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Conserved domains on  [gi|119568570|gb|EAW48185|]
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mannosidase, alpha, class 1A, member 1, isoform CRA_a [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 ...
 225-353 2.45e-62

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: 206.25  E-value: 2.45e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568570  225 MMKHAWNNYKGYAWGLNELKPISKGGHSSslFGNIkGATIVDALDTLFIMEMKHEFEEAKSWVEENLDFNVNA-EISVFE 303
Cdd:pfam01532   1 AFLHAWDGYKKYAWGHDELRPISGGGNDT--FGGW-GATIVDSLDTLIIMGLTDEFEEAVDWVEKTLDFDKDStEVSVFE 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 119568570  304 VNIRFVGGLLSAYYLS--GEEIFRKKAVELGVKLLPAFHTPSGIPWALLNMK 353
Cdd:pfam01532  78 TTIRYLGGLLSAYDLSgdGDDVLLEKAVDLADRLLPAFDTPTGIPYPRVNLK 129
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 114-205 2.03e-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: 40.44  E-value: 2.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568570   114 EAALED------NLARIRENHERALREAKETLQKLPEEIQR-----DILLEKKKVAQDQLR--DKAPFRGLPPVDFVPPI 180
Cdd:TIGR02169  874 EAALRDlesrlgDLKKERDELEAQLRELERKIEELEAQIEKkrkrlSELKAKLEALEEELSeiEDPKGEDEEIPEEELSL 953

                           90       100
                   ....*....|....*....|....*
gi 119568570   181 GVesrepadaaIREKRAKIKEEIEA 205
Cdd:TIGR02169  954 ED---------VQAELQRVEEEIRA 969
 
Name Accession Description Interval E-value
Glyco_hydro_47 pfam01532
Glycosyl hydrolase family 47; Members of this family are alpha-mannosidases that catalyze the ...
 225-353 2.45e-62

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: 206.25  E-value: 2.45e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568570  225 MMKHAWNNYKGYAWGLNELKPISKGGHSSslFGNIkGATIVDALDTLFIMEMKHEFEEAKSWVEENLDFNVNA-EISVFE 303
Cdd:pfam01532   1 AFLHAWDGYKKYAWGHDELRPISGGGNDT--FGGW-GATIVDSLDTLIIMGLTDEFEEAVDWVEKTLDFDKDStEVSVFE 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 119568570  304 VNIRFVGGLLSAYYLS--GEEIFRKKAVELGVKLLPAFHTPSGIPWALLNMK 353
Cdd:pfam01532  78 TTIRYLGGLLSAYDLSgdGDDVLLEKAVDLADRLLPAFDTPTGIPYPRVNLK 129
PTZ00470 PTZ00470
glycoside hydrolase family 47 protein; Provisional
 225-359 2.17e-49

glycoside hydrolase family 47 protein; Provisional


Pssm-ID: 240427  Cd Length: 522  Bit Score: 173.37  E-value: 2.17e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568570 225 MMKHAWNNYKGYAWGLNELKPISKGGHSSslFGniKGATIVDALDTLFIMEMKHEFEEAKSWVEENL--DFNVNAEISVF 302
Cdd:PTZ00470  79 AMKHAWEGYKEYAWGHDELRPLTKRHHEW--FG--LGLTIIDSLDTLKIMGLKKEYKEGRDWVANNLkqSKDTGLGVSVF 154

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119568570 303 EVNIRFVGGLLSAYYLSGEEIFRKKAVELGVKLLPAFHTPSGIPWALLNMK-------RWM--CNI 359
Cdd:PTZ00470 155 ETTIRVLGGLLSAYDLTGDEMYLEKAREIADRLLPAFNEDTGFPASEINLAtgrksypGWAggCSI 220
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 114-205 2.03e-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: 40.44  E-value: 2.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568570   114 EAALED------NLARIRENHERALREAKETLQKLPEEIQR-----DILLEKKKVAQDQLR--DKAPFRGLPPVDFVPPI 180
Cdd:TIGR02169  874 EAALRDlesrlgDLKKERDELEAQLRELERKIEELEAQIEKkrkrlSELKAKLEALEEELSeiEDPKGEDEEIPEEELSL 953

                           90       100
                   ....*....|....*....|....*
gi 119568570   181 GVesrepadaaIREKRAKIKEEIEA 205
Cdd:TIGR02169  954 ED---------VQAELQRVEEEIRA 969
 
Name Accession Description Interval E-value
Glyco_hydro_47 pfam01532
Glycosyl hydrolase family 47; Members of this family are alpha-mannosidases that catalyze the ...
 225-353 2.45e-62

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: 206.25  E-value: 2.45e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568570  225 MMKHAWNNYKGYAWGLNELKPISKGGHSSslFGNIkGATIVDALDTLFIMEMKHEFEEAKSWVEENLDFNVNA-EISVFE 303
Cdd:pfam01532   1 AFLHAWDGYKKYAWGHDELRPISGGGNDT--FGGW-GATIVDSLDTLIIMGLTDEFEEAVDWVEKTLDFDKDStEVSVFE 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 119568570  304 VNIRFVGGLLSAYYLS--GEEIFRKKAVELGVKLLPAFHTPSGIPWALLNMK 353
Cdd:pfam01532  78 TTIRYLGGLLSAYDLSgdGDDVLLEKAVDLADRLLPAFDTPTGIPYPRVNLK 129
PTZ00470 PTZ00470
glycoside hydrolase family 47 protein; Provisional
 225-359 2.17e-49

glycoside hydrolase family 47 protein; Provisional


Pssm-ID: 240427  Cd Length: 522  Bit Score: 173.37  E-value: 2.17e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568570 225 MMKHAWNNYKGYAWGLNELKPISKGGHSSslFGniKGATIVDALDTLFIMEMKHEFEEAKSWVEENL--DFNVNAEISVF 302
Cdd:PTZ00470  79 AMKHAWEGYKEYAWGHDELRPLTKRHHEW--FG--LGLTIIDSLDTLKIMGLKKEYKEGRDWVANNLkqSKDTGLGVSVF 154

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119568570 303 EVNIRFVGGLLSAYYLSGEEIFRKKAVELGVKLLPAFHTPSGIPWALLNMK-------RWM--CNI 359
Cdd:PTZ00470 155 ETTIRVLGGLLSAYDLTGDEMYLEKAREIADRLLPAFNEDTGFPASEINLAtgrksypGWAggCSI 220
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 114-205 2.03e-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: 40.44  E-value: 2.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568570   114 EAALED------NLARIRENHERALREAKETLQKLPEEIQR-----DILLEKKKVAQDQLR--DKAPFRGLPPVDFVPPI 180
Cdd:TIGR02169  874 EAALRDlesrlgDLKKERDELEAQLRELERKIEELEAQIEKkrkrlSELKAKLEALEEELSeiEDPKGEDEEIPEEELSL 953

                           90       100
                   ....*....|....*....|....*
gi 119568570   181 GVesrepadaaIREKRAKIKEEIEA 205
Cdd:TIGR02169  954 ED---------VQAELQRVEEEIRA 969
 
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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