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Conserved domains on  [gi|22330396|ref|NP_176499|]
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GPI transamidase subunit PIG-U [Arabidopsis thaliana]

Protein Classification

PIG-U family protein( domain architecture ID 10535524)

PIG-U family protein similar to human phosphatidylinositol glycan anchor biosynthesis class U protein and Saccharomyces cerevisiae GPI transamidase component GAB1 (Cdc91p), which attach GPI-anchors to proteins

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PIG-U pfam06728
GPI transamidase subunit PIG-U; Many eukaryotic proteins are anchored to the cell surface via ...
33-363 1.49e-83

GPI transamidase subunit PIG-U; Many eukaryotic proteins are anchored to the cell surface via glycosylphosphatidylinositol (GPI), which is posttranslationally attached to the carboxyl-terminus by GPI transamidase. The mammalian GPI transamidase is a complex of at least four subunits, GPI8, GAA1, PIG-S, and PIG-T. PIG-U is thought to represent a fifth subunit in this complex and may be involved in the recognition of either the GPI attachment signal or the lipid portion of GPI.


:

Pssm-ID: 429085  Cd Length: 375  Bit Score: 259.85  E-value: 1.49e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330396    33 ADILSAMLLRAIGQKLQmayglnARLLGFLKSSRDKVIlpCGDIAALVYLWNPFTIVSCVGLSTSPIENLAVILALFGAV 112
Cdd:pfam06728  88 IDLLIALLLYAIAKSYQ------KDISKLFKSKRDKSL--SPLLIAALYLFNPLTILSCIALSTTVFSNLFILLSLYSAV 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330396   113 TRRVPLAAFGLVIATHLSLYPATLTIPIIFLLGYGLDAPPIKLFLQtrsveneesststvskqaklkqtthlpflwktva 192
Cdd:pfam06728 160 KGNRALSAIALALASYLSLYPILLLAPLLLLLIFKSKNNLSSNSLS---------------------------------- 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330396   193 HFLFWVLLWSLYVLILCALSLnKYGGLEEMFKRTYGFILSIEDLSPNIGVFWYFFAEVFDFFRNFFLIVLHVNILFMLLP 272
Cdd:pfam06728 206 KFLSFLLLFLLTLAALLLASF-LITGSWDFLDATYGFILTFEDLTPNLGLWWYFFTEMFDHFRPFFLFVFNLHPFIYILP 284
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330396   273 LAIRLKHRPCFLAFIYLAISSILKSYPSVGDSALYLSLWALFVNELLDMKFSFFLFCGYLGISLLSPVMHNLWIWRGTGN 352
Cdd:pfam06728 285 LTIRLRKQPLFALTLLLGLISIFKPYPTLGDLGLYLSLLPLFRHLFPYMRYSFLIGLTLLVALLLSPIFYHLWIVLGSGN 364
                         330
                  ....*....|.
gi 22330396   353 ANFYFGNAIGY 363
Cdd:pfam06728 365 ANFFYAITLVY 375
 
Name Accession Description Interval E-value
PIG-U pfam06728
GPI transamidase subunit PIG-U; Many eukaryotic proteins are anchored to the cell surface via ...
33-363 1.49e-83

GPI transamidase subunit PIG-U; Many eukaryotic proteins are anchored to the cell surface via glycosylphosphatidylinositol (GPI), which is posttranslationally attached to the carboxyl-terminus by GPI transamidase. The mammalian GPI transamidase is a complex of at least four subunits, GPI8, GAA1, PIG-S, and PIG-T. PIG-U is thought to represent a fifth subunit in this complex and may be involved in the recognition of either the GPI attachment signal or the lipid portion of GPI.


Pssm-ID: 429085  Cd Length: 375  Bit Score: 259.85  E-value: 1.49e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330396    33 ADILSAMLLRAIGQKLQmayglnARLLGFLKSSRDKVIlpCGDIAALVYLWNPFTIVSCVGLSTSPIENLAVILALFGAV 112
Cdd:pfam06728  88 IDLLIALLLYAIAKSYQ------KDISKLFKSKRDKSL--SPLLIAALYLFNPLTILSCIALSTTVFSNLFILLSLYSAV 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330396   113 TRRVPLAAFGLVIATHLSLYPATLTIPIIFLLGYGLDAPPIKLFLQtrsveneesststvskqaklkqtthlpflwktva 192
Cdd:pfam06728 160 KGNRALSAIALALASYLSLYPILLLAPLLLLLIFKSKNNLSSNSLS---------------------------------- 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330396   193 HFLFWVLLWSLYVLILCALSLnKYGGLEEMFKRTYGFILSIEDLSPNIGVFWYFFAEVFDFFRNFFLIVLHVNILFMLLP 272
Cdd:pfam06728 206 KFLSFLLLFLLTLAALLLASF-LITGSWDFLDATYGFILTFEDLTPNLGLWWYFFTEMFDHFRPFFLFVFNLHPFIYILP 284
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330396   273 LAIRLKHRPCFLAFIYLAISSILKSYPSVGDSALYLSLWALFVNELLDMKFSFFLFCGYLGISLLSPVMHNLWIWRGTGN 352
Cdd:pfam06728 285 LTIRLRKQPLFALTLLLGLISIFKPYPTLGDLGLYLSLLPLFRHLFPYMRYSFLIGLTLLVALLLSPIFYHLWIVLGSGN 364
                         330
                  ....*....|.
gi 22330396   353 ANFYFGNAIGY 363
Cdd:pfam06728 365 ANFFYAITLVY 375
 
Name Accession Description Interval E-value
PIG-U pfam06728
GPI transamidase subunit PIG-U; Many eukaryotic proteins are anchored to the cell surface via ...
33-363 1.49e-83

GPI transamidase subunit PIG-U; Many eukaryotic proteins are anchored to the cell surface via glycosylphosphatidylinositol (GPI), which is posttranslationally attached to the carboxyl-terminus by GPI transamidase. The mammalian GPI transamidase is a complex of at least four subunits, GPI8, GAA1, PIG-S, and PIG-T. PIG-U is thought to represent a fifth subunit in this complex and may be involved in the recognition of either the GPI attachment signal or the lipid portion of GPI.


Pssm-ID: 429085  Cd Length: 375  Bit Score: 259.85  E-value: 1.49e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330396    33 ADILSAMLLRAIGQKLQmayglnARLLGFLKSSRDKVIlpCGDIAALVYLWNPFTIVSCVGLSTSPIENLAVILALFGAV 112
Cdd:pfam06728  88 IDLLIALLLYAIAKSYQ------KDISKLFKSKRDKSL--SPLLIAALYLFNPLTILSCIALSTTVFSNLFILLSLYSAV 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330396   113 TRRVPLAAFGLVIATHLSLYPATLTIPIIFLLGYGLDAPPIKLFLQtrsveneesststvskqaklkqtthlpflwktva 192
Cdd:pfam06728 160 KGNRALSAIALALASYLSLYPILLLAPLLLLLIFKSKNNLSSNSLS---------------------------------- 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330396   193 HFLFWVLLWSLYVLILCALSLnKYGGLEEMFKRTYGFILSIEDLSPNIGVFWYFFAEVFDFFRNFFLIVLHVNILFMLLP 272
Cdd:pfam06728 206 KFLSFLLLFLLTLAALLLASF-LITGSWDFLDATYGFILTFEDLTPNLGLWWYFFTEMFDHFRPFFLFVFNLHPFIYILP 284
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22330396   273 LAIRLKHRPCFLAFIYLAISSILKSYPSVGDSALYLSLWALFVNELLDMKFSFFLFCGYLGISLLSPVMHNLWIWRGTGN 352
Cdd:pfam06728 285 LTIRLRKQPLFALTLLLGLISIFKPYPTLGDLGLYLSLLPLFRHLFPYMRYSFLIGLTLLVALLLSPIFYHLWIVLGSGN 364
                         330
                  ....*....|.
gi 22330396   353 ANFYFGNAIGY 363
Cdd:pfam06728 365 ANFFYAITLVY 375
 
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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