| Basic Information | |
|---|---|
| Species | Chlamydomonas reinhardtii |
| Cazyme ID | g5228.t1 |
| Family | GH18 |
| Protein Properties | Length: 2500 Molecular Weight: 555789 Isoelectric Point: 5.2122 |
| Chromosome | Chromosome/Scaffold: 5 Start: 1230113 End: 1267568 |
| Description | Glycosyl hydrolase family protein with chitinase insertion domain |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH18 | 792 | 1123 | 1e-34 |
| RLVAYFTNRRPDKSPACVASVADVVATPLQRATAATHLIFAHVRPNAETLGIDLINDRDGPVLANLDGNLLAVNPDIKVLVSVGGPGGNDAEFTRLVLNQ QSVTGFANATLAFLNTYNLDGLELSWPSLQAEQVFGFTALVELLSSSLRPAGKLLSLAVPPREVYLSLAWGRLGSLVDMINFQGFDLEGDEVLGAAPYVE TPLFDCLEAEGLSVNTLIDLILAAGAPPQLVNVVASSMGRSFVLDGDGYVGGPGSPGPCMGLEGLLDQSEIKLLLPPGAAKLDPEALANTGPYASNQFAH WEDGYTIVNKFCFARAHCLGGVGVWDVDGDSY | |||
| Full Sequence |
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| Protein Sequence Length: 2500 Download |
| MAASREVGAW RAFLAFGLLL VAIKSNAQTW FDDRDAAVIC KTLGLPTSRA KAVFKAWNVY 60 TRGGPWENGK PASAEEIVAY LNSVDPPIAM TNLRCRGDEA SITACERDVT NLGTCTRAQS 120 VGVQCFENDY AVRLVNSGSN PYLGNSLRGG WVQVWMGSGW SYVSAASFDV RDAYVVCKQL 180 KMPFGGARVF RGVVEGTALF GPANLTSSTR TLLPGLQCTG SEASLGECPI DPAAVDAAND 240 PTAPPQGGAS MLCEDAEFDV RLRGGTHVSE GRVEVYSKYG VWQTVCWSTF DASALDVVCR 300 QLGFQTTPLN PPSYLNFSSS GIPDARPAAG ISSIMNCPPG ANAISQCGNL TSYAAINSYT 360 SFPLGCTAAL DVVIKCYQRN PLYTQVEYRS ICTDPWSTQA GLSPEAGVTA MLVGEFDDQS 420 QGERSQDVLL LKYGSDGKLI GHAAFGRPWA STFSAEADID FGSTPKPEVL LLADMTGDGR 480 DDLVVMTSSQ VQVAVASGAR TFTQLSPWLD LAGSPFYIDT SNTTTRAYIV TDVTDDRAAD 540 LVFFDQPSLR LGLMPSNRVN KLLDDTDGDG TTWFELSTVS GRCASLGEDC FLLTTDYNRD 600 GLNDVAVVYL DRVTDTEEFY LTMVATSPPA PLTWHLSAAA IFPRGACTSP MAVALGQFVG 660 ADGSMDGTIS GTVNPQLVCL SSYDQRIYIG GLGVWGSLPG PVTSLHVRDV DVDGRDDLLI 720 FTEVGSFYLI STGAAFEPAL STAAFLSPAS VSLAVPNTPS LGQTDQTAST AVASADVVAA 780 APVEHRCGPP RRLVAYFTNR RPDKSPACVA SVADVVATPL QRATAATHLI FAHVRPNAET 840 LGIDLINDRD GPVLANLDGN LLAVNPDIKV LVSVGGPGGN DAEFTRLVLN QQSVTGFANA 900 TLAFLNTYNL DGLELSWPSL QAEQVFGFTA LVELLSSSLR PAGKLLSLAV PPREVYLSLA 960 WGRLGSLVDM INFQGFDLEG DEVLGAAPYV ETPLFDCLEA EGLSVNTLID LILAAGAPPQ 1020 LVNVVASSMG RSFVLDGDGY VGGPGSPGPC MGLEGLLDQS EIKLLLPPGA AKLDPEALAN 1080 TGPYASNQFA HWEDGYTIVN KFCFARAHCL GGVGVWDVDG DSYGELLAAV TRTMQGDPAV 1140 CEAYSPPECT NAVSTRGSED LGSPELVATL GDAEYLLYQV RKTWTDARDH CQQIGGDLVS 1200 VTSRGEAGVV YSLISSWASS GQLGQDDIYS GRDVYLWLGG TDAAQEGRFV WAATGAELTY 1260 TAWAGGQPDS RYGSEDCLAA SVRLGGSGGA GLREVLSPEA LWNDLGCSAV LPFVCQRNRD 1320 LARSFLQGAK EVPWLTATYH VMAPVPGSGD PGLMLTQPEA NKLCRTMGGE LPTLTDPWVR 1380 EDLTSQYHRD LPSHTWLGLR SYGDGQLFWN DGTFTTDGML NAWEPGEFGD AACGLIIGPN 1440 GANVTVSVGA LYSFWNATAF QGAIRVASPP PPPPSPPSPA PPGPTPPRPP PRPANVTPPA 1500 PPPSIPSAPF PPDFDTVLIY NLSTYFTDEP ELVTVFLPQG VYSLSCNERM PTTCQTGAPT 1560 VSLNPNFYCL SRANGRSYVV PGKELTGMPL YLTTERSCAS ACMLNIRCVY YTWLPRFRAS 1620 FLPSDEMLGR PNQLPGQGSC YLMGRPWASN ADRLPKLLSE ITDNDRVCFR SGAVFGGDSI 1680 PVNDTSLIQP PASIGRLHGN PTPTTPTPAA PPPSAPFSLL CGGDGSAAPL LSSLTFLVDN 1740 ATRGIQDVGT TCAGTYTAGV IGYLSAEGYE MRLRQLQRPI IQSYTARCGP GGVTGLLGSY 1800 DNRGMCQVSL MCTGGGVEPV LPPGASRNCS IGASAFDFEC PRGHYAVGLQ GVFLNPATYT 1860 AADNILATLR MVCAAVPVAQ VAPPPPSPPN PPPPPPPAQR RRRAALESSA AWRRSAAAAM 1920 ASAGRSSKDG QSAASGSFFE EALSNQQGRR LQQILPPSPS PPSPKPPSPS PPLPPKPPLP 1980 PSPPKPPSPS PPSPSPPSPK PPSPKPPSPS PPSPKPPNPP LPPSPGPKPP SPPLPPSPPA 2040 PPPAPPRPPR PPPAPKPPRP PAPRPPSPQP TPPIMSPPPP PSPPPAPRPP PAPTPTAPGV 2100 PNPPTPPPRP PSPPSPPPKP PTPSPPPAPP PRPPSPPPPP PSPPPPPSPS PPPPPPPSNA 2160 TSDVIPCRTC SPIFGETAGS NSPFANTSRP GALRCPQGHL LTQLFQPVVI NQLLAQQVCC 2220 TNFSQPITGL GGVCGPLAPS APGADDTMRA GLPATPSQPL SATTPFLTTV VNGSTCSGGI 2280 AQVTGLFLSF RPPSPGVGTP SYIMGLTARC RNVATPLPLP APASIFQRPF SYTCPPGTVL 2340 SEVLWNMQDW PAQPGTARSQ PVGVIANIVF KCSNAAFPTP ATPMPSPVPF TQVESSNMAL 2400 VSINCPAGSY VTSVYGSYDL SPANMGGVAF VRQVGITCSG ATTITREITT SLGATASATP 2460 FTSAVCPGGV GALTARALPA PGAPTTSPPA LLSLDAHCYD 2520 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd00037 | CLECT | 7.0e-12 | 3144 | 3279 | 138 | + C-type lectin (CTL)/C-type lectin-like (CTLD) domain. CLECT: C-type lectin (CTL)/C-type lectin-like (CTLD) domain; protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. This group is chiefly comprised of eukaryotic CTLDs, but contains some, as yet functionally uncharacterized, bacterial CTLDs. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces, including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. For example: mannose-binding lectin and lung surfactant proteins A and D bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, and apoptotic cells) and mediate functions associated with killing and phagocytosis; P (platlet)-, E (endothelial)-, and L (leukocyte)- selectins (sels) mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. Several CTLDs bind to protein ligands, and only some of these binding interactions are Ca2+-dependent; including the CTLDs of Coagulation Factors IX/X (IX/X) and Von Willebrand Factor (VWF) binding proteins, and natural killer cell receptors. C-type lectins, such as lithostathine, and some type II antifreeze glycoproteins function in a Ca2+-independent manner to bind inorganic surfaces. Many proteins in this group contain a single CTLD; these CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers, from which ligand-binding sites project in different orientations. Various vertebrate type 1 transmembrane proteins including macrophage mannose receptor, endo180, phospholipase A2 receptor, and dendritic and epithelial cell receptor (DEC205) have extracellular domains containing 8 or more CTLDs; these CTLDs remain in the parent model. In some members (IX/X and VWF binding proteins), a loop extends to the adjoining domain to form a loop-swapped dimer. A similar conformation is seen in the macrophage mannose receptor CRD4's putative non-sugar bound form of the domain in the acid environment of the endosome. Lineage specific expansions of CTLDs have occurred in several animal lineages including Drosophila melanogaster and Caenorhabditis elegans; these CTLDs also remain in the parent model. | ||
| cd00037 | CLECT | 5.0e-12 | 4963 | 5103 | 141 | + C-type lectin (CTL)/C-type lectin-like (CTLD) domain. CLECT: C-type lectin (CTL)/C-type lectin-like (CTLD) domain; protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. This group is chiefly comprised of eukaryotic CTLDs, but contains some, as yet functionally uncharacterized, bacterial CTLDs. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces, including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. For example: mannose-binding lectin and lung surfactant proteins A and D bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, and apoptotic cells) and mediate functions associated with killing and phagocytosis; P (platlet)-, E (endothelial)-, and L (leukocyte)- selectins (sels) mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. Several CTLDs bind to protein ligands, and only some of these binding interactions are Ca2+-dependent; including the CTLDs of Coagulation Factors IX/X (IX/X) and Von Willebrand Factor (VWF) binding proteins, and natural killer cell receptors. C-type lectins, such as lithostathine, and some type II antifreeze glycoproteins function in a Ca2+-independent manner to bind inorganic surfaces. Many proteins in this group contain a single CTLD; these CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers, from which ligand-binding sites project in different orientations. Various vertebrate type 1 transmembrane proteins including macrophage mannose receptor, endo180, phospholipase A2 receptor, and dendritic and epithelial cell receptor (DEC205) have extracellular domains containing 8 or more CTLDs; these CTLDs remain in the parent model. In some members (IX/X and VWF binding proteins), a loop extends to the adjoining domain to form a loop-swapped dimer. A similar conformation is seen in the macrophage mannose receptor CRD4's putative non-sugar bound form of the domain in the acid environment of the endosome. Lineage specific expansions of CTLDs have occurred in several animal lineages including Drosophila melanogaster and Caenorhabditis elegans; these CTLDs also remain in the parent model. | ||
| cd00037 | CLECT | 2.0e-22 | 1175 | 1317 | 143 | + C-type lectin (CTL)/C-type lectin-like (CTLD) domain. CLECT: C-type lectin (CTL)/C-type lectin-like (CTLD) domain; protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. This group is chiefly comprised of eukaryotic CTLDs, but contains some, as yet functionally uncharacterized, bacterial CTLDs. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces, including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. For example: mannose-binding lectin and lung surfactant proteins A and D bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, and apoptotic cells) and mediate functions associated with killing and phagocytosis; P (platlet)-, E (endothelial)-, and L (leukocyte)- selectins (sels) mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. Several CTLDs bind to protein ligands, and only some of these binding interactions are Ca2+-dependent; including the CTLDs of Coagulation Factors IX/X (IX/X) and Von Willebrand Factor (VWF) binding proteins, and natural killer cell receptors. C-type lectins, such as lithostathine, and some type II antifreeze glycoproteins function in a Ca2+-independent manner to bind inorganic surfaces. Many proteins in this group contain a single CTLD; these CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers, from which ligand-binding sites project in different orientations. Various vertebrate type 1 transmembrane proteins including macrophage mannose receptor, endo180, phospholipase A2 receptor, and dendritic and epithelial cell receptor (DEC205) have extracellular domains containing 8 or more CTLDs; these CTLDs remain in the parent model. In some members (IX/X and VWF binding proteins), a loop extends to the adjoining domain to form a loop-swapped dimer. A similar conformation is seen in the macrophage mannose receptor CRD4's putative non-sugar bound form of the domain in the acid environment of the endosome. Lineage specific expansions of CTLDs have occurred in several animal lineages including Drosophila melanogaster and Caenorhabditis elegans; these CTLDs also remain in the parent model. | ||
| pfam00704 | Glyco_hydro_18 | 7.0e-23 | 792 | 1110 | 334 | + Glycosyl hydrolases family 18. | ||
| cd00598 | GH18_chitinase-like | 6.0e-23 | 827 | 989 | 168 | + 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. | ||
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| RefSeq | XP_001698335.1 | 0 | 41 | 1873 | 566 | 2362 | hypothetical protein CHLREDRAFT_187642 [Chlamydomonas reinhardtii] |
| RefSeq | XP_001698335.1 | 0 | 2177 | 3318 | 2454 | 3593 | hypothetical protein CHLREDRAFT_187642 [Chlamydomonas reinhardtii] |
| RefSeq | XP_001698335.1 | 0 | 3325 | 3542 | 3681 | 3911 | hypothetical protein CHLREDRAFT_187642 [Chlamydomonas reinhardtii] |
| RefSeq | XP_001698335.1 | 0 | 3638 | 5215 | 3934 | 5425 | hypothetical protein CHLREDRAFT_187642 [Chlamydomonas reinhardtii] |
| RefSeq | XP_001698335.1 | 0.000003 | 4111 | 4314 | 3016 | 3214 | hypothetical protein CHLREDRAFT_187642 [Chlamydomonas reinhardtii] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1wb0_A | 4e-21 | 792 | 1123 | 2 | 344 | A Chain A, Crystal Structure Of Human Chitinase In Complex With Glucoallosamidin B |
| PDB | 1waw_A | 4e-21 | 792 | 1123 | 2 | 344 | A Chain A, Specificity And Affinity Of Natural Product Cyclopentapeptide Inhibitor Argadin Against Human Chitinase |
| PDB | 1hkm_A | 2e-20 | 792 | 1123 | 2 | 344 | A Chain A, Specificity And Affinity Of Natural Product Cyclopentapeptide Inhibitor Argadin Against Human Chitinase |
| PDB | 1hkj_A | 2e-20 | 792 | 1123 | 2 | 344 | A Chain A, Specificity And Affinity Of Natural Product Cyclopentapeptide Inhibitor Argadin Against Human Chitinase |
| PDB | 1hki_A | 2e-20 | 792 | 1123 | 2 | 344 | A Chain A, Crystal Structure Of Human Chitinase In Complex With Glucoallosamidin B |
| Signal Peptide | |||||
|---|---|---|---|---|---|
| Cleavage Site | |||||
| 27 | |||||
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| BU653090 | 61 | 4688 | 4748 | 2e-31 |
| BI999053 | 60 | 426 | 485 | 2e-28 |
| BU653089 | 55 | 4334 | 4388 | 1e-26 |
| BU653089 | 47 | 4287 | 4333 | 4e-16 |
| BI999053 | 31 | 396 | 426 | 0.00000003 |
| Orthologous Group | |||||
|---|---|---|---|---|---|
| Species | ID | ||||
| Chlamydomonas reinhardtii | Cre01.g002800.t1.3 | g5228.t2 | Cre10.g451600.t3.1 | Cre10.g451600.t2.1 | Cre10.g458350.t3.1 |
| Cre10.g458350.t2.1 | Cre10.g458350.t1.3 | ||||
| Sequence Alignments (This image is cropped. Click for full image.) |
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| Phylogeny |
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