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Conserved domains on  [gi|6323131|ref|NP_013203|]
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anaphase promoting complex subunit 9 [Saccharomyces cerevisiae S288C]

Protein Classification

ANAPC9 superfamily-containing protein( domain architecture ID 57584)

ANAPC9 superfamily-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ANAPC9 super family cl15122
Anaphase-promoting complex subunit 9; Apc9 is one of the subunits of the anaphase-promoting ...
91-170 3.17e-11

Anaphase-promoting complex subunit 9; Apc9 is one of the subunits of the anaphase-promoting complex, or cyclosome, which is essential for regulating entry into anaphase and exit from mitosis. The APC is a ubiquitin-protein ligase complex. All APC subunits are members of the cullin family proteins, which bind to a ring-finger subunit via a conserved cullin domain. The APC is made up of four parts, the third of which is a tetratricopeptide repeat arm (TPR) that contains Apc9.


The actual alignment was detected with superfamily member pfam12856:

Pssm-ID: 403916  Cd Length: 112  Bit Score: 59.12  E-value: 3.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323131     91 YDYSPFCERNT---------LRESRIDSFLKAERAAHCLVFHKvghldgidsyrPDIDIMCGEEANKYDSANPEGNGSML 161
Cdd:pfam12856  35 YDYSVFTNYTTghdhslppaIKESQIKAWESAERIAHNLIFDK-----------DDSDDDCDDDEDEEGSAKEVRENSNL 103

                  ....*....
gi 6323131    162 LESVPGCNK 170
Cdd:pfam12856 104 IVSIPGYTK 112
 
Name Accession Description Interval E-value
ANAPC9 pfam12856
Anaphase-promoting complex subunit 9; Apc9 is one of the subunits of the anaphase-promoting ...
91-170 3.17e-11

Anaphase-promoting complex subunit 9; Apc9 is one of the subunits of the anaphase-promoting complex, or cyclosome, which is essential for regulating entry into anaphase and exit from mitosis. The APC is a ubiquitin-protein ligase complex. All APC subunits are members of the cullin family proteins, which bind to a ring-finger subunit via a conserved cullin domain. The APC is made up of four parts, the third of which is a tetratricopeptide repeat arm (TPR) that contains Apc9.


Pssm-ID: 403916  Cd Length: 112  Bit Score: 59.12  E-value: 3.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323131     91 YDYSPFCERNT---------LRESRIDSFLKAERAAHCLVFHKvghldgidsyrPDIDIMCGEEANKYDSANPEGNGSML 161
Cdd:pfam12856  35 YDYSVFTNYTTghdhslppaIKESQIKAWESAERIAHNLIFDK-----------DDSDDDCDDDEDEEGSAKEVRENSNL 103

                  ....*....
gi 6323131    162 LESVPGCNK 170
Cdd:pfam12856 104 IVSIPGYTK 112
 
Name Accession Description Interval E-value
ANAPC9 pfam12856
Anaphase-promoting complex subunit 9; Apc9 is one of the subunits of the anaphase-promoting ...
91-170 3.17e-11

Anaphase-promoting complex subunit 9; Apc9 is one of the subunits of the anaphase-promoting complex, or cyclosome, which is essential for regulating entry into anaphase and exit from mitosis. The APC is a ubiquitin-protein ligase complex. All APC subunits are members of the cullin family proteins, which bind to a ring-finger subunit via a conserved cullin domain. The APC is made up of four parts, the third of which is a tetratricopeptide repeat arm (TPR) that contains Apc9.


Pssm-ID: 403916  Cd Length: 112  Bit Score: 59.12  E-value: 3.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323131     91 YDYSPFCERNT---------LRESRIDSFLKAERAAHCLVFHKvghldgidsyrPDIDIMCGEEANKYDSANPEGNGSML 161
Cdd:pfam12856  35 YDYSVFTNYTTghdhslppaIKESQIKAWESAERIAHNLIFDK-----------DDSDDDCDDDEDEEGSAKEVRENSNL 103

                  ....*....
gi 6323131    162 LESVPGCNK 170
Cdd:pfam12856 104 IVSIPGYTK 112
 
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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