-glucose:glycoprotein glucosyltransferase (UGGT).
Pssm-ID: 465750 Cd Length: 248 Bit Score: 216.38 E-value: 2.31e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859593 437 LDIRHS-----SIMWINDLENDDLYITWPTSCQKLLKPVFPGSVPSIRRNFHNLVLFIDPAQ-EYTLDFIKLADVFYSHE 510
Cdd:pfam18402 1 FDIRDRiegggVIIWLNDLEKDKRYSRWPSSLQELLRPTYPGQLPPIRKNLFNLVLVVDLSQpEDLLLLVETLQSFVQRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859593 511 VPLRIGFVFILNTDDEvdgandaGVALWRAFNYIAEEFDISEAFISIVHMYQKVKKDQNILTVDNVKSVLQNTFPHANIW 590
Cdd:pfam18402 81 IPVRFGLVPLVNSTED-------GLAQAKLFYYLLENYGLKAALSFLTASLYALAKKVLSPTKAIFSSALKERTLRPQAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859593 591 DILGI--HSKYDEERKAGASFYKMTGLGPL--PQALyNGEPFKHEEmNIKElkmAVLQRMMDASVYLQREVFLGTLNDRT 666
Cdd:pfam18402 154 SFDEVlkSEVYDERLKKAKEYLKRLGLDSLsgPVFV-NGVPLPRDE-NWLQ---ALSQRISEDLQLLQKAVYEGALTDDD 228
|
250 260
....*....|....*....|
gi 238859593 667 NAIDFLMDRNNVVPRINTLI 686
Cdd:pfam18402 229 DVPDFFYDLPNALPRRNPLI 248
|
|
| Thioredoxin_15 |
pfam18403 |
Thioredoxin-like domain; This is the fourth TRXL(thioredoxin-like) domain found in UDP-glucose: ... |
710-933 |
1.36e-57 |
|
Thioredoxin-like domain; This is the fourth TRXL(thioredoxin-like) domain found in UDP-glucose:glycoprotein glucosyltransferase (UGGT).
Pssm-ID: 465751 Cd Length: 205 Bit Score: 197.83 E-value: 1.36e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859593 710 TFFFLDSQdkSAVIAKNMYYLTqDDESIISAVTLWIIADFDKPSGRKLLFNALKHMKTSVHSRLGIIYNPTSKiNEENTA 789
Cdd:pfam18403 1 DLNKLYSE--HADLFDKMPYLE-ASSDKEDWATLWVVADLDSESGRKLLLSALEFRKSNPGVRLGIIHNPASP-SEASSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859593 790 ISRGILAAFLTQKNMFLRSFLGQLAKEEIATAIYSGdkiktfliegmdknafeKKYNTVGVNIFRTHQLFCQdVLKLRPG 869
Cdd:pfam18403 77 ISSALLAALLKLKNLDALEFLTKLLEEEEAAASESG-----------------KSSAEAAADYWKALQPFLR-VLGLKPG 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 238859593 870 EMGIVSNGRFLGPLDED--FYAEDFYLLEKITFSNLGEKIKGIVENMGINAN-NMSDFIMKVDALMS 933
Cdd:pfam18403 139 QNALVLNGRVVGPIPEDeeFSADDFELLLSYERSKRIEPVYKAIEELGLEDKiSDPDAVAKLTSLVA 205
|
|
| UDP-g_GGTase |
pfam06427 |
UDP-glucose:Glycoprotein Glucosyltransferase; This domain consists of 7 stranded ... |
1094-1199 |
5.26e-46 |
|
UDP-glucose:Glycoprotein Glucosyltransferase; This domain consists of 7 stranded beta-sandwiches found in UDP-glucose-glycoprotein glucosyltransferase-like proteins. UDP-g_GGTase is an important, central component of the QC system in the ER for checking that glycoproteins are folded correctly. This QC prevents incorrectly folded glycoproteins from leaving the ER.
Pssm-ID: 461910 Cd Length: 109 Bit Score: 160.73 E-value: 5.26e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859593 1094 GQCFDKVTEQPPRGLQFTLGTKNKPAVVDTIVMAHHGYFQLKANPGAWILRLHQGKSEDIYQIVGHEGTD-SQADLEDII 1172
Cdd:pfam06427 2 GHARDVTTGSPPRGLQLVLGTEKNPHVADTIVMANLGYFQLKANPGVWKLELREGRSSDIYEIESVGAEGwPSPGDEGTE 81
|
90 100
....*....|....*....|....*..
gi 238859593 1173 VVLNSFKSKILKVKVKKETDKIKEDIL 1199
Cdd:pfam06427 82 VALTSFEGLTLYPRLSRKPGMENEDVL 108
|
|
| Thioredoxin_13 |
pfam18401 |
Thioredoxin-like domain; This is the second out of four TRXL(thioredoxin-like) domains found ... |
296-424 |
1.10e-44 |
|
Thioredoxin-like domain; This is the second out of four TRXL(thioredoxin-like) domains found in UDP-glucose:glycoprotein glucosyltransferase (UGGT).
Pssm-ID: 465749 Cd Length: 136 Bit Score: 158.11 E-value: 1.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859593 296 ESNKQMMPLKVWELQDLSFQAASQIMSAPvyDSIKLMKDISQNFPIKARSLTRIAVNQHMREEIKENQKDLqvrfkIQPG 375
Cdd:pfam18401 1 EEVEDLKPLSVWELQDLGLQAAQFIMSSD--DPLDTLLKLSQDFPKYASSLARHNVSDELREEIEENQERL-----LPPG 73
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 238859593 376 DARLFINGLRVDMDVYDAFSILDMLKLEGKMMNGLRNLGINGEDMSKFL 424
Cdd:pfam18401 74 DNALWLNGLQLDERDIDPFSLLDILRRERKLINGLRKLGLSGSEAVDLL 122
|
|
| RfaJ |
COG1442 |
Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope ... |
1228-1447 |
3.03e-14 |
|
Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441051 [Multi-domain] Cd Length: 301 Bit Score: 75.40 E-value: 3.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859593 1228 KDVLNIFSVASGHlYERFLRIMMLSVLRNTK-TPVKFWLLKNYLSPTFKEVIPHMAKEYGFRYELVQY------------ 1294
Cdd:COG1442 3 KNTINIVFAIDDN-YLPGLGVSIASLLENNPdRPYDFHILTDGLSDENKERLEALAAKYNVSIEFIDVddellkdlpvsk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859593 1295 RWPR--WLRqqterqriiwgykiLFLDVLFPLAVDKIIFVDADQIVRHDLKELRDFDLDGAPYGytpfcdSRREMDGYRF 1372
Cdd:COG1442 82 HISKatYYR--------------LLIPELLPDDYDKVLYLDADTLVLGDLSELWDIDLGGNLLA------AVRDGTVTGS 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 238859593 1373 WKtgYWASHL---LRRKYHISALYVVDLKKFRRIGAGDRLrsqYQALSQDPNSLSNLDQD-LpnNMIYQVAIKSLPQDW 1447
Cdd:COG1442 142 QK--KRAKRLglpDDDGYFNSGVLLINLKKWREENITEKA---LEFLKENPDKLKYPDQDiL--NIVLGGKVKFLPPRY 213
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Glyco_transf_24 |
pfam18404 |
Glucosyltransferase 24; This is the catalytic domain found in UDP-glucose:glycoprotein ... |
1232-1498 |
0e+00 |
|
Glucosyltransferase 24; This is the catalytic domain found in UDP-glucose:glycoprotein glucosyltransferase (UGGT). This domain belongs to glucosyltransferase 24 family (GT24) A-type domain. The GT domain displays the expected glycosyltransferase type A (GT-A) fold.
Pssm-ID: 436473 Cd Length: 268 Bit Score: 583.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859593 1232 NIFSVASGHLYERFLRIMMLSVLRNTKTPVKFWLLKNYLSPTFKEVIPHMAKEYGFRYELVQYRWPRWLRQQTERQRIIW 1311
Cdd:pfam18404 2 NIFSVASGHLYERFLKIMMLSVRKNTKSPVKFWFIENFLSPSFKAFLPHLAKEYGFEYELVTYKWPSWLRKQTEKQRIIW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859593 1312 GYKILFLDVLFPLAVDKIIFVDADQIVRHDLKELRDFDLDGAPYGYTPFCDSRREMDGYRFWKTGYWASHLLRRKYHISA 1391
Cdd:pfam18404 82 GYKILFLDVLFPLDLDKVIFVDADQVVRTDLKELVDMDLEGAPYGYTPMCDSRKEMEGFRFWKQGYWKDHLRGRPYHISA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859593 1392 LYVVDLKKFRRIGAGDRLRSQYQALSQDPNSLSNLDQDLPNNMIYQVAIKSLPQDWLWCETWCDDESKQRAKTIDLCNNP 1471
Cdd:pfam18404 162 LYVVDLKRFRQMAAGDRLRSHYQQLSADPNSLANLDQDLPNNMQHQVPIFSLPQEWLWCETWCSDESLKKAKTIDLCNNP 241
|
250 260
....*....|....*....|....*..
gi 238859593 1472 KTKESKLKAAARIVPEWVEYDAEIRQL 1498
Cdd:pfam18404 242 LTKEPKLDRAKRIIPEWTDYDEEVAAL 268
|
|
| GT8_HUGT1_C_like |
cd06432 |
The C-terminal domain of HUGT1-like is highly homologous to the GT 8 family; C-terminal domain ... |
1231-1478 |
4.11e-180 |
|
The C-terminal domain of HUGT1-like is highly homologous to the GT 8 family; C-terminal domain of glycoprotein glucosyltransferase (UGT). UGT is a large glycoprotein whose C-terminus contains the catalytic activity. This catalytic C-terminal domain is highly homologous to Glycosyltransferase Family 8 (GT 8) and contains the DXD motif that coordinates donor sugar binding, characteristic for Family 8 glycosyltransferases. GT 8 proteins are retaining enzymes based on the relative anomeric stereochemistry of the substrate and product in the reaction catalyzed. The non-catalytic N-terminal portion of the human UTG1 (HUGT1) has been shown to monitor the protein folding status and activate its glucosyltransferase activity.
Pssm-ID: 133054 Cd Length: 248 Bit Score: 536.20 E-value: 4.11e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859593 1231 LNIFSVASGHLYERFLRIMMLSVLRNTKTPVKFWLLKNYLSPTFKEVIPHMAKEYGFRYELVQYRWPRWLRQQTERQRII 1310
Cdd:cd06432 1 INIFSVASGHLYERFLRIMMLSVMKNTKSPVKFWFIKNFLSPQFKEFLPEMAKEYGFEYELVTYKWPRWLHKQTEKQRII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859593 1311 WGYKILFLDVLFPLAVDKIIFVDADQIVRHDLKELRDFDLDGAPYGYTPFCDSRREMDGYRFWKTGYWASHLLRRKYHIS 1390
Cdd:cd06432 81 WGYKILFLDVLFPLNVDKVIFVDADQIVRTDLKELMDMDLKGAPYGYTPFCDSRKEMDGFRFWKQGYWKSHLRGRPYHIS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859593 1391 ALYVVDLKKFRRIGAGDRLRSQYQALSQDPNSLSNLDQDLPNNMIYQVAIKSLPQDWLWCETWCDDESKQRAKTIDLCNN 1470
Cdd:cd06432 161 ALYVVDLKRFRRIAAGDRLRGQYQQLSQDPNSLANLDQDLPNNMQHQVPIFSLPQEWLWCETWCSDESKKKAKTIDLCNN 240
|
....*...
gi 238859593 1471 PKTKESKL 1478
Cdd:cd06432 241 PLTKEPKL 248
|
|
| Glyco_transf_8 |
cd00505 |
Members of glycosyltransferase family 8 (GT-8) are involved in lipopolysaccharide biosynthesis ... |
1231-1472 |
2.49e-75 |
|
Members of glycosyltransferase family 8 (GT-8) are involved in lipopolysaccharide biosynthesis and glycogen synthesis; Members of this family are involved in lipopolysaccharide biosynthesis and glycogen synthesis. GT-8 comprises enzymes with a number of known activities: lipopolysaccharide galactosyltransferase, lipopolysaccharide glucosyltransferase 1, glycogenin glucosyltransferase, and N-acetylglucosaminyltransferase. GT-8 enzymes contains a conserved DXD motif which is essential in the coordination of a catalytic divalent cation, most commonly Mn2+.
Pssm-ID: 132996 [Multi-domain] Cd Length: 246 Bit Score: 250.44 E-value: 2.49e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859593 1231 LNIFSVASGHLYERFLRIMMLSVLRNTKTPVKFWLLKNYLSPTFKEVIPHMAKEYGFRYELVQYRWPRWLRQQTE-RQRI 1309
Cdd:cd00505 1 IAIVIVATGDEYLRGAIVLMKSVLRHRTKPLRFHVLTNPLSDTFKAALDNLRKLYNFNYELIPVDILDSVDSEHLkRPIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859593 1310 IWGYKILFLDVLFPlAVDKIIFVDADQIVRHDLKELRDFDLDGAPYGYTPFCDSRREMDGYRfwktgYWASHLLRRKYHI 1389
Cdd:cd00505 81 IVTLTKLHLPNLVP-DYDKILYVDADILVLTDIDELWDTPLGGQELAAAPDPGDRREGKYYR-----QKRSHLAGPDYFN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859593 1390 SALYVVDLKKFRR-IGAGDRLRSQYQALSqdpnSLSNLDQDLPNNMIYQVA--IKSLPQDWLWCETWCDDESK------Q 1460
Cdd:cd00505 155 SGVFVVNLSKERRnQLLKVALEKWLQSLS----SLSGGDQDLLNTFFKQVPfiVKSLPCIWNVRLTGCYRSLNcfkafvK 230
|
250
....*....|..
gi 238859593 1461 RAKTIDLCNNPK 1472
Cdd:cd00505 231 NAKVIHFNGPTK 242
|
|
| Thioredoxin_12 |
pfam18400 |
Thioredoxin-like domain; This is one of four TRXL(thioredoxin-like) domains found in ... |
45-226 |
1.76e-69 |
|
Thioredoxin-like domain; This is one of four TRXL(thioredoxin-like) domains found in UDP-glucose:glycoprotein glucosyltransferase (UGGT).
Pssm-ID: 465748 Cd Length: 187 Bit Score: 231.36 E-value: 1.76e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859593 45 ETPLLLEASEFMAEESNEKFWQFLETVQELAIY-KQTESDYSYYNLILKKAGQFLDNLHINLLKFAFSIRAYSPAIQMFQ 123
Cdd:pfam18400 1 ATPLLLEALETLAEENPDLFFPFLDALTNLDGEfADASTDEELYEAALKLASDHLSPLALSLFKLALSLRSASPRIEAFY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859593 124 QIAAD----EPPPDGCNAFVVIHKKHTCKINEIKKLLKKAA-SRTRPYLFKGDHKFPTNKEnLPVVILYAEMGTRTFSAF 198
Cdd:pfam18400 81 QIYAEsvsfEGAPPECDSWVDWGGEVYCDPEDLDALLKSEAsSRPQPELLPFDHVYPDSGS-SPVAILYADLGSPNFREF 159
|
170 180
....*....|....*....|....*...
gi 238859593 199 HKVLSEKAQNEEILYVLRHYIQKPSSRK 226
Cdd:pfam18400 160 HKYLSELAKDGKIRYVLRHVPPSGSESK 187
|
|
| Thioredoxin_14 |
pfam18402 |
Thioredoxin-like domain; This is the third out of four TRXL(thioredoxin-like) domains found in ... |
437-686 |
2.31e-63 |
|
Thioredoxin-like domain; This is the third out of four TRXL(thioredoxin-like) domains found in UDP-glucose:glycoprotein glucosyltransferase (UGGT).
Pssm-ID: 465750 Cd Length: 248 Bit Score: 216.38 E-value: 2.31e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859593 437 LDIRHS-----SIMWINDLENDDLYITWPTSCQKLLKPVFPGSVPSIRRNFHNLVLFIDPAQ-EYTLDFIKLADVFYSHE 510
Cdd:pfam18402 1 FDIRDRiegggVIIWLNDLEKDKRYSRWPSSLQELLRPTYPGQLPPIRKNLFNLVLVVDLSQpEDLLLLVETLQSFVQRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859593 511 VPLRIGFVFILNTDDEvdgandaGVALWRAFNYIAEEFDISEAFISIVHMYQKVKKDQNILTVDNVKSVLQNTFPHANIW 590
Cdd:pfam18402 81 IPVRFGLVPLVNSTED-------GLAQAKLFYYLLENYGLKAALSFLTASLYALAKKVLSPTKAIFSSALKERTLRPQAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859593 591 DILGI--HSKYDEERKAGASFYKMTGLGPL--PQALyNGEPFKHEEmNIKElkmAVLQRMMDASVYLQREVFLGTLNDRT 666
Cdd:pfam18402 154 SFDEVlkSEVYDERLKKAKEYLKRLGLDSLsgPVFV-NGVPLPRDE-NWLQ---ALSQRISEDLQLLQKAVYEGALTDDD 228
|
250 260
....*....|....*....|
gi 238859593 667 NAIDFLMDRNNVVPRINTLI 686
Cdd:pfam18402 229 DVPDFFYDLPNALPRRNPLI 248
|
|
| Thioredoxin_15 |
pfam18403 |
Thioredoxin-like domain; This is the fourth TRXL(thioredoxin-like) domain found in UDP-glucose: ... |
710-933 |
1.36e-57 |
|
Thioredoxin-like domain; This is the fourth TRXL(thioredoxin-like) domain found in UDP-glucose:glycoprotein glucosyltransferase (UGGT).
Pssm-ID: 465751 Cd Length: 205 Bit Score: 197.83 E-value: 1.36e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859593 710 TFFFLDSQdkSAVIAKNMYYLTqDDESIISAVTLWIIADFDKPSGRKLLFNALKHMKTSVHSRLGIIYNPTSKiNEENTA 789
Cdd:pfam18403 1 DLNKLYSE--HADLFDKMPYLE-ASSDKEDWATLWVVADLDSESGRKLLLSALEFRKSNPGVRLGIIHNPASP-SEASSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859593 790 ISRGILAAFLTQKNMFLRSFLGQLAKEEIATAIYSGdkiktfliegmdknafeKKYNTVGVNIFRTHQLFCQdVLKLRPG 869
Cdd:pfam18403 77 ISSALLAALLKLKNLDALEFLTKLLEEEEAAASESG-----------------KSSAEAAADYWKALQPFLR-VLGLKPG 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 238859593 870 EMGIVSNGRFLGPLDED--FYAEDFYLLEKITFSNLGEKIKGIVENMGINAN-NMSDFIMKVDALMS 933
Cdd:pfam18403 139 QNALVLNGRVVGPIPEDeeFSADDFELLLSYERSKRIEPVYKAIEELGLEDKiSDPDAVAKLTSLVA 205
|
|
| UDP-g_GGTase |
pfam06427 |
UDP-glucose:Glycoprotein Glucosyltransferase; This domain consists of 7 stranded ... |
1094-1199 |
5.26e-46 |
|
UDP-glucose:Glycoprotein Glucosyltransferase; This domain consists of 7 stranded beta-sandwiches found in UDP-glucose-glycoprotein glucosyltransferase-like proteins. UDP-g_GGTase is an important, central component of the QC system in the ER for checking that glycoproteins are folded correctly. This QC prevents incorrectly folded glycoproteins from leaving the ER.
Pssm-ID: 461910 Cd Length: 109 Bit Score: 160.73 E-value: 5.26e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859593 1094 GQCFDKVTEQPPRGLQFTLGTKNKPAVVDTIVMAHHGYFQLKANPGAWILRLHQGKSEDIYQIVGHEGTD-SQADLEDII 1172
Cdd:pfam06427 2 GHARDVTTGSPPRGLQLVLGTEKNPHVADTIVMANLGYFQLKANPGVWKLELREGRSSDIYEIESVGAEGwPSPGDEGTE 81
|
90 100
....*....|....*....|....*..
gi 238859593 1173 VVLNSFKSKILKVKVKKETDKIKEDIL 1199
Cdd:pfam06427 82 VALTSFEGLTLYPRLSRKPGMENEDVL 108
|
|
| Thioredoxin_13 |
pfam18401 |
Thioredoxin-like domain; This is the second out of four TRXL(thioredoxin-like) domains found ... |
296-424 |
1.10e-44 |
|
Thioredoxin-like domain; This is the second out of four TRXL(thioredoxin-like) domains found in UDP-glucose:glycoprotein glucosyltransferase (UGGT).
Pssm-ID: 465749 Cd Length: 136 Bit Score: 158.11 E-value: 1.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859593 296 ESNKQMMPLKVWELQDLSFQAASQIMSAPvyDSIKLMKDISQNFPIKARSLTRIAVNQHMREEIKENQKDLqvrfkIQPG 375
Cdd:pfam18401 1 EEVEDLKPLSVWELQDLGLQAAQFIMSSD--DPLDTLLKLSQDFPKYASSLARHNVSDELREEIEENQERL-----LPPG 73
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 238859593 376 DARLFINGLRVDMDVYDAFSILDMLKLEGKMMNGLRNLGINGEDMSKFL 424
Cdd:pfam18401 74 DNALWLNGLQLDERDIDPFSLLDILRRERKLINGLRKLGLSGSEAVDLL 122
|
|
| RfaJ |
COG1442 |
Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope ... |
1228-1447 |
3.03e-14 |
|
Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441051 [Multi-domain] Cd Length: 301 Bit Score: 75.40 E-value: 3.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859593 1228 KDVLNIFSVASGHlYERFLRIMMLSVLRNTK-TPVKFWLLKNYLSPTFKEVIPHMAKEYGFRYELVQY------------ 1294
Cdd:COG1442 3 KNTINIVFAIDDN-YLPGLGVSIASLLENNPdRPYDFHILTDGLSDENKERLEALAAKYNVSIEFIDVddellkdlpvsk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859593 1295 RWPR--WLRqqterqriiwgykiLFLDVLFPLAVDKIIFVDADQIVRHDLKELRDFDLDGAPYGytpfcdSRREMDGYRF 1372
Cdd:COG1442 82 HISKatYYR--------------LLIPELLPDDYDKVLYLDADTLVLGDLSELWDIDLGGNLLA------AVRDGTVTGS 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 238859593 1373 WKtgYWASHL---LRRKYHISALYVVDLKKFRRIGAGDRLrsqYQALSQDPNSLSNLDQD-LpnNMIYQVAIKSLPQDW 1447
Cdd:COG1442 142 QK--KRAKRLglpDDDGYFNSGVLLINLKKWREENITEKA---LEFLKENPDKLKYPDQDiL--NIVLGGKVKFLPPRY 213
|
|
| GT8_A4GalT_like |
cd04194 |
A4GalT_like proteins catalyze the addition of galactose or glucose residues to the ... |
1242-1447 |
1.15e-09 |
|
A4GalT_like proteins catalyze the addition of galactose or glucose residues to the lipooligosaccharide (LOS) or lipopolysaccharide (LPS) of the bacterial cell surface; The members of this family of glycosyltransferases catalyze the addition of galactose or glucose residues to the lipooligosaccharide (LOS) or lipopolysaccharide (LPS) of the bacterial cell surface. The enzymes exhibit broad substrate specificities. The known functions found in this family include: Alpha-1,4-galactosyltransferase, LOS-alpha-1,3-D-galactosyltransferase, UDP-glucose:(galactosyl) LPS alpha1,2-glucosyltransferase, UDP-galactose: (glucosyl) LPS alpha1,2-galactosyltransferase, and UDP-glucose:(glucosyl) LPS alpha1,2-glucosyltransferase. Alpha-1,4-galactosyltransferase from N. meningitidis adds an alpha-galactose from UDP-Gal (the donor) to a terminal lactose (the acceptor) of the LOS structure of outer membrane. LOSs are virulence factors that enable the organism to evade the immune system of host cells. In E. coli, the three alpha-1,2-glycosyltransferases, that are involved in the synthesis of the outer core region of the LPS, are all members of this family. The three enzymes share 40 % of sequence identity, but have different sugar donor or acceptor specificities, representing the structural diversity of LPS.
Pssm-ID: 133037 [Multi-domain] Cd Length: 248 Bit Score: 60.69 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859593 1242 YERFLRIMMLSVLRNT-KTPVKFWLLKNYLSPTFKEVIPHMAKEYGFRYELVQYRWPRwLRQQTERQRIIWG---YKiLF 1317
Cdd:cd04194 11 YAPYLAVTIKSILANNsKRDYDFYILNDDISEENKKKLKELLKKYNSSIEFIKIDNDD-FKFFPATTDHISYatyYR-LL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238859593 1318 LDVLFPlAVDKIIFVDADQIVRHDLKELRDFDLDGAPYG-----YTPFCDSRREMDGYRFWKTGYWASHLLrrkyhisal 1392
Cdd:cd04194 89 IPDLLP-DYDKVLYLDADIIVLGDLSELFDIDLGDNLLAavrdpFIEQEKKRKRRLGGYDDGSYFNSGVLL--------- 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 238859593 1393 yvVDLKKFRRIGAGDRLrsqYQALSQDPNSLSNLDQD-LpnNMIYQVAIKSLPQDW 1447
Cdd:cd04194 159 --INLKKWREENITEKL---LELIKEYGGRLIYPDQDiL--NAVLKDKILYLPPRY 207
|
|
| |
