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Conserved domains on  [gi|1350326819|ref|XP_024035066|]
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protein NLP2 [Citrus x clementina]

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 ...
 848-928 3.22e-46

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: 159.80  E-value: 3.22e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1350326819 848 FRVKASFGEEKIRFSLQPNWGFKDLQQEIARRFNIEDFNEIDLKYLDDDHEWVLLTCDADLEECIDIYKSSQSHTIKISL 927
Cdd:cd06407     1 VRVKATYGEEKIRFRLPPSWGFTELKQEIAKRFKLDDMSAFDLKYLDDDEEWVLLTCDADLEECIDVYRSSGSHTIRLLV 80


                  .
gi 1350326819 928 H 928
Cdd:cd06407    81 H 81
RWP-RK pfam02042
RWP-RK domain; This domain is named RWP-RK after a conserved motif at the C terminus of the ...
 627-675 2.72e-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: 93.34  E-value: 2.72e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1350326819 627 TISLQVLRQYFAGSLKDAAKSIGVCPTTLKRICRQHGITRWPSRKIKKV 675
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 ...
 848-928 3.22e-46

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: 159.80  E-value: 3.22e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1350326819 848 FRVKASFGEEKIRFSLQPNWGFKDLQQEIARRFNIEDFNEIDLKYLDDDHEWVLLTCDADLEECIDIYKSSQSHTIKISL 927
Cdd:cd06407     1 VRVKATYGEEKIRFRLPPSWGFTELKQEIAKRFKLDDMSAFDLKYLDDDEEWVLLTCDADLEECIDVYRSSGSHTIRLLV 80


                  .
gi 1350326819 928 H 928
Cdd:cd06407    81 H 81
PB1 smart00666
PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. ...
 847-928 7.58e-27

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: 104.59  E-value: 7.58e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1350326819  847 TFRVKASFGEEKIRFSLQPNWGFKDLQQEIARRFNIEDFNeIDLKYLDDDHEWVLLTCDADLEECIDIYKSSQSHTIKIS 926
Cdd:smart00666   1 TVDVKLRYGGETRRLSVPRDISFEDLRSKVAKRFGLDNQS-FTLKYQDEDGDLVSLTSDEDLEEAIEEYDSLGSKKLRLH 79


                   ..
gi 1350326819  927 LH 928
Cdd:smart00666  80 VF 81
RWP-RK pfam02042
RWP-RK domain; This domain is named RWP-RK after a conserved motif at the C terminus of the ...
 627-675 2.72e-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: 93.34  E-value: 2.72e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1350326819 627 TISLQVLRQYFAGSLKDAAKSIGVCPTTLKRICRQHGITRWPSRKIKKV 675
Cdd:pfam02042   1 SITLEDLSQYFHLPIKEAAKELGVSLTTLKRICRRLGIPRWPHRKLKSL 49
PB1 pfam00564
PB1 domain;
847-930 6.73e-22

PB1 domain;


Pssm-ID: 395447  Cd Length: 84  Bit Score: 90.43  E-value: 6.73e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1350326819 847 TFRVKASFGEEKIRF-SLQPNWGFKDLQQEIARRFNIEDFNeIDLKYLDDDHEWVLLTCDADLEECIDIYKSSQSHTIKI 925
Cdd:pfam00564   1 TVRLKLRYGGGIRRFlSVSRGISFEELRALVEQRFGLDDVD-FKLKYPDEDGDLVSLTSDEDLEEALEEARSLGSKSLRL 79


                  ....*
gi 1350326819 926 SLHRA 930
Cdd:pfam00564  80 HVFPT 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 ...
 848-928 3.22e-46

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: 159.80  E-value: 3.22e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1350326819 848 FRVKASFGEEKIRFSLQPNWGFKDLQQEIARRFNIEDFNEIDLKYLDDDHEWVLLTCDADLEECIDIYKSSQSHTIKISL 927
Cdd:cd06407     1 VRVKATYGEEKIRFRLPPSWGFTELKQEIAKRFKLDDMSAFDLKYLDDDEEWVLLTCDADLEECIDVYRSSGSHTIRLLV 80


                  .
gi 1350326819 928 H 928
Cdd:cd06407    81 H 81
PB1 smart00666
PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. ...
 847-928 7.58e-27

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: 104.59  E-value: 7.58e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1350326819  847 TFRVKASFGEEKIRFSLQPNWGFKDLQQEIARRFNIEDFNeIDLKYLDDDHEWVLLTCDADLEECIDIYKSSQSHTIKIS 926
Cdd:smart00666   1 TVDVKLRYGGETRRLSVPRDISFEDLRSKVAKRFGLDNQS-FTLKYQDEDGDLVSLTSDEDLEEAIEEYDSLGSKKLRLH 79


                   ..
gi 1350326819  927 LH 928
Cdd:smart00666  80 VF 81
RWP-RK pfam02042
RWP-RK domain; This domain is named RWP-RK after a conserved motif at the C terminus of the ...
 627-675 2.72e-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: 93.34  E-value: 2.72e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1350326819 627 TISLQVLRQYFAGSLKDAAKSIGVCPTTLKRICRQHGITRWPSRKIKKV 675
Cdd:pfam02042   1 SITLEDLSQYFHLPIKEAAKELGVSLTTLKRICRRLGIPRWPHRKLKSL 49
PB1 pfam00564
PB1 domain;
847-930 6.73e-22

PB1 domain;


Pssm-ID: 395447  Cd Length: 84  Bit Score: 90.43  E-value: 6.73e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1350326819 847 TFRVKASFGEEKIRF-SLQPNWGFKDLQQEIARRFNIEDFNeIDLKYLDDDHEWVLLTCDADLEECIDIYKSSQSHTIKI 925
Cdd:pfam00564   1 TVRLKLRYGGGIRRFlSVSRGISFEELRALVEQRFGLDDVD-FKLKYPDEDGDLVSLTSDEDLEEALEEARSLGSKSLRL 79


                  ....*
gi 1350326819 926 SLHRA 930
Cdd:pfam00564  80 HVFPT 84
PB1 cd05992
The PB1 domain is a modular domain mediating specific protein-protein interactions which play ...
 848-928 8.10e-22

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: 90.03  E-value: 8.10e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1350326819 848 FRVKASFGEEKIRFSLQ-PNWGFKDLQQEIARRFNIEDFNeIDLKYLDDDHEWVLLTCDADLEECIDIYKSSQSHTIKIS 926
Cdd:cd05992     1 VRVKVKYGGEIRRFVVVsRSISFEDLRSKIAEKFGLDAVS-FKLKYPDEDGDLVTISSDEDLEEAIEEARRSGSKKLRLF 79


                  ..
gi 1350326819 927 LH 928
Cdd:cd05992    80 VF 81
PB1_MUG70 cd06409
The MUG70 protein is a product of the meiotically up-regulated gene 70 which has a role in ...
 860-928 1.33e-07

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: 50.01  E-value: 1.33e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1350326819 860 RFSLQPNWGFKDLQQEIARRFNIEDFNEID--LKYLDDDHEWVLLTCDADLEECIDIYKSSQSHTIKISLH 928
Cdd:cd06409    14 RFRLRPSESLEELRTLISQRLGDDDFETHLyaLSYVDDEGDIVLITSDSDLVAAVLVARSAGLKKLDLHLH 84
PB1_Joka2 cd06398
The PB1 domain is present in the Nicotiana plumbaginifolia Joka2 protein which interacts with ...
 850-927 6.18e-03

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: 37.00  E-value: 6.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1350326819 850 VKASFGEEKIRFSL-----QPNWGFKDLQQEIARRFNIEDFNEIDLKYLDDDHEWVLLTCDADLEECIdiyKSSQSHTIK 924
Cdd:cd06398     3 VKVKYGGTLRRFTFpvaenQLDLNMDGLREKVEELFSLSPDADLSLTYTDEDGDVVTLVDDNDLTDAI---QYFCSGSRL 79


                  ...
gi 1350326819 925 ISL 927
Cdd:cd06398    80 NPL 82
 
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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