|
Name |
Accession |
Description |
Interval |
E-value |
| Glyco_hydro_31 |
pfam01055 |
Glycosyl hydrolases family 31; Glycosyl hydrolases are key enzymes of carbohydrate metabolism. ... |
1-433 |
3.26e-157 |
|
Glycosyl hydrolases family 31; Glycosyl hydrolases are key enzymes of carbohydrate metabolism. Family 31 comprises of enzymes that are, or similar to, alpha- galactosidases.
Pssm-ID: 460044 [Multi-domain] Cd Length: 443 Bit Score: 478.59 E-value: 3.26e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 1 MNRKLDFTL-SANFQNLSLLIEQMKKNGMRFILILDPAISGNETQYLPFIRGQENNVFIKWPDTNDIVWGkvWPDlpnvi 79
Cdd:pfam01055 69 MDGYRDFTWdPERFPDPKGMVDELHAKGQKLVVIIDPGIKKVDPGYPPYDEGLEKGYFVKNPDGSLYVGG--WPG----- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 80 vdgsldhetqvklyraYVAFPDFFRNSTAAWWKKEIEELYANprepeksLKFDGLWIDMNEPSNFVdGSVRGCSNEMLNN 159
Cdd:pfam01055 142 ----------------MSAFPDFTNPEARDWWADQLFKFLLD-------MGVDGIWNDMNEPSVFC-GSGPEDTVAKDND 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 160 PPYmpylesrdkglssktlcmesqqilpdssPVEHYNVHNLYGWSQTRPTYEAVQEVTG-QRGVIITRSTFPSSGRWGGH 238
Cdd:pfam01055 198 PGG----------------------------GVEHYDVHNLYGLLMAKATYEGLREKRPnKRPFVLTRSGFAGSQRYAAH 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 239 RLGNNTAAWDQLGKSIIGMMEFSLFGIPYTGADICGFFGDAEYEMCVRWMQLGAFYPFSRNHNNIGTRRQDPVAWNSTFE 318
Cdd:pfam01055 250 WSGDNTSTWEHLRFSIPGGLSLGLSGIPFWGADIGGFFNPTTPELYVRWYQLGAFSPFFRNHSSIDTRRREPWLFGEEVE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 319 MLSRKVLETRYTLLPYLYTLMHKAHVEGSTVVRPLLHEFTDDRTTWDIDRQFMLGPAILISPVLETSTFEISAYFPRARW 398
Cdd:pfam01055 330 EIIRKAIRLRYRLLPYLYTLFYEAHETGLPVMRPLFLEFPDDPNTFDIDDQFMFGPSLLVAPVLEEGATSVDVYLPGGRW 409
|
410 420 430
....*....|....*....|....*....|....*
gi 767949047 399 YDYsTGTSSTSTGQRKILKAPLDHINLHVRGGYIL 433
Cdd:pfam01055 410 YDF-WTGERYEGGGTVPVTAPLDRIPLFVRGGSII 443
|
|
| GH31_MGAM_SI_GAA |
cd06602 |
maltase-glucoamylase, sucrase-isomaltase, lysosomal acid alpha-glucosidase; This subgroup ... |
1-343 |
2.37e-154 |
|
maltase-glucoamylase, sucrase-isomaltase, lysosomal acid alpha-glucosidase; This subgroup includes the following three closely related glycosyl hydrolase family 31 (GH31) enzymes: maltase-glucoamylase (MGAM), sucrase-isomaltase (SI), and lysosomal acid alpha-glucosidase (GAA), also known as acid-maltase. MGAM is one of the two enzymes responsible for catalyzing the last glucose-releasing step in starch digestion. SI is implicated in the digestion of dietary starch and major disaccharides such as sucrose and isomaltose, while GAA degrades glycogen in the lysosome, cleaving both alpha-1,4 and alpha-1,6 glucosidic linkages. MGAM and SI are anchored to small-intestinal brush-border epithelial cells. The absence of SI from the brush border membrane or its malfunction is associated with malabsorption disorders such as congenital sucrase-isomaltase deficiency (CSID). The domain architectures of MGAM and SI include two tandem GH31 catalytic domains, an N-terminal domain found near the membrane-bound end, and a C-terminal luminal domain. Both of the tandem GH31 domains of MGAM and SI are included in this family. The domain architecture of GAA includes an N-terminal TFF (trefoil factor family) domain in addition to the GH31 catalytic domain. Deficient GAA expression causes Pompe disease, an autosomal recessive genetic disorder also known as glycogen storage disease type II (GSDII).
Pssm-ID: 269888 Cd Length: 367 Bit Score: 467.76 E-value: 2.37e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 1 MNRKLDFTLS-ANFQNLSLLIEQMKKNGMRFILILDPAISGNETQ-YLPFIRGQENNVFIKWPDTNDIVwGKVWPDlpnv 78
Cdd:cd06602 50 MDRYRDFTLDpVNFPGLPAFVDDLHANGQHYVPILDPGISANESGgYPPYDRGLEMDVFIKNDDGSPYV-GKVWPG---- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 79 ivdgsldhetqvklyraYVAFPDFFRNSTAAWWKKEIEELYanprepeKSLKFDGLWIDMNEPSNFVDGSV------RGC 152
Cdd:cd06602 125 -----------------YTVFPDFTNPNTQEWWTEEIKDFH-------DQVPFDGLWIDMNEPSNFCTGSCgnspnaPGC 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 153 SNEMLNNPPYMPYLeSRDKGLSSKTLCMESQQilpdSSPVEHYNVHNLYGWSQTRPTYEAVQEV-TGQRGVIITRSTFPS 231
Cdd:cd06602 181 PDNKLNNPPYVPNN-LGGGSLSDKTICMDAVH----YDGGLHYDVHNLYGLSEAIATYKALKEIfPGKRPFIISRSTFPG 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 232 SGRWGGHRLGNNTAAWDQLGKSIIGMMEFSLFGIPYTGADICGFFGDAEYEMCVRWMQLGAFYPFSRNHNNIGTRRQDPV 311
Cdd:cd06602 256 SGKYAGHWLGDNYSTWEDMRYSIPGMLEFNLFGIPMVGADICGFNGNTTEELCARWMQLGAFYPFSRNHNDIGAIDQEPY 335
|
330 340 350
....*....|....*....|....*....|..
gi 767949047 312 AWNSTFEMLSRKVLETRYTLLPYLYTLMHKAH 343
Cdd:cd06602 336 VWGPSVADASRKALLIRYSLLPYLYTLFYRAH 367
|
|
| GH31_GANC_GANAB_alpha |
cd06603 |
neutral alpha-glucosidase C, neutral alpha-glucosidase AB; This subgroup includes the closely ... |
10-473 |
1.46e-91 |
|
neutral alpha-glucosidase C, neutral alpha-glucosidase AB; This subgroup includes the closely related glycosyl hydrolase family 31 (GH31) isozymes, neutral alpha-glucosidase C (GANC) and the alpha subunit of heterodimeric neutral alpha-glucosidase AB (GANAB). Initially distinguished on the basis of differences in electrophoretic mobility in starch gel, GANC and GANAB have been shown to have other differences, including those of substrate specificity. GANC and GANAB are key enzymes in glycogen metabolism that hydrolyze terminal, non-reducing 1,4-linked alpha-D-glucose residues from glycogen in the endoplasmic reticulum. The GANC/GANAB family includes the alpha-glucosidase II (ModA) from Dictyostelium discoideum as well as the alpha-glucosidase II (GLS2, or ROT2 - Reversal of TOR2 lethality protein 2) from Saccharomyces cerevisiae.
Pssm-ID: 269889 Cd Length: 467 Bit Score: 303.67 E-value: 1.46e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 10 SANFQNLSLLIEQMKKNGMRFILILDPAISgNETQYLPFIRGQENNVFIKWPDTNDIVwGKVWPdlpnvivdGSldhetq 89
Cdd:cd06603 60 KKKFPDPKKMQEKLASKGRKLVTIVDPHIK-RDDDYFVYKEAKEKDYFVKDSDGKDFE-GWCWP--------GS------ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 90 vklyrayVAFPDFFRNSTAAWWKKeieeLYANPREPEKSLKFdGLWIDMNEPSNFvdgsvrgcsnemlNNPPY-MPyles 168
Cdd:cd06603 124 -------SSWPDFLNPEVRDWWAS----LFSYDKYKGSTENL-YIWNDMNEPSVF-------------NGPEItMP---- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 169 RDkglssktlCMESQQilpdsspVEHYNVHNLYGWSQTRPTYEAV--QEVTGQRGVIITRSTFPSSGRWGGHRLGNNTAA 246
Cdd:cd06603 175 KD--------AIHYGG-------VEHRDVHNIYGLYMHMATFEGLlkRSNGKKRPFVLTRSFFAGSQRYGAVWTGDNMAT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 247 WDQLGKSIIGMMEFSLFGIPYTGADICGFFGDAEYEMCVRWMQLGAFYPFSRNHNNIGTRRQDPvaWNSTFEMLS--RKV 324
Cdd:cd06603 240 WEHLKISIPMLLSLSIAGIPFVGADVGGFFGNPDEELLVRWYQAGAFYPFFRAHAHIDTKRREP--WLFGEETTEiiREA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 325 LETRYTLLPYLYTLMHKAHVEGSTVVRPLLHEFTDDRTTWDIDRQFMLGPAILISPVLETSTFEISAYFPR-ARWYDYsT 403
Cdd:cd06603 318 IRLRYRLLPYWYTLFYEASRTGLPIMRPLWYEFPEDESTFDIDDQFMLGDSLLVKPVVEEGATSVTVYLPGgEVWYDY-F 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767949047 404 GTSSTSTGQRKILKAPLDHINLHVRGGYILP-WQEPAMNTHSSRQNFMGLIVALDDNGTAEGQVFWDDGQS 473
Cdd:cd06603 397 TGQRVTGGGTKTVPVPLDSIPVFQRGGSIIPrKERVRRSSKLMRNDPYTLVVALDENGEAEGELYLDDGES 467
|
|
| GH31_glucosidase_II_MalA |
cd06604 |
Alpha-glucosidase II-like; Alpha-glucosidase II (alpha-D-glucoside glucohydrolase) is a ... |
1-346 |
9.86e-76 |
|
Alpha-glucosidase II-like; Alpha-glucosidase II (alpha-D-glucoside glucohydrolase) is a glycosyl hydrolase family 31 (GH31) enzyme, found in bacteria and plants, which has exo-alpha-1,4-glucosidase and oligo-1,6-glucosidase activities. Alpha-glucosidase II has been characterized in Bacillus thermoamyloliquefaciens where it forms a homohexamer. This subgroup also includes the MalA alpha-glucosidase from Sulfolobus solfataricus and the AglA alpha-glucosidase from Picrophilus torridus. MalA is part of the carbohydrate-metabolizing machinery that allows this organism to utilize carbohydrates, such as maltose, as the sole carbon and energy source.
Pssm-ID: 269890 [Multi-domain] Cd Length: 339 Bit Score: 254.74 E-value: 9.86e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 1 MNRKLDFTLS-ANFQNLSLLIEQMKKNGMRFILILDPAISGNEtQYLPFIRGQENNVFIKWPDtNDIVWGKVWPDLpnvi 79
Cdd:cd06604 50 MDGYRVFTWDkERFPDPKELIKELHEQGFRLVTIVDPGVKVDP-GYEVYEEGLENDYFVKDPD-GELYVGKVWPGK---- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 80 vdgsldhetqvklyrayVAFPDFFRNSTAAWWKKEIEELYanprepekSLKFDGLWIDMNEPSNFVDgsvrgcsnemlNN 159
Cdd:cd06604 124 -----------------SVFPDFTNPEVREWWGDLYKELV--------DLGVDGIWNDMNEPAVFNA-----------PG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 160 PPYMPyLESRDKGlssktlcmesqqilpDSSPVEHYNVHNLYGWSQTRPTYEAVQEV-TGQRGVIITRSTFPSSGRWGGH 238
Cdd:cd06604 168 GTTMP-LDAVHRL---------------DGGKITHEEVHNLYGLLMARATYEGLRRLrPNKRPFVLSRAGYAGIQRYAAI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 239 RLGNNTAAWDQLGKSIIGMMEFSLFGIPYTGADICGFFGDAEYEMCVRWMQLGAFYPFSRNHNNIGTRRQDPVAWNSTFE 318
Cdd:cd06604 232 WTGDNSSSWEHLRLSIPMLLNLGLSGVPFVGADIGGFAGDPSPELLARWYQLGAFFPFFRNHSAKGTRDQEPWAFGEEVE 311
|
330 340
....*....|....*....|....*...
gi 767949047 319 MLSRKVLETRYTLLPYLYTLMHKAHVEG 346
Cdd:cd06604 312 EIARKAIELRYRLLPYLYTLFYEAHETG 339
|
|
| YicI |
COG1501 |
Alpha-glucosidase/xylosidase, GH31 family [Carbohydrate transport and metabolism]; |
19-474 |
1.60e-58 |
|
Alpha-glucosidase/xylosidase, GH31 family [Carbohydrate transport and metabolism];
Pssm-ID: 441110 [Multi-domain] Cd Length: 609 Bit Score: 213.48 E-value: 1.60e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 19 LIEQMKKNGMRFILILDPAISgneTQYLPFIRGQENnvFIKWPdtNDIVW-GKVWPDlpnvivdgsldhetqvklyraYV 97
Cdd:COG1501 233 MVKELHDRGVKLVLWINPYVA---PDSAIFAEGMAN--FVKIA--SGTVFvGKMWPG---------------------TT 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 98 AFPDFFRNSTAAWWKKEIEELYAnprepekSLKFDGLWIDMNEPsnfvdgsvrgcsnemlnnppyMPylesrdkglsskt 177
Cdd:COG1501 285 GLLDFTRPDAREWFWAGLEKELL-------SIGVDGIKLDMNEG---------------------WP------------- 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 178 lcmESQQILPDSSPVEhynVHNLYGWSQTRPTYEAVQEVTGQRGVIITRSTFPSSGRWGGHRLGNNTAAWDQLGKSIIGM 257
Cdd:COG1501 324 ---TDVATFPSNVPQQ---MRNLYGLLEAKATFEGFRTSRNNRTFILTRSGFAGGQRYPVIWTGDNTSSWESLEDQLTQG 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 258 MEFSLFGIPYTGADICGFFGDAEYEMCVRWMQLGAFYPFSRNHNNigTRRQDPVAWNSTFEMLSRKVLETRYTLLPYLYT 337
Cdd:COG1501 398 LNLSLSGVPFWTPDIGGFFGSPSRELWIRWFQVGAFSPFARIHGW--ASSTEPWFFDEEAKQIVKEYAQLRYRLLPYIYS 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 338 LMHKAHVEGSTVVRPLLHEFTDDRTTWDIDRQFMLGPAILISPVLeTSTFEISAYFPRARWYDYSTGTSSTSTGQRKIlK 417
Cdd:COG1501 476 LFAKASTDGTPVIRPLFLEFPDDPTTRFIDDQYMFGEYLLVAPIF-AGTESRLVYLPKGKWYDFWTGELIEGGQWITV-T 553
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 767949047 418 APLDHINLHVRGGYILPWQePAMNtHSSRQNFMGLIVALDDNGTAEGQVFWDDGQSI 474
Cdd:COG1501 554 APLDRLPLYVRDGSIIPLG-PVSL-RPSMQKIDGIELRVYGSGETAYTLYDDDGETV 608
|
|
| GH31_MGAM-like |
cd06600 |
maltase-glucoamylase (MGAM)-like; This family includes the following closely related glycosyl ... |
1-331 |
5.75e-58 |
|
maltase-glucoamylase (MGAM)-like; This family includes the following closely related glycosyl hydrolase family 31 (GH31) enzymes: maltase-glucoamylase (MGAM), sucrase-isomaltase (SI), lysosomal acid alpha-glucosidase (GAA), neutral alpha-glucosidase C (GANC), the alpha subunit of neutral alpha-glucosidase AB (GANAB), and alpha-glucosidase II. MGAM is one of the two enzymes responsible for catalyzing the last glucose-releasing step in starch digestion. SI is implicated in the digestion of dietary starch and major disaccharides such as sucrose and isomaltose, while GAA degrades glycogen in the lysosome, cleaving both alpha-1,4 and alpha-1,6 glucosidic linkages. MGAM and SI are anchored to small-intestinal brush-border epithelial cells. The absence of SI from the brush border membrane or its malfunction is associated with malabsorption disorders such as congenital sucrase-isomaltase deficiency (CSID). The domain architectures of MGAM and SI include two tandem GH31 catalytic domains, an N-terminal domain found near the membrane-bound end and a C-terminal luminal domain. Both of the tandem GH31 domains of MGAM and SI are included in this family. The domain architecture of GAA includes an N-terminal TFF (trefoil factor family) domain in addition to the GH31 catalytic domain. Deficient GAA expression causes Pompe disease, an autosomal recessive genetic disorder also known as glycogen storage disease type II (GSDII). GANC and GANAB are key enzymes in glycogen metabolism that hydrolyze terminal, non-reducing 1,4-linked alpha-D-glucose residues from glycogen in the endoplasmic reticulum. Alpha-glucosidase II is a GH31 enzyme, found in bacteria and plants, which has exo-alpha-1,4-glucosidase and oligo-1,6-glucosidase activities. Alpha-glucosidase II has been characterized in Bacillus thermoamyloliquefaciens where it forms a homohexamer. This family also includes the MalA alpha-glucosidase from Sulfolobus solfataricus and the AglA alpha-glucosidase from Picrophilus torridus. MalA is part of the carbohydrate-metabolizing machinery that allows this organism to utilize carbohydrates, such as maltose, as the sole carbon and energy source. The MGAM-like family corresponds to subgroup 1 in the Ernst et al classification of GH31 enzymes.
Pssm-ID: 269886 [Multi-domain] Cd Length: 256 Bit Score: 200.80 E-value: 5.75e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 1 MNRKLDFTL-SANFQNLSLLIEQMKKNGMRFILILDPAIsgnetqylpfirgqennvfikwpdtndivwgkvwpdlpnvi 79
Cdd:cd06600 50 MDSYKDFTWdPVRFPEPKKFVDELHKNGQKLVTIVDPGI----------------------------------------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 80 vdgsldhetqvklyrayvafpdffrnsTAAWWKKEIEElyanprePEKSLKFDGLWIDMNEPSNFvdgsvrgcsnemlnn 159
Cdd:cd06600 89 ---------------------------TREWWAGLISE-------FLYSQGIDGIWIDMNEPSNF--------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 160 ppympylesrdkglssktlcmesqqilpdsspvehYNVHNLYGWSQTRPTYEAVQEVTGQRGVIITRSTFPSSGRWGGHR 239
Cdd:cd06600 120 -----------------------------------YKVHNLYGFYEAMATAEGLRTSHNERPFILSRSTFAGSQKYAAHW 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 240 LGNNTAAWDQLGKSIIGMMEFSLFGIPYTGADICGFFGDAEYEMCVRWMQLGAFYPFSRNHNNIGTRRQDPVAWNSTFEM 319
Cdd:cd06600 165 TGDNTASWDDLKLSIPLVLGLSLSGIPFVGADIGGFAGDTSEELLVRWYQLGAFYPFSRSHKATDTKDQEPVLFPEYYKE 244
|
330
....*....|..
gi 767949047 320 LSRKVLETRYTL 331
Cdd:cd06600 245 SVREILELRYKL 256
|
|
| PLN02763 |
PLN02763 |
hydrolase, hydrolyzing O-glycosyl compounds |
1-491 |
2.97e-55 |
|
hydrolase, hydrolyzing O-glycosyl compounds
Pssm-ID: 215408 [Multi-domain] Cd Length: 978 Bit Score: 209.75 E-value: 2.97e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 1 MNRKLDFTLSAN-FQNLSLLIEQMKKNGMRFILILDPAISgNETQYLPFIRGQENNVFIKWPDTNDIVwGKVWPDLpnvi 79
Cdd:PLN02763 227 MDGFRCFTFDKErFPDPKGLADDLHSIGFKAIWMLDPGIK-AEEGYFVYDSGCENDVWIQTADGKPFV-GEVWPGP---- 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 80 vdgsldhetqvklyrayVAFPDFFRNSTAAWWKKEIEELYANprepekslKFDGLWIDMNEPSNFvdgsvRGCSNEMLNN 159
Cdd:PLN02763 301 -----------------CVFPDFTNKKTRSWWANLVKDFVSN--------GVDGIWNDMNEPAVF-----KTVTKTMPET 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 160 PPYMPYLESrdKGLSSKTlcmesqqilpdsspveHYnvHNLYGWSQTRPTYEAVQEV-TGQRGVIITRSTFPSSGRWGGH 238
Cdd:PLN02763 351 NIHRGDEEL--GGVQNHS----------------HY--HNVYGMLMARSTYEGMLLAnKNKRPFVLTRAGFIGSQRYAAT 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 239 RLGNNTAAWDQLGKSIIGMMEFSLFGIPYTGADICGFFGDAEYEMCVRWMQLGAFYPFSRNHNNIGTRRQDPVAWNSTFE 318
Cdd:PLN02763 411 WTGDNLSNWEHLHMSIPMVLQLGLSGQPLSGPDIGGFAGDATPKLFGRWMGVGAMFPFARGHSEQGTIDHEPWSFGEECE 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 319 MLSRKVLETRYTLLPYLYTLMHKAHVEGSTVVRPLLHEFTDDRTTWDIDRQFMLGPA-ILISPVLETSTFEISAYFPRAR 397
Cdd:PLN02763 491 EVCRLALKRRYRLLPHFYTLFYKAHTTGLPVMTPIFFADPKDPSLRKVENSFLLGPLlISASTLPDQGSDNLQHVLPKGI 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 398 W--YDYSTgtsststgqrkilkaplDHINL---HVRGGYILPWQEPAMNT-HSSRQNFMGLIVALDDNGTAEGQVFWDDG 471
Cdd:PLN02763 571 WqrFDFDD-----------------SHPDLpllYLQGGSIIPLGPPIQHVgEASLSDDLTLLIALDENGKAEGVLYEDDG 633
|
490 500
....*....|....*....|
gi 767949047 472 QSIDtYENGNYFLANFIAAQ 491
Cdd:PLN02763 634 DGFG-YTKGDYLLTHYEAEL 652
|
|
| GH31 |
cd06589 |
glycosyl hydrolase family 31 (GH31); GH31 enzymes occur in prokaryotes, eukaryotes, and ... |
108-325 |
7.07e-30 |
|
glycosyl hydrolase family 31 (GH31); GH31 enzymes occur in prokaryotes, eukaryotes, and archaea with a wide range of hydrolytic activities, including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-xylosidase, 6-alpha-glucosyltransferase, 3-alpha-isomaltosyltransferase and alpha-1,4-glucan lyase. All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. In most cases, the pyranose moiety recognized in subsite -1 of the substrate binding site is an alpha-D-glucose, though some GH31 family members show a preference for alpha-D-xylose. Several GH31 enzymes can accommodate both glucose and xylose and different levels of discrimination between the two have been observed. Most characterized GH31 enzymes are alpha-glucosidases. In mammals, GH31 members with alpha-glucosidase activity are implicated in at least three distinct biological processes. The lysosomal acid alpha-glucosidase (GAA) is essential for glycogen degradation and a deficiency or malfunction of this enzyme causes glycogen storage disease II, also known as Pompe disease. In the endoplasmic reticulum, alpha-glucosidase II catalyzes the second step in the N-linked oligosaccharide processing pathway that constitutes part of the quality control system for glycoprotein folding and maturation. The intestinal enzymes sucrase-isomaltase (SI) and maltase-glucoamylase (MGAM) play key roles in the final stage of carbohydrate digestion, making alpha-glucosidase inhibitors useful in the treatment of type 2 diabetes. GH31 alpha-glycosidases are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively.
Pssm-ID: 269876 [Multi-domain] Cd Length: 265 Bit Score: 120.15 E-value: 7.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 108 AAWWKKEIEELYAnprepekSLKFDGLWIDMNEPSNFVDGSVRGCSNemlnnppympylesrdkglssktlcmesqqilp 187
Cdd:cd06589 92 RDWWWENIKKLLL-------EQGVDGWWTDMGEPLPFDDATFHNGGK--------------------------------- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 188 dsspveHYNVHNLYGWSQTRPTYEAVQEVTG-QRGVIITRSTFPSSGRWGGHRLGNNTAAWDQLGKSIIGMMEFSLFGIP 266
Cdd:cd06589 132 ------AQKIHNAYPLNMAEATYEGQKKTFPnKRPFILSRSGYAGAQRYPAIWSGDNTTTWDSLAFQIRAGLSASLSGVG 205
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 267 YTGADICGF-FGDAEYEMCVRWMQLGAFYPFSRNHNNIGTRRQDPVAWNSTFEMLSRKVL 325
Cdd:cd06589 206 YWGHDIGGFtGGDPDKELYTRWVQFGAFSPIFRLHGDNSPRDKEPWVYGEEALAIFRKYL 265
|
|
| GH31_NET37 |
cd06592 |
glucosidase NET37; NET37 (also known as KIAA1161) is a human lamina-associated nuclear ... |
6-398 |
3.72e-24 |
|
glucosidase NET37; NET37 (also known as KIAA1161) is a human lamina-associated nuclear envelope transmembrane protein. A member of the glycosyl hydrolase family 31 (GH31) , it has been shown to be required for myogenic differentiation of C2C12 cells. Related proteins are found in eukaryotes and prokaryotes. Enzymes of the GH31 family possess a wide range of different hydrolytic activities including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-xylosidase, 6-alpha-glucosyltransferase, 3-alpha-isomaltosyltransferase and alpha-1,4-glucan lyase. All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein.
Pssm-ID: 269878 [Multi-domain] Cd Length: 364 Bit Score: 105.76 E-value: 3.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 6 DFTLSAN-FQNLSLLIEQMKKNGMRFILILDPAISgNETQylPFIRGQENNVFIKWPDTNDIVWGKVWPdlpnvivdgsl 84
Cdd:cd06592 49 DFEFDPEkFPDPKGMIDKLHEMGFRVTLWVHPFIN-PDSP--NFRELRDKGYLVKEDSGGPPLIVKWWN----------- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 85 dhetqvklyrAYVAFPDFFRNSTAAWWKKEIEELyanprepEKSLKFDGLWIDmnepsnFVDGSvrgcsnemlnnppYMP 164
Cdd:cd06592 115 ----------GYGAVLDFTNPEARDWFKERLREL-------QEDYGIDGFKFD------AGEAS-------------YLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 165 YlesrdkglssktlcmESQQILPDSSPVEHynvHNLYGwsQTRPTYEAVQEVT----GQRGVIITRSTFPSSgRWGGhrl 240
Cdd:cd06592 159 A---------------DPATFPSGLNPNEY---TTLYA--ELAAEFGLLNEVRsgwkSQGLPLFVRMSDKDS-HWGY--- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 241 gnntaaWDQLGKSIIGMMEFSLFGIPYTGADICGffGDAEY------EMCVRWMQLGAFYP---FSrnhnnigtrrqdPV 311
Cdd:cd06592 215 ------WNGLRSLIPTALTQGLLGYPFVLPDMIG--GNAYGnfppdkELYIRWLQLSAFMPamqFS------------VA 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 312 AWNSTFEM---LSRKVLETRYTLLPYLYTLMHKAHVEGSTVVRPLLHEFTDDRTTWDIDRQFMLGPAILISPVLETSTFE 388
Cdd:cd06592 275 PWRNYDEEvvdIARKLAKLREKLLPYIYELAAEAVDTGEPIIRPLWWIAPEDEEALTIDDQFLLGDDILVAPVLEKGARS 354
|
410
....*....|
gi 767949047 389 ISAYFPRARW 398
Cdd:cd06592 355 RDVYLPKGRW 364
|
|
| GH31_transferase_CtsZ |
cd06598 |
CtsZ (cyclic tetrasaccharide-synthesizing enzyme Z)-like; CtsZ is a bacterial ... |
101-341 |
1.08e-23 |
|
CtsZ (cyclic tetrasaccharide-synthesizing enzyme Z)-like; CtsZ is a bacterial 6-alpha-glucosyltransferase, first identified in Arthrobacter globiformis, that produces cyclic tetrasaccharides together with a closely related enzyme CtsY. CtsZ and CtsY both have a glycosyl hydrolase family 31 (GH31) catalytic domain; CtsY belongs to a different subfamily. All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein.
Pssm-ID: 269884 Cd Length: 332 Bit Score: 103.92 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 101 DFFRNSTAAWWkkeieelYANPREPeKSLKFDGLWIDMNEPSNFvdgsvrgcsnemlnnPPYMPYLesrdKGlssktlcm 180
Cdd:cd06598 136 DWSDPEARAWW-------HDRYKDL-IDMGVAGWWTDLGEPEMH---------------PPDMVHA----DG-------- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 181 esqqilpdsspvEHYNVHNLYG--WSQTrpTYEA-VQEVTGQRGVIITRSTFPSSGRWG-GHRLGNNTAAWDQLGKSIIG 256
Cdd:cd06598 181 ------------DAADVHNIYNllWAKS--IYDGyQRNFPEQRPFIMSRSGTAGSQRYGvIPWSGDIGRTWGGLASQINL 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 257 MMEFSLFGIPYTGADICGFFGDAEY--EMCVRWMQLGAFYPFSRNHNNiGTRRQDPVAWNSTFEMLSRKVLETRYTLLPY 334
Cdd:cd06598 247 QLHMSLSGIDYYGSDIGGFARGETLdpELYTRWFQYGAFDPPVRPHGQ-NLCNPETAPDREGTKAINRENIKLRYQLLPY 325
|
....*..
gi 767949047 335 LYTLMHK 341
Cdd:cd06598 326 YYSLAYR 332
|
|
| PRK10426 |
PRK10426 |
alpha-glucosidase; Provisional |
186-398 |
1.99e-23 |
|
alpha-glucosidase; Provisional
Pssm-ID: 236691 [Multi-domain] Cd Length: 635 Bit Score: 107.00 E-value: 1.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 186 LPDSSPVEHYnvHNLYG--WSQTrpTYEAVQEvTGQRG--VIITRSTFPSSGR-----WGGHRLgnntAAW---DQLGKS 253
Cdd:PRK10426 371 LHNGVSAEIM--HNAWPalWAKC--NYEALEE-TGKLGeiLFFMRAGYTGSQKystlfWAGDQN----VDWsldDGLASV 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 254 IIGMMEFSLFGIPYTGADICGFFGDAEY----EMCVRWMQLGAFYPFSRNHNniGTRRQDPVAWNSTFEMLSR--KVLET 327
Cdd:PRK10426 442 VPAALSLGMSGHGLHHSDIGGYTTLFGMkrtkELLLRWCEFSAFTPVMRTHE--GNRPGDNWQFDSDAETIAHfaRMTRV 519
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767949047 328 RYTLLPYLYTLMHKAHVEGSTVVRPLLHEFTDDRTTWDIDRQFMLGPAILISPVLETSTFEISAYFPRARW 398
Cdd:PRK10426 520 FTTLKPYLKELVAEAAKTGLPVMRPLFLHYEDDAATYTLKYQYLLGRDLLVAPVHEEGRTDWTVYLPEDKW 590
|
|
| GH31_CPE1046 |
cd06596 |
Clostridium CPE1046-like; CPE1046 is an uncharacterized Clostridium perfringens protein with a ... |
210-401 |
8.54e-22 |
|
Clostridium CPE1046-like; CPE1046 is an uncharacterized Clostridium perfringens protein with a glycosyl hydrolase family 31 (GH31) domain. The domain architecture of CPE1046 and its orthologs includes a C-terminal fibronectin type 3 (FN3) domain and a coagulation factor 5/8 type C domain in addition to the GH31 domain. Enzymes of the GH31 family possess a wide range of different hydrolytic activities including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-xylosidase, 6-alpha-glucosyltransferase, 3-alpha-isomaltosyltransferase and alpha-1,4-glucan lyase. All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein.
Pssm-ID: 269882 Cd Length: 334 Bit Score: 98.19 E-value: 8.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 210 YEAVQEVTGQRGVIITRSTFPSSGRWGGHRLGNNTAAWDQLGKSIIGMMEFSLFGIPYTGADICGFFGDAEyEMCVRWMQ 289
Cdd:cd06596 135 ADGIENNSNARPFIWTVDGWAGTQRYAVIWTGDQSGSWEYIRFHIPTYIGSGLSGQAYATSDVDGIFGGSP-ETYTRDLQ 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 290 LGAFYPFSRNHNNIGTRRQDPVAWNSTFEMLSRKVLETRYTLLPYLYTLMHKAHVEGSTVVRPLLHEFTDDRTTWDIDR- 368
Cdd:cd06596 214 WKAFTPVLMNMSGWAANDKQPWVFGEPYTSINRKYLKLKMRLMPYIYTYAREASVTGLPMVRAMFLEYPNDPTAYGTATq 293
|
170 180 190
....*....|....*....|....*....|....*...
gi 767949047 369 -QFMLGPAILISPVLETSTFEISA----YFPRARWYDY 401
Cdd:cd06596 294 yQFMWGPDFLVAPVYQNTAAGNDVrngiYLPAGTWIDY 331
|
|
| GH31_lyase_GLase |
cd06601 |
alpha-1,4-glucan lyase; GLases (alpha-1,4-glucan lyases) are glycosyl hydrolase family 31 ... |
99-346 |
9.92e-21 |
|
alpha-1,4-glucan lyase; GLases (alpha-1,4-glucan lyases) are glycosyl hydrolase family 31 (GH31) enzymes that degrade alpha-1,4-glucans and maltooligosaccharides via a nonhydrolytic pathway to yield 1,5-D-anhydrofructose from the nonreducing end. GLases cleave the bond between C1 and O1 of the nonreducing sugar residue of alpha-glucans to generate a monosaccharide product with a double bond between C1 and C2. This family corresponds to subgroup 2 in the Ernst et al classification of GH31 enzymes.
Pssm-ID: 269887 [Multi-domain] Cd Length: 347 Bit Score: 95.17 E-value: 9.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 99 FPDFFRNSTAAWWKKEIEELYanprepekSLKFDGLWIDMNEPSnfvdgsvrgCSNEMLNNPPYMPYLESRdkglssktL 178
Cdd:cd06601 108 YPDLGRPEVREWWGQQYKYLF--------DMGLEMVWQDMTTPA---------IAPHKINGYGDMKTFPLR--------L 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 179 CMESQQILPDSSPVEHYNVHNLYGWSQTRPTYEAVQEVTG---QRGVIITRSTFPSSGRWGGHRLGNNTAAWDQLGKSII 255
Cdd:cd06601 163 LVTDDSVKNEHTYKPAATLWNLYAYNLHKATYHGLNRLNArpnRRNFIIGRGGYAGAQRFAGLWTGDNASTWDFLQINIP 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 256 GMMEFSLFGIPYTGADICGF--FGDA------EYEMCVRWMQLGAFYPFSRNHNNIGTRRQDPVAWNSTFEMLS------ 321
Cdd:cd06601 243 QVLNLGLSGVPISGSDIGGFasGSDEnegkwcDPELLIRWVQAGAFLPWFRNHYDRYIKKKQQEKLYEPYYYYEpvlpic 322
|
250 260
....*....|....*....|....*
gi 767949047 322 RKVLETRYTLLPYLYTLMHKAHVEG 346
Cdd:cd06601 323 RKYVELRYRLMQVFYDAMYENTQNG 347
|
|
| PRK10658 |
PRK10658 |
putative alpha-glucosidase; Provisional |
198-398 |
1.17e-19 |
|
putative alpha-glucosidase; Provisional
Pssm-ID: 236731 [Multi-domain] Cd Length: 665 Bit Score: 94.96 E-value: 1.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 198 HNLYGWSQTRPTYEAVQEVTGQR-GVIITRST------FPSsgRWGGhrlgNNTAAWDQLGKSIIGMMEFSLFGIPYTGA 270
Cdd:PRK10658 436 HNYYTYLYNKTVFDVLKETRGEGeAVLFARSAtvggqqFPV--HWGG----DCYSNYESMAESLRGGLSLGLSGFGFWSH 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 271 DICGFFGDAEYEMCVRWMQLGAFYPFSRNHNNIGTRrqdpVAWNSTFEM--LSRKVLETRYTLLPYLYTLMHKAHVEGST 348
Cdd:PRK10658 510 DIGGFENTATADVYKRWCAFGLLSSHSRLHGSKSYR----VPWAYDEEAvdVVRFFTKLKCRLMPYLYREAAEAHERGTP 585
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767949047 349 VVRPLLHEFTDDRTTWDIDRQFMLGPAILISPVLeTSTFEISAYFPRARW 398
Cdd:PRK10658 586 MMRAMVLEFPDDPACDYLDRQYMLGDSLLVAPVF-SEAGDVEYYLPEGRW 634
|
|
| GH31_glycosidase_Aec37 |
cd06599 |
E.coli Aec37-like; Glycosyl hydrolase family 31 (GH31) domain of a bacterial protein family ... |
19-297 |
8.14e-17 |
|
E.coli Aec37-like; Glycosyl hydrolase family 31 (GH31) domain of a bacterial protein family represented by Escherichia coli protein Aec37. The gene encoding Aec37 (aec-37) is located within a genomic island (AGI-3) isolated from the extraintestinal avian pathogenic Escherichia coli strain BEN2908. The function of Aec37 and its orthologs is unknown; however, deletion of a region of the genome that includes aec-37 affects the assimilation of seven carbohydrates, decreases growth rate of the strain in minimal medium containing galacturonate or trehalose, and attenuates the virulence of E. coli BEN2908 in chickens. All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein.
Pssm-ID: 269885 [Multi-domain] Cd Length: 319 Bit Score: 83.03 E-value: 8.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 19 LIEQMKKNGMRFILILDPAISGNETQYLPFirgQENNVFIKWPDTNDIVWGKVWPDLpnvivdGSldhetqvklyrayva 98
Cdd:cd06599 77 FFRKFHERGIRLVANIKPGLLTDHPHYDEL---AEKGAFIKDDDGGEPAVGRFWGGG------GS--------------- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 99 FPDFFRNSTAAWWKKEIEELYanprepeKSLKFDGLWIDMNEPSNFVDgsvrgcsnemlnnppympylESRDKGLSSKTL 178
Cdd:cd06599 133 YLDFTNPEGREWWKEGLKEQL-------LDYGIDSVWNDNNEYEIWDD--------------------DAACCGFGKGGP 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 179 CMESQQILPdsspvehynvhNLygwsQTRPTYEAVQEV-TGQRGVIITRSTFPSSGRWGGHRLGNNTAAWDQLGKSIIGM 257
Cdd:cd06599 186 ISELRPIQP-----------LL----MARASREAQLEHaPNKRPFVISRSGCAGIQRYAQTWSGDNRTSWKTLKYNIAMG 250
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 767949047 258 MEFSLFGIPYTGADICGFFGDA-EYEMCVRWMQLGAFYP-FS 297
Cdd:cd06599 251 LGMSLSGVANYGHDIGGFAGPApEPELFVRWVQNGIFQPrFS 292
|
|
| GH31_xylosidase_YicI |
cd06593 |
alpha-xylosidase YicI-like; YicI alpha-xylosidase is a glycosyl hydrolase family 31 (GH31) ... |
196-331 |
2.12e-16 |
|
alpha-xylosidase YicI-like; YicI alpha-xylosidase is a glycosyl hydrolase family 31 (GH31) enzyme that catalyzes the release of an alpha-xylosyl residue from the non-reducing end of alpha-xyloside substrates such as alpha-xylosyl fluoride and isoprimeverose. YicI forms a homohexamer (a trimer of dimers). All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. The YicI family corresponds to subgroup 4 in the Ernst et al classification of GH31 enzymes.
Pssm-ID: 269879 [Multi-domain] Cd Length: 308 Bit Score: 81.46 E-value: 2.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 196 NVHNLYGWSQTRPTYEAVQEVTGQRGVIITRSTFPSSGRWGGHRLGNNTAAWDQLGKSIIGMMEFSLFGIPYTGADICGF 275
Cdd:cd06593 176 KMHNLYPLLYNKAVYEATKEVKGEEAVLWARSAWAGSQRYPVHWGGDSESTFEGMAASLRGGLSLGLSGFGFWSHDIGGF 255
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 767949047 276 FGDAEYEMCVRWMQLGAFYPFSRNHnniGTRRQDPVAWNSTFEMLSRKVLETRYTL 331
Cdd:cd06593 256 EGTPSPELYKRWTQFGLLSSHSRLH---GSTPREPWEYGEEALDVVRKFAKLRYRL 308
|
|
| GH31_xylosidase_XylS |
cd06591 |
xylosidase XylS-like; XylS is a glycosyl hydrolase family 31 (GH31) alpha-xylosidase found in ... |
84-306 |
1.40e-14 |
|
xylosidase XylS-like; XylS is a glycosyl hydrolase family 31 (GH31) alpha-xylosidase found in prokaryotes, eukaryotes, and archaea, that catalyzes the release of alpha-xylose from the non-reducing terminal side of the alpha-xyloside substrate. XylS has been characterized in Sulfolobus solfataricus where it hydrolyzes isoprimeverose, the p-nitrophenyl-beta derivative of isoprimeverose, and xyloglucan oligosaccharides, and has transxylosidic activity. All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. The XylS family corresponds to subgroup 3 in the Ernst et al classification of GH31 enzymes.
Pssm-ID: 269877 [Multi-domain] Cd Length: 322 Bit Score: 76.44 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 84 LDHETQVKLYRAYVAFPDFFRNSTAAWWKKEIEELYanprepeKSLKFDGLWIDMNEPSNFvdgsvrgcsnemlnnppym 163
Cdd:cd06591 107 LRTNRGNGGFGGGTAFYDATNPEAREIYWKQLKDNY-------FDKGIDAWWLDATEPELD------------------- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 164 PYLESRDKGLSSktlcmesqqILPDSSpvehynVHNLYGWSQTRPTYEAVQEVT-GQRGVIITRSTFPSSGR-----WGG 237
Cdd:cd06591 161 PYDFDNYDGRTA---------LGPGAE------VGNAYPLMHAKGIYEGQRATGpDKRVVILTRSAFAGQQRygaavWSG 225
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767949047 238 hrlgNNTAAWDQLGKSIIGMMEFSLFGIPYTGADICGFFG--------DAEY-EMCVRWMQLGAFYPFSRNHnniGTR 306
Cdd:cd06591 226 ----DISSSWETLRRQIPAGLNFGASGIPYWTTDIGGFFGgdpepgedDPAYrELYVRWFQFGAFCPIFRSH---GTR 296
|
|
| GH31_transferase_CtsY |
cd06597 |
CtsY (cyclic tetrasaccharide-synthesizing enzyme Y)-like; CtsY is a bacterial ... |
198-314 |
2.50e-12 |
|
CtsY (cyclic tetrasaccharide-synthesizing enzyme Y)-like; CtsY is a bacterial 3-alpha-isomaltosyltransferase, first identified in Arthrobacter globiformis, that produces cyclic tetrasaccharides together with a closely related enzyme CtsZ. CtsY and CtsZ both have a glycosyl hydrolase family 31 (GH31) catalytic domain; CtsZ belongs to a different subfamily. All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein.
Pssm-ID: 269883 [Multi-domain] Cd Length: 326 Bit Score: 69.65 E-value: 2.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 198 HNLYGWSQTRPTYEAVQEVTGQrGVIITRSTFPSSGRWGGHRLGNNTAAWDQLGKSIIGMMEFSLFGIPYTGADICGFFG 277
Cdd:cd06597 186 RNEYPNLYYKAYFDYIREIGND-GVLFSRAGDSGAQRYPIGWVGDQDSTFEGLQSALKAGLSAAWSGYPFWGWDIGGFSG 264
|
90 100 110
....*....|....*....|....*....|....*....
gi 767949047 278 DA-EYEMCVRWMQLGAFYPFSRNH-NNIGTRRQDPVAWN 314
Cdd:cd06597 265 PLpTAELYLRWTQLAAFSPIMQNHsEKNHRPWSEERRWN 303
|
|
| COG4625 |
COG4625 |
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ... |
688-1230 |
3.09e-10 |
|
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function unknown];
Pssm-ID: 443664 [Multi-domain] Cd Length: 900 Bit Score: 64.80 E-value: 3.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 688 TNASTASTNATVPITTTCFATSTIGVTTNATVPDTTAPFPTNTTTASTNATIPITTTPFATSTISVTTSTTVPDTTAPFP 767
Cdd:COG4625 1 GGGGGGGGGGGGGGGGTGGGGAGGGGGAGGGAGGGGAGGGGGGGGGGGGAGGGGGGGGTGGGGGGGGGGGGGGAGGGGGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 768 TSTTSASTNATPVPITTTLFATSTIGVTTGTTVPDTTAPFPTSTTSTSTSATVPITTTPSPTNTADANTSNTVPNTTMPS 847
Cdd:COG4625 81 GGGGGGGGGTGGVGGGGGGGGGGGGGGGGGGGGGGGGSAGGGGGGAGGAGGGGGGGAGGGGGGGGGGGAGGGGGGGAGGA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 848 PTSSTTVSTIATVPISVTPSLTSTADATISTTVLIATTSSLTGTTDVSTSTTINNISTPVQTNTTNASTSTNVANITATS 927
Cdd:COG4625 161 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGNGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGGGGGGGGGGGG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 928 HTSTDDTVPNNTVPVTAIPSLANTGVDTTSNSFSIMTTSFSESTNAMNTTVIMATTSPTSTDVASTNNDASMTNFLLATM 1007
Cdd:COG4625 241 GGGGGGGAGGGGGGGGGNGGGGGAGGGGGGGGGGSGGGGGGGGGGGSGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 1008 SAGNITSNSISITTTSFGNSVPFVTTpspSTDATTTSNNTNPGMTTYYQTSPTIPTHTLTSIPSSITSILSMFPTSNTFT 1087
Cdd:COG4625 321 GGGGGGGGGGGGGAGGGGGSGGAGAG---GGGAGGGGAGGGGGGGTGGGGGGGGGGGGGSGGGGAGGGGGSGGGGGGGAG 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 1088 TDKITNFTTPTNANTIIFNTLDTKSTMVIDATVTTTSTKDNTMSPDTTVTSIDKFTTHITQFATPHSATTTTLALSHTSL 1167
Cdd:COG4625 398 GGGGGGGAGGTGGGGAGGGGGAAGGGGGGTGAGGGGGGGGTGAGGGGATGGGGGGGGGAGGSGGGAGAGGGSGSGAGTLT 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767949047 1168 APTNLSNLGTMDITDADNSSSVTGNTTHISVSnlTTASVTITATGLDSQTPHMVINSVATYLP 1230
Cdd:COG4625 478 LTGNNTYTGTTTVNGGGNYTQSAGSTLAVEVD--AANSDRLVVTGTATLNGGTVVVLAGGYAP 538
|
|
| FhaB |
COG3210 |
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ... |
594-1212 |
2.00e-09 |
|
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442443 [Multi-domain] Cd Length: 1698 Bit Score: 62.48 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 594 STTNATSSETITSSASANTTTGTTDTVPITTTSFPSTTSVTTNTTVPDTTSPFPTSTTNASTNATVPITTTPFPTSTIGV 673
Cdd:COG3210 95 GLTSNIGGGSVNGSNSTGNGTLTTTAASATTGNNTGGTTTSSTNTVTTLGGTTTGNTVLSTSGAGNNTNTNNSSSGTNIG 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 674 TTNATVPNTTAPFPTNASTASTNATVPITTTCFATSTIGVTTNATVPDTTAPFPTNTTTASTNATIPITTTPFATSTISV 753
Cdd:COG3210 175 NSIPTTGGSLNVVAANPTGVTGVGGALINATAGVLANAGGGTAGGVASANSTLTGGVVAAGTGAGVISTGGTDISSLSVA 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 754 TTSTTVPDTTAPFPTSTTSASTNATPVPITTTLFATSTIGVTTGTTVPDTTAPFPTSTTSTSTSATVPITTTPSPTNTAD 833
Cdd:COG3210 255 AGAGTGGAGGTGNAGNTTIGTTVTGTNATGSNTAGASSGDTTTNGTSSVTGAGGTGVLGGGTAAGITTTNTVGGNGDGNN 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 834 ANTSNTVPNTTMPSPTSSTTVSTIATVPISVTPSLTSTADATISTTVLIATTSSLTGTTDVSTSTTINNISTPVQTNTTN 913
Cdd:COG3210 335 TTANSGAGLVSGGTGGNNGTTGTGAGSGLTGTGNGGGLTTAGAGTVASTVGTATASTGNASSTTVLGSGSLATGNTGTTI 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 914 ASTSTNVANITATSHTSTDDTVPNNTVPVTAIPSLANTGVDTTSNSFSIMTTSFSESTNAMNTTVIMATTSPTSTDVAST 993
Cdd:COG3210 415 AGNGGSANAGGFTTTGGVLGITGNGTVTGGTIGGLTGSGTTNGAGLSGNTDVSGTGTVTNSAGNTTSATTLAGGGIGTVT 494
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 994 NNDASMTNFLLATMSAGNITSNSISITTTSFGNSVPFVTTPSP-STDATTTSNNTNPGMTTYYQTSPTIPTHTLTSIPSS 1072
Cdd:COG3210 495 TNATISNNAGGDANGIATGLTGITAGGGGGGNATSGGTGGDGTtLSGSGLTTTVSGGASGTTAASGSNTANTLGVLAATG 574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 1073 ITSILSMFPTSNTFTTDKITNFTTPTNANTIIFNTLDTKSTMVIDATVTTTSTKDNTMSPDTTVTSIDKFTTHITQFATP 1152
Cdd:COG3210 575 GTSNATTAGNSTSATGGTGTNSGGTVLSIGTGSAGATGTITLGAGTSGAGANATGGGAGLTGSAVGAALSGTGSGTTGTA 654
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767949047 1153 HSATTTTLALSHTSLAPTNLSNLGTMDITDADNSSSVTGNTTHISV---SNLTTASVTITATG 1212
Cdd:COG3210 655 SANGSNTTGVNTAGGTGGGTTGTVTSGATGGTTGTTLNAATGGTLNnagNTLTISTGSITVTG 717
|
|
| COG4625 |
COG4625 |
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ... |
768-1251 |
1.19e-08 |
|
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function unknown];
Pssm-ID: 443664 [Multi-domain] Cd Length: 900 Bit Score: 59.79 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 768 TSTTSASTNATPVPITTTLFATSTIGVTTGTTVPDTTAPFPTSTTSTSTSATVPITTTPSPTNTADANTSNTVPNTTMPS 847
Cdd:COG4625 12 GGGGGTGGGGAGGGGGAGGGAGGGGAGGGGGGGGGGGGAGGGGGGGGTGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGTG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 848 PTSSTTVSTIATVPISVTPSLTSTADATISTTVLIATTSSLTGTTDVSTSTTINNISTPVQTNTTNASTSTNVANITATS 927
Cdd:COG4625 92 GVGGGGGGGGGGGGGGGGGGGGGGGGSAGGGGGGAGGAGGGGGGGAGGGGGGGGGGGAGGGGGGGAGGAGGGGGGGGGGG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 928 HTSTDDTVPNNTVPVTAIPSLANTGVDTTSNSFSIMTTSFSESTNAMNTTVIMATTSPTSTDVASTNNDASMTNFLLAtm 1007
Cdd:COG4625 172 GGGGGGGGGGGGGGGGGGGGGNGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGAG-- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 1008 SAGNITSNSISITTTSFGNSVPFVTTPSPSTDATTTSNNTNPGMTTYYQTSPTIPTHTLTSIPSSITSIlsmfpTSNTFT 1087
Cdd:COG4625 250 GGGGGGGGNGGGGGAGGGGGGGGGGSGGGGGGGGGGGSGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGG-----GGGGGG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 1088 TDKITNFTTPTNANTIIFNTLDTKSTMVIDATVTTTSTKDNTMSPDTTVTSIDKFTTHITQFATPHSATTTTLALSHTSL 1167
Cdd:COG4625 325 GGGGGGGGGAGGGGGSGGAGAGGGGAGGGGAGGGGGGGTGGGGGGGGGGGGGSGGGGAGGGGGSGGGGGGGAGGGGGGGG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 1168 APTNLSNLGTMDITDADNSSSVTGNTTHISVSNLTTASVTITATGLDSQTPHMVINSV-ATYLPITATSATTDTTNITKY 1246
Cdd:COG4625 405 AGGTGGGGAGGGGGAAGGGGGGTGAGGGGGGGGTGAGGGGATGGGGGGGGGAGGSGGGaGAGGGSGSGAGTLTLTGNNTY 484
|
....*
gi 767949047 1247 ALNTT 1251
Cdd:COG4625 485 TGTTT 489
|
|
| COG4625 |
COG4625 |
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ... |
599-1125 |
2.97e-08 |
|
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function unknown];
Pssm-ID: 443664 [Multi-domain] Cd Length: 900 Bit Score: 58.25 E-value: 2.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 599 TSSETITSSASANTTTGTTDTVPITTTSFPSTTSVTTNTTVPDTTSPFPTSTTNASTNATVPITTTPFPTSTIGVTTNAT 678
Cdd:COG4625 1 GGGGGGGGGGGGGGGGTGGGGAGGGGGAGGGAGGGGAGGGGGGGGGGGGAGGGGGGGGTGGGGGGGGGGGGGGAGGGGGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 679 VPNTTAPFPTNASTASTNATVPITTTCFATSTIGVTTNATVPDTTAPFPTNTTTASTNATIPITTTPFATSTISVTtstt 758
Cdd:COG4625 81 GGGGGGGGGTGGVGGGGGGGGGGGGGGGGGGGGGGGGSAGGGGGGAGGAGGGGGGGAGGGGGGGGGGGAGGGGGGG---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 759 vpdttapfpTSTTSASTNATPVPITTTLFATSTIGVTTGTTVPDTTAPFPTSTTSTSTSATVPITTTPSPTNTADANTSN 838
Cdd:COG4625 157 ---------AGGAGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGNGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGGGGG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 839 TVPNTTMPSPTSSTTVSTIATVPISVTPSLTSTADATISTTVLIATTSSLTGTTDVSTSTTINNISTPVQTNTTNASTST 918
Cdd:COG4625 228 GGGGGGGGGGGGGGGGGGGGAGGGGGGGGGNGGGGGAGGGGGGGGGGSGGGGGGGGGGGSGGGGGGGGGGGGGGGGGGGG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 919 NVANITATSHTSTDDTVPNNTVPVTAIPSLANTGVDTTSNSFSIMTTSFSESTNAMNTTVIMATTSPTSTDVASTNNDAS 998
Cdd:COG4625 308 GGGGGGGGGGGGGGGGGGGGGGGGGGAGGGGGSGGAGAGGGGAGGGGAGGGGGGGTGGGGGGGGGGGGGSGGGGAGGGGG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 999 MTNFLLATMSAGNITSNSISITTTSFGNSVPFVTTPSPSTDATTTSNNTNPGMTTYYQTSPTIPTHTLTSIPSSITSILS 1078
Cdd:COG4625 388 SGGGGGGGAGGGGGGGGAGGTGGGGAGGGGGAAGGGGGGTGAGGGGGGGGTGAGGGGATGGGGGGGGGAGGSGGGAGAGG 467
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 767949047 1079 MFPT-SNTFTTDKITNFTTPTNANTIIFNTLDTKSTMVIDATVTTTST 1125
Cdd:COG4625 468 GSGSgAGTLTLTGNNTYTGTTTVNGGGNYTQSAGSTLAVEVDAANSDR 515
|
|
| FhaB |
COG3210 |
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ... |
546-1210 |
6.60e-08 |
|
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442443 [Multi-domain] Cd Length: 1698 Bit Score: 57.47 E-value: 6.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 546 YNQILTIQLTDKTINLEKLTEVTWIDGGPVLPTPTKTSTIPMSSHPSPSTTNATSSETITSSASANTTTGTTDTVPITTT 625
Cdd:COG3210 94 TGLTSNIGGGSVNGSNSTGNGTLTTTAASATTGNNTGGTTTSSTNTVTTLGGTTTGNTVLSTSGAGNNTNTNNSSSGTNI 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 626 SFPSTTSVTTNTTVPDTTSPFPTSTTNASTNATVPITTTPFPTSTIGVTTNATVPNTTAPFPTNASTASTNATVPITTTC 705
Cdd:COG3210 174 GNSIPTTGGSLNVVAANPTGVTGVGGALINATAGVLANAGGGTAGGVASANSTLTGGVVAAGTGAGVISTGGTDISSLSV 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 706 FATSTIGVTTNATVPDTTAPFPTNTTTASTNATIPITTTPFATSTISVTTSTTVPDTTAPFPTSTTSASTNATPVPITTT 785
Cdd:COG3210 254 AAGAGTGGAGGTGNAGNTTIGTTVTGTNATGSNTAGASSGDTTTNGTSSVTGAGGTGVLGGGTAAGITTTNTVGGNGDGN 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 786 LFATSTIGVTTGTTVPDTTApfpTSTTSTSTSATVPITTTPSPTNTADANTSNTVPNTTMPSPTSSTTVSTIATVPISVT 865
Cdd:COG3210 334 NTTANSGAGLVSGGTGGNNG---TTGTGAGSGLTGTGNGGGLTTAGAGTVASTVGTATASTGNASSTTVLGSGSLATGNT 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 866 PSLTSTADATISTTVLIATTSSLTGTTDVSTSTTINNISTPVQTNTTNASTSTNVANITATSHTSTDDTVPNNTVPVTAI 945
Cdd:COG3210 411 GTTIAGNGGSANAGGFTTTGGVLGITGNGTVTGGTIGGLTGSGTTNGAGLSGNTDVSGTGTVTNSAGNTTSATTLAGGGI 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 946 PSLANTGVDTTSNSFSIMTTSFSESTNAMNTTVIMATTSPTSTDVASTNNDASMTNFLLATMSAGNITSNSISITTTSFG 1025
Cdd:COG3210 491 GTVTTNATISNNAGGDANGIATGLTGITAGGGGGGNATSGGTGGDGTTLSGSGLTTTVSGGASGTTAASGSNTANTLGVL 570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 1026 NSVPFVTTPSPSTDATTTSNNTNPGMTTYYQTSPTIPTHTLTSIPSSITSILSMFPTSNTFTTDKITNFTTPTNANTIIF 1105
Cdd:COG3210 571 AATGGTSNATTAGNSTSATGGTGTNSGGTVLSIGTGSAGATGTITLGAGTSGAGANATGGGAGLTGSAVGAALSGTGSGT 650
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 1106 NTLDTKSTMVIDATVTTTSTKDNTMSPDTTVTSIDKFTTHITQFATphsaTTTTLALSHTSLAPTNLSNLGTMDITDADN 1185
Cdd:COG3210 651 TGTASANGSNTTGVNTAGGTGGGTTGTVTSGATGGTTGTTLNAATG----GTLNNAGNTLTISTGSITVTGQIGALANAN 726
|
650 660
....*....|....*....|....*
gi 767949047 1186 SSSVTGNTTHISVSNLTTASVTITA 1210
Cdd:COG3210 727 GDTVTFGNLGTGATLTLNAGVTITS 751
|
|
| FhaB |
COG3210 |
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ... |
593-1275 |
1.31e-06 |
|
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442443 [Multi-domain] Cd Length: 1698 Bit Score: 53.23 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 593 PSTTNATSSETITSSASANTTTGTTDTVPITTTSFPSTTSVTTNTTVPDTTSPFPTSTTNASTNATVPITTTPFPTSTIG 672
Cdd:COG3210 306 AGGTGVLGGGTAAGITTTNTVGGNGDGNNTTANSGAGLVSGGTGGNNGTTGTGAGSGLTGTGNGGGLTTAGAGTVASTVG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 673 VTTNATVPNTTApfpTNASTASTNATVPITTTCFATSTIGVTTNATVPDTTAPFPTNTTTASTNATIPITTTPFATSTIS 752
Cdd:COG3210 386 TATASTGNASST---TVLGSGSLATGNTGTTIAGNGGSANAGGFTTTGGVLGITGNGTVTGGTIGGLTGSGTTNGAGLSG 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 753 VTTSTTVPDTTAPFPTSTTSASTNATPVPITTTLFATSTIGVTTGTTVPDTTAPFPTSTTSTSTSATVPITTTPSPTNTA 832
Cdd:COG3210 463 NTDVSGTGTVTNSAGNTTSATTLAGGGIGTVTTNATISNNAGGDANGIATGLTGITAGGGGGGNATSGGTGGDGTTLSGS 542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 833 DANTSNTVPNTTMPSPTSSTTVSTIATVPISVTPSLTSTADATISTTVLIATTSSLTGTTDVSTSTTINNISTPVQTNTT 912
Cdd:COG3210 543 GLTTTVSGGASGTTAASGSNTANTLGVLAATGGTSNATTAGNSTSATGGTGTNSGGTVLSIGTGSAGATGTITLGAGTSG 622
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 913 NASTSTNVANITATSHTSTDDTVPNNTVPVTAIPSLANTGVDTTSNSFSIMTTSFSESTNAMNTTVIMATTSPTSTDVAS 992
Cdd:COG3210 623 AGANATGGGAGLTGSAVGAALSGTGSGTTGTASANGSNTTGVNTAGGTGGGTTGTVTSGATGGTTGTTLNAATGGTLNNA 702
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 993 TNNDASMTNFLLATMSAGNITSNSISITTTSFGNSVPFVTTPSPSTDATTTSNNTNPGMTTYYQTSPTIPTHTLTSIPSS 1072
Cdd:COG3210 703 GNTLTISTGSITVTGQIGALANANGDTVTFGNLGTGATLTLNAGVTITSGNAGTLSIGLTANTTASGTTLTLANANGNTS 782
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 1073 ITSILSmfpTSNTFTTDKITNFTTPTNANTIIFNTLDTKSTMVIDATVTTTSTKDNTMSPDTTVTSIDKFTTHITQFATP 1152
Cdd:COG3210 783 AGATLD---NAGAEISIDITADGTITAAGTTAINVTGSGGTITINTATTGLTGTGDTTSGAGGSNTTDTTTGTTSDGASG 859
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 1153 HSATTTTLALSHTSLAPTNLSNLGTMDITDADNSSSVTGNTTHISVSNLTTASVTITATGLDSQTPHMVINSVATYLPIT 1232
Cdd:COG3210 860 GGTAGANSGSLAATAASITVGSGGVATSTGTANAGTLTNLGTTTNAASGNGAVLATVTATGTGGGGLTGGNAAAGGTGAG 939
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 767949047 1233 ATSATTDTTNITKYALNTTTPDSTVHTSATAPTYIANAINATQ 1275
Cdd:COG3210 940 NGTTALSGTQGNAGLSAASASDGAGDTGASSAAGSSAVGTSAN 982
|
|
| FhaB |
COG3210 |
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ... |
582-1274 |
2.07e-06 |
|
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442443 [Multi-domain] Cd Length: 1698 Bit Score: 52.46 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 582 TSTIPMSSHPSPSTTNATSSETITSSASANTTTGTTDTVPITTTSFPSTTSVTTNTTVPDTTSPFPTSTTNASTNATVPI 661
Cdd:COG3210 610 ATGTITLGAGTSGAGANATGGGAGLTGSAVGAALSGTGSGTTGTASANGSNTTGVNTAGGTGGGTTGTVTSGATGGTTGT 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 662 TTTPFPTSTIGVTTNATVPNTTAPFPTNASTASTNATVPITTTCFATSTIGVTTNATVPDTTAPFPTNTTTASTNATIPI 741
Cdd:COG3210 690 TLNAATGGTLNNAGNTLTISTGSITVTGQIGALANANGDTVTFGNLGTGATLTLNAGVTITSGNAGTLSIGLTANTTASG 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 742 TTTPFATSTISVTTSTTVPDTTAPFPTSTTSASTNATPVPITTTLFATSTIGVTTGTTVPDTTAPFPTSTTSTSTSATVP 821
Cdd:COG3210 770 TTLTLANANGNTSAGATLDNAGAEISIDITADGTITAAGTTAINVTGSGGTITINTATTGLTGTGDTTSGAGGSNTTDTT 849
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 822 ITTTPSPTNTADANTSNTVPNTTMPSPTSSTTVSTIATVPISVTPSLTSTADATISTTVLIATTSSLTGTTDVSTSTTIN 901
Cdd:COG3210 850 TGTTSDGASGGGTAGANSGSLAATAASITVGSGGVATSTGTANAGTLTNLGTTTNAASGNGAVLATVTATGTGGGGLTGG 929
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 902 NISTPVQTNTTNASTSTNVANITATSHTSTDDTVPNNTVPVTAIPSLANTGVDTTSNSFSIMTTSFSESTNAMNTTVIMA 981
Cdd:COG3210 930 NAAAGGTGAGNGTTALSGTQGNAGLSAASASDGAGDTGASSAAGSSAVGTSANSAGSTGGVIAATGILVAGNSGTTASTT 1009
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 982 TTSPTST-DVASTNNDASMTNFLLATMSAGNITSNSISITTTSFGNSVPFVTTPSPSTDATTTSNNTNPGMTTYYQTSPT 1060
Cdd:COG3210 1010 GGSGAIVaGGNGVTGTTGTASATGTGTAATAGGQNGVGVNASGISGGNAAALTASGTAGTTGGTAASNGGGGTAQASGAG 1089
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 1061 IPTHTLTSIPSSITSILSMFPTSNTFTTDKITNFTTPTNANTIIFNTLDTKSTMVIDATVTTTSTKDNTMSPDTTVTSID 1140
Cdd:COG3210 1090 TTHTLGGITNGGATGTSGGTTTSTGGVTASKVGGTTTVGATGTSTASTEAAGAGTLTGLVAVSAVAGGASSASAGDTTAV 1169
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 1141 KFTTHITQFATPHSATTTTLALSHTSLAPTNLSNLGTMDITDADNSSSVTGNTTHISVSNLTTASVTITATGLDSQTPHM 1220
Cdd:COG3210 1170 AAATTTTTGSAINGGADSAATEGTAGTDLKGGDSTGGSTTTIGTTNVTTTTTLTASDTGNTTATGGSSAGQTGSFVAAGS 1249
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 767949047 1221 VINSVATYLPITATSATTDTTNITKYALNTTTPDSTVHTSATAPTYIANAINAT 1274
Cdd:COG3210 1250 ASGTGDATTGATAGAVSNGATSTVAGNAGATATGSTVDIGSTSATSAGGSLDTT 1303
|
|
| GH31_u1 |
cd06595 |
glycosyl hydrolase family 31 (GH31); uncharacterized subgroup; This family represents an ... |
233-335 |
8.87e-06 |
|
glycosyl hydrolase family 31 (GH31); uncharacterized subgroup; This family represents an uncharacterized GH31 enzyme subgroup found in bacteria and eukaryotes. Enzymes of the GH31 family possess a wide range of different hydrolytic activities including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-xylosidase, 6-alpha-glucosyltransferase, 3-alpha-isomaltosyltransferase and alpha-1,4-glucan lyase. All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein.
Pssm-ID: 269881 [Multi-domain] Cd Length: 304 Bit Score: 49.12 E-value: 8.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 233 GRWGG---HRL-----GNNTAAWDqlgksiigMMEF--------SLFGIPYTGADICGFFGDAE-YEMCVRWMQLGAFYP 295
Cdd:cd06595 192 SRWGGlgsHRYpigfsGDTEVSWE--------TLAFqpyftataANVGYSWWSHDIGGHKGGIEdPELYLRWVQFGVFSP 263
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 767949047 296 FSRNHNNIGTR-RQDPVAWNSTFEMLSRKVLETRYTLLPYL 335
Cdd:cd06595 264 ILRLHSDKGPYyKREPWLWDAKTFEIAKDYLRLRHRLIPYL 304
|
|
| Chi1 |
COG3469 |
Chitinase [Carbohydrate transport and metabolism]; |
858-1075 |
2.27e-05 |
|
Chitinase [Carbohydrate transport and metabolism];
Pssm-ID: 442692 [Multi-domain] Cd Length: 534 Bit Score: 48.60 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 858 ATVPISVTPSLTSTADATISTTVLIATTSSLTGTTDVSTSTTINNISTPVQTNTTNASTSTNVANITATSHTSTDDTVPN 937
Cdd:COG3469 2 SSVSTAASPTAGGASATAVTLLGAAATAASVTLTAATATTVVSTTGSVVVAASGSAGSGTGTTAASSTAATSSTTSTTAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 938 NTVPVTAIPSLANTGVDTTSNSfsimTTSFSESTNAMNTTVIMATTSPTSTDVASTNNDASmtnfllatmSAGNITSNSI 1017
Cdd:COG3469 82 ATAAAAAATSTSATLVATSTAS----GANTGTSTVTTTSTGAGSVTSTTSSTAGSTTTSGA---------SATSSAGSTT 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 767949047 1018 SITTTSFGNSVPFVTTPSPSTDATTTSNNTNPGMTTYYQTSPTIPTHTLTSIPSSITS 1075
Cdd:COG3469 149 TTTTVSGTETATGGTTTTSTTTTTTSASTTPSATTTATATTASGATTPSATTTATTTG 206
|
|
| Chi1 |
COG3469 |
Chitinase [Carbohydrate transport and metabolism]; |
567-779 |
4.87e-05 |
|
Chitinase [Carbohydrate transport and metabolism];
Pssm-ID: 442692 [Multi-domain] Cd Length: 534 Bit Score: 47.44 E-value: 4.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 567 VTWIDGGPVLPTPTKTSTIPMSSHPSPSTTNATSSETITSSASANTTTGTTDTVPITTTSFPSTTSVTTNTTVPDTTSPF 646
Cdd:COG3469 4 VSTAASPTAGGASATAVTLLGAAATAASVTLTAATATTVVSTTGSVVVAASGSAGSGTGTTAASSTAATSSTTSTTATAT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 647 ptsttnASTNATVPITTTPFPTSTIGVTTNATVPNTTAPFPTNASTASTNATVPITTTCFATSTIGVTTNATVPDTTAPF 726
Cdd:COG3469 84 ------AAAAAATSTSATLVATSTASGANTGTSTVTTTSTGAGSVTSTTSSTAGSTTTSGASATSSAGSTTTTTTVSGTE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767949047 727 PTNTTTASTNATIPITTTPFATSTISVTTSTTVPDTTAPFPTSTTSASTNATP 779
Cdd:COG3469 158 TATGGTTTTSTTTTTTSASTTPSATTTATATTASGATTPSATTTATTTGPPTP 210
|
|
| Chi1 |
COG3469 |
Chitinase [Carbohydrate transport and metabolism]; |
824-1050 |
6.52e-05 |
|
Chitinase [Carbohydrate transport and metabolism];
Pssm-ID: 442692 [Multi-domain] Cd Length: 534 Bit Score: 47.05 E-value: 6.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 824 TTPSPTNTADANTSNTVPNTTMPSPTSSTTVSTIATVPISVTPSLTSTADATISTTVLIATTSSLTGTTDVSTSTTINNI 903
Cdd:COG3469 6 TAASPTAGGASATAVTLLGAAATAASVTLTAATATTVVSTTGSVVVAASGSAGSGTGTTAASSTAATSSTTSTTATATAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 904 STPVQTNTTNASTSTNVANITATSHTSTDDTVPNNTVPVTaipSLANTGVDTTSNSFSIMTTSFSESTNAMNTTVIMATT 983
Cdd:COG3469 86 AAAATSTSATLVATSTASGANTGTSTVTTTSTGAGSVTST---TSSTAGSTTTSGASATSSAGSTTTTTTVSGTETATGG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767949047 984 SPTSTDVASTnndasmtnfllatmsagnITSNSISITTTSFGNSVPFVTTPSPSTDATTTSNNTNPG 1050
Cdd:COG3469 163 TTTTSTTTTT------------------TSASTTPSATTTATATTASGATTPSATTTATTTGPPTPG 211
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
683-1075 |
7.43e-05 |
|
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 47.22 E-value: 7.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 683 TAPFPTNASTASTNATVPITTTCFATSTIGVTTNATVPDTTAPFPTNTTTASTNATIPITTTPFATSTISVTTSTTVpdt 762
Cdd:pfam05109 398 TAPKTLIITRTATNATTTTHKVIFSKAPESTTTSPTLNTTGFAAPNTTTGLPSSTHVPTNLTAPASTGPTVSTADVT--- 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 763 tAPFPTSTTSASTNATPVPitttlfatstigvttgttvpdttAPFPTSTTSTSTSATVPITTTPSPTNTADANT---SNT 839
Cdd:pfam05109 475 -SPTPAGTTSGASPVTPSP-----------------------SPRDNGTESKAPDMTSPTSAVTTPTPNATSPTpavTTP 530
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 840 VPNTTMPSPTSSTTVSTIAT-VPISVTPS---LTSTADATISTTVLIATTSSLTGTTDVSTSTTINNIStpvqtnttnas 915
Cdd:pfam05109 531 TPNATSPTLGKTSPTSAVTTpTPNATSPTpavTTPTPNATIPTLGKTSPTSAVTTPTPNATSPTVGETS----------- 599
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 916 tstnvANITATSHTSTDDTvpnNTVPVTAIPSLANTGVDTTSNSFsimtTSFSESTNAMNTTVIMATTSPTSTDVASTNN 995
Cdd:pfam05109 600 -----PQANTTNHTLGGTS---STPVVTSPPKNATSAVTTGQHNI----TSSSTSSMSLRPSSISETLSPSTSDNSTSHM 667
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 996 DASMTNFLLATMSAGNITSNSISITTTSFGNSVPFVTTPSPSTDATTTSNNTNPGMTTYYQ-------TSPTIPTHTLTS 1068
Cdd:pfam05109 668 PLLTSAHPTGGENITQVTPASTSTHHVSTSSPAPRPGTTSQASGPGNSSTSTKPGEVNVTKgtppknaTSPQAPSGQKTA 747
|
....*..
gi 767949047 1069 IPSSITS 1075
Cdd:pfam05109 748 VPTVTST 754
|
|
| Chi1 |
COG3469 |
Chitinase [Carbohydrate transport and metabolism]; |
820-998 |
6.58e-04 |
|
Chitinase [Carbohydrate transport and metabolism];
Pssm-ID: 442692 [Multi-domain] Cd Length: 534 Bit Score: 43.97 E-value: 6.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 820 VPITTTPSPTNTADANTSNTVPNTTMPSPTSSTTVSTIATVPISVTPSLTSTADATISTTVLIATTSSLTGTTDVSTSTT 899
Cdd:COG3469 30 ASVTLTAATATTVVSTTGSVVVAASGSAGSGTGTTAASSTAATSSTTSTTATATAAAAAATSTSATLVATSTASGANTGT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 900 INNISTPV-QTNTTNASTSTNVANITATSHTSTDDTVPNNTVPVTAIPSLANTGVDTTSNSFSIMTTSFSESTNAMNTTV 978
Cdd:COG3469 110 STVTTTSTgAGSVTSTTSSTAGSTTTSGASATSSAGSTTTTTTVSGTETATGGTTTTSTTTTTTSASTTPSATTTATATT 189
|
170 180
....*....|....*....|
gi 767949047 979 IMATTSPTSTDVASTNNDAS 998
Cdd:COG3469 190 ASGATTPSATTTATTTGPPT 209
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
863-1102 |
6.99e-04 |
|
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
Pssm-ID: 465521 [Multi-domain] Cd Length: 506 Bit Score: 43.80 E-value: 6.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 863 SVTPSLTSTADATISTTVLIATTSSLTGTTDVSTSTTINNISTPVQTNTTNASTSTNVANITATSHTSTDDTVPNNTVPV 942
Cdd:pfam17823 109 GAASRALAAAASSSPSSAAQSLPAAIAALPSEAFSAPRAAACRANASAAPRAAIAAASAPHAASPAPRTAASSTTAASST 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 943 TAIPSLANTGVDTTSNSFSIMTTSFSESTNAMNTTVIMATTS-PTSTDVASTNNDASMTnFLLATMSAGNITSNSISITT 1021
Cdd:pfam17823 189 TAASSAPTTAASSAPATLTPARGISTAATATGHPAAGTALAAvGNSSPAAGTVTAAVGT-VTPAALATLAAAAGTVASAA 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 1022 TSFGNSVPFVTTPSPSTDATTTSNNTNPGMTTYYQTSPTI-------PTHTLTSIPSSITSILSMFPTSNTFTTDKITNF 1094
Cdd:pfam17823 268 GTINMGDPHARRLSPAKHMPSDTMARNPAAPMGAQAQGPIiqvstdqPVHNTAGEPTPSPSNTTLEPNTPKSVASTNLAV 347
|
....*...
gi 767949047 1095 TTPTNANT 1102
Cdd:pfam17823 348 VTTTKAQA 355
|
|
| GH31_glucosidase_YihQ |
cd06594 |
alpha-glucosidase YihQ-like; YihQ is a bacterial alpha-glucosidase with a conserved glycosyl ... |
197-300 |
8.26e-04 |
|
alpha-glucosidase YihQ-like; YihQ is a bacterial alpha-glucosidase with a conserved glycosyl hydrolase family 31 (GH31) domain that catalyzes the release of an alpha-glucosyl residue from the non-reducing end of alpha-glucoside substrates such as alpha-glucosyl fluoride. Orthologs of YihQ that have not yet been functionally characterized are present in plants and fungi. YihQ has sequence similarity to other GH31 enzymes such as CtsZ, a 6-alpha-glucosyltransferase from Bacillus globisporus, and YicI, an alpha-xylosidase from Echerichia coli. These latter two belong to different GH31 subfamilies than YihQ. In bacteria, YihQ (along with YihO) is important for bacterial O-antigen capsule assembly and translocation.
Pssm-ID: 269880 [Multi-domain] Cd Length: 325 Bit Score: 42.96 E-value: 8.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 197 VHNLYG--WSQTrpTYEAVQEVTGQRGVII-TRSTFPSSGR-----WGGHRLGNntaaW---DQLGKSIIGMMEFSLFGI 265
Cdd:cd06594 184 YHNRYPelWARL--NREAVEEAGKEGEIVFfMRSGYTGSPRystlfWAGDQNVD----WsrdDGLKSVIPGALSSGLSGF 257
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 767949047 266 PYTGADICG----FFGDAEY----EMCVRWMQLGAFYPFSRNH 300
Cdd:cd06594 258 SLTHSDIGGyttlFNPLVGYkrskELLMRWAEMAAFTPVMRTH 300
|
|
| Chi1 |
COG3469 |
Chitinase [Carbohydrate transport and metabolism]; |
924-1114 |
1.21e-03 |
|
Chitinase [Carbohydrate transport and metabolism];
Pssm-ID: 442692 [Multi-domain] Cd Length: 534 Bit Score: 43.20 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 924 TATSHTSTDDTVPNNTVPVTAIPSLANTGVDTTSNSFSIMTTSFSESTNAMN--TTVIMATTSPTSTDVASTNNDASMTN 1001
Cdd:COG3469 13 GGASATAVTLLGAAATAASVTLTAATATTVVSTTGSVVVAASGSAGSGTGTTaaSSTAATSSTTSTTATATAAAAAATST 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 1002 FLLATMSAGNITSNSISITTTSFGNSVPFVTTPSPSTDATTTSNNTNPGMTTYYQTSPTIPTHTLTSIPSSITSILSMFP 1081
Cdd:COG3469 93 SATLVATSTASGANTGTSTVTTTSTGAGSVTSTTSSTAGSTTTSGASATSSAGSTTTTTTVSGTETATGGTTTTSTTTTT 172
|
170 180 190
....*....|....*....|....*....|...
gi 767949047 1082 TSNTFTTDKITNFTTPTNANTIIFNTLDTKSTM 1114
Cdd:COG3469 173 TSASTTPSATTTATATTASGATTPSATTTATTT 205
|
|
| FhaB |
COG3210 |
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ... |
594-1276 |
1.37e-03 |
|
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442443 [Multi-domain] Cd Length: 1698 Bit Score: 43.22 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 594 STTNATSSETITSSASANTTTGTTDTVPITTTSFPSTTSVTTNTTVPDTTSPFPTSTTNASTNATVPITTTPFPTSTIGV 673
Cdd:COG3210 499 ISNNAGGDANGIATGLTGITAGGGGGGNATSGGTGGDGTTLSGSGLTTTVSGGASGTTAASGSNTANTLGVLAATGGTSN 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 674 TTNATVPNTTAPFPTNASTASTNATVPITTTCFATSTIGVTTNATVPDTTAPFPTNTTTASTNATIPITTTPFATSTISV 753
Cdd:COG3210 579 ATTAGNSTSATGGTGTNSGGTVLSIGTGSAGATGTITLGAGTSGAGANATGGGAGLTGSAVGAALSGTGSGTTGTASANG 658
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 754 TTSTTVPDTTAPFPTSTTSASTNATPVPITTTLFATSTIGVTTGTTVPDTTAPFPTSTTSTSTSATVP------ITTTPS 827
Cdd:COG3210 659 SNTTGVNTAGGTGGGTTGTVTSGATGGTTGTTLNAATGGTLNNAGNTLTISTGSITVTGQIGALANANgdtvtfGNLGTG 738
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 828 PTNTADAN-TSNTVPNTTMPSPTSSTTVSTIATVPISVTPSLTSTADATISTTVLIATTSSLTGTTDVSTSTTINNISTP 906
Cdd:COG3210 739 ATLTLNAGvTITSGNAGTLSIGLTANTTASGTTLTLANANGNTSAGATLDNAGAEISIDITADGTITAAGTTAINVTGSG 818
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 907 VQTNTTNASTStnVANITATSHTSTDDTVPNNTVPVTAIPSLANTGVDTTSNSFSIMTTSFSESTNAMNTTVIMATTSPT 986
Cdd:COG3210 819 GTITINTATTG--LTGTGDTTSGAGGSNTTDTTTGTTSDGASGGGTAGANSGSLAATAASITVGSGGVATSTGTANAGTL 896
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 987 STDVASTNNDASMTNFLLATMSAGNITSNSISITTTSFGNSVPFVTTPSPSTDATTTSNNTNPGMTTYYQTSPTIPTHTL 1066
Cdd:COG3210 897 TNLGTTTNAASGNGAVLATVTATGTGGGGLTGGNAAAGGTGAGNGTTALSGTQGNAGLSAASASDGAGDTGASSAAGSSA 976
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 1067 TSIPSSITSILSMFPTSNTFTTDKITNFTTPTNANTIIFNTLDTKSTMVIDATVTTTSTKDNTMSPDTTVTSIDKFTTHI 1146
Cdd:COG3210 977 VGTSANSAGSTGGVIAATGILVAGNSGTTASTTGGSGAIVAGGNGVTGTTGTASATGTGTAATAGGQNGVGVNASGISGG 1056
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 1147 TQFATPHSATTTTLALSHTSLAPTNLSNLGTMDITDADNSSSVTGNTTHISVSNLTTASVTITATGLDSQTPHMVINSVA 1226
Cdd:COG3210 1057 NAAALTASGTAGTTGGTAASNGGGGTAQASGAGTTHTLGGITNGGATGTSGGTTTSTGGVTASKVGGTTTVGATGTSTAS 1136
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 767949047 1227 TYLPITATSATTDTTNITKYALNTTTPDSTVHTSATAPTYIANAINATQV 1276
Cdd:COG3210 1137 TEAAGAGTLTGLVAVSAVAGGASSASAGDTTAVAAATTTTTGSAINGGAD 1186
|
|
| Chi1 |
COG3469 |
Chitinase [Carbohydrate transport and metabolism]; |
652-845 |
1.43e-03 |
|
Chitinase [Carbohydrate transport and metabolism];
Pssm-ID: 442692 [Multi-domain] Cd Length: 534 Bit Score: 42.82 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 652 NASTNATVPITTTPFPTSTIGVTTNATVPNTTAPFPTNASTASTNATVPITTTCFATSTIGVTTNATVPDTTAPFPTNTT 731
Cdd:COG3469 15 ASATAVTLLGAAATAASVTLTAATATTVVSTTGSVVVAASGSAGSGTGTTAASSTAATSSTTSTTATATAAAAAATSTSA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 732 TASTNATIPITTTPFATSTISVTTSTTVPDTTAPFPTSTTSASTNATPVPITTTLfatSTIGVTTGTTVPDTTAPFPTST 811
Cdd:COG3469 95 TLVATSTASGANTGTSTVTTTSTGAGSVTSTTSSTAGSTTTSGASATSSAGSTTT---TTTVSGTETATGGTTTTSTTTT 171
|
170 180 190
....*....|....*....|....*....|....
gi 767949047 812 TSTSTSATVPITTTPSPTNTADANTSNTVPNTTM 845
Cdd:COG3469 172 TTSASTTPSATTTATATTASGATTPSATTTATTT 205
|
|
| FhaB |
COG3210 |
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ... |
592-1274 |
1.81e-03 |
|
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442443 [Multi-domain] Cd Length: 1698 Bit Score: 42.83 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 592 SPSTTNATSSETITSSASANTTTGTTDTVPITTTSFPSTTSVTTNTTVPDTTSPFPTSTTNASTNATVPITTTPFPTSTI 671
Cdd:COG3210 490 IGTVTTNATISNNAGGDANGIATGLTGITAGGGGGGNATSGGTGGDGTTLSGSGLTTTVSGGASGTTAASGSNTANTLGV 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 672 GVTTNATVPNTTAPFPTNASTASTNATVPITTTCFATSTIGVTTNATVPDTTAPFPTNTTTASTNATIPITTTPFATSTI 751
Cdd:COG3210 570 LAATGGTSNATTAGNSTSATGGTGTNSGGTVLSIGTGSAGATGTITLGAGTSGAGANATGGGAGLTGSAVGAALSGTGSG 649
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 752 SVTTSTTVPDTTAPFPTSTTSASTNATPVPITTTLFATSTIGVTTGTTVPDTTAPFPTSTTSTSTSATVPITTTPSPTNT 831
Cdd:COG3210 650 TTGTASANGSNTTGVNTAGGTGGGTTGTVTSGATGGTTGTTLNAATGGTLNNAGNTLTISTGSITVTGQIGALANANGDT 729
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 832 ADANTSNTVPNTTMPSPTSSTTVSTIATVPISVTPSLTSTADATISTTVLIATTSSLTGTTDVSTSTTINNISTPVQTNT 911
Cdd:COG3210 730 VTFGNLGTGATLTLNAGVTITSGNAGTLSIGLTANTTASGTTLTLANANGNTSAGATLDNAGAEISIDITADGTITAAGT 809
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 912 TNASTSTNVANITATSHTSTDDTVPNNTVPVTAIPSLANTGVDTTSNSFSIMTTSFSESTNAMNTTVIMATTSpTSTDVA 991
Cdd:COG3210 810 TAINVTGSGGTITINTATTGLTGTGDTTSGAGGSNTTDTTTGTTSDGASGGGTAGANSGSLAATAASITVGSG-GVATST 888
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 992 STNNDASMTNFLLATMSAGNITSNSISITTTSFGNSVPFVTTPSPSTDATTTSNNTNPGMTTYYQTSPTIPTHTLTSIPS 1071
Cdd:COG3210 889 GTANAGTLTNLGTTTNAASGNGAVLATVTATGTGGGGLTGGNAAAGGTGAGNGTTALSGTQGNAGLSAASASDGAGDTGA 968
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 1072 SITSILSMFPTSNTFTTDKITNFTTPTNANTIIFNTLDTKSTMVIDATVTTTSTKDNTMSPDTTVTSIDKFTTHITQFAT 1151
Cdd:COG3210 969 SSAAGSSAVGTSANSAGSTGGVIAATGILVAGNSGTTASTTGGSGAIVAGGNGVTGTTGTASATGTGTAATAGGQNGVGV 1048
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 1152 PHSATTTTLALSHTSLAPTNLSNLGTMDITDADNSSSVTGNTTHISVSNLTTASVTITATGLDSQTPHMVINSVATYLPI 1231
Cdd:COG3210 1049 NASGISGGNAAALTASGTAGTTGGTAASNGGGGTAQASGAGTTHTLGGITNGGATGTSGGTTTSTGGVTASKVGGTTTVG 1128
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 767949047 1232 TATSATTDTTNITKYALNTTTPDSTVHTSATAPTYIANAINAT 1274
Cdd:COG3210 1129 ATGTSTASTEAAGAGTLTGLVAVSAVAGGASSASAGDTTAVAA 1171
|
|
| Chi1 |
COG3469 |
Chitinase [Carbohydrate transport and metabolism]; |
975-1159 |
2.29e-03 |
|
Chitinase [Carbohydrate transport and metabolism];
Pssm-ID: 442692 [Multi-domain] Cd Length: 534 Bit Score: 42.05 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 975 NTTVIMATTSPTSTDVASTNNDASMTNFLLATMSAGNITSNSISITTTSFGNSVPFVTTPSPSTDATTTSNNTNPGMTTY 1054
Cdd:COG3469 22 LLGAAATAASVTLTAATATTVVSTTGSVVVAASGSAGSGTGTTAASSTAATSSTTSTTATATAAAAAATSTSATLVATST 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 1055 YQTSPTIPTHTLTSIPSSITSILSmfPTSNTFTTDKITNFTTPTNANTIIFNTLDTKSTMVIDATVTTTSTKDNTMSPDT 1134
Cdd:COG3469 102 ASGANTGTSTVTTTSTGAGSVTST--TSSTAGSTTTSGASATSSAGSTTTTTTVSGTETATGGTTTTSTTTTTTSASTTP 179
|
170 180
....*....|....*....|....*
gi 767949047 1135 TVTSIDKFTTHITQFATPHSATTTT 1159
Cdd:COG3469 180 SATTTATATTASGATTPSATTTATT 204
|
|
| MSCRAMM_ClfA |
NF033609 |
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ... |
922-1105 |
3.34e-03 |
|
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.
Pssm-ID: 468110 [Multi-domain] Cd Length: 934 Bit Score: 41.82 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 922 NITATSHTSTDDTVPNNTVPVTAIPSLANTGVD---TTSNSFSIMT----------TSFSESTNA-MNTTVIMATTSPTS 987
Cdd:NF033609 42 NSVTQSDSASNESKSNDSSSVSAAPKTDDTNVSdtkTSSNTNNGETsvaqnpaqqeTTQSASTNAtTEETPVTGEATTTA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 988 TDVASTNNDASMTNfllatMSAGNITSNSISITTTSFGNSVPFVTTPSPSTDA------------TTTSNNTNPGMTTYY 1055
Cdd:NF033609 122 TNQANTPATTQSSN-----TNAEELVNQTSNETTSNDTNTVSSVNSPQNSTNAenvsttqdtsteATPSNNESAPQSTDA 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767949047 1056 QTSPTIPTHTLTSIPS----SITSILSMFPTSNTFTTDKITNFTTPTNANTIIF 1105
Cdd:NF033609 197 SNKDVVNQAVNTSAPRmrafSLAAVAADAPAAGTDITNQLTNVTVGIDSGTTVY 250
|
|
| PRK10856 |
PRK10856 |
cytoskeleton protein RodZ; |
654-727 |
3.75e-03 |
|
cytoskeleton protein RodZ;
Pssm-ID: 236776 [Multi-domain] Cd Length: 331 Bit Score: 41.17 E-value: 3.75e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767949047 654 STNATVPITTTPFPTSTIGVT-TNATVPNTTAPfPTNASTASTNATVPITTTCFATSTIGVTTNATVPDTTAPFP 727
Cdd:PRK10856 165 DTSTTTDPATTPAPAAPVDTTpTNSQTPAVATA-PAPAVDPQQNAVVAPSQANVDTAATPAPAAPATPDGAAPLP 238
|
|
| Chi1 |
COG3469 |
Chitinase [Carbohydrate transport and metabolism]; |
568-779 |
4.82e-03 |
|
Chitinase [Carbohydrate transport and metabolism];
Pssm-ID: 442692 [Multi-domain] Cd Length: 534 Bit Score: 41.28 E-value: 4.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 568 TWIDGGPVLPTPTKTSTIPMSSHPSPSTTNATSSETITSSASANTTTGTTDTVPITTTSFPSTTSVTTNTTVPDTTSPFP 647
Cdd:COG3469 15 ASATAVTLLGAAATAASVTLTAATATTVVSTTGSVVVAASGSAGSGTGTTAASSTAATSSTTSTTATATAAAAAATSTSA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 648 TSTTNASTNATVPITTTPFPTSTiGVTTNATVPNTTAPFPTNASTASTNATVPITTTCFATSTIGVTTNATVPDTTAPFP 727
Cdd:COG3469 95 TLVATSTASGANTGTSTVTTTST-GAGSVTSTTSSTAGSTTTSGASATSSAGSTTTTTTVSGTETATGGTTTTSTTTTTT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 767949047 728 TNtttastnatipiTTTPFATSTISVTTSTTVPDTTAPFPTSTTSASTNATP 779
Cdd:COG3469 174 SA------------STTPSATTTATATTASGATTPSATTTATTTGPPTPGLP 213
|
|
| 34 |
PHA02584 |
long tail fiber, proximal subunit; Provisional |
859-1139 |
5.44e-03 |
|
long tail fiber, proximal subunit; Provisional
Pssm-ID: 222890 [Multi-domain] Cd Length: 1229 Bit Score: 41.28 E-value: 5.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 859 TVPISVTPSLTSTADATISTTVLIATTSSLTGTTDVSTSTTINNISTP-VQTNTTNASTSTNVANITATSHTSTDDTVPn 937
Cdd:PHA02584 902 DIDQTVNGSLTFTKNTNLSAPLVSSSTATFGGSVTANSTLTTQNTSNGtVVVVDETSIAFYSQNNTTGNIVFNIDGTVD- 980
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 938 nTVPVTAIPSLANTGVDTTSNSfSIMTTSFSESTNAMNTTV---IMATTSPTSTDVASTNNDASMTNFLLATMSAGNITS 1014
Cdd:PHA02584 981 -PINVNANGTLNATGVATNGRA-VYAEGGGIARTNNAARAItggFTIRNDGSTTVFLLTAAGDQTGGFNGLKSLIINNAN 1058
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 1015 NSISITTTSFGNSVPFVTTPSPSTDATTTSNNTNPGMTtyyqTSPTIPTHTLTSIPSSITSILSMFPTSNTFTTDKITNF 1094
Cdd:PHA02584 1059 GQVTINDNYIINAGGTIMSGGLTVNSRIRSQGTKASYT----RAPTADTVGFWSVDINDSATYNQFPGYFQMVTKTKSPG 1134
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 767949047 1095 TTPTNANTIIFNTLDTKSTmviDATVTTTSTKDNTMSPDTTVTSI 1139
Cdd:PHA02584 1135 TLTQFGNTLDSLYQDWSPD---GRTTRYTRTWQKNKNAWTSFGEV 1176
|
|
| PHA03255 |
PHA03255 |
BDLF3; Provisional |
962-1114 |
8.76e-03 |
|
BDLF3; Provisional
Pssm-ID: 165513 [Multi-domain] Cd Length: 234 Bit Score: 39.50 E-value: 8.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949047 962 IMTTSFSESTNAMNTTVIMATTSPT-STDVASTNNDASMTNfllatmsagniTSNSISITTTSFGNSVPFVTTPSPSTDA 1040
Cdd:PHA03255 23 IWTSSGSSTASAGNVTGTTAVTTPSpSASGPSTNQSTTLTT-----------TSAPITTTAILSTNTTTVTSTGTTVTPV 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767949047 1041 TTTSNNTNPGMTTYYQTSPTIPTHTLTSIPSSITSILSMFPTSNTFTTDKITNFTT--PTNANTIIFNTLDTKSTM 1114
Cdd:PHA03255 92 PTTSNASTINVTTKVTAQNITATEAGTGTSTGVTSNVTTRSSSTTSATTRITNATTlaPTLSSKGTSNATKTTAEL 167
|
|
| |
