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Conserved domains on  [gi|1370466591|ref|XP_024305688|]
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alpha-mannosidase 2x isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02701 super family cl26659
alpha-mannosidase
136-1174 0e+00

alpha-mannosidase


The actual alignment was detected with superfamily member PLN02701:

Pssm-ID: 178304 [Multi-domain]  Cd Length: 1050  Bit Score: 1004.32  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  136 EELPFDNVDGGVWRQGFDISYDPHDWDAEDLQVFVVPHSHNDPGWIKTFDKYYTEQTQHILNSMVSKLQEDPRRRFLWAE 215
Cdd:PLN02701    10 DRIEFLDKDGGAWKQGWRVKYRGDEWDREKLKVFVVPHSHNDPGWILTVEEYYQEQSRHILDTIVESLSKDPRRKFIWEE 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  216 VSFFAKWWDNINVQKRAAVRRLVGNGQLEIATGGWVMPDEANSHYFALIDQLIEGHQWLERNLGATPRSGWAVDPFGYSS 295
Cdd:PLN02701    90 MSYLERWWRDASPSKKEAFTKLVKNGQLEIVGGGWVMNDEANSHYFAIIEQITEGNMWLNDTIGVAPKNSWAIDPFGYSS 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  296 TMPYLLRRANLTSMLIQRVHYAIKKHFAATHSLEFMWRQTWDSDSSTDIFCHMMPFYSYDVPHTCGPDPKICCQFDFKRL 375
Cdd:PLN02701   170 TMAYLLRRMGFENMLIQRTHYEVKKELAQNKNLEYIWRQSWDAEETTDIFVHMMPFYSYDIPHTCGPEPAICCQFDFARM 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  376 PGGRIN-CPWKVPPRAITEANVAERAALLLDQYRKKSQLFRSNVLLVPLGDDFRYDKPQEWDAQFFNYQRLFDFFNSRPN 454
Cdd:PLN02701   250 RGFQYElCPWGKHPVETNDENVQERAMKLLDQYRKKSTLYRTNTLLVPLGDDFRYISIDEAEAQFRNYQKLFDYINSNPS 329
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  455 LHVQAQFGTLSDYFDAL--------YKRTGVEPGARPPGFPVLSGDFFSYADREDHYWTGYYTSRPFYKSLDRVLEAHLR 526
Cdd:PLN02701   330 LKAEVKFGTLEDYFSTLrdeadrinYSRPGEVGSGEVPGFPSLSGDFFTYADRQQDYWSGYYVSRPFFKAVDRVLEQTLR 409
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  527 GAEVLYSLAAAHARRSGLAgRYPLSDFTLLTEARRTLGLFQHHDAITGTAKEAVVVDYGVRLLRSLVNLkQVIIHAAHYL 606
Cdd:PLN02701   410 AAEILFSFLLGYCRRFQCE-KLPTSFSYKLTAARRNLALFQHHDGVTGTAKDHVVVDYGTRMHTSLQDL-QIFMSAAVEV 487
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  607 VLGDKETyHFDPEAPFLQVDDTRLSHDALPERTVIQLDS-SPRFVVLFNPLEQERFSMVSLLVNSPRVRVLSEEGQPLAV 685
Cdd:PLN02701   488 LLGIRHE-KSDQTPSWFEPEQSRSKYDMLPVHKVINLREgKAHRVVFFNPLEQTREEVVMVVVDRPAVCVFDSNWTCVPS 566
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  686 QISAHWSSATEAV-PDVYQVSVPVRLPALGLGVLQLQLGLDG-HRTLPSSVRIYLHGRQL------SVSRHEAfplrvid 757
Cdd:PLN02701   567 QISPEWQHDGEKLfTGRHRLYWKASVPALGLETYFIANGNVScEKAVPAKLKVFNSDDKFpcpepySCSKLEG------- 639
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  758 sgtSDFALSNRYMQVWFSGLTGLLKSIRRVDEEHEQQVDMQVLVYgtrtSKDKSGAYLFLPDGEAKPYVPKEPPVLrVTE 837
Cdd:PLN02701   640 ---DTVEISNSHQTLGFDVKTGLLRKIKIHKNGSETVVGEEIGMY----SSQGSGAYLFKPDGEAQPIVQAGGLVV-VSE 711
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  838 GPFFSEVVAYYEH------IHQAVRLYNLP-GVEGLSLDISSLVDI--RDYVNKELALHIHTDIDSQGIFFTDLNGFQVQ 908
Cdd:PLN02701   712 GPLVQEVHSVPKTkwekspLSRSTRLYHGGkSVQDLSVEKEYHVELlgHDFNDKELIVRFKTDIDNKRVFYSDLNGFQMS 791
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  909 PRRYLKKLPLQANFYPMPVMAYIQDAQ-KRLTLHTAQALGVSSLKDGQLEVILDRRLMQDDNRGLGQGLKDNKRTCNRFR 987
Cdd:PLN02701   792 RRETYDKIPLQGNYYPMPSLAFLQGSNgQRFSVHSRQSLGVASLKNGWLEIMLDRRLVQDDGRGLGQGVMDNRPMNVVFH 871
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  988 LLLERRTVGSEPdffsklaamfrgliFHSSRSGNrevqdshstsyPSLLSHLTSMYLNAPALALPVARMQ---LPGPGLR 1064
Cdd:PLN02701   872 LLLESNISSSPP--------------ASNPLPLQ-----------PSLLSHRVGAHLNYPMHAFLAKKPQatsVENPQDT 926
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591 1065 SFHPLASSLPCDFHLLNLRTL---QAEEDTLPSAETALILHRKGFDCGLEAKNlGFNCTT-SQGKVALGSLFHGLDVVFL 1140
Cdd:PLN02701   927 SFAPLAKPLPCDLHIVNFKVPrpsKYSQQEAEDPRFGLLLQRRGWDSSYCRKG-GTQCTTlANEPVNLFDMFKDLAVSKV 1005
                         1050      1060      1070      1080
                   ....*....|....*....|....*....|....*....|....
gi 1370466591 1141 QPTSLTLLYP----------LASPSNSTDVYLEPMEIATFRLRL 1174
Cdd:PLN02701  1006 KATSLNLLHDdaemlgyrkqAGSAAQEGIVLISPMEIQAYKLDL 1049
 
Name Accession Description Interval E-value
PLN02701 PLN02701
alpha-mannosidase
136-1174 0e+00

alpha-mannosidase


Pssm-ID: 178304 [Multi-domain]  Cd Length: 1050  Bit Score: 1004.32  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  136 EELPFDNVDGGVWRQGFDISYDPHDWDAEDLQVFVVPHSHNDPGWIKTFDKYYTEQTQHILNSMVSKLQEDPRRRFLWAE 215
Cdd:PLN02701    10 DRIEFLDKDGGAWKQGWRVKYRGDEWDREKLKVFVVPHSHNDPGWILTVEEYYQEQSRHILDTIVESLSKDPRRKFIWEE 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  216 VSFFAKWWDNINVQKRAAVRRLVGNGQLEIATGGWVMPDEANSHYFALIDQLIEGHQWLERNLGATPRSGWAVDPFGYSS 295
Cdd:PLN02701    90 MSYLERWWRDASPSKKEAFTKLVKNGQLEIVGGGWVMNDEANSHYFAIIEQITEGNMWLNDTIGVAPKNSWAIDPFGYSS 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  296 TMPYLLRRANLTSMLIQRVHYAIKKHFAATHSLEFMWRQTWDSDSSTDIFCHMMPFYSYDVPHTCGPDPKICCQFDFKRL 375
Cdd:PLN02701   170 TMAYLLRRMGFENMLIQRTHYEVKKELAQNKNLEYIWRQSWDAEETTDIFVHMMPFYSYDIPHTCGPEPAICCQFDFARM 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  376 PGGRIN-CPWKVPPRAITEANVAERAALLLDQYRKKSQLFRSNVLLVPLGDDFRYDKPQEWDAQFFNYQRLFDFFNSRPN 454
Cdd:PLN02701   250 RGFQYElCPWGKHPVETNDENVQERAMKLLDQYRKKSTLYRTNTLLVPLGDDFRYISIDEAEAQFRNYQKLFDYINSNPS 329
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  455 LHVQAQFGTLSDYFDAL--------YKRTGVEPGARPPGFPVLSGDFFSYADREDHYWTGYYTSRPFYKSLDRVLEAHLR 526
Cdd:PLN02701   330 LKAEVKFGTLEDYFSTLrdeadrinYSRPGEVGSGEVPGFPSLSGDFFTYADRQQDYWSGYYVSRPFFKAVDRVLEQTLR 409
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  527 GAEVLYSLAAAHARRSGLAgRYPLSDFTLLTEARRTLGLFQHHDAITGTAKEAVVVDYGVRLLRSLVNLkQVIIHAAHYL 606
Cdd:PLN02701   410 AAEILFSFLLGYCRRFQCE-KLPTSFSYKLTAARRNLALFQHHDGVTGTAKDHVVVDYGTRMHTSLQDL-QIFMSAAVEV 487
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  607 VLGDKETyHFDPEAPFLQVDDTRLSHDALPERTVIQLDS-SPRFVVLFNPLEQERFSMVSLLVNSPRVRVLSEEGQPLAV 685
Cdd:PLN02701   488 LLGIRHE-KSDQTPSWFEPEQSRSKYDMLPVHKVINLREgKAHRVVFFNPLEQTREEVVMVVVDRPAVCVFDSNWTCVPS 566
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  686 QISAHWSSATEAV-PDVYQVSVPVRLPALGLGVLQLQLGLDG-HRTLPSSVRIYLHGRQL------SVSRHEAfplrvid 757
Cdd:PLN02701   567 QISPEWQHDGEKLfTGRHRLYWKASVPALGLETYFIANGNVScEKAVPAKLKVFNSDDKFpcpepySCSKLEG------- 639
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  758 sgtSDFALSNRYMQVWFSGLTGLLKSIRRVDEEHEQQVDMQVLVYgtrtSKDKSGAYLFLPDGEAKPYVPKEPPVLrVTE 837
Cdd:PLN02701   640 ---DTVEISNSHQTLGFDVKTGLLRKIKIHKNGSETVVGEEIGMY----SSQGSGAYLFKPDGEAQPIVQAGGLVV-VSE 711
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  838 GPFFSEVVAYYEH------IHQAVRLYNLP-GVEGLSLDISSLVDI--RDYVNKELALHIHTDIDSQGIFFTDLNGFQVQ 908
Cdd:PLN02701   712 GPLVQEVHSVPKTkwekspLSRSTRLYHGGkSVQDLSVEKEYHVELlgHDFNDKELIVRFKTDIDNKRVFYSDLNGFQMS 791
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  909 PRRYLKKLPLQANFYPMPVMAYIQDAQ-KRLTLHTAQALGVSSLKDGQLEVILDRRLMQDDNRGLGQGLKDNKRTCNRFR 987
Cdd:PLN02701   792 RRETYDKIPLQGNYYPMPSLAFLQGSNgQRFSVHSRQSLGVASLKNGWLEIMLDRRLVQDDGRGLGQGVMDNRPMNVVFH 871
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  988 LLLERRTVGSEPdffsklaamfrgliFHSSRSGNrevqdshstsyPSLLSHLTSMYLNAPALALPVARMQ---LPGPGLR 1064
Cdd:PLN02701   872 LLLESNISSSPP--------------ASNPLPLQ-----------PSLLSHRVGAHLNYPMHAFLAKKPQatsVENPQDT 926
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591 1065 SFHPLASSLPCDFHLLNLRTL---QAEEDTLPSAETALILHRKGFDCGLEAKNlGFNCTT-SQGKVALGSLFHGLDVVFL 1140
Cdd:PLN02701   927 SFAPLAKPLPCDLHIVNFKVPrpsKYSQQEAEDPRFGLLLQRRGWDSSYCRKG-GTQCTTlANEPVNLFDMFKDLAVSKV 1005
                         1050      1060      1070      1080
                   ....*....|....*....|....*....|....*....|....
gi 1370466591 1141 QPTSLTLLYP----------LASPSNSTDVYLEPMEIATFRLRL 1174
Cdd:PLN02701  1006 KATSLNLLHDdaemlgyrkqAGSAAQEGIVLISPMEIQAYKLDL 1049
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: 818.07  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  165 DLQVFVVPHSHNDPGWIKTFDKYYTEQTQHILNSMVSKLQEDPRRRFLWAEVSFFAKWWDNINVQKRAAVRRLVGNGQLE 244
Cdd:cd11667      1 PLQVFVVPHSHNDPGWIKTFDKYYYDQTQHILNSMVVKLQEDPRRRFIWSEISFFSKWWDNINAQKRAAVRRLVGNGQLE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  245 IATGGWVMPDEANSHYFALIDQLIEGHQWLERNLGATPRSGWAVDPFGYSSTMPYLLRRANLTSMLIQRVHYAIKKHFAA 324
Cdd:cd11667     81 MATGGWVMPDEANSHYFAMIDQLIEGHQWLEKNIGVTPRSGWAVDPFGHSSTMPYILRRSNLTSMLIQRVHYAIKKHFAA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  325 THSLEFMWRQTWDSDSSTDIFCHMMPFYSYDVPHTCGPDPKICCQFDFKRLPGGRINCPWKVPPRAITEANVAERAALLL 404
Cdd:cd11667    161 TQSLEFMWRQTWDPDSSTDIFCHMMPFYSYDVPHTCGPDPKICCQFDFKRLPGGRINCPWKVPPRAITEANVAERAQLLL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  405 DQYRKKSQLFRSNVLLVPLGDDFRYDKPQEWDAQFFNYQRLFDFFNSRPNLHVQAQFGTLSDYFDALYKRTGVEPGARPP 484
Cdd:cd11667    241 DQYRKKSKLYRSKVLLVPLGDDFRYDKPQEWDAQFLNYQRLFDFLNSHPELHVQAQFGTLSDYFDALYKRTGVVPGMRPP 320
                          330       340
                   ....*....|....*....|....
gi 1370466591  485 GFPVLSGDFFSYADREDHYWTGYY 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 3.92e-105

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: 331.90  E-value: 3.92e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  167 QVFVVPHSHNDPGWIKTFDKYyTEQTQHILNSMVSKLQEDPRRRFLWAEVSFFAKWWDNINvQKRAAVRRLVGNGQLEIA 246
Cdd:pfam01074    1 TVHLVGHSHIDVGWLWTVDET-RRKVQRTFSSVLALLDRDPDRRFIWSEAQFFAWWWEDQP-ELFKRIKKLVAEGRLEPV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  247 TGGWVMPDEANSHYFALIDQLIEGHQWLERNLGATPRSGWAVDPFGYSSTMPYLLRRANLTSMLIQRVHYAIKKHFaaTH 326
Cdd:pfam01074   79 GGGWVEPDENLPSGESLIRQFLYGQRFFKEEFGVRPRVGWLPDPFGYSATLPQILKQAGIDYFLTQRLHWNDKNKF--NP 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  327 SLEFMWRQTWDsdssTDIFCHMMPFYSYdvphtcgpdPKICCQFdfkrlpggrincpwkvppraiteanvAERAALLLDQ 406
Cdd:pfam01074  157 HLEFIWRGSDG----TEIFTHMPPFDYY---------PTYGFQF--------------------------QERAEDLLAY 197
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  407 YRKKSQLFRSNVLLVPLGDDfrydkpqewDAQFFNYQRLFDFFNSRPNL--HVQAQFGTLSDYFDALYKRTgvepgarpp 484
Cdd:pfam01074  198 ARNYADKTRTNHVLLPFGDG---------DGGGGPTDEMLEYINRWNALpgLPKVQYGTPSDYFDALEKAT--------- 259
                          330
                   ....*....|...
gi 1370466591  485 gFPVLSGDFFSYA 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 7.08e-30

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: 113.42  E-value: 7.08e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591   503 YWTGYYTSRPFYKSLDRVLEAHLRGAEVLYSLAAAHArrsgLAGRYPLSDftlLTEARRTLGLFQHHDAITGTAKEAVVV 582
Cdd:smart00872    1 YHRGTYTSRPYLKRLNRRAESLLRAAEELAALAALLS----LGYKYPSEQ---LEELWKALLLNQHHDAITGTSIDEVYD 73

                    ....*.
gi 1370466591   583 DYGVRL 588
Cdd:smart00872   74 DYEKRL 79
 
Name Accession Description Interval E-value
PLN02701 PLN02701
alpha-mannosidase
136-1174 0e+00

alpha-mannosidase


Pssm-ID: 178304 [Multi-domain]  Cd Length: 1050  Bit Score: 1004.32  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  136 EELPFDNVDGGVWRQGFDISYDPHDWDAEDLQVFVVPHSHNDPGWIKTFDKYYTEQTQHILNSMVSKLQEDPRRRFLWAE 215
Cdd:PLN02701    10 DRIEFLDKDGGAWKQGWRVKYRGDEWDREKLKVFVVPHSHNDPGWILTVEEYYQEQSRHILDTIVESLSKDPRRKFIWEE 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  216 VSFFAKWWDNINVQKRAAVRRLVGNGQLEIATGGWVMPDEANSHYFALIDQLIEGHQWLERNLGATPRSGWAVDPFGYSS 295
Cdd:PLN02701    90 MSYLERWWRDASPSKKEAFTKLVKNGQLEIVGGGWVMNDEANSHYFAIIEQITEGNMWLNDTIGVAPKNSWAIDPFGYSS 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  296 TMPYLLRRANLTSMLIQRVHYAIKKHFAATHSLEFMWRQTWDSDSSTDIFCHMMPFYSYDVPHTCGPDPKICCQFDFKRL 375
Cdd:PLN02701   170 TMAYLLRRMGFENMLIQRTHYEVKKELAQNKNLEYIWRQSWDAEETTDIFVHMMPFYSYDIPHTCGPEPAICCQFDFARM 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  376 PGGRIN-CPWKVPPRAITEANVAERAALLLDQYRKKSQLFRSNVLLVPLGDDFRYDKPQEWDAQFFNYQRLFDFFNSRPN 454
Cdd:PLN02701   250 RGFQYElCPWGKHPVETNDENVQERAMKLLDQYRKKSTLYRTNTLLVPLGDDFRYISIDEAEAQFRNYQKLFDYINSNPS 329
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  455 LHVQAQFGTLSDYFDAL--------YKRTGVEPGARPPGFPVLSGDFFSYADREDHYWTGYYTSRPFYKSLDRVLEAHLR 526
Cdd:PLN02701   330 LKAEVKFGTLEDYFSTLrdeadrinYSRPGEVGSGEVPGFPSLSGDFFTYADRQQDYWSGYYVSRPFFKAVDRVLEQTLR 409
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  527 GAEVLYSLAAAHARRSGLAgRYPLSDFTLLTEARRTLGLFQHHDAITGTAKEAVVVDYGVRLLRSLVNLkQVIIHAAHYL 606
Cdd:PLN02701   410 AAEILFSFLLGYCRRFQCE-KLPTSFSYKLTAARRNLALFQHHDGVTGTAKDHVVVDYGTRMHTSLQDL-QIFMSAAVEV 487
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  607 VLGDKETyHFDPEAPFLQVDDTRLSHDALPERTVIQLDS-SPRFVVLFNPLEQERFSMVSLLVNSPRVRVLSEEGQPLAV 685
Cdd:PLN02701   488 LLGIRHE-KSDQTPSWFEPEQSRSKYDMLPVHKVINLREgKAHRVVFFNPLEQTREEVVMVVVDRPAVCVFDSNWTCVPS 566
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  686 QISAHWSSATEAV-PDVYQVSVPVRLPALGLGVLQLQLGLDG-HRTLPSSVRIYLHGRQL------SVSRHEAfplrvid 757
Cdd:PLN02701   567 QISPEWQHDGEKLfTGRHRLYWKASVPALGLETYFIANGNVScEKAVPAKLKVFNSDDKFpcpepySCSKLEG------- 639
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  758 sgtSDFALSNRYMQVWFSGLTGLLKSIRRVDEEHEQQVDMQVLVYgtrtSKDKSGAYLFLPDGEAKPYVPKEPPVLrVTE 837
Cdd:PLN02701   640 ---DTVEISNSHQTLGFDVKTGLLRKIKIHKNGSETVVGEEIGMY----SSQGSGAYLFKPDGEAQPIVQAGGLVV-VSE 711
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  838 GPFFSEVVAYYEH------IHQAVRLYNLP-GVEGLSLDISSLVDI--RDYVNKELALHIHTDIDSQGIFFTDLNGFQVQ 908
Cdd:PLN02701   712 GPLVQEVHSVPKTkwekspLSRSTRLYHGGkSVQDLSVEKEYHVELlgHDFNDKELIVRFKTDIDNKRVFYSDLNGFQMS 791
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  909 PRRYLKKLPLQANFYPMPVMAYIQDAQ-KRLTLHTAQALGVSSLKDGQLEVILDRRLMQDDNRGLGQGLKDNKRTCNRFR 987
Cdd:PLN02701   792 RRETYDKIPLQGNYYPMPSLAFLQGSNgQRFSVHSRQSLGVASLKNGWLEIMLDRRLVQDDGRGLGQGVMDNRPMNVVFH 871
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  988 LLLERRTVGSEPdffsklaamfrgliFHSSRSGNrevqdshstsyPSLLSHLTSMYLNAPALALPVARMQ---LPGPGLR 1064
Cdd:PLN02701   872 LLLESNISSSPP--------------ASNPLPLQ-----------PSLLSHRVGAHLNYPMHAFLAKKPQatsVENPQDT 926
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591 1065 SFHPLASSLPCDFHLLNLRTL---QAEEDTLPSAETALILHRKGFDCGLEAKNlGFNCTT-SQGKVALGSLFHGLDVVFL 1140
Cdd:PLN02701   927 SFAPLAKPLPCDLHIVNFKVPrpsKYSQQEAEDPRFGLLLQRRGWDSSYCRKG-GTQCTTlANEPVNLFDMFKDLAVSKV 1005
                         1050      1060      1070      1080
                   ....*....|....*....|....*....|....*....|....
gi 1370466591 1141 QPTSLTLLYP----------LASPSNSTDVYLEPMEIATFRLRL 1174
Cdd:PLN02701  1006 KATSLNLLHDdaemlgyrkqAGSAAQEGIVLISPMEIQAYKLDL 1049
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: 818.07  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  165 DLQVFVVPHSHNDPGWIKTFDKYYTEQTQHILNSMVSKLQEDPRRRFLWAEVSFFAKWWDNINVQKRAAVRRLVGNGQLE 244
Cdd:cd11667      1 PLQVFVVPHSHNDPGWIKTFDKYYYDQTQHILNSMVVKLQEDPRRRFIWSEISFFSKWWDNINAQKRAAVRRLVGNGQLE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  245 IATGGWVMPDEANSHYFALIDQLIEGHQWLERNLGATPRSGWAVDPFGYSSTMPYLLRRANLTSMLIQRVHYAIKKHFAA 324
Cdd:cd11667     81 MATGGWVMPDEANSHYFAMIDQLIEGHQWLEKNIGVTPRSGWAVDPFGHSSTMPYILRRSNLTSMLIQRVHYAIKKHFAA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  325 THSLEFMWRQTWDSDSSTDIFCHMMPFYSYDVPHTCGPDPKICCQFDFKRLPGGRINCPWKVPPRAITEANVAERAALLL 404
Cdd:cd11667    161 TQSLEFMWRQTWDPDSSTDIFCHMMPFYSYDVPHTCGPDPKICCQFDFKRLPGGRINCPWKVPPRAITEANVAERAQLLL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  405 DQYRKKSQLFRSNVLLVPLGDDFRYDKPQEWDAQFFNYQRLFDFFNSRPNLHVQAQFGTLSDYFDALYKRTGVEPGARPP 484
Cdd:cd11667    241 DQYRKKSKLYRSKVLLVPLGDDFRYDKPQEWDAQFLNYQRLFDFLNSHPELHVQAQFGTLSDYFDALYKRTGVVPGMRPP 320
                          330       340
                   ....*....|....*....|....
gi 1370466591  485 GFPVLSGDFFSYADREDHYWTGYY 508
Cdd:cd11667    321 GFPVVSGDFFSYADREDHYWTGYY 344
GH38N_AMII_GMII_SfManIII_like cd10809
N-terminal catalytic domain of Golgi alpha-mannosidase II, Spodoptera frugiperda Sf9 ...
166-508 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: 713.27  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  166 LQVFVVPHSHNDPGWIKTFDKYYTEQTQHILNSMVSKLQEDPRRRFLWAEVSFFAKWWDNINVQKRAAVRRLVGNGQLEI 245
Cdd:cd10809      2 LKVFVVPHSHNDPGWIKTFEEYYQDQTKHILDNMVDKLSKNPKMKFIWAEISFLERWWDDASPDKKEAVKKLVKNGQLEI 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  246 ATGGWVMPDEANSHYFALIDQLIEGHQWLERNLGATPRSGWAVDPFGYSSTMPYLLRRANLTSMLIQRVHYAIKKHFAAT 325
Cdd:cd10809     82 VTGGWVMTDEANSHYFAMIDQLIEGHQWLKENLGVKPKSGWSIDPFGHSPTMPYLLKRAGFKNMVIQRIHYEVKKYLAQR 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  326 HSLEFMWRQTWDSDSSTDIFCHMMPFYSYDVPHTCGPDPKICCQFDFKRLPGGRINCPWKVPPRAITEANVAERAALLLD 405
Cdd:cd10809    162 KALEFMWRQYWDATGSTDILTHMMPFYSYDIPHTCGPDPAVCCQFDFKRLPGGGESCPWKKPPQPITDDNVAERAELLLD 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  406 QYRKKSQLFRSNVLLVPLGDDFRYDKPQEWDAQFFNYQRLFDFFNSRPNLHVQAQFGTLSDYFDALYKRTgvepGARPPG 485
Cdd:cd10809    242 QYRKKSQLYRSNVVLIPLGDDFRYDSDEEWDAQYDNYQKLFDYINSNPELNVEIQFGTLSDYFNALRKRT----GTNTPG 317
                          330       340
                   ....*....|....*....|...
gi 1370466591  486 FPVLSGDFFSYADREDHYWTGYY 508
Cdd:cd10809    318 FPTLSGDFFTYADRDDDYWSGYY 340
GH38N_Man2A1 cd11666
N-terminal catalytic domain of Golgi alpha-mannosidase II and similar proteins; glycoside ...
166-508 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: 645.10  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  166 LQVFVVPHSHNDPGWIKTFDKYYTEQTQHILNSMVSKLQEDPRRRFLWAEVSFFAKWWDNINVQKRAAVRRLVGNGQLEI 245
Cdd:cd11666      2 LQVFVVPHSHNDPGWLKTFDDYFRDQTQHILNNMVLKLKEDSRRKFIWSEISYFAKWWDIIDGQKKDAVKRLIENGQLEI 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  246 ATGGWVMPDEANSHYFALIDQLIEGHQWLERNLGATPRSGWAVDPFGYSSTMPYLLRRANLTSMLIQRVHYAIKKHFAAT 325
Cdd:cd11666     82 VTGGWVMPDEATAHYFALIDQLIEGHQWLERNLGVKPKSGWAVDPFGHSPTMAYLLKRAGLSNMLIQRVHYSVKKHFSLQ 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  326 HSLEFMWRQTWDSDSSTDIFCHMMPFYSYDVPHTCGPDPKICCQFDFKRLPGGRINCPWKVPPRAITEANVAERAALLLD 405
Cdd:cd11666    162 KTLEFFWRQNWDLGSSTDILCHMMPFYSYDVPHTCGPDPKICCQFDFKRLPGGRISCPWRVPPEAIHPGNVQSRAQMLLD 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  406 QYRKKSQLFRSNVLLVPLGDDFRYDKPQEWDAQFFNYQRLFDFFNSRPNLHVQAQFGTLSDYFDALYKRTGVEPGARPPG 485
Cdd:cd11666    242 QYRKKSKLFRTKVLLAPLGDDFRYTEYTEWDQQFENYQKLFDYMNSHPELHVKAQFGTLSDYFDALRKSTGMDPVGGQSA 321
                          330       340
                   ....*....|....*....|...
gi 1370466591  486 FPVLSGDFFSYADREDHYWTGYY 508
Cdd:cd11666    322 FPVLSGDFFTYADRDDHYWSGYF 344
Glyco_hydro_38N pfam01074
Glycosyl hydrolases family 38 N-terminal domain; Glycosyl hydrolases are key enzymes of ...
167-497 3.92e-105

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: 331.90  E-value: 3.92e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  167 QVFVVPHSHNDPGWIKTFDKYyTEQTQHILNSMVSKLQEDPRRRFLWAEVSFFAKWWDNINvQKRAAVRRLVGNGQLEIA 246
Cdd:pfam01074    1 TVHLVGHSHIDVGWLWTVDET-RRKVQRTFSSVLALLDRDPDRRFIWSEAQFFAWWWEDQP-ELFKRIKKLVAEGRLEPV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  247 TGGWVMPDEANSHYFALIDQLIEGHQWLERNLGATPRSGWAVDPFGYSSTMPYLLRRANLTSMLIQRVHYAIKKHFaaTH 326
Cdd:pfam01074   79 GGGWVEPDENLPSGESLIRQFLYGQRFFKEEFGVRPRVGWLPDPFGYSATLPQILKQAGIDYFLTQRLHWNDKNKF--NP 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  327 SLEFMWRQTWDsdssTDIFCHMMPFYSYdvphtcgpdPKICCQFdfkrlpggrincpwkvppraiteanvAERAALLLDQ 406
Cdd:pfam01074  157 HLEFIWRGSDG----TEIFTHMPPFDYY---------PTYGFQF--------------------------QERAEDLLAY 197
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  407 YRKKSQLFRSNVLLVPLGDDfrydkpqewDAQFFNYQRLFDFFNSRPNL--HVQAQFGTLSDYFDALYKRTgvepgarpp 484
Cdd:pfam01074  198 ARNYADKTRTNHVLLPFGDG---------DGGGGPTDEMLEYINRWNALpgLPKVQYGTPSDYFDALEKAT--------- 259
                          330
                   ....*....|...
gi 1370466591  485 gFPVLSGDFFSYA 497
Cdd:pfam01074  260 -WPTKTDDFPPYA 271
GH38N_AMII_euk cd00451
N-terminal catalytic domain of eukaryotic class II alpha-mannosidases; glycoside hydrolase ...
166-451 6.01e-103

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: 325.33  E-value: 6.01e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  166 LQVFVVPHSHNDPGWIKTFDKYYTEQTQHILNSMVSKLQEDPRRRFLWAEVSFFAKWWDNINVQKRAAVRRLVGNGQLEI 245
Cdd:cd00451      1 LNVHLIPHSHCDVGWLKTFDEYYNGDVKSILDSVVKALNNDPERKFIWAEIGFLERWWEDQGNDTKQQFKKLVKNGQLEF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  246 ATGGWVMPDEANSHYFALIDQLIEGHQWLERNLGATPRSGWAVDPFGYSSTMPYLLRRANLTSMLIQRVHYAIKKHFAAT 325
Cdd:cd00451     81 VGGGWVMNDEACTTYESIIDQMTEGHQFLKDTFGVRPRVGWQIDPFGHSSTTPTLFSKMGFKGLVINRIPYSLKAEMKDN 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  326 HSLEFMWRQTWDSDSSTDIFCHMMP-FYSYDVPHTCGPDPkiccqfdfkrlpggrincpwkvppraITEANVAERAALLL 404
Cdd:cd00451    161 KQLEFVWRGSPSLGPDSEIFTHVLDdHYSYPESLDFGGPP--------------------------ITDYNIAERADEFV 214
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1370466591  405 DQYRKKSQLFRSNVLLVPLGDDFRYdkpQEWDAQFFNYQRLFDFFNS 451
Cdd:cd00451    215 EYIKKRSKTYRTNHILIPLGDDFRF---KNASLQFSNMDKLIAYINS 258
GH38N_AMII_LAM_like cd10810
N-terminal catalytic domain of lysosomal alpha-mannosidase and similar proteins; glycoside ...
166-451 1.16e-72

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: 243.27  E-value: 1.16e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  166 LQVFVVPHSHNDPGWIKTFDKYYT---EQTQH-----ILNSMVSKLQEDPRRRFLWAEVSFFAKWWDNINVQKRAAVRRL 237
Cdd:cd10810      1 LNVHLVPHTHDDVGWLKTVDQYYYgsnNSIQHagvqyILDSVIEELLKNPDRKFIYVEIAFFSRWWREQSEDTRQKVKKL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  238 VGNGQLEIATGGWVMPDEANSHYFALIDQLIEGHQWLERNLG--ATPRSGWAVDPFGYSSTMPYLLRRANLTSMLIQRVH 315
Cdd:cd10810     81 VKNGQLEFINGGWCMNDEATTHYEDIIDQMTLGHQFLKDTFGecARPRVGWQIDPFGHSRTQASLFAQMGFDGLFFGRID 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  316 YAIKKHFAATHSLEFMWRQTWDSDSSTDIFCHMmpFYSydvpHTCGPDPkiccqFDFKRLPGgriNCPWKVPPRaITEAN 395
Cdd:cd10810    161 YQDKAQRLKNKEMEFIWRGSPSLGPDADIFTGV--LYN----HYGPPPG-----FCFDILCG---DEPIQDDPN-LEDYN 225
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370466591  396 VAERAALLLDQYRKKSQLFRSNVLLVPLGDDFRYDKPQEWdaqFFNYQRLFDFFNS 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 7.85e-70

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: 234.22  E-value: 7.85e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  168 VFVVPHSHNDPGWIKTFDKYYTEQTQHILNSMVSKLQEDPRRRFLWAEVSFFAKWWDnINVQKRAAVRRLVGNGQLEIAT 247
Cdd:cd10786      2 VHLVPHSHYDVGWLQTFEQYYQINFKAILDKALRLLDANPEYKFLIEEVILLERYWD-VRPDLKAKLKQAVRSGRLEIAG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  248 GGWVMPDEANSHYFALIDQLIEGHQWLERNLGATPRSGWAVDPFGYSSTMPYLLRRANLTSMLIQRVHYAIKKhfAATHS 327
Cdd:cd10786     81 GGYVMPDTNLPDGESLVRQILLGKRWLKEFLGARPPVMWQADVFGHSPQLPQILAKSGFTGFAFGRGPYSQKR--MQRPS 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  328 lEFMWRQTWdsdsSTDIFCHMMPFYSYDVPHTCGPDpkiccqfdfkrlpggrincpwkvPPRAITEANVAERAALLLDQY 407
Cdd:cd10786    159 -EFLWRGLD----GTRILTHWMPNGYSDGPFLCGPD-----------------------IPGDNSGPNALASLEALVEQW 210
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1370466591  408 RKKSQLFRSNVLLVPLGDDFRydkPQEWDAQFFNYQRLFDFFNS 451
Cdd:cd10786    211 KKLAELGATNHLLMPSGGDFT---IPQADPLQVNQARLVEPWNS 251
GH38N_AMII_Epman_like cd10811
N-terminal catalytic domain of mammalian core-specific lysosomal alpha 1,6-mannosidase and ...
166-474 2.64e-50

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: 181.24  E-value: 2.64e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  166 LQVFVVPHSHNDPGWIKTFDKYYTEQTQHILNSMVSKLQEDPRRRFLWAEVSFFAKWWDNI--NVQKRAaVRRLVGNGQL 243
Cdd:cd10811      1 IQAFVIPHSHMDVGWVYTVQESMHAYAANVYTSVVEELMRGKQRRFIAVEQEFFRLWWDGVatDKQKQQ-VRQLLSEGRL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  244 EIATGGWVMPDEANSHYFALIDQLIEGHQWLERNLGATPRSGWAVDPFGYSSTMPYLLRRANLTSMLIQRVHYAIKKHFA 323
Cdd:cd10811     80 EFVIGGQVMHDEAVTELDDQILQLTEGHGFLYETFGVRPRFSWHVDPFGASATTPTLFALAGFNAHLISRIDYDLKAAMQ 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  324 ATHSLEFMWRQTWDSDSSTDIFCHMMPFYSYdvphtCGPDpkiccQFDFKRLPGGRIN--CPWKVPPR---------AIT 392
Cdd:cd10811    160 KAKGLQFVWRGSPSLSESQEIFTHVMDQYSY-----CTPS-----YIPFSNRSGFYWNgvAVFPDPPKdgiypnmslPVT 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  393 EANVAERAALLLDQYRKKSQLFRSNVLLVPLGDDfrydkPQEWDA--QFFNYQRLFDFFNS-RPNLHVQAQFGTLSDYFD 469
Cdd:cd10811    230 TQNIHQYAETMVANIKQRAAWFRTPHVLWPWGCD-----KQFFNAsvQFSNMDPLLDYINQhSSEFGVTVQYATLGDYFQ 304

                   ....*
gi 1370466591  470 ALYKR 474
Cdd:cd10811    305 ALHNS 309
Glyco_hydro_38C pfam07748
Glycosyl hydrolases family 38 C-terminal domain; Glycosyl hydrolases are key enzymes of ...
765-970 1.57e-48

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: 171.67  E-value: 1.57e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  765 LSNRYMQVWFSGLTGLLKSIRR--VDEEHEQQVDMQVLVYgtRTSKDKSGAYLFLPDGEAKPYVPKEPPVLRVTEGPFFS 842
Cdd:pfam07748    1 LENGFLKVEFDNDTGTLTSIYDkeLSREVLAEVGNQFGLY--EDIPGYSDAWDFRPFYEAKPLEVDEQSIEVVEDGPLVA 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  843 EVVAYYEH----IHQAVRLYnlpgVEGLSLDISSLVDIRdyvNKELALHIHTDIDSQGIFFTDLNGFQVQPRRYLKKLPL 918
Cdd:pfam07748   79 EVHVKFKIggseISQVIRLY----KGSPRLEFETTVDWH---EREVLLKVAFPIDSQAEFATDENGFGVIKRPTHQNTSW 151
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1370466591  919 QANFY--PMPVMAYIQDAQKRLTLHTAQALGVSSLkDGQLEVILDRRLMQDDNR 970
Cdd:pfam07748  152 DLARFevPIHSWVDLSDSNYGVSLLNDSKYGGSSL-DGQLELSLLRRPLYPDPR 204
Alpha-mann_mid pfam09261
Alpha mannosidase middle domain; Members of this family adopt a structure consisting of three ...
502-606 2.64e-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: 115.44  E-value: 2.64e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  502 HYWTGYYTSRPFYKSLDRVLEAHLRGAEVLYSLAAAharrSGLAGRYPLSDftlLTEARRTLGLFQHHDAITGTAKEAVV 581
Cdd:pfam09261    1 EYHRGTYTSRADLKRLNRKLEHLLRAAEQLSSLAAL----SLLGYEYPKEE---LEELWKALLLNQFHDILPGSSIQEVY 73
                           90       100
                   ....*....|....*....|....*
gi 1370466591  582 VDYGVRLLRSLVNLKQVIIHAAHYL 606
Cdd:pfam09261   74 RDAEARLAEALKETEKLLEDALRLL 98
Alpha-mann_mid smart00872
Alpha mannosidase, middle domain; Members of this entry belong to the glycosyl hydrolase ...
503-588 7.08e-30

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: 113.42  E-value: 7.08e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591   503 YWTGYYTSRPFYKSLDRVLEAHLRGAEVLYSLAAAHArrsgLAGRYPLSDftlLTEARRTLGLFQHHDAITGTAKEAVVV 582
Cdd:smart00872    1 YHRGTYTSRPYLKRLNRRAESLLRAAEELAALAALLS----LGYKYPSEQ---LEELWKALLLNQHHDAITGTSIDEVYD 73

                    ....*.
gi 1370466591   583 DYGVRL 588
Cdd:smart00872   74 DYEKRL 79
GH38-57_N_LamB_YdjC_SF cd10785
Catalytic domain of glycoside hydrolase (GH) families 38 and 57, lactam utilization protein ...
169-347 5.77e-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: 109.65  E-value: 5.77e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  169 FVVPHSHNDPGWIKTFDKYYTEQTQHILNSMVSKLQEDPRRRFLWAEVSFFAKWWDNINVQKRAAVRRLVGNGQLEIATG 248
Cdd:cd10785      1 FINAHSHNPYVWIQTFEEWYFEATKATYIPLLMHFHRNFEMSFNIAPISYEALFYHDLGENIKLQMKSIQKNGQLEIGTH 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  249 GWVMPD--EANSHYFALIDQLIEGHQWLERNLGATPRSGWAVDPFG-----YSSTMPYLLRRANLTSMLIQRVHYAIKKH 321
Cdd:cd10785     81 GATHPDesEAQSHPENVYAQITEGITWLEKHMGVTPRHIWLHECFYnqakqLSQGIPYILQKSGFLYLFVQSRSISVKKE 160
                          170       180
                   ....*....|....*....|....*.
gi 1370466591  322 FAathslefMWRQTWDSDSSTDIFCH 347
Cdd:cd10785    161 LA-------LWRQIWYNKKDSGVFTF 179
GH38N_AMII_ER_cytosolic cd10789
N-terminal catalytic domain of endoplasmic reticulum(ER)/cytosolic class II alpha-mannosidases; ...
167-355 7.41e-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: 75.62  E-value: 7.41e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  167 QVFVVPHSHNDPGWIKTFdkyytEQT-QHILNSMVSKL---QEDPRRRFLWAEVSFFAkwWdninVQKR-----AAVRRL 237
Cdd:cd10789      1 KIYAVGHAHIDLAWLWPV-----RETrRKAARTFSTVLdlmEEYPDFVFTQSQAQLYE--W----LEEDypelfERIKER 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  238 VGNGQLEIATGGWVMPD------EAnshyfaLIDQLIEGHQWLERNLGATPRSGWAVDPFGYSSTMPYLLRRANLTSMLI 311
Cdd:cd10789     70 VKEGRWEPVGGMWVEPDcnlpsgES------LVRQFLYGQRYFREEFGVESRILWLPDSFGFSAALPQILKKSGIDYFVT 143
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1370466591  312 QRVHYAIKKHFaaTHSLeFMWRqtwdSDSSTDIFCHMMPFYSYD 355
Cdd:cd10789    144 QKLSWNDTNKF--PYDT-FRWR----GIDGSEVLAHFIPTGYYN 180
GH38N_AMII_ScAms1_like cd10812
N-terminal catalytic domain of yeast vacuolar alpha-mannosidases and similar proteins; ...
167-355 1.69e-12

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: 69.00  E-value: 1.69e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  167 QVFVVPHSHNDPGWIKTFdkyyTEQTQHILNSMVSKL---QEDPRRRFLWAEVSFFaKWWDNINVQKRAAVRRLVGNGQL 243
Cdd:cd10812      1 NVYGIGNCHIDTAWLWPF----SETQQKVARSWSTQCdlmDRYPEYRFVASQAQQF-KWLETLYPDLFEKVKEYVKQGRF 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  244 EIATGGWVMPDEANSHYFALIDQLIEGHQWLERNLGATPRSGWAVDPFGYSSTMPYLLRRANLTSMLIQRVHYAIKKHFA 323
Cdd:cd10812     76 HPIGGSWVENDTNMPSGESLARQFLYGQRYFESRFGKRCDTFWLPDTFGYSSQIPQLCRLAGMDYFFTQKLSWNNINSFP 155
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1370466591  324 atHSlEFMWRQTwdsdSSTDIFCHMMPFYSYD 355
Cdd:cd10812    156 --HS-TFNWVGI----DGTQVLVHMTPVNTYT 180
GH38N_AMII_EcMngB_like cd10815
N-terminal catalytic domain of Escherichia coli alpha-mannosidase MngB and its bacterial ...
167-495 1.98e-06

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: 50.61  E-value: 1.98e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  167 QVFVVPHSHNDPGWiktfdkYYTEQTQHIL--NSM---VSKLQEDPRRRF--LWAEVS----FFAkwwdnINVQKRAAVR 235
Cdd:cd10815      1 KVHVVPHTHWDREW------YFTTEDSRILlvNHMdevLDELENNPDFPYyvLDGQSSilddYLA-----VRPEDKERIK 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  236 RLVGNGQLEIatGGWvmpdeanshyFALIDQLIEGHQWLERNL----------GATPRSGWAVDPFGYSSTMPYLLRRAN 305
Cdd:cd10815     70 KLVKEGRLFI--GPW----------YTQTDELVVSGESIVRNLlygikdarklGGYMKIGYLPDSFGQSAQMPQIYNGFG 137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  306 LTSMLIQRvhyAIKKHfaATHSLEFMWRqtwdSDSSTDIFCHMMPF-YSYdvphtcgpdpkiccqfdFKRLPggrincpw 384
Cdd:cd10815    138 IDNAVFWR---GVSED--LVKSTEFIWK----SLDGSKVLAANIPFgYGI-----------------GKYLP-------- 183
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  385 kvppraITEANVAERaalLLDQYRKKSQLFRSNVLLVPLGDDFRYdkpqeWDaqfFNYQRLFDFFNSR-PNLHVQAqfGT 463
Cdd:cd10815    184 ------EDPDYLKKR---LDPILEKLERRATTDNILLPNGGDQMP-----IR---KNLPEVIEELNEIsPDYEYVI--SS 244
                          330       340       350
                   ....*....|....*....|....*....|..
gi 1370466591  464 LSDYFDALYKrtgvepgaRPPGFPVLSGDFFS 495
Cdd:cd10815    245 YEEFFKALEK--------NKDLLPTIEGELLD 268
GH38N_AMII_SpGH38_like cd10814
N-terminal catalytic domain of SPGH38, a putative alpha-mannosidase of Streptococcus pyogenes, ...
167-350 2.96e-06

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: 50.34  E-value: 2.96e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  167 QVFVVPHSHNDPGWIKTFDKYYTEQTqHILNSMVSKLQEDPRrrflwaEVSFfakWWD----------NINVQKRAAVRR 236
Cdd:cd10814      1 KVHIISHTHWDREWYLPFEEFRMRLI-DLIDRLLELLEEDPE------FKSF---HLDgqtivledylEVRPEKRERLKK 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  237 LVGNGQLEIatGGW-VMPDEanshyF-----ALIDQLIEGHQWLERnLGATPRSGWAVDPFGYSSTMPYLLRRANLTSML 310
Cdd:cd10814     71 LIREGKLVI--GPWyVLQDE-----FltsgeANIRNLLIGKKVAEE-FGKSMKIGYFPDTFGHIGQMPQILKGFGIDNAV 142
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1370466591  311 IQRvhyAIKKHFAATHslEFMWRqtwdSDSSTDIFCHMMP 350
Cdd:cd10814    143 FGR---GVKPTESQYS--EFWWE----SPDGSRVLGILLA 173
PRK09819 PRK09819
mannosylglycerate hydrolase;
168-354 7.77e-05

mannosylglycerate hydrolase;


Pssm-ID: 182093 [Multi-domain]  Cd Length: 875  Bit Score: 46.89  E-value: 7.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  168 VFVVPHSHNDPGWiktfdkYYTEQTQHIL--NSM---VSKLQEDPRRRF--LWAEVS----FFAkwwdnINVQKRAAVRR 236
Cdd:PRK09819     6 VHIVPHMHWDREW------YFTTERSRILlvNNMeeiLDRLEQDNDYKYyvLDGQTSlledYLA-----VKPEDKERVKK 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  237 LVGNGQLEIatGGWvmpdeanshyFALIDQLIEGHQWLERNL----------GATPRSGWAVDPFGYSSTMPYLLRRANL 306
Cdd:PRK09819    75 LVQAGKLII--GPW----------YTQTDQLVVSGESIVRNLlygirdcrefGEPMKIGYLPDSFGQSGQMPQIYNGFGI 142
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1370466591  307 TSMLIQRvhyAIKKHfAATHSLEFMWRqtwdSDSSTDIFCHMMPF-YSY 354
Cdd:PRK09819   143 TRTLFWR---GVSDR-HGTDKTEFLWQ----SDDGSEVLAQQLPLgYAI 183
GH38N_AMII_like_1 cd10791
N-terminal catalytic domain of mainly uncharacterized eukaryotic proteins similar to ...
167-301 1.08e-04

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: 1.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  167 QVFVVPHSHNDPGWIKTFDKYYTEQTQHILNSMVSKLQ---EDPRRRFLWAEVSFFA--KWWDNINVQKRAAVRRLVGNG 241
Cdd:cd10791      1 TVHVVHHSHTDIGYTDLQEKVDRYHVDYIPQALDLAEAtknYPEDARFRWTTESTWLveEYLKCASPEQRERLEQAVRRG 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  242 QLEIATGGWVMPDEANSHyfALIDQLIEGHQWLERNLGATPRSGWAVDPFGYSSTMPYLL 301
Cdd:cd10791     81 RIGWHALPLNITTELMDE--ELLRRGLYLSKELDRRFGLPIIVAMQTDVPGHTWGLVDVL 138
GH38N_AMII_1 cd10790
N-terminal catalytic domain of putative prokaryotic class II alpha-mannosidases; glycoside ...
168-332 7.50e-04

N-terminal catalytic domain of putative prokaryotic class II alpha-mannosidases; glycoside hydrolase family 38 (GH38); This mainly bacterial subfamily corresponds to a group of putative class II alpha-mannosidases, including various proteins assigned as alpha-mannosidases, Streptococcus pyogenes (SpGH38) encoded by ORF spy1604. Escherichia coli MngB encoded by the mngB/ybgG gene, and Thermotoga maritime TMM, and similar proteins. SpGH38 targets alpha-1,3 mannosidic linkages. 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. MngB exhibits alpha-mannosidase activity that catalyzes the conversion of 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. TMM is a homodimeric enzyme that hydrolyzes p-nitrophenyl-alpha-D-mannopyranoside, alpha -1,2-mannobiose, alpha -1,3-mannobiose, alpha -1,4-mannobiose, and alpha -1,6-mannobiose. The GH38 family contains retaining glycosyl hydrolases that 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. Divalent metal ions, such as zinc or cobalt ions, are suggested to be required for the catalytic activities of typical class II alpha-mannosidases. However, TMM requires the cobalt or cadmium for its activity. The cadmium ion dependency is unique to TMM. Moreover, TMM is inhibited by swainsonine but not 1-deoxymannojirimycin, which is in agreement with the features of cytosolic alpha-mannosidase.


Pssm-ID: 212102 [Multi-domain]  Cd Length: 273  Bit Score: 42.83  E-value: 7.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  168 VFVVPHSHNDPGWIKTfdkyyTEQTQHILNSMVSKL----QEDPRRRFLWAEVSFFAKWWDNINVQKRAAVRRLVGNGQL 243
Cdd:cd10790      2 VHIISHTHWDREWFAT-----TEQTHKWLINLFERLleliQKDPEYSFVLDGQTAILEDYLKVFPEREKKLRQAIKSGKL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  244 EIATggwvmpdeanshYFALIDQLIEGHQWLERNL----------GATPRSGWAVDPFGYSSTMPYLLRRANLTSMLIQR 313
Cdd:cd10790     77 IIGP------------YYIQIDWRITSEESIVRNFeigkkdcdrfGASMKIGWLPDSFGFISQLPQLMRKFGIEAVFLWR 144
                          170
                   ....*....|....*....
gi 1370466591  314 vhyAIKKHfAATHSLEFMW 332
Cdd:cd10790    145 ---GISPE-GSSPKIEFSW 159
GH38N_AMII_Man2C1 cd10813
N-terminal catalytic domain of mammalian cytosolic alpha-mannosidase Man2C1 and similar ...
167-332 1.73e-03

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: 41.61  E-value: 1.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  167 QVFVVPHSHNDPGWIKTfdkyYTEQTQHILNSMVSKLQ---EDPRRRFLWAEVSFFA---KWWDNI--NVQKRAAVRRLV 238
Cdd:cd10813      1 TIHAMGHCHIDSAWLWP----YEETIRKCARSWVTVLRlmeDYPDFTFACSQAQQLEwvkSWYPGLyeEIQERVKNGRFI 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466591  239 GNGqleiatGGWVMPDEANSHYFALIDQLIEGHQWLERNLGATPRSGWAVDPFGYSSTMPYLLRRANLTSMLIQRVHYAI 318
Cdd:cd10813     77 PVG------GTWVEMDGNLPSGESMVRQFLYGQRFFKEEFGITCKEFWLPDTFGYSAQLPQIMKGCGISRFLTQKLSWNL 150
                          170
                   ....*....|....
gi 1370466591  319 KKHFAatHSlEFMW 332
Cdd:cd10813    151 VNKFP--HH-TFFW 161
 
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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