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Conserved domains on  [gi|2462502415|ref|XP_054189928|]
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mannosyl-oligosaccharide 1,2-alpha-mannosidase IB 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 ...
 187-319 6.61e-67

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: 216.65  E-value: 6.61e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502415 187 MMKHAWDNYRTYGWGHNELRPIARKGHSPniFGSsqMGATIVDALDTLYIMGLHDEFLDGQRWIEDNLDFSVNS-EVSVF 265
Cdd:pfam01532   1 AFLHAWDGYKKYAWGHDELRPISGGGNDT--FGG--WGATIVDSLDTLIIMGLTDEFEEAVDWVEKTLDFDKDStEVSVF 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462502415 266 EVNIRFIGGLLAAYYLS--GEEIFKIKAVQLAEKLLPAFNTPTGIPWAMVNLKRSY 319
Cdd:pfam01532  77 ETTIRYLGGLLSAYDLSgdGDDVLLEKAVDLADRLLPAFDTPTGIPYPRVNLKTGK 132
PTZ00121 super family cl31754
MAEBL; Provisional
 109-208 1.30e-03

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 1.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502415  109 NKIRAdhEKALEEAKEKLRKSrEEIRAEiQTEKNKVVQEMKIKENKPLPPVPIPNLVGIRGGDPEDNDIREKREKikeMM 188
Cdd:PTZ00121  1728 NKIKA--EEAKKEAEEDKKKA-EEAKKD-EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK---KI 1800

                           90       100
                   ....*....|....*....|
gi 2462502415  189 KHAWDNYRTYGWGHNELRPI 208
Cdd:PTZ00121  1801 KDIFDNFANIIEGGKEGNLV 1820
 
Name Accession Description Interval E-value
Glyco_hydro_47 pfam01532
Glycosyl hydrolase family 47; Members of this family are alpha-mannosidases that catalyze the ...
 187-319 6.61e-67

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: 216.65  E-value: 6.61e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502415 187 MMKHAWDNYRTYGWGHNELRPIARKGHSPniFGSsqMGATIVDALDTLYIMGLHDEFLDGQRWIEDNLDFSVNS-EVSVF 265
Cdd:pfam01532   1 AFLHAWDGYKKYAWGHDELRPISGGGNDT--FGG--WGATIVDSLDTLIIMGLTDEFEEAVDWVEKTLDFDKDStEVSVF 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462502415 266 EVNIRFIGGLLAAYYLS--GEEIFKIKAVQLAEKLLPAFNTPTGIPWAMVNLKRSY 319
Cdd:pfam01532  77 ETTIRYLGGLLSAYDLSgdGDDVLLEKAVDLADRLLPAFDTPTGIPYPRVNLKTGK 132
PTZ00470 PTZ00470
glycoside hydrolase family 47 protein; Provisional
 173-325 2.79e-57

glycoside hydrolase family 47 protein; Provisional


Pssm-ID: 240427  Cd Length: 522  Bit Score: 193.40  E-value: 2.79e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502415 173 EDNDIrEKREKIKEMMKHAWDNYRTYGWGHNELRPIARKGHspNIFGssqMGATIVDALDTLYIMGLHDEFLDGQRWIED 252
Cdd:PTZ00470   66 EKLNI-KRRESVREAMKHAWEGYKEYAWGHDELRPLTKRHH--EWFG---LGLTIIDSLDTLKIMGLKKEYKEGRDWVAN 139

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462502415 253 NLDFS--VNSEVSVFEVNIRFIGGLLAAYYLSGEEIFKIKAVQLAEKLLPAFNTPTGIPWAMVNLK--RSYICRWPG 325
Cdd:PTZ00470  140 NLKQSkdTGLGVSVFETTIRVLGGLLSAYDLTGDEMYLEKAREIADRLLPAFNEDTGFPASEINLAtgRKSYPGWAG 216
PTZ00121 PTZ00121
MAEBL; Provisional
 109-208 1.30e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 1.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502415  109 NKIRAdhEKALEEAKEKLRKSrEEIRAEiQTEKNKVVQEMKIKENKPLPPVPIPNLVGIRGGDPEDNDIREKREKikeMM 188
Cdd:PTZ00121  1728 NKIKA--EEAKKEAEEDKKKA-EEAKKD-EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK---KI 1800

                           90       100
                   ....*....|....*....|
gi 2462502415  189 KHAWDNYRTYGWGHNELRPI 208
Cdd:PTZ00121  1801 KDIFDNFANIIEGGKEGNLV 1820
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 110-149 2.35e-03

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 37.42  E-value: 2.35e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2462502415 110 KIRADHEK--ALEEAKEKLRKSREEIRAEIQTEKNKVVQEMK 149
Cdd:cd06503    75 RKEAEKIKeeILAEAKEEAERILEQAKAEIEQEKEKALAELR 116
AhaH TIGR02926
ATP synthase archaeal, H subunit; he A1/A0 ATP synthase is homologous to the V-type (V1/V0, ...
 108-151 6.33e-03

ATP synthase archaeal, H subunit; he A1/A0 ATP synthase is homologous to the V-type (V1/V0, vacuolar) ATPase, but functions in the ATP synthetic direction as does the F1/F0 ATPase of bacteria. The hydrophilic A1 "stalk" complex (AhaABCDEFG) is the site of ATP generation and is coupled to the membrane-embedded proton translocating A0 complex. It is unclear precisely where AhaH fits into these complexes.


Pssm-ID: 131972 [Multi-domain]  Cd Length: 85  Bit Score: 35.21  E-value: 6.33e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462502415 108 RNKIRADHEKALEEAKEK----LRKSREEIRAE---IQTEKNKVVQEMKIK 151
Cdd:TIGR02926  30 REEARELLEEAEEEASKLgeeiIKEAEEEIEKEaekIREEGEKEIEAMKSK 80
 
Name Accession Description Interval E-value
Glyco_hydro_47 pfam01532
Glycosyl hydrolase family 47; Members of this family are alpha-mannosidases that catalyze the ...
 187-319 6.61e-67

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: 216.65  E-value: 6.61e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502415 187 MMKHAWDNYRTYGWGHNELRPIARKGHSPniFGSsqMGATIVDALDTLYIMGLHDEFLDGQRWIEDNLDFSVNS-EVSVF 265
Cdd:pfam01532   1 AFLHAWDGYKKYAWGHDELRPISGGGNDT--FGG--WGATIVDSLDTLIIMGLTDEFEEAVDWVEKTLDFDKDStEVSVF 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462502415 266 EVNIRFIGGLLAAYYLS--GEEIFKIKAVQLAEKLLPAFNTPTGIPWAMVNLKRSY 319
Cdd:pfam01532  77 ETTIRYLGGLLSAYDLSgdGDDVLLEKAVDLADRLLPAFDTPTGIPYPRVNLKTGK 132
PTZ00470 PTZ00470
glycoside hydrolase family 47 protein; Provisional
 173-325 2.79e-57

glycoside hydrolase family 47 protein; Provisional


Pssm-ID: 240427  Cd Length: 522  Bit Score: 193.40  E-value: 2.79e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502415 173 EDNDIrEKREKIKEMMKHAWDNYRTYGWGHNELRPIARKGHspNIFGssqMGATIVDALDTLYIMGLHDEFLDGQRWIED 252
Cdd:PTZ00470   66 EKLNI-KRRESVREAMKHAWEGYKEYAWGHDELRPLTKRHH--EWFG---LGLTIIDSLDTLKIMGLKKEYKEGRDWVAN 139

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462502415 253 NLDFS--VNSEVSVFEVNIRFIGGLLAAYYLSGEEIFKIKAVQLAEKLLPAFNTPTGIPWAMVNLK--RSYICRWPG 325
Cdd:PTZ00470  140 NLKQSkdTGLGVSVFETTIRVLGGLLSAYDLTGDEMYLEKAREIADRLLPAFNEDTGFPASEINLAtgRKSYPGWAG 216
PTZ00121 PTZ00121
MAEBL; Provisional
 109-208 1.30e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 1.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502415  109 NKIRAdhEKALEEAKEKLRKSrEEIRAEiQTEKNKVVQEMKIKENKPLPPVPIPNLVGIRGGDPEDNDIREKREKikeMM 188
Cdd:PTZ00121  1728 NKIKA--EEAKKEAEEDKKKA-EEAKKD-EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK---KI 1800

                           90       100
                   ....*....|....*....|
gi 2462502415  189 KHAWDNYRTYGWGHNELRPI 208
Cdd:PTZ00121  1801 KDIFDNFANIIEGGKEGNLV 1820
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 110-149 2.35e-03

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 37.42  E-value: 2.35e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2462502415 110 KIRADHEK--ALEEAKEKLRKSREEIRAEIQTEKNKVVQEMK 149
Cdd:cd06503    75 RKEAEKIKeeILAEAKEEAERILEQAKAEIEQEKEKALAELR 116
AhaH TIGR02926
ATP synthase archaeal, H subunit; he A1/A0 ATP synthase is homologous to the V-type (V1/V0, ...
 108-151 6.33e-03

ATP synthase archaeal, H subunit; he A1/A0 ATP synthase is homologous to the V-type (V1/V0, vacuolar) ATPase, but functions in the ATP synthetic direction as does the F1/F0 ATPase of bacteria. The hydrophilic A1 "stalk" complex (AhaABCDEFG) is the site of ATP generation and is coupled to the membrane-embedded proton translocating A0 complex. It is unclear precisely where AhaH fits into these complexes.


Pssm-ID: 131972 [Multi-domain]  Cd Length: 85  Bit Score: 35.21  E-value: 6.33e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462502415 108 RNKIRADHEKALEEAKEK----LRKSREEIRAE---IQTEKNKVVQEMKIK 151
Cdd:TIGR02926  30 REEARELLEEAEEEASKLgeeiIKEAEEEIEKEaekIREEGEKEIEAMKSK 80
 
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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