| Basic Information | |
|---|---|
| Species | Chlamydomonas reinhardtii |
| Cazyme ID | Cre01.g002800.t1.3 |
| Family | GH18 |
| Protein Properties | Length: 2500 Molecular Weight: 453876 Isoelectric Point: 4.8166 |
| Chromosome | Chromosome/Scaffold: 1 Start: 473706 End: 504317 |
| 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 | 788 | 1123 | 1.4e-30 |
| RVIAYFSNRRPDRSAACTAAASADPSVSPSALTRAASSATHVIFSRLLPDADALDVALANDRDGPVLANLAGNLHSASPGTKVLVSVGGPGAGSDALSRL VLNAQSVGRFANASADYLQRQGLDGMELSWPELRAEQVPAFLSLVWALSHEVRARRGLLLGLAVPPRAVYLDLPWAGLGAGLDLINFHAFDLEGDEVLGA APYVETPLFSCLEATGLSVNTMVDTMLASGAPPQKVTLVASALGRSFVLDADGWVGGPGSAGPCLGSEGLLDQAELRLLVPPGGAQLDTEAFANTAPFAG NQWTHFDDPFTIANKVCFARYHCFGGIGLWDADADS | |||
| Full Sequence |
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| Protein Sequence Length: 2500 Download |
| MPVSAQYQLR LTDDYTPANA VKYEGRVEVV SPLGSICSFG EFDDKDAAVI CRQLGLPTAR 60 ARALYQAYKF MSGPWNDPQA SPPEVLSLVS AGAPPIVLTN LRCKGDETNI GSCLSDTSTL 120 ALSACSRGQA AGVQCFEEDY TVRLMTNSVN PANATAVAAL TEGRVEVWLG EGWGLVGATN 180 FGPDTARVVC AQLGLPVSGA TVVPNGAAAY GAPASNTAVV LDGLACSGKE ENIGFCSPPS 240 NTPPRGTAFA AVACRQADFS VRLSGGGHPS EGRLEVYNRG QWGTVCLGGF DRSALFTVCV 300 QAGWRTSDAR RPSFTAFNAS RLPADPRPGT GANALTSLRW CPDDAESITQ CGEYKYDAAA 360 TCPAGLDVVV RCYESPPLSL NVRPTSLCTD PWTTSATISP RPGRTTMLVG EFDGASGGAR 420 GQDVLLASYA NDGTLVGHVA YSRPWGSSFI AEADINLGPT PEPRALVLAD LNGDGLDDVV 480 AITSELVSVA TATSSRSFTP LTVWLDLSTT SDSIDTSNTT TRAYILTDVT GDAAADLVFF 540 DRPTLRLAFF PSNRISQLMD DTDGEGITWF ELSTISARCK SLGEDCFLLA ADVNGDSLND 600 AVLVYLDRVT ADQEVYMTFV AASPPAPLTW HMAAPAFFPR GACTSPWAVV MGQFVGPDGS 660 IDNVNAGSSV PQVACISSFD ARIYVAGLGS WGVVPGPPTR VHARDVDLDG RDDLVLFTEA 720 GSYYLLSTGS AFEPPVSTAR FGDGYTASVP TSGDRSLGET DQTASTIIAS SQPVGDAPVE 780 QRCGAPDRVI AYFSNRRPDR SAACTAAASA DPSVSPSALT RAASSATHVI FSRLLPDADA 840 LDVALANDRD GPVLANLAGN LHSASPGTKV LVSVGGPGAG SDALSRLVLN AQSVGRFANA 900 SADYLQRQGL DGMELSWPEL RAEQVPAFLS LVWALSHEVR ARRGLLLGLA VPPRAVYLDL 960 PWAGLGAGLD LINFHAFDLE GDEVLGAAPY VETPLFSCLE ATGLSVNTMV DTMLASGAPP 1020 QKVTLVASAL GRSFVLDADG WVGGPGSAGP CLGSEGLLDQ AELRLLVPPG GAQLDTEAFA 1080 NTAPFAGNQW THFDDPFTIA NKVCFARYHC FGGIGLWDAD ADSFGALLGA AASTVNGDPA 1140 LCSEYETPEC TNTVSSYGTT DLGQPELVGS VGDAEYSLFQ VRKSWSDARS HCKALGGDLA 1200 AVTSRSEAGV LYSLLSNWAG SGQLGEADVY SGRDVFVWLG GSDAVQEGRF RWVNTSADLT 1260 YTAWASGQPD GRYGGEDCMA AAIRLGGSSG GGLRIVVSQE AQWYDMGCTA ALPFVCQRSR 1320 AGGMGVAGVK LVPYLTTSLL VFPPLNRGEP GLQLTMAQGQ KLCRTYGAEL PSLTDYWTRS 1380 DMTSPTGWSL DLPPYMWLGL RSYGEGQLFW SDGSFSTDGV LNAWEPGEFG DAACAIIVGP 1440 QGVELELEVD SLYSRWNATA TGGAVRISPP PPPPPNPSPP PPPPQPPPRP SNSTPSPPSP 1500 PNPAPNSSPP PSPPGTPPDP RQRLQLSQGV YSLSCQERMP VVCQKSSPPV SLSPTFHCLT 1560 RPNGLAFMVP GETLAPGGNA LTPVASELEC AVGCMIAPRC VYYIYLPGWR PAGWVPPNNQ 1620 PPEDFAPNTC YLMGRPWVTS WAPKKLSEVV TAADRVCFRS NSIFSGDTAP MSDPLVLDPP 1680 TAAGPLFGYP APSPTATALP FSLLCSPTAG APVLASVSLT VANTSRNTQD VGVGCTGADG 1740 GGAEQRLWLY RPAAGGVYEA EADCGLSGVQ GVSGAFDAAG LCWLQLQCGS GAVLPVLAPA 1800 DARPGCPMPQ AAGSGGGGNF QYTCPPGMVG TGLQGSALSA PSPATNSIAT LRLMCGARPP 1860 ALTPPPPSQP PPAPAPSPLA VGRRRLLHSV AAPVSVVKDP FLAIAESGAR RHLNQFSVCT 1920 TSALAGRRYT TGGFSFNPSQ PGGTSVAATT ASACCSACAA QATRMYGYTL ISTYINPMSP 1980 TLYEVACYCY SNVPSGGTVD AATTATADVV SGSLTYRCSG GVVQWPAPPP PRPPPPPLPP 2040 KPPLPPPRPP PSPAPLPPRP PLPPSPPSPR PSPPSPPPPS PPRPPSPPPS PPPPSPAPRP 2100 PPAPKPPKPP GPRPPSPPSP SPPSPSPPSP QPPPSPPAPS PGVPPPSPKP PGPLPPSPRP 2160 RPPSPPSPPP RPAPPPSPPP APPPPPAPPP PSPPPPQPPS PPPPPPPPGP ITSDAPACSD 2220 CSPWFGDSTS DSPFYSSGTV QQQQQQRGAA TCPPGFGVSS LTAWFPPASQ YGTQPNASQP 2280 YSSLSAACTP LLPTPAGQDH TVRVGGGWLP PSNVTFSQTA LNATACDTLG GIASVVGAFT 2340 HFTPQRPGFI TAMSTRCRLT ATPLAQPALG SPFVGWNFTC PAGLVVVEVL WAQQTLTRPG 2400 LGPLPLITRV AFRCGLSAGL LPSPPVPYVS GFTATESSGL EPLSLLCPPG EYVTQVFGRY 2460 DVPTALSGVA LFIRDLGLVC SGGAAVTKDL DTGIATVNSS 2520 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd00037 | CLECT | 5.0e-8 | 3046 | 3182 | 142 | + 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 | 6.0e-9 | 3556 | 3694 | 139 | + 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 | 3.0e-13 | 3199 | 3343 | 147 | + 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-24 | 1176 | 1318 | 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 | 1.0e-24 | 862 | 1122 | 268 | + Glycosyl hydrolases family 18. | ||
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| RefSeq | XP_001700347.1 | 0 | 1 | 1465 | 22 | 1477 | predicted protein [Chlamydomonas reinhardtii] |
| RefSeq | XP_001700347.1 | 0 | 1526 | 1858 | 1477 | 1810 | predicted protein [Chlamydomonas reinhardtii] |
| RefSeq | XP_001700347.1 | 3e-23 | 1957 | 2025 | 1806 | 1874 | predicted protein [Chlamydomonas reinhardtii] |
| RefSeq | XP_001700347.1 | 0 | 2214 | 4058 | 1911 | 3684 | predicted protein [Chlamydomonas reinhardtii] |
| RefSeq | XP_001700347.1 | 0 | 4195 | 4346 | 3684 | 3843 | predicted protein [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-22 | 788 | 1127 | 2 | 347 | A Chain A, Crystal Structure Of A Family Gt4 Glycosyltransferase From Bacillus Anthracis Orf Ba1558. |
| PDB | 1waw_A | 4e-22 | 788 | 1127 | 2 | 347 | A Chain A, Specificity And Affinity Of Natural Product Cyclopentapeptide Inhibitor Argadin Against Human Chitinase |
| PDB | 1hkm_A | 5e-21 | 788 | 1127 | 2 | 347 | A Chain A, Specificity And Affinity Of Natural Product Cyclopentapeptide Inhibitor Argadin Against Human Chitinase |
| PDB | 1hkj_A | 5e-21 | 788 | 1127 | 2 | 347 | A Chain A, Specificity And Affinity Of Natural Product Cyclopentapeptide Inhibitor Argadin Against Human Chitinase |
| PDB | 1hki_A | 5e-21 | 788 | 1127 | 2 | 347 | A Chain A, Crystal Structure Of Human Chitinase In Complex With Glucoallosamidin B |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| GR283228 | 133 | 1521 | 1653 | 0 |
| GR283226 | 133 | 1521 | 1653 | 0 |
| GR283225 | 133 | 1521 | 1653 | 0 |
| GR283236 | 130 | 1521 | 1650 | 0 |
| GR283233 | 124 | 1521 | 1644 | 0 |
| Orthologous Group | |||||
|---|---|---|---|---|---|
| Species | ID | ||||
| Chlamydomonas reinhardtii | g5228.t2 | 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.) |
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| Phylogeny |
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