DRSC/TRiP Functional Genomics Resources

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Protein Alignment CG5397 and Aadac

DIOPT Version :10

Sequence 1:NP_608591.1 Gene:CG5397 / 33313 FlyBaseID:FBgn0031327 Length:665 Species:Drosophila melanogaster
Sequence 2:NP_075872.1 Gene:Aadac / 67758 MGIID:1915008 Length:398 Species:Mus musculus


Alignment Length:342 Identity:66/342 - (19%)
Similarity:107/342 - (31%) Gaps:125/342 - (36%)


- Green bases have known domain annotations that are detailed below.


  Fly   110 PPCIQPHPQFPQRIIGDEDCLLLNVYTPQMPDETTGLPVFVWIHPGGYRYGSAAQYDATPMA--- 171
            ||....|....:...   |.:.:.:|.|:.........:| :||.||:..||||.:....::   
Mouse    71 PPTSDEHVTVMETAF---DSVPVRIYIPKRKSMALRRGLF-YIHGGGWCLGSAAHFSYDTLSRWT 131

  Fly   172 --QRGAIVVAPQYRLGSLGIMGDGTKQFDGNLAMFDLAAALRWV--TDYISYFGGNPKQVQAIGH 232
              :..|:||:..|   .|.......:||:      |:..:|||.  .|.:..:|.:|::|...|.
Mouse   132 AHKLDAVVVSTDY---GLAPKHHFPRQFE------DVYRSLRWFLQEDVLEKYGVDPRRVGVSGD 187

  Fly   233 GSG----AASAMYLSMSP-----------------------TSRSAGDVHGV------------- 257
            .:|    ||....|...|                       .|:..|....|             
Mouse   188 SAGGNLAAAVTQQLIQDPDVKIKLKVQALIYPALQALDTNVPSQQEGSHFPVLTRSLMVRFWSEY 252

  Fly   258 ----------------VAMSGTALSQYA--------------MDKEPVQSVQEVAK-------IN 285
                            |.|..:.|.|:.              :.|.|.....|:|:       :.
Mouse   253 FTTDRGLEKAMLLNQHVPMESSHLLQFVNWSSLLPERYKKSPVYKNPTPGSSELAQKYPGFIDVK 317

  Fly   286 GCP---TGNELE------IVNCLRSKSAEDIIKNDDKVQTERLAGRALVKGLTGNVGF---QPHI 338
            .||   ..|.|.      |:.|     ..|::::|..:..:||.          |||.   ..|:
Mouse   318 ACPLLANDNILHHLPKTYIITC-----QYDVLRDDGLMYVKRLQ----------NVGVHVTHHHV 367

  Fly   339 ESEDDGR-ALPSLIVGE 354
            |....|. :.|.|.:.|
Mouse   368 EDGFHGTFSFPGLKLSE 384

Known Domains:


Indicated by green bases in alignment.

GeneSequenceDomainRegion External IDIdentity
CG5397NP_608591.1 COesterase 48..599 CDD:395084 66/342 (19%)
AadacNP_075872.1 Abhydrolase_3 106..356 CDD:400284 50/264 (19%)
Involved in the stabilization of the negatively charged intermediate by the formation of the oxyanion hole. /evidence=ECO:0000250|UniProtKB:Q5NUF3 110..112 1/1 (100%)

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