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Conserved domains on  [gi|1110313261|emb|SHI70685|]
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Glycosyl hydrolases family 16 [Pseudozobellia thermophila]

Protein Classification

PKD and GH16_laminarinase_like domain-containing protein( domain architecture ID 10065780)

PKD and GH16_laminarinase_like domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
BglS COG2273
Beta-glucanase, GH16 family [Carbohydrate transport and metabolism];
139-383 5.34e-91

Beta-glucanase, GH16 family [Carbohydrate transport and metabolism];


:

Pssm-ID: 441874 [Multi-domain]  Cd Length: 259  Bit Score: 274.17  E-value: 5.34e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313261 139 TLVFSDEFDYEGrPDPEKWHHQVippNNGSWHNNELQHYTDRsvNSFVDEGTLKIKALKEEYTTDnsTKAYTSARLNS-- 216
Cdd:COG2273    30 TLVFSDEFDGTS-LDTSKWTYDT---GGPGWGNGELQYYTDE--NVSVENGNLVITARKEPYGGG--GRPYTSGRITTkg 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313261 217 KFAFKYGKVEVRAKLPAQQGTWPAIWTLGANSneignyfgdqygNAGWPACGEIDIMEQNGWDKDHTIAHFHWGDlNTGE 296
Cdd:COG2273   102 KFSFTYGRFEARAKLPKGQGLWPAFWMLGGDI------------DGGWPASGEIDIMEFVGKDPNKVHGNVHYGG-YNGG 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313261 297 YQNSGDTIAVANSTDSFHVYSLEWDEASMKVFVDDKLVYELANSDNK---PYNHDHYLLLNLAMGGNLGGEVAEDFTEAT 373
Cdd:COG2273   169 EGIGASYDLPFDASDDFHTYAVEWTPDSIRWYVDGVLVHTVTPADVGgpwPFDQPFYLILNLAVGGNWPGAPDTTGFPAT 248
                         250
                  ....*....|
gi 1110313261 374 FEIDYVRVYQ 383
Cdd:COG2273   249 MEVDYVRVYQ 258
PKD cd00146
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ...
57-128 1.41e-04

polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an IG-like fold; domain probably functions as a ligand binding site in protein-protein or protein-carbohydrate interactions; a single instance of the repeat is presented here. The domain is also found in microbial collagenases and chitinases.


:

Pssm-ID: 238084 [Multi-domain]  Cd Length: 81  Bit Score: 40.17  E-value: 1.41e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1110313261  57 NNPNGDGSGLVEVSASAS---NAVRYAFRFDNGDLEESTDGTASHTFTTEGTHSYTIVAWAYSATGEFINKTIEV 128
Cdd:cd00146     7 APPVAELGASVTFSASDSsggSIVSYKWDFGDGEVSSSGEPTVTHTYTKPGTYTVTLTVTNAVGSSSTKTTTVVV 81
 
Name Accession Description Interval E-value
BglS COG2273
Beta-glucanase, GH16 family [Carbohydrate transport and metabolism];
139-383 5.34e-91

Beta-glucanase, GH16 family [Carbohydrate transport and metabolism];


Pssm-ID: 441874 [Multi-domain]  Cd Length: 259  Bit Score: 274.17  E-value: 5.34e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313261 139 TLVFSDEFDYEGrPDPEKWHHQVippNNGSWHNNELQHYTDRsvNSFVDEGTLKIKALKEEYTTDnsTKAYTSARLNS-- 216
Cdd:COG2273    30 TLVFSDEFDGTS-LDTSKWTYDT---GGPGWGNGELQYYTDE--NVSVENGNLVITARKEPYGGG--GRPYTSGRITTkg 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313261 217 KFAFKYGKVEVRAKLPAQQGTWPAIWTLGANSneignyfgdqygNAGWPACGEIDIMEQNGWDKDHTIAHFHWGDlNTGE 296
Cdd:COG2273   102 KFSFTYGRFEARAKLPKGQGLWPAFWMLGGDI------------DGGWPASGEIDIMEFVGKDPNKVHGNVHYGG-YNGG 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313261 297 YQNSGDTIAVANSTDSFHVYSLEWDEASMKVFVDDKLVYELANSDNK---PYNHDHYLLLNLAMGGNLGGEVAEDFTEAT 373
Cdd:COG2273   169 EGIGASYDLPFDASDDFHTYAVEWTPDSIRWYVDGVLVHTVTPADVGgpwPFDQPFYLILNLAVGGNWPGAPDTTGFPAT 248
                         250
                  ....*....|
gi 1110313261 374 FEIDYVRVYQ 383
Cdd:COG2273   249 MEVDYVRVYQ 258
GH16_laminarinase_like cd08023
Laminarinase, member of the glycosyl hydrolase family 16; Laminarinase, also known as glucan ...
142-382 4.40e-87

Laminarinase, member of the glycosyl hydrolase family 16; Laminarinase, also known as glucan endo-1,3-beta-D-glucosidase, is a glycosyl hydrolase family 16 member that hydrolyzes 1,3-beta-D-glucosidic linkages in 1,3-beta-D-glucans such as laminarins, curdlans, paramylons, and pachymans, with very limited action on mixed-link (1,3-1,4-)-beta-D-glucans.


Pssm-ID: 185693 [Multi-domain]  Cd Length: 235  Bit Score: 263.33  E-value: 4.40e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313261 142 FSDEFDYEGRPDPEKWHHQVippNNGSWHNNELQHYTDRSVNSFVDEGTLKIKALKEEYTtDNSTKAYTSARLNS--KFA 219
Cdd:cd08023     1 WSDEFDGDGLPDPSKWTYET---GGGGNGNNELQYYTYRPENAYVEDGNLVITARKEPDK-GGDGYPYTSGRITTkgKFS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313261 220 FKYGKVEVRAKLPAQQGTWPAIWTLGANSNEignyfgdqygnAGWPACGEIDIMEQNGWDKDHTIAHFHWGDLNTGEYQN 299
Cdd:cd08023    77 FTYGRVEARAKLPKGQGTWPAFWMLGENIKY-----------VGWPASGEIDIMEYVGNEPNTVYGTLHGGATNDGNNGS 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313261 300 SGD-TIAVANSTDSFHVYSLEWDEASMKVFVDDKLVYELANSD-----NKPYNHDHYLLLNLAMGGNLGG-EVAEDFTEA 372
Cdd:cd08023   146 GGSyTLPTDDLSDDFHTYAVEWTPDKITFYVDGKLYFTYTNPNtdnggQWPFDQPFYLILNLAVGGNWPGpPDDDTPFPA 225
                         250
                  ....*....|
gi 1110313261 373 TFEIDYVRVY 382
Cdd:cd08023   226 TMEVDYVRVY 235
Glyco_hydro_16 pfam00722
Glycosyl hydrolases family 16;
209-380 1.96e-22

Glycosyl hydrolases family 16;


Pssm-ID: 395585 [Multi-domain]  Cd Length: 168  Bit Score: 92.66  E-value: 1.96e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313261 209 YTSARLNSKFAFKYGKVEVRAKLPAQQGTWPAIWTLgansneignyfgdqygNAGWPACGEIDImEQNGWDKDHTIAHFH 288
Cdd:pfam00722  20 YTGSGFQSKFYYLYGKVEARIKAARGAGVVTAFYLS----------------SEDWDDHDEIDF-EFLGNDTGQVQTNVY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313261 289 W-GDLNTGEYQNSGDTiavaNSTDSFHVYSLEWDEASMKVFVDDKLVYELANSDNK--PYNHdhyLLLNLAMGGNLGGEV 365
Cdd:pfam00722  83 GnGKGNRGEQRFSLWF----DPTADFHTYSILWNPDKITWYVDGVPVRTLKNNDAGgvPYPQ---TPMRLYVSLWPGGDW 155
                         170
                  ....*....|....*
gi 1110313261 366 AEDFTEATfeIDYVR 380
Cdd:pfam00722 156 ATPGGGVK--IDWAG 168
PKD cd00146
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ...
57-128 1.41e-04

polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an IG-like fold; domain probably functions as a ligand binding site in protein-protein or protein-carbohydrate interactions; a single instance of the repeat is presented here. The domain is also found in microbial collagenases and chitinases.


Pssm-ID: 238084 [Multi-domain]  Cd Length: 81  Bit Score: 40.17  E-value: 1.41e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1110313261  57 NNPNGDGSGLVEVSASAS---NAVRYAFRFDNGDLEESTDGTASHTFTTEGTHSYTIVAWAYSATGEFINKTIEV 128
Cdd:cd00146     7 APPVAELGASVTFSASDSsggSIVSYKWDFGDGEVSSSGEPTVTHTYTKPGTYTVTLTVTNAVGSSSTKTTTVVV 81
PKD smart00089
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
79-131 2.74e-03

Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases.


Pssm-ID: 214510 [Multi-domain]  Cd Length: 79  Bit Score: 36.28  E-value: 2.74e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1110313261   79 YAFRFDNGDLEESTDGTASHTFTTEGTHSYTIVAWAYSATgefINKTIEVNVY 131
Cdd:smart00089  30 VSYTWDFGDGTSSTGPTVTHTYTKPGTYTVTLTVTNAVGS---ASATVTVVVQ 79
 
Name Accession Description Interval E-value
BglS COG2273
Beta-glucanase, GH16 family [Carbohydrate transport and metabolism];
139-383 5.34e-91

Beta-glucanase, GH16 family [Carbohydrate transport and metabolism];


Pssm-ID: 441874 [Multi-domain]  Cd Length: 259  Bit Score: 274.17  E-value: 5.34e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313261 139 TLVFSDEFDYEGrPDPEKWHHQVippNNGSWHNNELQHYTDRsvNSFVDEGTLKIKALKEEYTTDnsTKAYTSARLNS-- 216
Cdd:COG2273    30 TLVFSDEFDGTS-LDTSKWTYDT---GGPGWGNGELQYYTDE--NVSVENGNLVITARKEPYGGG--GRPYTSGRITTkg 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313261 217 KFAFKYGKVEVRAKLPAQQGTWPAIWTLGANSneignyfgdqygNAGWPACGEIDIMEQNGWDKDHTIAHFHWGDlNTGE 296
Cdd:COG2273   102 KFSFTYGRFEARAKLPKGQGLWPAFWMLGGDI------------DGGWPASGEIDIMEFVGKDPNKVHGNVHYGG-YNGG 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313261 297 YQNSGDTIAVANSTDSFHVYSLEWDEASMKVFVDDKLVYELANSDNK---PYNHDHYLLLNLAMGGNLGGEVAEDFTEAT 373
Cdd:COG2273   169 EGIGASYDLPFDASDDFHTYAVEWTPDSIRWYVDGVLVHTVTPADVGgpwPFDQPFYLILNLAVGGNWPGAPDTTGFPAT 248
                         250
                  ....*....|
gi 1110313261 374 FEIDYVRVYQ 383
Cdd:COG2273   249 MEVDYVRVYQ 258
GH16_laminarinase_like cd08023
Laminarinase, member of the glycosyl hydrolase family 16; Laminarinase, also known as glucan ...
142-382 4.40e-87

Laminarinase, member of the glycosyl hydrolase family 16; Laminarinase, also known as glucan endo-1,3-beta-D-glucosidase, is a glycosyl hydrolase family 16 member that hydrolyzes 1,3-beta-D-glucosidic linkages in 1,3-beta-D-glucans such as laminarins, curdlans, paramylons, and pachymans, with very limited action on mixed-link (1,3-1,4-)-beta-D-glucans.


Pssm-ID: 185693 [Multi-domain]  Cd Length: 235  Bit Score: 263.33  E-value: 4.40e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313261 142 FSDEFDYEGRPDPEKWHHQVippNNGSWHNNELQHYTDRSVNSFVDEGTLKIKALKEEYTtDNSTKAYTSARLNS--KFA 219
Cdd:cd08023     1 WSDEFDGDGLPDPSKWTYET---GGGGNGNNELQYYTYRPENAYVEDGNLVITARKEPDK-GGDGYPYTSGRITTkgKFS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313261 220 FKYGKVEVRAKLPAQQGTWPAIWTLGANSNEignyfgdqygnAGWPACGEIDIMEQNGWDKDHTIAHFHWGDLNTGEYQN 299
Cdd:cd08023    77 FTYGRVEARAKLPKGQGTWPAFWMLGENIKY-----------VGWPASGEIDIMEYVGNEPNTVYGTLHGGATNDGNNGS 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313261 300 SGD-TIAVANSTDSFHVYSLEWDEASMKVFVDDKLVYELANSD-----NKPYNHDHYLLLNLAMGGNLGG-EVAEDFTEA 372
Cdd:cd08023   146 GGSyTLPTDDLSDDFHTYAVEWTPDKITFYVDGKLYFTYTNPNtdnggQWPFDQPFYLILNLAVGGNWPGpPDDDTPFPA 225
                         250
                  ....*....|
gi 1110313261 373 TFEIDYVRVY 382
Cdd:cd08023   226 TMEVDYVRVY 235
GH16_Strep_laminarinase_like cd02182
Streptomyces laminarinase-like, member of glycosyl hydrolase family 16; Proteins similar to ...
139-383 1.45e-42

Streptomyces laminarinase-like, member of glycosyl hydrolase family 16; Proteins similar to Streptomyces sioyaensis beta-1,3-glucanase (laminarinase) present in Actinomycetales as well as Peziomycotina. Laminarinases belong to glycosyl hydrolase family 16 and hydrolyze the glycosidic bond of the 1,3-beta-linked glucan, a major component of fungal and plant cell walls and the structural and storage polysaccharides (laminarin) of marine macro-algae. Members of the GH16 family have a conserved jelly roll fold with an active site channel.


Pssm-ID: 185691  Cd Length: 259  Bit Score: 149.39  E-value: 1.45e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313261 139 TLVFSDEFDYE--GRPDPEKWhhQVIPPNNGSWHNNELQHYTDRSVNSFVDE-GTLKIKALKeeyttdNSTKAYTSARLN 215
Cdd:cd02182     3 TLVWSDDFDGSagSLPSSSKW--IIDTGTSANWGTGEIQTYTNSTANVQLSGnGTLQITPLR------DGSGKWTSGRIE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313261 216 SK---FAFKYGK---VEVRAKLP-----AQQGTWPAIWTLGANSNEIGNyfgdqygnaGWPACGEIDIMEQ-NGWDKDHT 283
Cdd:cd02182    75 TTrtdFAAPPGGklrVEASIRLGdvpgsNQQGIWPAFWMLGDSYRGNGT---------NWPACGELDIMENvNGLSTGYG 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313261 284 IAHF-HWGDLNTGEYqnSGDTIAVANSTDSFHVYSLEWD-----EASMKVFVDDKLVYELANSD-------NKPYNHDHY 350
Cdd:cd02182   146 TLHCgVAPGGPCNEP--TGIGAGTRLCDTGFHTYAVEIDrtngdAESIRWYLDGVVYHTVTGARvgdettwQALAHHPLF 223
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1110313261 351 LLLNLAMGGNLGGEVAE---DFTEATFEIDYVRVYQ 383
Cdd:cd02182   224 IILNVAVGGNWPGAPNGntaTGSGSAMEVDYVAVYS 259
GH16_CCF cd08024
Coelomic cytolytic factor, member of glycosyl hydrolase family 16; Subgroup of glucanases of ...
140-383 6.47e-41

Coelomic cytolytic factor, member of glycosyl hydrolase family 16; Subgroup of glucanases of unknown function that are related to beta-GRP (beta-1,3-glucan recognition protein), but contain active site residues. Beta-GRPs are one group of pattern recognition receptors (PRRs), also referred to as biosensor proteins, that complexes with pathogen-associated beta-1,3-glucans and then transduces signals necessary for activation of an appropriate innate immune response. Beta-GRPs are present in insects and lack all catalytic residues. This subgroup contains related proteins that still contain the active site and are widely distributed in eukaryotes. Their structures adopt a jelly roll fold with a deep active site channel harboring the catalytic residues, like those of other glycosyl hydrolase family 16 members.


Pssm-ID: 185694  Cd Length: 330  Bit Score: 147.01  E-value: 6.47e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313261 140 LVFSDEFDYEgrpDPEKWHHQVIPPNNGswhNNELQHYTDRSVNSFVDEGTLKIKA--LKEEY----------TTDNSTK 207
Cdd:cd08024     1 LVFEDDFDSF---DLSKWQHEVTAGGGG---NGEFQWYTNDRSNSYVRDGKLYIKPtlTADTFgedfltlgngNLDGLAP 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313261 208 AYT-----------------------SARLNS--KFAFKYGKVEVRAKLPAQQGTWPAIWTLGANSneignyfgdQYGna 262
Cdd:cd08024    75 WGTctnnanngcyrtgnaggiinpvmSARLRTknSFSFKYGRVEVRAKLPTGDWLWPAIWMLPRDN---------VYG-- 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313261 263 GWPACGEIDIMEQ--NGWDKDHTIAHF--------HWG--------DLNTGEYQNSGDTIAvanstDSFHVYSLEWDEAS 324
Cdd:cd08024   144 GWPRSGEIDIMESrgNRPLYDGGEAIGinsvgstlHWGpdpgqnryTKTTGKRSDSGGDFA-----DDFHTYGLDWTPDH 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313261 325 MKVFVDDKLVYEL-----------------------ANSDNKPYNHDHYLLLNLAMGG----------------NLGGEV 365
Cdd:cd08024   219 IRFYVDDRLILTLdvpgqgfwefggfsgtpidnpwaGGGKMAPFDQEFYLILNVAVGGtngffpdgwpggkpwsNGSPTA 298
                         330       340       350
                  ....*....|....*....|....*....|..
gi 1110313261 366 AEDFTEA--------------TFEIDYVRVYQ 383
Cdd:cd08024   299 MRDFWEArnqwlptwhggddaAMQVDYVKMWQ 330
Glyco_hydrolase_16 cd00413
glycosyl hydrolase family 16; The O-Glycosyl hydrolases are a widespread group of enzymes that ...
144-382 9.24e-31

glycosyl hydrolase family 16; The O-Glycosyl hydrolases are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A glycosyl hydrolase classification system based on sequence similarity has led to the definition of more than 95 different families inlcuding glycosyl hydrolase family 16. Family 16 includes lichenase, xyloglucan endotransglycosylase (XET), beta-agarase, kappa-carrageenase, endo-beta-1,3-glucanase, endo-beta-1,3-1,4-glucanase, and endo-beta-galactosidase, all of which have a conserved jelly roll fold with a deep active site channel harboring the catalytic residues.


Pssm-ID: 185683 [Multi-domain]  Cd Length: 210  Bit Score: 116.77  E-value: 9.24e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313261 144 DEFDYEGrPDPEKWHHQvippnngSWHNNELQHYTDRSVNSFVDEGTLKIKAlkeeyTTDNSTKAYTSARLNS-KFAFKY 222
Cdd:cd00413     1 DDFDGLA-LDTSKWTIQ-------DGPSWGGNMTNSPNNVYVENDGGLTLRT-----DRDQTDGPYSSAEIDSqKNNYTY 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313261 223 GKVEVRAKLPAQQGTWPAIWTlgansneignyfgdQYGNAGWPACGEIDImEQNGWD-KDHTIAHFHWGDLNTGEYQNSG 301
Cdd:cd00413    68 GYYEARAKLAGGPGAVSAFWT--------------YSDDDDPPDGGEIDI-EFLGRDpTTVQTNVHWPGYGAGATTGEEK 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313261 302 DTIAVANSTDSFHVYSLEWDEASMKVFVDDKLVyelANSDNKPYNHDHYLLLNLAMGGNLGGEVAEDFTEATFEIDYVRV 381
Cdd:cd00413   133 SVHLPFDPADDFHTYRVDWTPGEITFYVDGVLV---ATITNQVPDDPMNIILNLWSDGGWWWGGPPPGAPAYMEIDWVRV 209

                  .
gi 1110313261 382 Y 382
Cdd:cd00413   210 Y 210
GH16_fungal_KRE6_glucanase cd02180
Saccharomyces cerevisiae KRE6 and related glucanses, member of glycosyl hydrolase family 16; ...
140-383 1.45e-23

Saccharomyces cerevisiae KRE6 and related glucanses, member of glycosyl hydrolase family 16; KRE6 is a Saccharomyces cerevisiae glucanase that participates in the synthesis of beta-1,6-glucan, a major structural component of the cell wall. It is a golgi membrane protein required for normal beta-1,6-glucan levels in the cell wall. KRE6 is closely realted to laminarinase, a glycosyl hydrolase family 16 member that hydrolyzes 1,3-beta-D-glucosidic linkages in 1,3-beta-D-glucans such as laminarins, curdlans, paramylons, and pachymans, with very limited action on mixed-link (1,3-1,4-)-beta-D-glucans.


Pssm-ID: 185689 [Multi-domain]  Cd Length: 295  Bit Score: 99.31  E-value: 1.45e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313261 140 LVFSDEFDYEGRP-----DP-----EKWHhqvippnngsWHNNELQHYTDRSVNSFVdeGTLKIKALKEeyttDNSTKAY 209
Cdd:cd02180     1 LVFSDEFNVDGRTfypgdDPfweavDLHY----------WATNDLEWYDPDAVTTIN--GSLRITMDQF----RNHGLNF 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313261 210 TSARLNS--KFAFKYGKVEVRAKLPAQ---QGTWPAIWTLGaNSNEIGnYFGDQYGNagWP------ACGEIDIMEQNG- 277
Cdd:cd02180    65 RSGMLQSwnKLCFTGGYIEASASLPGKpdvSGLWPAVWTMG-NLGRPG-YLATTEGV--WPysydgrGAPEIDIIEAQVg 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313261 278 --------------------WDKDHTIAHFHWGDLNT--------GEYQNSGDTIAVANST------DSFHVYSLEW--- 320
Cdd:cd02180   141 nglgigqvsqslqvapfdawYRPDYSSDFVTIYNDTTtimntytgGVFQQAISCVTRLNDSwypgngNEFQTYGFEYrpd 220
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1110313261 321 --DEASMKVFVDDKLVYEL----ANSDNK---------PYnhdhYLLLNLAMGGNLGG-EVAEDFTEATFEIDYVRVYQ 383
Cdd:cd02180   221 deDDGYITWFVDDEPTWTIyakaLGPNGNigwriipeePM----YIILNLGISSNFQDiDWDELQFPATMRIDYVRVYQ 295
Glyco_hydro_16 pfam00722
Glycosyl hydrolases family 16;
209-380 1.96e-22

Glycosyl hydrolases family 16;


Pssm-ID: 395585 [Multi-domain]  Cd Length: 168  Bit Score: 92.66  E-value: 1.96e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313261 209 YTSARLNSKFAFKYGKVEVRAKLPAQQGTWPAIWTLgansneignyfgdqygNAGWPACGEIDImEQNGWDKDHTIAHFH 288
Cdd:pfam00722  20 YTGSGFQSKFYYLYGKVEARIKAARGAGVVTAFYLS----------------SEDWDDHDEIDF-EFLGNDTGQVQTNVY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313261 289 W-GDLNTGEYQNSGDTiavaNSTDSFHVYSLEWDEASMKVFVDDKLVYELANSDNK--PYNHdhyLLLNLAMGGNLGGEV 365
Cdd:pfam00722  83 GnGKGNRGEQRFSLWF----DPTADFHTYSILWNPDKITWYVDGVPVRTLKNNDAGgvPYPQ---TPMRLYVSLWPGGDW 155
                         170
                  ....*....|....*
gi 1110313261 366 AEDFTEATfeIDYVR 380
Cdd:pfam00722 156 ATPGGGVK--IDWAG 168
GH16_beta_GRP cd02179
beta-1,3-glucan recognition protein, member of glycosyl hydrolase family 16; Beta-GRP (beta-1, ...
140-382 1.48e-21

beta-1,3-glucan recognition protein, member of glycosyl hydrolase family 16; Beta-GRP (beta-1,3-glucan recognition protein) is one of several pattern recognition receptors (PRRs), also referred to as biosensor proteins, that complexes with pathogen-associated beta-1,3-glucans and then transduces signals necessary for activation of an appropriate innate immune response. They are present in insects and lack all catalytic residues. This subgroup also contains related proteins of unknown function that still contain the active site. Their structures adopt a jelly roll fold with a deep active site channel harboring the catalytic residues, like those of other glycosyl hydrolase family 16 members.


Pssm-ID: 185688 [Multi-domain]  Cd Length: 321  Bit Score: 93.99  E-value: 1.48e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313261 140 LVFSDEFDYEGRpDPEKWHHQVIPPNNGSwhnNELQHYTDRSVNSFVDEGTLKIKA--LKEEYTTDNSTKAY-------- 209
Cdd:cd02179     1 LIFEENFNGALL-DLNKWTIEVRFPGEPD---YEFVVYDDAPENLFVKDGNLVIEPtlLEEKFGEGFVREGLdllerctg 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313261 210 --------------------TSARLNSK--FAFKYGKVEVRAKLPaqQGTW--PAIWTLGANsneignyfgDQYGNAGWp 265
Cdd:cd02179    77 qlgttecrrdargssilppvVSARINTKnsFAFKYGRVEIRAKLP--KGDWiyPELLLEPVN---------NYYGSSDY- 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313261 266 ACGEIDIMEQNG-----WDKDHTIAHFHWGD--LNTGEYQNS---GDTIAVANSTDSFHVYSLEWDEASMKVFVDDKlVY 335
Cdd:cd02179   145 ASGQIRIAFARGnavlrADGTDIGGKKLYGGpvLTDAEPHRSanlKTKINNELWSDDFHVYTLEWKPDGITLMVDGE-EY 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313261 336 ---------------------ELANSDNKPYNHDHYLLLNLAMGG-----------------NLGGEVAEDFTEATFE-- 375
Cdd:cd02179   224 geiepgeggyseaannpaasrWLGGTVMAPFDKEFYLSLGVGVGGhndfpdssirgyvkpwkNTGPKAMLKFWQARDKwf 303
                         330
                  ....*....|....*..
gi 1110313261 376 ----------IDYVRVY 382
Cdd:cd02179   304 ptwsddsalkVDYVKVY 320
GH16_beta_agarase cd02178
Beta-agarase, member of glycosyl hydrolase family 16; Beta-agarase is a glycosyl hydrolase ...
142-383 2.32e-18

Beta-agarase, member of glycosyl hydrolase family 16; Beta-agarase is a glycosyl hydrolase family 16 (GH16) member that hydrolyzes the internal beta-1,4-linkage of agarose, a hydrophilic polysaccharide found in the cell wall of Rhodophyceaea, marine red algae. Agarose is a linear chain of galactose units linked by alternating L-alpha-1,3- and D-beta-1,4-linkages that are additionally modified by a 3,6-anhydro-bridge. Agarose forms thermo-reversible gels that are widely used in the food industry or as a laboratory medium. While beta-agarases are also found in two other families derived from the sequence-based classification of glycosyl hydrolases (GH50, and GH86) the GH16 members are most abundant. This domain adopts a curved beta-sandwich conformation, with a tunnel-shaped active site cavity, referred to as a jellyroll fold.


Pssm-ID: 185687  Cd Length: 258  Bit Score: 83.94  E-value: 2.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313261 142 FSDEFDYeGRPDPEKWHhqviPPNNGSWHNNELQHYTDRsvNSFVDEGTLKIKALKEE-YTTDNSTKAYTSArLNSKFAF 220
Cdd:cd02178    25 VSDEFNG-TSLDTSKWN----PNNPNGWTGRGPTEFSAD--NVSVEDGNLVLSATRHPgTELGNGYKVTTGS-ITSKEKV 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313261 221 KYGKVEVRAKlpAQQGTWP-AIWTLGANSNEIgnyfgdqygnagwpacGEIDIMEQNG------WDKDHTIAHFHWGDLN 293
Cdd:cd02178    97 KYGYFEARAK--ASNLPMSsAFWLLSDTKDST----------------TEIDILEHYGgdreewFATRMNSNTHVFIRDP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313261 294 TGEYQNSGDTIAVANST---DSFHVYSLEW-DEASMKVFVDDKLVYELANS---DNKPYNHDHYLLLN-LAMG--GNLGG 363
Cdd:cd02178   159 EQDYQPKDDGSWYYNPTelaDDFHVYGVYWkDPDTIRFYIDGVLVRTVENSeitDGTGFDQPMYIIIDtETYDwrGEPTD 238
                         250       260
                  ....*....|....*....|
gi 1110313261 364 EVAEDFTEATFEIDYVRVYQ 383
Cdd:cd02178   239 EELADDSKNTFYVDYVRVYK 258
GH16_fungal_Lam16A_glucanase cd02181
fungal 1,3(4)-beta-D-glucanases, similar to Phanerochaete chrysosporium laminarinase 16A; ...
142-383 6.65e-09

fungal 1,3(4)-beta-D-glucanases, similar to Phanerochaete chrysosporium laminarinase 16A; Group of fungal 1,3(4)-beta-D-glucanases, similar to Phanerochaete chrysosporium laminarinase 16A. Lam16A belongs to the 'nonspecific' 1,3(4)-beta-glucanase subfamily, although beta-1,6 branching and beta-1,4 bonds specifically define where Lam16A hydrolyzes its substrates, like curdlan (beta-1,3-glucan), lichenin (beta-1,3-1,4-mixed linkage glucan), and laminarin (beta-1,6-branched-1,3-glucan).


Pssm-ID: 185690 [Multi-domain]  Cd Length: 293  Bit Score: 56.47  E-value: 6.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313261 142 FSDEFDYEGRPDPekwhhqvippNNGSwhnnelQHYTDRSVNS-----FVDEGTLKIKAlkeeyttDNSTKAYT-----S 211
Cdd:cd02181    13 FFDGFDFFTGDDP----------THGF------VNYVDQSTATslglaYVNSGNVYLGV-------DSTTTLPSgagrnS 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313261 212 ARLNSKFAFKYGKVEVR-AKLPAQQGTWPAIWTLGANsneignyfgdqygnagWPACGEIDIMEqnGWDKD-------HT 283
Cdd:cd02181    70 VRIESKKTYNTGLFIADiAHMPGGCGTWPAFWTVGPN----------------WPNGGEIDIIE--GVNLQtsnqmtlHT 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313261 284 ------------IAHFHWGDLNTGEYQNSGDTIAvANSTDSFH---------VYSLEWDEASMKVF--------VDDKL- 333
Cdd:cd02181   132 gpgctisnsgsfTGTVTTTNCDVNQNGNAGCGVT-STSTNSYGagfnaagggVYAMEWTSDGIKVWffprgsipADITSg 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313261 334 ----------VYELANSDNKPYNH--DHYLLLNLAMGGNLGGEVA---------------------EDFTEATFEIDYVR 380
Cdd:cd02181   211 spdpstwgtpAASFPGSSCDIDSFfkDQRIVFDTTFCGDWAGNVWisssgcaaktstcedyvannpSAFSEAYWEINSIK 290

                  ...
gi 1110313261 381 VYQ 383
Cdd:cd02181   291 VYQ 293
SKN1_KRE6_Sbg1 pfam03935
Beta-glucan synthesis-associated protein SKN1/KRE6/Sbg1; This family consists of the ...
99-383 3.90e-07

Beta-glucan synthesis-associated protein SKN1/KRE6/Sbg1; This family consists of the beta-glucan synthesis-associated proteins KRE6, SKN1 and Sbg1. Beta1,6-Glucan is a key component of the yeast cell wall, interconnecting cell wall proteins, beta1,3-glucan, and chitin. SKN1 and KRE6 show similarities to glycoside hydrolase family 16 glycoside hydrolases, suggesting that they are glycosyl hydrolases or transglycosylases. They are related with the synthesis and anchorage of cell wall proteins of glucan polymers of the yeast cell wall, although they play redundant roles. SKN1, KRE6 and Sbg1 share the SKN1 domain which is conserved in SKN1 and KRE6 proteins of many fungal species. Sbg1 is an integral membrane protein essential for contractile-ring constriction and septum formation during cytokinesis, which interacts with the conserved beta-glucan synthase Bgs1 and regulates its protein levels ans localization.


Pssm-ID: 397841 [Multi-domain]  Cd Length: 500  Bit Score: 51.90  E-value: 3.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313261  99 TFTTEGTH-SYTIVAWAYSATGEF-INKTIEVNVYRSDEPFD------------TLVFSDEFDYEGRP----DPEKWHhq 160
Cdd:pfam03935  64 TYTGVTEHgSTKGNLGEILTTYQYpLLSAIRTGLIDPDTPQSaytrksqdgktwKLVFSDEFNKDGRTfydgDDPFWT-- 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313261 161 viPPNNGSWHNNELQHYTDRSVNSfvDEGTLKIKaLKEEYTTD-NstkaYTSARLNS--KFAFKYGKVEVRAKLPAQ--- 234
Cdd:pfam03935 142 --AVDLHYWATQDLEWYDPDAVTT--ANGTLVIR-MDAFKNHDlN----YRSGMLQSwnKLCFTGGYIEVSASLPGYgdv 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313261 235 QGTWPAIWTLG--------ANSNEIGNYFGDQ--YG---NAGW------------PACG----------------EIDIM 273
Cdd:pfam03935 213 SGLWPGLWTMGnlgrpgylATTEGVWPYSYDScdAGitpNQSSpdgisylpgqrlPSCTcsgedhpnpgvgrgapEIDIL 292
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313261 274 E-------------QNG----------WDKDHTIAHF----HWGDLNTGEYQNSGDTIAVANST-----DSFHVYSLEW- 320
Cdd:pfam03935 293 EaevdtdlgigvasQSLqiapfdiwymPDYDFVEIYNtsvtTMNSYTGGPFQQAVSGLTTLNNTwyeggGQFQTYGFEYl 372
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313261 321 ----DEASMKVFVDDKLVYEL--------ANSDNKPYNHD-HYLLLNLAMGGNLGgevAEDFTE----ATFEIDYVRVYQ 383
Cdd:pfam03935 373 pnddDDGYITWFVGDEPTWTMyaralgpnGNIGQRLISEEpMSIIMNLGISNNWA---YIDWRSlqfpATMRIDYVRIYQ 449
GH16_lichenase cd02175
lichenase, member of glycosyl hydrolase family 16; Lichenase, also known as 1,3-1, ...
142-343 3.49e-05

lichenase, member of glycosyl hydrolase family 16; Lichenase, also known as 1,3-1,4-beta-glucanase, is a member of glycosyl hydrolase family 16, that specifically cleaves 1,4-beta-D-glucosidic bonds in mixed-linked beta glucans that also contain 1,3-beta-D-glucosidic linkages. Natural substrates of beta-glucanase are beta-glucans from grain endosperm cell walls or lichenan from the Islandic moss, Cetraria islandica. This protein is found not only in bacteria but also in anaerobic fungi. This domain includes two seven-stranded antiparallel beta-sheets that are adjacent to one another forming a compact, jellyroll beta-sandwich structure.


Pssm-ID: 185684 [Multi-domain]  Cd Length: 212  Bit Score: 44.57  E-value: 3.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313261 142 FSDEFDYegrPDPEKWHhqvipPNNGsWHNNELQHYTDRSVNSFVDEGTLKIKALKEEYttdnSTKAYTSARLNSKFAFK 221
Cdd:cd02175     1 FFEDFNS---LDTGRWY-----KSDG-WSNGGPFNCTWSADNVEFSDGGLALTLTNDTY----GEKPYACGEYRTRGFYG 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313261 222 YGKVEVRAKLPAQQGTWPAIWTLgansneIGNYFGDQYGnagwpacgEIDImEQNGwdKDHTIAHFHWgdlntgeYQN-- 299
Cdd:cd02175    68 YGRYEVRMKPAKGSGVVSSFFTY------TGPYDGDPHD--------EIDI-EFLG--KDTTKVQFNY-------YTNgv 123
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1110313261 300 SGDTIAVA---NSTDSFHVYSLEWDEASMKVFVDDKLVYELANSDNK 343
Cdd:cd02175   124 GGHEKLIDlgfDASEGFHTYAFEWEPDSIRWYVDGELVHEATATDPN 170
PKD cd00146
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ...
57-128 1.41e-04

polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an IG-like fold; domain probably functions as a ligand binding site in protein-protein or protein-carbohydrate interactions; a single instance of the repeat is presented here. The domain is also found in microbial collagenases and chitinases.


Pssm-ID: 238084 [Multi-domain]  Cd Length: 81  Bit Score: 40.17  E-value: 1.41e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1110313261  57 NNPNGDGSGLVEVSASAS---NAVRYAFRFDNGDLEESTDGTASHTFTTEGTHSYTIVAWAYSATGEFINKTIEV 128
Cdd:cd00146     7 APPVAELGASVTFSASDSsggSIVSYKWDFGDGEVSSSGEPTVTHTYTKPGTYTVTLTVTNAVGSSSTKTTTVVV 81
GH16_fungal_CRH1_transglycosylase cd02183
glycosylphosphatidylinositol-glucanosyltransferase; Group of fungal GH16 members related to ...
206-346 5.13e-04

glycosylphosphatidylinositol-glucanosyltransferase; Group of fungal GH16 members related to Saccharomyces cerevisiae Crh1p. Chr1p and Crh2p are transglycosylases that are required for the linkage of chitin to beta(1-3)glucose branches of beta(1-6)glucan, an important step in the assembly of new cell wall. Both have been shown to be glycosylphosphatidylinositol (GPI)-anchored. A third homologous protein, Crr1p, functions in the formation of the spore wall. They belongs to the family 16 of glycosyl hydrolases that includes lichenase, xyloglucan endotransglycosylase (XET), beta-agarase, kappa-carrageenase, endo-beta-1,3-glucanase, endo-beta-1,3-1,4-glucanase, and endo-beta-galactosidase, all of which have a conserved jelly roll fold with a deep active site channel harboring the catalytic residues.


Pssm-ID: 185692 [Multi-domain]  Cd Length: 203  Bit Score: 41.00  E-value: 5.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313261 206 TKAYTSARLNSKFAFKYGKVEVRAKLPAQQGTWPAIWTLGANsneignyfGDqygnagwpacgEIDImEQNGWDKDHTIA 285
Cdd:cd02183    31 PKRGDGPTISSTFYIFYGKVEVTMKAAPGQGIVSSFVLQSDD--------LD-----------EIDW-EWVGGDLTQVQT 90
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1110313261 286 HFHW-GDLNTgeYQNSGDTIAVANSTDSFHVYSLEWDEASMKVFVDDKLVYELANSD-NKPYN 346
Cdd:cd02183    91 NYFGkGNTTT--YDRGGYHPVPNPQTEEFHTYTIDWTKDRITWYIDGKVVRTLTKADtTGGYG 151
GH16_kappa_carrageenase cd02177
Kappa-carrageenase, member of glycosyl hydrolase family 16; Kappa-carrageenase is a glycosyl ...
143-383 2.34e-03

Kappa-carrageenase, member of glycosyl hydrolase family 16; Kappa-carrageenase is a glycosyl hydrolase family 16 (GH16) member that hydrolyzes the internal beta-1,4-linkage of kappa-carrageenans, a hydrophilic polysaccharide found in the cell wall of Rhodophyceaea, marine red algae. Carrageenans are linear chains of galactose units linked by alternating D-alpha-1,3- and D-beta-1,4-linkages that are additionally modified by a 3,6-anhydro-bridge. Depending on the position and number of sulfate ester modifications they are subdivided into kappa-, iota-, and lambda-carrageenases, kappa being modified once. Carrageenans form thermo-reversible gels widely used for industrial applications. Kappa-carrageenases exist in bacteria belonging to at least three phylogenetically distant branches, including pseudoalteromonas, planctomycetes, and baceroidetes. This domain adopts a curved beta-sandwich conformation, with a tunnel-shaped active site cavity, referred to as a jellyroll fold.


Pssm-ID: 185686  Cd Length: 269  Bit Score: 39.19  E-value: 2.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313261 143 SDEFDyEGRPDPEKWHHQviPPNNGSWH-NNElqhytdrsVNSFVDEGTLKIKALKEEYTTDNSTKA--------YTSAR 213
Cdd:cd02177    15 SDEFN-KNDPDWAKWNKT--GENTGAWKwNNE--------KNVVISNGILELTMRRNANNTTFWDQQqvpdgptyFTSGI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313261 214 LNSKFAFKYGKVEVRAK-LPAQQGTWPAIWTLGANSNEIGNYFGDQYgnagwpacGEIDIME--QNGW-------DKDHT 283
Cdd:cd02177    84 FKSYAKGTYGYYEARIKgADIFPGVCPSFWLYSDIDYSVANEGEVVY--------SEIDVVElqQFDWyhqddirDMDHN 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1110313261 284 IAHF-------HWGDLNTGEYQNSGDTIAVANSTDSFHVYSLEWDEASMKVFVDDKlvyELANSDNKPYNHDHYLLLNLA 356
Cdd:cd02177   156 LHAIvkengqgVWKRPKMYPPTEQLNYHRPFDPSKDFHTYGCNVNQDEIIWYVDGV---EVGRKPNKYWHRPMNVTLSLG 232
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1110313261 357 M-------GGNL----GGEVAEDFTeATFEIDYVRVYQ 383
Cdd:cd02177   233 LrkpfvkfFDNKnnakAREKASDFP-TSMYVDYVRVWE 269
PKD smart00089
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
79-131 2.74e-03

Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases.


Pssm-ID: 214510 [Multi-domain]  Cd Length: 79  Bit Score: 36.28  E-value: 2.74e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1110313261   79 YAFRFDNGDLEESTDGTASHTFTTEGTHSYTIVAWAYSATgefINKTIEVNVY 131
Cdd:smart00089  30 VSYTWDFGDGTSSTGPTVTHTYTKPGTYTVTLTVTNAVGS---ASATVTVVVQ 79
 
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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