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Conserved domains on  [gi|966963308|ref|XP_015003009|]
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nuclear receptor-binding factor 2 isoform X2 [Macaca mulatta]

Protein Classification

NRBF2_MIT and NRBF2 domain-containing protein( domain architecture ID 11977866)

NRBF2_MIT and NRBF2 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NRBF2 pfam08961
Nuclear receptor-binding factor 2, autophagy regulator; NRBF2 plays an essential role in ...
72-267 2.82e-121

Nuclear receptor-binding factor 2, autophagy regulator; NRBF2 plays an essential role in autophagy, the cellular pathway that degrades long-lived proteins and other cytoplasmic contents through lysosomes. NRBF2 binds Atg14L - a Beclin-binding protein - directly via the MIT domain and enhances Atg14L-linked Vps34 kinase (a class III phosphatidylinositol-3 kinase) activity and autophagy induction.


:

Pssm-ID: 430345  Cd Length: 200  Bit Score: 344.60  E-value: 2.82e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966963308   72 NTDKDVAAHLQASHKPSAEDAEGQS---PLSQKYSPSTEKCLPEIQGIFDRDPDTLLYLLQQKSEPAEPCIGSKAPKDDK 148
Cdd:pfam08961   1 VTDRDAAAHLQASPKPSAEEADGQSvlgPASQKYSPSPEKYLQEIQSVFDRDPDTLLFLLQKRKEPTETCIGSKAPKDDK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966963308  149 TIIEEQATKIADLKRHVEFLVAENERLRKENKQLKAEKARLLKGPIEKELDVDADFVETSELWSLPPHSET-ATASSTWQ 227
Cdd:pfam08961  81 TKIEEQATKIAELKRHVEFLLAENERLRKENKQLKAEKARLQKNPIEKELDVDADFVEKSELWGLQQHSESaATAASTWQ 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 966963308  228 KFAANTGKAKDIPIPNLPPLDFPSPELPLMELSEDILKGF 267
Cdd:pfam08961 161 KFTANAGKAKDIPIPNLPPLDIPSPELPLLELSEDILKGL 200
NRBF2_MIT super family cl28842
MIT domain of nuclear receptor-binding factor 2; This MIT domain is the microtubule ...
22-69 2.71e-24

MIT domain of nuclear receptor-binding factor 2; This MIT domain is the microtubule interaction and trafficking of nuclear receptor-binding factor 2 - NRBF2 - in higher eukaryotes. It is a coiled-coil region at the N-terminus of pfam08961. NRBF2 plays an essential role in autophagy, the cellular pathway that degrades long-lived proteins and other cytoplasmic contents through lysosomes. NRBF2 binds Atg14L - a Beclin-binding protein - directly via the MIT domain and enhances Atg14L-linked Vps34 kinase (a class III phosphatidylinositol-3 kinase) activity and autophagy induction.


The actual alignment was detected with superfamily member pfam17169:

Pssm-ID: 465368  Cd Length: 83  Bit Score: 93.23  E-value: 2.71e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 966963308   22 AYLSEAMKLTQSEQAHLSLELQRDSHMKQLLLIQERWKRAQREERLKA 69
Cdd:pfam17169  36 AYLSEAMKLTKSEQAHLSLELQRDSHMKQLLLIQERWKRAKREERLKA 83
 
Name Accession Description Interval E-value
NRBF2 pfam08961
Nuclear receptor-binding factor 2, autophagy regulator; NRBF2 plays an essential role in ...
72-267 2.82e-121

Nuclear receptor-binding factor 2, autophagy regulator; NRBF2 plays an essential role in autophagy, the cellular pathway that degrades long-lived proteins and other cytoplasmic contents through lysosomes. NRBF2 binds Atg14L - a Beclin-binding protein - directly via the MIT domain and enhances Atg14L-linked Vps34 kinase (a class III phosphatidylinositol-3 kinase) activity and autophagy induction.


Pssm-ID: 430345  Cd Length: 200  Bit Score: 344.60  E-value: 2.82e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966963308   72 NTDKDVAAHLQASHKPSAEDAEGQS---PLSQKYSPSTEKCLPEIQGIFDRDPDTLLYLLQQKSEPAEPCIGSKAPKDDK 148
Cdd:pfam08961   1 VTDRDAAAHLQASPKPSAEEADGQSvlgPASQKYSPSPEKYLQEIQSVFDRDPDTLLFLLQKRKEPTETCIGSKAPKDDK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966963308  149 TIIEEQATKIADLKRHVEFLVAENERLRKENKQLKAEKARLLKGPIEKELDVDADFVETSELWSLPPHSET-ATASSTWQ 227
Cdd:pfam08961  81 TKIEEQATKIAELKRHVEFLLAENERLRKENKQLKAEKARLQKNPIEKELDVDADFVEKSELWGLQQHSESaATAASTWQ 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 966963308  228 KFAANTGKAKDIPIPNLPPLDFPSPELPLMELSEDILKGF 267
Cdd:pfam08961 161 KFTANAGKAKDIPIPNLPPLDIPSPELPLLELSEDILKGL 200
NRBF2_MIT pfam17169
MIT domain of nuclear receptor-binding factor 2; This MIT domain is the microtubule ...
22-69 2.71e-24

MIT domain of nuclear receptor-binding factor 2; This MIT domain is the microtubule interaction and trafficking of nuclear receptor-binding factor 2 - NRBF2 - in higher eukaryotes. It is a coiled-coil region at the N-terminus of pfam08961. NRBF2 plays an essential role in autophagy, the cellular pathway that degrades long-lived proteins and other cytoplasmic contents through lysosomes. NRBF2 binds Atg14L - a Beclin-binding protein - directly via the MIT domain and enhances Atg14L-linked Vps34 kinase (a class III phosphatidylinositol-3 kinase) activity and autophagy induction.


Pssm-ID: 465368  Cd Length: 83  Bit Score: 93.23  E-value: 2.71e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 966963308   22 AYLSEAMKLTQSEQAHLSLELQRDSHMKQLLLIQERWKRAQREERLKA 69
Cdd:pfam17169  36 AYLSEAMKLTKSEQAHLSLELQRDSHMKQLLLIQERWKRAKREERLKA 83
FtsB COG2919
Cell division protein FtsB [Cell cycle control, cell division, chromosome partitioning];
157-196 1.30e-03

Cell division protein FtsB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442163 [Multi-domain]  Cd Length: 96  Bit Score: 37.17  E-value: 1.30e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 966963308 157 KIADLKRHVEFLVAENERLRKENKQLKAEKARLLKGP--IEK 196
Cdd:COG2919   30 AYRELRQEIAELEAENAKLKARNAELEAEVADLKDGPdyIEE 71
 
Name Accession Description Interval E-value
NRBF2 pfam08961
Nuclear receptor-binding factor 2, autophagy regulator; NRBF2 plays an essential role in ...
72-267 2.82e-121

Nuclear receptor-binding factor 2, autophagy regulator; NRBF2 plays an essential role in autophagy, the cellular pathway that degrades long-lived proteins and other cytoplasmic contents through lysosomes. NRBF2 binds Atg14L - a Beclin-binding protein - directly via the MIT domain and enhances Atg14L-linked Vps34 kinase (a class III phosphatidylinositol-3 kinase) activity and autophagy induction.


Pssm-ID: 430345  Cd Length: 200  Bit Score: 344.60  E-value: 2.82e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966963308   72 NTDKDVAAHLQASHKPSAEDAEGQS---PLSQKYSPSTEKCLPEIQGIFDRDPDTLLYLLQQKSEPAEPCIGSKAPKDDK 148
Cdd:pfam08961   1 VTDRDAAAHLQASPKPSAEEADGQSvlgPASQKYSPSPEKYLQEIQSVFDRDPDTLLFLLQKRKEPTETCIGSKAPKDDK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966963308  149 TIIEEQATKIADLKRHVEFLVAENERLRKENKQLKAEKARLLKGPIEKELDVDADFVETSELWSLPPHSET-ATASSTWQ 227
Cdd:pfam08961  81 TKIEEQATKIAELKRHVEFLLAENERLRKENKQLKAEKARLQKNPIEKELDVDADFVEKSELWGLQQHSESaATAASTWQ 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 966963308  228 KFAANTGKAKDIPIPNLPPLDFPSPELPLMELSEDILKGF 267
Cdd:pfam08961 161 KFTANAGKAKDIPIPNLPPLDIPSPELPLLELSEDILKGL 200
NRBF2_MIT pfam17169
MIT domain of nuclear receptor-binding factor 2; This MIT domain is the microtubule ...
22-69 2.71e-24

MIT domain of nuclear receptor-binding factor 2; This MIT domain is the microtubule interaction and trafficking of nuclear receptor-binding factor 2 - NRBF2 - in higher eukaryotes. It is a coiled-coil region at the N-terminus of pfam08961. NRBF2 plays an essential role in autophagy, the cellular pathway that degrades long-lived proteins and other cytoplasmic contents through lysosomes. NRBF2 binds Atg14L - a Beclin-binding protein - directly via the MIT domain and enhances Atg14L-linked Vps34 kinase (a class III phosphatidylinositol-3 kinase) activity and autophagy induction.


Pssm-ID: 465368  Cd Length: 83  Bit Score: 93.23  E-value: 2.71e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 966963308   22 AYLSEAMKLTQSEQAHLSLELQRDSHMKQLLLIQERWKRAQREERLKA 69
Cdd:pfam17169  36 AYLSEAMKLTKSEQAHLSLELQRDSHMKQLLLIQERWKRAKREERLKA 83
FtsB COG2919
Cell division protein FtsB [Cell cycle control, cell division, chromosome partitioning];
157-196 1.30e-03

Cell division protein FtsB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442163 [Multi-domain]  Cd Length: 96  Bit Score: 37.17  E-value: 1.30e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 966963308 157 KIADLKRHVEFLVAENERLRKENKQLKAEKARLLKGP--IEK 196
Cdd:COG2919   30 AYRELRQEIAELEAENAKLKARNAELEAEVADLKDGPdyIEE 71
 
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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