| Basic Information | |
|---|---|
| Species | Volvox carteri |
| Cazyme ID | Vocar20008356m |
| Family | GH38 |
| Protein Properties | Length: 1911 Molecular Weight: 205818 Isoelectric Point: 6.926 |
| Chromosome | Chromosome/Scaffold: 1 Start: 10095049 End: 10120730 |
| Description | golgi alpha-mannosidase II |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH38 | 367 | 596 | 0 |
| QVYAVGHCHIDTAWLWPFSETHRKTARSWSSQLRLAERYPWHVFTASSAQQYEWLLQDYPGLFSEIQEAAARGTFVPVGGTWVEMDTNLPSGESLIRQFL YGQRFFEAHFGSRCDVFWLPDTFGYSGQLPQIARGAGIRYFLTQKLSWNNINTFPHSTFQWAGLDGSSLLTHFPPANTYNAQADAHDILLTATNSKDKDR APAGYMLYGNGDGGGGPTVDMCESLSRLAG | |||
| Full Sequence |
|---|
| Protein Sequence Length: 1911 Download |
| MHLSIARQCP PFNPRPPFLS CSLYPSQSST QTPMLSPPPV IFVRSPYTEL LPLLSRLPCP 60 SPTPPHYGPH PPNFKLAYRI SAFNSPSSPI QEMAGPAPPN LGGRVPGSSS SRVWVPQHHR 120 DITLGRLDGY LAADGQFSDR TIRADMWSRK CAECVSLEVY SHPRGIPYPT YDEAIRMPYC 180 PAKVGDSFGP SWTTHWFRVR ARVPPDWDGL GPLMFRWDSG SEAMLYTEGP TPRQGITDQR 240 NEYQLGEWAV GGQELLFYVE MAANGMFGNG PSTNNIQPPD ENRYFTLKTA ELAIPNLPVV 300 ALFHDLRALT GLAKELPAGN ATGEIALYTA NKIVNTYFQG APPECVSVCR SLAAEVLAVR 360 DPGERLQVYA VGHCHIDTAW LWPFSETHRK TARSWSSQLR LAERYPWHVF TASSAQQYEW 420 LLQDYPGLFS EIQEAAARGT FVPVGGTWVE MDTNLPSGES LIRQFLYGQR FFEAHFGSRC 480 DVFWLPDTFG YSGQLPQIAR GAGIRYFLTQ KLSWNNINTF PHSTFQWAGL DGSSLLTHFP 540 PANTYNAQAD AHDILLTATN SKDKDRAPAG YMLYGNGDGG GGPTVDMCES LSRLAGCRGL 600 ASLTVASPSE RGELYFELHR GTYTSHAANK SHNRSCELLL REAEAAGALA AAVLPADVYC 660 YPRSEIDAIW KDVLLFQFHD VLPGSSIGQV YDYTAERYPI LEFNIRKIRD AALEALLAAA 720 GGATATAAVG ATVPCGSSSC NDSNYYCVGG GGGGGGVGTL HSAEVVGARP LNPHVCHSAP 780 SPYNNPLSVA QDCYVVPRAG GQVSAIARAL ARIVSCGHCW RRCGSQRCTA GSGRPPPPPP 840 PAQHQSHYRQ GAEGETEGGR GALPRVVTAA AAAAAAAAAP VTGSGGFSPG TVVGAAARVR 900 TTVGWVYNSM AFHRREVVSV PVEMLPPGVS VRQLSADRTA ALVVVDVPPL SLTPLLQQDL 960 AAGYGSAAPA LAPAPSAPAC GGRDDAPWVG GGATILRETT RKDGVVYVMQ NSLIRAMFDS 1020 CGRLISLYDM IWQRELVPEG EAGNVFRLYE DIPLYWDAWD IEIYHLEKGY PAGQGLPPPK 1080 VEWSENRTAL KVEFPWLLDA PNASYEVQFG AVQRPTHTNT SWDWARFEVC AHKWADLSEP 1140 GYGIALLNDC KYGHATHGNI MRLTLLRGRP PPGPLVTLPP ASPRPPFGGP PPPLPSLGWA 1200 FNGPLRVVGP PQPPSPRKPH PAAARAATPR HLYTMSPSPS PSPSPAHSYS PLCTPATTNT 1260 TNTITCSLTS PVASSVARGA RAPADEPPGA LVVRLYEPHG GRGVARVRWP AWLRVSHVAL 1320 CNLLEEDQGG VEGEGEGAEG GDGSGGKAGL LVVRWDGAGG SVDIEYGPFK VITLKLYLEQ 1380 ELVVDDSGQP EAYEINYITF YAFNGHYHIP ANVPLFRTGH HVGDWEHLTV RLDATSLELQ 1440 VEPGAGPCTQ GVWYNAHRNI EGEWVPGVAV PRTPCGRILG FVAINGHGIY PKCGTIHRLF 1500 FIVNDRTSRR GPVWAPTRLV RLCGLEFLKV VEVLVLVLCY KVQSLFLPTI GGKLDDRRFM 1560 RMKLIDESLK AWKLGLEGMP SSQRITMLEL AFPNMGAQII TEQHLRVIPG VAPGQDGGYY 1620 FCSSHKHQIV RLLSNNDGML WESWSGLESG FMKESRMYAA LLTSSLPPMV SRNRLCTSGC 1680 SLPHASPLCS GGPPPPTCRL LHPPPAAGAT AGWGRHWGYC DSVVLAGGTE GAAVPGEAEE 1740 EEEGRGPVAV GKVGGLPPTA MLEPEVMLMT GLAVSSRVDP GSQAAQGAFP PSVGEAVPAG 1800 RGGGHLDDGD GGGGLHGARR SPFPLPTVVH DTSPWQRYRG RWGSVVSPTL QGWFLNAEPP 1860 VSRGCLRRLF LPLARGVERL EPACCVTSDF SFLGGQVDPD IDPPGGVHDG * 1920 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| COG0383 | AMS1 | 9.0e-91 | 184 | 698 | 524 | + Alpha-mannosidase [Carbohydrate transport and metabolism] | ||
| pfam01074 | Glyco_hydro_38 | 1.0e-94 | 367 | 617 | 255 | + Glycosyl hydrolases family 38 N-terminal domain. Glycosyl hydrolases are key enzymes of carbohydrate metabolism. | ||
| cd10812 | GH38N_AMII_ScAms1_like | 1.0e-116 | 367 | 605 | 239 | + 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 | 7.0e-120 | 367 | 617 | 251 | + 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-120 | 367 | 610 | 244 | + 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. | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
| GO:0004559 | alpha-mannosidase activity |
| GO:0005975 | carbohydrate metabolic process |
| GO:0006013 | mannose metabolic process |
| GO:0008270 | zinc ion binding |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| RefSeq | XP_001400300.1 | 0 | 115 | 753 | 21 | 701 | hypothetical protein An02g11720 [Aspergillus niger] |
| RefSeq | XP_001400300.1 | 1.99993e-41 | 1006 | 1378 | 726 | 1089 | hypothetical protein An02g11720 [Aspergillus niger] |
| RefSeq | XP_001690386.1 | 0 | 114 | 710 | 31 | 632 | hypothetical protein CHLREDRAFT_144252 [Chlamydomonas reinhardtii] |
| RefSeq | XP_001690386.1 | 0 | 903 | 1211 | 701 | 1119 | hypothetical protein CHLREDRAFT_144252 [Chlamydomonas reinhardtii] |
| RefSeq | XP_001690386.1 | 0.0000000005 | 1252 | 1379 | 1241 | 1358 | hypothetical protein CHLREDRAFT_144252 [Chlamydomonas reinhardtii] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3lvt_A | 0.0000004 | 365 | 504 | 6 | 145 | A Chain A, The Crystal Structure Of A Protein In The Glycosyl Hydrolase Family 38 From Enterococcus Faecalis To 2.55a |
| PDB | 2wyi_B | 0.00003 | 367 | 505 | 27 | 165 | A Chain A, The Crystal Structure Of A Protein In The Glycosyl Hydrolase Family 38 From Enterococcus Faecalis To 2.55a |
| PDB | 2wyi_A | 0.00003 | 367 | 505 | 27 | 165 | A Chain A, The Crystal Structure Of A Protein In The Glycosyl Hydrolase Family 38 From Enterococcus Faecalis To 2.55a |
| PDB | 2wyh_B | 0.00003 | 367 | 505 | 27 | 165 | A Chain A, Structure Of The Streptococcus Pyogenes Family Gh38 Alpha- Mannosidase |
| PDB | 2wyh_A | 0.00003 | 367 | 505 | 27 | 165 | 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 |
| FL686454 | 289 | 262 | 532 | 0 |
| BU655170 | 156 | 1370 | 1524 | 0 |
| GW776638 | 179 | 1026 | 1161 | 5e-35 |
| EY038546 | 81 | 1081 | 1161 | 3e-24 |
| HS663175 | 141 | 1391 | 1522 | 2e-23 |
| Orthologous Group | |||||
|---|---|---|---|---|---|
| Species | ID | ||||
| Chlamydomonas reinhardtii | Cre10.g437950.t1.2 | ||||
| Physcomitrella patens | Pp1s725_2V6.1 | ||||
| Sequence Alignments (This image is cropped. Click for full image.) |
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| Phylogeny |
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