| Basic Information | |
|---|---|
| Species | Chlamydomonas reinhardtii |
| Cazyme ID | g5228.t2 |
| Family | GH18 |
| Protein Properties | Length: 2500 Molecular Weight: 557008 Isoelectric Point: 5.2303 |
| Chromosome | Chromosome/Scaffold: 5 Start: 1230113 End: 1267568 |
| Description | Glycosyl hydrolase family protein with chitinase insertion domain |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH18 | 803 | 1134 | 1e-34 |
| RLVAYFTNRRPDKSPACVASVADVVATPLQRATAATHLIFAHVRPNAETLGIDLINDRDGPVLANLDGNLLAVNPDIKVLVSVGGPGGNDAEFTRLVLNQ QSVTGFANATLAFLNTYNLDGLELSWPSLQAEQVFGFTALVELLSSSLRPAGKLLSLAVPPREVYLSLAWGRLGSLVDMINFQGFDLEGDEVLGAAPYVE TPLFDCLEAEGLSVNTLIDLILAAGAPPQLVNVVASSMGRSFVLDGDGYVGGPGSPGPCMGLEGLLDQSEIKLLLPPGAAKLDPEALANTGPYASNQFAH WEDGYTIVNKFCFARAHCLGGVGVWDVDGDSY | |||
| Full Sequence |
|---|
| 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 VQLSCRLSAF MPIVAVASGA RTFTQLSPWL DLAGSPFYID TSNTTTRAYI 540 VTDVTDDRAA DLVFFDQPSL RLGLMPSNRV NKLLDDTDGD GTTWFELSTV SGRCASLGED 600 CFLLTTDYNR DGLNDVAVVY LDRVTDTEEF YLTMVATSPP APLTWHLSAA AIFPRGACTS 660 PMAVALGQFV GADGSMDGTI SGTVNPQLVC LSSYDQRIYI GGLGVWGSLP GPVTSLHVRD 720 VDVDGRDDLL IFTEVGSFYL ISTGAAFEPA LSTAAFLSPA SVSLAVPNTP SLGQTDQTAS 780 TAVASADVVA AAPVEHRCGP PRRLVAYFTN RRPDKSPACV ASVADVVATP LQRATAATHL 840 IFAHVRPNAE TLGIDLINDR DGPVLANLDG NLLAVNPDIK VLVSVGGPGG NDAEFTRLVL 900 NQQSVTGFAN ATLAFLNTYN LDGLELSWPS LQAEQVFGFT ALVELLSSSL RPAGKLLSLA 960 VPPREVYLSL AWGRLGSLVD MINFQGFDLE GDEVLGAAPY VETPLFDCLE AEGLSVNTLI 1020 DLILAAGAPP QLVNVVASSM GRSFVLDGDG YVGGPGSPGP CMGLEGLLDQ SEIKLLLPPG 1080 AAKLDPEALA NTGPYASNQF AHWEDGYTIV NKFCFARAHC LGGVGVWDVD GDSYGELLAA 1140 VTRTMQGDPA VCEAYSPPEC TNAVSTRGSE DLGSPELVAT LGDAEYLLYQ VRKTWTDARD 1200 HCQQIGGDLV SVTSRGEAGV VYSLISSWAS SGQLGQDDIY SGRDVYLWLG GTDAAQEGRF 1260 VWAATGAELT YTAWAGGQPD SRYGSEDCLA ASVRLGGSGG AGLREVLSPE ALWNDLGCSA 1320 VLPFVCQRNR DLARSFLQGA KEVPWLTATY HVMAPVPGSG DPGLMLTQPE ANKLCRTMGG 1380 ELPTLTDPWV REDLTSQYHR DLPSHTWLGL RSYGDGQLFW NDGTFTTDGM LNAWEPGEFG 1440 DAACGLIIGP NGANVTVSVG ALYSFWNATA FQGAIRVASP PPPPPSPPSP APPGPTPPRP 1500 PPRPANVTPP APPPSIPSAP FPPDFDTVLI YNLSTYFTDE PELVTVFLPQ GVYSLSCNER 1560 MPTTCQTGAP TVSLNPNFYC LSRANGRSYV VPGKELTGMP LYLTTERSCA SACMLNIRCV 1620 YYTWLPRFRA SFLPSDEMLG RPNQLPGQGS CYLMGRPWAS NADRLPKLLS EITDNDRVCF 1680 RSGAVFGGDS IPVNDTSLIQ PPASIGRLHG NPTPTTPTPA APPPSAPFSL LCGGDGSAAP 1740 LLSSLTFLVD NATRGIQDVG TTCAGTYTAG VIGYLSAEGY EMRLRQLQRP IIQSYTARCG 1800 PGGVTGLLGS YDNRGMCQVS LMCTGGGVEP VLPPGASRNC SIGASAFDFE CPRGHYAVGL 1860 QGVFLNPATY TAADNILATL RMVCAAVPVA QVAPPPPSPP NPPPPPPPAQ RRRRAALESS 1920 AAWRRSAAAA MASAGRSSKD GQSAASGSFF EEALSNQQGR RLQQILPPSP SPPSPKPPSP 1980 SPPLPPKPPL PPSPPKPPSP SPPSPSPPSP KPPSPKPPSP SPPSPKPPNP PLPPSPGPKP 2040 PSPPLPPSPP APPPAPPRPP RPPPAPKPPR PPAPRPPSPQ PTPPIMSPPP PPSPPPAPRP 2100 PPAPTPTAPG VPNPPTPPPR PPSPPSPPPK PPTPSPPPAP PPRPPSPPPP PPSPPPPPSP 2160 SPPPPPPPSN ATSDVIPCRT CSPIFGETAG SNSPFANTSR PGALRCPQGH LLTQLFQPVV 2220 INQLLAQQVC CTNFSQPITG LGGVCGPLAP SAPGADDTMR AGLPATPSQP LSATTPFLTT 2280 VVNGSTCSGG IAQVTGLFLS FRPPSPGVGT PSYIMGLTAR CRNVATPLPL PAPASIFQRP 2340 FSYTCPPGTV LSEVLWNMQD WPAQPGTARS QPVGVIANIV FKCSNAAFPT PATPMPSPVP 2400 FTQVESSNMA LVSINCPAGS YVTSVYGSYD LSPANMGGVA FVRQVGITCS GATTITREIT 2460 TSLGATASAT PFTSAVCPGG VGALTARALP APGAPTTSPP 2520 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd00037 | CLECT | 7.0e-12 | 3155 | 3290 | 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 | 4974 | 5114 | 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 | 1186 | 1328 | 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 | 803 | 1121 | 334 | + Glycosyl hydrolases family 18. | ||
| cd00598 | GH18_chitinase-like | 6.0e-23 | 838 | 1000 | 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 | 1884 | 566 | 2362 | hypothetical protein CHLREDRAFT_187642 [Chlamydomonas reinhardtii] |
| RefSeq | XP_001698335.1 | 0 | 2188 | 3329 | 2454 | 3593 | hypothetical protein CHLREDRAFT_187642 [Chlamydomonas reinhardtii] |
| RefSeq | XP_001698335.1 | 0 | 3336 | 3553 | 3681 | 3911 | hypothetical protein CHLREDRAFT_187642 [Chlamydomonas reinhardtii] |
| RefSeq | XP_001698335.1 | 0 | 3649 | 5226 | 3934 | 5425 | hypothetical protein CHLREDRAFT_187642 [Chlamydomonas reinhardtii] |
| RefSeq | XP_001698335.1 | 0.000003 | 4122 | 4325 | 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 | 803 | 1134 | 2 | 344 | A Chain A, Crystal Structure Of Mutation Of An Acylptide HydrolaseESTERASE FROM AEROPYRUM PERNIX K1 |
| PDB | 1waw_A | 4e-21 | 803 | 1134 | 2 | 344 | A Chain A, Specificity And Affinity Of Natural Product Cyclopentapeptide Inhibitor Argadin Against Human Chitinase |
| PDB | 1hkm_A | 2e-20 | 803 | 1134 | 2 | 344 | A Chain A, Specificity And Affinity Of Natural Product Cyclopentapeptide Inhibitor Argadin Against Human Chitinase |
| PDB | 1hkj_A | 2e-20 | 803 | 1134 | 2 | 344 | A Chain A, Specificity And Affinity Of Natural Product Cyclopentapeptide Inhibitor Argadin Against Human Chitinase |
| PDB | 1hki_A | 2e-20 | 803 | 1134 | 2 | 344 | A Chain A, Crystal Structure Of Human Chitinase In Complex With Glucoallosamidin B |
| Signal Peptide | |||||
|---|---|---|---|---|---|
| Cleavage Site | |||||
| 27 | |||||
| Hydropathy |
|---|
 |
| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| BU653090 | 61 | 4699 | 4759 | 2e-31 |
| BI999053 | 60 | 426 | 485 | 2e-28 |
| BU653089 | 55 | 4345 | 4399 | 1e-26 |
| BU653089 | 47 | 4298 | 4344 | 5e-16 |
| BI999053 | 31 | 396 | 426 | 0.00000003 |
| Orthologous Group | |||||
|---|---|---|---|---|---|
| Species | ID | ||||
| Chlamydomonas reinhardtii | Cre01.g002800.t1.3 | g5228.t1 | 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.) |
|---|
 |
| Phylogeny |
|---|
 |