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Conserved domains on  [gi|334187181|ref|NP_195253|]
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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 ...
 864-944 1.31e-41

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: 146.70  E-value: 1.31e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187181 864 KVKATFGEAKVRFTLLPTWGFRELQHEIARRFNIDNIAPFDLKYLDDDKEWVLLTCEADLEECIDIYRSSQSRTIKISVH 943
Cdd:cd06407    2 RVKATYGEEKIRFRLPPSWGFTELKQEIAKRFKLDDMSAFDLKYLDDDEEWVLLTCDADLEECIDVYRSSGSHTIRLLVH 81


                 .
gi 334187181 944 E 944
Cdd:cd06407   82 A 82
RWP-RK pfam02042
RWP-RK domain; This domain is named RWP-RK after a conserved motif at the C terminus of the ...
 648-696 3.54e-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: 92.95  E-value: 3.54e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 334187181  648 TIGLEVLRQYFAGSLKDAAKSIGVCPTTLKRICRQHGITRWPSRKIKKV 696
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 ...
 864-944 1.31e-41

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: 146.70  E-value: 1.31e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187181 864 KVKATFGEAKVRFTLLPTWGFRELQHEIARRFNIDNIAPFDLKYLDDDKEWVLLTCEADLEECIDIYRSSQSRTIKISVH 943
Cdd:cd06407    2 RVKATYGEEKIRFRLPPSWGFTELKQEIAKRFKLDDMSAFDLKYLDDDEEWVLLTCDADLEECIDVYRSSGSHTIRLLVH 81


                 .
gi 334187181 944 E 944
Cdd:cd06407   82 A 82
RWP-RK pfam02042
RWP-RK domain; This domain is named RWP-RK after a conserved motif at the C terminus of the ...
 648-696 3.54e-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: 92.95  E-value: 3.54e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 334187181  648 TIGLEVLRQYFAGSLKDAAKSIGVCPTTLKRICRQHGITRWPSRKIKKV 696
Cdd:pfam02042   1 SITLEDLSQYFHLPIKEAAKELGVSLTTLKRICRRLGIPRWPHRKLKSL 49
PB1 smart00666
PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. ...
 864-943 5.82e-23

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: 93.42  E-value: 5.82e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187181   864 KVKATFGEAKVRFTLLPTWGFRELQHEIARRFNIDNiAPFDLKYLDDDKEWVLLTCEADLEECIDIYRSSQSRTIKISVH 943
Cdd:smart00666   3 DVKLRYGGETRRLSVPRDISFEDLRSKVAKRFGLDN-QSFTLKYQDEDGDLVSLTSDEDLEEAIEEYDSLGSKKLRLHVF 81
PB1 pfam00564
PB1 domain;
864-945 2.66e-20

PB1 domain;


Pssm-ID: 395447  Cd Length: 84  Bit Score: 86.19  E-value: 2.66e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187181  864 KVKATFGEAKVRFT-LLPTWGFRELQHEIARRFNIDNiAPFDLKYLDDDKEWVLLTCEADLEECIDIYRSSQSRTIKISV 942
Cdd:pfam00564   3 RLKLRYGGGIRRFLsVSRGISFEELRALVEQRFGLDD-VDFKLKYPDEDGDLVSLTSDEDLEEALEEARSLGSKSLRLHV 81


                  ...
gi 334187181  943 HEA 945
Cdd:pfam00564  82 FPT 84
 
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 ...
 864-944 1.31e-41

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: 146.70  E-value: 1.31e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187181 864 KVKATFGEAKVRFTLLPTWGFRELQHEIARRFNIDNIAPFDLKYLDDDKEWVLLTCEADLEECIDIYRSSQSRTIKISVH 943
Cdd:cd06407    2 RVKATYGEEKIRFRLPPSWGFTELKQEIAKRFKLDDMSAFDLKYLDDDEEWVLLTCDADLEECIDVYRSSGSHTIRLLVH 81


                 .
gi 334187181 944 E 944
Cdd:cd06407   82 A 82
RWP-RK pfam02042
RWP-RK domain; This domain is named RWP-RK after a conserved motif at the C terminus of the ...
 648-696 3.54e-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: 92.95  E-value: 3.54e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 334187181  648 TIGLEVLRQYFAGSLKDAAKSIGVCPTTLKRICRQHGITRWPSRKIKKV 696
Cdd:pfam02042   1 SITLEDLSQYFHLPIKEAAKELGVSLTTLKRICRRLGIPRWPHRKLKSL 49
PB1 smart00666
PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. ...
 864-943 5.82e-23

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: 93.42  E-value: 5.82e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187181   864 KVKATFGEAKVRFTLLPTWGFRELQHEIARRFNIDNiAPFDLKYLDDDKEWVLLTCEADLEECIDIYRSSQSRTIKISVH 943
Cdd:smart00666   3 DVKLRYGGETRRLSVPRDISFEDLRSKVAKRFGLDN-QSFTLKYQDEDGDLVSLTSDEDLEEAIEEYDSLGSKKLRLHVF 81
PB1 pfam00564
PB1 domain;
864-945 2.66e-20

PB1 domain;


Pssm-ID: 395447  Cd Length: 84  Bit Score: 86.19  E-value: 2.66e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187181  864 KVKATFGEAKVRFT-LLPTWGFRELQHEIARRFNIDNiAPFDLKYLDDDKEWVLLTCEADLEECIDIYRSSQSRTIKISV 942
Cdd:pfam00564   3 RLKLRYGGGIRRFLsVSRGISFEELRALVEQRFGLDD-VDFKLKYPDEDGDLVSLTSDEDLEEALEEARSLGSKSLRLHV 81


                  ...
gi 334187181  943 HEA 945
Cdd:pfam00564  82 FPT 84
PB1 cd05992
The PB1 domain is a modular domain mediating specific protein-protein interactions which play ...
 864-943 5.20e-19

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: 82.33  E-value: 5.20e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187181 864 KVKATFGEAKVRFTL-LPTWGFRELQHEIARRFNIDNIaPFDLKYLDDDKEWVLLTCEADLEECIDIYRSSQSRTIKISV 942
Cdd:cd05992    2 RVKVKYGGEIRRFVVvSRSISFEDLRSKIAEKFGLDAV-SFKLKYPDEDGDLVTISSDEDLEEAIEEARRSGSKKLRLFV 80


                 .
gi 334187181 943 H 943
Cdd:cd05992   81 F 81
PB1_Joka2 cd06398
The PB1 domain is present in the Nicotiana plumbaginifolia Joka2 protein which interacts with ...
 865-942 6.25e-06

The PB1 domain is present in the Nicotiana plumbaginifolia Joka2 protein which interacts with sulfur stress inducible UP9 protein. 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 noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants.


Pssm-ID: 99720  Cd Length: 91  Bit Score: 45.48  E-value: 6.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187181 865 VKATFGEAKVRFTL-----LPTWGFRELQHEIARRFNIDNIAPFDLKYLDDDKEWVLLTCEADLEECIdIYRSSQSR--T 937
Cdd:cd06398    3 VKVKYGGTLRRFTFpvaenQLDLNMDGLREKVEELFSLSPDADLSLTYTDEDGDVVTLVDDNDLTDAI-QYFCSGSRlnP 81


                 ....*
gi 334187181 938 IKISV 942
Cdd:cd06398   82 LRIDV 86
PB1_MUG70 cd06409
The MUG70 protein is a product of the meiotically up-regulated gene 70 which has a role in ...
 875-945 2.02e-05

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: 43.84  E-value: 2.02e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334187181 875 RFTLLPTWGFRELQHEIARRFNIDNIAP--FDLKYLDDDKEWVLLTCEADLEECIDIYRSSQSRTIKISVHEA 945
Cdd:cd06409   14 RFRLRPSESLEELRTLISQRLGDDDFEThlYALSYVDDEGDIVLITSDSDLVAAVLVARSAGLKKLDLHLHYP 86
 
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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