NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|767935902|ref|XP_011541697|]
View 

alpha-mannosidase 2 isoform X3 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PLN02701 super family cl26659
alpha-mannosidase
128-857 0e+00

alpha-mannosidase


The actual alignment was detected with superfamily member PLN02701:

Pssm-ID: 178304 [Multi-domain]  Cd Length: 1050  Bit Score: 796.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902  128 DVQMLDVYSLISFDNPDGGVWKQGFDITYESNEWDTEPLQVFVVPHSHNDPGWLKTFNDYFRDKTQYIFNNMVLKLKEDS 207
Cdd:PLN02701    2 DITTKDLYDRIEFLDKDGGAWKQGWRVKYRGDEWDREKLKVFVVPHSHNDPGWILTVEEYYQEQSRHILDTIVESLSKDP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902  208 RRKFIWSEISYLSKWWDIIDIQKKDAVKSLIENGQLEIVTGGWVMPDEATPHYFALIDQLIEGHQWLENNIGVKPRSGWA 287
Cdd:PLN02701   82 RRKFIWEEMSYLERWWRDASPSKKEAFTKLVKNGQLEIVGGGWVMNDEANSHYFAIIEQITEGNMWLNDTIGVAPKNSWA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902  288 IDPFGHSPTMAYLLNRAGLSHMLIQRVHYAVKKHFALHKTLEFFWRQNWDLGSVTDILCHMMPFYSYDIPHTCGPDPKIC 367
Cdd:PLN02701  162 IDPFGYSSTMAYLLRRMGFENMLIQRTHYEVKKELAQNKNLEYIWRQSWDAEETTDIFVHMMPFYSYDIPHTCGPEPAIC 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902  368 CQFDFKRLPGGRFG-CPWGVPPETIHPGNVQSRARMLLDQYRKKSKLFRTKVLLAPLGDDFRYCEYTEWDLQFKNYQQLF 446
Cdd:PLN02701  242 CQFDFARMRGFQYElCPWGKHPVETNDENVQERAMKLLDQYRKKSTLYRTNTLLVPLGDDFRYISIDEAEAQFRNYQKLF 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902  447 DYMNSQSKFKVKIQFGTLSDFFDAL-DKADETQRDKGQSM-------FPVLSGDFFTYADRDDHYWSGYFTSRPFYKRMD 518
Cdd:PLN02701  322 DYINSNPSLKAEVKFGTLEDYFSTLrDEADRINYSRPGEVgsgevpgFPSLSGDFFTYADRQQDYWSGYYVSRPFFKAVD 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902  519 RIMESHLRAAEILYYFALRQAHKYKINKFLSSSLYtALTEARRNLGLFQHHDAITGTAKDWVVVDYGTRLFHSLMVLEKI 598
Cdd:PLN02701  402 RVLEQTLRAAEILFSFLLGYCRRFQCEKLPTSFSY-KLTAARRNLALFQHHDGVTGTAKDHVVVDYGTRMHTSLQDLQIF 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902  599 IGNS--AFLLILKDKltydSYSPDTFLEMDLKQKSQDSLPQKNIIRLSA-EPRYLVVYNPLEQDRISLVSVYVSSPTVQV 675
Cdd:PLN02701  481 MSAAveVLLGIRHEK----SDQTPSWFEPEQSRSKYDMLPVHKVINLREgKAHRVVFFNPLEQTREEVVMVVVDRPAVCV 556
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902  676 FSASGKPVEVQVSAVWDTANT-ISETAYEISFRAHIPPLGLKVYKIlesASSNSHLADYVLYKNKVedsgiFTIKNMI-- 752
Cdd:PLN02701  557 FDSNWTCVPSQISPEWQHDGEkLFTGRHRLYWKASVPALGLETYFI---ANGNVSCEKAVPAKLKV-----FNSDDKFpc 628
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902  753 ------NTEEGITLE--NSFVLLRFD-QTGLMKQMMTKEDGKHHEVNVQFSWYGTTikrdKSGAYLFLPDGNAKPYVYTT 823
Cdd:PLN02701  629 pepyscSKLEGDTVEisNSHQTLGFDvKTGLLRKIKIHKNGSETVVGEEIGMYSSQ----GSGAYLFKPDGEAQPIVQAG 704
                         730       740       750       760
                  ....*....|....*....|....*....|....*....|....
gi 767935902  824 PPFVrVTHGRIYSEV------TCFFDHVTHRVRLYH----IQGM 857
Cdd:PLN02701  705 GLVV-VSEGPLVQEVhsvpktKWEKSPLSRSTRLYHggksVQDL 747
 
Name Accession Description Interval E-value
PLN02701 PLN02701
alpha-mannosidase
128-857 0e+00

alpha-mannosidase


Pssm-ID: 178304 [Multi-domain]  Cd Length: 1050  Bit Score: 796.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902  128 DVQMLDVYSLISFDNPDGGVWKQGFDITYESNEWDTEPLQVFVVPHSHNDPGWLKTFNDYFRDKTQYIFNNMVLKLKEDS 207
Cdd:PLN02701    2 DITTKDLYDRIEFLDKDGGAWKQGWRVKYRGDEWDREKLKVFVVPHSHNDPGWILTVEEYYQEQSRHILDTIVESLSKDP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902  208 RRKFIWSEISYLSKWWDIIDIQKKDAVKSLIENGQLEIVTGGWVMPDEATPHYFALIDQLIEGHQWLENNIGVKPRSGWA 287
Cdd:PLN02701   82 RRKFIWEEMSYLERWWRDASPSKKEAFTKLVKNGQLEIVGGGWVMNDEANSHYFAIIEQITEGNMWLNDTIGVAPKNSWA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902  288 IDPFGHSPTMAYLLNRAGLSHMLIQRVHYAVKKHFALHKTLEFFWRQNWDLGSVTDILCHMMPFYSYDIPHTCGPDPKIC 367
Cdd:PLN02701  162 IDPFGYSSTMAYLLRRMGFENMLIQRTHYEVKKELAQNKNLEYIWRQSWDAEETTDIFVHMMPFYSYDIPHTCGPEPAIC 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902  368 CQFDFKRLPGGRFG-CPWGVPPETIHPGNVQSRARMLLDQYRKKSKLFRTKVLLAPLGDDFRYCEYTEWDLQFKNYQQLF 446
Cdd:PLN02701  242 CQFDFARMRGFQYElCPWGKHPVETNDENVQERAMKLLDQYRKKSTLYRTNTLLVPLGDDFRYISIDEAEAQFRNYQKLF 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902  447 DYMNSQSKFKVKIQFGTLSDFFDAL-DKADETQRDKGQSM-------FPVLSGDFFTYADRDDHYWSGYFTSRPFYKRMD 518
Cdd:PLN02701  322 DYINSNPSLKAEVKFGTLEDYFSTLrDEADRINYSRPGEVgsgevpgFPSLSGDFFTYADRQQDYWSGYYVSRPFFKAVD 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902  519 RIMESHLRAAEILYYFALRQAHKYKINKFLSSSLYtALTEARRNLGLFQHHDAITGTAKDWVVVDYGTRLFHSLMVLEKI 598
Cdd:PLN02701  402 RVLEQTLRAAEILFSFLLGYCRRFQCEKLPTSFSY-KLTAARRNLALFQHHDGVTGTAKDHVVVDYGTRMHTSLQDLQIF 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902  599 IGNS--AFLLILKDKltydSYSPDTFLEMDLKQKSQDSLPQKNIIRLSA-EPRYLVVYNPLEQDRISLVSVYVSSPTVQV 675
Cdd:PLN02701  481 MSAAveVLLGIRHEK----SDQTPSWFEPEQSRSKYDMLPVHKVINLREgKAHRVVFFNPLEQTREEVVMVVVDRPAVCV 556
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902  676 FSASGKPVEVQVSAVWDTANT-ISETAYEISFRAHIPPLGLKVYKIlesASSNSHLADYVLYKNKVedsgiFTIKNMI-- 752
Cdd:PLN02701  557 FDSNWTCVPSQISPEWQHDGEkLFTGRHRLYWKASVPALGLETYFI---ANGNVSCEKAVPAKLKV-----FNSDDKFpc 628
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902  753 ------NTEEGITLE--NSFVLLRFD-QTGLMKQMMTKEDGKHHEVNVQFSWYGTTikrdKSGAYLFLPDGNAKPYVYTT 823
Cdd:PLN02701  629 pepyscSKLEGDTVEisNSHQTLGFDvKTGLLRKIKIHKNGSETVVGEEIGMYSSQ----GSGAYLFKPDGEAQPIVQAG 704
                         730       740       750       760
                  ....*....|....*....|....*....|....*....|....
gi 767935902  824 PPFVrVTHGRIYSEV------TCFFDHVTHRVRLYH----IQGM 857
Cdd:PLN02701  705 GLVV-VSEGPLVQEVhsvpktKWEKSPLSRSTRLYHggksVQDL 747
GH38N_Man2A1 cd11666
N-terminal catalytic domain of Golgi alpha-mannosidase II and similar proteins; glycoside ...
165-508 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: 776.06  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 165 PLQVFVVPHSHNDPGWLKTFNDYFRDKTQYIFNNMVLKLKEDSRRKFIWSEISYLSKWWDIIDIQKKDAVKSLIENGQLE 244
Cdd:cd11666    1 PLQVFVVPHSHNDPGWLKTFDDYFRDQTQHILNNMVLKLKEDSRRKFIWSEISYFAKWWDIIDGQKKDAVKRLIENGQLE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 245 IVTGGWVMPDEATPHYFALIDQLIEGHQWLENNIGVKPRSGWAIDPFGHSPTMAYLLNRAGLSHMLIQRVHYAVKKHFAL 324
Cdd:cd11666   81 IVTGGWVMPDEATAHYFALIDQLIEGHQWLERNLGVKPKSGWAVDPFGHSPTMAYLLKRAGLSNMLIQRVHYSVKKHFSL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 325 HKTLEFFWRQNWDLGSVTDILCHMMPFYSYDIPHTCGPDPKICCQFDFKRLPGGRFGCPWGVPPETIHPGNVQSRARMLL 404
Cdd:cd11666  161 QKTLEFFWRQNWDLGSSTDILCHMMPFYSYDVPHTCGPDPKICCQFDFKRLPGGRISCPWRVPPEAIHPGNVQSRAQMLL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 405 DQYRKKSKLFRTKVLLAPLGDDFRYCEYTEWDLQFKNYQQLFDYMNSQSKFKVKIQFGTLSDFFDALDKADETQRDKGQS 484
Cdd:cd11666  241 DQYRKKSKLFRTKVLLAPLGDDFRYTEYTEWDQQFENYQKLFDYMNSHPELHVKAQFGTLSDYFDALRKSTGMDPVGGQS 320
                        330       340
                 ....*....|....*....|....
gi 767935902 485 MFPVLSGDFFTYADRDDHYWSGYF 508
Cdd:cd11666  321 AFPVLSGDFFTYADRDDHYWSGYF 344
Glyco_hydro_38N pfam01074
Glycosyl hydrolases family 38 N-terminal domain; Glycosyl hydrolases are key enzymes of ...
167-497 9.62e-106

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: 327.66  E-value: 9.62e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902  167 QVFVVPHSHNDPGWLKTFNDYFRdKTQYIFNNMVLKLKEDSRRKFIWSEISYLSKWWDIIDIQKKdAVKSLIENGQLEIV 246
Cdd:pfam01074   1 TVHLVGHSHIDVGWLWTVDETRR-KVQRTFSSVLALLDRDPDRRFIWSEAQFFAWWWEDQPELFK-RIKKLVAEGRLEPV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902  247 TGGWVMPDEATPHYFALIDQLIEGHQWLENNIGVKPRSGWAIDPFGHSPTMAYLLNRAGLSHMLIQRVHYAVKKHFalHK 326
Cdd:pfam01074  79 GGGWVEPDENLPSGESLIRQFLYGQRFFKEEFGVRPRVGWLPDPFGYSATLPQILKQAGIDYFLTQRLHWNDKNKF--NP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902  327 TLEFFWRQNWDlgsvTDILCHMMPFYSYdiphtcgpdPKICCQFdfkrlpggrfgcpwgvppetihpgnvQSRARMLLDQ 406
Cdd:pfam01074 157 HLEFIWRGSDG----TEIFTHMPPFDYY---------PTYGFQF--------------------------QERAEDLLAY 197
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902  407 YRKKSKLFRTKVLLAPLGDDfryceytewDLQFKNYQQLFDYMNSQ--SKFKVKIQFGTLSDFFDALDKADetqrdkgqs 484
Cdd:pfam01074 198 ARNYADKTRTNHVLLPFGDG---------DGGGGPTDEMLEYINRWnaLPGLPKVQYGTPSDYFDALEKAT--------- 259
                         330
                  ....*....|...
gi 767935902  485 mFPVLSGDFFTYA 497
Cdd:pfam01074 260 -WPTKTDDFPPYA 271
Alpha-mann_mid smart00872
Alpha mannosidase, middle domain; Members of this entry belong to the glycosyl hydrolase ...
503-588 3.45e-32

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: 119.58  E-value: 3.45e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902   503 YWSGYFTSRPFYKRMDRIMESHLRAAEILYYFALRQAHKYKinkflssSLYTALTEARRNLGLFQHHDAITGTAKDWVVV 582
Cdd:smart00872   1 YHRGTYTSRPYLKRLNRRAESLLRAAEELAALAALLSLGYK-------YPSEQLEELWKALLLNQHHDAITGTSIDEVYD 73

                   ....*.
gi 767935902   583 DYGTRL 588
Cdd:smart00872  74 DYEKRL 79
MngB COG0383
Alpha-mannosidase [Carbohydrate transport and metabolism];
167-786 1.34e-28

Alpha-mannosidase [Carbohydrate transport and metabolism];


Pssm-ID: 440152 [Multi-domain]  Cd Length: 798  Bit Score: 123.03  E-value: 1.34e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 167 QVFVVPHSHNDPGWLKTFNDYFRdKTQYIFNNMVLKLKEDSRRKFIWSeISYLSKWWDIIDIQKKDAVKSLIENGQLEIV 246
Cdd:COG0383    7 KVHAVGHAHIDRAWLWPVEETRR-KLARTFSTVLDLLEEYPEFVFDGS-TAQLYDYLKEHYPELFERIKKLVKEGRWEPV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 247 TGGWVMPDEATPHYFALIDQLIEGHQWLENNIGVKPRSGWAIDPFGHSPTMAYLLNRAGLSHMLIQRVHYAVKKHFALHk 326
Cdd:COG0383   85 GGMWVEPDTNLPSGESLVRQLLYGQRFFKEEFGVDMKVGWLPDSFGYSAQLPQILKGAGIDYFVTQKGSWNDTNRFPYH- 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 327 tlEFFWRqnwdlgSV--TDILCHMMPF-YSYdiphtcgpdpkiccqfdfkrlpggrfgcpwGVPPETIHPgnvqsrarmL 403
Cdd:COG0383  164 --TFWWE------GIdgSEVLTHFFPNgYNS------------------------------GLDPEELAG---------A 196
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 404 LDQYRKKSklfRTKVLLAP--LGDD----FRycEYTEwdlqfkNYQQLfdymnSQSKFKVKIQFGTLSDFFDALDKADET 477
Cdd:COG0383  197 WRNFEQKA---VTDELLLPfgYGDGgggpTR--EMLE------RARRL-----NDLPGLPEVVISTPEDFFEALEEELPD 260
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 478 qrdkgqsmFPVLSGDFFTYADRddhywsGYFTSRPFYKRMDRIMESHLRAAEILYYFALRQAHKYKinkflssslYTALT 557
Cdd:COG0383  261 --------LPVWQGELYLELHR------GTYTSRADLKRLNRRAERLLREAEPLAALAALLGAEYP---------QEELD 317
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 558 EARRNLgLFQH-HDAITGTAKDWVVVDYGTRLFHSLMVLEKIIgNSAFLLILKdkltydsyspdtflEMDLKQKSQDslp 636
Cdd:COG0383  318 EAWKLL-LLNQfHDILPGSSIDEVYREAEARYEEALEEAESLI-DEALRAIAG--------------AIDLPEDGDP--- 378
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 637 qkniirlsaepryLVVYNPLEQDRISLVSV--YVSSPTVQVFSASGKPVEVQVSAvwdtantisetAYEISFRA-HIPPL 713
Cdd:COG0383  379 -------------LVVFNTLPWPRSEVVELplYTPGKNFQLVDSDGKELPAQILE-----------DGKILFSAeDLPAL 434
                        570       580       590       600       610       620       630
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767935902 714 GLKVYKILESASSNSHLAdyvlyknkvedsgiftiknminTEEGITLENSFVLLRFDQTGLMKQMMTKEDGKH 786
Cdd:COG0383  435 GYKTLSLVEGEASPESSV----------------------SVSENVLENEFLRVEIDENGSLTSIYDKETGRE 485
 
Name Accession Description Interval E-value
PLN02701 PLN02701
alpha-mannosidase
128-857 0e+00

alpha-mannosidase


Pssm-ID: 178304 [Multi-domain]  Cd Length: 1050  Bit Score: 796.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902  128 DVQMLDVYSLISFDNPDGGVWKQGFDITYESNEWDTEPLQVFVVPHSHNDPGWLKTFNDYFRDKTQYIFNNMVLKLKEDS 207
Cdd:PLN02701    2 DITTKDLYDRIEFLDKDGGAWKQGWRVKYRGDEWDREKLKVFVVPHSHNDPGWILTVEEYYQEQSRHILDTIVESLSKDP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902  208 RRKFIWSEISYLSKWWDIIDIQKKDAVKSLIENGQLEIVTGGWVMPDEATPHYFALIDQLIEGHQWLENNIGVKPRSGWA 287
Cdd:PLN02701   82 RRKFIWEEMSYLERWWRDASPSKKEAFTKLVKNGQLEIVGGGWVMNDEANSHYFAIIEQITEGNMWLNDTIGVAPKNSWA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902  288 IDPFGHSPTMAYLLNRAGLSHMLIQRVHYAVKKHFALHKTLEFFWRQNWDLGSVTDILCHMMPFYSYDIPHTCGPDPKIC 367
Cdd:PLN02701  162 IDPFGYSSTMAYLLRRMGFENMLIQRTHYEVKKELAQNKNLEYIWRQSWDAEETTDIFVHMMPFYSYDIPHTCGPEPAIC 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902  368 CQFDFKRLPGGRFG-CPWGVPPETIHPGNVQSRARMLLDQYRKKSKLFRTKVLLAPLGDDFRYCEYTEWDLQFKNYQQLF 446
Cdd:PLN02701  242 CQFDFARMRGFQYElCPWGKHPVETNDENVQERAMKLLDQYRKKSTLYRTNTLLVPLGDDFRYISIDEAEAQFRNYQKLF 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902  447 DYMNSQSKFKVKIQFGTLSDFFDAL-DKADETQRDKGQSM-------FPVLSGDFFTYADRDDHYWSGYFTSRPFYKRMD 518
Cdd:PLN02701  322 DYINSNPSLKAEVKFGTLEDYFSTLrDEADRINYSRPGEVgsgevpgFPSLSGDFFTYADRQQDYWSGYYVSRPFFKAVD 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902  519 RIMESHLRAAEILYYFALRQAHKYKINKFLSSSLYtALTEARRNLGLFQHHDAITGTAKDWVVVDYGTRLFHSLMVLEKI 598
Cdd:PLN02701  402 RVLEQTLRAAEILFSFLLGYCRRFQCEKLPTSFSY-KLTAARRNLALFQHHDGVTGTAKDHVVVDYGTRMHTSLQDLQIF 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902  599 IGNS--AFLLILKDKltydSYSPDTFLEMDLKQKSQDSLPQKNIIRLSA-EPRYLVVYNPLEQDRISLVSVYVSSPTVQV 675
Cdd:PLN02701  481 MSAAveVLLGIRHEK----SDQTPSWFEPEQSRSKYDMLPVHKVINLREgKAHRVVFFNPLEQTREEVVMVVVDRPAVCV 556
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902  676 FSASGKPVEVQVSAVWDTANT-ISETAYEISFRAHIPPLGLKVYKIlesASSNSHLADYVLYKNKVedsgiFTIKNMI-- 752
Cdd:PLN02701  557 FDSNWTCVPSQISPEWQHDGEkLFTGRHRLYWKASVPALGLETYFI---ANGNVSCEKAVPAKLKV-----FNSDDKFpc 628
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902  753 ------NTEEGITLE--NSFVLLRFD-QTGLMKQMMTKEDGKHHEVNVQFSWYGTTikrdKSGAYLFLPDGNAKPYVYTT 823
Cdd:PLN02701  629 pepyscSKLEGDTVEisNSHQTLGFDvKTGLLRKIKIHKNGSETVVGEEIGMYSSQ----GSGAYLFKPDGEAQPIVQAG 704
                         730       740       750       760
                  ....*....|....*....|....*....|....*....|....
gi 767935902  824 PPFVrVTHGRIYSEV------TCFFDHVTHRVRLYH----IQGM 857
Cdd:PLN02701  705 GLVV-VSEGPLVQEVhsvpktKWEKSPLSRSTRLYHggksVQDL 747
GH38N_Man2A1 cd11666
N-terminal catalytic domain of Golgi alpha-mannosidase II and similar proteins; glycoside ...
165-508 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: 776.06  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 165 PLQVFVVPHSHNDPGWLKTFNDYFRDKTQYIFNNMVLKLKEDSRRKFIWSEISYLSKWWDIIDIQKKDAVKSLIENGQLE 244
Cdd:cd11666    1 PLQVFVVPHSHNDPGWLKTFDDYFRDQTQHILNNMVLKLKEDSRRKFIWSEISYFAKWWDIIDGQKKDAVKRLIENGQLE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 245 IVTGGWVMPDEATPHYFALIDQLIEGHQWLENNIGVKPRSGWAIDPFGHSPTMAYLLNRAGLSHMLIQRVHYAVKKHFAL 324
Cdd:cd11666   81 IVTGGWVMPDEATAHYFALIDQLIEGHQWLERNLGVKPKSGWAVDPFGHSPTMAYLLKRAGLSNMLIQRVHYSVKKHFSL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 325 HKTLEFFWRQNWDLGSVTDILCHMMPFYSYDIPHTCGPDPKICCQFDFKRLPGGRFGCPWGVPPETIHPGNVQSRARMLL 404
Cdd:cd11666  161 QKTLEFFWRQNWDLGSSTDILCHMMPFYSYDVPHTCGPDPKICCQFDFKRLPGGRISCPWRVPPEAIHPGNVQSRAQMLL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 405 DQYRKKSKLFRTKVLLAPLGDDFRYCEYTEWDLQFKNYQQLFDYMNSQSKFKVKIQFGTLSDFFDALDKADETQRDKGQS 484
Cdd:cd11666  241 DQYRKKSKLFRTKVLLAPLGDDFRYTEYTEWDQQFENYQKLFDYMNSHPELHVKAQFGTLSDYFDALRKSTGMDPVGGQS 320
                        330       340
                 ....*....|....*....|....
gi 767935902 485 MFPVLSGDFFTYADRDDHYWSGYF 508
Cdd:cd11666  321 AFPVLSGDFFTYADRDDHYWSGYF 344
GH38N_AMII_GMII_SfManIII_like cd10809
N-terminal catalytic domain of Golgi alpha-mannosidase II, Spodoptera frugiperda Sf9 ...
165-508 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: 685.92  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 165 PLQVFVVPHSHNDPGWLKTFNDYFRDKTQYIFNNMVLKLKEDSRRKFIWSEISYLSKWWDIIDIQKKDAVKSLIENGQLE 244
Cdd:cd10809    1 KLKVFVVPHSHNDPGWIKTFEEYYQDQTKHILDNMVDKLSKNPKMKFIWAEISFLERWWDDASPDKKEAVKKLVKNGQLE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 245 IVTGGWVMPDEATPHYFALIDQLIEGHQWLENNIGVKPRSGWAIDPFGHSPTMAYLLNRAGLSHMLIQRVHYAVKKHFAL 324
Cdd:cd10809   81 IVTGGWVMTDEANSHYFAMIDQLIEGHQWLKENLGVKPKSGWSIDPFGHSPTMPYLLKRAGFKNMVIQRIHYEVKKYLAQ 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 325 HKTLEFFWRQNWDLGSVTDILCHMMPFYSYDIPHTCGPDPKICCQFDFKRLPGGRFGCPWGVPPETIHPGNVQSRARMLL 404
Cdd:cd10809  161 RKALEFMWRQYWDATGSTDILTHMMPFYSYDIPHTCGPDPAVCCQFDFKRLPGGGESCPWKKPPQPITDDNVAERAELLL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 405 DQYRKKSKLFRTKVLLAPLGDDFRYCEYTEWDLQFKNYQQLFDYMNSQSKFKVKIQFGTLSDFFDALDKADETQrdkgQS 484
Cdd:cd10809  241 DQYRKKSQLYRSNVVLIPLGDDFRYDSDEEWDAQYDNYQKLFDYINSNPELNVEIQFGTLSDYFNALRKRTGTN----TP 316
                        330       340
                 ....*....|....*....|....
gi 767935902 485 MFPVLSGDFFTYADRDDHYWSGYF 508
Cdd:cd10809  317 GFPTLSGDFFTYADRDDDYWSGYY 340
GH38N_Man2A2 cd11667
N-terminal catalytic domain of Golgi alpha-mannosidase IIx, and similar proteins; glycoside ...
165-508 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: 621.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 165 PLQVFVVPHSHNDPGWLKTFNDYFRDKTQYIFNNMVLKLKEDSRRKFIWSEISYLSKWWDIIDIQKKDAVKSLIENGQLE 244
Cdd:cd11667    1 PLQVFVVPHSHNDPGWIKTFDKYYYDQTQHILNSMVVKLQEDPRRRFIWSEISFFSKWWDNINAQKRAAVRRLVGNGQLE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 245 IVTGGWVMPDEATPHYFALIDQLIEGHQWLENNIGVKPRSGWAIDPFGHSPTMAYLLNRAGLSHMLIQRVHYAVKKHFAL 324
Cdd:cd11667   81 MATGGWVMPDEANSHYFAMIDQLIEGHQWLEKNIGVTPRSGWAVDPFGHSSTMPYILRRSNLTSMLIQRVHYAIKKHFAA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 325 HKTLEFFWRQNWDLGSVTDILCHMMPFYSYDIPHTCGPDPKICCQFDFKRLPGGRFGCPWGVPPETIHPGNVQSRARMLL 404
Cdd:cd11667  161 TQSLEFMWRQTWDPDSSTDIFCHMMPFYSYDVPHTCGPDPKICCQFDFKRLPGGRINCPWKVPPRAITEANVAERAQLLL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 405 DQYRKKSKLFRTKVLLAPLGDDFRYCEYTEWDLQFKNYQQLFDYMNSQSKFKVKIQFGTLSDFFDALDKADETQRDKGQS 484
Cdd:cd11667  241 DQYRKKSKLYRSKVLLVPLGDDFRYDKPQEWDAQFLNYQRLFDFLNSHPELHVQAQFGTLSDYFDALYKRTGVVPGMRPP 320
                        330       340
                 ....*....|....*....|....
gi 767935902 485 MFPVLSGDFFTYADRDDHYWSGYF 508
Cdd:cd11667  321 GFPVVSGDFFSYADREDHYWTGYY 344
Glyco_hydro_38N pfam01074
Glycosyl hydrolases family 38 N-terminal domain; Glycosyl hydrolases are key enzymes of ...
167-497 9.62e-106

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: 327.66  E-value: 9.62e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902  167 QVFVVPHSHNDPGWLKTFNDYFRdKTQYIFNNMVLKLKEDSRRKFIWSEISYLSKWWDIIDIQKKdAVKSLIENGQLEIV 246
Cdd:pfam01074   1 TVHLVGHSHIDVGWLWTVDETRR-KVQRTFSSVLALLDRDPDRRFIWSEAQFFAWWWEDQPELFK-RIKKLVAEGRLEPV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902  247 TGGWVMPDEATPHYFALIDQLIEGHQWLENNIGVKPRSGWAIDPFGHSPTMAYLLNRAGLSHMLIQRVHYAVKKHFalHK 326
Cdd:pfam01074  79 GGGWVEPDENLPSGESLIRQFLYGQRFFKEEFGVRPRVGWLPDPFGYSATLPQILKQAGIDYFLTQRLHWNDKNKF--NP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902  327 TLEFFWRQNWDlgsvTDILCHMMPFYSYdiphtcgpdPKICCQFdfkrlpggrfgcpwgvppetihpgnvQSRARMLLDQ 406
Cdd:pfam01074 157 HLEFIWRGSDG----TEIFTHMPPFDYY---------PTYGFQF--------------------------QERAEDLLAY 197
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902  407 YRKKSKLFRTKVLLAPLGDDfryceytewDLQFKNYQQLFDYMNSQ--SKFKVKIQFGTLSDFFDALDKADetqrdkgqs 484
Cdd:pfam01074 198 ARNYADKTRTNHVLLPFGDG---------DGGGGPTDEMLEYINRWnaLPGLPKVQYGTPSDYFDALEKAT--------- 259
                         330
                  ....*....|...
gi 767935902  485 mFPVLSGDFFTYA 497
Cdd:pfam01074 260 -WPTKTDDFPPYA 271
GH38N_AMII_euk cd00451
N-terminal catalytic domain of eukaryotic class II alpha-mannosidases; glycoside hydrolase ...
166-451 1.96e-102

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: 318.40  E-value: 1.96e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 166 LQVFVVPHSHNDPGWLKTFNDYFRDKTQYIFNNMVLKLKEDSRRKFIWSEISYLSKWWDIIDIQKKDAVKSLIENGQLEI 245
Cdd:cd00451    1 LNVHLIPHSHCDVGWLKTFDEYYNGDVKSILDSVVKALNNDPERKFIWAEIGFLERWWEDQGNDTKQQFKKLVKNGQLEF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 246 VTGGWVMPDEATPHYFALIDQLIEGHQWLENNIGVKPRSGWAIDPFGHSPTMAYLLNRAGLSHMLIQRVHYAVKKHFALH 325
Cdd:cd00451   81 VGGGWVMNDEACTTYESIIDQMTEGHQFLKDTFGVRPRVGWQIDPFGHSSTTPTLFSKMGFKGLVINRIPYSLKAEMKDN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 326 KTLEFFWRQNWDLGSVTDILCHMMP-FYSYDIPHTCGPDPkiccqfdfkrlpggrfgcpwgvppetIHPGNVQSRARMLL 404
Cdd:cd00451  161 KQLEFVWRGSPSLGPDSEIFTHVLDdHYSYPESLDFGGPP--------------------------ITDYNIAERADEFV 214
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 767935902 405 DQYRKKSKLFRTKVLLAPLGDDFRyceYTEWDLQFKNYQQLFDYMNS 451
Cdd:cd00451  215 EYIKKRSKTYRTNHILIPLGDDFR---FKNASLQFSNMDKLIAYINS 258
GH38N_AMII_LAM_like cd10810
N-terminal catalytic domain of lysosomal alpha-mannosidase and similar proteins; glycoside ...
166-451 1.20e-71

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: 237.50  E-value: 1.20e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 166 LQVFVVPHSHNDPGWLKTFNDYF--------RDKTQYIFNNMVLKLKEDSRRKFIWSEISYLSKWWDIIDIQKKDAVKSL 237
Cdd:cd10810    1 LNVHLVPHTHDDVGWLKTVDQYYygsnnsiqHAGVQYILDSVIEELLKNPDRKFIYVEIAFFSRWWREQSEDTRQKVKKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 238 IENGQLEIVTGGWVMPDEATPHYFALIDQLIEGHQWLENNIGV--KPRSGWAIDPFGHSPTMAYLLNRAGLSHMLIQRVH 315
Cdd:cd10810   81 VKNGQLEFINGGWCMNDEATTHYEDIIDQMTLGHQFLKDTFGEcaRPRVGWQIDPFGHSRTQASLFAQMGFDGLFFGRID 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 316 YAVKKHFALHKTLEFFWRQNWDLGSVTDILCHMmpFYSydipHTCGPDPkiccqFDFKRLPGGrfgcPWGVPPETIHPGN 395
Cdd:cd10810  161 YQDKAQRLKNKEMEFIWRGSPSLGPDADIFTGV--LYN----HYGPPPG-----FCFDILCGD----EPIQDDPNLEDYN 225
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767935902 396 VQSRARMLLDQYRKKSKLFRTKVLLAPLGDDFRYCEYTEWdlqFKNYQQLFDYMNS 451
Cdd:cd10810  226 VDERVDDFVQYAKEQAQHYRTNHIMLTMGSDFQYQNAEMW---FKNMDKLIKYVNK 278
GH38N_AMII_like cd10786
N-terminal catalytic domain of class II alpha-mannosidases and similar proteins; glycoside ...
168-451 2.25e-65

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: 219.19  E-value: 2.25e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 168 VFVVPHSHNDPGWLKTFNDYFRDKTQYIFNNmVLKLKEDSR-RKFIWSEISYLSKWWDIIDiQKKDAVKSLIENGQLEIV 246
Cdd:cd10786    2 VHLVPHSHYDVGWLQTFEQYYQINFKAILDK-ALRLLDANPeYKFLIEEVILLERYWDVRP-DLKAKLKQAVRSGRLEIA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 247 TGGWVMPDEATPHYFALIDQLIEGHQWLENNIGVKPRSGWAIDPFGHSPTMAYLLNRAGLSHMLIQRVHYAVKKhfaLHK 326
Cdd:cd10786   80 GGGYVMPDTNLPDGESLVRQILLGKRWLKEFLGARPPVMWQADVFGHSPQLPQILAKSGFTGFAFGRGPYSQKR---MQR 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 327 TLEFFWRQNWDlgsvTDILCHMMPFYSYDIPHTCGPDpkiccqfdfkrlpggrfgcpwgvPPETIHPGNVQSRARMLLDQ 406
Cdd:cd10786  157 PSEFLWRGLDG----TRILTHWMPNGYSDGPFLCGPD-----------------------IPGDNSGPNALASLEALVEQ 209
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 767935902 407 YRKKSKLFRTKVLLAPLGDDFRyceYTEWDLQFKNYQQLFDYMNS 451
Cdd:cd10786  210 WKKLAELGATNHLLMPSGGDFT---IPQADPLQVNQARLVEPWNS 251
GH38N_AMII_Epman_like cd10811
N-terminal catalytic domain of mammalian core-specific lysosomal alpha 1,6-mannosidase and ...
166-497 1.55e-52

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: 186.63  E-value: 1.55e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 166 LQVFVVPHSHNDPGWLKTFNDYFRDKTQYIFNNMVLKLKEDSRRKFIWSEISYLSKWWDII--DIQKKDaVKSLIENGQL 243
Cdd:cd10811    1 IQAFVIPHSHMDVGWVYTVQESMHAYAANVYTSVVEELMRGKQRRFIAVEQEFFRLWWDGVatDKQKQQ-VRQLLSEGRL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 244 EIVTGGWVMPDEATPHYFALIDQLIEGHQWLENNIGVKPRSGWAIDPFGHSPTMAYLLNRAGLSHMLIQRVHYAVKKHFA 323
Cdd:cd10811   80 EFVIGGQVMHDEAVTELDDQILQLTEGHGFLYETFGVRPRFSWHVDPFGASATTPTLFALAGFNAHLISRIDYDLKAAMQ 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 324 LHKTLEFFWRQNWDLGSVTDILCHMMPFYSYdiphtCGPdpkiccqfdfKRLP-GGRFGCPW-GV-----PP-------- 388
Cdd:cd10811  160 KAKGLQFVWRGSPSLSESQEIFTHVMDQYSY-----CTP----------SYIPfSNRSGFYWnGVavfpdPPkdgiypnm 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 389 -ETIHPGNVQSRARMLLDQYRKKSKLFRTKVLLAPLGDDFRYCEYTewdLQFKNYQQLFDYMNSQS-KFKVKIQFGTLSD 466
Cdd:cd10811  225 sLPVTTQNIHQYAETMVANIKQRAAWFRTPHVLWPWGCDKQFFNAS---VQFSNMDPLLDYINQHSsEFGVTVQYATLGD 301
                        330       340       350
                 ....*....|....*....|....*....|.
gi 767935902 467 FFDALDKADETQRDKGqsmfpvlSGDFFTYA 497
Cdd:cd10811  302 YFQALHNSNLTWEVRG-------SQDFLPYS 325
Alpha-mann_mid smart00872
Alpha mannosidase, middle domain; Members of this entry belong to the glycosyl hydrolase ...
503-588 3.45e-32

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: 119.58  E-value: 3.45e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902   503 YWSGYFTSRPFYKRMDRIMESHLRAAEILYYFALRQAHKYKinkflssSLYTALTEARRNLGLFQHHDAITGTAKDWVVV 582
Cdd:smart00872   1 YHRGTYTSRPYLKRLNRRAESLLRAAEELAALAALLSLGYK-------YPSEQLEELWKALLLNQHHDAITGTSIDEVYD 73

                   ....*.
gi 767935902   583 DYGTRL 588
Cdd:smart00872  74 DYEKRL 79
Alpha-mann_mid pfam09261
Alpha mannosidase middle domain; Members of this family adopt a structure consisting of three ...
502-606 1.48e-30

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: 115.82  E-value: 1.48e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902  502 HYWSGYFTSRPFYKRMDRIMESHLRAAEILYYFALRQAHKYKINkflssslYTALTEARRNLGLFQHHDAITGTAKDWVV 581
Cdd:pfam09261   1 EYHRGTYTSRADLKRLNRKLEHLLRAAEQLSSLAALSLLGYEYP-------KEELEELWKALLLNQFHDILPGSSIQEVY 73
                          90       100
                  ....*....|....*....|....*
gi 767935902  582 VDYGTRLFHSLMVLEKIIGNSAFLL 606
Cdd:pfam09261  74 RDAEARLAEALKETEKLLEDALRLL 98
MngB COG0383
Alpha-mannosidase [Carbohydrate transport and metabolism];
167-786 1.34e-28

Alpha-mannosidase [Carbohydrate transport and metabolism];


Pssm-ID: 440152 [Multi-domain]  Cd Length: 798  Bit Score: 123.03  E-value: 1.34e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 167 QVFVVPHSHNDPGWLKTFNDYFRdKTQYIFNNMVLKLKEDSRRKFIWSeISYLSKWWDIIDIQKKDAVKSLIENGQLEIV 246
Cdd:COG0383    7 KVHAVGHAHIDRAWLWPVEETRR-KLARTFSTVLDLLEEYPEFVFDGS-TAQLYDYLKEHYPELFERIKKLVKEGRWEPV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 247 TGGWVMPDEATPHYFALIDQLIEGHQWLENNIGVKPRSGWAIDPFGHSPTMAYLLNRAGLSHMLIQRVHYAVKKHFALHk 326
Cdd:COG0383   85 GGMWVEPDTNLPSGESLVRQLLYGQRFFKEEFGVDMKVGWLPDSFGYSAQLPQILKGAGIDYFVTQKGSWNDTNRFPYH- 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 327 tlEFFWRqnwdlgSV--TDILCHMMPF-YSYdiphtcgpdpkiccqfdfkrlpggrfgcpwGVPPETIHPgnvqsrarmL 403
Cdd:COG0383  164 --TFWWE------GIdgSEVLTHFFPNgYNS------------------------------GLDPEELAG---------A 196
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 404 LDQYRKKSklfRTKVLLAP--LGDD----FRycEYTEwdlqfkNYQQLfdymnSQSKFKVKIQFGTLSDFFDALDKADET 477
Cdd:COG0383  197 WRNFEQKA---VTDELLLPfgYGDGgggpTR--EMLE------RARRL-----NDLPGLPEVVISTPEDFFEALEEELPD 260
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 478 qrdkgqsmFPVLSGDFFTYADRddhywsGYFTSRPFYKRMDRIMESHLRAAEILYYFALRQAHKYKinkflssslYTALT 557
Cdd:COG0383  261 --------LPVWQGELYLELHR------GTYTSRADLKRLNRRAERLLREAEPLAALAALLGAEYP---------QEELD 317
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 558 EARRNLgLFQH-HDAITGTAKDWVVVDYGTRLFHSLMVLEKIIgNSAFLLILKdkltydsyspdtflEMDLKQKSQDslp 636
Cdd:COG0383  318 EAWKLL-LLNQfHDILPGSSIDEVYREAEARYEEALEEAESLI-DEALRAIAG--------------AIDLPEDGDP--- 378
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 637 qkniirlsaepryLVVYNPLEQDRISLVSV--YVSSPTVQVFSASGKPVEVQVSAvwdtantisetAYEISFRA-HIPPL 713
Cdd:COG0383  379 -------------LVVFNTLPWPRSEVVELplYTPGKNFQLVDSDGKELPAQILE-----------DGKILFSAeDLPAL 434
                        570       580       590       600       610       620       630
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767935902 714 GLKVYKILESASSNSHLAdyvlyknkvedsgiftiknminTEEGITLENSFVLLRFDQTGLMKQMMTKEDGKH 786
Cdd:COG0383  435 GYKTLSLVEGEASPESSV----------------------SVSENVLENEFLRVEIDENGSLTSIYDKETGRE 485
GH38-57_N_LamB_YdjC_SF cd10785
Catalytic domain of glycoside hydrolase (GH) families 38 and 57, lactam utilization protein ...
169-347 2.03e-26

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: 107.73  E-value: 2.03e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 169 FVVPHSHNDPGWLKTFNDYFRDKTQYIFNNMVLKLKEDSRRKFIWSEISYLSKWWDIIDIQKKDAVKSLIENGQLEIVTG 248
Cdd:cd10785    1 FINAHSHNPYVWIQTFEEWYFEATKATYIPLLMHFHRNFEMSFNIAPISYEALFYHDLGENIKLQMKSIQKNGQLEIGTH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 249 GWVMPD--EATPHYFALIDQLIEGHQWLENNIGVKPRSGWAIDPFG-----HSPTMAYLLNRAGLSHMLIQRVHYAVKKH 321
Cdd:cd10785   81 GATHPDesEAQSHPENVYAQITEGITWLEKHMGVTPRHIWLHECFYnqakqLSQGIPYILQKSGFLYLFVQSRSISVKKE 160
                        170       180
                 ....*....|....*....|....*.
gi 767935902 322 FALhktleffWRQNWDLGSVTDILCH 347
Cdd:cd10785  161 LAL-------WRQIWYNKKDSGVFTF 179
GH38N_AMII_ER_cytosolic cd10789
N-terminal catalytic domain of endoplasmic reticulum(ER)/cytosolic class II alpha-mannosidases; ...
167-359 4.04e-15

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: 76.01  E-value: 4.04e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 167 QVFVVPHSHNDPGWLKTFNDYfRDKTQYIFNNMVLKLKEDSRRKFIWSEiSYLSKWwdiidIQKKD-----AVKSLIENG 241
Cdd:cd10789    1 KIYAVGHAHIDLAWLWPVRET-RRKAARTFSTVLDLMEEYPDFVFTQSQ-AQLYEW-----LEEDYpelfeRIKERVKEG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 242 QLEIVTGGWVMPDEATPHYFALIDQLIEGHQWLENNIGVKPRSGWAIDPFGHSPTMAYLLNRAGLSHMLIQRVHYAVKKH 321
Cdd:cd10789   74 RWEPVGGMWVEPDCNLPSGESLVRQFLYGQRYFREEFGVESRILWLPDSFGFSAALPQILKKSGIDYFVTQKLSWNDTNK 153
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 767935902 322 FALHKtleFFWRQNwDlGSvtDILCHMMPFYSYDIPHT 359
Cdd:cd10789  154 FPYDT---FRWRGI-D-GS--EVLAHFIPTGYYNGDLT 184
Glyco_hydro_38C pfam07748
Glycosyl hydrolases family 38 C-terminal domain; Glycosyl hydrolases are key enzymes of ...
760-853 4.84e-12

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


Pssm-ID: 400208 [Multi-domain]  Cd Length: 204  Bit Score: 66.13  E-value: 4.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902  760 LENSFVLLRFD-QTGLMKQMMTKEDGKHH--EVNVQFSWYGTtiKRDKSGAYLFLPDGNAKPYVYTTPPFVRVTHGRIYS 836
Cdd:pfam07748   1 LENGFLKVEFDnDTGTLTSIYDKELSREVlaEVGNQFGLYED--IPGYSDAWDFRPFYEAKPLEVDEQSIEVVEDGPLVA 78
                          90       100
                  ....*....|....*....|.
gi 767935902  837 EVTCFF----DHVTHRVRLYH 853
Cdd:pfam07748  79 EVHVKFkiggSEISQVIRLYK 99
GH38N_AMII_ScAms1_like cd10812
N-terminal catalytic domain of yeast vacuolar alpha-mannosidases and similar proteins; ...
167-355 7.16e-11

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: 63.61  E-value: 7.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 167 QVFVVPHSHNDPGWLKTFnDYFRDKTQYIFNNMVLKLKEDSRRKFIWSEISYLsKWWDIIDIQKKDAVKSLIENGQLEIV 246
Cdd:cd10812    1 NVYGIGNCHIDTAWLWPF-SETQQKVARSWSTQCDLMDRYPEYRFVASQAQQF-KWLETLYPDLFEKVKEYVKQGRFHPI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 247 TGGWVMPDEATPHYFALIDQLIEGHQWLENNIGVKPRSGWAIDPFGHSPTMAYLLNRAGLSHMLIQRVHYAVKKHFAlHK 326
Cdd:cd10812   79 GGSWVENDTNMPSGESLARQFLYGQRYFESRFGKRCDTFWLPDTFGYSSQIPQLCRLAGMDYFFTQKLSWNNINSFP-HS 157
                        170       180
                 ....*....|....*....|....*....
gi 767935902 327 TLeffwrqNWDLGSVTDILCHMMPFYSYD 355
Cdd:cd10812  158 TF------NWVGIDGTQVLVHMTPVNTYT 180
GH38N_AMII_Man2C1 cd10813
N-terminal catalytic domain of mammalian cytosolic alpha-mannosidase Man2C1 and similar ...
167-354 7.20e-07

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: 51.62  E-value: 7.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 167 QVFVVPHSHNDPGWLKTFNDYFRdKTQYIFNNMVLKLKEDSRRKFIWSE---ISYLSKWWDIIDIQKKDAVKslieNGQL 243
Cdd:cd10813    1 TIHAMGHCHIDSAWLWPYEETIR-KCARSWVTVLRLMEDYPDFTFACSQaqqLEWVKSWYPGLYEEIQERVK----NGRF 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 244 EIVTGGWVMPDEATPHYFALIDQLIEGHQWLENNIGVKPRSGWAIDPFGHSPTMAYLLNRAGLSHMLIQRVHYAVKKHFA 323
Cdd:cd10813   76 IPVGGTWVEMDGNLPSGESMVRQFLYGQRFFKEEFGITCKEFWLPDTFGYSAQLPQIMKGCGISRFLTQKLSWNLVNKFP 155
                        170       180       190
                 ....*....|....*....|....*....|.
gi 767935902 324 LHKtleFFWrQNWDlGSvtDILCHMMPFYSY 354
Cdd:cd10813  156 HHT---FFW-EGID-GS--RVLTHFPPGDSY 179
GH38N_AMII_like_1 cd10791
N-terminal catalytic domain of mainly uncharacterized eukaryotic proteins similar to ...
167-333 6.85e-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: 45.39  E-value: 6.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 167 QVFVVPHSHNDPGWLKT---FNDYFRDktqYIFNNMVLKLK---EDSRRKFIWS-EISYL-SKWWDIIDIQKKDAVKSLI 238
Cdd:cd10791    1 TVHVVHHSHTDIGYTDLqekVDRYHVD---YIPQALDLAEAtknYPEDARFRWTtESTWLvEEYLKCASPEQRERLEQAV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 239 ENGQLEIvtggwvmpdEATPHYF-------ALIDQLIEGHQWLENNIGVKPRSGWAIDPFGHSPTMAYLLNRAGLsHMLI 311
Cdd:cd10791   78 RRGRIGW---------HALPLNIttelmdeELLRRGLYLSKELDRRFGLPIIVAMQTDVPGHTWGLVDVLADAGI-KYLS 147
                        170       180
                 ....*....|....*....|..
gi 767935902 312 QRVHYAVKKHFALHKTLeFFWR 333
Cdd:cd10791  148 IGVNGHSGPYPPRVPGP-FYWE 168
GH38N_AMII_SpGH38_like cd10814
N-terminal catalytic domain of SPGH38, a putative alpha-mannosidase of Streptococcus pyogenes, ...
167-313 5.44e-04

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: 42.63  E-value: 5.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 167 QVFVVPHSHNDPGWLKTFnDYFRDKTQYIFNNMVLKLKEDSrrkfiwseiSYLSKWWD----------IIDIQKKDAVKS 236
Cdd:cd10814    1 KVHIISHTHWDREWYLPF-EEFRMRLIDLIDRLLELLEEDP---------EFKSFHLDgqtivledylEVRPEKRERLKK 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 237 LIENGQLEIvtGGW-VMPDEatphyF-----ALIDQLIEGHQWLENnIGVKPRSGWAIDPFGHSPTMAYLLNRAGLSHML 310
Cdd:cd10814   71 LIREGKLVI--GPWyVLQDE-----FltsgeANIRNLLIGKKVAEE-FGKSMKIGYFPDTFGHIGQMPQILKGFGIDNAV 142

                 ...
gi 767935902 311 IQR 313
Cdd:cd10814  143 FGR 145
GH38N_AMII_EcMngB_like cd10815
N-terminal catalytic domain of Escherichia coli alpha-mannosidase MngB and its bacterial ...
167-493 8.42e-04

N-terminal catalytic domain of Escherichia coli alpha-mannosidase MngB and its bacterial homologs; glycoside hydrolase family 38 (GH38); The bacterial subfamily is represented by Escherichia coli alpha-mannosidase MngB, which is encoded by the mngB gene (previously called ybgG). MngB exhibits alpha-mannosidase activity that converts 2-O-(6-phospho-alpha-mannosyl)-D-glycerate to mannose-6-phosphate and glycerate in the pathway which enables use of mannosyl-D-glycerate as a sole carbon source. A divalent metal ion is required for its activity.


Pssm-ID: 212126 [Multi-domain]  Cd Length: 270  Bit Score: 42.13  E-value: 8.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 167 QVFVVPHSHNDPGWlktfndYF--RDKTQYIFNNM--VLK-LKEDSrrkfiwSEISYL-----SKWWDIIDI--QKKDAV 234
Cdd:cd10815    1 KVHVVPHTHWDREW------YFttEDSRILLVNHMdeVLDeLENNP------DFPYYVldgqsSILDDYLAVrpEDKERI 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 235 KSLIENGQLEIvtGGW-VMPDEATPHYFALIDQLIEGHQWLEN-----NIGVKPrsgwaiDPFGHSPTMAYLLNRAGLSH 308
Cdd:cd10815   69 KKLVKEGRLFI--GPWyTQTDELVVSGESIVRNLLYGIKDARKlggymKIGYLP------DSFGQSAQMPQIYNGFGIDN 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 309 MLIQR-VHYAVKKHfalhktLEFFWRQnwDLGSVtdILCHMMPF-YSYdiphtcgpdpkiccqfdFKRLPggrfgcpwgv 386
Cdd:cd10815  141 AVFWRgVSEDLVKS------TEFIWKS--LDGSK--VLAANIPFgYGI-----------------GKYLP---------- 183
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767935902 387 ppetIHPGNVQSRarmLLDQYRKKSKLFRTKVLLAPLGDDFRYCEytewdlqfKNYQQLFDYMNSQS-KFKVKIqfGTLS 465
Cdd:cd10815  184 ----EDPDYLKKR---LDPILEKLERRATTDNILLPNGGDQMPIR--------KNLPEVIEELNEISpDYEYVI--SSYE 246
                        330       340
                 ....*....|....*....|....*...
gi 767935902 466 DFFDALDKADEtqrdkgqsMFPVLSGDF 493
Cdd:cd10815  247 EFFKALEKNKD--------LLPTIEGEL 266
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH