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Conserved domains on  [gi|442615769|ref|NP_001259402|]
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alpha-Mannosidase class I a, isoform P [Drosophila melanogaster]

Protein Classification

glycoside hydrolase family protein( domain architecture ID 721)

glycoside hydrolase (GH) family protein may catalyze the hydrolysis of glycosidic bonds in complex sugars; may be a member of glycosyl hydrolase families GH47, GH76, GH88, or GH127

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
LanC_like super family cl04955
Cyclases involved in the biosynthesis of lantibiotics, and similar proteins; LanC is the ...
175-623 0e+00

Cyclases involved in the biosynthesis of lantibiotics, and similar proteins; LanC is the cyclase enzyme of the lanthionine synthetase. Lanthionine is a lantibiotic, a unique class of peptide antibiotics. They are ribosomally synthesized as a precursor peptide and then post-translationally modified to contain thioether cross-links called lanthionines (Lans) or methyllanthionines (MeLans), in addition to 2,3-didehydroalanine (Dha) and (Z)-2,3-didehydrobutyrine (Dhb). These unusual amino acids are introduced by the dehydration of serine and threonine residues, followed by thioether formation via addition of cysteine thiols, catalysed by LanB and LanC or LanM. LanC, the cyclase component, is a zinc metalloprotein, whose bound metal has been proposed to activate the thiol substrate for nucleophilic addition. A related domain is also present in LanM and other pro- and eukaryotic proteins with poorly characterized functions.


The actual alignment was detected with superfamily member PTZ00470:

Pssm-ID: 471159  Cd Length: 522  Bit Score: 637.92  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615769 175 EKRNQVVKMMEHAWHNYKLYAWGKNELRPLSQRPHSasifgSYDLGATIVDGLDTLYIMGLEKEYREGRDWIERKFSLD- 253
Cdd:PTZ00470  71 KRRESVREAMKHAWEGYKEYAWGHDELRPLTKRHHE-----WFGLGLTIIDSLDTLKIMGLKKEYKEGRDWVANNLKQSk 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615769 254 NISAELSVFETNIRFVGGMLTLYAFTGDPLYKEKAQHVADKLLPAFQTPTGIPYALVNTKTGVAKNYGWAsGGSSILSEF 333
Cdd:PTZ00470 146 DTGLGVSVFETTIRVLGGLLSAYDLTGDEMYLEKAREIADRLLPAFNEDTGFPASEINLATGRKSYPGWA-GGCSILSEV 224
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615769 334 GTLHLEFAYLSDITGNPLYRERVQTIRQVLKEIEKP-KGLYPNFLNPKTGKWGQLHMSLGALGDSYYEYLLKAWLQSGQT 412
Cdd:PTZ00470 225 GTLQLEFNYLSEITGDPKYAEYVDKVMDALFSMKPAiNGLYPIFLNPDAGRFCGNHISLGALGDSYYEYLLKQWLYTNGR 304
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615769 413 DEEAREMFDEAMLAILDKMVRTSPGGLTYVSDLKFDRLEHKMDHLACFSGGLFALGAATRQN---DYTDKYMEVGKGITN 489
Cdd:PTZ00470 305 EERYRRLFVESAKGIIEHLYKRSPKGLTYIAEMDGGSLTNKMEHLACFAGGMFALGAAINITpddEKSARYMEVGEEVTK 384
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615769 490 TCHESYIRAPTQLGPEAFRFSEAVEARALRSQEKYYILRPETFESYFVLWRLTHDQKYRDWGWEAVLALEKHCRTAHGYC 569
Cdd:PTZ00470 385 TCYETYATSPTGLGPEIFHFDPNSGDISPNVHDSHYILRPETVESIFILYRLTGDPKYREWAWKIFQAIEKHCKTENGYS 464
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 442615769 570 GLRNVYQQEPQKDDVQQSFFLAETLKYLYLLFSDDSVLPLDEWVFNTEAHPLPI 623
Cdd:PTZ00470 465 GLKNVLTVHPQQDDFQESFFLAETLKYLYLLFQPDHVIPLDKYVFNTEAHPIPI 518
 
Name Accession Description Interval E-value
PTZ00470 PTZ00470
glycoside hydrolase family 47 protein; Provisional
175-623 0e+00

glycoside hydrolase family 47 protein; Provisional


Pssm-ID: 240427  Cd Length: 522  Bit Score: 637.92  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615769 175 EKRNQVVKMMEHAWHNYKLYAWGKNELRPLSQRPHSasifgSYDLGATIVDGLDTLYIMGLEKEYREGRDWIERKFSLD- 253
Cdd:PTZ00470  71 KRRESVREAMKHAWEGYKEYAWGHDELRPLTKRHHE-----WFGLGLTIIDSLDTLKIMGLKKEYKEGRDWVANNLKQSk 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615769 254 NISAELSVFETNIRFVGGMLTLYAFTGDPLYKEKAQHVADKLLPAFQTPTGIPYALVNTKTGVAKNYGWAsGGSSILSEF 333
Cdd:PTZ00470 146 DTGLGVSVFETTIRVLGGLLSAYDLTGDEMYLEKAREIADRLLPAFNEDTGFPASEINLATGRKSYPGWA-GGCSILSEV 224
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615769 334 GTLHLEFAYLSDITGNPLYRERVQTIRQVLKEIEKP-KGLYPNFLNPKTGKWGQLHMSLGALGDSYYEYLLKAWLQSGQT 412
Cdd:PTZ00470 225 GTLQLEFNYLSEITGDPKYAEYVDKVMDALFSMKPAiNGLYPIFLNPDAGRFCGNHISLGALGDSYYEYLLKQWLYTNGR 304
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615769 413 DEEAREMFDEAMLAILDKMVRTSPGGLTYVSDLKFDRLEHKMDHLACFSGGLFALGAATRQN---DYTDKYMEVGKGITN 489
Cdd:PTZ00470 305 EERYRRLFVESAKGIIEHLYKRSPKGLTYIAEMDGGSLTNKMEHLACFAGGMFALGAAINITpddEKSARYMEVGEEVTK 384
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615769 490 TCHESYIRAPTQLGPEAFRFSEAVEARALRSQEKYYILRPETFESYFVLWRLTHDQKYRDWGWEAVLALEKHCRTAHGYC 569
Cdd:PTZ00470 385 TCYETYATSPTGLGPEIFHFDPNSGDISPNVHDSHYILRPETVESIFILYRLTGDPKYREWAWKIFQAIEKHCKTENGYS 464
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 442615769 570 GLRNVYQQEPQKDDVQQSFFLAETLKYLYLLFSDDSVLPLDEWVFNTEAHPLPI 623
Cdd:PTZ00470 465 GLKNVLTVHPQQDDFQESFFLAETLKYLYLLFQPDHVIPLDKYVFNTEAHPIPI 518
Glyco_hydro_47 pfam01532
Glycosyl hydrolase family 47; Members of this family are alpha-mannosidases that catalyze the ...
183-623 0e+00

Glycosyl hydrolase family 47; Members of this family are alpha-mannosidases that catalyze the hydrolysis of the terminal 1,2-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man(9)(GlcNAc)(2).


Pssm-ID: 460241  Cd Length: 453  Bit Score: 631.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615769  183 MMEHAWHNYKLYAWGKNELRPLSQRPHSAsiFGsyDLGATIVDGLDTLYIMGLEKEYREGRDWIERKFSLDNISAELSVF 262
Cdd:pfam01532   1 AFLHAWDGYKKYAWGHDELRPISGGGNDT--FG--GWGATIVDSLDTLIIMGLTDEFEEAVDWVEKTLDFDKDSTEVSVF 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615769  263 ETNIRFVGGMLTLYAFT--GDPLYKEKAQHVADKLLPAFQTPTGIPYALVNTKTGVAKNYGWAsGGSSILSEFGTLHLEF 340
Cdd:pfam01532  77 ETTIRYLGGLLSAYDLSgdGDDVLLEKAVDLADRLLPAFDTPTGIPYPRVNLKTGKGGNGHVA-GGASSLAEAGTLQLEF 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615769  341 AYLSDITGNPLYRERVQTIRQVLKEIE---KPKGLYPNFLNPKTGKWGQLHMSLGALGDSYYEYLLKAWLQSGQTDEEAR 417
Cdd:pfam01532 156 TRLSQLTGDPKYEDLAQKIMDVLWKNQsrtPLPGLVPIYIDPDTGKFVGSNIGLGARGDSYYEYLLKQYLLTGGTDPEYR 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615769  418 EMFDEAMLAILDKMV--RTSPGGLTYVSDLKFD---RLEHKMDHLACFSGGLFALGAATRQNDytDKYMEVGKGITNTCH 492
Cdd:pfam01532 236 DMYEEAMDAIKKHLLfrPSTPSDLLFIGELDSGgggKLSPKMDHLSCFAGGMLALGATLGLPR--EGDLELAEKLTEGCY 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615769  493 ESYIRAPTQLGPEAFRFS---------EAVEARALRSQEKYYILRPETFESYFVLWRLTHDQKYRDWGWEAVLALEKHCR 563
Cdd:pfam01532 314 KTYDSTPTGLGPEIFYFDpcdedcpwdEDKWDFYVKIEDPHYLLRPETIESLFYLYRATGDPKYREWGWEIFQAIEKYTR 393
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615769  564 TAHGYCGLRNVYQQEPQKDDVQQSFFLAETLKYLYLLFSDDSVLPLDEWVFNTEAHPLPI 623
Cdd:pfam01532 394 TECGYSGLQDVTSPPGEKEDNMESFWLAETLKYLYLLFSDDDLLSLDEWVFNTEAHPLPV 453
LanC_SerThrkinase cd04791
Lanthionine synthetase C-like domain associated with serine/threonine kinases; Some members of ...
229-365 7.94e-04

Lanthionine synthetase C-like domain associated with serine/threonine kinases; Some members of this subgroup lack the zinc binding site and the active site residues, and therefore are most likely inactive. The function of this domain is unknown.


Pssm-ID: 271199 [Multi-domain]  Cd Length: 327  Bit Score: 41.87  E-value: 7.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615769 229 TLYIMGLEKEyreGRDWIERKFSLDNISAELSVFetnirfvGGM-------LTLYAFTGDPLYKEKAQHVADKLLPAFQT 301
Cdd:cd04791   55 VLYELGRREE---AERLLDRALALPLDSLDPSLY-------SGLagiglalLHLARATGDPEFLERAARIAERLAARLRE 124
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442615769 302 PTGIPYAlvntKTGVAKNYGWASGGSSIlSEFgtlhleFAYLSDITGNPLYRER-VQTIRQVLKE 365
Cdd:cd04791  125 DDPGVYW----NDAGAVRAGLLHGWSGI-ALF------LLRLYEATGDPAYLDLaERALRKDLAR 178
 
Name Accession Description Interval E-value
PTZ00470 PTZ00470
glycoside hydrolase family 47 protein; Provisional
175-623 0e+00

glycoside hydrolase family 47 protein; Provisional


Pssm-ID: 240427  Cd Length: 522  Bit Score: 637.92  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615769 175 EKRNQVVKMMEHAWHNYKLYAWGKNELRPLSQRPHSasifgSYDLGATIVDGLDTLYIMGLEKEYREGRDWIERKFSLD- 253
Cdd:PTZ00470  71 KRRESVREAMKHAWEGYKEYAWGHDELRPLTKRHHE-----WFGLGLTIIDSLDTLKIMGLKKEYKEGRDWVANNLKQSk 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615769 254 NISAELSVFETNIRFVGGMLTLYAFTGDPLYKEKAQHVADKLLPAFQTPTGIPYALVNTKTGVAKNYGWAsGGSSILSEF 333
Cdd:PTZ00470 146 DTGLGVSVFETTIRVLGGLLSAYDLTGDEMYLEKAREIADRLLPAFNEDTGFPASEINLATGRKSYPGWA-GGCSILSEV 224
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615769 334 GTLHLEFAYLSDITGNPLYRERVQTIRQVLKEIEKP-KGLYPNFLNPKTGKWGQLHMSLGALGDSYYEYLLKAWLQSGQT 412
Cdd:PTZ00470 225 GTLQLEFNYLSEITGDPKYAEYVDKVMDALFSMKPAiNGLYPIFLNPDAGRFCGNHISLGALGDSYYEYLLKQWLYTNGR 304
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615769 413 DEEAREMFDEAMLAILDKMVRTSPGGLTYVSDLKFDRLEHKMDHLACFSGGLFALGAATRQN---DYTDKYMEVGKGITN 489
Cdd:PTZ00470 305 EERYRRLFVESAKGIIEHLYKRSPKGLTYIAEMDGGSLTNKMEHLACFAGGMFALGAAINITpddEKSARYMEVGEEVTK 384
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615769 490 TCHESYIRAPTQLGPEAFRFSEAVEARALRSQEKYYILRPETFESYFVLWRLTHDQKYRDWGWEAVLALEKHCRTAHGYC 569
Cdd:PTZ00470 385 TCYETYATSPTGLGPEIFHFDPNSGDISPNVHDSHYILRPETVESIFILYRLTGDPKYREWAWKIFQAIEKHCKTENGYS 464
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 442615769 570 GLRNVYQQEPQKDDVQQSFFLAETLKYLYLLFSDDSVLPLDEWVFNTEAHPLPI 623
Cdd:PTZ00470 465 GLKNVLTVHPQQDDFQESFFLAETLKYLYLLFQPDHVIPLDKYVFNTEAHPIPI 518
Glyco_hydro_47 pfam01532
Glycosyl hydrolase family 47; Members of this family are alpha-mannosidases that catalyze the ...
183-623 0e+00

Glycosyl hydrolase family 47; Members of this family are alpha-mannosidases that catalyze the hydrolysis of the terminal 1,2-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man(9)(GlcNAc)(2).


Pssm-ID: 460241  Cd Length: 453  Bit Score: 631.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615769  183 MMEHAWHNYKLYAWGKNELRPLSQRPHSAsiFGsyDLGATIVDGLDTLYIMGLEKEYREGRDWIERKFSLDNISAELSVF 262
Cdd:pfam01532   1 AFLHAWDGYKKYAWGHDELRPISGGGNDT--FG--GWGATIVDSLDTLIIMGLTDEFEEAVDWVEKTLDFDKDSTEVSVF 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615769  263 ETNIRFVGGMLTLYAFT--GDPLYKEKAQHVADKLLPAFQTPTGIPYALVNTKTGVAKNYGWAsGGSSILSEFGTLHLEF 340
Cdd:pfam01532  77 ETTIRYLGGLLSAYDLSgdGDDVLLEKAVDLADRLLPAFDTPTGIPYPRVNLKTGKGGNGHVA-GGASSLAEAGTLQLEF 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615769  341 AYLSDITGNPLYRERVQTIRQVLKEIE---KPKGLYPNFLNPKTGKWGQLHMSLGALGDSYYEYLLKAWLQSGQTDEEAR 417
Cdd:pfam01532 156 TRLSQLTGDPKYEDLAQKIMDVLWKNQsrtPLPGLVPIYIDPDTGKFVGSNIGLGARGDSYYEYLLKQYLLTGGTDPEYR 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615769  418 EMFDEAMLAILDKMV--RTSPGGLTYVSDLKFD---RLEHKMDHLACFSGGLFALGAATRQNDytDKYMEVGKGITNTCH 492
Cdd:pfam01532 236 DMYEEAMDAIKKHLLfrPSTPSDLLFIGELDSGgggKLSPKMDHLSCFAGGMLALGATLGLPR--EGDLELAEKLTEGCY 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615769  493 ESYIRAPTQLGPEAFRFS---------EAVEARALRSQEKYYILRPETFESYFVLWRLTHDQKYRDWGWEAVLALEKHCR 563
Cdd:pfam01532 314 KTYDSTPTGLGPEIFYFDpcdedcpwdEDKWDFYVKIEDPHYLLRPETIESLFYLYRATGDPKYREWGWEIFQAIEKYTR 393
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615769  564 TAHGYCGLRNVYQQEPQKDDVQQSFFLAETLKYLYLLFSDDSVLPLDEWVFNTEAHPLPI 623
Cdd:pfam01532 394 TECGYSGLQDVTSPPGEKEDNMESFWLAETLKYLYLLFSDDDLLSLDEWVFNTEAHPLPV 453
LanC_SerThrkinase cd04791
Lanthionine synthetase C-like domain associated with serine/threonine kinases; Some members of ...
229-365 7.94e-04

Lanthionine synthetase C-like domain associated with serine/threonine kinases; Some members of this subgroup lack the zinc binding site and the active site residues, and therefore are most likely inactive. The function of this domain is unknown.


Pssm-ID: 271199 [Multi-domain]  Cd Length: 327  Bit Score: 41.87  E-value: 7.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615769 229 TLYIMGLEKEyreGRDWIERKFSLDNISAELSVFetnirfvGGM-------LTLYAFTGDPLYKEKAQHVADKLLPAFQT 301
Cdd:cd04791   55 VLYELGRREE---AERLLDRALALPLDSLDPSLY-------SGLagiglalLHLARATGDPEFLERAARIAERLAARLRE 124
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442615769 302 PTGIPYAlvntKTGVAKNYGWASGGSSIlSEFgtlhleFAYLSDITGNPLYRER-VQTIRQVLKE 365
Cdd:cd04791  125 DDPGVYW----NDAGAVRAGLLHGWSGI-ALF------LLRLYEATGDPAYLDLaERALRKDLAR 178
 
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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