| Basic Information | |
|---|---|
| Species | Chlamydomonas reinhardtii |
| Cazyme ID | Cre10.g451600.t3.1 |
| Family | GH18 |
| Protein Properties | Length: 2500 Molecular Weight: 821331 Isoelectric Point: 5.1371 |
| Chromosome | Chromosome/Scaffold: 10 Start: 4408462 End: 4470573 |
| 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 | 332 | 662 | 5.5e-34 |
| RVVAYYTNRRPDKSPACLASVADVETTALQRAAAATHVIFAHVKPNAETISVDLANERDGPVLANLDGNLFNVNPDIRVLVSVGGPGGLDSDYSRLVLNE QSVVGFANATVTFLNAYNLDGAELSWPNLQSEQVEGYTALLEILSATLRPAGKLLSLAVPPREVYVSMDWGRLGLLVDMINFQGFDLEGDEVLGASPYVE TPLFDCQEAEGLSVNSLVDLILAAGAPPQLLTVVASSMGRSFVLDGDGFVGGPGSPGPCMGVEGLLDQSEIKLLLPPGAARHDPEAFANVGPFAANQYAH WEDAYSIVNKVCFARSHCLGGVGLWDVDGDS | |||
| Full Sequence |
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| Protein Sequence Length: 2500 Download |
| MLFRDEVRQK QRAGRLVAVL GARARDLLRV CIVAIASGSR GFSPLTTWLD LTGSPFSIDV 60 TNTTTRSYVF TDVTGDRASD MVFFDQPTLR LAYMPSNRNN KLVDDTDGDG TTWFELSTVS 120 GRCASLGEDC FLITSDVNND KLNDIALVYL DRVTETEEFY LTLVTTSPPA PLNWYMTSAA 180 VFPRGACTSP QAVALGQFVG LDGSLDGTIA GTNQPQLLCL SSYDQRIYVG GLGVWGSLPG 240 PVTSLHVRDV DVDGRDDLLI FTEVGSYYLV STGASFGPAL PTAAWLSPSS VSLAVPLTLD 300 LGQTDQTASS VVASADVIGA APVEHRCGPP RRVVAYYTNR RPDKSPACLA SVADVETTAL 360 QRAAAATHVI FAHVKPNAET ISVDLANERD GPVLANLDGN LFNVNPDIRV LVSVGGPGGL 420 DSDYSRLVLN EQSVVGFANA TVTFLNAYNL DGAELSWPNL QSEQVEGYTA LLEILSATLR 480 PAGKLLSLAV PPREVYVSMD WGRLGLLVDM INFQGFDLEG DEVLGASPYV ETPLFDCQEA 540 EGLSVNSLVD LILAAGAPPQ LLTVVASSMG RSFVLDGDGF VGGPGSPGPC MGVEGLLDQS 600 EIKLLLPPGA ARHDPEAFAN VGPFAANQYA HWEDAYSIVN KVCFARSHCL GGVGLWDVDG 660 DSYGELLGAV GRAVLGDPAI CTEYSPPECT NTVSTRGSED LGSPELVATL GDSEFLLYQV 720 RKNWPDARDH CQQIGGDLVS VTSRGEAGVV YSLITAWASS GQLGPDDIYS GRDVYVWLGG 780 SDAAQEGRFV WAESGADFTF TSWAGGQPDG RFGGEDCVAT TVRLAGSSGA GLRQVISSEA 840 LWNDVGCTAA LPFVCQRDTA LARSLLRAAK EVPWLSATYH VLAPAEEGDP GLMLTQPEAN 900 KLCRSLGGEL PTLTDPWVRE DLTSQYHRDL PTHTWLGLRS YGDGQLFWND GTFTTDGMLN 960 AWEPGEFGDA ACGLIVGPSG ANVTVSAGTL YSFWNATTFQ GAIRVASPPP PPPRPPSPGP 1020 PGPKPPSPPP RPANLTPPAP PPGLPNAPPS PVYEDLTIYN LTDYFAPQVQ MYSVFLPQGV 1080 YSLSCNERMP TTCQTGMPAV SLTPNFYCLT RPNGRAYVVP GKELPSMPLY LSTERACAAA 1140 CMLNFRCVYY TWLPRFRASF LPTDEVLGRP NQLQDQGSCY LMGRPWMPNS DRLPKLLSEI 1200 TDSDRVCFRS GSIFSGDTLP ISDDTLIQPP AAVGPLFGNP AAVAANPAGT PPATPFSLLC 1260 GSDGAAAPLL SSLTFLVDNG TRGIQDVGAA CAGTVSAGVL GSVSAEGYEL RVRQLQRPVI 1320 QSYTARCGPG GVTGMLGSYD NRGMCQVSLT CASGAVEPVL PPTASRNCTA AASFFDYECP 1380 PGQLAIGLQG LFLNAATYTA SDNILAAIRM LCAAVPVAMV APSPPSPPLP PPSPPPAGRR 1440 RAALETASAA WRRAAAAATD AGSSSSSSSS SNTQAAATGA FFQELMQSRR VDLGINGGGS 1500 ARRRLQQTSP PSPSPPSPKP PSPSPPSPTP PSPKPPSPKP PSPSPPSPLP PAPPKPPLPP 1560 SPKPPSPSPP LPPRPPSPSP PSPKPPSPSP PSPKPPSPSP PSPKPPTLPV PPSPRSPPSP 1620 PAPPPAPPRP PRPPPAPKPP RPPAPKPPSP VPFPPRASPP FPPSPPPVPS PPNPPPSPAP 1680 QIPTPPSPPP RPPAPPSPPP IPPTPSPPPA PPPRPPSPPP PPPSPPPPPS PSPPPPPPPA 1740 NVTYADVILC RDCSPLFGEG PGAASPLVTT SRQGVLRCPQ RHIITQLQTP IVSAGALPLQ 1800 SGAVANQPLT GLGGVCAPLA SAPGAVDTVS AGLPAVPTLP PISGQPFNVS IVGGAACPTG 1860 IVQVTGLHLS FRIGPPANPS YVNNLAVRCR TVATPLPLPT APVGYPSHRP FSYTCPPSTV 1920 LSEIFWNTQE WPASSPGTVR NQPVPVITSL VFKCTPWTVP TPAAPIPPPS PFSQIEANSM 1980 TSLTLACPLG QFLTSVYGRF DSAPANMGGV AFVRSLSITC SGPTTVTREV STIMAPTAAT 2040 TPFTSAVCPG GIGALTARTL AVPGAPTTTP PALLSLDAHC YDTQLHTRKL SFLPPALSNA 2100 APQVADRISE LTDRCLGLTL VSGITVLRSM FSGGVLITSG VPTSSFLHGI KVSCFDVPEP 2160 NPPALAVSAQ LPPNQLPAAP AVTFKYECPA GSKVVSVLSR VDADDDLLNV RIECDNAPLG 2220 DAESLASIAA RLTPFFAPPQ IFVANCTNCT TAANVSSMGY GQRRYISPDI AISAPRTSYV 2280 IERTCPLGIA GIINTATSSR IVPELGGAAT PVSSAALPSS VVTGATIALF DVLLDWGNAV 2340 AFCMAQDGAL MTIEDELQRL AVGSVVQEWA AENTGDAVLG VWIGARRTGN GLYDFTYQDN 2400 TPMGGYVAPW APGEPNDLSG VEDCVELVVN VTSGLVSWND RVCTGLVRRP LCKLLPKATV 2460 EGANSADVAP PNVQISATNN DELSFYNVSL TWYEGLNFCQ 2520 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd00037 | CLECT | 2.0e-11 | 3858 | 3984 | 128 | + 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 | 1.0e-11 | 4538 | 4677 | 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-13 | 4202 | 4330 | 131 | + 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 | 713 | 857 | 145 | + 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 | 5.0e-23 | 332 | 648 | 334 | + 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_001698335.1 | 0 | 33 | 1412 | 1002 | 2362 | hypothetical protein CHLREDRAFT_187642 [Chlamydomonas reinhardtii] |
| RefSeq | XP_001698335.1 | 0 | 1769 | 2909 | 2458 | 3598 | hypothetical protein CHLREDRAFT_187642 [Chlamydomonas reinhardtii] |
| RefSeq | XP_001698335.1 | 0 | 2909 | 3138 | 3680 | 3909 | hypothetical protein CHLREDRAFT_187642 [Chlamydomonas reinhardtii] |
| RefSeq | XP_001698335.1 | 0 | 3234 | 7504 | 3934 | 8106 | hypothetical protein CHLREDRAFT_187642 [Chlamydomonas reinhardtii] |
| RefSeq | XP_001698335.1 | 0 | 3795 | 7652 | 4439 | 8188 | 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 | 2e-20 | 367 | 672 | 31 | 353 | A Chain A, Glucoamylase, Granular Starch-Binding Domain Complex With Cyclodextrin, Nmr, Minimized Average Structure |
| PDB | 1waw_A | 2e-20 | 367 | 672 | 31 | 353 | A Chain A, Specificity And Affinity Of Natural Product Cyclopentapeptide Inhibitor Argadin Against Human Chitinase |
| PDB | 1hkm_A | 6e-20 | 367 | 672 | 31 | 353 | A Chain A, Specificity And Affinity Of Natural Product Cyclopentapeptide Inhibitor Argadin Against Human Chitinase |
| PDB | 1hkj_A | 6e-20 | 367 | 672 | 31 | 353 | A Chain A, Specificity And Affinity Of Natural Product Cyclopentapeptide Inhibitor Argadin Against Human Chitinase |
| PDB | 1hki_A | 6e-20 | 367 | 672 | 31 | 353 | A Chain A, Crystal Structure Of Human Chitinase In Complex With Glucoallosamidin B |
| Transmembrane Domains | |||||
|---|---|---|---|---|---|
| Start | End | ||||
| 7573 | 7595 | ||||
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| AV396964 | 105 | 6882 | 6986 | 0 |
| AV645111 | 152 | 7077 | 7224 | 9.94922e-44 |
| BU653090 | 96 | 4237 | 4332 | 2e-24 |
| GR283226 | 133 | 1076 | 1204 | 9e-24 |
| GR283225 | 133 | 1076 | 1204 | 1e-23 |
| Orthologous Group | |||||
|---|---|---|---|---|---|
| Species | ID | ||||
| Chlamydomonas reinhardtii | Cre01.g002800.t1.3 | g5228.t2 | g5228.t1 | 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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