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Conserved domains on  [gi|21358195|ref|NP_650314|]
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chitinase 5 [Drosophila melanogaster]

Protein Classification

glycoside hydrolase family 18 protein( domain architecture ID 10120821)

glycoside hydrolase family 18 protein such as Mus musculus chitotriosidase-1 (also called chitinase-1) that degrades chitin, chitotriose and chitobiose; also contains C-terminal peritrophin-A or chitin-binding domain

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GH18_chitolectin_chitotriosidase cd02872
This conserved domain family includes a large number of catalytically inactive chitinase-like ...
 29-397 1.77e-170

This conserved domain family includes a large number of catalytically inactive chitinase-like lectins (chitolectins) including YKL-39, YKL-40 (HCGP39), YM1, oviductin, and AMCase (acidic mammalian chitinase), as well as catalytically active chitotriosidases. The conserved domain is an eight-stranded alpha/beta barrel fold belonging to the family 18 glycosyl hydrolases. The fold has a pronounced active-site cleft at the C-terminal end of the beta-barrel. The chitolectins lack a key active site glutamate (the proton donor required for hydrolytic activity) but retain highly conserved residues involved in oligosaccharide binding. Chitotriosidase is a chitinolytic enzyme expressed in maturing macrophages, which suggests that it plays a part in antimicrobial defense. Chitotriosidase hydrolyzes chitotriose, as well as colloidal chitin to yield chitobiose and is therefore considered an exochitinase. Chitotriosidase occurs in two major forms, the large form being converted to the small form by either RNA or post-translational processing. Although the small form, containing the chitinase domain alone, is sufficient for the chitinolytic activity, the additional C-terminal chitin-binding domain of the large form plays a role in processing colloidal chitin. The chitotriosidase gene is nonessential in humans, as about 35% of the population are heterozygous and 6% homozygous for an inactivated form of the gene. HCGP39 is a 39-kDa human cartilage glycoprotein thought to play a role in connective tissue remodeling and defense against pathogens.


:

Pssm-ID: 119351 [Multi-domain]  Cd Length: 362  Bit Score: 488.22  E-value: 1.77e-170
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195  29 IVCYFSNWAVYRTGIGRYGLEDVPADLCTHIIYSFIGVNDKSwDVLVIDPELDVDQGGFSKFTQLKKSNPNVKLEIAVGG 108
Cdd:cd02872   1 VVCYFTNWAQYRPGNGKFVPENIDPFLCTHIIYAFAGLNPDG-NIIILDEWNDIDLGLYERFNALKEKNPNLKTLLAIGG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195 109 WAEGGSKYSQMVAVRDRRQSFIRSVVRFMKQYNFDGFDLDWEYPGAtdRGGNYGDKDKFLYFVEELRRAFDREGRGWEIT 188
Cdd:cd02872  80 WNFGSAKFSAMAASPENRKTFIKSAIAFLRKYGFDGLDLDWEYPGQ--RGGPPEDKENFVTLLKELREAFEPEAPRLLLT 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195 189 MAVPVAKFRLNEGYHVPELCEALDAIHAMTYDLRGNWAGFADVHSPLYKRKHDQYAYEKLNVNDGLALWEEMGCPANKLV 268
Cdd:cd02872 158 AAVSAGKETIDAAYDIPEISKYLDFINVMTYDFHGSWEGVTGHNSPLYAGSADTGDQKYLNVDYAIKYWLSKGAPPEKLV 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195 269 VGVPFYGRTFTLSNSNKNynmGTYINkEAGGGAPGPYTNASGFLAYYEICTEVmdkSKGWTVEWDDAGMVPYTYKDTQWV 348
Cdd:cd02872 238 LGIPTYGRSFTLASPSNT---GVGAP-ASGPGTAGPYTREAGFLAYYEICEFL---KSGWTVVWDDEQKVPYAYKGNQWV 310

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 21358195 349 GYENEASIQIKMDFIKQRGYAGAMTWAIDMDDFHGMCG-RKNGLTQILYD 397
Cdd:cd02872 311 GYDDEESIALKVQYLKSKGLGGAMVWSIDLDDFRGTCGqGKYPLLNAINR 360
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
 531-578 4.12e-12

Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.


:

Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 61.28  E-value: 4.12e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 21358195   531 CTNRD--FVPHP-NCRKYFRCVHGKPVEFECKEGTAFHTVLNVCDWIENSD 578
Cdd:pfam01607   1 CAGKEdgYYADPgDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDYPDNVV 51
PTZ00449 super family cl33186
104 kDa microneme/rhoptry antigen; Provisional
 400-546 9.37e-03

104 kDa microneme/rhoptry antigen; Provisional


The actual alignment was detected with superfamily member PTZ00449:

Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 38.90  E-value: 9.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195  400 KNYRVPE-PTRQTTP-RPEWAKPPATPPNPDEGAV----VAPTTSTTKRPKPKPKPTSSPLSPTSAPGPV-PT------- 465
Cdd:PTZ00449 598 KRPRSAQrPTRPKSPkLPELLDIPKSPKRPESPKSpkrpPPPQRPSSPERPEGPKIIKSPKPPKSPKPPFdPKfkekfyd 677

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195  466 --VGSSTPKPTTKKPKKPKKTTTTTTTTPAPEkSTEEPEEVVYPVDPVEPTDPEQPMGPQFDPNEIDCTNRDFVPHPNCR 543
Cdd:PTZ00449 678 dyLDAAAKSKETKTTVVLDESFESILKETLPE-TPGTPFTTPRPLPPKLPRDEEFPFEPIGDPDAEQPDDIEFFTPPEEE 756


                 ...
gi 21358195  544 KYF 546
Cdd:PTZ00449 757 RTF 759
 
Name Accession Description Interval E-value
GH18_chitolectin_chitotriosidase cd02872
This conserved domain family includes a large number of catalytically inactive chitinase-like ...
 29-397 1.77e-170

This conserved domain family includes a large number of catalytically inactive chitinase-like lectins (chitolectins) including YKL-39, YKL-40 (HCGP39), YM1, oviductin, and AMCase (acidic mammalian chitinase), as well as catalytically active chitotriosidases. The conserved domain is an eight-stranded alpha/beta barrel fold belonging to the family 18 glycosyl hydrolases. The fold has a pronounced active-site cleft at the C-terminal end of the beta-barrel. The chitolectins lack a key active site glutamate (the proton donor required for hydrolytic activity) but retain highly conserved residues involved in oligosaccharide binding. Chitotriosidase is a chitinolytic enzyme expressed in maturing macrophages, which suggests that it plays a part in antimicrobial defense. Chitotriosidase hydrolyzes chitotriose, as well as colloidal chitin to yield chitobiose and is therefore considered an exochitinase. Chitotriosidase occurs in two major forms, the large form being converted to the small form by either RNA or post-translational processing. Although the small form, containing the chitinase domain alone, is sufficient for the chitinolytic activity, the additional C-terminal chitin-binding domain of the large form plays a role in processing colloidal chitin. The chitotriosidase gene is nonessential in humans, as about 35% of the population are heterozygous and 6% homozygous for an inactivated form of the gene. HCGP39 is a 39-kDa human cartilage glycoprotein thought to play a role in connective tissue remodeling and defense against pathogens.


Pssm-ID: 119351 [Multi-domain]  Cd Length: 362  Bit Score: 488.22  E-value: 1.77e-170
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195  29 IVCYFSNWAVYRTGIGRYGLEDVPADLCTHIIYSFIGVNDKSwDVLVIDPELDVDQGGFSKFTQLKKSNPNVKLEIAVGG 108
Cdd:cd02872   1 VVCYFTNWAQYRPGNGKFVPENIDPFLCTHIIYAFAGLNPDG-NIIILDEWNDIDLGLYERFNALKEKNPNLKTLLAIGG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195 109 WAEGGSKYSQMVAVRDRRQSFIRSVVRFMKQYNFDGFDLDWEYPGAtdRGGNYGDKDKFLYFVEELRRAFDREGRGWEIT 188
Cdd:cd02872  80 WNFGSAKFSAMAASPENRKTFIKSAIAFLRKYGFDGLDLDWEYPGQ--RGGPPEDKENFVTLLKELREAFEPEAPRLLLT 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195 189 MAVPVAKFRLNEGYHVPELCEALDAIHAMTYDLRGNWAGFADVHSPLYKRKHDQYAYEKLNVNDGLALWEEMGCPANKLV 268
Cdd:cd02872 158 AAVSAGKETIDAAYDIPEISKYLDFINVMTYDFHGSWEGVTGHNSPLYAGSADTGDQKYLNVDYAIKYWLSKGAPPEKLV 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195 269 VGVPFYGRTFTLSNSNKNynmGTYINkEAGGGAPGPYTNASGFLAYYEICTEVmdkSKGWTVEWDDAGMVPYTYKDTQWV 348
Cdd:cd02872 238 LGIPTYGRSFTLASPSNT---GVGAP-ASGPGTAGPYTREAGFLAYYEICEFL---KSGWTVVWDDEQKVPYAYKGNQWV 310

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 21358195 349 GYENEASIQIKMDFIKQRGYAGAMTWAIDMDDFHGMCG-RKNGLTQILYD 397
Cdd:cd02872 311 GYDDEESIALKVQYLKSKGLGGAMVWSIDLDDFRGTCGqGKYPLLNAINR 360
Glyco_18 smart00636
Glyco_18 domain;
28-379 5.88e-132

Glyco_18 domain;


Pssm-ID: 214753 [Multi-domain]  Cd Length: 334  Bit Score: 388.96  E-value: 5.88e-132
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195     28 RIVCYFSNWAVYRTgigRYGLEDVPADLCTHIIYSFIGVnDKSWDVLVIDPELDVDQggFSKFTQLKKSNPNVKLEIAVG 107
Cdd:smart00636   1 RVVGYFTNWGVYGR---NFPVDDIPASKLTHIIYAFANI-DPDGTVTIGDEWADIGN--FGQLKALKKKNPGLKVLLSIG 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195    108 GWAEGgSKYSQMVAVRDRRQSFIRSVVRFMKQYNFDGFDLDWEYPGATDRggnygDKDKFLYFVEELRRAFDRE---GRG 184
Cdd:smart00636  75 GWTES-DNFSSMLSDPASRKKFIDSIVSFLKKYGFDGIDIDWEYPGGRGD-----DRENYTALLKELREALDKEgaeGKG 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195    185 WEITMAVPVAKFRLNEGYH-VPELCEALDAIHAMTYDLRGNWAGFADVHSPLYKRKHDQyayEKLNVNDGLALWEEMGCP 263
Cdd:smart00636 149 YLLTIAVPAGPDKIDKGYGdLPAIAKYLDFINLMTYDFHGAWSNPTGHNAPLYAGPGDP---EKYNVDYAVKYYLCKGVP 225

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195    264 ANKLVVGVPFYGRTFTLSNSNKNynmgTYINKEAGGGAPGPYTNASGFLAYYEICtevmdKSKGWTVEWDDAGMVPYTYK 343
Cdd:smart00636 226 PSKLVLGIPFYGRGWTLVDGSNN----GPGAPFTGPATGGPGTWEGGVVDYREIC-----KLLGATVVYDDTAKAPYAYN 296

                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 21358195    344 DT--QWVGYENEASIQIKMDFIKQRGYAGAMTWAIDMD 379
Cdd:smart00636 297 PGtgQWVSYDDPRSIKAKADYVKDKGLGGVMIWELDAD 334
Glyco_hydro_18 pfam00704
Glycosyl hydrolases family 18;
28-379 4.12e-117

Glycosyl hydrolases family 18;


Pssm-ID: 425828 [Multi-domain]  Cd Length: 311  Bit Score: 350.22  E-value: 4.12e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195    28 RIVCYFSNWAVYRTGigryglEDVPADLCTHIIYSFIGVNDKSWDVLVIDPeldvDQGGFSKFTQLKK-SNPNVKLEIAV 106
Cdd:pfam00704   1 RIVGYYTSWGVYRNG------NFLPSDKLTHIIYAFANIDGSDGTLFIGDW----DLGNFEQLKKLKKqKNPGVKVLLSI 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195   107 GGWAeGGSKYSQMVAVRDRRQSFIRSVVRFMKQYNFDGFDLDWEYPGatdrgGNYGDKDKFLYFVEELRRAFDR--EGRG 184
Cdd:pfam00704  71 GGWT-DSTGFSLMASNPASRKKFADSIVSFLRKYGFDGIDIDWEYPG-----GNPEDKENYDLLLRELRAALDEakGGKK 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195   185 WEITMAVPVAKFRLNEGYHVPELCEALDAIHAMTYDLRGNWAGFADVHSPLYkrkhdqyAYEKLNVNDGLALWEEMGCPA 264
Cdd:pfam00704 145 YLLSAAVPASYPDLDKGYDLPKIAKYLDFINVMTYDFHGSWDNVTGHHAPLY-------GGGSYNVDYAVKYYLKQGVPA 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195   265 NKLVVGVPFYGRTFTLSNSNKNynmgtyinkeagggapgpyTNASGFLAYYEICTevMDKSKGWTVEWDDAGMVPYTYKD 344
Cdd:pfam00704 218 SKLVLGVPFYGRSWTLVNGSGN-------------------TWEDGVLAYKEICN--LLKDNGATVVWDDVAKAPYVYDG 276

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 21358195   345 TQWVGYENEASIQIKMDFIKQRGYAGAMTWAIDMD 379
Cdd:pfam00704 277 DQFITYDDPRSIATKVDYVKAKGLGGVMIWSLDAD 311
ChiA COG3325
Chitinase, GH18 family [Carbohydrate transport and metabolism];
17-383 6.95e-94

Chitinase, GH18 family [Carbohydrate transport and metabolism];


Pssm-ID: 442554 [Multi-domain]  Cd Length: 391  Bit Score: 293.36  E-value: 6.95e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195  17 PAATVASDQASRIVCYFSNWAVYRTGigrYGLEDVPADLCTHIIYSFIGVN--------DKSWDVLVIDPELDVDQ---G 85
Cdd:COG3325   9 TAAAATATSGKRVVGYFTQWGIYGRN---YLVKDIPASKLTHINYAFANVDpdgkcsvgDAWAKPSVDGAADDWDQplkG 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195  86 GFSKFTQLKKSNPNVKLEIAVGGWaeGGSKY-SQMVAVRDRRQSFIRSVVRFMKQYNFDGFDLDWEYPGATDRGGNYG-- 162
Cdd:COG3325  86 NFNQLKKLKAKNPNLKVLISIGGW--TWSKGfSDAAATPASRAAFVDSCVDLLRKYNFDGIDIDWEYPGSGGAPGNVYrp 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195 163 -DKDKFLYFVEELRRAFDR----EGRGWEITMAVPVAKFRLnEGYHVPELCEALDAIHAMTYDLRGNWAGFADVHSPLYK 237
Cdd:COG3325 164 eDKANFTALLKELRAQLDAlgaeTGKHYLLTAAAPAGPDKL-DGIELPKVAQYLDYVNVMTYDFHGAWSPTTGHQAPLYD 242

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195 238 RKHDQYAyEKLNVNDGLALWEEMGCPANKLVVGVPFYGRTFTlsnSNKNYNMGTYinKEAGGGAPGPYTNasGFLAYYEI 317
Cdd:COG3325 243 SPKDPEA-QGYSVDSAVQAYLAAGVPASKLVLGVPFYGRGWT---GVTGGNNGLY--QPATGPAPGTWEA--GVNDYKDL 314

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21358195 318 cTEVMDKSKGWTVEWDDAGMVPYTYKDT--QWVGYENEASIQIKMDFIKQRGYAGAMTWAIDMDDFHG 383
Cdd:COG3325 315 -KALYLGSNGYTRYWDDVAKAPYLYNGDtgTFISYDDPRSIAAKADYVKDKGLGGVMFWELSGDTADG 381
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
 531-578 4.12e-12

Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.


Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 61.28  E-value: 4.12e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 21358195   531 CTNRD--FVPHP-NCRKYFRCVHGKPVEFECKEGTAFHTVLNVCDWIENSD 578
Cdd:pfam01607   1 CAGKEdgYYADPgDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDYPDNVV 51
ChtBD2 smart00494
Chitin-binding domain type 2;
529-573 2.58e-10

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 55.91  E-value: 2.58e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 21358195    529 IDCTNRD--FVPHP-NCRKYFRCVHGKPVEFECKEGTAFHTVLNVCDW 573
Cdd:smart00494   1 NECPGRGdgLYPHPtDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 400-546 9.37e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 38.90  E-value: 9.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195  400 KNYRVPE-PTRQTTP-RPEWAKPPATPPNPDEGAV----VAPTTSTTKRPKPKPKPTSSPLSPTSAPGPV-PT------- 465
Cdd:PTZ00449 598 KRPRSAQrPTRPKSPkLPELLDIPKSPKRPESPKSpkrpPPPQRPSSPERPEGPKIIKSPKPPKSPKPPFdPKfkekfyd 677

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195  466 --VGSSTPKPTTKKPKKPKKTTTTTTTTPAPEkSTEEPEEVVYPVDPVEPTDPEQPMGPQFDPNEIDCTNRDFVPHPNCR 543
Cdd:PTZ00449 678 dyLDAAAKSKETKTTVVLDESFESILKETLPE-TPGTPFTTPRPLPPKLPRDEEFPFEPIGDPDAEQPDDIEFFTPPEEE 756


                 ...
gi 21358195  544 KYF 546
Cdd:PTZ00449 757 RTF 759
 
Name Accession Description Interval E-value
GH18_chitolectin_chitotriosidase cd02872
This conserved domain family includes a large number of catalytically inactive chitinase-like ...
 29-397 1.77e-170

This conserved domain family includes a large number of catalytically inactive chitinase-like lectins (chitolectins) including YKL-39, YKL-40 (HCGP39), YM1, oviductin, and AMCase (acidic mammalian chitinase), as well as catalytically active chitotriosidases. The conserved domain is an eight-stranded alpha/beta barrel fold belonging to the family 18 glycosyl hydrolases. The fold has a pronounced active-site cleft at the C-terminal end of the beta-barrel. The chitolectins lack a key active site glutamate (the proton donor required for hydrolytic activity) but retain highly conserved residues involved in oligosaccharide binding. Chitotriosidase is a chitinolytic enzyme expressed in maturing macrophages, which suggests that it plays a part in antimicrobial defense. Chitotriosidase hydrolyzes chitotriose, as well as colloidal chitin to yield chitobiose and is therefore considered an exochitinase. Chitotriosidase occurs in two major forms, the large form being converted to the small form by either RNA or post-translational processing. Although the small form, containing the chitinase domain alone, is sufficient for the chitinolytic activity, the additional C-terminal chitin-binding domain of the large form plays a role in processing colloidal chitin. The chitotriosidase gene is nonessential in humans, as about 35% of the population are heterozygous and 6% homozygous for an inactivated form of the gene. HCGP39 is a 39-kDa human cartilage glycoprotein thought to play a role in connective tissue remodeling and defense against pathogens.


Pssm-ID: 119351 [Multi-domain]  Cd Length: 362  Bit Score: 488.22  E-value: 1.77e-170
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195  29 IVCYFSNWAVYRTGIGRYGLEDVPADLCTHIIYSFIGVNDKSwDVLVIDPELDVDQGGFSKFTQLKKSNPNVKLEIAVGG 108
Cdd:cd02872   1 VVCYFTNWAQYRPGNGKFVPENIDPFLCTHIIYAFAGLNPDG-NIIILDEWNDIDLGLYERFNALKEKNPNLKTLLAIGG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195 109 WAEGGSKYSQMVAVRDRRQSFIRSVVRFMKQYNFDGFDLDWEYPGAtdRGGNYGDKDKFLYFVEELRRAFDREGRGWEIT 188
Cdd:cd02872  80 WNFGSAKFSAMAASPENRKTFIKSAIAFLRKYGFDGLDLDWEYPGQ--RGGPPEDKENFVTLLKELREAFEPEAPRLLLT 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195 189 MAVPVAKFRLNEGYHVPELCEALDAIHAMTYDLRGNWAGFADVHSPLYKRKHDQYAYEKLNVNDGLALWEEMGCPANKLV 268
Cdd:cd02872 158 AAVSAGKETIDAAYDIPEISKYLDFINVMTYDFHGSWEGVTGHNSPLYAGSADTGDQKYLNVDYAIKYWLSKGAPPEKLV 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195 269 VGVPFYGRTFTLSNSNKNynmGTYINkEAGGGAPGPYTNASGFLAYYEICTEVmdkSKGWTVEWDDAGMVPYTYKDTQWV 348
Cdd:cd02872 238 LGIPTYGRSFTLASPSNT---GVGAP-ASGPGTAGPYTREAGFLAYYEICEFL---KSGWTVVWDDEQKVPYAYKGNQWV 310

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 21358195 349 GYENEASIQIKMDFIKQRGYAGAMTWAIDMDDFHGMCG-RKNGLTQILYD 397
Cdd:cd02872 311 GYDDEESIALKVQYLKSKGLGGAMVWSIDLDDFRGTCGqGKYPLLNAINR 360
Glyco_18 smart00636
Glyco_18 domain;
28-379 5.88e-132

Glyco_18 domain;


Pssm-ID: 214753 [Multi-domain]  Cd Length: 334  Bit Score: 388.96  E-value: 5.88e-132
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195     28 RIVCYFSNWAVYRTgigRYGLEDVPADLCTHIIYSFIGVnDKSWDVLVIDPELDVDQggFSKFTQLKKSNPNVKLEIAVG 107
Cdd:smart00636   1 RVVGYFTNWGVYGR---NFPVDDIPASKLTHIIYAFANI-DPDGTVTIGDEWADIGN--FGQLKALKKKNPGLKVLLSIG 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195    108 GWAEGgSKYSQMVAVRDRRQSFIRSVVRFMKQYNFDGFDLDWEYPGATDRggnygDKDKFLYFVEELRRAFDRE---GRG 184
Cdd:smart00636  75 GWTES-DNFSSMLSDPASRKKFIDSIVSFLKKYGFDGIDIDWEYPGGRGD-----DRENYTALLKELREALDKEgaeGKG 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195    185 WEITMAVPVAKFRLNEGYH-VPELCEALDAIHAMTYDLRGNWAGFADVHSPLYKRKHDQyayEKLNVNDGLALWEEMGCP 263
Cdd:smart00636 149 YLLTIAVPAGPDKIDKGYGdLPAIAKYLDFINLMTYDFHGAWSNPTGHNAPLYAGPGDP---EKYNVDYAVKYYLCKGVP 225

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195    264 ANKLVVGVPFYGRTFTLSNSNKNynmgTYINKEAGGGAPGPYTNASGFLAYYEICtevmdKSKGWTVEWDDAGMVPYTYK 343
Cdd:smart00636 226 PSKLVLGIPFYGRGWTLVDGSNN----GPGAPFTGPATGGPGTWEGGVVDYREIC-----KLLGATVVYDDTAKAPYAYN 296

                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 21358195    344 DT--QWVGYENEASIQIKMDFIKQRGYAGAMTWAIDMD 379
Cdd:smart00636 297 PGtgQWVSYDDPRSIKAKADYVKDKGLGGVMIWELDAD 334
Glyco_hydro_18 pfam00704
Glycosyl hydrolases family 18;
28-379 4.12e-117

Glycosyl hydrolases family 18;


Pssm-ID: 425828 [Multi-domain]  Cd Length: 311  Bit Score: 350.22  E-value: 4.12e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195    28 RIVCYFSNWAVYRTGigryglEDVPADLCTHIIYSFIGVNDKSWDVLVIDPeldvDQGGFSKFTQLKK-SNPNVKLEIAV 106
Cdd:pfam00704   1 RIVGYYTSWGVYRNG------NFLPSDKLTHIIYAFANIDGSDGTLFIGDW----DLGNFEQLKKLKKqKNPGVKVLLSI 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195   107 GGWAeGGSKYSQMVAVRDRRQSFIRSVVRFMKQYNFDGFDLDWEYPGatdrgGNYGDKDKFLYFVEELRRAFDR--EGRG 184
Cdd:pfam00704  71 GGWT-DSTGFSLMASNPASRKKFADSIVSFLRKYGFDGIDIDWEYPG-----GNPEDKENYDLLLRELRAALDEakGGKK 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195   185 WEITMAVPVAKFRLNEGYHVPELCEALDAIHAMTYDLRGNWAGFADVHSPLYkrkhdqyAYEKLNVNDGLALWEEMGCPA 264
Cdd:pfam00704 145 YLLSAAVPASYPDLDKGYDLPKIAKYLDFINVMTYDFHGSWDNVTGHHAPLY-------GGGSYNVDYAVKYYLKQGVPA 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195   265 NKLVVGVPFYGRTFTLSNSNKNynmgtyinkeagggapgpyTNASGFLAYYEICTevMDKSKGWTVEWDDAGMVPYTYKD 344
Cdd:pfam00704 218 SKLVLGVPFYGRSWTLVNGSGN-------------------TWEDGVLAYKEICN--LLKDNGATVVWDDVAKAPYVYDG 276

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 21358195   345 TQWVGYENEASIQIKMDFIKQRGYAGAMTWAIDMD 379
Cdd:pfam00704 277 DQFITYDDPRSIATKVDYVKAKGLGGVMIWSLDAD 311
ChiA COG3325
Chitinase, GH18 family [Carbohydrate transport and metabolism];
17-383 6.95e-94

Chitinase, GH18 family [Carbohydrate transport and metabolism];


Pssm-ID: 442554 [Multi-domain]  Cd Length: 391  Bit Score: 293.36  E-value: 6.95e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195  17 PAATVASDQASRIVCYFSNWAVYRTGigrYGLEDVPADLCTHIIYSFIGVN--------DKSWDVLVIDPELDVDQ---G 85
Cdd:COG3325   9 TAAAATATSGKRVVGYFTQWGIYGRN---YLVKDIPASKLTHINYAFANVDpdgkcsvgDAWAKPSVDGAADDWDQplkG 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195  86 GFSKFTQLKKSNPNVKLEIAVGGWaeGGSKY-SQMVAVRDRRQSFIRSVVRFMKQYNFDGFDLDWEYPGATDRGGNYG-- 162
Cdd:COG3325  86 NFNQLKKLKAKNPNLKVLISIGGW--TWSKGfSDAAATPASRAAFVDSCVDLLRKYNFDGIDIDWEYPGSGGAPGNVYrp 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195 163 -DKDKFLYFVEELRRAFDR----EGRGWEITMAVPVAKFRLnEGYHVPELCEALDAIHAMTYDLRGNWAGFADVHSPLYK 237
Cdd:COG3325 164 eDKANFTALLKELRAQLDAlgaeTGKHYLLTAAAPAGPDKL-DGIELPKVAQYLDYVNVMTYDFHGAWSPTTGHQAPLYD 242

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195 238 RKHDQYAyEKLNVNDGLALWEEMGCPANKLVVGVPFYGRTFTlsnSNKNYNMGTYinKEAGGGAPGPYTNasGFLAYYEI 317
Cdd:COG3325 243 SPKDPEA-QGYSVDSAVQAYLAAGVPASKLVLGVPFYGRGWT---GVTGGNNGLY--QPATGPAPGTWEA--GVNDYKDL 314

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21358195 318 cTEVMDKSKGWTVEWDDAGMVPYTYKDT--QWVGYENEASIQIKMDFIKQRGYAGAMTWAIDMDDFHG 383
Cdd:COG3325 315 -KALYLGSNGYTRYWDDVAKAPYLYNGDtgTFISYDDPRSIAAKADYVKDKGLGGVMFWELSGDTADG 381
GH18_chitinase cd06548
The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant ...
 29-379 1.42e-79

The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant polymer of N-acetylglucosamine and have been identified in bacteria, fungi, insects, plants, viruses, and protozoan parasites. The structure of this domain is an eight-stranded alpha/beta barrel with a pronounced active-site cleft at the C-terminal end of the beta-barrel.


Pssm-ID: 119365 [Multi-domain]  Cd Length: 322  Bit Score: 253.71  E-value: 1.42e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195  29 IVCYFSNWAVYrtgIGRYGLE-DVPADLCTHIIYSFIGVN--------DKSWDVL-------VIDPELDVDQGGFSKFTQ 92
Cdd:cd06548   1 VVGYFTNWGIY---GRNYFVTdDIPADKLTHINYAFADIDgdggvvtsDDEAADEaaqsvdgGADTDDQPLKGNFGQLRK 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195  93 LKKSNPNVKLEIAVGGWAEGGsKYSQMVAVRDRRQSFIRSVVRFMKQYNFDGFDLDWEYPGATDRGGNYG---DKDKFLY 169
Cdd:cd06548  78 LKQKNPHLKILLSIGGWTWSG-GFSDAAATEASRAKFADSAVDFIRKYGFDGIDIDWEYPGSGGAPGNVArpeDKENFTL 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195 170 FVEELRRAFD----REGRGWEITMAVPVAKFRLNEGYhVPELCEALDAIHAMTYDLRGNWAGFADVHSPLYKRKHDQyaY 245
Cdd:cd06548 157 LLKELREALDalgaETGRKYLLTIAAPAGPDKLDKLE-VAEIAKYLDFINLMTYDFHGAWSNTTGHHSNLYASPADP--P 233

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195 246 EKLNVNDGLALWEEMGCPANKLVVGVPFYGRTFTlsnsnknynmgtyinkeagggapgpytnasgflayyeictevmdks 325
Cdd:cd06548 234 GGYSVDAAVNYYLSAGVPPEKLVLGVPFYGRGWT---------------------------------------------- 267

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 21358195 326 kGWTVEWDDAGMVPYTYKDT--QWVGYENEASIQIKMDFIKQRGYAGAMTWAIDMD 379
Cdd:cd06548 268 -GYTRYWDEVAKAPYLYNPStkTFISYDDPRSIKAKADYVKDKGLGGVMFWELSGD 322
GH18_IDGF cd02873
The IDGF's (imaginal disc growth factors) are a family of growth factors identified in insects ...
 28-386 1.78e-55

The IDGF's (imaginal disc growth factors) are a family of growth factors identified in insects that include at least five members, some of which are encoded by genes in a tight cluster. The IDGF's have an eight-stranded alpha/beta barrel fold and are related to the glycosyl hydrolase family 18 (GH18) chitinases, but they have an amino acid substitution known to abolish chitinase catalytic activity. IDGFs may have evolved from chitinases to gain new functions as growth factors, interacting with cell surface glycoproteins involved in growth-promoting processes.


Pssm-ID: 119352 [Multi-domain]  Cd Length: 413  Bit Score: 193.30  E-value: 1.78e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195  28 RIVCYFSNWAVYRTGIGRYGLEDV-PA-DLCTHIIYSFIGVNDKSWDVLVIDPELDVDQGGFSKFTQLKKSNPNVKLEIA 105
Cdd:cd02873   1 KLVCYYDSKSYLREGLAKMSLEDLePAlQFCTHLVYGYAGIDADTYKIKSLNEDLDLDKSHYRAITSLKRKYPHLKVLLS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195 106 VGGWAEGGS-----KYSQMVAVRDRRQSFIRSVVRFMKQYNFDGFDLDWEYPGAT---DRG--GNY---------GD--- 163
Cdd:cd02873  81 VGGDRDTDEegeneKYLLLLESSESRNAFINSAHSLLKTYGFDGLDLAWQFPKNKpkkVRGtfGSAwhsfkklftGDsvv 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195 164 -------KDKFLYFVEELRRAFDREGRGWEITMA--VPVAKFrlnegYHVPELCEALDAIHAMTYD----LRGNWAgfAD 230
Cdd:cd02873 161 dekaaehKEQFTALVRELKNALRPDGLLLTLTVLphVNSTWY-----FDVPAIANNVDFVNLATFDfltpERNPEE--AD 233

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195 231 VHSPLYkrkhdqYAYEKL---NVNDGLALWEEMGCPANKLVVGVPFYGRTFTLS-NSNKNynmGTYINKEAGG-GAPGPY 305
Cdd:cd02873 234 YTAPIY------ELYERNphhNVDYQVKYWLNQGTPASKLNLGIATYGRAWKLTkDSGIT---GVPPVLETDGpGPAGPQ 304

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195 306 TNASGFLAYYEICT----------------EVMDKSKGWtvewddaGMVPYTYKDTQ-----WVGYENEASIQIKMDFIK 364
Cdd:cd02873 305 TKTPGLLSWPEICSklpnpanlkgadaplrKVGDPTKRF-------GSYAYRPADENgehgiWVSYEDPDTAANKAGYAK 377

                       410       420
                ....*....|....*....|..
gi 21358195 365 QRGYAGAMTWAIDMDDFHGMCG 386
Cdd:cd02873 378 AKGLGGVALFDLSLDDFRGQCT 399
GH18_chitinase-like cd00598
The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant ...
 29-221 2.01e-47

The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant polymer of beta-1,4-linked N-acetylglucosamine (GlcNAc) which is a major component of the cell wall of fungi and the exoskeleton of arthropods. Chitinases have been identified in viruses, bacteria, fungi, protozoan parasites, insects, and plants. The structure of the GH18 domain is an eight-stranded beta/alpha barrel with a pronounced active-site cleft at the C-terminal end of the beta-barrel. The GH18 family includes chitotriosidase, chitobiase, hevamine, zymocin-alpha, narbonin, SI-CLP (stabilin-1 interacting chitinase-like protein), IDGF (imaginal disc growth factor), CFLE (cortical fragment-lytic enzyme) spore hydrolase, the type III and type V plant chitinases, the endo-beta-N-acetylglucosaminidases, and the chitolectins. The GH85 (glycosyl hydrolase, family 85) ENGases (endo-beta-N-acetylglucosaminidases) are closely related to the GH18 chitinases and are included in this alignment model.


Pssm-ID: 119349 [Multi-domain]  Cd Length: 210  Bit Score: 165.24  E-value: 2.01e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195  29 IVCYFSNWAVYRTGIgrygLEDVPADLCTHIIYSFIGVNdksWDVLVIDPELDVDQGGFSKFTQLKKSNPNVKLEIAVGG 108
Cdd:cd00598   1 VICYYDGWSSGRGPD----PTDIPLSLCTHIIYAFAEIS---SDGSLNLFGDKSEEPLKGALEELASKKPGLKVLISIGG 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195 109 WaeGGSKYSQMVAVRDRRQSFIRSVVRFMKQYNFDGFDLDWEYPGATDRggnyGDKDKFLYFVEELRRAFDREgrGWEIT 188
Cdd:cd00598  74 W--TDSSPFTLASDPASRAAFANSLVSFLKTYGFDGVDIDWEYPGAADN----SDRENFITLLRELRSALGAA--NYLLT 145

                       170       180       190
                ....*....|....*....|....*....|...
gi 21358195 189 MAVPVAKFRLNEGYHVPELCEALDAIHAMTYDL 221
Cdd:cd00598 146 IAVPASYFDLGYAYDVPAIGDYVDFVNVMTYDL 178
GH18_plant_chitinase_class_V cd02879
The class V plant chitinases have a glycosyl hydrolase family 18 (GH18) domain, but lack the ...
 50-380 1.92e-45

The class V plant chitinases have a glycosyl hydrolase family 18 (GH18) domain, but lack the chitin-binding domain present in other GH18 enzymes. The GH18 domain of the class V chitinases has endochitinase activity in some cases and no catalytic activity in others. Included in this family is a lectin found in black locust (Robinia pseudoacacia) bark, which binds chitin but lacks chitinase activity. Also included is a chitinase-related receptor-like kinase (CHRK1) from tobacco (Nicotiana tabacum), with an N-terminal GH18 domain and a C-terminal kinase domain, which is thought to be part of a plant signaling pathway. The GH18 domain of CHRK1 is expressed extracellularly where it binds chitin but lacks chitinase activity.


Pssm-ID: 119358 [Multi-domain]  Cd Length: 299  Bit Score: 162.53  E-value: 1.92e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195  50 DVPADLCTHIIYSFIGVNDKSWDVLVIDPeldvDQGGFSKFTQ-LKKSNPNVKLEIAVGGWAEGGSKYSQMVAVRDRRQS 128
Cdd:cd02879  20 NIDSSLFTHLFYAFADLDPSTYEVVISPS----DESEFSTFTEtVKRKNPSVKTLLSIGGGGSDSSAFAAMASDPTARKA 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195 129 FIRSVVRFMKQYNFDGFDLDWEYPgATDRggnygDKDKFLYFVEELRRAFDREGRGWE-----ITMAVPVA-KFRLNEG- 201
Cdd:cd02879  96 FINSSIKVARKYGFDGLDLDWEFP-SSQV-----EMENFGKLLEEWRAAVKDEARSSGrppllLTAAVYFSpILFLSDDs 169

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195 202 --YHVPELCEALDAIHAMTYDLRGNWAGFA-DVHSPLYKRKhdqyayEKLNVNDGLALWEEMGCPANKLVVGVPFYGRTF 278
Cdd:cd02879 170 vsYPIEAINKNLDWVNVMAYDYYGSWESNTtGPAAALYDPN------SNVSTDYGIKSWIKAGVPAKKLVLGLPLYGRAW 243

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195 279 TLsnsnknynmgtyinkeagggapgpytnasgflayyeictevmdkskgwtveWDDAGMVPYTYKDTQWVGYENEASIQI 358
Cdd:cd02879 244 TL---------------------------------------------------YDTTTVSSYVYAGTTWIGYDDVQSIAV 272

                       330       340
                ....*....|....*....|..
gi 21358195 359 KMDFIKQRGYAGAMTWAIDMDD 380
Cdd:cd02879 273 KVKYAKQKGLLGYFAWAVGYDD 294
GH18_zymocin_alpha cd02878
Zymocin, alpha subunit. Zymocin is a heterotrimeric enzyme that inhibits yeast cell cycle ...
 57-379 4.88e-42

Zymocin, alpha subunit. Zymocin is a heterotrimeric enzyme that inhibits yeast cell cycle progression. The zymocin alpha subunit has a chitinase activity that is essential for holoenzyme action from the cell exterior while the gamma subunit contains the intracellular toxin responsible for G1 phase cell cycle arrest. The zymocin alpha and beta subunits are thought to act from the cell's exterior by docking to the cell wall-associated chitin, thus mediating gamma-toxin translocation. The alpha subunit has an eight-stranded TIM barrel fold similar to that of family 18 glycosyl hydrolases such as hevamine, chitolectin, and chitobiase.


Pssm-ID: 119357 [Multi-domain]  Cd Length: 345  Bit Score: 154.77  E-value: 4.88e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195  57 THIIYSFIGVNdkswdvlvidPELDVD----QGGFSKFTQLKksnpNVKLEIAVGGWAeggskYSQMVA----VRD---- 124
Cdd:cd02878  29 THIHFAFANIT----------SDFSVDvssvQEQFSDFKKLK----GVKKILSFGGWD-----FSTSPStyqiFRDavkp 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195 125 -RRQSFIRSVVRFMKQYNFDGFDLDWEYPGATD----RGGNYGDKDKFLYFVEELRRAFdreGRGWEITMAVPVAKFRLn 199
Cdd:cd02878  90 aNRDTFANNVVNFVNKYNLDGVDFDWEYPGAPDipgiPAGDPDDGKNYLEFLKLLKSKL---PSGKSLSIAAPASYWYL- 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195 200 EGYHVPELCEALDAIHAMTYDLRGNW---AGFADVHSPL--YKRKHdqyaYEKLNVNDGLALWEEMGCPANKLVVGVPFY 274
Cdd:cd02878 166 KGFPIKDMAKYVDYIVYMTYDLHGQWdygNKWASPGCPAgnCLRSH----VNKTETLDALSMITKAGVPSNKVVVGVASY 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195 275 GRTFTLSNSNKNYNMGTYiNKEAGGGAPGPYTNASGFLAYYEICTEVMDKSKGWTVEWDDAGMVPYTYKDTQWVGYENEA 354
Cdd:cd02878 242 GRSFKMADPGCTGPGCTF-TGPGSGAEAGRCTCTAGYGAISEIEIIDISKSKNKRWYDTDSDSDILVYDDDQWVAYMSPA 320

                       330       340
                ....*....|....*....|....*
gi 21358195 355 SIQIKMDFIKQRGYAGAMTWAIDMD 379
Cdd:cd02878 321 TKAARIEWYKGLNFGGTSDWAVDLQ 345
GH18_CFLE_spore_hydrolase cd02874
Cortical fragment-lytic enzyme (CFLE) is a peptidoglycan hydrolase involved in bacterial ...
 117-380 8.13e-22

Cortical fragment-lytic enzyme (CFLE) is a peptidoglycan hydrolase involved in bacterial endospore germination. CFLE is expressed as an inactive preprotein (called SleB) in the forespore compartment of sporulating cells. SleB translocates across the forespore inner membrane and is deposited as a mature enzyme in the cortex layer of the spore. As part of a sensory mechanism capable of initiating germination, CFLE degrades a spore-specific peptidoglycan constituent called muramic-acid delta-lactam that comprises the outer cortex. CFLE has a C-terminal glycosyl hydrolase family 18 (GH18) catalytic domain as well as two N-terminal LysM peptidoglycan-binding domains. In addition to SleB, this family includes YaaH, YdhD, and YvbX from Bacillus subtilis.


Pssm-ID: 119353 [Multi-domain]  Cd Length: 313  Bit Score: 96.57  E-value: 8.13e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195 117 SQMVAVRDRRQSFIRSVVRFMKQYNFDGFDLDWEYPgatdrggNYGDKDKFLYFVEELRRAFDREGRgwEITMAVPVAKF 196
Cdd:cd02874  79 HAVLSNPEARQRLINNILALAKKYGYDGVNIDFENV-------PPEDREAYTQFLRELSDRLHPAGY--TLSTAVVPKTS 149

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195 197 -----RLNEGYHVPELCEALDAIHAMTYDLRGNWAGFADVHSPLYKRKHDQYAYEKLnvndglalweemgcPANKLVVGV 271
Cdd:cd02874 150 adqfgNWSGAYDYAAIGKIVDFVVLMTYDWHWRGGPPGPVAPIGWVERVLQYAVTQI--------------PREKILLGI 215

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195 272 PFYGRTFTLsnsnknynmgtyinKEAGGGAPGPYTNAsgflayyeictEVMD--KSKGWTVEWDDAGMVP-YTYKDTQ-- 346
Cdd:cd02874 216 PLYGYDWTL--------------PYKKGGKASTISPQ-----------QAINlaKRYGAEIQYDEEAQSPfFRYVDEQgr 270

                       250       260       270
                ....*....|....*....|....*....|....*.
gi 21358195 347 --WVGYENEASIQIKMDFIKQRGYAGAMTWAIDMDD 380
Cdd:cd02874 271 rhEVWFEDARSLQAKFELAKEYGLRGVSYWRLGLED 306
GH18_3CO4_chitinase cd06545
The Bacteroides thetaiotaomicron protein represented by pdb structure 3CO4 is an ...
 99-299 1.59e-15

The Bacteroides thetaiotaomicron protein represented by pdb structure 3CO4 is an uncharacterized bacterial member of the family 18 glycosyl hydrolases with homologs found in Flavobacterium, Stigmatella, and Pseudomonas.


Pssm-ID: 119362 [Multi-domain]  Cd Length: 253  Bit Score: 76.72  E-value: 1.59e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195  99 NVKLEIAVGGwaEGGSKYSQMVAVRDRRQSFIRSVVRFMKQYNFDGFDLDWEYPGATdrGGNYGDkdkflyFVEELRRAF 178
Cdd:cd06545  59 NVKILISLAG--GSPPEFTAALNDPAKRKALVDKIINYVVSYNLDGIDVDLEGPDVT--FGDYLV------FIRALYAAL 128

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195 179 DREGRgwEITMAVPvakfRLNEGYHVPELCEALDAIHAMTYDLRGNWAGFADVhsplykrKHDQYAYEklnVNDgLALWE 258
Cdd:cd06545 129 KKEGK--LLTAAVS----SWNGGAVSDSTLAYFDFINIMSYDATGPWWGDNPG-------QHSSYDDA---VND-LNYWN 191

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 21358195 259 EMG-CPANKLVVGVPFYGRTFTLSNSNKNYNMGTYINKEAGG 299
Cdd:cd06545 192 ERGlASKDKLVLGLPFYGYGFYYNGIPTIRNKVAFAKQNYGG 233
GH18_chitobiase cd02875
Chitobiase (also known as di-N-acetylchitobiase) is a lysosomal glycosidase that hydrolyzes ...
 126-383 1.71e-14

Chitobiase (also known as di-N-acetylchitobiase) is a lysosomal glycosidase that hydrolyzes the reducing-end N-acetylglucosamine from the chitobiose core of oligosaccharides during the ordered degradation of asparagine-linked glycoproteins in eukaryotes. Chitobiase can only do so if the asparagine that joins the oligosaccharide to protein is previously removed by a glycosylasparaginase. Chitobiase is therefore the final step in the lysosomal degradation of the protein/carbohydrate linkage component of asparagine-linked glycoproteins. The catalytic domain of chitobiase is an eight-stranded alpha/beta barrel fold similar to that of other family 18 glycosyl hydrolases such as hevamine and chitotriosidase.


Pssm-ID: 119354 [Multi-domain]  Cd Length: 358  Bit Score: 75.16  E-value: 1.71e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195 126 RQSFIRSVVRFMKQYNFDGFDLDWEYPGATDrGGNYgdkDKFLYFVEELRRAFDREGRGWEITMAVPVA----KFRLneg 201
Cdd:cd02875  97 RTQWIQQKVELAKSQFMDGINIDIEQPITKG-SPEY---YALTELVKETTKAFKKENPGYQISFDVAWSpsciDKRC--- 169

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195 202 YHVPELCEALDAIHAMTYDLRGN-WAG--FADVHSPLykrkhdqyayekLNVNDGLALWEEMGCPANKLVVGVPFYGRTF 278
Cdd:cd02875 170 YDYTGIADASDFLVVMDYDEQSQiWGKecIAGANSPY------------SQTLSGYNNFTKLGIDPKKLVMGLPWYGYDY 237

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195 279 TLSNSNKNYNMGTyINKEAGGGAPGpyTNASGF-LAYYEICTEVMDKSKGwtVEWDDAGMVP-YTYKDTQ----WVGYEN 352
Cdd:cd02875 238 PCLNGNLEDVVCT-IPKVPFRGANC--SDAAGRqIPYSEIMKQINSSIGG--RLWDSEQKSPfYNYKDKQgnlhQVWYDN 312

                       250       260       270
                ....*....|....*....|....*....|.
gi 21358195 353 EASIQIKMDFIKQRGYAGAMTWAIDMDDFHG 383
Cdd:cd02875 313 PQSLSIKVAYAKNLGLKGIGMWNGDLLDYSG 343
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
 531-578 4.12e-12

Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.


Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 61.28  E-value: 4.12e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 21358195   531 CTNRD--FVPHP-NCRKYFRCVHGKPVEFECKEGTAFHTVLNVCDWIENSD 578
Cdd:pfam01607   1 CAGKEdgYYADPgDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDYPDNVV 51
ChtBD2 smart00494
Chitin-binding domain type 2;
529-573 2.58e-10

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 55.91  E-value: 2.58e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 21358195    529 IDCTNRD--FVPHP-NCRKYFRCVHGKPVEFECKEGTAFHTVLNVCDW 573
Cdd:smart00494   1 NECPGRGdgLYPHPtDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
GH18_EndoS-like cd06542
Endo-beta-N-acetylglucosaminidases are bacterial chitinases that hydrolyze the chitin core of ...
 129-183 3.34e-06

Endo-beta-N-acetylglucosaminidases are bacterial chitinases that hydrolyze the chitin core of various asparagine (N)-linked glycans and glycoproteins. The endo-beta-N-acetylglucosaminidases have a glycosyl hydrolase family 18 (GH18) catalytic domain. Some members also have an additional C-terminal glycosyl hydrolase family 20 (GH20) domain while others have an N-terminal domain of unknown function (pfam08522). Members of this family include endo-beta-N-acetylglucosaminidase S (EndoS) from Streptococcus pyogenes, EndoF1, EndoF2, EndoF3, and EndoH from Flavobacterium meningosepticum, and EndoE from Enterococcus faecalis. EndoS is a secreted endoglycosidase from Streptococcus pyogenes that specifically hydrolyzes the glycan on human IgG between two core N-acetylglucosamine residues. EndoE is a secreted endoglycosidase, encoded by the ndoE gene in Enterococcus faecalis, that hydrolyzes the glycan on human RNase B.


Pssm-ID: 119359  Cd Length: 255  Bit Score: 48.91  E-value: 3.34e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 21358195 129 FIRSVVRFMKQYNFDGFDLDWEYPGATDRGGNYGDKDKFLYFVEELRRAFDREGR 183
Cdd:cd06542  92 YAKAIVDTVDKYGLDGVDFDDEYSGYGKNGTSQPSNEAFVRLIKELRKYMGPTDK 146
GH18_SI-CLP cd02876
Stabilin-1 interacting chitinase-like protein (SI-CLP) is a eukaryotic chitinase-like protein ...
 74-283 1.29e-05

Stabilin-1 interacting chitinase-like protein (SI-CLP) is a eukaryotic chitinase-like protein of unknown function that interacts with the endocytic/sorting transmembrane receptor stabilin-1 and is secreted from the lysosome. SI-CLP has a glycosyl hydrolase family 18 (GH18) domain but lacks a chitin-binding domain. The catalytic amino acids of the GH18 domain are not conserved in SI-CLP, similar to the chitolectins YKL-39, YKL-40, and YM1/2. Human SI-CLP is sorted to late endosomes and secretory lysosomes in alternatively activated macrophages.


Pssm-ID: 119355 [Multi-domain]  Cd Length: 318  Bit Score: 47.30  E-value: 1.29e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195  74 LVIDPELDVDQGGFSKftqLKKSNPNVKL--EIAVGGWAegGSKYSQMVAVRDRRQSFIRSVVRFMKQYNFDGFDLD-WE 150
Cdd:cd02876  44 FVIEGTHDIDKGWIEE---VRKANKNIKIlpRVLFEGWS--YQDLQSLLNDEQEREKLIKLLVTTAKKNHFDGIVLEvWS 118

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195 151 YPGATdrggNYGDKDKFLY-FVEELRRAFDREGRgwEITMAVP--VAKFRLNEGY---HVPELCEALDAIHAMTYDLRGn 224
Cdd:cd02876 119 QLAAY----GVPDKRKELIqLVIHLGETLHSANL--KLILVIPppREKGNQNGLFtrkDFEKLAPHVDGFSLMTYDYSS- 191

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195 225 wAGFADVHSPLYKrkhdqyayeklnVNDGLALWEEMGCP-ANKLVVGVPFYGRTFTLSNS 283
Cdd:cd02876 192 -PQRPGPNAPLSW------------VRSCLELLLPESGKkRAKILLGLNFYGNDYTLPGG 238
GH18_CTS3_chitinase cd06546
GH18 domain of CTS3 (chitinase 3), an uncharacterized protein from the human fungal pathogen ...
 28-203 3.39e-05

GH18 domain of CTS3 (chitinase 3), an uncharacterized protein from the human fungal pathogen Coccidioides posadasii. CTS3 has a chitinase-like glycosyl hydrolase family 18 (GH18) domain; and has homologs in bacteria as well as fungi.


Pssm-ID: 119363  Cd Length: 256  Bit Score: 45.79  E-value: 3.39e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195  28 RIVCYFSNWAVYRTGIGRYGLEDVPADL-CTHIIYSFIGVNDkswDVLVIdpeLDVDQGGFSKFTQL-------KKSNpn 99
Cdd:cd06546   1 RLVIYYQTTHPSNGDPISSLLLVTEKGIaLTHLIVAALHIND---DGNIH---LNDHPPDHPRFTTLwtelailQSSG-- 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195 100 VKLEIAVGGWAEGgsKYSQMVAVRDRRQSFIRSVVRFMKQYNFDGFDLDWEYPGAtdrggnygdKDKFLYFVEELRRAFd 179
Cdd:cd06546  73 VKVMGMLGGAAPG--SFSRLDDDDEDFERYYGQLRDMIRRRGLDGLDLDVEEPMS---------LDGIIRLIDRLRSDF- 140

                       170       180
                ....*....|....*....|....
gi 21358195 180 reGRGWEITMAvPVAKFRLNEGYH 203
Cdd:cd06546 141 --GPDFIITLA-PVASALTGGEAN 161
Chi1 COG3469
Chitinase [Carbohydrate transport and metabolism];
104-190 4.17e-05

Chitinase [Carbohydrate transport and metabolism];


Pssm-ID: 442692 [Multi-domain]  Cd Length: 534  Bit Score: 46.28  E-value: 4.17e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195 104 IAVGGwAEGGskysqmVAVRDR--RQSFIRSVVRFMKQYNFDGFDLDWEyPGATDRGGNYGDKDKFLYFVEELRRAFDRE 181
Cdd:COG3469 293 LSIGG-ANGT------VQLNTAaaADNFVNSVIALIDEYGFDGLDIDLE-GGSNSLNAGDTDTPVITNLISALKQLKAKY 364


                ....*....
gi 21358195 182 GRGWEITMA 190
Cdd:COG3469 365 GPGFVLTMA 373
GH18_chitinase_D-like cd02871
GH18 domain of Chitinase D (ChiD). ChiD, a chitinase found in Bacillus circulans, hydrolyzes ...
 29-333 2.49e-04

GH18 domain of Chitinase D (ChiD). ChiD, a chitinase found in Bacillus circulans, hydrolyzes the 1,4-beta-linkages of N-acetylglucosamine in chitin and chitodextrins. The domain architecture of ChiD includes a catalytic glycosyl hydrolase family 18 (GH18) domain, a chitin-binding domain, and a fibronectin type III domain. The chitin-binding and fibronectin type III domains are located either N-terminal or C-terminal to the catalytic domain. This family includes exochitinase Chi36 from Bacillus cereus.


Pssm-ID: 119350 [Multi-domain]  Cd Length: 312  Bit Score: 43.48  E-value: 2.49e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195  29 IVCYFSNWAVYrTGIGRYGLEDVPadlcthiiysfigvndKSWDVLVID-PELDVDQGGFSKFTQLKKSNPNVKLE---- 103
Cdd:cd02871   3 LVGYWHNWDNG-AGSGRQDLDDVP----------------SKYNVINVAfAEPTSDGGGEVTFNNGSSPGGYSPAEfkad 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195 104 ------------IAVGGwAEGGSkysqMVAVRDRRQSFIRSVVRFMKQYNFDGFDLDWEYpGATdrggNYGDKDKFLYFV 171
Cdd:cd02871  66 ikalqakgkkvlISIGG-ANGHV----DLNHTAQEDNFVDSIVAIIKEYGFDGLDIDLES-GSN----PLNATPVITNLI 135

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195 172 EELRRAFDREGRGWEITMA-------VPVAKFRLNEGYHVP---ELCEALDAIH--------AMTYDLRGNWAGFADVHS 233
Cdd:cd02871 136 SALKQLKDHYGPNFILTMApetpyvqGGYAAYGGIWGAYLPlidNLRDDLTWLNvqyynsggMGGCDGQSYSQGTADFLV 215

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195 234 PLYKRKHDQYAYEKLNVNDGLalweemgcPANKLVVGVPfygrtftlsnSNKNYNMGTYINKEA---------GGGAPGP 304
Cdd:cd02871 216 ALADMLLTGFPIAGNDRFPPL--------PADKVVIGLP----------ASPSAAGGGYVSPSEvikaldclmKGTNCGS 277

                       330       340
                ....*....|....*....|....*....
gi 21358195 305 YTNASGFLAYYEICTevmdkskgWTVEWD 333
Cdd:cd02871 278 YYPAGGYPSLRGLMT--------WSINWD 298
GH18_trifunctional cd06549
GH18 domain of an uncharacterized family of bacterial proteins, which share a common ...
 126-220 1.14e-03

GH18 domain of an uncharacterized family of bacterial proteins, which share a common three-domain architecture: an N-terminal glycosyl hydrolase family 18 (GH18) domain, a glycosyl transferase family 2 domain, and a C-terminal polysaccharide deacetylase domain.


Pssm-ID: 119366 [Multi-domain]  Cd Length: 298  Bit Score: 41.24  E-value: 1.14e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195 126 RQSFIRSVVRFMKQYNFDGFDLDWEYPGATdrggnygDKDKFLYFVEELRRAFdrEGRGWEITMAVPVAkfrlNEGYHVP 205
Cdd:cd06549  89 RAKFIANIAAYLERNQADGIVLDFEELPAD-------DLPKYVAFLSELRRRL--PAQGKQLTVTVPAD----EADWNLK 155

                        90
                ....*....|....*
gi 21358195 206 ELCEALDAIHAMTYD 220
Cdd:cd06549 156 ALARNADKLILMAYD 170
GH18_narbonin cd06544
Narbonin is a plant 2S protein from the globulin fraction of narbon bean (Vicia narbonensis L.) ...
 48-150 2.24e-03

Narbonin is a plant 2S protein from the globulin fraction of narbon bean (Vicia narbonensis L.) cotyledons with unknown function. Narbonin has a glycosyl hydrolase family 18 (GH18) domain without the conserved catalytic residues and with no known enzymatic activity. Narbonin amounts to up to 3% of the total seed globulins of mature seeds and was thought to be a storage protein but was found to degrade too slowly during germination. This family also includes the VfNOD32 nodulin from Vicia faba.


Pssm-ID: 119361  Cd Length: 253  Bit Score: 40.05  E-value: 2.24e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195  48 LEDVP--ADLCTHIIYSFI-----------GVNDKSWDVLVIDPEldvdqggfsKFTQLKKSNPNVKLEIAVGGWAEG-- 112
Cdd:cd06544  15 FSDVPinPKVEFHFILSFAidydtesnptnGKFNPYWDTENLTPE---------AVKSIKAQHPNVKVVISIGGRGVQnn 85

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 21358195 113 ---GSKYSQMVAVRDRRQSfIRSVVrfmKQYNFDGFDLDWE 150
Cdd:cd06544  86 ptpFDPSNVDSWVSNAVSS-LTSII---QTYNLDGIDIDYE 122
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 400-546 9.37e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 38.90  E-value: 9.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195  400 KNYRVPE-PTRQTTP-RPEWAKPPATPPNPDEGAV----VAPTTSTTKRPKPKPKPTSSPLSPTSAPGPV-PT------- 465
Cdd:PTZ00449 598 KRPRSAQrPTRPKSPkLPELLDIPKSPKRPESPKSpkrpPPPQRPSSPERPEGPKIIKSPKPPKSPKPPFdPKfkekfyd 677

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358195  466 --VGSSTPKPTTKKPKKPKKTTTTTTTTPAPEkSTEEPEEVVYPVDPVEPTDPEQPMGPQFDPNEIDCTNRDFVPHPNCR 543
Cdd:PTZ00449 678 dyLDAAAKSKETKTTVVLDESFESILKETLPE-TPGTPFTTPRPLPPKLPRDEEFPFEPIGDPDAEQPDDIEFFTPPEEE 756


                 ...
gi 21358195  544 KYF 546
Cdd:PTZ00449 757 RTF 759
 
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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