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Conserved domains on  [gi|374532775|ref|NP_001243423|]
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alpha-mannosidase 2C1 isoform 2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MngB COG0383
Alpha-mannosidase [Carbohydrate transport and metabolism];
247-1043 0e+00

Alpha-mannosidase [Carbohydrate transport and metabolism];


:

Pssm-ID: 440152 [Multi-domain]  Cd Length: 798  Bit Score: 829.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  247 GESQHTIHATGHCHIDTAWLWPFKETVRKCARSWVTALQLMERNPEFIFACSQAQQLEWVKSRYPGLYSRIQEFACRGQF 326
Cdd:COG0383     2 GMKKKKVHAVGHAHIDRAWLWPVEETRRKLARTFSTVLDLLEEYPEFVFDGSTAQLYDYLKEHYPELFERIKKLVKEGRW 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  327 VPVGGTWVEMDGNLPSGEAMVRQFLQGQNFFLQEFGKMCSEFWLPDTFGYSAQLPQIMHGCGIRRFLTQKLSWNLVNSFP 406
Cdd:COG0383    82 EPVGGMWVEPDTNLPSGESLVRQLLYGQRFFKEEFGVDMKVGWLPDSFGYSAQLPQILKGAGIDYFVTQKGSWNDTNRFP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  407 HHTFFWEGLDGSRVLVHFPPgDSYGMQGSVEEVLKTVANNRDKGRANHSAFLFGFGDGGGGPTQTMLDRLKRLSNTDGLP 486
Cdd:COG0383   162 YHTFWWEGIDGSEVLTHFFP-NGYNSGLDPEELAGAWRNFEQKAVTDELLLPFGYGDGGGGPTREMLERARRLNDLPGLP 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  487 RVQLSSPRQLFSALESDSEQLCTWVGELFLELHNGTYTTHAQIKKGNRECERILHDVELLSSLALARSAQflYPAAQLQH 566
Cdd:COG0383   241 EVVISTPEDFFEALEEELPDLPVWQGELYLELHRGTYTSRADLKRLNRRAERLLREAEPLAALAALLGAE--YPQEELDE 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  567 LWRLLLLNQFHDVVTGSCIQMVAEEAMCHYEDIRSHGNTLLSAAAAALCAGEPGPEG---LLIVNTLPWKRIEVMALPKP 643
Cdd:COG0383   319 AWKLLLLNQFHDILPGSSIDEVYREAEARYEEALEEAESLIDEALRAIAGAIDLPEDgdpLVVFNTLPWPRSEVVELPLY 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  644 GGAHSLGLTPSPGDsaqhglcscssPHLTAAPAAPAACVRSARAP---------TDSASRPPPTKTDGSVTLDNGIIRVK 714
Cdd:COG0383   399 TPGKNFQLVDSDGK-----------ELPAQILEDGKILFSAEDLPalgyktlslVEGEASPESSVSVSENVLENEFLRVE 467
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  715 LDPTGRLTSLVLVASGREAIAEGavGNQFVLFDDVPLYWDAWDVmDYHLETRKPVLGQAGTLAVGTEGGLRGSAWFLLQI 794
Cdd:COG0383   468 IDENGSLTSIYDKETGREVLAGR--GNQLQLFEDSPDAGDAWDI-DPPYEDKPIELDELASIEVVESGPLRARLRVTRTF 544
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  795 SpNSRLSQEVVLDVGCPYVRFHTEVHWHEAHKFLKVEFPARVRSSQATYEIQFGHLQRPTHYNTSWDWARFEVWAHRWMD 874
Cdd:COG0383   545 G-RSTITQTITLRAGSPRLDFKTEVDWQERDHLLKVAFPTDVRADEATAEIQFGVIKRPTHPNTSWEKARFEVPAHRWVD 623
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  875 LSEHGFGLALLNDCKYGASVRGSILSLSLLRAPKAPDATADTGRHEFTYALMPHKGSFQDAGVIQAAYSLN--FPLLALP 952
Cdd:COG0383   624 LSEGGYGVALLNDGKYGYDVKDNTIRLTLLRSPVFPDPDADLGEHTFTYALYPHAGDWDEADVVQEAYELNtpLRVYQQP 703
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  953 APSPAPATSWSAFSVSSPAVVLETVKQAEsspQRRSLVLRLYEAHGSHVDCWLHLSLPVQEAILCDLLERPDPAghLTLR 1032
Cdd:COG0383   704 PHEGGLPPEFSLLSLDGPNLVLSAVKKAE---DGSGLILRLYEPSGERGTATLKFDFPLASAEEVNLLEEPLEE--LEVE 778
                         810
                  ....*....|.
gi 374532775 1033 DNRLKLTFSPF 1043
Cdd:COG0383   779 DNTVELELKPF 789
 
Name Accession Description Interval E-value
MngB COG0383
Alpha-mannosidase [Carbohydrate transport and metabolism];
247-1043 0e+00

Alpha-mannosidase [Carbohydrate transport and metabolism];


Pssm-ID: 440152 [Multi-domain]  Cd Length: 798  Bit Score: 829.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  247 GESQHTIHATGHCHIDTAWLWPFKETVRKCARSWVTALQLMERNPEFIFACSQAQQLEWVKSRYPGLYSRIQEFACRGQF 326
Cdd:COG0383     2 GMKKKKVHAVGHAHIDRAWLWPVEETRRKLARTFSTVLDLLEEYPEFVFDGSTAQLYDYLKEHYPELFERIKKLVKEGRW 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  327 VPVGGTWVEMDGNLPSGEAMVRQFLQGQNFFLQEFGKMCSEFWLPDTFGYSAQLPQIMHGCGIRRFLTQKLSWNLVNSFP 406
Cdd:COG0383    82 EPVGGMWVEPDTNLPSGESLVRQLLYGQRFFKEEFGVDMKVGWLPDSFGYSAQLPQILKGAGIDYFVTQKGSWNDTNRFP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  407 HHTFFWEGLDGSRVLVHFPPgDSYGMQGSVEEVLKTVANNRDKGRANHSAFLFGFGDGGGGPTQTMLDRLKRLSNTDGLP 486
Cdd:COG0383   162 YHTFWWEGIDGSEVLTHFFP-NGYNSGLDPEELAGAWRNFEQKAVTDELLLPFGYGDGGGGPTREMLERARRLNDLPGLP 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  487 RVQLSSPRQLFSALESDSEQLCTWVGELFLELHNGTYTTHAQIKKGNRECERILHDVELLSSLALARSAQflYPAAQLQH 566
Cdd:COG0383   241 EVVISTPEDFFEALEEELPDLPVWQGELYLELHRGTYTSRADLKRLNRRAERLLREAEPLAALAALLGAE--YPQEELDE 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  567 LWRLLLLNQFHDVVTGSCIQMVAEEAMCHYEDIRSHGNTLLSAAAAALCAGEPGPEG---LLIVNTLPWKRIEVMALPKP 643
Cdd:COG0383   319 AWKLLLLNQFHDILPGSSIDEVYREAEARYEEALEEAESLIDEALRAIAGAIDLPEDgdpLVVFNTLPWPRSEVVELPLY 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  644 GGAHSLGLTPSPGDsaqhglcscssPHLTAAPAAPAACVRSARAP---------TDSASRPPPTKTDGSVTLDNGIIRVK 714
Cdd:COG0383   399 TPGKNFQLVDSDGK-----------ELPAQILEDGKILFSAEDLPalgyktlslVEGEASPESSVSVSENVLENEFLRVE 467
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  715 LDPTGRLTSLVLVASGREAIAEGavGNQFVLFDDVPLYWDAWDVmDYHLETRKPVLGQAGTLAVGTEGGLRGSAWFLLQI 794
Cdd:COG0383   468 IDENGSLTSIYDKETGREVLAGR--GNQLQLFEDSPDAGDAWDI-DPPYEDKPIELDELASIEVVESGPLRARLRVTRTF 544
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  795 SpNSRLSQEVVLDVGCPYVRFHTEVHWHEAHKFLKVEFPARVRSSQATYEIQFGHLQRPTHYNTSWDWARFEVWAHRWMD 874
Cdd:COG0383   545 G-RSTITQTITLRAGSPRLDFKTEVDWQERDHLLKVAFPTDVRADEATAEIQFGVIKRPTHPNTSWEKARFEVPAHRWVD 623
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  875 LSEHGFGLALLNDCKYGASVRGSILSLSLLRAPKAPDATADTGRHEFTYALMPHKGSFQDAGVIQAAYSLN--FPLLALP 952
Cdd:COG0383   624 LSEGGYGVALLNDGKYGYDVKDNTIRLTLLRSPVFPDPDADLGEHTFTYALYPHAGDWDEADVVQEAYELNtpLRVYQQP 703
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  953 APSPAPATSWSAFSVSSPAVVLETVKQAEsspQRRSLVLRLYEAHGSHVDCWLHLSLPVQEAILCDLLERPDPAghLTLR 1032
Cdd:COG0383   704 PHEGGLPPEFSLLSLDGPNLVLSAVKKAE---DGSGLILRLYEPSGERGTATLKFDFPLASAEEVNLLEEPLEE--LEVE 778
                         810
                  ....*....|.
gi 374532775 1033 DNRLKLTFSPF 1043
Cdd:COG0383   779 DNTVELELKPF 789
GH38N_AMII_Man2C1 cd10813
N-terminal catalytic domain of mammalian cytosolic alpha-mannosidase Man2C1 and similar ...
252-503 3.01e-179

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: 521.95  E-value: 3.01e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  252 TIHATGHCHIDTAWLWPFKETVRKCARSWVTALQLMERNPEFIFACSQAQQLEWVKSRYPGLYSRIQEFACRGQFVPVGG 331
Cdd:cd10813     1 TIHAMGHCHIDSAWLWPYEETIRKCARSWVTVLRLMEDYPDFTFACSQAQQLEWVKSWYPGLYEEIQERVKNGRFIPVGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  332 TWVEMDGNLPSGEAMVRQFLQGQNFFLQEFGKMCSEFWLPDTFGYSAQLPQIMHGCGIRRFLTQKLSWNLVNSFPHHTFF 411
Cdd:cd10813    81 TWVEMDGNLPSGESMVRQFLYGQRFFKEEFGITCKEFWLPDTFGYSAQLPQIMKGCGISRFLTQKLSWNLVNKFPHHTFF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  412 WEGLDGSRVLVHFPPGDSYGMQGSVEEVLKTVANNRDKGRANHSAFLFGFGDGGGGPTQTMLDRLKRLSNTDGLPRVQLS 491
Cdd:cd10813   161 WEGIDGSRVLTHFPPGDSYGMQGKVEEVLKTVANFKDKGRSNHSMMLFGFGDGGGGPTQNMLERLKRLQDTDGLPRVKLS 240
                         250
                  ....*....|..
gi 374532775  492 SPRQLFSALESD 503
Cdd:cd10813   241 TPDEFFSAVEKD 252
Glyco_hydro_38N pfam01074
Glycosyl hydrolases family 38 N-terminal domain; Glycosyl hydrolases are key enzymes of ...
252-511 1.68e-101

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: 319.96  E-value: 1.68e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775   252 TIHATGHCHIDTAWLWPFKETVRKCARSWVTALQLMERNPEFIFACSQAQQLEWVKSRYPGLYSRIQEFACRGQFVPVGG 331
Cdd:pfam01074    1 TVHLVGHSHIDVGWLWTVDETRRKVQRTFSSVLALLDRDPDRRFIWSEAQFFAWWWEDQPELFKRIKKLVAEGRLEPVGG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775   332 TWVEMDGNLPSGEAMVRQFLQGQNFFLQEFGKMCSEFWLPDTFGYSAQLPQIMHGCGIRRFLTQKLSWNLVNSF-PHHTF 410
Cdd:pfam01074   81 GWVEPDENLPSGESLIRQFLYGQRFFKEEFGVRPRVGWLPDPFGYSATLPQILKQAGIDYFLTQRLHWNDKNKFnPHLEF 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775   411 FWEGLDGSRVLVHFPPGDSY-----GMQGSVEEVLKTVANNRDKGRANHSAFLFGFGDGGGGPTQTMLDRLKRLSNTDGL 485
Cdd:pfam01074  161 IWRGSDGTEIFTHMPPFDYYptygfQFQERAEDLLAYARNYADKTRTNHVLLPFGDGDGGGGPTDEMLEYINRWNALPGL 240
                          250       260       270
                   ....*....|....*....|....*....|.
gi 374532775   486 PRVQLSSPRQLFSALESD-----SEQLCTWV 511
Cdd:pfam01074  241 PKVQYGTPSDYFDALEKAtwptkTDDFPPYA 271
Alpha-mann_mid smart00872
Alpha mannosidase, middle domain; Members of this entry belong to the glycosyl hydrolase ...
518-596 1.21e-23

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: 95.31  E-value: 1.21e-23
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 374532775    518 LHNGTYTTHAQIKKGNRECERILHDVELLSSLALARSAQFLYPAAQLQHLWRLLLLNQFHDVVTGSCIQMVAEEAMCHY 596
Cdd:smart00872    1 YHRGTYTSRPYLKRLNRRAESLLRAAEELAALAALLSLGYKYPSEQLEELWKALLLNQHHDAITGTSIDEVYDDYEKRL 79
PRK09819 PRK09819
mannosylglycerate hydrolase;
252-994 1.81e-14

mannosylglycerate hydrolase;


Pssm-ID: 182093 [Multi-domain]  Cd Length: 875  Bit Score: 78.09  E-value: 1.81e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  252 TIHATGHCHIDTAWLWPFKETVRKCARSWVTALQLMERNPEFIFACSQAQQ--LEWVKSRYPGLYSRIQEFACRGQFVpV 329
Cdd:PRK09819    5 KVHIVPHMHWDREWYFTTERSRILLVNNMEEILDRLEQDNDYKYYVLDGQTslLEDYLAVKPEDKERVKKLVQAGKLI-I 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  330 GGTWVEMDGNLPSGEAMVRQFLQGQNFfLQEFGKMCSEFWLPDTFGYSAQLPQIMHGCGIRRFLTqklsWNLV--NSFPH 407
Cdd:PRK09819   84 GPWYTQTDQLVVSGESIVRNLLYGIRD-CREFGEPMKIGYLPDSFGQSGQMPQIYNGFGITRTLF----WRGVsdRHGTD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  408 HT-FFWEGLDGSRVLVH-FPPGDSYGmqGSVEEVLKTVANNRDK-----GRANHSAFLFGFGDGGGGPTQ----TMLDRL 476
Cdd:PRK09819  159 KTeFLWQSDDGSEVLAQqLPLGYAIG--KYLPEDEEELKKRLDEyfgvlEKKSSTKNILLPNGHDQMPLQknlfEVMDKL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  477 KRLSNTDglpRVQLSSPRQLFSALESDSEQLCTWVGEL----FLELHNGTYTTHAQIKKGNRECERILHDVeLLSSLALA 552
Cdd:PRK09819  237 NEIYPER---EFVISRFENVFEKLEKQRDNLPTLKGEFidgkYMRVHRSIFSTRMDIKIANARIENKIVNV-LEPLASIA 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  553 RSAQFLYPAAQLQHLWRLLLLNQFHDVVTGSCIQMVAEEAMCHY---EDI-----------------RSHGNTllsaaaa 612
Cdd:PRK09819  313 YSLGFEYPHGLLEKIWKEMFKNHAHDSIGCCCSDTVHRDIVARYklaEDLadnlldfymrkiadnmpQSDADK------- 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  613 alcagepgpegLLIVNTLPWKRIEV--MALPKPGGAHSlgLTPSPGDSAQHglcscssphltaapaapaaCVRSARAPTD 690
Cdd:PRK09819  386 -----------LTVFNLLPYEREEVinTTVYLPASQFT--LRDDRGNPLPY-------------------TIREKRDIDP 433
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  691 ---------SASRPPPTKTDGSVTLDN----GIIRVKLDPtGRLTSLVLVASGREAIAEgavgNQF-------------- 743
Cdd:PRK09819  434 glldrqivhYGNYDPFMEFDIQINVQIlpamGYRTLYIEL-NEEGNVIEPKSSAEGIIE----NEFyqitlnengtltiv 508
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  744 -----VLFDDVPLY---WDAWDVMDYHlETRKPVLGQAGTLAVGTEggLRGSAW-------FLLQISPN--SR------- 799
Cdd:PRK09819  509 dkksgKTYDRQLIIeenGDDGDEYDYS-PPREDWVITSAEAVPSVE--ISHSAWqsravirYRLAVPKNleERaagqktg 585
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  800 ---LSQEVVLDVGCPYVRFHTEVHWH-EAHKfLKVEFPARVRSSQATYEIQFGHLQRPThYNTSWDWARFEVWAHR---- 871
Cdd:PRK09819  586 rmpVKLVVTLSKNSRRIDFDVNLDNQaDDHR-LRVLFPTEIASKFSLADQQFGSITRPV-NDPAMDVWEQEGWQEApisi 663
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  872 -----WMDLSEHGFGLALLNDCKYGASVRGS---ILSLSLLRA------------PKAPD----ATADT---GRHEFTYA 924
Cdd:PRK09819  664 epmqsFVALHDERHGVAVFTEGVREYEIIGEnydTIALTLFRGvgllgkedllyrPGRPSgikiPTPDSqllGELSFRFS 743
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  925 LMPHKGSFQDAGVIQAA---------YS-LNFPLLALPAPSPAPATSWSAFSVSSPAVVLETVKQAESspqRRSLVLRLY 994
Cdd:PRK09819  744 LTSYEGTFDEAGVAQQAkeyltpvqcYNkIPFLNMRLNDEEFTLPESYSLLKMPPDGAVLSAVKKAED---RDGLILRFF 820
 
Name Accession Description Interval E-value
MngB COG0383
Alpha-mannosidase [Carbohydrate transport and metabolism];
247-1043 0e+00

Alpha-mannosidase [Carbohydrate transport and metabolism];


Pssm-ID: 440152 [Multi-domain]  Cd Length: 798  Bit Score: 829.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  247 GESQHTIHATGHCHIDTAWLWPFKETVRKCARSWVTALQLMERNPEFIFACSQAQQLEWVKSRYPGLYSRIQEFACRGQF 326
Cdd:COG0383     2 GMKKKKVHAVGHAHIDRAWLWPVEETRRKLARTFSTVLDLLEEYPEFVFDGSTAQLYDYLKEHYPELFERIKKLVKEGRW 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  327 VPVGGTWVEMDGNLPSGEAMVRQFLQGQNFFLQEFGKMCSEFWLPDTFGYSAQLPQIMHGCGIRRFLTQKLSWNLVNSFP 406
Cdd:COG0383    82 EPVGGMWVEPDTNLPSGESLVRQLLYGQRFFKEEFGVDMKVGWLPDSFGYSAQLPQILKGAGIDYFVTQKGSWNDTNRFP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  407 HHTFFWEGLDGSRVLVHFPPgDSYGMQGSVEEVLKTVANNRDKGRANHSAFLFGFGDGGGGPTQTMLDRLKRLSNTDGLP 486
Cdd:COG0383   162 YHTFWWEGIDGSEVLTHFFP-NGYNSGLDPEELAGAWRNFEQKAVTDELLLPFGYGDGGGGPTREMLERARRLNDLPGLP 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  487 RVQLSSPRQLFSALESDSEQLCTWVGELFLELHNGTYTTHAQIKKGNRECERILHDVELLSSLALARSAQflYPAAQLQH 566
Cdd:COG0383   241 EVVISTPEDFFEALEEELPDLPVWQGELYLELHRGTYTSRADLKRLNRRAERLLREAEPLAALAALLGAE--YPQEELDE 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  567 LWRLLLLNQFHDVVTGSCIQMVAEEAMCHYEDIRSHGNTLLSAAAAALCAGEPGPEG---LLIVNTLPWKRIEVMALPKP 643
Cdd:COG0383   319 AWKLLLLNQFHDILPGSSIDEVYREAEARYEEALEEAESLIDEALRAIAGAIDLPEDgdpLVVFNTLPWPRSEVVELPLY 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  644 GGAHSLGLTPSPGDsaqhglcscssPHLTAAPAAPAACVRSARAP---------TDSASRPPPTKTDGSVTLDNGIIRVK 714
Cdd:COG0383   399 TPGKNFQLVDSDGK-----------ELPAQILEDGKILFSAEDLPalgyktlslVEGEASPESSVSVSENVLENEFLRVE 467
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  715 LDPTGRLTSLVLVASGREAIAEGavGNQFVLFDDVPLYWDAWDVmDYHLETRKPVLGQAGTLAVGTEGGLRGSAWFLLQI 794
Cdd:COG0383   468 IDENGSLTSIYDKETGREVLAGR--GNQLQLFEDSPDAGDAWDI-DPPYEDKPIELDELASIEVVESGPLRARLRVTRTF 544
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  795 SpNSRLSQEVVLDVGCPYVRFHTEVHWHEAHKFLKVEFPARVRSSQATYEIQFGHLQRPTHYNTSWDWARFEVWAHRWMD 874
Cdd:COG0383   545 G-RSTITQTITLRAGSPRLDFKTEVDWQERDHLLKVAFPTDVRADEATAEIQFGVIKRPTHPNTSWEKARFEVPAHRWVD 623
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  875 LSEHGFGLALLNDCKYGASVRGSILSLSLLRAPKAPDATADTGRHEFTYALMPHKGSFQDAGVIQAAYSLN--FPLLALP 952
Cdd:COG0383   624 LSEGGYGVALLNDGKYGYDVKDNTIRLTLLRSPVFPDPDADLGEHTFTYALYPHAGDWDEADVVQEAYELNtpLRVYQQP 703
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  953 APSPAPATSWSAFSVSSPAVVLETVKQAEsspQRRSLVLRLYEAHGSHVDCWLHLSLPVQEAILCDLLERPDPAghLTLR 1032
Cdd:COG0383   704 PHEGGLPPEFSLLSLDGPNLVLSAVKKAE---DGSGLILRLYEPSGERGTATLKFDFPLASAEEVNLLEEPLEE--LEVE 778
                         810
                  ....*....|.
gi 374532775 1033 DNRLKLTFSPF 1043
Cdd:COG0383   779 DNTVELELKPF 789
GH38N_AMII_Man2C1 cd10813
N-terminal catalytic domain of mammalian cytosolic alpha-mannosidase Man2C1 and similar ...
252-503 3.01e-179

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: 521.95  E-value: 3.01e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  252 TIHATGHCHIDTAWLWPFKETVRKCARSWVTALQLMERNPEFIFACSQAQQLEWVKSRYPGLYSRIQEFACRGQFVPVGG 331
Cdd:cd10813     1 TIHAMGHCHIDSAWLWPYEETIRKCARSWVTVLRLMEDYPDFTFACSQAQQLEWVKSWYPGLYEEIQERVKNGRFIPVGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  332 TWVEMDGNLPSGEAMVRQFLQGQNFFLQEFGKMCSEFWLPDTFGYSAQLPQIMHGCGIRRFLTQKLSWNLVNSFPHHTFF 411
Cdd:cd10813    81 TWVEMDGNLPSGESMVRQFLYGQRFFKEEFGITCKEFWLPDTFGYSAQLPQIMKGCGISRFLTQKLSWNLVNKFPHHTFF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  412 WEGLDGSRVLVHFPPGDSYGMQGSVEEVLKTVANNRDKGRANHSAFLFGFGDGGGGPTQTMLDRLKRLSNTDGLPRVQLS 491
Cdd:cd10813   161 WEGIDGSRVLTHFPPGDSYGMQGKVEEVLKTVANFKDKGRSNHSMMLFGFGDGGGGPTQNMLERLKRLQDTDGLPRVKLS 240
                         250
                  ....*....|..
gi 374532775  492 SPRQLFSALESD 503
Cdd:cd10813   241 TPDEFFSAVEKD 252
GH38N_AMII_ER_cytosolic cd10789
N-terminal catalytic domain of endoplasmic reticulum(ER)/cytosolic class II alpha-mannosidases; ...
252-503 1.33e-123

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: 377.62  E-value: 1.33e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  252 TIHATGHCHIDTAWLWPFKETVRKCARSWVTALQLMERNPEFIFACSQAQQLEWVKSRYPGLYSRIQEFACRGQFVPVGG 331
Cdd:cd10789     1 KIYAVGHAHIDLAWLWPVRETRRKAARTFSTVLDLMEEYPDFVFTQSQAQLYEWLEEDYPELFERIKERVKEGRWEPVGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  332 TWVEMDGNLPSGEAMVRQFLQGQNFFLQEFGKMCSEFWLPDTFGYSAQLPQIMHGCGIRRFLTQKLSWNLVNSFPHHTFF 411
Cdd:cd10789    81 MWVEPDCNLPSGESLVRQFLYGQRYFREEFGVESRILWLPDSFGFSAALPQILKKSGIDYFVTQKLSWNDTNKFPYDTFR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  412 WEGLDGSRVLVHFPPGDSYGMQGSVEEVLKTVANNRDKGRANHSAFLFGFGDGGGGPTQTMLDRLKRLSNTDGLPRVQLS 491
Cdd:cd10789   161 WRGIDGSEVLAHFIPTGYYNGDLTPEEILEAWRNFRDKDVSDELLLLYGVGDGGGGPTREMLERLRRLKDLPGLPRVEFS 240
                         250
                  ....*....|..
gi 374532775  492 SPRQLFSALESD 503
Cdd:cd10789   241 TPEEFFERLEEE 252
GH38N_AMII_ScAms1_like cd10812
N-terminal catalytic domain of yeast vacuolar alpha-mannosidases and similar proteins; ...
253-490 2.22e-104

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: 327.09  E-value: 2.22e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  253 IHATGHCHIDTAWLWPFKETVRKCARSWVTALQLMERNPEFIFACSQAQQLEWVKSRYPGLYSRIQEFACRGQFVPVGGT 332
Cdd:cd10812     2 VYGIGNCHIDTAWLWPFSETQQKVARSWSTQCDLMDRYPEYRFVASQAQQFKWLETLYPDLFEKVKEYVKQGRFHPIGGS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  333 WVEMDGNLPSGEAMVRQFLQGQNFFLQEFGKMCSEFWLPDTFGYSAQLPQIMHGCGIRRFLTQKLSWNLVNSFPHHTFFW 412
Cdd:cd10812    82 WVENDTNMPSGESLARQFLYGQRYFESRFGKRCDTFWLPDTFGYSSQIPQLCRLAGMDYFFTQKLSWNNINSFPHSTFNW 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  413 EGLDGSRVLVHFPPGDSYGMQGSVEEVLKTVANNRDKGRANHSAFLFGFGDGGGGPTQTMLDRLKRL-----SNTDGLPR 487
Cdd:cd10812   162 VGIDGTQVLVHMTPVNTYTADASVGDVLRSIKNHKDLENDDTGLLLFGKGDGGGGPLAEMLEKLRRIraaanNGAGDLPK 241

                  ...
gi 374532775  488 VQL 490
Cdd:cd10812   242 VQL 244
Glyco_hydro_38N pfam01074
Glycosyl hydrolases family 38 N-terminal domain; Glycosyl hydrolases are key enzymes of ...
252-511 1.68e-101

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: 319.96  E-value: 1.68e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775   252 TIHATGHCHIDTAWLWPFKETVRKCARSWVTALQLMERNPEFIFACSQAQQLEWVKSRYPGLYSRIQEFACRGQFVPVGG 331
Cdd:pfam01074    1 TVHLVGHSHIDVGWLWTVDETRRKVQRTFSSVLALLDRDPDRRFIWSEAQFFAWWWEDQPELFKRIKKLVAEGRLEPVGG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775   332 TWVEMDGNLPSGEAMVRQFLQGQNFFLQEFGKMCSEFWLPDTFGYSAQLPQIMHGCGIRRFLTQKLSWNLVNSF-PHHTF 410
Cdd:pfam01074   81 GWVEPDENLPSGESLIRQFLYGQRFFKEEFGVRPRVGWLPDPFGYSATLPQILKQAGIDYFLTQRLHWNDKNKFnPHLEF 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775   411 FWEGLDGSRVLVHFPPGDSY-----GMQGSVEEVLKTVANNRDKGRANHSAFLFGFGDGGGGPTQTMLDRLKRLSNTDGL 485
Cdd:pfam01074  161 IWRGSDGTEIFTHMPPFDYYptygfQFQERAEDLLAYARNYADKTRTNHVLLPFGDGDGGGGPTDEMLEYINRWNALPGL 240
                          250       260       270
                   ....*....|....*....|....*....|.
gi 374532775   486 PRVQLSSPRQLFSALESD-----SEQLCTWV 511
Cdd:pfam01074  241 PKVQYGTPSDYFDALEKAtwptkTDDFPPYA 271
Glyco_hydro_38C pfam07748
Glycosyl hydrolases family 38 C-terminal domain; Glycosyl hydrolases are key enzymes of ...
706-913 3.98e-74

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: 243.32  E-value: 3.98e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775   706 LDNGIIRVKLDP-TGRLTSLVLVASGREAIAEgaVGNQFVLFDDVPLYWDAWDVMDYHleTRKPVLGQAGTLAVGTEGGL 784
Cdd:pfam07748    1 LENGFLKVEFDNdTGTLTSIYDKELSREVLAE--VGNQFGLYEDIPGYSDAWDFRPFY--EAKPLEVDEQSIEVVEDGPL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775   785 RGSAWFLLQISPnSRLSQEVVLDVGCPYVRFHTEVHWHEAHKFLKVEFPARVRSSQATYEIQFGHLQRPTHYNTSWDWAR 864
Cdd:pfam07748   77 VAEVHVKFKIGG-SEISQVIRLYKGSPRLEFETTVDWHEREVLLKVAFPIDSQAEFATDENGFGVIKRPTHQNTSWDLAR 155
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 374532775   865 FEVWAHRWMDLSEHGFGLALLNDCKYGASVRGSILSLSLLRAPKAPDAT 913
Cdd:pfam07748  156 FEVPIHSWVDLSDSNYGVSLLNDSKYGGSSLDGQLELSLLRRPLYPDPR 204
GH38N_AMII_like cd10786
N-terminal catalytic domain of class II alpha-mannosidases and similar proteins; glycoside ...
252-454 9.34e-39

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: 144.85  E-value: 9.34e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  252 TIHATGHCHIDTAWLWPFKETVRKCARSWV-TALQLMERNPEFIFACSQAQQLEWVKSRYPGLYSRIQEFACRGQFVPVG 330
Cdd:cd10786     1 TVHLVPHSHYDVGWLQTFEQYYQINFKAILdKALRLLDANPEYKFLIEEVILLERYWDVRPDLKAKLKQAVRSGRLEIAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  331 GTWVEMDGNLPSGEAMVRQFLQGQNFFLQEFGKMCSEFWLPDTFGYSAQLPQIMHGCGIRRFLTQKLSWNLVNSFPHHTF 410
Cdd:cd10786    81 GGYVMPDTNLPDGESLVRQILLGKRWLKEFLGARPPVMWQADVFGHSPQLPQILAKSGFTGFAFGRGPYSQKRMQRPSEF 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 374532775  411 FWEGLDGSRVLVHF---------------PPGDSYGMQG--SVEEVLKTVANNRDKGRANH 454
Cdd:cd10786   161 LWRGLDGTRILTHWmpngysdgpflcgpdIPGDNSGPNAlaSLEALVEQWKKLAELGATNH 221
Alpha-mann_mid pfam09261
Alpha mannosidase middle domain; Members of this family adopt a structure consisting of three ...
517-604 2.66e-24

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: 98.10  E-value: 2.66e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775   517 ELHNGTYTTHAQIKKGNRECERILHDVELLSSLALARSAQFLYPAAQLQHLWRLLLLNQFHDVVTGSCIQMVAEEAMCHY 596
Cdd:pfam09261    1 EYHRGTYTSRADLKRLNRKLEHLLRAAEQLSSLAALSLLGYEYPKEELEELWKALLLNQFHDILPGSSIQEVYRDAEARL 80

                   ....*...
gi 374532775   597 EDIRSHGN 604
Cdd:pfam09261   81 AEALKETE 88
Alpha-mann_mid smart00872
Alpha mannosidase, middle domain; Members of this entry belong to the glycosyl hydrolase ...
518-596 1.21e-23

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: 95.31  E-value: 1.21e-23
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 374532775    518 LHNGTYTTHAQIKKGNRECERILHDVELLSSLALARSAQFLYPAAQLQHLWRLLLLNQFHDVVTGSCIQMVAEEAMCHY 596
Cdd:smart00872    1 YHRGTYTSRPYLKRLNRRAESLLRAAEELAALAALLSLGYKYPSEQLEELWKALLLNQHHDAITGTSIDEVYDDYEKRL 79
GH38N_AMII_1 cd10790
N-terminal catalytic domain of putative prokaryotic class II alpha-mannosidases; glycoside ...
253-427 6.81e-19

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: 87.90  E-value: 6.81e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  253 IHATGHCHIDTAWLWPFKETvrkcaRSWVTAL-----QLMERNPEFIFACS-QAQQLEWVKSRYPGLYSRIQEFACRGQF 326
Cdd:cd10790     2 VHIISHTHWDREWFATTEQT-----HKWLINLferllELIQKDPEYSFVLDgQTAILEDYLKVFPEREKKLRQAIKSGKL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  327 VpVGGTWVEMDGNLPSGEAMVRQFLQGQNFFLQeFGKMCSEFWLPDTFGYSAQLPQIMHGCGIRR-FLTQKLSwnLVNSF 405
Cdd:cd10790    77 I-IGPYYIQIDWRITSEESIVRNFEIGKKDCDR-FGASMKIGWLPDSFGFISQLPQLMRKFGIEAvFLWRGIS--PEGSS 152
                         170       180
                  ....*....|....*....|..
gi 374532775  406 PHHTFFWEGLDGSRVLVHFPPG 427
Cdd:cd10790   153 PKIEFSWQSPDGSRVLGVFLAG 174
GH38N_AMII_SpGH38_like cd10814
N-terminal catalytic domain of SPGH38, a putative alpha-mannosidase of Streptococcus pyogenes, ...
252-422 5.11e-17

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: 82.31  E-value: 5.11e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  252 TIHATGHCHIDTAWLWPFkETVRKCARSWV-TALQLMERNPEF--IFACSQAQQLEWVKSRYPGLYSRIQEFACRGQFVp 328
Cdd:cd10814     1 KVHIISHTHWDREWYLPF-EEFRMRLIDLIdRLLELLEEDPEFksFHLDGQTIVLEDYLEVRPEKRERLKKLIREGKLV- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  329 VGGTWVEMDGNLPSGEAMVRQFLQGQNFfLQEFGKMCSEFWLPDTFGYSAQLPQIMHGCGIR-----RFLTQKLSwnlvn 403
Cdd:cd10814    79 IGPWYVLQDEFLTSGEANIRNLLIGKKV-AEEFGKSMKIGYFPDTFGHIGQMPQILKGFGIDnavfgRGVKPTES----- 152
                         170
                  ....*....|....*....
gi 374532775  404 sfPHHTFFWEGLDGSRVLV 422
Cdd:cd10814   153 --QYSEFWWESPDGSRVLG 169
GH38N_AMII_EcMngB_like cd10815
N-terminal catalytic domain of Escherichia coli alpha-mannosidase MngB and its bacterial ...
252-514 7.93e-16

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: 78.73  E-value: 7.93e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  252 TIHATGHCHIDTAW-----------LWPFKETvrkcarswvtaLQLMERNPEFIFACSQAQQ------LEWvksrYPGLY 314
Cdd:cd10815     1 KVHVVPHTHWDREWyfttedsrillVNHMDEV-----------LDELENNPDFPYYVLDGQSsilddyLAV----RPEDK 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  315 SRIQEFACRGQ-FVpvgGTW-VEMDGNLPSGEAMVRQFLQGQnfflqefgKMCSEF-------WLPDTFGYSAQLPQIMH 385
Cdd:cd10815    66 ERIKKLVKEGRlFI---GPWyTQTDELVVSGESIVRNLLYGI--------KDARKLggymkigYLPDSFGQSAQMPQIYN 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  386 GCGIRRFLTQK-LSWNLVNSFphhTFFWEGLDGSRVL-VHFPPGDSYGM-----QGSVEEVLKTVANNRDKGRANHsafl 458
Cdd:cd10815   135 GFGIDNAVFWRgVSEDLVKST---EFIWKSLDGSKVLaANIPFGYGIGKylpedPDYLKKRLDPILEKLERRATTD---- 207
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 374532775  459 fgfgdGGGGPT-----------QTMLDRLKRLSNTDglpRVQLSSPRQLFSALESDSEQLCTWVGEL 514
Cdd:cd10815   208 -----NILLPNggdqmpirknlPEVIEELNEISPDY---EYVISSYEEFFKALEKNKDLLPTIEGEL 266
PRK09819 PRK09819
mannosylglycerate hydrolase;
252-994 1.81e-14

mannosylglycerate hydrolase;


Pssm-ID: 182093 [Multi-domain]  Cd Length: 875  Bit Score: 78.09  E-value: 1.81e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  252 TIHATGHCHIDTAWLWPFKETVRKCARSWVTALQLMERNPEFIFACSQAQQ--LEWVKSRYPGLYSRIQEFACRGQFVpV 329
Cdd:PRK09819    5 KVHIVPHMHWDREWYFTTERSRILLVNNMEEILDRLEQDNDYKYYVLDGQTslLEDYLAVKPEDKERVKKLVQAGKLI-I 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  330 GGTWVEMDGNLPSGEAMVRQFLQGQNFfLQEFGKMCSEFWLPDTFGYSAQLPQIMHGCGIRRFLTqklsWNLV--NSFPH 407
Cdd:PRK09819   84 GPWYTQTDQLVVSGESIVRNLLYGIRD-CREFGEPMKIGYLPDSFGQSGQMPQIYNGFGITRTLF----WRGVsdRHGTD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  408 HT-FFWEGLDGSRVLVH-FPPGDSYGmqGSVEEVLKTVANNRDK-----GRANHSAFLFGFGDGGGGPTQ----TMLDRL 476
Cdd:PRK09819  159 KTeFLWQSDDGSEVLAQqLPLGYAIG--KYLPEDEEELKKRLDEyfgvlEKKSSTKNILLPNGHDQMPLQknlfEVMDKL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  477 KRLSNTDglpRVQLSSPRQLFSALESDSEQLCTWVGEL----FLELHNGTYTTHAQIKKGNRECERILHDVeLLSSLALA 552
Cdd:PRK09819  237 NEIYPER---EFVISRFENVFEKLEKQRDNLPTLKGEFidgkYMRVHRSIFSTRMDIKIANARIENKIVNV-LEPLASIA 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  553 RSAQFLYPAAQLQHLWRLLLLNQFHDVVTGSCIQMVAEEAMCHY---EDI-----------------RSHGNTllsaaaa 612
Cdd:PRK09819  313 YSLGFEYPHGLLEKIWKEMFKNHAHDSIGCCCSDTVHRDIVARYklaEDLadnlldfymrkiadnmpQSDADK------- 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  613 alcagepgpegLLIVNTLPWKRIEV--MALPKPGGAHSlgLTPSPGDSAQHglcscssphltaapaapaaCVRSARAPTD 690
Cdd:PRK09819  386 -----------LTVFNLLPYEREEVinTTVYLPASQFT--LRDDRGNPLPY-------------------TIREKRDIDP 433
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  691 ---------SASRPPPTKTDGSVTLDN----GIIRVKLDPtGRLTSLVLVASGREAIAEgavgNQF-------------- 743
Cdd:PRK09819  434 glldrqivhYGNYDPFMEFDIQINVQIlpamGYRTLYIEL-NEEGNVIEPKSSAEGIIE----NEFyqitlnengtltiv 508
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  744 -----VLFDDVPLY---WDAWDVMDYHlETRKPVLGQAGTLAVGTEggLRGSAW-------FLLQISPN--SR------- 799
Cdd:PRK09819  509 dkksgKTYDRQLIIeenGDDGDEYDYS-PPREDWVITSAEAVPSVE--ISHSAWqsravirYRLAVPKNleERaagqktg 585
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  800 ---LSQEVVLDVGCPYVRFHTEVHWH-EAHKfLKVEFPARVRSSQATYEIQFGHLQRPThYNTSWDWARFEVWAHR---- 871
Cdd:PRK09819  586 rmpVKLVVTLSKNSRRIDFDVNLDNQaDDHR-LRVLFPTEIASKFSLADQQFGSITRPV-NDPAMDVWEQEGWQEApisi 663
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  872 -----WMDLSEHGFGLALLNDCKYGASVRGS---ILSLSLLRA------------PKAPD----ATADT---GRHEFTYA 924
Cdd:PRK09819  664 epmqsFVALHDERHGVAVFTEGVREYEIIGEnydTIALTLFRGvgllgkedllyrPGRPSgikiPTPDSqllGELSFRFS 743
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  925 LMPHKGSFQDAGVIQAA---------YS-LNFPLLALPAPSPAPATSWSAFSVSSPAVVLETVKQAESspqRRSLVLRLY 994
Cdd:PRK09819  744 LTSYEGTFDEAGVAQQAkeyltpvqcYNkIPFLNMRLNDEEFTLPESYSLLKMPPDGAVLSAVKKAED---RDGLILRFF 820
Glyco_hydro38C2 pfam17677
Glycosyl hydrolases family 38 C-terminal beta sandwich domain; This domain is found at the ...
971-1043 4.81e-13

Glycosyl hydrolases family 38 C-terminal beta sandwich domain; This domain is found at the C-terminal end of various glycosyl hydrolases belonging to family 38. The domain has a beta sandwich fold.


Pssm-ID: 465454 [Multi-domain]  Cd Length: 71  Bit Score: 64.96  E-value: 4.81e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 374532775   971 AVVLETVKQAESSpqrRSLVLRLYEAHGSHVDCWLHLSLPVQEAILCDLLERPdpaghLTLRDNRLKLTFSPF 1043
Cdd:pfam17677    1 NVILTALKKAEDS---DDIILRLYNLSGEEEKLTLKLPGPPKSVYETNLLEES-----LEGSPGEVEVTLKPY 65
GH38N_AMII_GMII_SfManIII_like cd10809
N-terminal catalytic domain of Golgi alpha-mannosidase II, Spodoptera frugiperda Sf9 ...
258-430 1.31e-07

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: 54.96  E-value: 1.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  258 HCHIDTAWLWPFKETVRKCARSWV-TALQLMERNPEFIFACSQAQQLE-WVKSRYPGLYSRIQEFACRGQFVPVGGTWVE 335
Cdd:cd10809     9 HSHNDPGWIKTFEEYYQDQTKHILdNMVDKLSKNPKMKFIWAEISFLErWWDDASPDKKEAVKKLVKNGQLEIVTGGWVM 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  336 MDGNLPSGEAMVRQFLQGQNFFLQEFGKMCSEFWLPDTFGYSAQLPQIMHGCGIRRFLTQKLSWNLVNSFPHHT---FFW 412
Cdd:cd10809    89 TDEANSHYFAMIDQLIEGHQWLKENLGVKPKSGWSIDPFGHSPTMPYLLKRAGFKNMVIQRIHYEVKKYLAQRKaleFMW 168
                         170       180
                  ....*....|....*....|..
gi 374532775  413 EGLDGSR----VLVHFPPGDSY 430
Cdd:cd10809   169 RQYWDATgstdILTHMMPFYSY 190
GH38N_AMII_euk cd00451
N-terminal catalytic domain of eukaryotic class II alpha-mannosidases; glycoside hydrolase ...
252-454 2.43e-06

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: 50.30  E-value: 2.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  252 TIHATGHCHIDTAWLWPFKETVRKCARSWV-TALQLMERNPE--FIFAcsQAQQLE-WVKSRYPGLYSRIQEFACRGQFV 327
Cdd:cd00451     2 NVHLIPHSHCDVGWLKTFDEYYNGDVKSILdSVVKALNNDPErkFIWA--EIGFLErWWEDQGNDTKQQFKKLVKNGQLE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  328 PVGGTWVEMDGNLPSGEAMVRQFLQGQNFFLQEFGKMCSEFWLPDTFGYSAQLPQIMHGCGIRRFLTQKLSWNLVNSF-- 405
Cdd:cd00451    80 FVGGGWVMNDEACTTYESIIDQMTEGHQFLKDTFGVRPRVGWQIDPFGHSSTTPTLFSKMGFKGLVINRIPYSLKAEMkd 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 374532775  406 -PHHTFFWEG----LDGSRVLVH------------FPPGDS---YGMQGSVEEVLKTVANNRDKGRANH 454
Cdd:cd00451   160 nKQLEFVWRGspslGPDSEIFTHvlddhysypeslDFGGPPitdYNIAERADEFVEYIKKRSKTYRTNH 228
GH38N_Man2A1 cd11666
N-terminal catalytic domain of Golgi alpha-mannosidase II and similar proteins; glycoside ...
258-430 4.30e-05

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: 46.88  E-value: 4.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  258 HCHIDTAWLWPFKETVRKCARSWVT--ALQLMERNP-EFIFAcsqaqQLEWVKSRYPGLYSRIQEFACR----GQFVPVG 330
Cdd:cd11666     9 HSHNDPGWLKTFDDYFRDQTQHILNnmVLKLKEDSRrKFIWS-----EISYFAKWWDIIDGQKKDAVKRlienGQLEIVT 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  331 GTWVEMDGNLPSGEAMVRQFLQGQNFFLQEFGKMCSEFWLPDTFGYSAQLPQIMHGCGIRRFLTQKLSWNLVNSFPHHT- 409
Cdd:cd11666    84 GGWVMPDEATAHYFALIDQLIEGHQWLERNLGVKPKSGWAVDPFGHSPTMAYLLKRAGLSNMLIQRVHYSVKKHFSLQKt 163
                         170       180
                  ....*....|....*....|....*..
gi 374532775  410 --FFWE---GLDGSR-VLVHFPPGDSY 430
Cdd:cd11666   164 leFFWRqnwDLGSSTdILCHMMPFYSY 190
GH38N_AMII_like_1 cd10791
N-terminal catalytic domain of mainly uncharacterized eukaryotic proteins similar to ...
252-432 1.17e-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: 45.00  E-value: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  252 TIHATGHCHIDTAWLWPFKETVRKCARSWVTALQLMER------NPEFIFACSQAQQLE-WVKSRYPGLYSRIQEFACRG 324
Cdd:cd10791     1 TVHVVHHSHTDIGYTDLQEKVDRYHVDYIPQALDLAEAtknypeDARFRWTTESTWLVEeYLKCASPEQRERLEQAVRRG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  325 QFVpVGGTWVEMDGNLPSgEAMVRQFLQGQNFFLQEFGKMCSEFWLPDTFGYSAQLPQIMHGCGIRRFLTQklswnlVNs 404
Cdd:cd10791    81 RIG-WHALPLNITTELMD-EELLRRGLYLSKELDRRFGLPIIVAMQTDVPGHTWGLVDVLADAGIKYLSIG------VN- 151
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 374532775  405 fPHHT---------FFWEGLDGSRVLVHFPpgDSYGM 432
Cdd:cd10791   152 -GHSGpypprvpgpFYWESPDGRKVLVWYG--GHYGG 185
GH38N_Man2A2 cd11667
N-terminal catalytic domain of Golgi alpha-mannosidase IIx, and similar proteins; glycoside ...
258-430 1.72e-04

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: 44.98  E-value: 1.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  258 HCHIDTAWLWPFK----ETVRKCARSWVTALQlmeRNPEFIFACSQAQQL-EWVKSRYPGLYSRIQEFACRGQFVPVGGT 332
Cdd:cd11667     9 HSHNDPGWIKTFDkyyyDQTQHILNSMVVKLQ---EDPRRRFIWSEISFFsKWWDNINAQKRAAVRRLVGNGQLEMATGG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  333 WVEMDGNLPSGEAMVRQFLQGQNFFLQEFGKMCSEFWLPDTFGYSAQLPQIMHGCGIRRFLTQKLSWNLVNSFP--HHTF 410
Cdd:cd11667    86 WVMPDEANSHYFAMIDQLIEGHQWLEKNIGVTPRSGWAVDPFGHSSTMPYILRRSNLTSMLIQRVHYAIKKHFAatQSLE 165
                         170       180
                  ....*....|....*....|....*
gi 374532775  411 F-----WEGLDGSRVLVHFPPGDSY 430
Cdd:cd11667   166 FmwrqtWDPDSSTDIFCHMMPFYSY 190
GH57N_TLGT_like cd10793
N-terminal catalytic domain of 4-alpha-glucanotransferase; glycoside hydrolase family 57 (GH57) ...
267-371 2.97e-04

N-terminal catalytic domain of 4-alpha-glucanotransferase; glycoside hydrolase family 57 (GH57); 4-alpha-glucanotransferase (TLGT, EC 2.4.1.25) plays a key role in the maltose metabolism. It catalyzes the disproportionation of amylose and the formation of large cyclic alpha-1,4-glucan (cycloamylose) from linear amylose. TLGT functions as a homodimer. Each monomer is composed of two domains, an N-terminal catalytic domain with a (beta/alpha)7 barrel fold and a C-terminal domain with a twisted beta-sandwich fold. Some family members have been designated as alpha-amylases, such as the heat-stable eubacterial amylase from Dictyoglomus thermophilum (DtAmyA) and the extremely thermostable archaeal amylase from Pyrococcus furiosus(PfAmyA). However, both of these proteins are 4-alpha-glucanotransferases. DtAmyA was shown to have transglycosylating activity and PfAmyA exhibits 4-alpha-glucanotransferase activity.


Pssm-ID: 212105 [Multi-domain]  Cd Length: 279  Bit Score: 44.11  E-value: 2.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  267 WPFKETVRKCARSWvtaLQLMERNPEFIFA--CSqAQQLEWVKSRYPGLYSRIQEFACRGQFVPVGGTWVE----MdgnL 340
Cdd:cd10793    17 EVFEEAYEKSYKPF---LEVLKKYPDFKFSlhFS-GWLLEWLEENHPEYLDLLRKLVDRGQIEILGGGFYEpilaS---I 89
                          90       100       110
                  ....*....|....*....|....*....|.
gi 374532775  341 PSgEAMVRQFLQGQNFFLQEFGKMCSEFWLP 371
Cdd:cd10793    90 PS-EDRVGQIKKLNRFIEKNFGQRPKGLWLT 119
GH38N_AMII_Epman_like cd10811
N-terminal catalytic domain of mammalian core-specific lysosomal alpha 1,6-mannosidase and ...
258-401 7.85e-03

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: 39.87  E-value: 7.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374532775  258 HCHIDTAWLWPFKETVRK-CARSWVTALQLMERNPE--FIFACSQAQQLEWVKSRYPGLYSRIQEFACRGQFVPVGGTWV 334
Cdd:cd10811     8 HSHMDVGWVYTVQESMHAyAANVYTSVVEELMRGKQrrFIAVEQEFFRLWWDGVATDKQKQQVRQLLSEGRLEFVIGGQV 87
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 374532775  335 EMDGNLPSGEAMVRQFLQGQNFFLQEFGKMCSEFWLPDTFGYSAQLPQIMHGCGIRRFLTQKLSWNL 401
Cdd:cd10811    88 MHDEAVTELDDQILQLTEGHGFLYETFGVRPRFSWHVDPFGASATTPTLFALAGFNAHLISRIDYDL 154
 
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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