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Conserved domains on  [gi|807679|gb|AAA66457|]
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alpha-mannosidase II, partial [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GH38N_Man2A1 cd11666
N-terminal catalytic domain of Golgi alpha-mannosidase II and similar proteins; glycoside ...
 131-474 0e+00

N-terminal catalytic domain of Golgi alpha-mannosidase II and similar proteins; glycoside hydrolase family 38 (GH38); This subfamily is represented by Golgi alpha-mannosidase II (GMII, also known as mannosyl-oligosaccharide 1,3- 1,6-alpha mannosidase, EC 3.2.1.114, Man2A1), a monomeric, membrane-anchored class II alpha-mannosidase existing in the Golgi apparatus of eukaryotes. GMII plays a key role in the N-glycosylation pathway. It catalyzes the hydrolysis of the terminal of both alpha-1,3-linked and alpha-1,6-linked mannoses from the high-mannose oligosaccharide GlcNAc(Man)5(GlcNAc)2 to yield GlcNAc(Man)3(GlcNAc)2(GlcNAc, N-acetylglucosmine), which is the committed step of complex N-glycan synthesis. GMII is activated by zinc or cobalt ions and is strongly inhibited by swainsonine. Inhibition of GMII provides a route to block cancer-induced changes in cell surface oligosaccharide structures. GMII has a pH optimum of 5.5-6.0, which is intermediate between those of acidic (lysosomal alpha-mannosidase) and neutral (ER/cytosolic alpha-mannosidase) enzymes. GMII is a retaining glycosyl hydrolase 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.


:

Pssm-ID: 212131 [Multi-domain]  Cd Length: 344  Bit Score: 753.34  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679   131 PLQVFVVPHSHNDPGWLKTFNDYFRDKTQYIFNNMVLKLKEDSSRKFIWSEISYLAKWWDIIDNPKKEAVKSLLQNGQLE 210
Cdd:cd11666   1 PLQVFVVPHSHNDPGWLKTFDDYFRDQTQHILNNMVLKLKEDSRRKFIWSEISYFAKWWDIIDGQKKDAVKRLIENGQLE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679   211 IVTGGWVMADEATTHYFALIDQLIEGHQWLEKNLGVKPRSGWAIDPFGHSPTMTYLLKRAGFSHMLIQRVHYSVKKHFSL 290
Cdd:cd11666  81 IVTGGWVMPDEATAHYFALIDQLIEGHQWLERNLGVKPKSGWAVDPFGHSPTMAYLLKRAGLSNMLIQRVHYSVKKHFSL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679   291 QKTLEFFWRQNWDLGSTTDILCHMMPFYSYDIPHTCGPDPKICCQFDFKRLPGGRYGCPWGVPPEAISPGNVQSRAQMLL 370
Cdd:cd11666 161 QKTLEFFWRQNWDLGSSTDILCHMMPFYSYDVPHTCGPDPKICCQFDFKRLPGGRISCPWRVPPEAIHPGNVQSRAQMLL 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679   371 DQYRKKSKLFRTKVLLAPLGDDFRFSEYTEWDLQYRNYEQLFSYMNSQPHLKVKIQFGTLSDYFDALEKSVAAEKKGGQS 450
Cdd:cd11666 241 DQYRKKSKLFRTKVLLAPLGDDFRYTEYTEWDQQFENYQKLFDYMNSHPELHVKAQFGTLSDYFDALRKSTGMDPVGGQS 320

                       330       340
                ....*....|....*....|....
gi 807679   451 VFPALSGDFFTYADRDDHYWSGYF 474
Cdd:cd11666 321 AFPVLSGDFFTYADRDDHYWSGYF 344
Alpha-mann_mid super family cl47049
Alpha mannosidase, middle domain; Members of this entry belong to the glycosyl hydrolase ...
 469-487 5.29e-05

Alpha mannosidase, middle domain; Members of this entry belong to the glycosyl hydrolase family 38, This domain, which is found in the central region adopts a structure consisting of three alpha helices, in an immunoglobulin/albumin-binding domain-like fold. The domain is predominantly found in the enzyme alpha-mannosidase.


The actual alignment was detected with superfamily member smart00872:

Pssm-ID: 214875 [Multi-domain]  Cd Length: 79  Bit Score: 41.38  E-value: 5.29e-05
                           10
                   ....*....|....*....
gi 807679      469 YWSGYFTSRPFYKRMDRIM 487
Cdd:smart00872   1 YHRGTYTSRPYLKRLNRRA 19
 
Name Accession Description Interval E-value
GH38N_Man2A1 cd11666
N-terminal catalytic domain of Golgi alpha-mannosidase II and similar proteins; glycoside ...
 131-474 0e+00

N-terminal catalytic domain of Golgi alpha-mannosidase II and similar proteins; glycoside hydrolase family 38 (GH38); This subfamily is represented by Golgi alpha-mannosidase II (GMII, also known as mannosyl-oligosaccharide 1,3- 1,6-alpha mannosidase, EC 3.2.1.114, Man2A1), a monomeric, membrane-anchored class II alpha-mannosidase existing in the Golgi apparatus of eukaryotes. GMII plays a key role in the N-glycosylation pathway. It catalyzes the hydrolysis of the terminal of both alpha-1,3-linked and alpha-1,6-linked mannoses from the high-mannose oligosaccharide GlcNAc(Man)5(GlcNAc)2 to yield GlcNAc(Man)3(GlcNAc)2(GlcNAc, N-acetylglucosmine), which is the committed step of complex N-glycan synthesis. GMII is activated by zinc or cobalt ions and is strongly inhibited by swainsonine. Inhibition of GMII provides a route to block cancer-induced changes in cell surface oligosaccharide structures. GMII has a pH optimum of 5.5-6.0, which is intermediate between those of acidic (lysosomal alpha-mannosidase) and neutral (ER/cytosolic alpha-mannosidase) enzymes. GMII is a retaining glycosyl hydrolase 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.


Pssm-ID: 212131 [Multi-domain]  Cd Length: 344  Bit Score: 753.34  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679   131 PLQVFVVPHSHNDPGWLKTFNDYFRDKTQYIFNNMVLKLKEDSSRKFIWSEISYLAKWWDIIDNPKKEAVKSLLQNGQLE 210
Cdd:cd11666   1 PLQVFVVPHSHNDPGWLKTFDDYFRDQTQHILNNMVLKLKEDSRRKFIWSEISYFAKWWDIIDGQKKDAVKRLIENGQLE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679   211 IVTGGWVMADEATTHYFALIDQLIEGHQWLEKNLGVKPRSGWAIDPFGHSPTMTYLLKRAGFSHMLIQRVHYSVKKHFSL 290
Cdd:cd11666  81 IVTGGWVMPDEATAHYFALIDQLIEGHQWLERNLGVKPKSGWAVDPFGHSPTMAYLLKRAGLSNMLIQRVHYSVKKHFSL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679   291 QKTLEFFWRQNWDLGSTTDILCHMMPFYSYDIPHTCGPDPKICCQFDFKRLPGGRYGCPWGVPPEAISPGNVQSRAQMLL 370
Cdd:cd11666 161 QKTLEFFWRQNWDLGSSTDILCHMMPFYSYDVPHTCGPDPKICCQFDFKRLPGGRISCPWRVPPEAIHPGNVQSRAQMLL 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679   371 DQYRKKSKLFRTKVLLAPLGDDFRFSEYTEWDLQYRNYEQLFSYMNSQPHLKVKIQFGTLSDYFDALEKSVAAEKKGGQS 450
Cdd:cd11666 241 DQYRKKSKLFRTKVLLAPLGDDFRYTEYTEWDQQFENYQKLFDYMNSHPELHVKAQFGTLSDYFDALRKSTGMDPVGGQS 320

                       330       340
                ....*....|....*....|....
gi 807679   451 VFPALSGDFFTYADRDDHYWSGYF 474
Cdd:cd11666 321 AFPVLSGDFFTYADRDDHYWSGYF 344
PLN02701 PLN02701
alpha-mannosidase
 94-487 0e+00

alpha-mannosidase


Pssm-ID: 178304 [Multi-domain]  Cd Length: 1050  Bit Score: 621.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679      94 DVQMLDVYDLIPFDNPDGGVWKQGFDIKYEADEWDREPLQVFVVPHSHNDPGWLKTFNDYFRDKTQYIFNNMVLKLKEDS 173
Cdd:PLN02701    2 DITTKDLYDRIEFLDKDGGAWKQGWRVKYRGDEWDREKLKVFVVPHSHNDPGWILTVEEYYQEQSRHILDTIVESLSKDP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679     174 SRKFIWSEISYLAKWWDIIDNPKKEAVKSLLQNGQLEIVTGGWVMADEATTHYFALIDQLIEGHQWLEKNLGVKPRSGWA 253
Cdd:PLN02701   82 RRKFIWEEMSYLERWWRDASPSKKEAFTKLVKNGQLEIVGGGWVMNDEANSHYFAIIEQITEGNMWLNDTIGVAPKNSWA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679     254 IDPFGHSPTMTYLLKRAGFSHMLIQRVHYSVKKHFSLQKTLEFFWRQNWDLGSTTDILCHMMPFYSYDIPHTCGPDPKIC 333
Cdd:PLN02701  162 IDPFGYSSTMAYLLRRMGFENMLIQRTHYEVKKELAQNKNLEYIWRQSWDAEETTDIFVHMMPFYSYDIPHTCGPEPAIC 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679     334 CQFDFKRLPGGRYG-CPWGVPPEAISPGNVQSRAQMLLDQYRKKSKLFRTKVLLAPLGDDFRFSEYTEWDLQYRNYEQLF 412
Cdd:PLN02701  242 CQFDFARMRGFQYElCPWGKHPVETNDENVQERAMKLLDQYRKKSTLYRTNTLLVPLGDDFRYISIDEAEAQFRNYQKLF 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679     413 SYMNSQPHLKVKIQFGTLSDYFDALE-------KSVAAEKKGGQSV-FPALSGDFFTYADRDDHYWSGYFTSRPFYKRMD 484
Cdd:PLN02701  322 DYINSNPSLKAEVKFGTLEDYFSTLRdeadrinYSRPGEVGSGEVPgFPSLSGDFFTYADRQQDYWSGYYVSRPFFKAVD 401


                  ...
gi 807679     485 RIM 487
Cdd:PLN02701  402 RVL 404
Glyco_hydro_38N pfam01074
Glycosyl hydrolases family 38 N-terminal domain; Glycosyl hydrolases are key enzymes of ...
 133-463 1.83e-108

Glycosyl hydrolases family 38 N-terminal domain; Glycosyl hydrolases are key enzymes of carbohydrate metabolism.


Pssm-ID: 426030 [Multi-domain]  Cd Length: 271  Bit Score: 323.04  E-value: 1.83e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679     133 QVFVVPHSHNDPGWLKTFNDYFRdKTQYIFNNMVLKLKEDSSRKFIWSEISYLAKWWDIIdNPKKEAVKSLLQNGQLEIV 212
Cdd:pfam01074   1 TVHLVGHSHIDVGWLWTVDETRR-KVQRTFSSVLALLDRDPDRRFIWSEAQFFAWWWEDQ-PELFKRIKKLVAEGRLEPV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679     213 TGGWVMADEATTHYFALIDQLIEGHQWLEKNLGVKPRSGWAIDPFGHSPTMTYLLKRAGFSHMLIQRVHYSVKKHFslQK 292
Cdd:pfam01074  79 GGGWVEPDENLPSGESLIRQFLYGQRFFKEEFGVRPRVGWLPDPFGYSATLPQILKQAGIDYFLTQRLHWNDKNKF--NP 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679     293 TLEFFWRQNWDlgstTDILCHMMPFYSYdiphtcgpdPKICCQFdfkrlpggrygcpwgvppeaispgnvQSRAQMLLDQ 372
Cdd:pfam01074 157 HLEFIWRGSDG----TEIFTHMPPFDYY---------PTYGFQF--------------------------QERAEDLLAY 197

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679     373 YRKKSKLFRTKVLLAPLGDDfrfseytewDLQYRNYEQLFSYMN-SQPHL-KVKIQFGTLSDYFDALEKsvaaekkggqS 450
Cdd:pfam01074 198 ARNYADKTRTNHVLLPFGDG---------DGGGGPTDEMLEYINrWNALPgLPKVQYGTPSDYFDALEK----------A 258

                         330
                  ....*....|...
gi 807679     451 VFPALSGDFFTYA 463
Cdd:pfam01074 259 TWPTKTDDFPPYA 271
Alpha-mann_mid smart00872
Alpha mannosidase, middle domain; Members of this entry belong to the glycosyl hydrolase ...
 469-487 5.29e-05

Alpha mannosidase, middle domain; Members of this entry belong to the glycosyl hydrolase family 38, This domain, which is found in the central region adopts a structure consisting of three alpha helices, in an immunoglobulin/albumin-binding domain-like fold. The domain is predominantly found in the enzyme alpha-mannosidase.


Pssm-ID: 214875 [Multi-domain]  Cd Length: 79  Bit Score: 41.38  E-value: 5.29e-05
                           10
                   ....*....|....*....
gi 807679      469 YWSGYFTSRPFYKRMDRIM 487
Cdd:smart00872   1 YHRGTYTSRPYLKRLNRRA 19
Alpha-mann_mid pfam09261
Alpha mannosidase middle domain; Members of this family adopt a structure consisting of three ...
 468-487 9.58e-05

Alpha mannosidase middle domain; Members of this family adopt a structure consisting of three alpha helices, in an immunoglobulin/albumin-binding domain-like fold. They are predominantly found in the enzyme alpha-mannosidase.


Pssm-ID: 462728 [Multi-domain]  Cd Length: 98  Bit Score: 41.48  E-value: 9.58e-05
                          10        20
                  ....*....|....*....|
gi 807679     468 HYWSGYFTSRPFYKRMDRIM 487
Cdd:pfam09261   1 EYHRGTYTSRADLKRLNRKL 20
 
Name Accession Description Interval E-value
GH38N_Man2A1 cd11666
N-terminal catalytic domain of Golgi alpha-mannosidase II and similar proteins; glycoside ...
 131-474 0e+00

N-terminal catalytic domain of Golgi alpha-mannosidase II and similar proteins; glycoside hydrolase family 38 (GH38); This subfamily is represented by Golgi alpha-mannosidase II (GMII, also known as mannosyl-oligosaccharide 1,3- 1,6-alpha mannosidase, EC 3.2.1.114, Man2A1), a monomeric, membrane-anchored class II alpha-mannosidase existing in the Golgi apparatus of eukaryotes. GMII plays a key role in the N-glycosylation pathway. It catalyzes the hydrolysis of the terminal of both alpha-1,3-linked and alpha-1,6-linked mannoses from the high-mannose oligosaccharide GlcNAc(Man)5(GlcNAc)2 to yield GlcNAc(Man)3(GlcNAc)2(GlcNAc, N-acetylglucosmine), which is the committed step of complex N-glycan synthesis. GMII is activated by zinc or cobalt ions and is strongly inhibited by swainsonine. Inhibition of GMII provides a route to block cancer-induced changes in cell surface oligosaccharide structures. GMII has a pH optimum of 5.5-6.0, which is intermediate between those of acidic (lysosomal alpha-mannosidase) and neutral (ER/cytosolic alpha-mannosidase) enzymes. GMII is a retaining glycosyl hydrolase 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.


Pssm-ID: 212131 [Multi-domain]  Cd Length: 344  Bit Score: 753.34  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679   131 PLQVFVVPHSHNDPGWLKTFNDYFRDKTQYIFNNMVLKLKEDSSRKFIWSEISYLAKWWDIIDNPKKEAVKSLLQNGQLE 210
Cdd:cd11666   1 PLQVFVVPHSHNDPGWLKTFDDYFRDQTQHILNNMVLKLKEDSRRKFIWSEISYFAKWWDIIDGQKKDAVKRLIENGQLE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679   211 IVTGGWVMADEATTHYFALIDQLIEGHQWLEKNLGVKPRSGWAIDPFGHSPTMTYLLKRAGFSHMLIQRVHYSVKKHFSL 290
Cdd:cd11666  81 IVTGGWVMPDEATAHYFALIDQLIEGHQWLERNLGVKPKSGWAVDPFGHSPTMAYLLKRAGLSNMLIQRVHYSVKKHFSL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679   291 QKTLEFFWRQNWDLGSTTDILCHMMPFYSYDIPHTCGPDPKICCQFDFKRLPGGRYGCPWGVPPEAISPGNVQSRAQMLL 370
Cdd:cd11666 161 QKTLEFFWRQNWDLGSSTDILCHMMPFYSYDVPHTCGPDPKICCQFDFKRLPGGRISCPWRVPPEAIHPGNVQSRAQMLL 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679   371 DQYRKKSKLFRTKVLLAPLGDDFRFSEYTEWDLQYRNYEQLFSYMNSQPHLKVKIQFGTLSDYFDALEKSVAAEKKGGQS 450
Cdd:cd11666 241 DQYRKKSKLFRTKVLLAPLGDDFRYTEYTEWDQQFENYQKLFDYMNSHPELHVKAQFGTLSDYFDALRKSTGMDPVGGQS 320

                       330       340
                ....*....|....*....|....
gi 807679   451 VFPALSGDFFTYADRDDHYWSGYF 474
Cdd:cd11666 321 AFPVLSGDFFTYADRDDHYWSGYF 344
GH38N_AMII_GMII_SfManIII_like cd10809
N-terminal catalytic domain of Golgi alpha-mannosidase II, Spodoptera frugiperda Sf9 ...
 131-474 0e+00

N-terminal catalytic domain of Golgi alpha-mannosidase II, Spodoptera frugiperda Sf9 alpha-mannosidase III, and similar proteins; glycoside hydrolase family 38 (GH38); This subfamily is represented by Golgi alpha-mannosidase II (GMII, also known as mannosyl-oligosaccharide 1,3- 1,6-alpha mannosidase, EC 3.2.1.114, Man2A1), a monomeric, membrane-anchored class II alpha-mannosidase existing in the Golgi apparatus of eukaryotes. GMII plays a key role in the N-glycosylation pathway. It catalyzes the hydrolysis of the terminal both alpha-1,3-linked and alpha-1,6-linked mannoses from the high-mannose oligosaccharide GlcNAc(Man)5(GlcNAc)2 to yield GlcNAc(Man)3(GlcNAc)2(GlcNAc, N-acetylglucosmine), which is the committed step of complex N-glycan synthesis. GMII is activated by zinc or cobalt ions and is strongly inhibited by swainsonine. Inhibition of GMII provides a route to block cancer-induced changes in cell surface oligosaccharide structures. GMII has a pH optimum of 5.5-6.0, which is intermediate between those of acidic (lysosomal alpha-mannosidase) and neutral (ER/cytosolic alpha-mannosidase) enzymes. GMII is a retaining glycosyl hydrolase 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. This subfamily also includes human alpha-mannosidase 2x (MX, also known as mannosyl-oligosaccharide 1,3- 1,6-alpha mannosidase, EC 3.2.1.114, Man2A2). MX is enzymatically and functionally very similar to GMII, and is thought to also function in the N-glycosylation pathway. Also found in this subfamily is class II alpha-mannosidase encoded by Spodoptera frugiperda Sf9 cell. This alpha-mannosidase is an integral membrane glycoprotein localized in the Golgi apparatus. It shows high sequence homology with mammalian Golgi alpha-mannosidase II(GMII). It can hydrolyze p-nitrophenyl alpha-D-mannopyranoside (pNP-alpha-Man), and it is inhibited by swainsonine. However, the Sf9 enzyme is stimulated by cobalt and can hydrolyze (Man)5(GlcNAc)2 to (Man)3(GlcNAc)2, but it cannot hydrolyze GlcNAc(Man)5(GlcNAc)2, which is distinct from that of GMII. Thus, this enzyme has been designated as Sf9 alpha-mannosidase III (SfManIII). It probably functions in an alternate N-glycan processing pathway in Sf9 cells.


Pssm-ID: 212120 [Multi-domain]  Cd Length: 340  Bit Score: 669.74  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679   131 PLQVFVVPHSHNDPGWLKTFNDYFRDKTQYIFNNMVLKLKEDSSRKFIWSEISYLAKWWDIIDNPKKEAVKSLLQNGQLE 210
Cdd:cd10809   1 KLKVFVVPHSHNDPGWIKTFEEYYQDQTKHILDNMVDKLSKNPKMKFIWAEISFLERWWDDASPDKKEAVKKLVKNGQLE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679   211 IVTGGWVMADEATTHYFALIDQLIEGHQWLEKNLGVKPRSGWAIDPFGHSPTMTYLLKRAGFSHMLIQRVHYSVKKHFSL 290
Cdd:cd10809  81 IVTGGWVMTDEANSHYFAMIDQLIEGHQWLKENLGVKPKSGWSIDPFGHSPTMPYLLKRAGFKNMVIQRIHYEVKKYLAQ 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679   291 QKTLEFFWRQNWDLGSTTDILCHMMPFYSYDIPHTCGPDPKICCQFDFKRLPGGRYGCPWGVPPEAISPGNVQSRAQMLL 370
Cdd:cd10809 161 RKALEFMWRQYWDATGSTDILTHMMPFYSYDIPHTCGPDPAVCCQFDFKRLPGGGESCPWKKPPQPITDDNVAERAELLL 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679   371 DQYRKKSKLFRTKVLLAPLGDDFRFSEYTEWDLQYRNYEQLFSYMNSQPHLKVKIQFGTLSDYFDALEKSVAAEKKGgqs 450
Cdd:cd10809 241 DQYRKKSQLYRSNVVLIPLGDDFRYDSDEEWDAQYDNYQKLFDYINSNPELNVEIQFGTLSDYFNALRKRTGTNTPG--- 317

                       330       340
                ....*....|....*....|....
gi 807679   451 vFPALSGDFFTYADRDDHYWSGYF 474
Cdd:cd10809 318 -FPTLSGDFFTYADRDDDYWSGYY 340
PLN02701 PLN02701
alpha-mannosidase
 94-487 0e+00

alpha-mannosidase


Pssm-ID: 178304 [Multi-domain]  Cd Length: 1050  Bit Score: 621.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679      94 DVQMLDVYDLIPFDNPDGGVWKQGFDIKYEADEWDREPLQVFVVPHSHNDPGWLKTFNDYFRDKTQYIFNNMVLKLKEDS 173
Cdd:PLN02701    2 DITTKDLYDRIEFLDKDGGAWKQGWRVKYRGDEWDREKLKVFVVPHSHNDPGWILTVEEYYQEQSRHILDTIVESLSKDP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679     174 SRKFIWSEISYLAKWWDIIDNPKKEAVKSLLQNGQLEIVTGGWVMADEATTHYFALIDQLIEGHQWLEKNLGVKPRSGWA 253
Cdd:PLN02701   82 RRKFIWEEMSYLERWWRDASPSKKEAFTKLVKNGQLEIVGGGWVMNDEANSHYFAIIEQITEGNMWLNDTIGVAPKNSWA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679     254 IDPFGHSPTMTYLLKRAGFSHMLIQRVHYSVKKHFSLQKTLEFFWRQNWDLGSTTDILCHMMPFYSYDIPHTCGPDPKIC 333
Cdd:PLN02701  162 IDPFGYSSTMAYLLRRMGFENMLIQRTHYEVKKELAQNKNLEYIWRQSWDAEETTDIFVHMMPFYSYDIPHTCGPEPAIC 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679     334 CQFDFKRLPGGRYG-CPWGVPPEAISPGNVQSRAQMLLDQYRKKSKLFRTKVLLAPLGDDFRFSEYTEWDLQYRNYEQLF 412
Cdd:PLN02701  242 CQFDFARMRGFQYElCPWGKHPVETNDENVQERAMKLLDQYRKKSTLYRTNTLLVPLGDDFRYISIDEAEAQFRNYQKLF 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679     413 SYMNSQPHLKVKIQFGTLSDYFDALE-------KSVAAEKKGGQSV-FPALSGDFFTYADRDDHYWSGYFTSRPFYKRMD 484
Cdd:PLN02701  322 DYINSNPSLKAEVKFGTLEDYFSTLRdeadrinYSRPGEVGSGEVPgFPSLSGDFFTYADRQQDYWSGYYVSRPFFKAVD 401


                  ...
gi 807679     485 RIM 487
Cdd:PLN02701  402 RVL 404
GH38N_Man2A2 cd11667
N-terminal catalytic domain of Golgi alpha-mannosidase IIx, and similar proteins; glycoside ...
 131-474 0e+00

N-terminal catalytic domain of Golgi alpha-mannosidase IIx, and similar proteins; glycoside hydrolase family 38 (GH38); This subfamily is represented by human alpha-mannosidase 2x (MX, also known as mannosyl-oligosaccharide 1,3- 1,6-alpha mannosidase, EC 3.2.1.114, Man2A2). MX is enzymatically and functionally very similar to GMII (found in another subfamily), and as an isoenzyme of GMII. It is thought to also function in the N-glycosylation pathway. MX specifically hydrolyzes the same oligosaccharide substrate as does MII. It specifically removes two mannosyl residues from GlcNAc(Man)5(GlcNAc)2 to yield GlcNAc(Man)3(GlcNAc)2(GlcNAc, N-acetylglucosmine).


Pssm-ID: 212132 [Multi-domain]  Cd Length: 344  Bit Score: 608.14  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679   131 PLQVFVVPHSHNDPGWLKTFNDYFRDKTQYIFNNMVLKLKEDSSRKFIWSEISYLAKWWDIIDNPKKEAVKSLLQNGQLE 210
Cdd:cd11667   1 PLQVFVVPHSHNDPGWIKTFDKYYYDQTQHILNSMVVKLQEDPRRRFIWSEISFFSKWWDNINAQKRAAVRRLVGNGQLE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679   211 IVTGGWVMADEATTHYFALIDQLIEGHQWLEKNLGVKPRSGWAIDPFGHSPTMTYLLKRAGFSHMLIQRVHYSVKKHFSL 290
Cdd:cd11667  81 MATGGWVMPDEANSHYFAMIDQLIEGHQWLEKNIGVTPRSGWAVDPFGHSSTMPYILRRSNLTSMLIQRVHYAIKKHFAA 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679   291 QKTLEFFWRQNWDLGSTTDILCHMMPFYSYDIPHTCGPDPKICCQFDFKRLPGGRYGCPWGVPPEAISPGNVQSRAQMLL 370
Cdd:cd11667 161 TQSLEFMWRQTWDPDSSTDIFCHMMPFYSYDVPHTCGPDPKICCQFDFKRLPGGRINCPWKVPPRAITEANVAERAQLLL 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679   371 DQYRKKSKLFRTKVLLAPLGDDFRFSEYTEWDLQYRNYEQLFSYMNSQPHLKVKIQFGTLSDYFDALEKSVAAEKKGGQS 450
Cdd:cd11667 241 DQYRKKSKLYRSKVLLVPLGDDFRYDKPQEWDAQFLNYQRLFDFLNSHPELHVQAQFGTLSDYFDALYKRTGVVPGMRPP 320

                       330       340
                ....*....|....*....|....
gi 807679   451 VFPALSGDFFTYADRDDHYWSGYF 474
Cdd:cd11667 321 GFPVVSGDFFSYADREDHYWTGYY 344
GH38N_AMII_euk cd00451
N-terminal catalytic domain of eukaryotic class II alpha-mannosidases; glycoside hydrolase ...
 132-417 1.96e-110

N-terminal catalytic domain of eukaryotic class II alpha-mannosidases; glycoside hydrolase family 38 (GH38); The family corresponds to a group of eukaryotic class II alpha-mannosidases (AlphaMII), which contain Golgi alpha-mannosidases II (GMII), the major broad specificity lysosomal alpha-mannosidases (LAM, MAN2B1), the noval core-specific lysosomal alpha 1,6-mannosidases (Epman, MAN2B2), and similar proteins. GMII catalyzes the hydrolysis of the terminal both alpha-1,3-linked and alpha-1,6-linked mannoses from the high-mannose oligosaccharide GlcNAc(Man)5(GlcNAc)2 to yield GlcNAc(Man)3(GlcNAc)2 (GlcNAc, N-acetylglucosmine), which is the committed step of complex N-glycan synthesis. LAM is a broad specificity exoglycosidase hydrolyzing all known alpha 1,2-, alpha 1,3-, and alpha 1,6-mannosidic linkages from numerous high mannose type oligosaccharides. Different from LAM, Epman can efficiently cleave only the alpha 1,6-linked mannose residue from (Man)3GlcNAc, but not (Man)3(GlcNAc)2 or other larger high mannose oligosaccharides, in the core of N-linked glycans. 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.


Pssm-ID: 212095 [Multi-domain]  Cd Length: 258  Bit Score: 327.26  E-value: 1.96e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679   132 LQVFVVPHSHNDPGWLKTFNDYFRDKTQYIFNNMVLKLKEDSSRKFIWSEISYLAKWWDIIDNPKKEAVKSLLQNGQLEI 211
Cdd:cd00451   1 LNVHLIPHSHCDVGWLKTFDEYYNGDVKSILDSVVKALNNDPERKFIWAEIGFLERWWEDQGNDTKQQFKKLVKNGQLEF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679   212 VTGGWVMADEATTHYFALIDQLIEGHQWLEKNLGVKPRSGWAIDPFGHSPTMTYLLKRAGFSHMLIQRVHYSVKKHFSLQ 291
Cdd:cd00451  81 VGGGWVMNDEACTTYESIIDQMTEGHQFLKDTFGVRPRVGWQIDPFGHSSTTPTLFSKMGFKGLVINRIPYSLKAEMKDN 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679   292 KTLEFFWRQNWDLGSTTDILCHMMP-FYSYDIPHTCGPDPkiccqfdfkrlpggrygcpwgvppeaISPGNVQSRAQMLL 370
Cdd:cd00451 161 KQLEFVWRGSPSLGPDSEIFTHVLDdHYSYPESLDFGGPP--------------------------ITDYNIAERADEFV 214

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 807679   371 DQYRKKSKLFRTKVLLAPLGDDFRFSeytEWDLQYRNYEQLFSYMNS 417
Cdd:cd00451 215 EYIKKRSKTYRTNHILIPLGDDFRFK---NASLQFSNMDKLIAYINS 258
Glyco_hydro_38N pfam01074
Glycosyl hydrolases family 38 N-terminal domain; Glycosyl hydrolases are key enzymes of ...
 133-463 1.83e-108

Glycosyl hydrolases family 38 N-terminal domain; Glycosyl hydrolases are key enzymes of carbohydrate metabolism.


Pssm-ID: 426030 [Multi-domain]  Cd Length: 271  Bit Score: 323.04  E-value: 1.83e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679     133 QVFVVPHSHNDPGWLKTFNDYFRdKTQYIFNNMVLKLKEDSSRKFIWSEISYLAKWWDIIdNPKKEAVKSLLQNGQLEIV 212
Cdd:pfam01074   1 TVHLVGHSHIDVGWLWTVDETRR-KVQRTFSSVLALLDRDPDRRFIWSEAQFFAWWWEDQ-PELFKRIKKLVAEGRLEPV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679     213 TGGWVMADEATTHYFALIDQLIEGHQWLEKNLGVKPRSGWAIDPFGHSPTMTYLLKRAGFSHMLIQRVHYSVKKHFslQK 292
Cdd:pfam01074  79 GGGWVEPDENLPSGESLIRQFLYGQRFFKEEFGVRPRVGWLPDPFGYSATLPQILKQAGIDYFLTQRLHWNDKNKF--NP 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679     293 TLEFFWRQNWDlgstTDILCHMMPFYSYdiphtcgpdPKICCQFdfkrlpggrygcpwgvppeaispgnvQSRAQMLLDQ 372
Cdd:pfam01074 157 HLEFIWRGSDG----TEIFTHMPPFDYY---------PTYGFQF--------------------------QERAEDLLAY 197

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679     373 YRKKSKLFRTKVLLAPLGDDfrfseytewDLQYRNYEQLFSYMN-SQPHL-KVKIQFGTLSDYFDALEKsvaaekkggqS 450
Cdd:pfam01074 198 ARNYADKTRTNHVLLPFGDG---------DGGGGPTDEMLEYINrWNALPgLPKVQYGTPSDYFDALEK----------A 258

                         330
                  ....*....|...
gi 807679     451 VFPALSGDFFTYA 463
Cdd:pfam01074 259 TWPTKTDDFPPYA 271
GH38N_AMII_LAM_like cd10810
N-terminal catalytic domain of lysosomal alpha-mannosidase and similar proteins; glycoside ...
 132-417 1.20e-73

N-terminal catalytic domain of lysosomal alpha-mannosidase and similar proteins; glycoside hydrolase family 38 (GH38); The subfamily is represented by lysosomal alpha-mannosidase (LAM, Man2B1, EC 3.2.1.114), which is a broad specificity exoglycosidase hydrolyzing all known alpha 1,2-, alpha 1,3-, and alpha 1,6-mannosidic linkages from numerous high mannose type oligosaccharides. LAM is expressed in all tissues and in many species. In mammals, the absence of LAM can cause the autosomal recessive disease alpha-mannosidosis. LAM has an acidic pH optimum at 4.0-4.5. It is stimulated by zinc ion and is inhibited by cobalt ion and plant alkaloids, such as swainsonine (SW). LAM catalyzes hydrolysis by a double displacement mechanism in which a glycosyl-enzyme intermediate is formed and hydrolyzed via oxacarbenium ion-like transition states. A carboxylic acid in the active site acts as the catalytic nucleophile in the formation of the covalent intermediate while a second carboxylic acid acts as a general acid catalyst. The same residue is thought to assist in the hydrolysis (deglycosylation) step, this time acting as a general base.


Pssm-ID: 212121 [Multi-domain]  Cd Length: 278  Bit Score: 233.64  E-value: 1.20e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679   132 LQVFVVPHSHNDPGWLKTFNDYF--------RDKTQYIFNNMVLKLKEDSSRKFIWSEISYLAKWWDIIDNPKKEAVKSL 203
Cdd:cd10810   1 LNVHLVPHTHDDVGWLKTVDQYYygsnnsiqHAGVQYILDSVIEELLKNPDRKFIYVEIAFFSRWWREQSEDTRQKVKKL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679   204 LQNGQLEIVTGGWVMADEATTHYFALIDQLIEGHQWLEKNLGV--KPRSGWAIDPFGHSPTMTYLLKRAGFSHMLIQRVH 281
Cdd:cd10810  81 VKNGQLEFINGGWCMNDEATTHYEDIIDQMTLGHQFLKDTFGEcaRPRVGWQIDPFGHSRTQASLFAQMGFDGLFFGRID 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679   282 YSVKKHFSLQKTLEFFWRQNWDLGSTTDILCHMMPFYsYDIPH------TCGPDPKIccqfDFKRLPGgrYgcpwgvppe 355
Cdd:cd10810 161 YQDKAQRLKNKEMEFIWRGSPSLGPDADIFTGVLYNH-YGPPPgfcfdiLCGDEPIQ----DDPNLED--Y--------- 224

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 807679   356 aispgNVQSRAQMLLDQYRKKSKLFRTKVLLAPLGDDFRFSEYTEWdlqYRNYEQLFSYMNS 417
Cdd:cd10810 225 -----NVDERVDDFVQYAKEQAQHYRTNHIMLTMGSDFQYQNAEMW---FKNMDKLIKYVNK 278
GH38N_AMII_like cd10786
N-terminal catalytic domain of class II alpha-mannosidases and similar proteins; glycoside ...
 134-412 3.83e-68

N-terminal catalytic domain of class II alpha-mannosidases and similar proteins; glycoside hydrolase family 38 (GH38); Alpha-mannosidases (EC 3.2.1.24) are extensively found in eukaryotes and play important roles in the processing of newly formed N-glycans and in degradation of mature glycoproteins. A deficiency of this enzyme causes the lysosomal storage disease alpha-mannosidosis. Many bacterial and archaeal species also possess putative alpha-mannosidases, but their activity and specificity is largely unknown. Based on different functional characteristics and sequence homology, alpha-mannosidases have been organized into two classes (class I, belonging to glycoside hydrolase family 47, and class II, belonging to glycoside hydrolase family 38). Members of this family corresponds to class II alpha-mannosidases (alphaMII), which contain intermediate Golgi alpha-mannosidases II, acidic lysosomal alpha-mannosidases, animal sperm and epididymal alpha -mannosidases, neutral ER/cytosolic alpha-mannosidases, and some putative prokaryotic alpha-mannosidases. AlphaMII possess a-1,3, a-1,6, and a-1,2 hydrolytic activity, and catalyzes the degradation of N-linked oligosaccharides. The N-terminal catalytic domain of alphaMII adopts a structure consisting of parallel 7-stranded beta/alpha barrel. 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.


Pssm-ID: 212098 [Multi-domain]  Cd Length: 251  Bit Score: 218.42  E-value: 3.83e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679   134 VFVVPHSHNDPGWLKTFNDYFRDKTQYIFNNMVLKLKEDSSRKFIWSEISYLAKWWDiiDNPK-KEAVKSLLQNGQLEIV 212
Cdd:cd10786   2 VHLVPHSHYDVGWLQTFEQYYQINFKAILDKALRLLDANPEYKFLIEEVILLERYWD--VRPDlKAKLKQAVRSGRLEIA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679   213 TGGWVMADEATTHYFALIDQLIEGHQWLEKNLGVKPRSGWAIDPFGHSPTMTYLLKRAGFSHMLIQRVHYSVKKhfsLQK 292
Cdd:cd10786  80 GGGYVMPDTNLPDGESLVRQILLGKRWLKEFLGARPPVMWQADVFGHSPQLPQILAKSGFTGFAFGRGPYSQKR---MQR 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679   293 TLEFFWRQNWDlgstTDILCHMMPFYSYDIPHTCGPDpkiccqfdfkrlpggrygcpwgvPPEAISPGNVQSRAQMLLDQ 372
Cdd:cd10786 157 PSEFLWRGLDG----TRILTHWMPNGYSDGPFLCGPD-----------------------IPGDNSGPNALASLEALVEQ 209

                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 807679   373 YRKKSKLFRTKVLLAPLGDDFRFSEYTEWDLQYRNYEQLF 412
Cdd:cd10786 210 WKKLAELGATNHLLMPSGGDFTIPQADPLQVNQARLVEPW 249
GH38N_AMII_Epman_like cd10811
N-terminal catalytic domain of mammalian core-specific lysosomal alpha 1,6-mannosidase and ...
 132-453 1.34e-55

N-terminal catalytic domain of mammalian core-specific lysosomal alpha 1,6-mannosidase and similar proteins; glycoside hydrolase family 38 (GH38); The subfamily is represented by a novel human core-specific lysosomal alpha 1,6-mannosidase (Epman, Man2B2) and similar proteins. Although it was previously named as epididymal alpha-mannosidase, Epman has a broadly distributed transcript expression profile. Different from the major broad specificity lysosomal alpha-mannosidases (LAM, MAN2B1), Epman is not associated with genetic alpha-mannosidosis that is caused by the absence of LAM. Furthermore, Epman has unique substrate specificity. It can efficiently cleave only the alpha 1,6-linked mannose residue from (Man)3GlcNAc, but not (Man)3(GlcNAc)2 or other larger high mannose oligosaccharides, in the core of N-linked glycans. In contrast, the major LAM can cleave all of the alpha-linked mannose residues from high mannose oligosaccharides except the core alpha 1,6-linked mannose residue. Moreover, it is suggested that the catalytic activity of Epman is dependent on prior action by di-N-acetyl-chitobiase (chitobiase), which indicates there is a functional cooperation between these two enzymes for the full and efficient catabolism of mammalian lysosomal N-glycan core structures. Epman has an acidic pH optimum. It is strongly stimulated by cobalt or zinc ions and strongly inhibited by furanose analogues swainsonine (SW) and 1,4-dideoxy-1,4-imino-d-mannitol (DIM).


Pssm-ID: 212122 [Multi-domain]  Cd Length: 326  Bit Score: 188.56  E-value: 1.34e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679   132 LQVFVVPHSHNDPGWLKTFNDYFRDKTQYIFNNMVLKLKEDSSRKFIWSEISYLAKWWDII-DNPKKEAVKSLLQNGQLE 210
Cdd:cd10811   1 IQAFVIPHSHMDVGWVYTVQESMHAYAANVYTSVVEELMRGKQRRFIAVEQEFFRLWWDGVaTDKQKQQVRQLLSEGRLE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679   211 IVTGGWVMADEATTHYFALIDQLIEGHQWLEKNLGVKPRSGWAIDPFGHSPTMTYLLKRAGFSHMLIQRVHYSVKKHFSL 290
Cdd:cd10811  81 FVIGGQVMHDEAVTELDDQILQLTEGHGFLYETFGVRPRFSWHVDPFGASATTPTLFALAGFNAHLISRIDYDLKAAMQK 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679   291 QKTLEFFWRQNWDLGSTTDILCHMMPFYSYdiphtCGPdpkiccqfdfKRLP-GGRYGCPW-GV-----PP--------- 354
Cdd:cd10811 161 AKGLQFVWRGSPSLSESQEIFTHVMDQYSY-----CTP----------SYIPfSNRSGFYWnGVavfpdPPkdgiypnms 225

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679   355 EAISPGNVQSRAQMLLDQYRKKSKLFRTKVLLAPLGDDFRFSEYTewdLQYRNYEQLFSYMNSQ-PHLKVKIQFGTLSDY 433
Cdd:cd10811 226 LPVTTQNIHQYAETMVANIKQRAAWFRTPHVLWPWGCDKQFFNAS---VQFSNMDPLLDYINQHsSEFGVTVQYATLGDY 302

                       330       340
                ....*....|....*....|.
gi 807679   434 FDALEKS-VAAEKKGGQSVFP 453
Cdd:cd10811 303 FQALHNSnLTWEVRGSQDFLP 323
GH38-57_N_LamB_YdjC_SF cd10785
Catalytic domain of glycoside hydrolase (GH) families 38 and 57, lactam utilization protein ...
 135-313 2.56e-27

Catalytic domain of glycoside hydrolase (GH) families 38 and 57, lactam utilization protein LamB/YcsF family proteins, YdjC-family proteins, and similar proteins; The superfamily possesses strong sequence similarities across a wide range of all three kingdoms of life. It mainly includes four families, glycoside hydrolases family 38 (GH38), heat stable retaining glycoside hydrolases family 57 (GH57), lactam utilization protein LamB/YcsF family, and YdjC-family. The GH38 family corresponds to class II alpha-mannosidases (alphaMII, EC 3.2.1.24), which contain intermediate Golgi alpha-mannosidases II, acidic lysosomal alpha-mannosidases, animal sperm and epididymal alpha -mannosidases, neutral ER/cytosolic alpha-mannosidases, and some putative prokaryotic alpha-mannosidases. AlphaMII possess a-1,3, a-1,6, and a-1,2 hydrolytic activity, and catalyzes the degradation of N-linked oligosaccharides by employing a two-step mechanism involving the formation of a covalent glycosyl enzyme complex. GH57 is a purely prokaryotic family with the majority of thermostable enzymes from extremophiles (many of them are archaeal hyperthermophiles), which exhibit the enzyme specificities of alpha-amylase (EC 3.2.1.1), 4-alpha-glucanotransferase (EC 2.4.1.25), amylopullulanase (EC 3.2.1.1/41), and alpha-galactosidase (EC 3.2.1.22). This family also includes many hypothetical proteins with uncharacterized activity and specificity. GH57 cleaves alpha-glycosidic bond by employing a retaining mechanism, which involves a glycosyl-enzyme intermediate, allowing transglycosylation. Although the exact molecular function of LamB/YcsF family and YdjC-family remains unclear, they show high sequence and structure homology to the members of GH38 and GH57. Their catalytic domains adopt a similar parallel 7-stranded beta/alpha barrel, which is remotely related to catalytic NodB homology domain of the carbohydrate esterase 4 superfamily.


Pssm-ID: 212097 [Multi-domain]  Cd Length: 203  Bit Score: 108.50  E-value: 2.56e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679   135 FVVPHSHNDPGWLKTFNDYFRDKTQYIFNNMVLKLKEDSSRKFIWSEISYLAKWWDIIDNPKKEAVKSLLQNGQLEIVTG 214
Cdd:cd10785   1 FINAHSHNPYVWIQTFEEWYFEATKATYIPLLMHFHRNFEMSFNIAPISYEALFYHDLGENIKLQMKSIQKNGQLEIGTH 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679   215 GWVMAD--EATTHYFALIDQLIEGHQWLEKNLGVKPRSGWAIDPFG-----HSPTMTYLLKRAGFSHMLIQRVHYSVKKH 287
Cdd:cd10785  81 GATHPDesEAQSHPENVYAQITEGITWLEKHMGVTPRHIWLHECFYnqakqLSQGIPYILQKSGFLYLFVQSRSISVKKE 160

                       170       180
                ....*....|....*....|....*.
gi 807679   288 FSLqktleffWRQNWDLGSTTDILCH 313
Cdd:cd10785 161 LAL-------WRQIWYNKKDSGVFTF 179
GH38N_AMII_ER_cytosolic cd10789
N-terminal catalytic domain of endoplasmic reticulum(ER)/cytosolic class II alpha-mannosidases; ...
 133-325 2.72e-14

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.


Pssm-ID: 212101 [Multi-domain]  Cd Length: 252  Bit Score: 72.54  E-value: 2.72e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679   133 QVFVVPHSHNDPGWLKTFNDYfRDKTQYIFNNMVLKLKEDSSRKFIWSEISYLAkwWDIIDNPKK-EAVKSLLQNGQLEI 211
Cdd:cd10789   1 KIYAVGHAHIDLAWLWPVRET-RRKAARTFSTVLDLMEEYPDFVFTQSQAQLYE--WLEEDYPELfERIKERVKEGRWEP 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679   212 VTGGWVMAD------EAtthyfaLIDQLIEGHQWLEKNLGVKPRSGWAIDPFGHSPTMTYLLKRAGFSHMLIQRVHYSVK 285
Cdd:cd10789  78 VGGMWVEPDcnlpsgES------LVRQFLYGQRYFREEFGVESRILWLPDSFGFSAALPQILKKSGIDYFVTQKLSWNDT 151

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 807679   286 KHFSLQKtleFFWRQNwDlGSttDILCHMMPFYSYDIPHT 325
Cdd:cd10789 152 NKFPYDT---FRWRGI-D-GS--EVLAHFIPTGYYNGDLT 184
GH38N_AMII_ScAms1_like cd10812
N-terminal catalytic domain of yeast vacuolar alpha-mannosidases and similar proteins; ...
 133-321 1.37e-09

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.


Pssm-ID: 212123 [Multi-domain]  Cd Length: 258  Bit Score: 58.60  E-value: 1.37e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679   133 QVFVVPHSHNDPGWLKTFnDYFRDKTQYIFNNMVLKLKEDSSRKFIWSEISYLaKWWDIIDNPKKEAVKSLLQNGQLEIV 212
Cdd:cd10812   1 NVYGIGNCHIDTAWLWPF-SETQQKVARSWSTQCDLMDRYPEYRFVASQAQQF-KWLETLYPDLFEKVKEYVKQGRFHPI 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679   213 TGGWVMADEATTHYFALIDQLIEGHQWLEKNLGVKPRSGWAIDPFGHSPTMTYLLKRAGFSHMLIQRVHYSVKKHFSlQK 292
Cdd:cd10812  79 GGSWVENDTNMPSGESLARQFLYGQRYFESRFGKRCDTFWLPDTFGYSSQIPQLCRLAGMDYFFTQKLSWNNINSFP-HS 157

                       170       180
                ....*....|....*....|....*....
gi 807679   293 TLeffwrqNWDLGSTTDILCHMMPFYSYD 321
Cdd:cd10812 158 TF------NWVGIDGTQVLVHMTPVNTYT 180
GH38N_AMII_Man2C1 cd10813
N-terminal catalytic domain of mammalian cytosolic alpha-mannosidase Man2C1 and similar ...
 133-320 1.44e-06

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.


Pssm-ID: 212124 [Multi-domain]  Cd Length: 252  Bit Score: 49.70  E-value: 1.44e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679   133 QVFVVPHSHNDPGWLKTFNDYFRdKTQYIFNNMVLKLKEDSSRKFIWSEISYLAkwWDIIDNPK-KEAVKSLLQNGQLEI 211
Cdd:cd10813   1 TIHAMGHCHIDSAWLWPYEETIR-KCARSWVTVLRLMEDYPDFTFACSQAQQLE--WVKSWYPGlYEEIQERVKNGRFIP 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679   212 VTGGWVMADEATTHYFALIDQLIEGHQWLEKNLGVKPRSGWAIDPFGHSPTMTYLLKRAGFSHMLIQRVHYSVKKHFSLQ 291
Cdd:cd10813  78 VGGTWVEMDGNLPSGESMVRQFLYGQRFFKEEFGITCKEFWLPDTFGYSAQLPQIMKGCGISRFLTQKLSWNLVNKFPHH 157

                       170       180
                ....*....|....*....|....*....
gi 807679   292 KtleFFWrQNWDlGSTtdILCHMMPFYSY 320
Cdd:cd10813 158 T---FFW-EGID-GSR--VLTHFPPGDSY 179
GH38N_AMII_SpGH38_like cd10814
N-terminal catalytic domain of SPGH38, a putative alpha-mannosidase of Streptococcus pyogenes, ...
 133-299 5.07e-05

N-terminal catalytic domain of SPGH38, a putative alpha-mannosidase of Streptococcus pyogenes, and its prokaryotic homologs; glycoside hydrolase family 38 (GH38); The subfamily is represented by SpGH38 of Streptococcus pyogenes, which has been assigned as a putative alpha-mannosidase, and is encoded by ORF spy1604. SpGH38 appears to exist as an elongated dimer and display alpha-1,3 mannosidase activity. It is active on disaccharides and some aryl glycosides. SpGH38 can also effectively deglycosylate human N-glycans in vitro. A divalent metal ion, such as a zinc ion, is required for its activity. SpGH38 is inhibited by swainsonine. The absence of any secretion signal peptide suggests that SpGH38 may be intracellular.


Pssm-ID: 212125 [Multi-domain]  Cd Length: 271  Bit Score: 44.94  E-value: 5.07e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679   133 QVFVVPHSHNDPGWLKTFnDYFRDKTQYIFNNMVLKLKEDSS-RKF------IWSEiSYLAkwwdiIDNPKKEAVKSLLQ 205
Cdd:cd10814   1 KVHIISHTHWDREWYLPF-EEFRMRLIDLIDRLLELLEEDPEfKSFhldgqtIVLE-DYLE-----VRPEKRERLKKLIR 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679   206 NGQLEIvtGGW-VMADEATTHYFALIDQLIEGHQWLEKnLGVKPRSGWAIDPFGHSPTMTYLLKRAGFSHMLIQRvhySV 284
Cdd:cd10814  74 EGKLVI--GPWyVLQDEFLTSGEANIRNLLIGKKVAEE-FGKSMKIGYFPDTFGHIGQMPQILKGFGIDNAVFGR---GV 147

                       170
                ....*....|....*
gi 807679   285 KKHFSlqKTLEFFWR 299
Cdd:cd10814 148 KPTES--QYSEFWWE 160
Alpha-mann_mid smart00872
Alpha mannosidase, middle domain; Members of this entry belong to the glycosyl hydrolase ...
 469-487 5.29e-05

Alpha mannosidase, middle domain; Members of this entry belong to the glycosyl hydrolase family 38, This domain, which is found in the central region adopts a structure consisting of three alpha helices, in an immunoglobulin/albumin-binding domain-like fold. The domain is predominantly found in the enzyme alpha-mannosidase.


Pssm-ID: 214875 [Multi-domain]  Cd Length: 79  Bit Score: 41.38  E-value: 5.29e-05
                           10
                   ....*....|....*....
gi 807679      469 YWSGYFTSRPFYKRMDRIM 487
Cdd:smart00872   1 YHRGTYTSRPYLKRLNRRA 19
Alpha-mann_mid pfam09261
Alpha mannosidase middle domain; Members of this family adopt a structure consisting of three ...
 468-487 9.58e-05

Alpha mannosidase middle domain; Members of this family adopt a structure consisting of three alpha helices, in an immunoglobulin/albumin-binding domain-like fold. They are predominantly found in the enzyme alpha-mannosidase.


Pssm-ID: 462728 [Multi-domain]  Cd Length: 98  Bit Score: 41.48  E-value: 9.58e-05
                          10        20
                  ....*....|....*....|
gi 807679     468 HYWSGYFTSRPFYKRMDRIM 487
Cdd:pfam09261   1 EYHRGTYTSRADLKRLNRKL 20
GH38N_AMII_like_1 cd10791
N-terminal catalytic domain of mainly uncharacterized eukaryotic proteins similar to ...
 133-299 9.71e-05

N-terminal catalytic domain of mainly uncharacterized eukaryotic proteins similar to alpha-mannosidases; glycoside hydrolase family 38 (GH38); The subfamily of mainly uncharacterized eukaryotic proteins shows sequence homology with class II alpha-mannosidases (AlphaAMIIs). AlphaAMIIs possess a-1,3, a-1,6, and a-1,2 hydrolytic activity, and catalyze the degradation of N-linked oligosaccharides. The N-terminal catalytic domain of alphaMII adopts a structure consisting of parallel 7-stranded beta/alpha barrel. This subfamily belongs to the GH38 family of retaining glycosyl hydrolases, which employ 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.


Pssm-ID: 212103 [Multi-domain]  Cd Length: 254  Bit Score: 43.84  E-value: 9.71e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679   133 QVFVVPHSHNDPGWLKT---FNDYFRDktqYIFNNMVLKLK---EDSSRKFIWS-EISYLAK-WWDIIDNPKKEAVKSLL 204
Cdd:cd10791   1 TVHVVHHSHTDIGYTDLqekVDRYHVD---YIPQALDLAEAtknYPEDARFRWTtESTWLVEeYLKCASPEQRERLEQAV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679   205 QNGQLEIVTGGWVMADEATTHyfALIDQLIEGHQWLEKNLGVKPRSGWAIDPFGHSPTMTYLLKRAGfshmlIQRVHYSV 284
Cdd:cd10791  78 RRGRIGWHALPLNITTELMDE--ELLRRGLYLSKELDRRFGLPIIVAMQTDVPGHTWGLVDVLADAG-----IKYLSIGV 150

                       170
                ....*....|....*....
gi 807679   285 KKHFSL----QKTLeFFWR 299
Cdd:cd10791 151 NGHSGPypprVPGP-FYWE 168
Glyco_hydro_57 pfam03065
Glycosyl hydrolase family 57; This family includes alpha-amylase (EC:3.2.1.1), ...
 119-276 9.77e-03

Glycosyl hydrolase family 57; This family includes alpha-amylase (EC:3.2.1.1), 4--glucanotransferase (EC:2.4.1.-) and amylopullulanase enzymes.


Pssm-ID: 397267 [Multi-domain]  Cd Length: 293  Bit Score: 38.11  E-value: 9.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679     119 DIKYEADEWDREPLQVFVVPHSHNDPGWLKTFNDYFRDKTQYIFNNMVLKLKEDSSRKFIWSEISYLAKWWDIIDNPKKE 198
Cdd:pfam03065  13 RPGEYGLPWVREHATEDYIDLLLNLEIFPRVHEKSYLPATELLLELIEKGLERCGDLKFNLSISGPLLEQAQKWNPEVLE 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807679     199 AVKSLLQNGQLEIVTGGWvmadeatTH-YFALID-------QLIEGHQWLEKNLGVKPRSGWAIDpFGHSPTMTYLLKRA 270
Cdd:pfam03065  93 LFRELAESGQVELLTSPY-------YHpLLPLLPdsedfiaQVKMARELYREYFGVEPRGFWLPE-LAYSPDILKILAEL 164


                  ....*.
gi 807679     271 GFSHML 276
Cdd:pfam03065 165 GFEYVF 170
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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