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Conserved domains on  [gi|2217361467|ref|XP_047274731|]
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mannosyl-oligosaccharide 1,2-alpha-mannosidase IA isoform X3 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Glyco_hydro_47 super family cl47677
Glycosyl hydrolase family 47; Members of this family are alpha-mannosidases that catalyze the ...
 285-381 4.33e-45

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).


The actual alignment was detected with superfamily member pfam01532:

Pssm-ID: 460241  Cd Length: 453  Bit Score: 161.96  E-value: 4.33e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361467 285 MMKHAWNNYKGYAWGLNELKPISKGGHSSslFGNIkGATIVDALDTLFIMEMKHEFEEAKSWVEENLDFNVNA-EISVFE 363
Cdd:pfam01532   1 AFLHAWDGYKKYAWGHDELRPISGGGNDT--FGGW-GATIVDSLDTLIIMGLTDEFEEAVDWVEKTLDFDKDStEVSVFE 77

                          90
                  ....*....|....*...
gi 2217361467 364 VNIRFVGGLLSAYYLSGE 381
Cdd:pfam01532  78 TTIRYLGGLLSAYDLSGD 95
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 197-276 6.75e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 38.90  E-value: 6.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361467  197 EAALED------NLARIRENHERALREAKETLQKLPEEIQR-----DILLEKKKVAQDQLR--DKAPFRGLPPVDFVPPI 263
Cdd:TIGR02169  874 EAALRDlesrlgDLKKERDELEAQLRELERKIEELEAQIEKkrkrlSELKAKLEALEEELSeiEDPKGEDEEIPEEELSL 953

                           90
                   ....*....|....*
gi 2217361467  264 G--VESREPADAAIR 276
Cdd:TIGR02169  954 EdvQAELQRVEEEIR 968
 
Name Accession Description Interval E-value
Glyco_hydro_47 pfam01532
Glycosyl hydrolase family 47; Members of this family are alpha-mannosidases that catalyze the ...
 285-381 4.33e-45

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: 161.96  E-value: 4.33e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361467 285 MMKHAWNNYKGYAWGLNELKPISKGGHSSslFGNIkGATIVDALDTLFIMEMKHEFEEAKSWVEENLDFNVNA-EISVFE 363
Cdd:pfam01532   1 AFLHAWDGYKKYAWGHDELRPISGGGNDT--FGGW-GATIVDSLDTLIIMGLTDEFEEAVDWVEKTLDFDKDStEVSVFE 77

                          90
                  ....*....|....*...
gi 2217361467 364 VNIRFVGGLLSAYYLSGE 381
Cdd:pfam01532  78 TTIRYLGGLLSAYDLSGD 95
PTZ00470 PTZ00470
glycoside hydrolase family 47 protein; Provisional
 261-384 9.21e-39

glycoside hydrolase family 47 protein; Provisional


Pssm-ID: 240427  Cd Length: 522  Bit Score: 146.02  E-value: 9.21e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361467 261 PPIGVESREPADAAIREKRAK-IKEMMKHAWNNYKGYAWGLNELKPISKGGHSSslFGniKGATIVDALDTLFIMEMKHE 339
Cdd:PTZ00470   54 PFNKIDEVYYQNEKLNIKRREsVREAMKHAWEGYKEYAWGHDELRPLTKRHHEW--FG--LGLTIIDSLDTLKIMGLKKE 129

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2217361467 340 FEEAKSWVEENL--DFNVNAEISVFEVNIRFVGGLLSAYYLSGEEWY 384
Cdd:PTZ00470  130 YKEGRDWVANNLkqSKDTGLGVSVFETTIRVLGGLLSAYDLTGDEMY 176
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 197-276 6.75e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 38.90  E-value: 6.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361467  197 EAALED------NLARIRENHERALREAKETLQKLPEEIQR-----DILLEKKKVAQDQLR--DKAPFRGLPPVDFVPPI 263
Cdd:TIGR02169  874 EAALRDlesrlgDLKKERDELEAQLRELERKIEELEAQIEKkrkrlSELKAKLEALEEELSeiEDPKGEDEEIPEEELSL 953

                           90
                   ....*....|....*
gi 2217361467  264 G--VESREPADAAIR 276
Cdd:TIGR02169  954 EdvQAELQRVEEEIR 968
 
Name Accession Description Interval E-value
Glyco_hydro_47 pfam01532
Glycosyl hydrolase family 47; Members of this family are alpha-mannosidases that catalyze the ...
 285-381 4.33e-45

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: 161.96  E-value: 4.33e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361467 285 MMKHAWNNYKGYAWGLNELKPISKGGHSSslFGNIkGATIVDALDTLFIMEMKHEFEEAKSWVEENLDFNVNA-EISVFE 363
Cdd:pfam01532   1 AFLHAWDGYKKYAWGHDELRPISGGGNDT--FGGW-GATIVDSLDTLIIMGLTDEFEEAVDWVEKTLDFDKDStEVSVFE 77

                          90
                  ....*....|....*...
gi 2217361467 364 VNIRFVGGLLSAYYLSGE 381
Cdd:pfam01532  78 TTIRYLGGLLSAYDLSGD 95
PTZ00470 PTZ00470
glycoside hydrolase family 47 protein; Provisional
 261-384 9.21e-39

glycoside hydrolase family 47 protein; Provisional


Pssm-ID: 240427  Cd Length: 522  Bit Score: 146.02  E-value: 9.21e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361467 261 PPIGVESREPADAAIREKRAK-IKEMMKHAWNNYKGYAWGLNELKPISKGGHSSslFGniKGATIVDALDTLFIMEMKHE 339
Cdd:PTZ00470   54 PFNKIDEVYYQNEKLNIKRREsVREAMKHAWEGYKEYAWGHDELRPLTKRHHEW--FG--LGLTIIDSLDTLKIMGLKKE 129

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2217361467 340 FEEAKSWVEENL--DFNVNAEISVFEVNIRFVGGLLSAYYLSGEEWY 384
Cdd:PTZ00470  130 YKEGRDWVANNLkqSKDTGLGVSVFETTIRVLGGLLSAYDLTGDEMY 176
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 197-276 6.75e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 38.90  E-value: 6.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361467  197 EAALED------NLARIRENHERALREAKETLQKLPEEIQR-----DILLEKKKVAQDQLR--DKAPFRGLPPVDFVPPI 263
Cdd:TIGR02169  874 EAALRDlesrlgDLKKERDELEAQLRELERKIEELEAQIEKkrkrlSELKAKLEALEEELSeiEDPKGEDEEIPEEELSL 953

                           90
                   ....*....|....*
gi 2217361467  264 G--VESREPADAAIR 276
Cdd:TIGR02169  954 EdvQAELQRVEEEIR 968
 
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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