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Conserved domains on  [gi|665393356|ref|NP_001287197|]
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uncharacterized protein Dmel_CG15186, isoform L [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG2433 super family cl43687
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
2-82 2.33e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


The actual alignment was detected with superfamily member COG2433:

Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 41.77  E-value: 2.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393356   2 LRERRRHAHyKLNSRLDRKSSRgmiyENEELRLRtininAEVERGQSDIKRLRRENEQLRREIWTLRDECDRLnKRFKAK 81
Cdd:COG2433  436 LEEKDERIE-RLERELSEARSE----ERREIRKD-----REISRLDREIERLERELEEERERIEELKRKLERL-KELWKL 504


                 .
gi 665393356  82 L 82
Cdd:COG2433  505 E 505
 
Name Accession Description Interval E-value
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
2-82 2.33e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 41.77  E-value: 2.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393356   2 LRERRRHAHyKLNSRLDRKSSRgmiyENEELRLRtininAEVERGQSDIKRLRRENEQLRREIWTLRDECDRLnKRFKAK 81
Cdd:COG2433  436 LEEKDERIE-RLERELSEARSE----ERREIRKD-----REISRLDREIERLERELEEERERIEELKRKLERL-KELWKL 504


                 .
gi 665393356  82 L 82
Cdd:COG2433  505 E 505
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 28-62 8.29e-03

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 39.43  E-value: 8.29e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 665393356  28 ENEELRLRTININAEVERGQSDIKRLRRENEQLRR 62
Cdd:PRK03992  16 QIRQLELKLRDLEAENEKLERELERLKSELEKLKS 50
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
 28-80 8.36e-03

Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.


Pssm-ID: 463295 [Multi-domain]  Cd Length: 151  Bit Score: 38.07  E-value: 8.36e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 665393356   28 ENEELRLRTI-NINAEVERGQSDIKRLRRENEQLRREIWTLRDECDRLNKRFKA 80
Cdd:pfam11559  52 EFRESLNETIrTLEAEIERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKT 105
 
Name Accession Description Interval E-value
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
2-82 2.33e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 41.77  E-value: 2.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393356   2 LRERRRHAHyKLNSRLDRKSSRgmiyENEELRLRtininAEVERGQSDIKRLRRENEQLRREIWTLRDECDRLnKRFKAK 81
Cdd:COG2433  436 LEEKDERIE-RLERELSEARSE----ERREIRKD-----REISRLDREIERLERELEEERERIEELKRKLERL-KELWKL 504


                 .
gi 665393356  82 L 82
Cdd:COG2433  505 E 505
ZapB COG3074
Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome ...
 28-68 2.43e-03

Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442308 [Multi-domain]  Cd Length: 79  Bit Score: 37.64  E-value: 2.43e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 665393356  28 ENEELRLRTININAEVERGQSDIKRLRRENEQLRREI--WTLR 68
Cdd:COG3074   26 EVEELKEKNEELEQENEELQSENEELQSENEQLKTENaeWQER 68
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 28-62 8.29e-03

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 39.43  E-value: 8.29e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 665393356  28 ENEELRLRTININAEVERGQSDIKRLRRENEQLRR 62
Cdd:PRK03992  16 QIRQLELKLRDLEAENEKLERELERLKSELEKLKS 50
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
 28-80 8.36e-03

Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.


Pssm-ID: 463295 [Multi-domain]  Cd Length: 151  Bit Score: 38.07  E-value: 8.36e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 665393356   28 ENEELRLRTI-NINAEVERGQSDIKRLRRENEQLRREIWTLRDECDRLNKRFKA 80
Cdd:pfam11559  52 EFRESLNETIrTLEAEIERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKT 105
 
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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