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Conserved domains on  [gi|1585761565|ref|XP_028106015|]
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protein NLP6-like isoform X3 [Camellia sinensis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PB1 pfam00564
PB1 domain;
974-1056 6.63e-17

PB1 domain;


:

Pssm-ID: 395447  Cd Length: 84  Bit Score: 76.56  E-value: 6.63e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585761565  974 VTIKAKYGNDIVIKFPLSSSSGLVELWQEVARRLNLDPETYHIKYKDEDGDLILIACDDDLLGFITSSRTLGNTTILLLL 1053
Cdd:pfam00564    2 VRLKLRYGGGIRRFLSVSRGISFEELRALVEQRFGLDDVDFKLKYPDEDGDLVSLTSDEDLEEALEEARSLGSKSLRLHV 81


                   ...
gi 1585761565 1054 EPR 1056
Cdd:pfam00564   82 FPT 84
RWP-RK pfam02042
RWP-RK domain; This domain is named RWP-RK after a conserved motif at the C terminus of the ...
 528-573 1.93e-12

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: 62.52  E-value: 1.93e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1585761565  528 LEDILQTSQMTIEDAAKSLHVSISTLKRACRKFGIPRWSRHHINQL 573
Cdd:pfam02042    4 LEDLSQYFHLPIKEAAKELGVSLTTLKRICRRLGIPRWPHRKLKSL 49
RWP-RK pfam02042
RWP-RK domain; This domain is named RWP-RK after a conserved motif at the C terminus of the ...
 666-703 4.83e-12

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: 61.37  E-value: 4.83e-12
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1585761565  666 EMSLNDAANSLHVSISTLKRACRKLGISRWPPRHINKI 703
Cdd:pfam02042   12 HLPIKEAAKELGVSLTTLKRICRRLGIPRWPHRKLKSL 49
RWP-RK super family cl03415
RWP-RK domain; This domain is named RWP-RK after a conserved motif at the C terminus of the ...
 887-924 1.89e-08

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.


The actual alignment was detected with superfamily member pfam02042:

Pssm-ID: 460427  Cd Length: 49  Bit Score: 51.35  E-value: 1.89e-08
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1585761565  887 EDLLQASEMSLNDAACRLNVSKSALKRVCRGYGIEKWP 924
Cdd:pfam02042    5 EDLSQYFHLPIKEAAKELGVSLTTLKRICRRLGIPRWP 42
 
Name Accession Description Interval E-value
PB1 pfam00564
PB1 domain;
974-1056 6.63e-17

PB1 domain;


Pssm-ID: 395447  Cd Length: 84  Bit Score: 76.56  E-value: 6.63e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585761565  974 VTIKAKYGNDIVIKFPLSSSSGLVELWQEVARRLNLDPETYHIKYKDEDGDLILIACDDDLLGFITSSRTLGNTTILLLL 1053
Cdd:pfam00564    2 VRLKLRYGGGIRRFLSVSRGISFEELRALVEQRFGLDDVDFKLKYPDEDGDLVSLTSDEDLEEALEEARSLGSKSLRLHV 81


                   ...
gi 1585761565 1054 EPR 1056
Cdd:pfam00564   82 FPT 84
PB1 smart00666
PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. ...
 974-1054 1.99e-16

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: 74.93  E-value: 1.99e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585761565   974 VTIKAKYGNDIVIkFPLSSSSGLVELWQEVARRLNLDPETYHIKYKDEDGDLILIACDDDLLGFITSSRTLGNTTILLLL 1053
Cdd:smart00666    2 VDVKLRYGGETRR-LSVPRDISFEDLRSKVAKRFGLDNQSFTLKYQDEDGDLVSLTSDEDLEEAIEEYDSLGSKKLRLHV 80


                    .
gi 1585761565  1054 E 1054
Cdd:smart00666   81 F 81
PB1_NLP cd06407
A PB1 domain is present in NIN like proteins (NLP), a key enzyme in a process of establishment ...
 974-1055 7.55e-15

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: 70.43  E-value: 7.55e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585761565  974 VTIKAKYGNDIvIKFPLSSSSGLVELWQEVARRLNLDPET-YHIKYKDEDGDLILIACDDDLLGFITSSRTLGNTTILLL 1052
Cdd:cd06407      1 VRVKATYGEEK-IRFRLPPSWGFTELKQEIAKRFKLDDMSaFDLKYLDDDEEWVLLTCDADLEECIDVYRSSGSHTIRLL 79


                   ...
gi 1585761565 1053 LEP 1055
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 ...
 528-573 1.93e-12

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: 62.52  E-value: 1.93e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1585761565  528 LEDILQTSQMTIEDAAKSLHVSISTLKRACRKFGIPRWSRHHINQL 573
Cdd:pfam02042    4 LEDLSQYFHLPIKEAAKELGVSLTTLKRICRRLGIPRWPHRKLKSL 49
RWP-RK pfam02042
RWP-RK domain; This domain is named RWP-RK after a conserved motif at the C terminus of the ...
 666-703 4.83e-12

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: 61.37  E-value: 4.83e-12
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1585761565  666 EMSLNDAANSLHVSISTLKRACRKLGISRWPPRHINKI 703
Cdd:pfam02042   12 HLPIKEAAKELGVSLTTLKRICRRLGIPRWPHRKLKSL 49
RWP-RK pfam02042
RWP-RK domain; This domain is named RWP-RK after a conserved motif at the C terminus of the ...
 887-924 1.89e-08

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: 51.35  E-value: 1.89e-08
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1585761565  887 EDLLQASEMSLNDAACRLNVSKSALKRVCRGYGIEKWP 924
Cdd:pfam02042    5 EDLSQYFHLPIKEAAKELGVSLTTLKRICRRLGIPRWP 42
 
Name Accession Description Interval E-value
PB1 pfam00564
PB1 domain;
974-1056 6.63e-17

PB1 domain;


Pssm-ID: 395447  Cd Length: 84  Bit Score: 76.56  E-value: 6.63e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585761565  974 VTIKAKYGNDIVIKFPLSSSSGLVELWQEVARRLNLDPETYHIKYKDEDGDLILIACDDDLLGFITSSRTLGNTTILLLL 1053
Cdd:pfam00564    2 VRLKLRYGGGIRRFLSVSRGISFEELRALVEQRFGLDDVDFKLKYPDEDGDLVSLTSDEDLEEALEEARSLGSKSLRLHV 81


                   ...
gi 1585761565 1054 EPR 1056
Cdd:pfam00564   82 FPT 84
PB1 smart00666
PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. ...
 974-1054 1.99e-16

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: 74.93  E-value: 1.99e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585761565   974 VTIKAKYGNDIVIkFPLSSSSGLVELWQEVARRLNLDPETYHIKYKDEDGDLILIACDDDLLGFITSSRTLGNTTILLLL 1053
Cdd:smart00666    2 VDVKLRYGGETRR-LSVPRDISFEDLRSKVAKRFGLDNQSFTLKYQDEDGDLVSLTSDEDLEEAIEEYDSLGSKKLRLHV 80


                    .
gi 1585761565  1054 E 1054
Cdd:smart00666   81 F 81
PB1_NLP cd06407
A PB1 domain is present in NIN like proteins (NLP), a key enzyme in a process of establishment ...
 974-1055 7.55e-15

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: 70.43  E-value: 7.55e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585761565  974 VTIKAKYGNDIvIKFPLSSSSGLVELWQEVARRLNLDPET-YHIKYKDEDGDLILIACDDDLLGFITSSRTLGNTTILLL 1052
Cdd:cd06407      1 VRVKATYGEEK-IRFRLPPSWGFTELKQEIAKRFKLDDMSaFDLKYLDDDEEWVLLTCDADLEECIDVYRSSGSHTIRLL 79


                   ...
gi 1585761565 1053 LEP 1055
Cdd:cd06407     80 VHA 82
PB1 cd05992
The PB1 domain is a modular domain mediating specific protein-protein interactions which play ...
 974-1053 8.75e-13

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: 64.61  E-value: 8.75e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585761565  974 VTIKAKYGNDIV-IKFPLSSSSgLVELWQEVARRLNLDPETYHIKYKDEDGDLILIACDDDLLGFITSSRTLGNTTILLL 1052
Cdd:cd05992      1 VRVKVKYGGEIRrFVVVSRSIS-FEDLRSKIAEKFGLDAVSFKLKYPDEDGDLVTISSDEDLEEAIEEARRSGSKKLRLF 79


                   .
gi 1585761565 1053 L 1053
Cdd:cd05992     80 V 80
RWP-RK pfam02042
RWP-RK domain; This domain is named RWP-RK after a conserved motif at the C terminus of the ...
 528-573 1.93e-12

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: 62.52  E-value: 1.93e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1585761565  528 LEDILQTSQMTIEDAAKSLHVSISTLKRACRKFGIPRWSRHHINQL 573
Cdd:pfam02042    4 LEDLSQYFHLPIKEAAKELGVSLTTLKRICRRLGIPRWPHRKLKSL 49
RWP-RK pfam02042
RWP-RK domain; This domain is named RWP-RK after a conserved motif at the C terminus of the ...
 666-703 4.83e-12

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: 61.37  E-value: 4.83e-12
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1585761565  666 EMSLNDAANSLHVSISTLKRACRKLGISRWPPRHINKI 703
Cdd:pfam02042   12 HLPIKEAAKELGVSLTTLKRICRRLGIPRWPHRKLKSL 49
RWP-RK pfam02042
RWP-RK domain; This domain is named RWP-RK after a conserved motif at the C terminus of the ...
 887-924 1.89e-08

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: 51.35  E-value: 1.89e-08
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1585761565  887 EDLLQASEMSLNDAACRLNVSKSALKRVCRGYGIEKWP 924
Cdd:pfam02042    5 EDLSQYFHLPIKEAAKELGVSLTTLKRICRRLGIPRWP 42
PB1_MUG70 cd06409
The MUG70 protein is a product of the meiotically up-regulated gene 70 which has a role in ...
 987-1054 3.93e-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: 48.85  E-value: 3.93e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1585761565  987 KFPLSSSSGLVELWQEVARRLNLDPE---TYHIKYKDEDGDLILIACDDDLLGFITSSRTLGNTTILLLLE 1054
Cdd:cd06409     14 RFRLRPSESLEELRTLISQRLGDDDFethLYALSYVDDEGDIVLITSDSDLVAAVLVARSAGLKKLDLHLH 84
 
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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