NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|193211208|ref|NP_001122747|]
View 

JNK-interacting protein [Caenorhabditis elegans]

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
WD40_2 super family cl41045
WD40 repeated domain; This entry contains an array of WD40 repeats found in RhoGEF proteins.
 207-408 7.19e-44

WD40 repeated domain; This entry contains an array of WD40 repeats found in RhoGEF proteins.


The actual alignment was detected with superfamily member pfam19056:

Pssm-ID: 465964  Cd Length: 487  Bit Score: 162.50  E-value: 7.19e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211208  207 PTVWMGGQNQYIYIHSAVTAWKQCLRRIKMPD--AVLSIVHYKSRIFAALANGTIAIFHRNKHGEWSDEGYHSLRVGSAt 284
Cdd:pfam19056 102 PTICLGLEDGSISVYGSVDTAKKCLLQHFTPErsPVLCLKHSPQFLFAGLVNGKVAVYARAEDGLWDPEPPKLVKLGVL- 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211208  285 sSVRSLCLVSTNIWATYKNCVVVLDAESLQIVKVFAAHPRKDSQVRNMQWVGAGVWLSIRLDSTLRLYHAHTYEHLQDVD 364
Cdd:pfam19056 181 -PVRSLLALEDTVWASCGNQVTVISGETLQTEQSFEAHQDEGMSVSHMVVAGGGVWMAFSSGSSIRLFHTETLEHLQDIN 259

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 193211208  365 IEPYVTKMLGTSKldfsYMRTTALLVSNRRLWIGTGTGVIISVP 408
Cdd:pfam19056 260 IATRVHFMLPGQK----RVSVTSLLICQGLLWVGTNLGVIVALP 299
 
Name Accession Description Interval E-value
WD40_2 pfam19056
WD40 repeated domain; This entry contains an array of WD40 repeats found in RhoGEF proteins.
 207-408 7.19e-44

WD40 repeated domain; This entry contains an array of WD40 repeats found in RhoGEF proteins.


Pssm-ID: 465964  Cd Length: 487  Bit Score: 162.50  E-value: 7.19e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211208  207 PTVWMGGQNQYIYIHSAVTAWKQCLRRIKMPD--AVLSIVHYKSRIFAALANGTIAIFHRNKHGEWSDEGYHSLRVGSAt 284
Cdd:pfam19056 102 PTICLGLEDGSISVYGSVDTAKKCLLQHFTPErsPVLCLKHSPQFLFAGLVNGKVAVYARAEDGLWDPEPPKLVKLGVL- 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211208  285 sSVRSLCLVSTNIWATYKNCVVVLDAESLQIVKVFAAHPRKDSQVRNMQWVGAGVWLSIRLDSTLRLYHAHTYEHLQDVD 364
Cdd:pfam19056 181 -PVRSLLALEDTVWASCGNQVTVISGETLQTEQSFEAHQDEGMSVSHMVVAGGGVWMAFSSGSSIRLFHTETLEHLQDIN 259

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 193211208  365 IEPYVTKMLGTSKldfsYMRTTALLVSNRRLWIGTGTGVIISVP 408
Cdd:pfam19056 260 IATRVHFMLPGQK----RVSVTSLLICQGLLWVGTNLGVIVALP 299
8prop_hemeD1_NirF cd20778
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; ...
 297-363 6.73e-03

eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; Denitrification is a process that enables biofilm formation of the opportunistic human pathogen Pseudomonas aeruginosa, making it more resilient to antibiotics and highly adaptable to different habitats. During denitrification, nitrate (Nar), nitrite (Nir), nitric oxide (Nor), and nitrous oxide (Nos) reductases catalyze the reaction cascade of NO3- -> NO2- -> NO -> N2O -> N2. The integral membrane proteins NorC, NorB, and NosR form the core assembly platform that binds the nitrate reductase NarGHI and the periplasmic cytochrome cd1 (nitrite reductase) NirS via its maturation factor NirF. The nirFDLGHJE genes encode proteins required for heme d1 biosynthesis. NirS, NirF, and NirN, the monomeric dihydro-heme d1 dehydrogenase form a stable complex during nitrite reductase maturation. The nitrite reductase NirS is bound to the denitrification supercomplex via NorB, while the electron donor system NirM and the enzyme maturation machinery NirN-NirF-NirQ, interacting with NirS, are bound via NorC.


Pssm-ID: 467722 [Multi-domain]  Cd Length: 381  Bit Score: 38.80  E-value: 6.73e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 193211208 297 IWATY---KNCVV-VLDAESLQIVKVFAAHPRkdsqVRNMQW--VGAGVWLSIRLDSTLRLYHAHTYEHLQDV 363
Cdd:cd20778  295 VWVNFsgpDNDTVqVIDTKTLKVVKTLEPGKR----VLHMEFtpRGEAVYISVNDDNKVVVYDTRTFREIKEV 363
 
Name Accession Description Interval E-value
WD40_2 pfam19056
WD40 repeated domain; This entry contains an array of WD40 repeats found in RhoGEF proteins.
 207-408 7.19e-44

WD40 repeated domain; This entry contains an array of WD40 repeats found in RhoGEF proteins.


Pssm-ID: 465964  Cd Length: 487  Bit Score: 162.50  E-value: 7.19e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211208  207 PTVWMGGQNQYIYIHSAVTAWKQCLRRIKMPD--AVLSIVHYKSRIFAALANGTIAIFHRNKHGEWSDEGYHSLRVGSAt 284
Cdd:pfam19056 102 PTICLGLEDGSISVYGSVDTAKKCLLQHFTPErsPVLCLKHSPQFLFAGLVNGKVAVYARAEDGLWDPEPPKLVKLGVL- 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193211208  285 sSVRSLCLVSTNIWATYKNCVVVLDAESLQIVKVFAAHPRKDSQVRNMQWVGAGVWLSIRLDSTLRLYHAHTYEHLQDVD 364
Cdd:pfam19056 181 -PVRSLLALEDTVWASCGNQVTVISGETLQTEQSFEAHQDEGMSVSHMVVAGGGVWMAFSSGSSIRLFHTETLEHLQDIN 259

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 193211208  365 IEPYVTKMLGTSKldfsYMRTTALLVSNRRLWIGTGTGVIISVP 408
Cdd:pfam19056 260 IATRVHFMLPGQK----RVSVTSLLICQGLLWVGTNLGVIVALP 299
8prop_hemeD1_NirF cd20778
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; ...
 297-363 6.73e-03

eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; Denitrification is a process that enables biofilm formation of the opportunistic human pathogen Pseudomonas aeruginosa, making it more resilient to antibiotics and highly adaptable to different habitats. During denitrification, nitrate (Nar), nitrite (Nir), nitric oxide (Nor), and nitrous oxide (Nos) reductases catalyze the reaction cascade of NO3- -> NO2- -> NO -> N2O -> N2. The integral membrane proteins NorC, NorB, and NosR form the core assembly platform that binds the nitrate reductase NarGHI and the periplasmic cytochrome cd1 (nitrite reductase) NirS via its maturation factor NirF. The nirFDLGHJE genes encode proteins required for heme d1 biosynthesis. NirS, NirF, and NirN, the monomeric dihydro-heme d1 dehydrogenase form a stable complex during nitrite reductase maturation. The nitrite reductase NirS is bound to the denitrification supercomplex via NorB, while the electron donor system NirM and the enzyme maturation machinery NirN-NirF-NirQ, interacting with NirS, are bound via NorC.


Pssm-ID: 467722 [Multi-domain]  Cd Length: 381  Bit Score: 38.80  E-value: 6.73e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 193211208 297 IWATY---KNCVV-VLDAESLQIVKVFAAHPRkdsqVRNMQW--VGAGVWLSIRLDSTLRLYHAHTYEHLQDV 363
Cdd:cd20778  295 VWVNFsgpDNDTVqVIDTKTLKVVKTLEPGKR----VLHMEFtpRGEAVYISVNDDNKVVVYDTRTFREIKEV 363
 
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