NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|937942412|dbj|BAT17324|]
View 

Os12g0510500 [Oryza sativa Japonica Group]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
RX-CC_like super family cl36576
Coiled-coil domain of the potato virux X resistance protein and similar proteins; The potato ...
22-80 1.99e-06

Coiled-coil domain of the potato virux X resistance protein and similar proteins; The potato virus X resistance protein (RX) confers resistance against potato virus X. It is a member of a family of resistance proteins with a domain architecture that includes an N-terminal coiled-coil domain (modeled here), a nucleotide-binding domain, and leucine-rich repeats (CC-NB-LRR). These intracellular resistance proteins recognize pathogen effector proteins and will subsequently trigger a response that may be as severe as localized cell death. The N-terminal coiled-coil domain of RX has been shown to interact with RanGAP2, which is a necessary co-factor in the resistance response.


The actual alignment was detected with superfamily member cd14798:

Pssm-ID: 453100 [Multi-domain]  Cd Length: 124  Bit Score: 42.61  E-value: 1.99e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 937942412  22 RRWLNSLRDVAYDAEDLIES----AVLQQQGDR--YSAVNSVLHPISRYRSAQKVEEIRSRIRDM 80
Cdd:cd14798   58 KDWVKQVRDVAYDAEDIIDSfllkLVPDKRRGGflKRLFSLLKELKELHQVAKEIQSIKSRIKDI 122
 
Name Accession Description Interval E-value
RX-CC_like cd14798
Coiled-coil domain of the potato virux X resistance protein and similar proteins; The potato ...
22-80 1.99e-06

Coiled-coil domain of the potato virux X resistance protein and similar proteins; The potato virus X resistance protein (RX) confers resistance against potato virus X. It is a member of a family of resistance proteins with a domain architecture that includes an N-terminal coiled-coil domain (modeled here), a nucleotide-binding domain, and leucine-rich repeats (CC-NB-LRR). These intracellular resistance proteins recognize pathogen effector proteins and will subsequently trigger a response that may be as severe as localized cell death. The N-terminal coiled-coil domain of RX has been shown to interact with RanGAP2, which is a necessary co-factor in the resistance response.


Pssm-ID: 271353 [Multi-domain]  Cd Length: 124  Bit Score: 42.61  E-value: 1.99e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 937942412  22 RRWLNSLRDVAYDAEDLIES----AVLQQQGDR--YSAVNSVLHPISRYRSAQKVEEIRSRIRDM 80
Cdd:cd14798   58 KDWVKQVRDVAYDAEDIIDSfllkLVPDKRRGGflKRLFSLLKELKELHQVAKEIQSIKSRIKDI 122
Rx_N pfam18052
Rx N-terminal domain; This entry represents the N-terminal domain found in many plant ...
16-50 1.78e-05

Rx N-terminal domain; This entry represents the N-terminal domain found in many plant resistance proteins. This domain has been predicted to be a coiled-coil, however the structure shows that it adopts a four helical bundle fold.


Pssm-ID: 436239  Cd Length: 93  Bit Score: 39.56  E-value: 1.78e-05
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 937942412  16 RQDATARRWLNSLRDVAYDAEDLIESAVLQQQGDR 50
Cdd:pfam18052 49 ITDEQVKLWLKQLRDVAYDAEDVLDEFLYEALRRK 83
 
Name Accession Description Interval E-value
RX-CC_like cd14798
Coiled-coil domain of the potato virux X resistance protein and similar proteins; The potato ...
22-80 1.99e-06

Coiled-coil domain of the potato virux X resistance protein and similar proteins; The potato virus X resistance protein (RX) confers resistance against potato virus X. It is a member of a family of resistance proteins with a domain architecture that includes an N-terminal coiled-coil domain (modeled here), a nucleotide-binding domain, and leucine-rich repeats (CC-NB-LRR). These intracellular resistance proteins recognize pathogen effector proteins and will subsequently trigger a response that may be as severe as localized cell death. The N-terminal coiled-coil domain of RX has been shown to interact with RanGAP2, which is a necessary co-factor in the resistance response.


Pssm-ID: 271353 [Multi-domain]  Cd Length: 124  Bit Score: 42.61  E-value: 1.99e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 937942412  22 RRWLNSLRDVAYDAEDLIES----AVLQQQGDR--YSAVNSVLHPISRYRSAQKVEEIRSRIRDM 80
Cdd:cd14798   58 KDWVKQVRDVAYDAEDIIDSfllkLVPDKRRGGflKRLFSLLKELKELHQVAKEIQSIKSRIKDI 122
Rx_N pfam18052
Rx N-terminal domain; This entry represents the N-terminal domain found in many plant ...
16-50 1.78e-05

Rx N-terminal domain; This entry represents the N-terminal domain found in many plant resistance proteins. This domain has been predicted to be a coiled-coil, however the structure shows that it adopts a four helical bundle fold.


Pssm-ID: 436239  Cd Length: 93  Bit Score: 39.56  E-value: 1.78e-05
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 937942412  16 RQDATARRWLNSLRDVAYDAEDLIESAVLQQQGDR 50
Cdd:pfam18052 49 ITDEQVKLWLKQLRDVAYDAEDVLDEFLYEALRRK 83
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH