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Conserved domains on  [gi|767949045|ref|XP_011514995|]
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putative maltase-glucoamylase-like protein FLJ16351 isoform X2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Glyco_hydro_31 pfam01055
Glycosyl hydrolases family 31; Glycosyl hydrolases are key enzymes of carbohydrate metabolism. ...
 316-816 0e+00

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: 588.76  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045   316 YIVLGPTPELVTQQYTELIGRPAMIPYWALGFHLSRYGYQNDAEISSLYDAMVAAQIPYDVQHVDIDYMNRKLDFTL-SA 394
Cdd:pfam01055    1 YFFLGPTPKDVVKQYTELTGRPPLPPYWALGYHQSRWGYKSEEEVLEVVDGFRERDIPLDVIWLDIDYMDGYRDFTWdPE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045   395 NFQNLSLLIEQMKKNGMRFILILDPAISGNETQYLPFIRGQENNVFIKWPDTNDIVWGkvWPDlpnvivdgsldhetqvk 474
Cdd:pfam01055   81 RFPDPKGMVDELHAKGQKLVVIIDPGIKKVDPGYPPYDEGLEKGYFVKNPDGSLYVGG--WPG----------------- 141

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045   475 lyraYVAFPDFFRNSTAAWWKKEIEELYANprepeksLKFDGLWIDMNEPSNFVdGSVRGCSNEMLNNPPYmpylesrdk 554
Cdd:pfam01055  142 ----MSAFPDFTNPEARDWWADQLFKFLLD-------MGVDGIWNDMNEPSVFC-GSGPEDTVAKDNDPGG--------- 200

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045   555 glssktlcmesqqilpdssPVEHYNVHNLYGWSQTRPTYEAVQEVTG-QRGVIITRSTFPSSGRWGGHRLGNNTAAWDQL 633
Cdd:pfam01055  201 -------------------GVEHYDVHNLYGLLMAKATYEGLREKRPnKRPFVLTRSGFAGSQRYAAHWSGDNTSTWEHL 261

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045   634 GKSIIGMMEFSLFGIPYTGADICGFFGDAEYEMCVRWMQLGAFYPFSRNHNNIGTRRQDPVAWNSTFEMLSRKVLETRYT 713
Cdd:pfam01055  262 RFSIPGGLSLGLSGIPFWGADIGGFFNPTTPELYVRWYQLGAFSPFFRNHSSIDTRRREPWLFGEEVEEIIRKAIRLRYR 341

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045   714 LLPYLYTLMHKAHVEGSTVVRPLLHEFTDDRTTWDIDRQFMLGPAILISPVLETSTFEISAYFPRARWYDYsTGTSSTST 793
Cdd:pfam01055  342 LLPYLYTLFYEAHETGLPVMRPLFLEFPDDPNTFDIDDQFMFGPSLLVAPVLEEGATSVDVYLPGGRWYDF-WTGERYEG 420

                          490       500
                   ....*....|....*....|...
gi 767949045   794 GQRKILKAPLDHINLHVRGGYIL 816
Cdd:pfam01055  421 GGTVPVTAPLDRIPLFVRGGSII 443
NtCtMGAM_N pfam16863
N-terminal barrel of NtMGAM and CtMGAM, maltase-glucoamylase; NtCtMGAM_N is a beta-barrel-like ...
 136-229 2.36e-32

N-terminal barrel of NtMGAM and CtMGAM, maltase-glucoamylase; NtCtMGAM_N is a beta-barrel-like structure just N-terminal to the catalytic domain of maltase-glucoamylase in eukaryotes. It contributes to the architecture of the substrate-binding site, by donating a loop that comes into close contact with two regions in the catalytic domain thereby creating the site. This family is frequently found at the N-terminus of Glycosyl hydrolase 31, pfam01055.to which it contributes as above.


:

Pssm-ID: 465286  Cd Length: 113  Bit Score: 122.20  E-value: 2.36e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045   136 ISFLHLKVIYHTATMLQVKIYDPTNKRYEVPVPLNTPPQPVGDPENRLYDVRIQNNPFGIQIQRKNSSTVIWDSQLPGFI 215
Cdd:pfam16863   20 IETLKLTVEYQTDNRLHVKITDPNNKRYEVPEELLPRPSPSSSASDSLYEFEYTNEPFGFKVTRKSTGEVLFDTSGGPLV 99

                           90
                   ....*....|....
gi 767949045   216 FNDMFLSISTRLPS 229
Cdd:pfam16863  100 FEDQFLQLSTRLPS 113
GH31_N cd14752
N-terminal domain of glycosyl hydrolase family 31 (GH31); This family is found N-terminal to ...
 221-335 6.15e-24

N-terminal domain of glycosyl hydrolase family 31 (GH31); This family is found N-terminal to the glycosyl-hydrolase domain of Glycoside hydrolase family 31 (GH31). GH31 includes the glycoside hydrolases alpha-glucosidase (EC 3.2.1.20), alpha-1,3-glucosidase (EC 3.2.1.84), alpha-xylosidase (EC 3.2.1.177), sucrase-isomaltase (EC 3.2.1.48 and EC 3.2.1.10), as well as alpha-glucan lyase (EC 4.2.2.13). 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 of the catalytic domain have been identified as the catalytic nucleophile and the acid/base, respectively. A loop of the N-terminal beta-sandwich domain is part of the active site pocket.


:

Pssm-ID: 270212 [Multi-domain]  Cd Length: 122  Bit Score: 98.41  E-value: 6.15e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  221 LSISTRLP-SQYIYGFGEteHTTfRRNMNWNTWGMFAHD--EPPAYKKNSYGVHPYYMALEedgsAHGVLLLNSNAMDVT 297
Cdd:cd14752    10 LRLSFKLPpDEHFYGLGE--RFG-GLNKRGKRYRLWNTDqgGYRGSTDPLYGSIPFYLSSK----GYGVFLDNPSRTEFD 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 767949045  298 LQPT--PALTYRTTGGILDFYIVLGPTPELVTQQYTELIG 335
Cdd:cd14752    83 FGSEdsDELTFSSEGGDLDYYFFAGPTPKEVIEQYTELTG 122
COG4625 COG4625
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ...
 1071-1613 6.02e-12

Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function unknown];


:

Pssm-ID: 443664 [Multi-domain]  Cd Length: 900  Bit Score: 70.96  E-value: 6.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1071 TNASTASTNATVPITTTCFATSTIGVTTNATVPDTTAPFPTNTTTASTNATIPITTTPFATSTISVTTSTTVPDTTAPFP 1150
Cdd:COG4625     1 GGGGGGGGGGGGGGGGTGGGGAGGGGGAGGGAGGGGAGGGGGGGGGGGGAGGGGGGGGTGGGGGGGGGGGGGGAGGGGGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1151 TSTTSASTNATPVPITTTLFATSTIGVTTGTTVPDTTAPFPTSTTSTSTSATVPITTTPSPTNTADANTSNTVPNTTMPS 1230
Cdd:COG4625    81 GGGGGGGGGTGGVGGGGGGGGGGGGGGGGGGGGGGGGSAGGGGGGAGGAGGGGGGGAGGGGGGGGGGGAGGGGGGGAGGA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1231 PTSSTTVSTIATVPISVTPSLTSTADATISTTVLIATTSSLTGTTDVSTSTTINNISTPVQTNTTNASTSTNVANITATS 1310
Cdd:COG4625   161 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGNGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGGGGGGGGGGGG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1311 HTSTDDTVPNNTVPVTAIPSLANTGVDTTSNSFSIMTTSFSESTNAMNTTVIMATTSPTSTDVASTNNDASMTNFLLATM 1390
Cdd:COG4625   241 GGGGGGGAGGGGGGGGGNGGGGGAGGGGGGGGGGSGGGGGGGGGGGSGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGG 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1391 SAGNITSNSISITTTSFGNSVPFVTTpspSTDATTTSNNTNPGMTTYYQTSPTIPTHTLTSIPSSITSILSMFPTSNTFT 1470
Cdd:COG4625   321 GGGGGGGGGGGGGAGGGGGSGGAGAG---GGGAGGGGAGGGGGGGTGGGGGGGGGGGGGSGGGGAGGGGGSGGGGGGGAG 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1471 TDKITNFTTPTNANTIIFNTLDTKSTMVIDATVTTTSTKDNTMSPDTTVTSIDKFTTHITQFATPHSATTTTLALSHTSL 1550
Cdd:COG4625   398 GGGGGGGAGGTGGGGAGGGGGAAGGGGGGTGAGGGGGGGGTGAGGGGATGGGGGGGGGAGGSGGGAGAGGGSGSGAGTLT 477

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767949045 1551 APTNLSNLGTMDITDADNSSSVTGNTTHISVSnlTTASVTITATGLDSQTPHMVINSVATYLP 1613
Cdd:COG4625   478 LTGNNTYTGTTTVNGGGNYTQSAGSTLAVEVD--AANSDRLVVTGTATLNGGTVVVLAGGYAP 538
PD smart00018
P or trefoil or TFF domain; Proposed role in renewal and pathology of mucous epithelia.
 53-93 3.07e-10

P or trefoil or TFF domain; Proposed role in renewal and pathology of mucous epithelia.


:

Pssm-ID: 197472  Cd Length: 46  Bit Score: 57.01  E-value: 3.07e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 767949045     53 VSDLEKFNCYPDDPTASEesCRQRGCLWeDTSTPGVPTCYY 93
Cdd:smart00018    5 VPPSERINCGPPGITEAE--CEARGCCF-DSSISGVPWCFY 42
Chi1 super family cl43877
Chitinase [Carbohydrate transport and metabolism];
950-1162 6.57e-05

Chitinase [Carbohydrate transport and metabolism];


The actual alignment was detected with superfamily member COG3469:

Pssm-ID: 442692 [Multi-domain]  Cd Length: 534  Bit Score: 47.44  E-value: 6.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  950 VTWIDGGPVLPTPTKTSTIPMSSHPSPSTTNATSSETITSSASANTTTGTTDTVPITTTSFPSTTSVTTNTTVPDTTSPF 1029
Cdd:COG3469     4 VSTAASPTAGGASATAVTLLGAAATAASVTLTAATATTVVSTTGSVVVAASGSAGSGTGTTAASSTAATSSTTSTTATAT 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1030 ptsttnASTNATVPITTTPFPTSTIGVTTNATVPNTTAPFPTNASTASTNATVPITTTCFATSTIGVTTNATVPDTTAPF 1109
Cdd:COG3469    84 ------AAAAAATSTSATLVATSTASGANTGTSTVTTTSTGAGSVTSTTSSTAGSTTTSGASATSSAGSTTTTTTVSGTE 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767949045 1110 PTNTTTASTNATIPITTTPFATSTISVTTSTTVPDTTAPFPTSTTSASTNATP 1162
Cdd:COG3469   158 TATGGTTTTSTTTTTTSASTTPSATTTATATTASGATTPSATTTATTTGPPTP 210
 
Name Accession Description Interval E-value
Glyco_hydro_31 pfam01055
Glycosyl hydrolases family 31; Glycosyl hydrolases are key enzymes of carbohydrate metabolism. ...
 316-816 0e+00

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: 588.76  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045   316 YIVLGPTPELVTQQYTELIGRPAMIPYWALGFHLSRYGYQNDAEISSLYDAMVAAQIPYDVQHVDIDYMNRKLDFTL-SA 394
Cdd:pfam01055    1 YFFLGPTPKDVVKQYTELTGRPPLPPYWALGYHQSRWGYKSEEEVLEVVDGFRERDIPLDVIWLDIDYMDGYRDFTWdPE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045   395 NFQNLSLLIEQMKKNGMRFILILDPAISGNETQYLPFIRGQENNVFIKWPDTNDIVWGkvWPDlpnvivdgsldhetqvk 474
Cdd:pfam01055   81 RFPDPKGMVDELHAKGQKLVVIIDPGIKKVDPGYPPYDEGLEKGYFVKNPDGSLYVGG--WPG----------------- 141

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045   475 lyraYVAFPDFFRNSTAAWWKKEIEELYANprepeksLKFDGLWIDMNEPSNFVdGSVRGCSNEMLNNPPYmpylesrdk 554
Cdd:pfam01055  142 ----MSAFPDFTNPEARDWWADQLFKFLLD-------MGVDGIWNDMNEPSVFC-GSGPEDTVAKDNDPGG--------- 200

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045   555 glssktlcmesqqilpdssPVEHYNVHNLYGWSQTRPTYEAVQEVTG-QRGVIITRSTFPSSGRWGGHRLGNNTAAWDQL 633
Cdd:pfam01055  201 -------------------GVEHYDVHNLYGLLMAKATYEGLREKRPnKRPFVLTRSGFAGSQRYAAHWSGDNTSTWEHL 261

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045   634 GKSIIGMMEFSLFGIPYTGADICGFFGDAEYEMCVRWMQLGAFYPFSRNHNNIGTRRQDPVAWNSTFEMLSRKVLETRYT 713
Cdd:pfam01055  262 RFSIPGGLSLGLSGIPFWGADIGGFFNPTTPELYVRWYQLGAFSPFFRNHSSIDTRRREPWLFGEEVEEIIRKAIRLRYR 341

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045   714 LLPYLYTLMHKAHVEGSTVVRPLLHEFTDDRTTWDIDRQFMLGPAILISPVLETSTFEISAYFPRARWYDYsTGTSSTST 793
Cdd:pfam01055  342 LLPYLYTLFYEAHETGLPVMRPLFLEFPDDPNTFDIDDQFMFGPSLLVAPVLEEGATSVDVYLPGGRWYDF-WTGERYEG 420

                          490       500
                   ....*....|....*....|...
gi 767949045   794 GQRKILKAPLDHINLHVRGGYIL 816
Cdd:pfam01055  421 GGTVPVTAPLDRIPLFVRGGSII 443
GH31_MGAM_SI_GAA cd06602
maltase-glucoamylase, sucrase-isomaltase, lysosomal acid alpha-glucosidase; This subgroup ...
 335-726 0e+00

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: 554.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  335 GRPAMIPYWALGFHLSRYGYQNDAEISSLYDAMVAAQIPYDVQHVDIDYMNRKLDFTLS-ANFQNLSLLIEQMKKNGMRF 413
Cdd:cd06602     1 GRPAMPPYWSLGFHLCRWGYKNLDELKEVVERYRAAGIPLDVQWNDIDYMDRYRDFTLDpVNFPGLPAFVDDLHANGQHY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  414 ILILDPAISGNETQ-YLPFIRGQENNVFIKWPDTNDIVwGKVWPDlpnvivdgsldhetqvklyraYVAFPDFFRNSTAA 492
Cdd:cd06602    81 VPILDPGISANESGgYPPYDRGLEMDVFIKNDDGSPYV-GKVWPG---------------------YTVFPDFTNPNTQE 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  493 WWKKEIEELYanprepeKSLKFDGLWIDMNEPSNFVDGSV------RGCSNEMLNNPPYMPYLeSRDKGLSSKTLCMESQ 566
Cdd:cd06602   139 WWTEEIKDFH-------DQVPFDGLWIDMNEPSNFCTGSCgnspnaPGCPDNKLNNPPYVPNN-LGGGSLSDKTICMDAV 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  567 QilpdSSPVEHYNVHNLYGWSQTRPTYEAVQEV-TGQRGVIITRSTFPSSGRWGGHRLGNNTAAWDQLGKSIIGMMEFSL 645
Cdd:cd06602   211 H----YDGGLHYDVHNLYGLSEAIATYKALKEIfPGKRPFIISRSTFPGSGKYAGHWLGDNYSTWEDMRYSIPGMLEFNL 286

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  646 FGIPYTGADICGFFGDAEYEMCVRWMQLGAFYPFSRNHNNIGTRRQDPVAWNSTFEMLSRKVLETRYTLLPYLYTLMHKA 725
Cdd:cd06602   287 FGIPMVGADICGFNGNTTEELCARWMQLGAFYPFSRNHNDIGAIDQEPYVWGPSVADASRKALLIRYSLLPYLYTLFYRA 366


                  .
gi 767949045  726 H 726
Cdd:cd06602   367 H 367
YicI COG1501
Alpha-glucosidase/xylosidase, GH31 family [Carbohydrate transport and metabolism];
228-857 6.74e-90

Alpha-glucosidase/xylosidase, GH31 family [Carbohydrate transport and metabolism];


Pssm-ID: 441110 [Multi-domain]  Cd Length: 609  Bit Score: 305.93  E-value: 6.74e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  228 PSQYIYGFGE---TEHTTFRRNMNWNTWGMFAHDEPPAYKknsygVHPYYMALEEDGsahgvLLLNSNAM---DVTLQPT 301
Cdd:COG1501    60 LGEQIYGLGErftTLHKRGRIVVNWNLDHGGHKDNGNTYA-----PIPFYVSSKGYG-----VFVNSASYvtfDVGSAYS 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  302 PALTYRTTGGILDFYIVLGPTPELVTQQYTELIGRPAMIPYWALGFHLSRYGYQNDAEISSLYDAMVAAQIPYDVQHVDI 381
Cdd:COG1501   130 DLVEFTVPGDSLEFYVIEGPSPEDVLEKYTELTGKPPLPPRWAFGYWQSRKSYYDQDQVLAFADEFRDRGFPLDVIHLDI 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  382 DYMNRKL--DFTLSAN-FQNLSLLIEQMKKNGMRFILILDPAISgneTQYLPFIRGQENnvFIKWPdtNDIVW-GKVWPD 457
Cdd:COG1501   210 RWMDKYYwgDFEWDPRrFPDPKAMVKELHDRGVKLVLWINPYVA---PDSAIFAEGMAN--FVKIA--SGTVFvGKMWPG 282

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  458 lpnvivdgsldhetqvklyraYVAFPDFFRNSTAAWWKKEIEELYAnprepekSLKFDGLWIDMNEPsnfvdgsvrgcsn 537
Cdd:COG1501   283 ---------------------TTGLLDFTRPDAREWFWAGLEKELL-------SIGVDGIKLDMNEG------------- 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  538 emlnnppyMPylesrdkglssktlcmESQQILPDSSPVEhynVHNLYGWSQTRPTYEAVQEVTGQRGVIITRSTFPSSGR 617
Cdd:COG1501   322 --------WP----------------TDVATFPSNVPQQ---MRNLYGLLEAKATFEGFRTSRNNRTFILTRSGFAGGQR 374

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  618 WGGHRLGNNTAAWDQLGKSIIGMMEFSLFGIPYTGADICGFFGDAEYEMCVRWMQLGAFYPFSRNHNNigTRRQDPVAWN 697
Cdd:COG1501   375 YPVIWTGDNTSSWESLEDQLTQGLNLSLSGVPFWTPDIGGFFGSPSRELWIRWFQVGAFSPFARIHGW--ASSTEPWFFD 452

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  698 STFEMLSRKVLETRYTLLPYLYTLMHKAHVEGSTVVRPLLHEFTDDRTTWDIDRQFMLGPAILISPVLeTSTFEISAYFP 777
Cdd:COG1501   453 EEAKQIVKEYAQLRYRLLPYIYSLFAKASTDGTPVIRPLFLEFPDDPTTRFIDDQYMFGEYLLVAPIF-AGTESRLVYLP 531

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  778 RARWYDYSTGTSSTSTGQRKIlKAPLDHINLHVRGGYILPWQePAMNtHSSRQNFMGLIVALDDNGTAEGQVFWDDGQSI 857
Cdd:COG1501   532 KGKWYDFWTGELIEGGQWITV-TAPLDRLPLYVRDGSIIPLG-PVSL-RPSMQKIDGIELRVYGSGETAYTLYDDDGETV 608
PLN02763 PLN02763
hydrolase, hydrolyzing O-glycosyl compounds
 233-874 6.96e-77

hydrolase, hydrolyzing O-glycosyl compounds


Pssm-ID: 215408 [Multi-domain]  Cd Length: 978  Bit Score: 277.16  E-value: 6.96e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  233 YGFGETE---HTTFRRNMNWNT--WGmfahdeppaYKKNS---YGVHPYYMALEEDGSAHGVLLLNSNAMDVTLQPTPAL 304
Cdd:PLN02763   77 YGTGEVSgplERTGKRVYTWNTdaWG---------YGQNTtslYQSHPWVFVVLPNGEALGVLADTTRRCEIDLRKESII 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  305 TYRTTGgildFY--IVLGP--TPELVTQQYTELIGRPAMIPYWALGFHLSRYGYQNDAEISSLYDAMVAAQIPYDVQHVD 380
Cdd:PLN02763  148 RIIAPA----SYpvITFGPfpSPEALLTSLSHAIGTVFMPPKWALGYQQCRWSYESAKRVAEIARTFREKKIPCDVVWMD 223

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  381 IDYMNRKLDFTLSAN-FQNLSLLIEQMKKNGMRFILILDPAISgNETQYLPFIRGQENNVFIKWPDTNDIVwGKVWPDLp 459
Cdd:PLN02763  224 IDYMDGFRCFTFDKErFPDPKGLADDLHSIGFKAIWMLDPGIK-AEEGYFVYDSGCENDVWIQTADGKPFV-GEVWPGP- 300

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  460 nvivdgsldhetqvklyrayVAFPDFFRNSTAAWWKKEIEELYANprepekslKFDGLWIDMNEPSNFvdgsvRGCSNEM 539
Cdd:PLN02763  301 --------------------CVFPDFTNKKTRSWWANLVKDFVSN--------GVDGIWNDMNEPAVF-----KTVTKTM 347

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  540 LNNPPYMPYLESrdKGLSSKTlcmesqqilpdsspveHYnvHNLYGWSQTRPTYEAVQEV-TGQRGVIITRSTFPSSGRW 618
Cdd:PLN02763  348 PETNIHRGDEEL--GGVQNHS----------------HY--HNVYGMLMARSTYEGMLLAnKNKRPFVLTRAGFIGSQRY 407

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  619 GGHRLGNNTAAWDQLGKSIIGMMEFSLFGIPYTGADICGFFGDAEYEMCVRWMQLGAFYPFSRNHNNIGTRRQDPVAWNS 698
Cdd:PLN02763  408 AATWTGDNLSNWEHLHMSIPMVLQLGLSGQPLSGPDIGGFAGDATPKLFGRWMGVGAMFPFARGHSEQGTIDHEPWSFGE 487

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  699 TFEMLSRKVLETRYTLLPYLYTLMHKAHVEGSTVVRPLLHEFTDDRTTWDIDRQFMLGPA-ILISPVLETSTFEISAYFP 777
Cdd:PLN02763  488 ECEEVCRLALKRRYRLLPHFYTLFYKAHTTGLPVMTPIFFADPKDPSLRKVENSFLLGPLlISASTLPDQGSDNLQHVLP 567

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  778 RARW--YDYSTgtsststgqrkilkaplDHINL---HVRGGYILPWQEPAMNT-HSSRQNFMGLIVALDDNGTAEGQVFW 851
Cdd:PLN02763  568 KGIWqrFDFDD-----------------SHPDLpllYLQGGSIIPLGPPIQHVgEASLSDDLTLLIALDENGKAEGVLYE 630

                         650       660
                  ....*....|....*....|...
gi 767949045  852 DDGQSIDtYENGNYFLANFIAAQ 874
Cdd:PLN02763  631 DDGDGFG-YTKGDYLLTHYEAEL 652
NtCtMGAM_N pfam16863
N-terminal barrel of NtMGAM and CtMGAM, maltase-glucoamylase; NtCtMGAM_N is a beta-barrel-like ...
 136-229 2.36e-32

N-terminal barrel of NtMGAM and CtMGAM, maltase-glucoamylase; NtCtMGAM_N is a beta-barrel-like structure just N-terminal to the catalytic domain of maltase-glucoamylase in eukaryotes. It contributes to the architecture of the substrate-binding site, by donating a loop that comes into close contact with two regions in the catalytic domain thereby creating the site. This family is frequently found at the N-terminus of Glycosyl hydrolase 31, pfam01055.to which it contributes as above.


Pssm-ID: 465286  Cd Length: 113  Bit Score: 122.20  E-value: 2.36e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045   136 ISFLHLKVIYHTATMLQVKIYDPTNKRYEVPVPLNTPPQPVGDPENRLYDVRIQNNPFGIQIQRKNSSTVIWDSQLPGFI 215
Cdd:pfam16863   20 IETLKLTVEYQTDNRLHVKITDPNNKRYEVPEELLPRPSPSSSASDSLYEFEYTNEPFGFKVTRKSTGEVLFDTSGGPLV 99

                           90
                   ....*....|....
gi 767949045   216 FNDMFLSISTRLPS 229
Cdd:pfam16863  100 FEDQFLQLSTRLPS 113
GH31_N cd14752
N-terminal domain of glycosyl hydrolase family 31 (GH31); This family is found N-terminal to ...
 221-335 6.15e-24

N-terminal domain of glycosyl hydrolase family 31 (GH31); This family is found N-terminal to the glycosyl-hydrolase domain of Glycoside hydrolase family 31 (GH31). GH31 includes the glycoside hydrolases alpha-glucosidase (EC 3.2.1.20), alpha-1,3-glucosidase (EC 3.2.1.84), alpha-xylosidase (EC 3.2.1.177), sucrase-isomaltase (EC 3.2.1.48 and EC 3.2.1.10), as well as alpha-glucan lyase (EC 4.2.2.13). 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 of the catalytic domain have been identified as the catalytic nucleophile and the acid/base, respectively. A loop of the N-terminal beta-sandwich domain is part of the active site pocket.


Pssm-ID: 270212 [Multi-domain]  Cd Length: 122  Bit Score: 98.41  E-value: 6.15e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  221 LSISTRLP-SQYIYGFGEteHTTfRRNMNWNTWGMFAHD--EPPAYKKNSYGVHPYYMALEedgsAHGVLLLNSNAMDVT 297
Cdd:cd14752    10 LRLSFKLPpDEHFYGLGE--RFG-GLNKRGKRYRLWNTDqgGYRGSTDPLYGSIPFYLSSK----GYGVFLDNPSRTEFD 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 767949045  298 LQPT--PALTYRTTGGILDFYIVLGPTPELVTQQYTELIG 335
Cdd:cd14752    83 FGSEdsDELTFSSEGGDLDYYFFAGPTPKEVIEQYTELTG 122
COG4625 COG4625
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ...
 1071-1613 6.02e-12

Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function unknown];


Pssm-ID: 443664 [Multi-domain]  Cd Length: 900  Bit Score: 70.96  E-value: 6.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1071 TNASTASTNATVPITTTCFATSTIGVTTNATVPDTTAPFPTNTTTASTNATIPITTTPFATSTISVTTSTTVPDTTAPFP 1150
Cdd:COG4625     1 GGGGGGGGGGGGGGGGTGGGGAGGGGGAGGGAGGGGAGGGGGGGGGGGGAGGGGGGGGTGGGGGGGGGGGGGGAGGGGGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1151 TSTTSASTNATPVPITTTLFATSTIGVTTGTTVPDTTAPFPTSTTSTSTSATVPITTTPSPTNTADANTSNTVPNTTMPS 1230
Cdd:COG4625    81 GGGGGGGGGTGGVGGGGGGGGGGGGGGGGGGGGGGGGSAGGGGGGAGGAGGGGGGGAGGGGGGGGGGGAGGGGGGGAGGA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1231 PTSSTTVSTIATVPISVTPSLTSTADATISTTVLIATTSSLTGTTDVSTSTTINNISTPVQTNTTNASTSTNVANITATS 1310
Cdd:COG4625   161 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGNGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGGGGGGGGGGGG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1311 HTSTDDTVPNNTVPVTAIPSLANTGVDTTSNSFSIMTTSFSESTNAMNTTVIMATTSPTSTDVASTNNDASMTNFLLATM 1390
Cdd:COG4625   241 GGGGGGGAGGGGGGGGGNGGGGGAGGGGGGGGGGSGGGGGGGGGGGSGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGG 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1391 SAGNITSNSISITTTSFGNSVPFVTTpspSTDATTTSNNTNPGMTTYYQTSPTIPTHTLTSIPSSITSILSMFPTSNTFT 1470
Cdd:COG4625   321 GGGGGGGGGGGGGAGGGGGSGGAGAG---GGGAGGGGAGGGGGGGTGGGGGGGGGGGGGSGGGGAGGGGGSGGGGGGGAG 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1471 TDKITNFTTPTNANTIIFNTLDTKSTMVIDATVTTTSTKDNTMSPDTTVTSIDKFTTHITQFATPHSATTTTLALSHTSL 1550
Cdd:COG4625   398 GGGGGGGAGGTGGGGAGGGGGAAGGGGGGTGAGGGGGGGGTGAGGGGATGGGGGGGGGAGGSGGGAGAGGGSGSGAGTLT 477

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767949045 1551 APTNLSNLGTMDITDADNSSSVTGNTTHISVSnlTTASVTITATGLDSQTPHMVINSVATYLP 1613
Cdd:COG4625   478 LTGNNTYTGTTTVNGGGNYTQSAGSTLAVEVD--AANSDRLVVTGTATLNGGTVVVLAGGYAP 538
PD smart00018
P or trefoil or TFF domain; Proposed role in renewal and pathology of mucous epithelia.
 53-93 3.07e-10

P or trefoil or TFF domain; Proposed role in renewal and pathology of mucous epithelia.


Pssm-ID: 197472  Cd Length: 46  Bit Score: 57.01  E-value: 3.07e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 767949045     53 VSDLEKFNCYPDDPTASEesCRQRGCLWeDTSTPGVPTCYY 93
Cdd:smart00018    5 VPPSERINCGPPGITEAE--CEARGCCF-DSSISGVPWCFY 42
Trefoil cd00111
P or trefoil or TFF domain; Trefoil factor family domain peptides are mucin-associated ...
 52-93 1.04e-09

P or trefoil or TFF domain; Trefoil factor family domain peptides are mucin-associated molecules, largely found in epithelia of gastrointestinal tissues. Function is not known but it was originally identified from mucosal tissues, where it may have a regulatory or structural role and has also been implicated as a growth fractor in other tissues.The domain is found in 1 to 6 copies where it occurs.


Pssm-ID: 238059  Cd Length: 44  Bit Score: 55.43  E-value: 1.04e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 767949045   52 PVSDLEKFNCYPDDPTASEesCRQRGCLWeDTSTPGVPTCYY 93
Cdd:cd00111     4 SVPPSERIDCGPPGITQEE--CEARGCCF-DPSISGVPWCFY 42
Trefoil pfam00088
Trefoil (P-type) domain;
53-93 1.72e-09

Trefoil (P-type) domain;


Pssm-ID: 459666  Cd Length: 43  Bit Score: 54.63  E-value: 1.72e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 767949045    53 VSDLEKFNCYPddPTASEESCRQRGCLWEDTSTPGVPTCYY 93
Cdd:pfam00088    4 VPPSDRFDCGY--PGITQEECEARGCCWDPSVDPGVPWCFY 42
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 1066-1458 1.63e-06

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: 53.00  E-value: 1.63e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  1066 TAPFPTNASTASTNATVPITTTCFATSTIGVTTNATVPDTTAPFPTNTTTASTNATIPITTTPFATSTISVTTSTTVpdt 1145
Cdd:pfam05109  398 TAPKTLIITRTATNATTTTHKVIFSKAPESTTTSPTLNTTGFAAPNTTTGLPSSTHVPTNLTAPASTGPTVSTADVT--- 474

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  1146 tAPFPTSTTSASTNATPVPitttlfatstigvttgttvpdttAPFPTSTTSTSTSATVPITTTPSPTNTADANT---SNT 1222
Cdd:pfam05109  475 -SPTPAGTTSGASPVTPSP-----------------------SPRDNGTESKAPDMTSPTSAVTTPTPNATSPTpavTTP 530

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  1223 VPNTTMPSPTSSTTVSTIAT-VPISVTPS---LTSTADATISTTVLIATTSSLTGTTDVSTSTTINNIStpvqtnttnas 1298
Cdd:pfam05109  531 TPNATSPTLGKTSPTSAVTTpTPNATSPTpavTTPTPNATIPTLGKTSPTSAVTTPTPNATSPTVGETS----------- 599

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  1299 tstnvANITATSHTSTDDTvpnNTVPVTAIPSLANTGVDTTSNSFsimtTSFSESTNAMNTTVIMATTSPTSTDVASTNN 1378
Cdd:pfam05109  600 -----PQANTTNHTLGGTS---STPVVTSPPKNATSAVTTGQHNI----TSSSTSSMSLRPSSISETLSPSTSDNSTSHM 667

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  1379 DASMTNFLLATMSAGNITSNSISITTTSFGNSVPFVTTPSPSTDATTTSNNTNPGMTTYYQ-------TSPTIPTHTLTS 1451
Cdd:pfam05109  668 PLLTSAHPTGGENITQVTPASTSTHHVSTSSPAPRPGTTSQASGPGNSSTSTKPGEVNVTKgtppknaTSPQAPSGQKTA 747


                   ....*..
gi 767949045  1452 IPSSITS 1458
Cdd:pfam05109  748 VPTVTST 754
PHA03255 PHA03255
BDLF3; Provisional
 1345-1497 5.92e-05

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 46.44  E-value: 5.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1345 IMTTSFSESTNAMNTTVIMATTSPT-STDVASTNNDASMTNfllatmsagniTSNSISITTTSFGNSVPFVTTPSPSTDA 1423
Cdd:PHA03255   23 IWTSSGSSTASAGNVTGTTAVTTPSpSASGPSTNQSTTLTT-----------TSAPITTTAILSTNTTTVTSTGTTVTPV 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767949045 1424 TTTSNNTNPGMTTYYQTSPTIPTHTLTSIPSSITSILSMFPTSNTFTTDKITNFTT--PTNANTIIFNTLDTKSTM 1497
Cdd:PHA03255   92 PTTSNASTINVTTKVTAQNITATEAGTGTSTGVTSNVTTRSSSTTSATTRITNATTlaPTLSSKGTSNATKTTAEL 167
Chi1 COG3469
Chitinase [Carbohydrate transport and metabolism];
950-1162 6.57e-05

Chitinase [Carbohydrate transport and metabolism];


Pssm-ID: 442692 [Multi-domain]  Cd Length: 534  Bit Score: 47.44  E-value: 6.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  950 VTWIDGGPVLPTPTKTSTIPMSSHPSPSTTNATSSETITSSASANTTTGTTDTVPITTTSFPSTTSVTTNTTVPDTTSPF 1029
Cdd:COG3469     4 VSTAASPTAGGASATAVTLLGAAATAASVTLTAATATTVVSTTGSVVVAASGSAGSGTGTTAASSTAATSSTTSTTATAT 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1030 ptsttnASTNATVPITTTPFPTSTIGVTTNATVPNTTAPFPTNASTASTNATVPITTTCFATSTIGVTTNATVPDTTAPF 1109
Cdd:COG3469    84 ------AAAAAATSTSATLVATSTASGANTGTSTVTTTSTGAGSVTSTTSSTAGSTTTSGASATSSAGSTTTTTTVSGTE 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767949045 1110 PTNTTTASTNATIPITTTPFATSTISVTTSTTVPDTTAPFPTSTTSASTNATP 1162
Cdd:COG3469   158 TATGGTTTTSTTTTTTSASTTPSATTTATATTASGATTPSATTTATTTGPPTP 210
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 1305-1488 1.89e-04

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: 46.44  E-value: 1.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1305 NITATSHTSTDDTVPNNTVPVTAIPSLANTGVD---TTSNSFSIMT----------TSFSESTNA-MNTTVIMATTSPTS 1370
Cdd:NF033609   42 NSVTQSDSASNESKSNDSSSVSAAPKTDDTNVSdtkTSSNTNNGETsvaqnpaqqeTTQSASTNAtTEETPVTGEATTTA 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1371 TDVAST--NNDASMTNfllaTMSAGNITSNSisiTTTSFGNSVPFVTTPSPSTDA------------TTTSNNTNPGMTT 1436
Cdd:NF033609  122 TNQANTpaTTQSSNTN----AEELVNQTSNE---TTSNDTNTVSSVNSPQNSTNAenvsttqdtsteATPSNNESAPQST 194

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767949045 1437 YYQTSPTIPTHTLTSIPS----SITSILSMFPTSNTFTTDKITNFTTPTNANTIIF 1488
Cdd:NF033609  195 DASNKDVVNQAVNTSAPRmrafSLAAVAADAPAAGTDITNQLTNVTVGIDSGTTVY 250
PRK10856 PRK10856
cytoskeleton protein RodZ;
1035-1104 8.24e-03

cytoskeleton protein RodZ;


Pssm-ID: 236776 [Multi-domain]  Cd Length: 331  Bit Score: 40.39  E-value: 8.24e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1035 NASTNATVPITTTPfPTSTIGVTTNATVPNTTAPFPTNASTASTNATVPITTTCFATSTIGVTTNATVPD 1104
Cdd:PRK10856  184 TTPTNSQTPAVATA-PAPAVDPQQNAVVAPSQANVDTAATPAPAAPATPDGAAPLPTDQAGVSTPAADPN 252
 
Name Accession Description Interval E-value
Glyco_hydro_31 pfam01055
Glycosyl hydrolases family 31; Glycosyl hydrolases are key enzymes of carbohydrate metabolism. ...
 316-816 0e+00

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: 588.76  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045   316 YIVLGPTPELVTQQYTELIGRPAMIPYWALGFHLSRYGYQNDAEISSLYDAMVAAQIPYDVQHVDIDYMNRKLDFTL-SA 394
Cdd:pfam01055    1 YFFLGPTPKDVVKQYTELTGRPPLPPYWALGYHQSRWGYKSEEEVLEVVDGFRERDIPLDVIWLDIDYMDGYRDFTWdPE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045   395 NFQNLSLLIEQMKKNGMRFILILDPAISGNETQYLPFIRGQENNVFIKWPDTNDIVWGkvWPDlpnvivdgsldhetqvk 474
Cdd:pfam01055   81 RFPDPKGMVDELHAKGQKLVVIIDPGIKKVDPGYPPYDEGLEKGYFVKNPDGSLYVGG--WPG----------------- 141

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045   475 lyraYVAFPDFFRNSTAAWWKKEIEELYANprepeksLKFDGLWIDMNEPSNFVdGSVRGCSNEMLNNPPYmpylesrdk 554
Cdd:pfam01055  142 ----MSAFPDFTNPEARDWWADQLFKFLLD-------MGVDGIWNDMNEPSVFC-GSGPEDTVAKDNDPGG--------- 200

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045   555 glssktlcmesqqilpdssPVEHYNVHNLYGWSQTRPTYEAVQEVTG-QRGVIITRSTFPSSGRWGGHRLGNNTAAWDQL 633
Cdd:pfam01055  201 -------------------GVEHYDVHNLYGLLMAKATYEGLREKRPnKRPFVLTRSGFAGSQRYAAHWSGDNTSTWEHL 261

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045   634 GKSIIGMMEFSLFGIPYTGADICGFFGDAEYEMCVRWMQLGAFYPFSRNHNNIGTRRQDPVAWNSTFEMLSRKVLETRYT 713
Cdd:pfam01055  262 RFSIPGGLSLGLSGIPFWGADIGGFFNPTTPELYVRWYQLGAFSPFFRNHSSIDTRRREPWLFGEEVEEIIRKAIRLRYR 341

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045   714 LLPYLYTLMHKAHVEGSTVVRPLLHEFTDDRTTWDIDRQFMLGPAILISPVLETSTFEISAYFPRARWYDYsTGTSSTST 793
Cdd:pfam01055  342 LLPYLYTLFYEAHETGLPVMRPLFLEFPDDPNTFDIDDQFMFGPSLLVAPVLEEGATSVDVYLPGGRWYDF-WTGERYEG 420

                          490       500
                   ....*....|....*....|...
gi 767949045   794 GQRKILKAPLDHINLHVRGGYIL 816
Cdd:pfam01055  421 GGTVPVTAPLDRIPLFVRGGSII 443
GH31_MGAM_SI_GAA cd06602
maltase-glucoamylase, sucrase-isomaltase, lysosomal acid alpha-glucosidase; This subgroup ...
 335-726 0e+00

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: 554.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  335 GRPAMIPYWALGFHLSRYGYQNDAEISSLYDAMVAAQIPYDVQHVDIDYMNRKLDFTLS-ANFQNLSLLIEQMKKNGMRF 413
Cdd:cd06602     1 GRPAMPPYWSLGFHLCRWGYKNLDELKEVVERYRAAGIPLDVQWNDIDYMDRYRDFTLDpVNFPGLPAFVDDLHANGQHY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  414 ILILDPAISGNETQ-YLPFIRGQENNVFIKWPDTNDIVwGKVWPDlpnvivdgsldhetqvklyraYVAFPDFFRNSTAA 492
Cdd:cd06602    81 VPILDPGISANESGgYPPYDRGLEMDVFIKNDDGSPYV-GKVWPG---------------------YTVFPDFTNPNTQE 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  493 WWKKEIEELYanprepeKSLKFDGLWIDMNEPSNFVDGSV------RGCSNEMLNNPPYMPYLeSRDKGLSSKTLCMESQ 566
Cdd:cd06602   139 WWTEEIKDFH-------DQVPFDGLWIDMNEPSNFCTGSCgnspnaPGCPDNKLNNPPYVPNN-LGGGSLSDKTICMDAV 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  567 QilpdSSPVEHYNVHNLYGWSQTRPTYEAVQEV-TGQRGVIITRSTFPSSGRWGGHRLGNNTAAWDQLGKSIIGMMEFSL 645
Cdd:cd06602   211 H----YDGGLHYDVHNLYGLSEAIATYKALKEIfPGKRPFIISRSTFPGSGKYAGHWLGDNYSTWEDMRYSIPGMLEFNL 286

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  646 FGIPYTGADICGFFGDAEYEMCVRWMQLGAFYPFSRNHNNIGTRRQDPVAWNSTFEMLSRKVLETRYTLLPYLYTLMHKA 725
Cdd:cd06602   287 FGIPMVGADICGFNGNTTEELCARWMQLGAFYPFSRNHNDIGAIDQEPYVWGPSVADASRKALLIRYSLLPYLYTLFYRA 366


                  .
gi 767949045  726 H 726
Cdd:cd06602   367 H 367
GH31_GANC_GANAB_alpha cd06603
neutral alpha-glucosidase C, neutral alpha-glucosidase AB; This subgroup includes the closely ...
 335-856 1.58e-107

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: 351.05  E-value: 1.58e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  335 GRPAMIPYWALGFHLSRYGYQNDAEISSLYDAMVAAQIPYDVQHVDIDYMNRKLDFTL-SANFQNLSLLIEQMKKNGMRF 413
Cdd:cd06603     1 GTPPLPPLFALGYHQCRWNYNDQEDVLEVDANFDEHDIPYDVIWLDIEHTDGKRYFTWdKKKFPDPKKMQEKLASKGRKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  414 ILILDPAISgNETQYLPFIRGQENNVFIKWPDTNDIVwGKVWPdlpnvivdGSldhetqvklyrayVAFPDFFRNSTAAW 493
Cdd:cd06603    81 VTIVDPHIK-RDDDYFVYKEAKEKDYFVKDSDGKDFE-GWCWP--------GS-------------SSWPDFLNPEVRDW 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  494 WKKeieeLYANPREPEKSLKFdGLWIDMNEPSNFvdgsvrgcsnemlNNPPY-MPylesRDkglssktlCMESQQilpds 572
Cdd:cd06603   138 WAS----LFSYDKYKGSTENL-YIWNDMNEPSVF-------------NGPEItMP----KD--------AIHYGG----- 182

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  573 spVEHYNVHNLYGWSQTRPTYEAV--QEVTGQRGVIITRSTFPSSGRWGGHRLGNNTAAWDQLGKSIIGMMEFSLFGIPY 650
Cdd:cd06603   183 --VEHRDVHNIYGLYMHMATFEGLlkRSNGKKRPFVLTRSFFAGSQRYGAVWTGDNMATWEHLKISIPMLLSLSIAGIPF 260

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  651 TGADICGFFGDAEYEMCVRWMQLGAFYPFSRNHNNIGTRRQDPvaWNSTFEMLS--RKVLETRYTLLPYLYTLMHKAHVE 728
Cdd:cd06603   261 VGADVGGFFGNPDEELLVRWYQAGAFYPFFRAHAHIDTKRREP--WLFGEETTEiiREAIRLRYRLLPYWYTLFYEASRT 338

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  729 GSTVVRPLLHEFTDDRTTWDIDRQFMLGPAILISPVLETSTFEISAYFPR-ARWYDYsTGTSSTSTGQRKILKAPLDHIN 807
Cdd:cd06603   339 GLPIMRPLWYEFPEDESTFDIDDQFMLGDSLLVKPVVEEGATSVTVYLPGgEVWYDY-FTGQRVTGGGTKTVPVPLDSIP 417

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 767949045  808 LHVRGGYILP-WQEPAMNTHSSRQNFMGLIVALDDNGTAEGQVFWDDGQS 856
Cdd:cd06603   418 VFQRGGSIIPrKERVRRSSKLMRNDPYTLVVALDENGEAEGELYLDDGES 467
GH31_glucosidase_II_MalA cd06604
Alpha-glucosidase II-like; Alpha-glucosidase II (alpha-D-glucoside glucohydrolase) is a ...
 335-729 2.25e-97

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: 317.53  E-value: 2.25e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  335 GRPAMIPYWALGFHLSRYGYQNDAEISSLYDAMVAAQIPYDVQHVDIDYMNRKLDFTLS-ANFQNLSLLIEQMKKNGMRF 413
Cdd:cd06604     1 GRPPLPPKWALGYQQSRWSYYPEEEVREVAKGFRERDIPCDAIYLDIDYMDGYRVFTWDkERFPDPKELIKELHEQGFRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  414 ILILDPAISGNEtQYLPFIRGQENNVFIKWPDtNDIVWGKVWPDLpnvivdgsldhetqvklyrayVAFPDFFRNSTAAW 493
Cdd:cd06604    81 VTIVDPGVKVDP-GYEVYEEGLENDYFVKDPD-GELYVGKVWPGK---------------------SVFPDFTNPEVREW 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  494 WKKEIEELYanprepekSLKFDGLWIDMNEPSNFVDgsvrgcsnemlNNPPYMPyLESRDKGlssktlcmesqqilpDSS 573
Cdd:cd06604   138 WGDLYKELV--------DLGVDGIWNDMNEPAVFNA-----------PGGTTMP-LDAVHRL---------------DGG 182

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  574 PVEHYNVHNLYGWSQTRPTYEAVQEV-TGQRGVIITRSTFPSSGRWGGHRLGNNTAAWDQLGKSIIGMMEFSLFGIPYTG 652
Cdd:cd06604   183 KITHEEVHNLYGLLMARATYEGLRRLrPNKRPFVLSRAGYAGIQRYAAIWTGDNSSSWEHLRLSIPMLLNLGLSGVPFVG 262

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767949045  653 ADICGFFGDAEYEMCVRWMQLGAFYPFSRNHNNIGTRRQDPVAWNSTFEMLSRKVLETRYTLLPYLYTLMHKAHVEG 729
Cdd:cd06604   263 ADIGGFAGDPSPELLARWYQLGAFFPFFRNHSAKGTRDQEPWAFGEEVEEIARKAIELRYRLLPYLYTLFYEAHETG 339
YicI COG1501
Alpha-glucosidase/xylosidase, GH31 family [Carbohydrate transport and metabolism];
228-857 6.74e-90

Alpha-glucosidase/xylosidase, GH31 family [Carbohydrate transport and metabolism];


Pssm-ID: 441110 [Multi-domain]  Cd Length: 609  Bit Score: 305.93  E-value: 6.74e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  228 PSQYIYGFGE---TEHTTFRRNMNWNTWGMFAHDEPPAYKknsygVHPYYMALEEDGsahgvLLLNSNAM---DVTLQPT 301
Cdd:COG1501    60 LGEQIYGLGErftTLHKRGRIVVNWNLDHGGHKDNGNTYA-----PIPFYVSSKGYG-----VFVNSASYvtfDVGSAYS 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  302 PALTYRTTGGILDFYIVLGPTPELVTQQYTELIGRPAMIPYWALGFHLSRYGYQNDAEISSLYDAMVAAQIPYDVQHVDI 381
Cdd:COG1501   130 DLVEFTVPGDSLEFYVIEGPSPEDVLEKYTELTGKPPLPPRWAFGYWQSRKSYYDQDQVLAFADEFRDRGFPLDVIHLDI 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  382 DYMNRKL--DFTLSAN-FQNLSLLIEQMKKNGMRFILILDPAISgneTQYLPFIRGQENnvFIKWPdtNDIVW-GKVWPD 457
Cdd:COG1501   210 RWMDKYYwgDFEWDPRrFPDPKAMVKELHDRGVKLVLWINPYVA---PDSAIFAEGMAN--FVKIA--SGTVFvGKMWPG 282

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  458 lpnvivdgsldhetqvklyraYVAFPDFFRNSTAAWWKKEIEELYAnprepekSLKFDGLWIDMNEPsnfvdgsvrgcsn 537
Cdd:COG1501   283 ---------------------TTGLLDFTRPDAREWFWAGLEKELL-------SIGVDGIKLDMNEG------------- 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  538 emlnnppyMPylesrdkglssktlcmESQQILPDSSPVEhynVHNLYGWSQTRPTYEAVQEVTGQRGVIITRSTFPSSGR 617
Cdd:COG1501   322 --------WP----------------TDVATFPSNVPQQ---MRNLYGLLEAKATFEGFRTSRNNRTFILTRSGFAGGQR 374

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  618 WGGHRLGNNTAAWDQLGKSIIGMMEFSLFGIPYTGADICGFFGDAEYEMCVRWMQLGAFYPFSRNHNNigTRRQDPVAWN 697
Cdd:COG1501   375 YPVIWTGDNTSSWESLEDQLTQGLNLSLSGVPFWTPDIGGFFGSPSRELWIRWFQVGAFSPFARIHGW--ASSTEPWFFD 452

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  698 STFEMLSRKVLETRYTLLPYLYTLMHKAHVEGSTVVRPLLHEFTDDRTTWDIDRQFMLGPAILISPVLeTSTFEISAYFP 777
Cdd:COG1501   453 EEAKQIVKEYAQLRYRLLPYIYSLFAKASTDGTPVIRPLFLEFPDDPTTRFIDDQYMFGEYLLVAPIF-AGTESRLVYLP 531

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  778 RARWYDYSTGTSSTSTGQRKIlKAPLDHINLHVRGGYILPWQePAMNtHSSRQNFMGLIVALDDNGTAEGQVFWDDGQSI 857
Cdd:COG1501   532 KGKWYDFWTGELIEGGQWITV-TAPLDRLPLYVRDGSIIPLG-PVSL-RPSMQKIDGIELRVYGSGETAYTLYDDDGETV 608
GH31_MGAM-like cd06600
maltase-glucoamylase (MGAM)-like; This family includes the following closely related glycosyl ...
 335-714 2.02e-83

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: 274.37  E-value: 2.02e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  335 GRPAMIPYWALGFHLSRYGYQNDAEISSLYDAMVAAQIPYDVQHVDIDYMNRKLDFTL-SANFQNLSLLIEQMKKNGMRF 413
Cdd:cd06600     1 GRPALPPYWAFGYHQSRYSYYDQDKVVEVVDIMQEAGIPYDVMWLDIDYMDSYKDFTWdPVRFPEPKKFVDELHKNGQKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  414 ILILDPAIsgnetqylpfirgqennvfikwpdtndivwgkvwpdlpnvivdgsldhetqvklyrayvafpdffrnsTAAW 493
Cdd:cd06600    81 VTIVDPGI--------------------------------------------------------------------TREW 92

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  494 WKKEIEElyanprePEKSLKFDGLWIDMNEPSNFvdgsvrgcsnemlnnppympylesrdkglssktlcmesqqilpdss 573
Cdd:cd06600    93 WAGLISE-------FLYSQGIDGIWIDMNEPSNF---------------------------------------------- 119

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  574 pvehYNVHNLYGWSQTRPTYEAVQEVTGQRGVIITRSTFPSSGRWGGHRLGNNTAAWDQLGKSIIGMMEFSLFGIPYTGA 653
Cdd:cd06600   120 ----YKVHNLYGFYEAMATAEGLRTSHNERPFILSRSTFAGSQKYAAHWTGDNTASWDDLKLSIPLVLGLSLSGIPFVGA 195

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767949045  654 DICGFFGDAEYEMCVRWMQLGAFYPFSRNHNNIGTRRQDPVAWNSTFEMLSRKVLETRYTL 714
Cdd:cd06600   196 DIGGFAGDTSEELLVRWYQLGAFYPFSRSHKATDTKDQEPVLFPEYYKESVREILELRYKL 256
PLN02763 PLN02763
hydrolase, hydrolyzing O-glycosyl compounds
 233-874 6.96e-77

hydrolase, hydrolyzing O-glycosyl compounds


Pssm-ID: 215408 [Multi-domain]  Cd Length: 978  Bit Score: 277.16  E-value: 6.96e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  233 YGFGETE---HTTFRRNMNWNT--WGmfahdeppaYKKNS---YGVHPYYMALEEDGSAHGVLLLNSNAMDVTLQPTPAL 304
Cdd:PLN02763   77 YGTGEVSgplERTGKRVYTWNTdaWG---------YGQNTtslYQSHPWVFVVLPNGEALGVLADTTRRCEIDLRKESII 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  305 TYRTTGgildFY--IVLGP--TPELVTQQYTELIGRPAMIPYWALGFHLSRYGYQNDAEISSLYDAMVAAQIPYDVQHVD 380
Cdd:PLN02763  148 RIIAPA----SYpvITFGPfpSPEALLTSLSHAIGTVFMPPKWALGYQQCRWSYESAKRVAEIARTFREKKIPCDVVWMD 223

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  381 IDYMNRKLDFTLSAN-FQNLSLLIEQMKKNGMRFILILDPAISgNETQYLPFIRGQENNVFIKWPDTNDIVwGKVWPDLp 459
Cdd:PLN02763  224 IDYMDGFRCFTFDKErFPDPKGLADDLHSIGFKAIWMLDPGIK-AEEGYFVYDSGCENDVWIQTADGKPFV-GEVWPGP- 300

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  460 nvivdgsldhetqvklyrayVAFPDFFRNSTAAWWKKEIEELYANprepekslKFDGLWIDMNEPSNFvdgsvRGCSNEM 539
Cdd:PLN02763  301 --------------------CVFPDFTNKKTRSWWANLVKDFVSN--------GVDGIWNDMNEPAVF-----KTVTKTM 347

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  540 LNNPPYMPYLESrdKGLSSKTlcmesqqilpdsspveHYnvHNLYGWSQTRPTYEAVQEV-TGQRGVIITRSTFPSSGRW 618
Cdd:PLN02763  348 PETNIHRGDEEL--GGVQNHS----------------HY--HNVYGMLMARSTYEGMLLAnKNKRPFVLTRAGFIGSQRY 407

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  619 GGHRLGNNTAAWDQLGKSIIGMMEFSLFGIPYTGADICGFFGDAEYEMCVRWMQLGAFYPFSRNHNNIGTRRQDPVAWNS 698
Cdd:PLN02763  408 AATWTGDNLSNWEHLHMSIPMVLQLGLSGQPLSGPDIGGFAGDATPKLFGRWMGVGAMFPFARGHSEQGTIDHEPWSFGE 487

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  699 TFEMLSRKVLETRYTLLPYLYTLMHKAHVEGSTVVRPLLHEFTDDRTTWDIDRQFMLGPA-ILISPVLETSTFEISAYFP 777
Cdd:PLN02763  488 ECEEVCRLALKRRYRLLPHFYTLFYKAHTTGLPVMTPIFFADPKDPSLRKVENSFLLGPLlISASTLPDQGSDNLQHVLP 567

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  778 RARW--YDYSTgtsststgqrkilkaplDHINL---HVRGGYILPWQEPAMNT-HSSRQNFMGLIVALDDNGTAEGQVFW 851
Cdd:PLN02763  568 KGIWqrFDFDD-----------------SHPDLpllYLQGGSIIPLGPPIQHVgEASLSDDLTLLIALDENGKAEGVLYE 630

                         650       660
                  ....*....|....*....|...
gi 767949045  852 DDGQSIDtYENGNYFLANFIAAQ 874
Cdd:PLN02763  631 DDGDGFG-YTKGDYLLTHYEAEL 652
GH31 cd06589
glycosyl hydrolase family 31 (GH31); GH31 enzymes occur in prokaryotes, eukaryotes, and ...
 335-708 6.64e-48

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: 172.54  E-value: 6.64e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  335 GRPAMIPYWALGFHLSRYGYQNDAEISSLYDAMVAAQIPYDVQHVDIDYMNRKLDFTL----SANFQNLSLLIEQMKKNG 410
Cdd:cd06589     1 GRPPLLPKWALGFWNSRYGYYSEDEVEELVDRYREEGIPLDGFVLDSDWMDWGGNWGGftwnREKFPDPKGMIDELHDKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  411 MRFILILDPAIsgnetqylpfirgqennvfikwpdtndivwgkvwpdlpnvivdgsldhetqvklyrayvafpdffrnst 490
Cdd:cd06589    81 VKLGLIVKPRL--------------------------------------------------------------------- 91

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  491 AAWWKKEIEELYAnprepekSLKFDGLWIDMNEPSNFVDGSVRGCSNemlnnppympylesrdkglssktlcmesqqilp 570
Cdd:cd06589    92 RDWWWENIKKLLL-------EQGVDGWWTDMGEPLPFDDATFHNGGK--------------------------------- 131

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  571 dsspveHYNVHNLYGWSQTRPTYEAVQEVTG-QRGVIITRSTFPSSGRWGGHRLGNNTAAWDQLGKSIIGMMEFSLFGIP 649
Cdd:cd06589   132 ------AQKIHNAYPLNMAEATYEGQKKTFPnKRPFILSRSGYAGAQRYPAIWSGDNTTTWDSLAFQIRAGLSASLSGVG 205

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  650 YTGADICGF-FGDAEYEMCVRWMQLGAFYPFSRNHNNIGTRRQDPVAWNSTFEMLSRKVL 708
Cdd:cd06589   206 YWGHDIGGFtGGDPDKELYTRWVQFGAFSPIFRLHGDNSPRDKEPWVYGEEALAIFRKYL 265
GH31_transferase_CtsZ cd06598
CtsZ (cyclic tetrasaccharide-synthesizing enzyme Z)-like; CtsZ is a bacterial ...
 335-724 4.63e-33

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: 131.65  E-value: 4.63e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  335 GRPAMIPYWALGFHLSRYGYQNDAEISSLYDAMVAAQIPYDVQHVDIDY-----------MNRkLDFtLSANFQNLSLLI 403
Cdd:cd06598     1 GRPPLPPKWAFGLWQSEFGYDNWAEVDELVDTLRQKDFPLDGVVLDLYWfggiiaspdgpMGD-LDW-DRKAFPDPAKMI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  404 EQMKKNGMRFILILDPAISGNETQYLPFirgQENNVFIKWPDTN------DIVWGKVwpdlpnvivdgsldhetqvklyr 477
Cdd:cd06598    79 ADLKQQGVGTILIEEPYVLKNSDEYDEL---VKKGLLAKDKAGKpeptlfNFWFGEG----------------------- 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  478 ayvAFPDFFRNSTAAWWkkeieelYANPREPeKSLKFDGLWIDMNEPSNFvdgsvrgcsnemlnnPPYMPYLesrdKGls 557
Cdd:cd06598   133 ---GMIDWSDPEARAWW-------HDRYKDL-IDMGVAGWWTDLGEPEMH---------------PPDMVHA----DG-- 180

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  558 sktlcmesqqilpdsspvEHYNVHNLYG--WSQTrpTYEA-VQEVTGQRGVIITRSTFPSSGRWG-GHRLGNNTAAWDQL 633
Cdd:cd06598   181 ------------------DAADVHNIYNllWAKS--IYDGyQRNFPEQRPFIMSRSGTAGSQRYGvIPWSGDIGRTWGGL 240

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  634 GKSIIGMMEFSLFGIPYTGADICGFFGDAEY--EMCVRWMQLGAFYPFSRNHNNiGTRRQDPVAWNSTFEMLSRKVLETR 711
Cdd:cd06598   241 ASQINLQLHMSLSGIDYYGSDIGGFARGETLdpELYTRWFQYGAFDPPVRPHGQ-NLCNPETAPDREGTKAINRENIKLR 319

                         410
                  ....*....|...
gi 767949045  712 YTLLPYLYTLMHK 724
Cdd:cd06598   320 YQLLPYYYSLAYR 332
NtCtMGAM_N pfam16863
N-terminal barrel of NtMGAM and CtMGAM, maltase-glucoamylase; NtCtMGAM_N is a beta-barrel-like ...
 136-229 2.36e-32

N-terminal barrel of NtMGAM and CtMGAM, maltase-glucoamylase; NtCtMGAM_N is a beta-barrel-like structure just N-terminal to the catalytic domain of maltase-glucoamylase in eukaryotes. It contributes to the architecture of the substrate-binding site, by donating a loop that comes into close contact with two regions in the catalytic domain thereby creating the site. This family is frequently found at the N-terminus of Glycosyl hydrolase 31, pfam01055.to which it contributes as above.


Pssm-ID: 465286  Cd Length: 113  Bit Score: 122.20  E-value: 2.36e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045   136 ISFLHLKVIYHTATMLQVKIYDPTNKRYEVPVPLNTPPQPVGDPENRLYDVRIQNNPFGIQIQRKNSSTVIWDSQLPGFI 215
Cdd:pfam16863   20 IETLKLTVEYQTDNRLHVKITDPNNKRYEVPEELLPRPSPSSSASDSLYEFEYTNEPFGFKVTRKSTGEVLFDTSGGPLV 99

                           90
                   ....*....|....
gi 767949045   216 FNDMFLSISTRLPS 229
Cdd:pfam16863  100 FEDQFLQLSTRLPS 113
GH31_lyase_GLase cd06601
alpha-1,4-glucan lyase; GLases (alpha-1,4-glucan lyases) are glycosyl hydrolase family 31 ...
 335-729 1.96e-31

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: 127.53  E-value: 1.96e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  335 GRPAMIPYWALGFHLSRYGYQNDAEISSLYDAMVAAQIPYDVQHVDIDYMNRKLDFTLSAN-FQNLSLLIEQMKKNGMRf 413
Cdd:cd06601     1 GRSRMKPRYVFGYHQGCYGYSSRESLEVVVQSYRDANIPLDGLHIDVDFQDNYRTFTTSKDkFPNPKEMFSNLHAQGFK- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  414 ilildpaISGNETqylPFIRgqenNVFIkwpdtndivwgkvwpdlpnvivdGSLDHETQVklyRAYVAFPDFFRNSTAAW 493
Cdd:cd06601    80 -------CSTNIT---PIIT----DPYI-----------------------GGVNYGGGL---GSPGFYPDLGRPEVREW 119

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  494 WKKEIEELYanprepekSLKFDGLWIDMNEPSnfvdgsvrgCSNEMLNNPPYMPYLESRdkglssktLCMESQQILPDSS 573
Cdd:cd06601   120 WGQQYKYLF--------DMGLEMVWQDMTTPA---------IAPHKINGYGDMKTFPLR--------LLVTDDSVKNEHT 174

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  574 PVEHYNVHNLYGWSQTRPTYEAVQEVTG---QRGVIITRSTFPSSGRWGGHRLGNNTAAWDQLGKSIIGMMEFSLFGIPY 650
Cdd:cd06601   175 YKPAATLWNLYAYNLHKATYHGLNRLNArpnRRNFIIGRGGYAGAQRFAGLWTGDNASTWDFLQINIPQVLNLGLSGVPI 254

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  651 TGADICGF--FGDA------EYEMCVRWMQLGAFYPFSRNHNNIGTRRQDPVAWNSTFEMLS------RKVLETRYTLLP 716
Cdd:cd06601   255 SGSDIGGFasGSDEnegkwcDPELLIRWVQAGAFLPWFRNHYDRYIKKKQQEKLYEPYYYYEpvlpicRKYVELRYRLMQ 334

                         410
                  ....*....|...
gi 767949045  717 YLYTLMHKAHVEG 729
Cdd:cd06601   335 VFYDAMYENTQNG 347
PRK10658 PRK10658
putative alpha-glucosidase; Provisional
 310-781 6.51e-30

putative alpha-glucosidase; Provisional


Pssm-ID: 236731 [Multi-domain]  Cd Length: 665  Bit Score: 128.09  E-value: 6.51e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  310 GGILDFYIVLGPTPELVTQQYTELIGRPAMIPYWALGFHLS-----RYgyqNDAEISSLYDAMVAAQIPYDVQHVDIDYM 384
Cdd:PRK10658  233 GEYLEYFVIDGPTPKEVLDRYTALTGRPALPPAWSFGLWLTtsfttNY---DEATVNSFIDGMAERDLPLHVFHFDCFWM 309

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  385 nRKL---DFTL-SANFQNLSLLIEQMKKNGMRFILILDPAISgnetQYLP-FIRGQENNVFIKWPDtndivwGKVWpdlp 459
Cdd:PRK10658  310 -KEFqwcDFEWdPRTFPDPEGMLKRLKAKGLKICVWINPYIA----QKSPlFKEGKEKGYLLKRPD------GSVW---- 374

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  460 nvivdgsldhetQVKLYRAYVAFPDFFRNSTAAWWKKEIEELYAnprepeksLKFDGLWIDMNE--PSNFV--DGSvrgc 535
Cdd:PRK10658  375 ------------QWDKWQPGMAIVDFTNPDACKWYADKLKGLLD--------MGVDCFKTDFGEriPTDVVwfDGS---- 430

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  536 snemlnNPPYMpylesrdkglssktlcmesqqilpdsspvehynvHNLYGWSQTRPTYEAVQEVTGQR-GVIITRST--- 611
Cdd:PRK10658  431 ------DPQKM----------------------------------HNYYTYLYNKTVFDVLKETRGEGeAVLFARSAtvg 470

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  612 ---FPSsgRWGGhrlgNNTAAWDQLGKSIIGMMEFSLFGIPYTGADICGFFGDAEYEMCVRWMQLGAFYPFSRNHNNIGT 688
Cdd:PRK10658  471 gqqFPV--HWGG----DCYSNYESMAESLRGGLSLGLSGFGFWSHDIGGFENTATADVYKRWCAFGLLSSHSRLHGSKSY 544

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  689 RrqdpVAWNSTFEM--LSRKVLETRYTLLPYLYTLMHKAHVEGSTVVRPLLHEFTDDRTTWDIDRQFMLGPAILISPVLe 766
Cdd:PRK10658  545 R----VPWAYDEEAvdVVRFFTKLKCRLMPYLYREAAEAHERGTPMMRAMVLEFPDDPACDYLDRQYMLGDSLLVAPVF- 619

                         490
                  ....*....|....*
gi 767949045  767 TSTFEISAYFPRARW 781
Cdd:PRK10658  620 SEAGDVEYYLPEGRW 634
GH31_xylosidase_YicI cd06593
alpha-xylosidase YicI-like; YicI alpha-xylosidase is a glycosyl hydrolase family 31 (GH31) ...
 335-714 4.29e-26

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: 110.74  E-value: 4.29e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  335 GRPAMIPYWALGFHLSRYGYQNDAEISSLYDAMVAAQIPYDVQHVDIDYM--NRKLDFTLSA-NFQNLSLLIEQMKKNGM 411
Cdd:cd06593     1 GRPPLPPAWSFGLWLSRSFYYSEEEVLEVADGMRERGIPCDVIHLDCFWMkeDWWCDFEWDEeRFPDPEGMIARLKEKGF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  412 RFILILDPAISgNETQYlpFIRGQENNVFIKWPDtndivwGKVWpdlpnvivdgsldheTQVKLYRAYVAFPDFFRNSTA 491
Cdd:cd06593    81 KVCLWINPYIS-QDSPL--FKEAAEKGYLVKNPD------GSPW---------------HQWDGWQPGMGIIDFTNPEAV 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  492 AWWKKEIEELYAnprepeksLKFDGLWIDMNE--PSNFV--DGSvrgcsnemlnNPPYMpylesrdkglssktlcmesqq 567
Cdd:cd06593   137 AWYKEKLKRLLD--------MGVDVIKTDFGEriPEDAVyyDGS----------DGRKM--------------------- 177

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  568 ilpdsspvehynvHNLYGWSQTRPTYEAVQEVTGQRGVIITRSTFPSSGRWGGHRLGNNTAAWDQLGKSIIGMMEFSLFG 647
Cdd:cd06593   178 -------------HNLYPLLYNKAVYEATKEVKGEEAVLWARSAWAGSQRYPVHWGGDSESTFEGMAASLRGGLSLGLSG 244

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767949045  648 IPYTGADICGFFGDAEYEMCVRWMQLGAFYPFSRNHnniGTRRQDPVAWNSTFEMLSRKVLETRYTL 714
Cdd:cd06593   245 FGFWSHDIGGFEGTPSPELYKRWTQFGLLSSHSRLH---GSTPREPWEYGEEALDVVRKFAKLRYRL 308
GH31_NET37 cd06592
glucosidase NET37; NET37 (also known as KIAA1161) is a human lamina-associated nuclear ...
 341-781 2.17e-25

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: 110.00  E-value: 2.17e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  341 PYWALGFhlsRYGY-QNDAEISSLYDAMVAAQIPYDVQHVDIDYMNRKLDFTLSAN-FQNLSLLIEQMKKNGMRFILILD 418
Cdd:cd06592     3 PIWSTWA---EYKYnINQEKVLEYAEEIRANGFPPSVIEIDDGWQTYYGDFEFDPEkFPDPKGMIDKLHEMGFRVTLWVH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  419 PAISgNETQylPFIRGQENNVFIKWPDTNDIVWGKVWPdlpnvivdgsldhetqvklyrAYVAFPDFFRNSTAAWWKKEI 498
Cdd:cd06592    80 PFIN-PDSP--NFRELRDKGYLVKEDSGGPPLIVKWWN---------------------GYGAVLDFTNPEARDWFKERL 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  499 EELyanprepEKSLKFDGLWIDmnepsnFVDGSvrgcsnemlnnppYMPYlesrdkglssktlcmESQQILPDSSPVEHy 578
Cdd:cd06592   136 REL-------QEDYGIDGFKFD------AGEAS-------------YLPA---------------DPATFPSGLNPNEY- 173

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  579 nvHNLYGwsQTRPTYEAVQEVT----GQRGVIITRSTFPSSgRWGGhrlgnntaaWDQLGKSIIGMMEFSLFGIPYTGAD 654
Cdd:cd06592   174 --TTLYA--ELAAEFGLLNEVRsgwkSQGLPLFVRMSDKDS-HWGY---------WNGLRSLIPTALTQGLLGYPFVLPD 239

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  655 ICGffGDAEY------EMCVRWMQLGAFYP---FSrnhnnigtrrqdPVAWNSTFEM---LSRKVLETRYTLLPYLYTLM 722
Cdd:cd06592   240 MIG--GNAYGnfppdkELYIRWLQLSAFMPamqFS------------VAPWRNYDEEvvdIARKLAKLREKLLPYIYELA 305

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767949045  723 HKAHVEGSTVVRPLLHEFTDDRTTWDIDRQFMLGPAILISPVLETSTFEISAYFPRARW 781
Cdd:cd06592   306 AEAVDTGEPIIRPLWWIAPEDEEALTIDDQFLLGDDILVAPVLEKGARSRDVYLPKGRW 364
GH31_N cd14752
N-terminal domain of glycosyl hydrolase family 31 (GH31); This family is found N-terminal to ...
 221-335 6.15e-24

N-terminal domain of glycosyl hydrolase family 31 (GH31); This family is found N-terminal to the glycosyl-hydrolase domain of Glycoside hydrolase family 31 (GH31). GH31 includes the glycoside hydrolases alpha-glucosidase (EC 3.2.1.20), alpha-1,3-glucosidase (EC 3.2.1.84), alpha-xylosidase (EC 3.2.1.177), sucrase-isomaltase (EC 3.2.1.48 and EC 3.2.1.10), as well as alpha-glucan lyase (EC 4.2.2.13). 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 of the catalytic domain have been identified as the catalytic nucleophile and the acid/base, respectively. A loop of the N-terminal beta-sandwich domain is part of the active site pocket.


Pssm-ID: 270212 [Multi-domain]  Cd Length: 122  Bit Score: 98.41  E-value: 6.15e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  221 LSISTRLP-SQYIYGFGEteHTTfRRNMNWNTWGMFAHD--EPPAYKKNSYGVHPYYMALEedgsAHGVLLLNSNAMDVT 297
Cdd:cd14752    10 LRLSFKLPpDEHFYGLGE--RFG-GLNKRGKRYRLWNTDqgGYRGSTDPLYGSIPFYLSSK----GYGVFLDNPSRTEFD 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 767949045  298 LQPT--PALTYRTTGGILDFYIVLGPTPELVTQQYTELIG 335
Cdd:cd14752    83 FGSEdsDELTFSSEGGDLDYYFFAGPTPKEVIEQYTELTG 122
PRK10426 PRK10426
alpha-glucosidase; Provisional
 569-781 2.88e-23

alpha-glucosidase; Provisional


Pssm-ID: 236691 [Multi-domain]  Cd Length: 635  Bit Score: 107.00  E-value: 2.88e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  569 LPDSSPVEHYnvHNLYG--WSQTrpTYEAVQEvTGQRG--VIITRSTFPSSGR-----WGGHRLgnntAAW---DQLGKS 636
Cdd:PRK10426  371 LHNGVSAEIM--HNAWPalWAKC--NYEALEE-TGKLGeiLFFMRAGYTGSQKystlfWAGDQN----VDWsldDGLASV 441

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  637 IIGMMEFSLFGIPYTGADICGFFGDAEY----EMCVRWMQLGAFYPFSRNHNniGTRRQDPVAWNSTFEMLSR--KVLET 710
Cdd:PRK10426  442 VPAALSLGMSGHGLHHSDIGGYTTLFGMkrtkELLLRWCEFSAFTPVMRTHE--GNRPGDNWQFDSDAETIAHfaRMTRV 519

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767949045  711 RYTLLPYLYTLMHKAHVEGSTVVRPLLHEFTDDRTTWDIDRQFMLGPAILISPVLETSTFEISAYFPRARW 781
Cdd:PRK10426  520 FTTLKPYLKELVAEAAKTGLPVMRPLFLHYEDDAATYTLKYQYLLGRDLLVAPVHEEGRTDWTVYLPEDKW 590
GH31_glycosidase_Aec37 cd06599
E.coli Aec37-like; Glycosyl hydrolase family 31 (GH31) domain of a bacterial protein family ...
 335-680 7.70e-22

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: 98.44  E-value: 7.70e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  335 GRPAMIPYWALGFHLSRYGY----QNDAEISSLYDAMVAAQIPYDVQHVDIDY----MNRKLDFTLSAN-FQNLSLLIEQ 405
Cdd:cd06599     1 GRPALPPRWSLGYLGSTMYYteapDAQEQILDFIDTCREHDIPCDGFHLSSGYtsieDGKRYVFNWNKDkFPDPKAFFRK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  406 MKKNGMRFILILDPAISGNETQYLPFirgQENNVFIKWPDTNDIVWGKVWPDLpnvivdGSldhetqvklyrayvaFPDF 485
Cdd:cd06599    81 FHERGIRLVANIKPGLLTDHPHYDEL---AEKGAFIKDDDGGEPAVGRFWGGG------GS---------------YLDF 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  486 FRNSTAAWWKKEIEELYanprepeKSLKFDGLWIDMNEPSNFVDgsvrgcsnemlnnppympylESRDKGLSSKTLCMES 565
Cdd:cd06599   137 TNPEGREWWKEGLKEQL-------LDYGIDSVWNDNNEYEIWDD--------------------DAACCGFGKGGPISEL 189

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  566 QQILPdsspvehynvhNLygwsQTRPTYEAVQEV-TGQRGVIITRSTFPSSGRWGGHRLGNNTAAWDQLGKSIIGMMEFS 644
Cdd:cd06599   190 RPIQP-----------LL----MARASREAQLEHaPNKRPFVISRSGCAGIQRYAQTWSGDNRTSWKTLKYNIAMGLGMS 254

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 767949045  645 LFGIPYTGADICGFFGDA-EYEMCVRWMQLGAFYP-FS 680
Cdd:cd06599   255 LSGVANYGHDIGGFAGPApEPELFVRWVQNGIFQPrFS 292
GH31_xylosidase_XylS cd06591
xylosidase XylS-like; XylS is a glycosyl hydrolase family 31 (GH31) alpha-xylosidase found in ...
 335-689 9.53e-22

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: 98.01  E-value: 9.53e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  335 GRPAMIPYWALGFHLSRYGYQNDAEISSLYDAMVAAQIPYDVQHVDIDYMNRKL--DFTL-SANFQNLSLLIEQMKKNGM 411
Cdd:cd06591     1 GKAPMLPKWALGFWQSKERYKTQEELLEVAREYRERGIPLDVIVQDWFYWTEQGwgDMKFdPERFPDPKGMVDELHKMNV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  412 RFILILDPAIsGNETQYLPFIRgqENNVFIkwpdtnDIVWGKVWPDlpnvivdgsldhetqvklyrAYVAFPDFFRNSTA 491
Cdd:cd06591    81 KLMISVWPTF-GPGSENYKELD--EKGLLL------RTNRGNGGFG--------------------GGTAFYDATNPEAR 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  492 AWWKKEIEELYanprepeKSLKFDGLWIDMNEPSNFvdgsvrgcsnemlnnppymPYLESRDKGLSSktlcmesqqILPD 571
Cdd:cd06591   132 EIYWKQLKDNY-------FDKGIDAWWLDATEPELD-------------------PYDFDNYDGRTA---------LGPG 176

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  572 SSpvehynVHNLYGWSQTRPTYEAVQEVT-GQRGVIITRSTFPSSGR-----WGGhrlgNNTAAWDQLGKSIIGMMEFSL 645
Cdd:cd06591   177 AE------VGNAYPLMHAKGIYEGQRATGpDKRVVILTRSAFAGQQRygaavWSG----DISSSWETLRRQIPAGLNFGA 246

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767949045  646 FGIPYTGADICGFFG--------DAEY-EMCVRWMQLGAFYPFSRNHnniGTR 689
Cdd:cd06591   247 SGIPYWTTDIGGFFGgdpepgedDPAYrELYVRWFQFGAFCPIFRSH---GTR 296
GH31_CPE1046 cd06596
Clostridium CPE1046-like; CPE1046 is an uncharacterized Clostridium perfringens protein with a ...
 593-784 1.73e-21

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: 97.80  E-value: 1.73e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  593 YEAVQEVTGQRGVIITRSTFPSSGRWGGHRLGNNTAAWDQLGKSIIGMMEFSLFGIPYTGADICGFFGDAEyEMCVRWMQ 672
Cdd:cd06596   135 ADGIENNSNARPFIWTVDGWAGTQRYAVIWTGDQSGSWEYIRFHIPTYIGSGLSGQAYATSDVDGIFGGSP-ETYTRDLQ 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  673 LGAFYPFSRNHNNIGTRRQDPVAWNSTFEMLSRKVLETRYTLLPYLYTLMHKAHVEGSTVVRPLLHEFTDDRTTWDIDR- 751
Cdd:cd06596   214 WKAFTPVLMNMSGWAANDKQPWVFGEPYTSINRKYLKLKMRLMPYIYTYAREASVTGLPMVRAMFLEYPNDPTAYGTATq 293

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 767949045  752 -QFMLGPAILISPVLETSTFEISA----YFPRARWYDY 784
Cdd:cd06596   294 yQFMWGPDFLVAPVYQNTAAGNDVrngiYLPAGTWIDY 331
GH31_transferase_CtsY cd06597
CtsY (cyclic tetrasaccharide-synthesizing enzyme Y)-like; CtsY is a bacterial ...
 335-697 1.84e-16

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: 82.36  E-value: 1.84e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  335 GRPAMIPYWALGFHLSRYGYQNDAEISSLYDAMVAAQIPYDVqhVDIDYMNRKLDF----TLSANFQNLSLLIEQMKKNG 410
Cdd:cd06597     1 GRAALPPKWAFGHWVSANEWNSQAEVLELVEEYLAYDIPVGA--VVIEAWSDEATFyifnDATGKWPDPKGMIDSLHEQG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  411 MRFILILDPAIsgNETQYLPFIR------GQENNVFIKWPDTNDIVWGKVWpdlpnvivdgsldHETQvklyrayvAFPD 484
Cdd:cd06597    79 IKVILWQTPVV--KTDGTDHAQKsndyaeAIAKGYYVKNGDGTPYIPEGWW-------------FGGG--------SLID 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  485 FFRNSTAAWWKKEIEELYanprepeKSLKFDGLWIDMNEP-----SNFVDGSvRGcsNEMLNNPPympylesrdkglssk 559
Cdd:cd06597   136 FTNPEAVAWWHDQRDYLL-------DELGIDGFKTDGGEPywgedLIFSDGK-KG--REMRNEYP--------------- 190

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  560 tlcmesqqilpdsspvehynvhNLYgwsqTRPTYEAVQEVTGQrGVIITRSTFPSSGRWGGHRLGNNTAAWDQLGKSIIG 639
Cdd:cd06597   191 ----------------------NLY----YKAYFDYIREIGND-GVLFSRAGDSGAQRYPIGWVGDQDSTFEGLQSALKA 243

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  640 MMEFSLFGIPYTGADICGFFGDA-EYEMCVRWMQLGAFYPFSRNH-NNIGTRRQDPVAWN 697
Cdd:cd06597   244 GLSAAWSGYPFWGWDIGGFSGPLpTAELYLRWTQLAAFSPIMQNHsEKNHRPWSEERRWN 303
COG4625 COG4625
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ...
 1071-1613 6.02e-12

Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function unknown];


Pssm-ID: 443664 [Multi-domain]  Cd Length: 900  Bit Score: 70.96  E-value: 6.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1071 TNASTASTNATVPITTTCFATSTIGVTTNATVPDTTAPFPTNTTTASTNATIPITTTPFATSTISVTTSTTVPDTTAPFP 1150
Cdd:COG4625     1 GGGGGGGGGGGGGGGGTGGGGAGGGGGAGGGAGGGGAGGGGGGGGGGGGAGGGGGGGGTGGGGGGGGGGGGGGAGGGGGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1151 TSTTSASTNATPVPITTTLFATSTIGVTTGTTVPDTTAPFPTSTTSTSTSATVPITTTPSPTNTADANTSNTVPNTTMPS 1230
Cdd:COG4625    81 GGGGGGGGGTGGVGGGGGGGGGGGGGGGGGGGGGGGGSAGGGGGGAGGAGGGGGGGAGGGGGGGGGGGAGGGGGGGAGGA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1231 PTSSTTVSTIATVPISVTPSLTSTADATISTTVLIATTSSLTGTTDVSTSTTINNISTPVQTNTTNASTSTNVANITATS 1310
Cdd:COG4625   161 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGNGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGGGGGGGGGGGG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1311 HTSTDDTVPNNTVPVTAIPSLANTGVDTTSNSFSIMTTSFSESTNAMNTTVIMATTSPTSTDVASTNNDASMTNFLLATM 1390
Cdd:COG4625   241 GGGGGGGAGGGGGGGGGNGGGGGAGGGGGGGGGGSGGGGGGGGGGGSGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGG 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1391 SAGNITSNSISITTTSFGNSVPFVTTpspSTDATTTSNNTNPGMTTYYQTSPTIPTHTLTSIPSSITSILSMFPTSNTFT 1470
Cdd:COG4625   321 GGGGGGGGGGGGGAGGGGGSGGAGAG---GGGAGGGGAGGGGGGGTGGGGGGGGGGGGGSGGGGAGGGGGSGGGGGGGAG 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1471 TDKITNFTTPTNANTIIFNTLDTKSTMVIDATVTTTSTKDNTMSPDTTVTSIDKFTTHITQFATPHSATTTTLALSHTSL 1550
Cdd:COG4625   398 GGGGGGGAGGTGGGGAGGGGGAAGGGGGGTGAGGGGGGGGTGAGGGGATGGGGGGGGGAGGSGGGAGAGGGSGSGAGTLT 477

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767949045 1551 APTNLSNLGTMDITDADNSSSVTGNTTHISVSnlTTASVTITATGLDSQTPHMVINSVATYLP 1613
Cdd:COG4625   478 LTGNNTYTGTTTVNGGGNYTQSAGSTLAVEVD--AANSDRLVVTGTATLNGGTVVVLAGGYAP 538
COG4625 COG4625
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ...
 1151-1634 2.05e-10

Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function unknown];


Pssm-ID: 443664 [Multi-domain]  Cd Length: 900  Bit Score: 65.96  E-value: 2.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1151 TSTTSASTNATPVPITTTLFATSTIGVTTGTTVPDTTAPFPTSTTSTSTSATVPITTTPSPTNTADANTSNTVPNTTMPS 1230
Cdd:COG4625    12 GGGGGTGGGGAGGGGGAGGGAGGGGAGGGGGGGGGGGGAGGGGGGGGTGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGTG 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1231 PTSSTTVSTIATVPISVTPSLTSTADATISTTVLIATTSSLTGTTDVSTSTTINNISTPVQTNTTNASTSTNVANITATS 1310
Cdd:COG4625    92 GVGGGGGGGGGGGGGGGGGGGGGGGGSAGGGGGGAGGAGGGGGGGAGGGGGGGGGGGAGGGGGGGAGGAGGGGGGGGGGG 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1311 HTSTDDTVPNNTVPVTAIPSLANTGVDTTSNSFSIMTTSFSESTNAMNTTVIMATTSPTSTDVASTNNDASMTNFLLAtm 1390
Cdd:COG4625   172 GGGGGGGGGGGGGGGGGGGGGNGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGAG-- 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1391 SAGNITSNSISITTTSFGNSVPFVTTPSPSTDATTTSNNTNPGMTTYYQTSPTIPTHTLTSIPSSITSIlsmfpTSNTFT 1470
Cdd:COG4625   250 GGGGGGGGNGGGGGAGGGGGGGGGGSGGGGGGGGGGGSGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGG-----GGGGGG 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1471 TDKITNFTTPTNANTIIFNTLDTKSTMVIDATVTTTSTKDNTMSPDTTVTSIDKFTTHITQFATPHSATTTTLALSHTSL 1550
Cdd:COG4625   325 GGGGGGGGGAGGGGGSGGAGAGGGGAGGGGAGGGGGGGTGGGGGGGGGGGGGSGGGGAGGGGGSGGGGGGGAGGGGGGGG 404

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1551 APTNLSNLGTMDITDADNSSSVTGNTTHISVSNLTTASVTITATGLDSQTPHMVINSV-ATYLPITATSATTDTTNITKY 1629
Cdd:COG4625   405 AGGTGGGGAGGGGGAAGGGGGGTGAGGGGGGGGTGAGGGGATGGGGGGGGGAGGSGGGaGAGGGSGSGAGTLTLTGNNTY 484


                  ....*
gi 767949045 1630 ALNTT 1634
Cdd:COG4625   485 TGTTT 489
PD smart00018
P or trefoil or TFF domain; Proposed role in renewal and pathology of mucous epithelia.
 53-93 3.07e-10

P or trefoil or TFF domain; Proposed role in renewal and pathology of mucous epithelia.


Pssm-ID: 197472  Cd Length: 46  Bit Score: 57.01  E-value: 3.07e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 767949045     53 VSDLEKFNCYPDDPTASEesCRQRGCLWeDTSTPGVPTCYY 93
Cdd:smart00018    5 VPPSERINCGPPGITEAE--CEARGCCF-DSSISGVPWCFY 42
Trefoil cd00111
P or trefoil or TFF domain; Trefoil factor family domain peptides are mucin-associated ...
 52-93 1.04e-09

P or trefoil or TFF domain; Trefoil factor family domain peptides are mucin-associated molecules, largely found in epithelia of gastrointestinal tissues. Function is not known but it was originally identified from mucosal tissues, where it may have a regulatory or structural role and has also been implicated as a growth fractor in other tissues.The domain is found in 1 to 6 copies where it occurs.


Pssm-ID: 238059  Cd Length: 44  Bit Score: 55.43  E-value: 1.04e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 767949045   52 PVSDLEKFNCYPDDPTASEesCRQRGCLWeDTSTPGVPTCYY 93
Cdd:cd00111     4 SVPPSERIDCGPPGITQEE--CEARGCCF-DPSISGVPWCFY 42
COG4625 COG4625
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ...
 982-1508 1.21e-09

Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function unknown];


Pssm-ID: 443664 [Multi-domain]  Cd Length: 900  Bit Score: 63.26  E-value: 1.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  982 TSSETITSSASANTTTGTTDTVPITTTSFPSTTSVTTNTTVPDTTSPFPTSTTNASTNATVPITTTPFPTSTIGVTTNAT 1061
Cdd:COG4625     1 GGGGGGGGGGGGGGGGTGGGGAGGGGGAGGGAGGGGAGGGGGGGGGGGGAGGGGGGGGTGGGGGGGGGGGGGGAGGGGGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1062 VPNTTAPFPTNASTASTNATVPITTTCFATSTIGVTTNATVPDTTAPFPTNTTTASTNATIPITTTPFATSTISVTtstt 1141
Cdd:COG4625    81 GGGGGGGGGTGGVGGGGGGGGGGGGGGGGGGGGGGGGSAGGGGGGAGGAGGGGGGGAGGGGGGGGGGGAGGGGGGG---- 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1142 vpdttapfpTSTTSASTNATPVPITTTLFATSTIGVTTGTTVPDTTAPFPTSTTSTSTSATVPITTTPSPTNTADANTSN 1221
Cdd:COG4625   157 ---------AGGAGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGNGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGGGGG 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1222 TVPNTTMPSPTSSTTVSTIATVPISVTPSLTSTADATISTTVLIATTSSLTGTTDVSTSTTINNISTPVQTNTTNASTST 1301
Cdd:COG4625   228 GGGGGGGGGGGGGGGGGGGGAGGGGGGGGGNGGGGGAGGGGGGGGGGSGGGGGGGGGGGSGGGGGGGGGGGGGGGGGGGG 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1302 NVANITATSHTSTDDTVPNNTVPVTAIPSLANTGVDTTSNSFSIMTTSFSESTNAMNTTVIMATTSPTSTDVASTNNDAS 1381
Cdd:COG4625   308 GGGGGGGGGGGGGGGGGGGGGGGGGGAGGGGGSGGAGAGGGGAGGGGAGGGGGGGTGGGGGGGGGGGGGSGGGGAGGGGG 387

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1382 MTNFLLATMSAGNITSNSISITTTSFGNSVPFVTTPSPSTDATTTSNNTNPGMTTYYQTSPTIPTHTLTSIPSSITSILS 1461
Cdd:COG4625   388 SGGGGGGGAGGGGGGGGAGGTGGGGAGGGGGAAGGGGGGTGAGGGGGGGGTGAGGGGATGGGGGGGGGAGGSGGGAGAGG 467

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 767949045 1462 MFPT-SNTFTTDKITNFTTPTNANTIIFNTLDTKSTMVIDATVTTTST 1508
Cdd:COG4625   468 GSGSgAGTLTLTGNNTYTGTTTVNGGGNYTQSAGSTLAVEVDAANSDR 515
Trefoil pfam00088
Trefoil (P-type) domain;
53-93 1.72e-09

Trefoil (P-type) domain;


Pssm-ID: 459666  Cd Length: 43  Bit Score: 54.63  E-value: 1.72e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 767949045    53 VSDLEKFNCYPddPTASEESCRQRGCLWEDTSTPGVPTCYY 93
Cdd:pfam00088    4 VPPSDRFDCGY--PGITQEECEARGCCWDPSVDPGVPWCFY 42
FhaB COG3210
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ...
 977-1595 1.03e-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: 60.55  E-value: 1.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  977 STTNATSSETITSSASANTTTGTTDTVPITTTSFPSTTSVTTNTTVPDTTSPFPTSTTNASTNATVPITTTPFPTSTIGV 1056
Cdd:COG3210    95 GLTSNIGGGSVNGSNSTGNGTLTTTAASATTGNNTGGTTTSSTNTVTTLGGTTTGNTVLSTSGAGNNTNTNNSSSGTNIG 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1057 TTNATVPNTTAPFPTNASTASTNATVPITTTCFATSTIGVTTNATVPDTTAPFPTNTTTASTNATIPITTTPFATSTISV 1136
Cdd:COG3210   175 NSIPTTGGSLNVVAANPTGVTGVGGALINATAGVLANAGGGTAGGVASANSTLTGGVVAAGTGAGVISTGGTDISSLSVA 254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1137 TTSTTVPDTTAPFPTSTTSASTNATPVPITTTLFATSTIGVTTGTTVPDTTAPFPTSTTSTSTSATVPITTTPSPTNTAD 1216
Cdd:COG3210   255 AGAGTGGAGGTGNAGNTTIGTTVTGTNATGSNTAGASSGDTTTNGTSSVTGAGGTGVLGGGTAAGITTTNTVGGNGDGNN 334

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1217 ANTSNTVPNTTMPSPTSSTTVSTIATVPISVTPSLTSTADATISTTVLIATTSSLTGTTDVSTSTTINNISTPVQTNTTN 1296
Cdd:COG3210   335 TTANSGAGLVSGGTGGNNGTTGTGAGSGLTGTGNGGGLTTAGAGTVASTVGTATASTGNASSTTVLGSGSLATGNTGTTI 414

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1297 ASTSTNVANITATSHTSTDDTVPNNTVPVTAIPSLANTGVDTTSNSFSIMTTSFSESTNAMNTTVIMATTSPTSTDVAST 1376
Cdd:COG3210   415 AGNGGSANAGGFTTTGGVLGITGNGTVTGGTIGGLTGSGTTNGAGLSGNTDVSGTGTVTNSAGNTTSATTLAGGGIGTVT 494

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1377 NNDASMTNFLLATMSAGNITSNSISITTTSFGNSVPFVTTPSP-STDATTTSNNTNPGMTTYYQTSPTIPTHTLTSIPSS 1455
Cdd:COG3210   495 TNATISNNAGGDANGIATGLTGITAGGGGGGNATSGGTGGDGTtLSGSGLTTTVSGGASGTTAASGSNTANTLGVLAATG 574

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1456 ITSILSMFPTSNTFTTDKITNFTTPTNANTIIFNTLDTKSTMVIDATVTTTSTKDNTMSPDTTVTSIDKFTTHITQFATP 1535
Cdd:COG3210   575 GTSNATTAGNSTSATGGTGTNSGGTVLSIGTGSAGATGTITLGAGTSGAGANATGGGAGLTGSAVGAALSGTGSGTTGTA 654

                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767949045 1536 HSATTTTLALSHTSLAPTNLSNLGTMDITDADNSSSVTGNTTHISV---SNLTTASVTITATG 1595
Cdd:COG3210   655 SANGSNTTGVNTAGGTGGGTTGTVTSGATGGTTGTTLNAATGGTLNnagNTLTISTGSITVTG 717
FhaB COG3210
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ...
 929-1593 3.84e-07

Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442443 [Multi-domain]  Cd Length: 1698  Bit Score: 55.54  E-value: 3.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  929 YNQILTIQLTDKTINLEKLTEVTWIDGGPVLPTPTKTSTIPMSSHPSPSTTNATSSETITSSASANTTTGTTDTVPITTT 1008
Cdd:COG3210    94 TGLTSNIGGGSVNGSNSTGNGTLTTTAASATTGNNTGGTTTSSTNTVTTLGGTTTGNTVLSTSGAGNNTNTNNSSSGTNI 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1009 SFPSTTSVTTNTTVPDTTSPFPTSTTNASTNATVPITTTPFPTSTIGVTTNATVPNTTAPFPTNASTASTNATVPITTTC 1088
Cdd:COG3210   174 GNSIPTTGGSLNVVAANPTGVTGVGGALINATAGVLANAGGGTAGGVASANSTLTGGVVAAGTGAGVISTGGTDISSLSV 253

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1089 FATSTIGVTTNATVPDTTAPFPTNTTTASTNATIPITTTPFATSTISVTTSTTVPDTTAPFPTSTTSASTNATPVPITTT 1168
Cdd:COG3210   254 AAGAGTGGAGGTGNAGNTTIGTTVTGTNATGSNTAGASSGDTTTNGTSSVTGAGGTGVLGGGTAAGITTTNTVGGNGDGN 333

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1169 LFATSTIGVTTGTTVPDTTApfpTSTTSTSTSATVPITTTPSPTNTADANTSNTVPNTTMPSPTSSTTVSTIATVPISVT 1248
Cdd:COG3210   334 NTTANSGAGLVSGGTGGNNG---TTGTGAGSGLTGTGNGGGLTTAGAGTVASTVGTATASTGNASSTTVLGSGSLATGNT 410

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1249 PSLTSTADATISTTVLIATTSSLTGTTDVSTSTTINNISTPVQTNTTNASTSTNVANITATSHTSTDDTVPNNTVPVTAI 1328
Cdd:COG3210   411 GTTIAGNGGSANAGGFTTTGGVLGITGNGTVTGGTIGGLTGSGTTNGAGLSGNTDVSGTGTVTNSAGNTTSATTLAGGGI 490

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1329 PSLANTGVDTTSNSFSIMTTSFSESTNAMNTTVIMATTSPTSTDVASTNNDASMTNFLLATMSAGNITSNSISITTTSFG 1408
Cdd:COG3210   491 GTVTTNATISNNAGGDANGIATGLTGITAGGGGGGNATSGGTGGDGTTLSGSGLTTTVSGGASGTTAASGSNTANTLGVL 570

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1409 NSVPFVTTPSPSTDATTTSNNTNPGMTTYYQTSPTIPTHTLTSIPSSITSILSMFPTSNTFTTDKITNFTTPTNANTIIF 1488
Cdd:COG3210   571 AATGGTSNATTAGNSTSATGGTGTNSGGTVLSIGTGSAGATGTITLGAGTSGAGANATGGGAGLTGSAVGAALSGTGSGT 650

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1489 NTLDTKSTMVIDATVTTTSTKDNTMSPDTTVTSIDKFTTHITQFATphsaTTTTLALSHTSLAPTNLSNLGTMDITDADN 1568
Cdd:COG3210   651 TGTASANGSNTTGVNTAGGTGGGTTGTVTSGATGGTTGTTLNAATG----GTLNNAGNTLTISTGSITVTGQIGALANAN 726

                         650       660
                  ....*....|....*....|....*
gi 767949045 1569 SSSVTGNTTHISVSNLTTASVTITA 1593
Cdd:COG3210   727 GDTVTFGNLGTGATLTLNAGVTITS 751
GH31_u1 cd06595
glycosyl hydrolase family 31 (GH31); uncharacterized subgroup; This family represents an ...
 335-718 1.61e-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: 51.82  E-value: 1.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  335 GRPAMIPYWALGFHLSRYGYQNDAEISSLYDAMVAAQIPYDVQHVDIDY---------------MNRKLdftlsanFQNL 399
Cdd:cd06595     2 GKPPLIPRYALGNWWSRYWAYSDDDILDLVDNFKRNEIPLSVLVLDMDWhitdkkykngwtgytWNKEL-------FPDP 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  400 SLLIEQMKKNGMRFILILDPA--ISGNETQYlpfirgqennvfikwpdtndivwgkvwpdlPNVIVDGSLDHETQVklyr 477
Cdd:cd06595    75 KGFLDWLHERGLRVGLNLHPAegIRPHEEAY------------------------------AEFAKYLGIDPAKII---- 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  478 aYVAFpDFF-RNSTAAWWKKEIEELYanprepekSLKFDGLWIDMNEpsnfvdgsvrGCSNEMLNNPPyMPYLEsrdkgl 556
Cdd:cd06595   121 -PIPF-DVTdPKFLDAYFKLLIHPLE--------KQGVDFWWLDWQQ----------GKDSPLAGLDP-LWWLN------ 173

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  557 ssktlcmesqqilpdsspveHYNVHNLYGWSQTRPtyeavqevtgqrgVIITRSTFPSSGRWGGHRLGNNTAAWDqlgks 636
Cdd:cd06595   174 --------------------HYHYLDSGRNGKRRP-------------LILSRWGGLGSHRYPIGFSGDTEVSWE----- 215

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  637 iigMMEF--------SLFGIPYTGADICGFFGDAE-YEMCVRWMQLGAFYPFSRNHNNIGTR-RQDPVAWNSTFEMLSRK 706
Cdd:cd06595   216 ---TLAFqpyftataANVGYSWWSHDIGGHKGGIEdPELYLRWVQFGVFSPILRLHSDKGPYyKREPWLWDAKTFEIAKD 292

                         410
                  ....*....|..
gi 767949045  707 VLETRYTLLPYL 718
Cdd:cd06595   293 YLRLRHRLIPYL 304
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 1066-1458 1.63e-06

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: 53.00  E-value: 1.63e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  1066 TAPFPTNASTASTNATVPITTTCFATSTIGVTTNATVPDTTAPFPTNTTTASTNATIPITTTPFATSTISVTTSTTVpdt 1145
Cdd:pfam05109  398 TAPKTLIITRTATNATTTTHKVIFSKAPESTTTSPTLNTTGFAAPNTTTGLPSSTHVPTNLTAPASTGPTVSTADVT--- 474

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  1146 tAPFPTSTTSASTNATPVPitttlfatstigvttgttvpdttAPFPTSTTSTSTSATVPITTTPSPTNTADANT---SNT 1222
Cdd:pfam05109  475 -SPTPAGTTSGASPVTPSP-----------------------SPRDNGTESKAPDMTSPTSAVTTPTPNATSPTpavTTP 530

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  1223 VPNTTMPSPTSSTTVSTIAT-VPISVTPS---LTSTADATISTTVLIATTSSLTGTTDVSTSTTINNIStpvqtnttnas 1298
Cdd:pfam05109  531 TPNATSPTLGKTSPTSAVTTpTPNATSPTpavTTPTPNATIPTLGKTSPTSAVTTPTPNATSPTVGETS----------- 599

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  1299 tstnvANITATSHTSTDDTvpnNTVPVTAIPSLANTGVDTTSNSFsimtTSFSESTNAMNTTVIMATTSPTSTDVASTNN 1378
Cdd:pfam05109  600 -----PQANTTNHTLGGTS---STPVVTSPPKNATSAVTTGQHNI----TSSSTSSMSLRPSSISETLSPSTSDNSTSHM 667

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  1379 DASMTNFLLATMSAGNITSNSISITTTSFGNSVPFVTTPSPSTDATTTSNNTNPGMTTYYQ-------TSPTIPTHTLTS 1451
Cdd:pfam05109  668 PLLTSAHPTGGENITQVTPASTSTHHVSTSSPAPRPGTTSQASGPGNSSTSTKPGEVNVTKgtppknaTSPQAPSGQKTA 747


                   ....*..
gi 767949045  1452 IPSSITS 1458
Cdd:pfam05109  748 VPTVTST 754
Chi1 COG3469
Chitinase [Carbohydrate transport and metabolism];
1241-1458 6.81e-06

Chitinase [Carbohydrate transport and metabolism];


Pssm-ID: 442692 [Multi-domain]  Cd Length: 534  Bit Score: 50.91  E-value: 6.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1241 ATVPISVTPSLTSTADATISTTVLIATTSSLTGTTDVSTSTTINNISTPVQTNTTNASTSTNVANITATSHTSTDDTVPN 1320
Cdd:COG3469     2 SSVSTAASPTAGGASATAVTLLGAAATAASVTLTAATATTVVSTTGSVVVAASGSAGSGTGTTAASSTAATSSTTSTTAT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1321 NTVPVTAIPSLANTGVDTTSNSfsimTTSFSESTNAMNTTVIMATTSPTSTDVASTNNDASmtnfllatmSAGNITSNSI 1400
Cdd:COG3469    82 ATAAAAAATSTSATLVATSTAS----GANTGTSTVTTTSTGAGSVTSTTSSTAGSTTTSGA---------SATSSAGSTT 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767949045 1401 SITTTSFGNSVPFVTTPSPSTDATTTSNNTNPGMTTYYQTSPTIPTHTLTSIPSSITS 1458
Cdd:COG3469   149 TTTTVSGTETATGGTTTTSTTTTTTSASTTPSATTTATATTASGATTPSATTTATTTG 206
FhaB COG3210
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ...
 976-1658 6.96e-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: 51.31  E-value: 6.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  976 PSTTNATSSETITSSASANTTTGTTDTVPITTTSFPSTTSVTTNTTVPDTTSPFPTSTTNASTNATVPITTTPFPTSTIG 1055
Cdd:COG3210   306 AGGTGVLGGGTAAGITTTNTVGGNGDGNNTTANSGAGLVSGGTGGNNGTTGTGAGSGLTGTGNGGGLTTAGAGTVASTVG 385

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1056 VTTNATVPNTTApfpTNASTASTNATVPITTTCFATSTIGVTTNATVPDTTAPFPTNTTTASTNATIPITTTPFATSTIS 1135
Cdd:COG3210   386 TATASTGNASST---TVLGSGSLATGNTGTTIAGNGGSANAGGFTTTGGVLGITGNGTVTGGTIGGLTGSGTTNGAGLSG 462

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1136 VTTSTTVPDTTAPFPTSTTSASTNATPVPITTTLFATSTIGVTTGTTVPDTTAPFPTSTTSTSTSATVPITTTPSPTNTA 1215
Cdd:COG3210   463 NTDVSGTGTVTNSAGNTTSATTLAGGGIGTVTTNATISNNAGGDANGIATGLTGITAGGGGGGNATSGGTGGDGTTLSGS 542

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1216 DANTSNTVPNTTMPSPTSSTTVSTIATVPISVTPSLTSTADATISTTVLIATTSSLTGTTDVSTSTTINNISTPVQTNTT 1295
Cdd:COG3210   543 GLTTTVSGGASGTTAASGSNTANTLGVLAATGGTSNATTAGNSTSATGGTGTNSGGTVLSIGTGSAGATGTITLGAGTSG 622

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1296 NASTSTNVANITATSHTSTDDTVPNNTVPVTAIPSLANTGVDTTSNSFSIMTTSFSESTNAMNTTVIMATTSPTSTDVAS 1375
Cdd:COG3210   623 AGANATGGGAGLTGSAVGAALSGTGSGTTGTASANGSNTTGVNTAGGTGGGTTGTVTSGATGGTTGTTLNAATGGTLNNA 702

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1376 TNNDASMTNFLLATMSAGNITSNSISITTTSFGNSVPFVTTPSPSTDATTTSNNTNPGMTTYYQTSPTIPTHTLTSIPSS 1455
Cdd:COG3210   703 GNTLTISTGSITVTGQIGALANANGDTVTFGNLGTGATLTLNAGVTITSGNAGTLSIGLTANTTASGTTLTLANANGNTS 782

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1456 ITSILSmfpTSNTFTTDKITNFTTPTNANTIIFNTLDTKSTMVIDATVTTTSTKDNTMSPDTTVTSIDKFTTHITQFATP 1535
Cdd:COG3210   783 AGATLD---NAGAEISIDITADGTITAAGTTAINVTGSGGTITINTATTGLTGTGDTTSGAGGSNTTDTTTGTTSDGASG 859

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1536 HSATTTTLALSHTSLAPTNLSNLGTMDITDADNSSSVTGNTTHISVSNLTTASVTITATGLDSQTPHMVINSVATYLPIT 1615
Cdd:COG3210   860 GGTAGANSGSLAATAASITVGSGGVATSTGTANAGTLTNLGTTTNAASGNGAVLATVTATGTGGGGLTGGNAAAGGTGAG 939

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|...
gi 767949045 1616 ATSATTDTTNITKYALNTTTPDSTVHTSATAPTYIANAINATQ 1658
Cdd:COG3210   940 NGTTALSGTQGNAGLSAASASDGAGDTGASSAAGSSAVGTSAN 982
FhaB COG3210
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ...
 965-1657 7.97e-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: 50.92  E-value: 7.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  965 TSTIPMSSHPSPSTTNATSSETITSSASANTTTGTTDTVPITTTSFPSTTSVTTNTTVPDTTSPFPTSTTNASTNATVPI 1044
Cdd:COG3210   610 ATGTITLGAGTSGAGANATGGGAGLTGSAVGAALSGTGSGTTGTASANGSNTTGVNTAGGTGGGTTGTVTSGATGGTTGT 689

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1045 TTTPFPTSTIGVTTNATVPNTTAPFPTNASTASTNATVPITTTCFATSTIGVTTNATVPDTTAPFPTNTTTASTNATIPI 1124
Cdd:COG3210   690 TLNAATGGTLNNAGNTLTISTGSITVTGQIGALANANGDTVTFGNLGTGATLTLNAGVTITSGNAGTLSIGLTANTTASG 769

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1125 TTTPFATSTISVTTSTTVPDTTAPFPTSTTSASTNATPVPITTTLFATSTIGVTTGTTVPDTTAPFPTSTTSTSTSATVP 1204
Cdd:COG3210   770 TTLTLANANGNTSAGATLDNAGAEISIDITADGTITAAGTTAINVTGSGGTITINTATTGLTGTGDTTSGAGGSNTTDTT 849

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1205 ITTTPSPTNTADANTSNTVPNTTMPSPTSSTTVSTIATVPISVTPSLTSTADATISTTVLIATTSSLTGTTDVSTSTTIN 1284
Cdd:COG3210   850 TGTTSDGASGGGTAGANSGSLAATAASITVGSGGVATSTGTANAGTLTNLGTTTNAASGNGAVLATVTATGTGGGGLTGG 929

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1285 NISTPVQTNTTNASTSTNVANITATSHTSTDDTVPNNTVPVTAIPSLANTGVDTTSNSFSIMTTSFSESTNAMNTTVIMA 1364
Cdd:COG3210   930 NAAAGGTGAGNGTTALSGTQGNAGLSAASASDGAGDTGASSAAGSSAVGTSANSAGSTGGVIAATGILVAGNSGTTASTT 1009

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1365 TTSPTST-DVASTNNDASMTNFLLATMSAGNITSNSISITTTSFGNSVPFVTTPSPSTDATTTSNNTNPGMTTYYQTSPT 1443
Cdd:COG3210  1010 GGSGAIVaGGNGVTGTTGTASATGTGTAATAGGQNGVGVNASGISGGNAAALTASGTAGTTGGTAASNGGGGTAQASGAG 1089

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1444 IPTHTLTSIPSSITSILSMFPTSNTFTTDKITNFTTPTNANTIIFNTLDTKSTMVIDATVTTTSTKDNTMSPDTTVTSID 1523
Cdd:COG3210  1090 TTHTLGGITNGGATGTSGGTTTSTGGVTASKVGGTTTVGATGTSTASTEAAGAGTLTGLVAVSAVAGGASSASAGDTTAV 1169

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1524 KFTTHITQFATPHSATTTTLALSHTSLAPTNLSNLGTMDITDADNSSSVTGNTTHISVSNLTTASVTITATGLDSQTPHM 1603
Cdd:COG3210  1170 AAATTTTTGSAINGGADSAATEGTAGTDLKGGDSTGGSTTTIGTTNVTTTTTLTASDTGNTTATGGSSAGQTGSFVAAGS 1249

                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767949045 1604 VINSVATYLPITATSATTDTTNITKYALNTTTPDSTVHTSATAPTYIANAINAT 1657
Cdd:COG3210  1250 ASGTGDATTGATAGAVSNGATSTVAGNAGATATGSTVDIGSTSATSAGGSLDTT 1303
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 1246-1485 1.21e-05

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: 49.96  E-value: 1.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  1246 SVTPSLTSTADATISTTVLIATTSSLTGTTDVSTSTTINNISTPVQTNTTNASTSTNVANITATSHTSTDDTVPNNTVPV 1325
Cdd:pfam17823  109 GAASRALAAAASSSPSSAAQSLPAAIAALPSEAFSAPRAAACRANASAAPRAAIAAASAPHAASPAPRTAASSTTAASST 188

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  1326 TAIPSLANTGvdtTSNSFSIMTTSFSESTNAMNTTVIMATTS----PTSTDVASTNNDASMTNFLLA----TMSAGNITS 1397
Cdd:pfam17823  189 TAASSAPTTA---ASSAPATLTPARGISTAATATGHPAAGTAlaavGNSSPAAGTVTAAVGTVTPAAlatlAAAAGTVAS 265

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  1398 NSISITTTSfgnsvPFVTTPSPSTDATTTSNNTNPGMTTYYQTSPTI-------PTHTLTSIPSSITSILSMFPTSNTFT 1470
Cdd:pfam17823  266 AAGTINMGD-----PHARRLSPAKHMPSDTMARNPAAPMGAQAQGPIiqvstdqPVHNTAGEPTPSPSNTTLEPNTPKSV 340

                          250
                   ....*....|....*
gi 767949045  1471 TDKITNFTTPTNANT 1485
Cdd:pfam17823  341 ASTNLAVVTTTKAQA 355
Chi1 COG3469
Chitinase [Carbohydrate transport and metabolism];
1207-1450 2.18e-05

Chitinase [Carbohydrate transport and metabolism];


Pssm-ID: 442692 [Multi-domain]  Cd Length: 534  Bit Score: 48.98  E-value: 2.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1207 TTPSPTNTADANTSNTVPNTTMPSPTSSTTVSTIATVPISVTPSLTSTADATISTTVLIATTSSLTGTTDVSTSTTINNI 1286
Cdd:COG3469     6 TAASPTAGGASATAVTLLGAAATAASVTLTAATATTVVSTTGSVVVAASGSAGSGTGTTAASSTAATSSTTSTTATATAA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1287 STPVQTNTTNASTSTNVANITATSHTSTDDTVPNNTVPVTaipSLANTGVDTTSNSFSIMTTSFSESTNAMNTTVIMATT 1366
Cdd:COG3469    86 AAAATSTSATLVATSTASGANTGTSTVTTTSTGAGSVTST---TSSTAGSTTTSGASATSSAGSTTTTTTVSGTETATGG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1367 SPTSTDVASTnndasmtnfllatmsagnitsnsisiTTTSFGNSVPFVTTPSPSTDATTTSNNTNPGMTTyyQTSPTIPT 1446
Cdd:COG3469   163 TTTTSTTTTT--------------------------TSASTTPSATTTATATTASGATTPSATTTATTTG--PPTPGLPK 214


                  ....
gi 767949045 1447 HTLT 1450
Cdd:COG3469   215 HVLV 218
PHA03255 PHA03255
BDLF3; Provisional
 1345-1497 5.92e-05

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 46.44  E-value: 5.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1345 IMTTSFSESTNAMNTTVIMATTSPT-STDVASTNNDASMTNfllatmsagniTSNSISITTTSFGNSVPFVTTPSPSTDA 1423
Cdd:PHA03255   23 IWTSSGSSTASAGNVTGTTAVTTPSpSASGPSTNQSTTLTT-----------TSAPITTTAILSTNTTTVTSTGTTVTPV 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767949045 1424 TTTSNNTNPGMTTYYQTSPTIPTHTLTSIPSSITSILSMFPTSNTFTTDKITNFTT--PTNANTIIFNTLDTKSTM 1497
Cdd:PHA03255   92 PTTSNASTINVTTKVTAQNITATEAGTGTSTGVTSNVTTRSSSTTSATTRITNATTlaPTLSSKGTSNATKTTAEL 167
Chi1 COG3469
Chitinase [Carbohydrate transport and metabolism];
950-1162 6.57e-05

Chitinase [Carbohydrate transport and metabolism];


Pssm-ID: 442692 [Multi-domain]  Cd Length: 534  Bit Score: 47.44  E-value: 6.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  950 VTWIDGGPVLPTPTKTSTIPMSSHPSPSTTNATSSETITSSASANTTTGTTDTVPITTTSFPSTTSVTTNTTVPDTTSPF 1029
Cdd:COG3469     4 VSTAASPTAGGASATAVTLLGAAATAASVTLTAATATTVVSTTGSVVVAASGSAGSGTGTTAASSTAATSSTTSTTATAT 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1030 ptsttnASTNATVPITTTPFPTSTIGVTTNATVPNTTAPFPTNASTASTNATVPITTTCFATSTIGVTTNATVPDTTAPF 1109
Cdd:COG3469    84 ------AAAAAATSTSATLVATSTASGANTGTSTVTTTSTGAGSVTSTTSSTAGSTTTSGASATSSAGSTTTTTTVSGTE 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767949045 1110 PTNTTTASTNATIPITTTPFATSTISVTTSTTVPDTTAPFPTSTTSASTNATP 1162
Cdd:COG3469   158 TATGGTTTTSTTTTTTSASTTPSATTTATATTASGATTPSATTTATTTGPPTP 210
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 1305-1488 1.89e-04

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: 46.44  E-value: 1.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1305 NITATSHTSTDDTVPNNTVPVTAIPSLANTGVD---TTSNSFSIMT----------TSFSESTNA-MNTTVIMATTSPTS 1370
Cdd:NF033609   42 NSVTQSDSASNESKSNDSSSVSAAPKTDDTNVSdtkTSSNTNNGETsvaqnpaqqeTTQSASTNAtTEETPVTGEATTTA 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1371 TDVAST--NNDASMTNfllaTMSAGNITSNSisiTTTSFGNSVPFVTTPSPSTDA------------TTTSNNTNPGMTT 1436
Cdd:NF033609  122 TNQANTpaTTQSSNTN----AEELVNQTSNE---TTSNDTNTVSSVNSPQNSTNAenvsttqdtsteATPSNNESAPQST 194

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767949045 1437 YYQTSPTIPTHTLTSIPS----SITSILSMFPTSNTFTTDKITNFTTPTNANTIIF 1488
Cdd:NF033609  195 DASNKDVVNQAVNTSAPRmrafSLAAVAADAPAAGTDITNQLTNVTVGIDSGTTVY 250
PHA03255 PHA03255
BDLF3; Provisional
 1415-1574 2.34e-04

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 44.51  E-value: 2.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1415 TTPSPSTDATTTSNNTNPGMTTYYQTSPTIPTHTLTSIPSSITSILSMFPTSNTFTTDKITNFTTPTNANTIIFNTLDTK 1494
Cdd:PHA03255   29 SSTASAGNVTGTTAVTTPSPSASGPSTNQSTTLTTTSAPITTTAILSTNTTTVTSTGTTVTPVPTTSNASTINVTTKVTA 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1495 STmvIDATVTTTSTKDNTMSPDTT-VTSIDKFTTHITqfatphSATTTTLALSHTSLAPTNLSNLGTMDITDADNSSSVT 1573
Cdd:PHA03255  109 QN--ITATEAGTGTSTGVTSNVTTrSSSTTSATTRIT------NATTLAPTLSSKGTSNATKTTAELPTVPDERQPSLSY 180


                  .
gi 767949045 1574 G 1574
Cdd:PHA03255  181 G 181
COG4935 COG4935
Regulatory P domain of the subtilisin-like proprotein convertases and other proteases ...
 981-1457 2.96e-04

Regulatory P domain of the subtilisin-like proprotein convertases and other proteases [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443962 [Multi-domain]  Cd Length: 641  Bit Score: 45.58  E-value: 2.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  981 ATSSETITSSASANTTTGTTDTVPITTTSFPSTTSVTTNTTVPDTTSPFPTSTTNASTNATVPITTTPFPTSTIGVTTNA 1060
Cdd:COG4935    72 AASGAAAGAVDAAPAAATVVGAALGVVAVAGAGLAATASGAAAGAVAAAANGNTGAGPGSGGTGGGSGGAGAAAAAAALS 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1061 TVPNTTAPFPTNASTASTNATVPITTTCFATSTIGVTTNATVPDTTAPFPTNTTTASTNATIPITTTPFATSTISVTTST 1140
Cdd:COG4935   152 AAGAAVGVAAVAGAAGGGGGVGVAAAVGVVLGAGLVADGGNGGGGAVAGGAAGGGGGGGGGGGLGGAAGGGGAGLAAAGG 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1141 TVPDTTAPFPTSTTSASTNATPVPITTTLFATSTIGVTTGTTVPDTTAPFPTSTTSTSTSATVPITTTPSPTNTADANTS 1220
Cdd:COG4935   232 GGGGAAAAAAAGVGGLGAAATAAAADGGGGGGAGAAGAGGSAGAAAGGAGAGVVGAAAGGGDAALGGAVGAAGTGNAAAA 311

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1221 NTVPNTTMPSPTSSTTVSTIATVPISVTPSLTSTADATISTTVLIATTSSLTGTTDVSTSTTINNISTPVQTNTTNASTS 1300
Cdd:COG4935   312 AAASAGSGGGGGSAAAAGAAAAAAAAAAGAAAGVSGAASVVAGASGGGAGTAAAAGGGAAAAAAGGAAAAGAAAGAAAGA 391

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1301 TNVANITATSHTSTDDTVPNNTVPVTAIPSLANTGVDTTSNSFSIMTTSFSESTNAMNTTVIMATTSPTSTDVASTNNDA 1380
Cdd:COG4935   392 AAGAAAAGGVASAAGAVGAGTAAGASATAAVSTGAASGSSTTSSTGTTATATGLGGGADAGSTSTGTGSAAGAAGGTTTA 471

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767949045 1381 SMTNFLLATMSAGNITSNSISITTTSFGNSVPFVTTPSPSTDATTTSNNTNPGMTTYYQTSP--TIPTHTLTSIPSSIT 1457
Cdd:COG4935   472 TSGLASSTTAAAAAAAAGLATTAAVAAGAAGAAAAAATAASVGGATGAAGTTNSTATFSNTTdvAIPDNGPAGVTSTIT 550
Chi1 COG3469
Chitinase [Carbohydrate transport and metabolism];
1203-1381 3.57e-04

Chitinase [Carbohydrate transport and metabolism];


Pssm-ID: 442692 [Multi-domain]  Cd Length: 534  Bit Score: 45.13  E-value: 3.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1203 VPITTTPSPTNTADANTSNTVPNTTMPSPTSSTTVSTIATVPISVTPSLTSTADATISTTVLIATTSSLTGTTDVSTSTT 1282
Cdd:COG3469    30 ASVTLTAATATTVVSTTGSVVVAASGSAGSGTGTTAASSTAATSSTTSTTATATAAAAAATSTSATLVATSTASGANTGT 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1283 INNISTPV-QTNTTNASTSTNVANITATSHTSTDDTVPNNTVPVTAIPSLANTGVDTTSNSFSIMTTSFSESTNAMNTTV 1361
Cdd:COG3469   110 STVTTTSTgAGSVTSTTSSTAGSTTTSGASATSSAGSTTTTTTVSGTETATGGTTTTSTTTTTTSASTTPSATTTATATT 189

                         170       180
                  ....*....|....*....|
gi 767949045 1362 IMATTSPTSTDVASTNNDAS 1381
Cdd:COG3469   190 ASGATTPSATTTATTTGPPT 209
Chi1 COG3469
Chitinase [Carbohydrate transport and metabolism];
1307-1497 4.09e-04

Chitinase [Carbohydrate transport and metabolism];


Pssm-ID: 442692 [Multi-domain]  Cd Length: 534  Bit Score: 45.13  E-value: 4.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1307 TATSHTSTDDTVPNNTVPVTAIPSLANTGVDTTSNSFSIMTTSFSESTNAMN--TTVIMATTSPTSTDVASTNNDASMTN 1384
Cdd:COG3469    13 GGASATAVTLLGAAATAASVTLTAATATTVVSTTGSVVVAASGSAGSGTGTTaaSSTAATSSTTSTTATATAAAAAATST 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1385 FLLATMSAGNITSNSISITTTSFGNSVPFVTTPSPSTDATTTSNNTNPGMTTYYQTSPTIPTHTLTSIPSSITSILSMFP 1464
Cdd:COG3469    93 SATLVATSTASGANTGTSTVTTTSTGAGSVTSTTSSTAGSTTTSGASATSSAGSTTTTTTVSGTETATGGTTTTSTTTTT 172

                         170       180       190
                  ....*....|....*....|....*....|...
gi 767949045 1465 TSNTFTTDKITNFTTPTNANTIIFNTLDTKSTM 1497
Cdd:COG3469   173 TSASTTPSATTTATATTASGATTPSATTTATTT 205
Chi1 COG3469
Chitinase [Carbohydrate transport and metabolism];
1309-1542 5.03e-04

Chitinase [Carbohydrate transport and metabolism];


Pssm-ID: 442692 [Multi-domain]  Cd Length: 534  Bit Score: 44.74  E-value: 5.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1309 TSHTSTDDTVPNNTVPVTAIPSLANTGVDTTSNSFSIMTTSFSESTNAMNTTVIMATTSPTSTDVASTNNDASMTNFLLA 1388
Cdd:COG3469     1 SSSVSTAASPTAGGASATAVTLLGAAATAASVTLTAATATTVVSTTGSVVVAASGSAGSGTGTTAASSTAATSSTTSTTA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1389 TMSAGnitsnsisiTTTSFGNSVPFVTTPSPSTDATTTSNNTNpgmTTYYQTSPTIPTHTLTSIPSSITSILSMFPTSNT 1468
Cdd:COG3469    81 TATAA---------AAAATSTSATLVATSTASGANTGTSTVTT---TSTGAGSVTSTTSSTAGSTTTSGASATSSAGSTT 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767949045 1469 FTTDKITNFTTPTnantiifntldtkstmviDATVTTTSTKDNTMSPDTTVTSIDKFTTHITQFATPHSATTTT 1542
Cdd:COG3469   149 TTTTVSGTETATG------------------GTTTTSTTTTTTSASTTPSATTTATATTASGATTPSATTTATT 204
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 1322-1647 5.36e-04

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: 44.91  E-value: 5.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  1322 TVPVTAIpsLANTGVDTTSNSFSIMTTSFSESTNA---MNTTVIMA----TTSPTSTDVASTNNDASMTNfllATMSAGN 1394
Cdd:pfam05109  398 TAPKTLI--ITRTATNATTTTHKVIFSKAPESTTTsptLNTTGFAApnttTGLPSSTHVPTNLTAPASTG---PTVSTAD 472

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  1395 ITSNSISITTTSfgnSVPFVTTPSPSTDATTTSNntnPGMTTYyQTSPTIPTHTLTSIPSSITSilsmfPTSNtfttdki 1474
Cdd:pfam05109  473 VTSPTPAGTTSG---ASPVTPSPSPRDNGTESKA---PDMTSP-TSAVTTPTPNATSPTPAVTT-----PTPN------- 533

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  1475 tnFTTPTNANTIIFNTLDTKSTMVIDAT-VTTTSTKDNTM------SPDTTVTSIDKFTTHITQFATPHSATTTTLALSH 1547
Cdd:pfam05109  534 --ATSPTLGKTSPTSAVTTPTPNATSPTpAVTTPTPNATIptlgktSPTSAVTTPTPNATSPTVGETSPQANTTNHTLGG 611

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  1548 TSLAPTnlsnlgtmdITDADNSSSVTGNTTHISVSNLTTASVTITATGLDSQTPHMVINSVATYLPITATSATTDTTNIT 1627
Cdd:pfam05109  612 TSSTPV---------VTSPPKNATSAVTTGQHNITSSSTSSMSLRPSSISETLSPSTSDNSTSHMPLLTSAHPTGGENIT 682

                          330       340
                   ....*....|....*....|
gi 767949045  1628 KYalnTTTPDSTVHTSATAP 1647
Cdd:pfam05109  683 QV---TPASTSTHHVSTSSP 699
PHA03255 PHA03255
BDLF3; Provisional
 1329-1458 6.87e-04

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 43.35  E-value: 6.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1329 PSLANTGvdTTSNSFSIMTTSFSESTNAMNTTVIMATTSPTSTDVASTNNDASMTNFLLATMSAGNITSNSISITTTSFG 1408
Cdd:PHA03255   29 SSTASAG--NVTGTTAVTTPSPSASGPSTNQSTTLTTTSAPITTTAILSTNTTTVTSTGTTVTPVPTTSNASTINVTTKV 106

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767949045 1409 NSVPFVTTPS-PSTDATTTSNNTNPGMTTYYQTSPTIPTHTLTSIPSSITS 1458
Cdd:PHA03255  107 TAQNITATEAgTGTSTGVTSNVTTRSSSTTSATTRITNATTLAPTLSSKGT 157
GH31_glucosidase_YihQ cd06594
alpha-glucosidase YihQ-like; YihQ is a bacterial alpha-glucosidase with a conserved glycosyl ...
 580-683 1.20e-03

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: 1.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  580 VHNLYG--WSQTrpTYEAVQEVTGQRGVII-TRSTFPSSGR-----WGGHRLGNntaaW---DQLGKSIIGMMEFSLFGI 648
Cdd:cd06594   184 YHNRYPelWARL--NREAVEEAGKEGEIVFfMRSGYTGSPRystlfWAGDQNVD----WsrdDGLKSVIPGALSSGLSGF 257

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 767949045  649 PYTGADICG----FFGDAEY----EMCVRWMQLGAFYPFSRNH 683
Cdd:cd06594   258 SLTHSDIGGyttlFNPLVGYkrskELLMRWAEMAAFTPVMRTH 300
34 PHA02584
long tail fiber, proximal subunit; Provisional
 1242-1522 1.56e-03

long tail fiber, proximal subunit; Provisional


Pssm-ID: 222890 [Multi-domain]  Cd Length: 1229  Bit Score: 43.59  E-value: 1.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1242 TVPISVTPSLTSTADATISTTVLIATTSSLTGTTDVSTSTTINNISTP-VQTNTTNASTSTNVANITATSHTSTDDTVPn 1320
Cdd:PHA02584  902 DIDQTVNGSLTFTKNTNLSAPLVSSSTATFGGSVTANSTLTTQNTSNGtVVVVDETSIAFYSQNNTTGNIVFNIDGTVD- 980

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1321 nTVPVTAIPSLANTGVDTTSNSfSIMTTSFSESTNAMNTTV---IMATTSPTSTDVASTNNDASMTNFLLATMSAGNITS 1397
Cdd:PHA02584  981 -PINVNANGTLNATGVATNGRA-VYAEGGGIARTNNAARAItggFTIRNDGSTTVFLLTAAGDQTGGFNGLKSLIINNAN 1058

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1398 NSISITTTSFGNSVPFVTTPSPSTDATTTSNNTNPGMTtyyqTSPTIPTHTLTSIPSSITSILSMFPTSNTFTTDKITNF 1477
Cdd:PHA02584 1059 GQVTINDNYIINAGGTIMSGGLTVNSRIRSQGTKASYT----RAPTADTVGFWSVDINDSATYNQFPGYFQMVTKTKSPG 1134

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 767949045 1478 TTPTNANTIIFNTLDTKSTmviDATVTTTSTKDNTMSPDTTVTSI 1522
Cdd:PHA02584 1135 TLTQFGNTLDSLYQDWSPD---GRTTRYTRTWQKNKNAWTSFGEV 1176
Chi1 COG3469
Chitinase [Carbohydrate transport and metabolism];
1035-1228 1.59e-03

Chitinase [Carbohydrate transport and metabolism];


Pssm-ID: 442692 [Multi-domain]  Cd Length: 534  Bit Score: 43.20  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1035 NASTNATVPITTTPFPTSTIGVTTNATVPNTTAPFPTNASTASTNATVPITTTCFATSTIGVTTNATVPDTTAPFPTNTT 1114
Cdd:COG3469    15 ASATAVTLLGAAATAASVTLTAATATTVVSTTGSVVVAASGSAGSGTGTTAASSTAATSSTTSTTATATAAAAAATSTSA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1115 TASTNATIPITTTPFATSTISVTTSTTVPDTTAPFPTSTTSASTNATPVPITTTLfatSTIGVTTGTTVPDTTAPFPTST 1194
Cdd:COG3469    95 TLVATSTASGANTGTSTVTTTSTGAGSVTSTTSSTAGSTTTSGASATSSAGSTTT---TTTVSGTETATGGTTTTSTTTT 171

                         170       180       190
                  ....*....|....*....|....*....|....
gi 767949045 1195 TSTSTSATVPITTTPSPTNTADANTSNTVPNTTM 1228
Cdd:COG3469   172 TTSASTTPSATTTATATTASGATTPSATTTATTT 205
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 1050-1279 1.81e-03

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: 43.02  E-value: 1.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  1050 PTSTIGVTTNATVPNTTAPFPTNASTASTnATVPITTTCFATSTIGVTTNATVPDTTAPFPTNTTTASTNATIPITTTPF 1129
Cdd:pfam17823  118 AASSSPSSAAQSLPAAIAALPSEAFSAPR-AAACRANASAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAASSAPT 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  1130 -ATSTISVTTSTTVPDTTAPFPTSTTSASTNATPVPITTTL---FATSTIGVTTGTTVPDTTAPFPTSTTSTSTSATVPI 1205
Cdd:pfam17823  197 tAASSAPATLTPARGISTAATATGHPAAGTALAAVGNSSPAagtVTAAVGTVTPAALATLAAAAGTVASAAGTINMGDPH 276

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767949045  1206 TTTPSPTNTADANTSNTVPNTTMPSPTSSTTVSTIATVPI-----SVTPSLTSTADATISTTVLIATTSSLTGTTDVST 1279
Cdd:pfam17823  277 ARRLSPAKHMPSDTMARNPAAPMGAQAQGPIIQVSTDQPVhntagEPTPSPSNTTLEPNTPKSVASTNLAVVTTTKAQA 355
PRK10856 PRK10856
cytoskeleton protein RodZ;
1037-1110 2.72e-03

cytoskeleton protein RodZ;


Pssm-ID: 236776 [Multi-domain]  Cd Length: 331  Bit Score: 41.94  E-value: 2.72e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767949045 1037 STNATVPITTTPFPTSTIGVT-TNATVPNTTAPfPTNASTASTNATVPITTTCFATSTIGVTTNATVPDTTAPFP 1110
Cdd:PRK10856  165 DTSTTTDPATTPAPAAPVDTTpTNSQTPAVATA-PAPAVDPQQNAVVAPSQANVDTAATPAPAAPATPDGAAPLP 238
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 1240-1515 2.76e-03

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: 42.25  E-value: 2.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  1240 IATVPISVTPSLTSTADATI-STTVLIATTSSLTGTTDVSTS-----------TTINNISTPVQTNTTNASTSTNVANIT 1307
Cdd:pfam17823   62 AATAAPAPVTLTKGTSAAHLnSTEVTAEHTPHGTDLSEPATRegaadgaasraLAAAASSSPSSAAQSLPAAIAALPSEA 141

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  1308 ATSHTSTDDTVPNNTVPVTAIPSLANTGVDTTSNSFSIMTTSFSESTNAMNTTVIMATTSPTSTDVASTNNDASMTNflL 1387
Cdd:pfam17823  142 FSAPRAAACRANASAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAASSAPTTAASSAPATLTPARGISTAATA--T 219

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  1388 ATMSAGNITSnSISITTTSFGNSVPFVTTPSPSTDATTTSN-----------NTNPGMTTYYQTSPTIPTHTLTSIPSSI 1456
Cdd:pfam17823  220 GHPAAGTALA-AVGNSSPAAGTVTAAVGTVTPAALATLAAAagtvasaagtiNMGDPHARRLSPAKHMPSDTMARNPAAP 298

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767949045  1457 TSILSMFPTSNTFTTDKITNFT---TPTNANTIIFNTLDTKSTMVIDATVTTT--STKDNTMSP 1515
Cdd:pfam17823  299 MGAQAQGPIIQVSTDQPVHNTAgepTPSPSNTTLEPNTPKSVASTNLAVVTTTkaQAKEPSASP 362
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 1321-1658 4.08e-03

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: 41.87  E-value: 4.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  1321 NTVPVTAIPSLANTGVDTTSNSFSIMTTSFSESTNAMNTTVIMATTSPTSTDVA--STNNDASMTNFLLATMSAGNITSN 1398
Cdd:pfam17823   45 DAVPRADNKSSEQ*NFCAATAAPAPVTLTKGTSAAHLNSTEVTAEHTPHGTDLSepATREGAADGAASRALAAAASSSPS 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  1399 SISITTTSFGNSVPFVTTPSPSTDATTTSNNTNPGMTTYYQTSPTIPTHTLTSIPSSITSILSMFPTSNTFTTDKITNFT 1478
Cdd:pfam17823  125 SAAQSLPAAIAALPSEAFSAPRAAACRANASAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAASSAPTTAASSAPA 204

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  1479 TPTNANTIIFNTLdtkSTMVIDATVTTTSTKDNTMSPDTTVTSIDKFTTHITQFATPHSATTTTLALSHTSLAP--TNLS 1556
Cdd:pfam17823  205 TLTPARGISTAAT---ATGHPAAGTALAAVGNSSPAAGTVTAAVGTVTPAALATLAAAAGTVASAAGTINMGDPhaRRLS 281

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  1557 NLGTMDI-TDADNSSSVTGNTTHISVSNLTTASVTITATGLDSQTPHMVINSVATYLPITATSATTDTTNITKYALNTTT 1635
Cdd:pfam17823  282 PAKHMPSdTMARNPAAPMGAQAQGPIIQVSTDQPVHNTAGEPTPSPSNTTLEPNTPKSVASTNLAVVTTTKAQAKEPSAS 361

                          330       340
                   ....*....|....*....|....*....
gi 767949045  1636 PDSTVHTS------ATAPTYIANAINATQ 1658
Cdd:pfam17823  362 PVPVLHTSmipeveATSPTTQPSPLLPTQ 390
COG4935 COG4935
Regulatory P domain of the subtilisin-like proprotein convertases and other proteases ...
 1067-1627 4.94e-03

Regulatory P domain of the subtilisin-like proprotein convertases and other proteases [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443962 [Multi-domain]  Cd Length: 641  Bit Score: 41.73  E-value: 4.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1067 APFPTNASTASTNATVPITTTCFATSTIGVTTNATVPDTTAPFPTNTTTASTNATIPITTTPFATSTISVTTSTTVPDTT 1146
Cdd:COG4935     6 AGSTTGLAAAVLAAAAGTGSAATAEGGAASTATSAAVAGASAAAAAATAVGAGASSLAASAAAAAAAASGAAAGAVDAAP 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1147 APFPTSTTSASTNATPVPITTTLFATSTIGVTTGTTVPDTTAPFPTSTTSTSTSATVPITTTPSPTNTADANTSNTVPNT 1226
Cdd:COG4935    86 AAATVVGAALGVVAVAGAGLAATASGAAAGAVAAAANGNTGAGPGSGGTGGGSGGAGAAAAAAALSAAGAAVGVAAVAGA 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1227 TMPSPTSSTTVSTIATVPISVTPSLTSTADATISTTVLIATTSSLTGTTDVSTSTTINNISTPVQTNTTNASTSTNVANI 1306
Cdd:COG4935   166 AGGGGGVGVAAAVGVVLGAGLVADGGNGGGGAVAGGAAGGGGGGGGGGGLGGAAGGGGAGLAAAGGGGGGAAAAAAAGVG 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1307 TATSHTSTDDTVPNNTVPVTAIPSLANTGVDTTSNSFSIMTTSFSESTNAMNTTVIMATTSPTSTDVASTNNDASMTNFL 1386
Cdd:COG4935   246 GLGAAATAAAADGGGGGGAGAAGAGGSAGAAAGGAGAGVVGAAAGGGDAALGGAVGAAGTGNAAAAAAASAGSGGGGGSA 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1387 LATMSAGNITSNSISITTTSFGNSVPFVTTPSPSTDATTTSNNTNPGMTTYYQTSPTIPTHTltsipssitsilsmfpTS 1466
Cdd:COG4935   326 AAAGAAAAAAAAAAGAAAGVSGAASVVAGASGGGAGTAAAAGGGAAAAAAGGAAAAGAAAGA----------------AA 389

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1467 NTFTTDKITNFTTPTNANTIIFNTLDTKSTMVIDATVTTTSTKDNTMSPDTTVTSIDKFTTHITQFATPHSATTTTLALS 1546
Cdd:COG4935   390 GAAAGAAAAGGVASAAGAVGAGTAAGASATAAVSTGAASGSSTTSSTGTTATATGLGGGADAGSTSTGTGSAAGAAGGTT 469

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1547 HTSLAPTNLSNLGTMDITDADNSSSVTGNTTHISVSNLTTASVTITATGLDSQTPHMVINSVATYLPITATSATTDTTNI 1626
Cdd:COG4935   470 TATSGLASSTTAAAAAAAAGLATTAAVAAGAAGAAAAAATAASVGGATGAAGTTNSTATFSNTTDVAIPDNGPAGVTSTI 549


                  .
gi 767949045 1627 T 1627
Cdd:COG4935   550 T 550
FhaB COG3210
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ...
 977-1659 5.97e-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: 41.68  E-value: 5.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  977 STTNATSSETITSSASANTTTGTTDTVPITTTSFPSTTSVTTNTTVPDTTSPFPTSTTNASTNATVPITTTPFPTSTIGV 1056
Cdd:COG3210   499 ISNNAGGDANGIATGLTGITAGGGGGGNATSGGTGGDGTTLSGSGLTTTVSGGASGTTAASGSNTANTLGVLAATGGTSN 578

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1057 TTNATVPNTTAPFPTNASTASTNATVPITTTCFATSTIGVTTNATVPDTTAPFPTNTTTASTNATIPITTTPFATSTISV 1136
Cdd:COG3210   579 ATTAGNSTSATGGTGTNSGGTVLSIGTGSAGATGTITLGAGTSGAGANATGGGAGLTGSAVGAALSGTGSGTTGTASANG 658

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1137 TTSTTVPDTTAPFPTSTTSASTNATPVPITTTLFATSTIGVTTGTTVPDTTAPFPTSTTSTSTSATVP------ITTTPS 1210
Cdd:COG3210   659 SNTTGVNTAGGTGGGTTGTVTSGATGGTTGTTLNAATGGTLNNAGNTLTISTGSITVTGQIGALANANgdtvtfGNLGTG 738

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1211 PTNTADAN-TSNTVPNTTMPSPTSSTTVSTIATVPISVTPSLTSTADATISTTVLIATTSSLTGTTDVSTSTTINNISTP 1289
Cdd:COG3210   739 ATLTLNAGvTITSGNAGTLSIGLTANTTASGTTLTLANANGNTSAGATLDNAGAEISIDITADGTITAAGTTAINVTGSG 818

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1290 VQTNTTNASTStnVANITATSHTSTDDTVPNNTVPVTAIPSLANTGVDTTSNSFSIMTTSFSESTNAMNTTVIMATTSPT 1369
Cdd:COG3210   819 GTITINTATTG--LTGTGDTTSGAGGSNTTDTTTGTTSDGASGGGTAGANSGSLAATAASITVGSGGVATSTGTANAGTL 896

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1370 STDVASTNNDASMTNFLLATMSAGNITSNSISITTTSFGNSVPFVTTPSPSTDATTTSNNTNPGMTTYYQTSPTIPTHTL 1449
Cdd:COG3210   897 TNLGTTTNAASGNGAVLATVTATGTGGGGLTGGNAAAGGTGAGNGTTALSGTQGNAGLSAASASDGAGDTGASSAAGSSA 976

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1450 TSIPSSITSILSMFPTSNTFTTDKITNFTTPTNANTIIFNTLDTKSTMVIDATVTTTSTKDNTMSPDTTVTSIDKFTTHI 1529
Cdd:COG3210   977 VGTSANSAGSTGGVIAATGILVAGNSGTTASTTGGSGAIVAGGNGVTGTTGTASATGTGTAATAGGQNGVGVNASGISGG 1056

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1530 TQFATPHSATTTTLALSHTSLAPTNLSNLGTMDITDADNSSSVTGNTTHISVSNLTTASVTITATGLDSQTPHMVINSVA 1609
Cdd:COG3210  1057 NAAALTASGTAGTTGGTAASNGGGGTAQASGAGTTHTLGGITNGGATGTSGGTTTSTGGVTASKVGGTTTVGATGTSTAS 1136

                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|
gi 767949045 1610 TYLPITATSATTDTTNITKYALNTTTPDSTVHTSATAPTYIANAINATQV 1659
Cdd:COG3210  1137 TEAAGAGTLTGLVAVSAVAGGASSASAGDTTAVAAATTTTTGSAINGGAD 1186
Chi1 COG3469
Chitinase [Carbohydrate transport and metabolism];
951-1162 6.24e-03

Chitinase [Carbohydrate transport and metabolism];


Pssm-ID: 442692 [Multi-domain]  Cd Length: 534  Bit Score: 41.28  E-value: 6.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  951 TWIDGGPVLPTPTKTSTIPMSSHPSPSTTNATSSETITSSASANTTTGTTDTVPITTTSFPSTTSVTTNTTVPDTTSPFP 1030
Cdd:COG3469    15 ASATAVTLLGAAATAASVTLTAATATTVVSTTGSVVVAASGSAGSGTGTTAASSTAATSSTTSTTATATAAAAAATSTSA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1031 TSTTNASTNATVPITTTPFPTSTiGVTTNATVPNTTAPFPTNASTASTNATVPITTTCFATSTIGVTTNATVPDTTAPFP 1110
Cdd:COG3469    95 TLVATSTASGANTGTSTVTTTST-GAGSVTSTTSSTAGSTTTSGASATSSAGSTTTTTTVSGTETATGGTTTTSTTTTTT 173

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767949045 1111 TNtttastnatipiTTTPFATSTISVTTSTTVPDTTAPFPTSTTSASTNATP 1162
Cdd:COG3469   174 SA------------STTPSATTTATATTASGATTPSATTTATTTGPPTPGLP 213
PRK08026 PRK08026
FliC/FljB family flagellin;
1266-1526 6.71e-03

FliC/FljB family flagellin;


Pssm-ID: 236140 [Multi-domain]  Cd Length: 529  Bit Score: 40.88  E-value: 6.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1266 ATTSSLTGTTDVSTSTTINNISTpvqtnttnaststnvaNITATSHTSTDDTVPNNTvPVTAIPSLANTGVDTTSNSFSI 1345
Cdd:PRK08026  186 ATVSDLTAAGATLDTTGLYDVKT----------------KNAALTTADALAKLGDGD-KVTATATGGDYTYNAKSGKYQA 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1346 MTTSFSESTNAMNTTVIMATTSPTSTDV-ASTNNDASMTNFLLATMSAGNITSNSISITTTSfgnSVPFVTTPSPSTDAT 1424
Cdd:PRK08026  249 ADLAATLTPDVGGTAGASYTIKDGTYEVnVDSDGKITLGGSALYIDATGNLTTNNAGAATKA---TLDALKKTASEGAAT 325

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1425 TTSNNTNPGMTTYYQTSPTIPTHTLTSIPSSITSILSMFPTSNTFTTDKITNFTTPTNANTIIFntLDTkstmviDATVT 1504
Cdd:PRK08026  326 AKAALAAAGVTVADGVTAKTVKMSYTDKNGKVIDGGYAVKTGDDYYAADYDEITGAISATTTYY--TAK------DGTTK 397

                         250       260
                  ....*....|....*....|..
gi 767949045 1505 TTSTKDNTMSPDTTVTSIDKFT 1526
Cdd:PRK08026  398 TAANKLGGADGKTEVVTIDGKT 419
FhaB COG3210
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ...
 975-1657 8.23e-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: 41.29  E-value: 8.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045  975 SPSTTNATSSETITSSASANTTTGTTDTVPITTTSFPSTTSVTTNTTVPDTTSPFPTSTTNASTNATVPITTTPFPTSTI 1054
Cdd:COG3210   490 IGTVTTNATISNNAGGDANGIATGLTGITAGGGGGGNATSGGTGGDGTTLSGSGLTTTVSGGASGTTAASGSNTANTLGV 569

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1055 GVTTNATVPNTTAPFPTNASTASTNATVPITTTCFATSTIGVTTNATVPDTTAPFPTNTTTASTNATIPITTTPFATSTI 1134
Cdd:COG3210   570 LAATGGTSNATTAGNSTSATGGTGTNSGGTVLSIGTGSAGATGTITLGAGTSGAGANATGGGAGLTGSAVGAALSGTGSG 649

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1135 SVTTSTTVPDTTAPFPTSTTSASTNATPVPITTTLFATSTIGVTTGTTVPDTTAPFPTSTTSTSTSATVPITTTPSPTNT 1214
Cdd:COG3210   650 TTGTASANGSNTTGVNTAGGTGGGTTGTVTSGATGGTTGTTLNAATGGTLNNAGNTLTISTGSITVTGQIGALANANGDT 729

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1215 ADANTSNTVPNTTMPSPTSSTTVSTIATVPISVTPSLTSTADATISTTVLIATTSSLTGTTDVSTSTTINNISTPVQTNT 1294
Cdd:COG3210   730 VTFGNLGTGATLTLNAGVTITSGNAGTLSIGLTANTTASGTTLTLANANGNTSAGATLDNAGAEISIDITADGTITAAGT 809

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1295 TNASTSTNVANITATSHTSTDDTVPNNTVPVTAIPSLANTGVDTTSNSFSIMTTSFSESTNAMNTTVIMATTSpTSTDVA 1374
Cdd:COG3210   810 TAINVTGSGGTITINTATTGLTGTGDTTSGAGGSNTTDTTTGTTSDGASGGGTAGANSGSLAATAASITVGSG-GVATST 888

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1375 STNNDASMTNFLLATMSAGNITSNSISITTTSFGNSVPFVTTPSPSTDATTTSNNTNPGMTTYYQTSPTIPTHTLTSIPS 1454
Cdd:COG3210   889 GTANAGTLTNLGTTTNAASGNGAVLATVTATGTGGGGLTGGNAAAGGTGAGNGTTALSGTQGNAGLSAASASDGAGDTGA 968

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1455 SITSILSMFPTSNTFTTDKITNFTTPTNANTIIFNTLDTKSTMVIDATVTTTSTKDNTMSPDTTVTSIDKFTTHITQFAT 1534
Cdd:COG3210   969 SSAAGSSAVGTSANSAGSTGGVIAATGILVAGNSGTTASTTGGSGAIVAGGNGVTGTTGTASATGTGTAATAGGQNGVGV 1048

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1535 PHSATTTTLALSHTSLAPTNLSNLGTMDITDADNSSSVTGNTTHISVSNLTTASVTITATGLDSQTPHMVINSVATYLPI 1614
Cdd:COG3210  1049 NASGISGGNAAALTASGTAGTTGGTAASNGGGGTAQASGAGTTHTLGGITNGGATGTSGGTTTSTGGVTASKVGGTTTVG 1128

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|...
gi 767949045 1615 TATSATTDTTNITKYALNTTTPDSTVHTSATAPTYIANAINAT 1657
Cdd:COG3210  1129 ATGTSTASTEAAGAGTLTGLVAVSAVAGGASSASAGDTTAVAA 1171
PRK10856 PRK10856
cytoskeleton protein RodZ;
1035-1104 8.24e-03

cytoskeleton protein RodZ;


Pssm-ID: 236776 [Multi-domain]  Cd Length: 331  Bit Score: 40.39  E-value: 8.24e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767949045 1035 NASTNATVPITTTPfPTSTIGVTTNATVPNTTAPFPTNASTASTNATVPITTTCFATSTIGVTTNATVPD 1104
Cdd:PRK10856  184 TTPTNSQTPAVATA-PAPAVDPQQNAVVAPSQANVDTAATPAPAAPATPDGAAPLPTDQAGVSTPAADPN 252
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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