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Conserved domains on  [gi|79315726|ref|NP_001030895|]
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Plant regulator RWP-RK family protein [Arabidopsis thaliana]

Protein Classification

NLP family protein( domain architecture ID 10488934)

NLP (NIN (nodule inception)-like proteins) family protein is involved in mediating the early nitrogen response

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PB1_NLP cd06407
A PB1 domain is present in NIN like proteins (NLP), a key enzyme in a process of establishment ...
 793-874 3.52e-34

A PB1 domain is present in NIN like proteins (NLP), a key enzyme in a process of establishment of symbiosis betweeen legumes and nitrogen fixing bacteria (Rhizobium). The PB1 domain is a modular domain mediating specific protein-protein interaction which play a role in many critical cell processes like osteoclastogenesis, angiogenesis, early cardiovascular development, and cell polarity. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domains, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants.


:

Pssm-ID: 99728  Cd Length: 82  Bit Score: 125.51  E-value: 3.52e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79315726 793 LTVKATYREDTVRFKLDPyVVGCSQLYREVAKRFKLQE-GAFQLKYLDDEEEWVMLVTDSDLHECFEILNGMRKHTVKFL 871
Cdd:cd06407   1 VRVKATYGEEKIRFRLPP-SWGFTELKQEIAKRFKLDDmSAFDLKYLDDDEEWVLLTCDADLEECIDVYRSSGSHTIRLL 79


                ...
gi 79315726 872 VRD 874
Cdd:cd06407  80 VHA 82
RWP-RK pfam02042
RWP-RK domain; This domain is named RWP-RK after a conserved motif at the C terminus of the ...
 535-583 1.51e-23

RWP-RK domain; This domain is named RWP-RK after a conserved motif at the C terminus of the presumed domain. The domain is found in algal minus dominance proteins as well as plant proteins involved in nitrogen-controlled development.


:

Pssm-ID: 460427  Cd Length: 49  Bit Score: 94.11  E-value: 1.51e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 79315726   535 NVSLNVLQQYFSGSLKDAAKSLGVCPTTLKRICRQHGIMRWPSRKINKV 583
Cdd:pfam02042   1 SITLEDLSQYFHLPIKEAAKELGVSLTTLKRICRRLGIPRWPHRKLKSL 49
 
Name Accession Description Interval E-value
PB1_NLP cd06407
A PB1 domain is present in NIN like proteins (NLP), a key enzyme in a process of establishment ...
 793-874 3.52e-34

A PB1 domain is present in NIN like proteins (NLP), a key enzyme in a process of establishment of symbiosis betweeen legumes and nitrogen fixing bacteria (Rhizobium). The PB1 domain is a modular domain mediating specific protein-protein interaction which play a role in many critical cell processes like osteoclastogenesis, angiogenesis, early cardiovascular development, and cell polarity. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domains, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants.


Pssm-ID: 99728  Cd Length: 82  Bit Score: 125.51  E-value: 3.52e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79315726 793 LTVKATYREDTVRFKLDPyVVGCSQLYREVAKRFKLQE-GAFQLKYLDDEEEWVMLVTDSDLHECFEILNGMRKHTVKFL 871
Cdd:cd06407   1 VRVKATYGEEKIRFRLPP-SWGFTELKQEIAKRFKLDDmSAFDLKYLDDDEEWVLLTCDADLEECIDVYRSSGSHTIRLL 79


                ...
gi 79315726 872 VRD 874
Cdd:cd06407  80 VHA 82
RWP-RK pfam02042
RWP-RK domain; This domain is named RWP-RK after a conserved motif at the C terminus of the ...
 535-583 1.51e-23

RWP-RK domain; This domain is named RWP-RK after a conserved motif at the C terminus of the presumed domain. The domain is found in algal minus dominance proteins as well as plant proteins involved in nitrogen-controlled development.


Pssm-ID: 460427  Cd Length: 49  Bit Score: 94.11  E-value: 1.51e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 79315726   535 NVSLNVLQQYFSGSLKDAAKSLGVCPTTLKRICRQHGIMRWPSRKINKV 583
Cdd:pfam02042   1 SITLEDLSQYFHLPIKEAAKELGVSLTTLKRICRRLGIPRWPHRKLKSL 49
PB1 smart00666
PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. ...
 792-872 6.17e-21

PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. The domain adopts a beta-grasp fold, similar to that found in ubiquitin and Ras-binding domains. A motif, variously termed OPR, PC and AID, represents the most conserved region of the majority of PB1 domains, and is necessary for PB1 domain function. This function is the formation of PB1 domain heterodimers, although not all PB1 domain pairs associate.


Pssm-ID: 214770  Cd Length: 81  Bit Score: 87.64  E-value: 6.17e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79315726    792 TLTVKATYREDTVRFKLDPyVVGCSQLYREVAKRFKLQEGAFQLKYLDDEEEWVMLVTDSDLHECFEILNGMRKHTVKFL 871
Cdd:smart00666   1 TVDVKLRYGGETRRLSVPR-DISFEDLRSKVAKRFGLDNQSFTLKYQDEDGDLVSLTSDEDLEEAIEEYDSLGSKKLRLH 79


                   .
gi 79315726    872 V 872
Cdd:smart00666  80 V 80
PB1 pfam00564
PB1 domain;
792-874 2.34e-19

PB1 domain;


Pssm-ID: 395447  Cd Length: 84  Bit Score: 83.11  E-value: 2.34e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79315726   792 TLTVKATYREDTVRFKLDPYVVGCSQLYREVAKRFKLQEGAFQLKYLDDEEEWVMLVTDSDLHECFEILNGMRKHTVKFL 871
Cdd:pfam00564   1 TVRLKLRYGGGIRRFLSVSRGISFEELRALVEQRFGLDDVDFKLKYPDEDGDLVSLTSDEDLEEALEEARSLGSKSLRLH 80


                  ...
gi 79315726   872 VRD 874
Cdd:pfam00564  81 VFP 83
 
Name Accession Description Interval E-value
PB1_NLP cd06407
A PB1 domain is present in NIN like proteins (NLP), a key enzyme in a process of establishment ...
 793-874 3.52e-34

A PB1 domain is present in NIN like proteins (NLP), a key enzyme in a process of establishment of symbiosis betweeen legumes and nitrogen fixing bacteria (Rhizobium). The PB1 domain is a modular domain mediating specific protein-protein interaction which play a role in many critical cell processes like osteoclastogenesis, angiogenesis, early cardiovascular development, and cell polarity. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domains, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants.


Pssm-ID: 99728  Cd Length: 82  Bit Score: 125.51  E-value: 3.52e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79315726 793 LTVKATYREDTVRFKLDPyVVGCSQLYREVAKRFKLQE-GAFQLKYLDDEEEWVMLVTDSDLHECFEILNGMRKHTVKFL 871
Cdd:cd06407   1 VRVKATYGEEKIRFRLPP-SWGFTELKQEIAKRFKLDDmSAFDLKYLDDDEEWVLLTCDADLEECIDVYRSSGSHTIRLL 79


                ...
gi 79315726 872 VRD 874
Cdd:cd06407  80 VHA 82
RWP-RK pfam02042
RWP-RK domain; This domain is named RWP-RK after a conserved motif at the C terminus of the ...
 535-583 1.51e-23

RWP-RK domain; This domain is named RWP-RK after a conserved motif at the C terminus of the presumed domain. The domain is found in algal minus dominance proteins as well as plant proteins involved in nitrogen-controlled development.


Pssm-ID: 460427  Cd Length: 49  Bit Score: 94.11  E-value: 1.51e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 79315726   535 NVSLNVLQQYFSGSLKDAAKSLGVCPTTLKRICRQHGIMRWPSRKINKV 583
Cdd:pfam02042   1 SITLEDLSQYFHLPIKEAAKELGVSLTTLKRICRRLGIPRWPHRKLKSL 49
PB1 smart00666
PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. ...
 792-872 6.17e-21

PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. The domain adopts a beta-grasp fold, similar to that found in ubiquitin and Ras-binding domains. A motif, variously termed OPR, PC and AID, represents the most conserved region of the majority of PB1 domains, and is necessary for PB1 domain function. This function is the formation of PB1 domain heterodimers, although not all PB1 domain pairs associate.


Pssm-ID: 214770  Cd Length: 81  Bit Score: 87.64  E-value: 6.17e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79315726    792 TLTVKATYREDTVRFKLDPyVVGCSQLYREVAKRFKLQEGAFQLKYLDDEEEWVMLVTDSDLHECFEILNGMRKHTVKFL 871
Cdd:smart00666   1 TVDVKLRYGGETRRLSVPR-DISFEDLRSKVAKRFGLDNQSFTLKYQDEDGDLVSLTSDEDLEEAIEEYDSLGSKKLRLH 79


                   .
gi 79315726    872 V 872
Cdd:smart00666  80 V 80
PB1 pfam00564
PB1 domain;
792-874 2.34e-19

PB1 domain;


Pssm-ID: 395447  Cd Length: 84  Bit Score: 83.11  E-value: 2.34e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79315726   792 TLTVKATYREDTVRFKLDPYVVGCSQLYREVAKRFKLQEGAFQLKYLDDEEEWVMLVTDSDLHECFEILNGMRKHTVKFL 871
Cdd:pfam00564   1 TVRLKLRYGGGIRRFLSVSRGISFEELRALVEQRFGLDDVDFKLKYPDEDGDLVSLTSDEDLEEALEEARSLGSKSLRLH 80


                  ...
gi 79315726   872 VRD 874
Cdd:pfam00564  81 VFP 83
PB1 cd05992
The PB1 domain is a modular domain mediating specific protein-protein interactions which play ...
 793-873 6.84e-17

The PB1 domain is a modular domain mediating specific protein-protein interactions which play a role in many critical cell processes, such as osteoclastogenesis, angiogenesis, early cardiovascular development, and cell polarity. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domain, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as a noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants.


Pssm-ID: 99716 [Multi-domain]  Cd Length: 81  Bit Score: 76.16  E-value: 6.84e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79315726 793 LTVKATYREDTVRFKLDPYVVGCSQLYREVAKRFKLQEGAFQLKYLDDEEEWVMLVTDSDLHECFEILNGMRKHTVKFLV 872
Cdd:cd05992   1 VRVKVKYGGEIRRFVVVSRSISFEDLRSKIAEKFGLDAVSFKLKYPDEDGDLVTISSDEDLEEAIEEARRSGSKKLRLFV 80


                .
gi 79315726 873 R 873
Cdd:cd05992  81 F 81
PB1_p62 cd06402
The PB1 domain is an essential part of p62 scaffold protein (alias sequestosome 1,SQSTM) ...
 793-862 1.75e-03

The PB1 domain is an essential part of p62 scaffold protein (alias sequestosome 1,SQSTM) involved in cell signaling, receptor internalization, and protein turnover. The PB1 domain is a modular domain mediating specific protein-protein interaction which play roles in many critical cell processes. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domains, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants.


Pssm-ID: 99723  Cd Length: 87  Bit Score: 38.08  E-value: 1.75e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 79315726 793 LTVKA-----TYREDTVRFKLDPYVVG-CSQLYREVAKRF-KLQEGAFQLKYLDDEEEWVMLVTDSDLHECFEILNG 862
Cdd:cd06402   1 LTVKAyllgkDANAEIRRFAIDEDVSTsYEYLVEKVAAVFpSLRGKNFQLFWKDEEGDLVAFSSDEELVMALGSLND 77
PB1_MUG70 cd06409
The MUG70 protein is a product of the meiotically up-regulated gene 70 which has a role in ...
 829-859 8.13e-03

The MUG70 protein is a product of the meiotically up-regulated gene 70 which has a role in meiosis and harbors a PB1 domain. The PB1 domain is a modular domain mediating specific protein-protein interactions which play a role in many critical cell processes such as osteoclastogenesis, angiogenesis, early cardiovascular development, and cell polarity. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domains, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domains depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic amino acid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants.


Pssm-ID: 99730  Cd Length: 86  Bit Score: 36.52  E-value: 8.13e-03
                        10        20        30
                ....*....|....*....|....*....|.
gi 79315726 829 QEGAFQLKYLDDEEEWVMLVTDSDLHECFEI 859
Cdd:cd06409  40 ETHLYALSYVDDEGDIVLITSDSDLVAAVLV 70
 
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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