| Basic Information | |
|---|---|
| Species | Chlamydomonas reinhardtii |
| Cazyme ID | Cre10.g437950.t1.2 |
| Family | GH38 |
| Protein Properties | Length: 1369 Molecular Weight: 145687 Isoelectric Point: 6.1706 |
| Chromosome | Chromosome/Scaffold: 10 Start: 2684806 End: 2695221 |
| Description | |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH38 | 280 | 540 | 0 |
| QVHAVGHCHIDTAWLWPFSETHRKTARSWSSQLRLAERYPWHVFTASSAQQYEWLLQDYPGLFTEIQAAAARGSFVPVGGTWVEMDTNVPSGESLVRQFL FGQRFFQRHFGAPCDVFWLPDTFGYSGQLPQIAAGAGIRYFLTQKLSWNNINAFPHTTFYWAGLDGASRLLTHFPPANTYNAQADAKDLLATATGSKDKD RAPLAYMLFGNGDGGGGPTVDMCESLARLGGCRGVAGSFDVTAPGDFFRRLEGASQDLLTW | |||
| Full Sequence |
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| Protein Sequence Length: 1369 Download |
| MRPASGGSGA AGPAAPAAGA APAVSDVPGR WVPQHHRDIT LGRLDGFLAA GQFADVNLRA 60 AMWRRRSADA VSLEVYSHPK DVPYPPYDVA IKMPYRPAAV GEAFGPSWTT HWFRVRARTP 120 ADWEGEGPLM FRWDSGSEAM LYLDGPTPRQ GITDQRNEYL LAPAAVAGQE LVFYVEMAAN 180 GMFGNTTDGI LPPNEDRYFT LKAAELAVPD VEVTGLYHDL RALTGLAREL PAGHATGEAA 240 LYTANKIVNT YRRGDPQSVA ACRALAASVL AVRDPGDRMQ VHAVGHCHID TAWLWPFSET 300 HRKTARSWSS QLRLAERYPW HVFTASSAQQ YEWLLQDYPG LFTEIQAAAA RGSFVPVGGT 360 WVEMDTNVPS GESLVRQFLF GQRFFQRHFG APCDVFWLPD TFGYSGQLPQ IAAGAGIRYF 420 LTQKLSWNNI NAFPHTTFYW AGLDGASRLL THFPPANTYN AQADAKDLLA TATGSKDKDR 480 APLAYMLFGN GDGGGGPTVD MCESLARLGG CRGVAGSFDV TAPGDFFRRL EGASQDLLTW 540 RGELYFELHR GTYTTHAANK NDNRTCELLL REAEAAGALA EAMLGDVGGY CYPRAELESI 600 WKDVLLYQFH DVLPGSSIGR VYDVTKTRYP QMKMQLRKIR DAALGALIAA AAAPQSAAAA 660 AANSAAVAAA VGTGSHLISL EEVVGARPLL QPPAAAAAAA ADAAGAGEPV AWVFNSLAVP 720 RTELVSLPVA SLPPDLRQRL AEGAWRPAVL GQGPQEGAAA GAALEVPAAS GPGGAAQVVL 780 AVVEVPPLTL TPLTAADLAA GIKRRACSSS SSTATVNGGI SDSSNSSEGV GYDGGCRLVR 840 MTASQAGLRG RRAAAAAEAT SRRLGVAVAA EDAAVYLLMN KMVRAYFDDA GRLLSLYDPA 900 WRRELVPEGQ PGNVFRLYED IPLFWDAWDI EVYHLEKGCL AGEGQPPPSV HIIESTPSRV 960 RLGLSMQITA ASSLQQVVSL NCCSPRLEFH TEVVWAENRT ALKVEFPTTL DAPAAAYEVQ 1020 FGAVERPTHT NTSWDWARFE VCAHKWADLS EPGYGLALLN DCKYGHAVHG HVMRLTLLRS 1080 PKAPDANTDM GTHALRYGLL PHAGSWQQAG VAAHGWAFNA PLRLMQAPPQ QQLAAASAAA 1140 AVSALSLAQA APAAGAAAAG AVDFCHARPR LAFSPEQPMF QVVNAQQNPL QPASPHHPDA 1200 TSSGVWQPPL ILDTVKLAEP PLQHTSTAPA AAAAAAASVP VLSALCPDGL AAPATSASAE 1260 QLLMPEVGAK LKEGATEVVL RLYEPHGARG VARIEWPDWL PVAGGMLCDL LEQELGPEQR 1320 QAQGQRDGQE EEGLRVVLGL SQGGGAGGYV EVPFKPFQII SIKLILQV* 1380 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam07748 | Glyco_hydro_38C | 4.0e-74 | 874 | 1125 | 255 | + Glycosyl hydrolases family 38 C-terminal domain. Glycosyl hydrolases are key enzymes of carbohydrate metabolism. | ||
| pfam01074 | Glyco_hydro_38 | 2.0e-82 | 280 | 541 | 273 | + Glycosyl hydrolases family 38 N-terminal domain. Glycosyl hydrolases are key enzymes of carbohydrate metabolism. | ||
| cd10812 | GH38N_AMII_ScAms1_like | 7.0e-98 | 280 | 515 | 236 | + N-terminal catalytic domain of yeast vacuolar alpha-mannosidases and similar proteins; glycoside hydrolase family 38 (GH38). The family is represented by Saccharomyces cerevisiae alpha-mannosidase (Ams1) and its eukaryotic homologs. Ams1 functions as a second resident vacuolar hydrolase in S. cerevisiae. It aids in recycling macromolecular components of the cell through hydrolysis of terminal, non-reducing alpha-d-mannose residues. Ams1 forms an oligomer in the cytoplasm and retains its oligomeric form during the import process. It utilizes both the Cvt (nutrient-rich conditions) and autophagic (starvation conditions) pathways for biosynthetic delivery to the vacuole. Mutants in either pathway are defective in Ams1 import. Members in this family show high sequence similarity with rat ER/cytosolic alpha-mannosidase Man2C1. | ||
| cd10789 | GH38N_AMII_ER_cytosolic | 2.0e-102 | 280 | 532 | 253 | + N-terminal catalytic domain of endoplasmic reticulum(ER)/cytosolic class II alpha-mannosidases; glycoside hydrolase family 38 (GH38). The subfamily is represented by Saccharomyces cerevisiae vacuolar alpha-mannosidase Ams1, rat ER/cytosolic alpha-mannosidase Man2C1, and similar proteins. Members in this family share high sequence similarity. None of them have any classical signal sequence or membrane spanning domains, which are typical of sorting or targeting signals. Ams1 functions as a second resident vacuolar hydrolase in S. cerevisiae. It aids in recycling macromolecular components of the cell through hydrolysis of terminal, non-reducing alpha-d-mannose residues. Ams1 utilizes both the cytoplasm to vacuole targeting (Cvt, nutrient-rich conditions) and autophagic (starvation conditions) pathways for biosynthetic delivery to the vacuole. Man2C1is involved in oligosaccharide catabolism in both the ER and cytosol. It can catalyze the cobalt-dependent cleavage of alpha 1,2-, alpha 1,3-, and alpha 1,6-linked mannose residues. Members in this family are retaining glycosyl hydrolases of family GH38 that employs a two-step mechanism involving the formation of a covalent glycosyl-enzyme complex. Two carboxylic acids positioned within the active site act in concert: one as a catalytic nucleophile and the other as a general acid/base catalyst. | ||
| cd10813 | GH38N_AMII_Man2C1 | 3.0e-108 | 280 | 531 | 252 | + N-terminal catalytic domain of mammalian cytosolic alpha-mannosidase Man2C1 and similar proteins; glycoside hydrolase family 38 (GH38). The subfamily corresponds to cytosolic alpha-mannosidase Man2C1 (also known as ER-mannosidase II or neutral/cytosolic mannosidase), mainly found in various vertebrates, and similar proteins. Man2C1 plays an essential role in the catabolism of cytosolic free oligomannosides derived from dolichol intermediates and the degradation of newly synthesized glycoproteins in ER or cytosol. It can catalyze the cleavage of alpha 1,2-, alpha 1,3-, and alpha 1,6-linked mannose residues. Man2C1 is a cobalt-dependent enzyme belonging to alpha-mannosidase class II. It has a neutral pH optimum and is strongly inhitibed by furanose analogs swainsonine (SW) and 1,4-dideoxy-1,4-imino-D-mannitol (DIM), moderately by deoxymannojirimycin (DMM), but not by kifunensine (KIF). DMM and KIF, both pyranose analogs, are normally known to inhibit class I alpha-mannosidase. | ||
| Annotations - NR Download unfiltered results here | |||||||
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| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| RefSeq | XP_001400300.1 | 0 | 20 | 659 | 9 | 667 | hypothetical protein An02g11720 [Aspergillus niger] |
| RefSeq | XP_001400300.1 | 0 | 859 | 1131 | 710 | 980 | hypothetical protein An02g11720 [Aspergillus niger] |
| RefSeq | XP_001690386.1 | 0 | 1 | 1368 | 1 | 1359 | hypothetical protein CHLREDRAFT_144252 [Chlamydomonas reinhardtii] |
| RefSeq | XP_660540.1 | 0 | 32 | 647 | 21 | 653 | hypothetical protein AN2936.2 [Aspergillus nidulans FGSC A4] |
| RefSeq | XP_660540.1 | 0 | 857 | 1138 | 702 | 984 | hypothetical protein AN2936.2 [Aspergillus nidulans FGSC A4] |
| Annotations - PDB Download unfiltered results here | |||||||
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| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3lvt_A | 0.00000000003 | 278 | 629 | 6 | 372 | A Chain A, The Crystal Structure Of A Protein In The Glycosyl Hydrolase Family 38 From Enterococcus Faecalis To 2.55a |
| PDB | 2wyi_B | 0.00000001 | 280 | 659 | 27 | 413 | A Chain A, The Crystal Structure Of A Protein In The Glycosyl Hydrolase Family 38 From Enterococcus Faecalis To 2.55a |
| PDB | 2wyi_A | 0.00000001 | 280 | 659 | 27 | 413 | A Chain A, The Crystal Structure Of A Protein In The Glycosyl Hydrolase Family 38 From Enterococcus Faecalis To 2.55a |
| PDB | 2wyh_B | 0.00000001 | 280 | 659 | 27 | 413 | A Chain A, Structure Of The Streptococcus Pyogenes Family Gh38 Alpha- Mannosidase |
| PDB | 2wyh_A | 0.00000001 | 280 | 659 | 27 | 413 | A Chain A, Structure Of The Streptococcus Pyogenes Family Gh38 Alpha- Mannosidase |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| GW776638 | 235 | 895 | 1125 | 0 |
| FL686454 | 288 | 178 | 445 | 0 |
| GO891460 | 134 | 992 | 1125 | 3.00004e-41 |
| EY038546 | 114 | 989 | 1102 | 1e-31 |
| CV881058 | 131 | 959 | 1085 | 4e-30 |
| Orthologous Group | |||||
|---|---|---|---|---|---|
| Species | ID | ||||
| Physcomitrella patens | Pp1s725_2V6.1 | ||||
| Volvox carteri | Vocar20008356m | ||||
| Sequence Alignments (This image is cropped. Click for full image.) |
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| Phylogeny |
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