DRSC/TRiP Functional Genomics Resources

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Protein Alignment CG6414 and AADACL2

DIOPT Version :10

Sequence 1:NP_570089.1 Gene:CG6414 / 31352 FlyBaseID:FBgn0029690 Length:583 Species:Drosophila melanogaster
Sequence 2:NP_997248.2 Gene:AADACL2 / 344752 HGNCID:24427 Length:401 Species:Homo sapiens


Alignment Length:336 Identity:67/336 - (19%)
Similarity:127/336 - (37%) Gaps:85/336 - (25%)


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


  Fly   114 LNVYTPERPRTNGSLPVMVWFHGGGWQCGSGISSFYGPDFL-----LDHDIVLVSANFRLGPLGF 173
            :.:|.|:| ::......:::|||||:..||.....:  |||     ...|.|:|..::||.|...
Human    91 VRLYLPKR-KSETRRRAVIYFHGGGFCFGSSKQRAF--DFLNRWTANTLDAVVVGVDYRLAPQHH 152

  Fly   174 LSTETLDCPGNNGLKDQLEVLHW--VRANIASFGGDPNSVTVFGESAGG---ASVTYHMLSE--- 230
            ...:         .:|.|..:.:  :...:..:|.||..:.:.|:|:||   .:||..:.::   
Human   153 FPAQ---------FEDGLAAVKFFLLEKILTKYGVDPTRICIAGDSSGGNLATAVTQQVQNDAEI 208

  Fly   231 ----KSRGLLHRGIAQSGTYFNPWAQPAHK----GVAAGR--ATKLAQIVGC-GNAGEWPEKLEC 284
                |.:.||:.|:..:.:|.     |:|:    |:...|  |.||..:... ..|..|     .
Human   209 KHKIKMQVLLYPGLQITDSYL-----PSHRENEHGIVLTRDVAIKLVSLYFTKDEALPW-----A 263

  Fly   285 LRKK---PAEDIVASLYDMFVWDF-------------DPMI-----PFPPVVEPEHDGAFLTVAP 328
            :|:.   |.|.  ..|:....|..             :|::     ..|.:.:..       ..|
Human   264 MRRNQHMPLES--RHLFKFVNWSILLPEKYRKDYVYTEPILGGLSYSLPGLTDSR-------ALP 319

  Fly   329 RQAAKPHGLQLPLMVGATAEEGLLKTAALLNLPQLLAEFKSQFEQVLPVVLNYDHHDDSVRQTIT 393
            ..|.......|||....|.:..||:...|:.:.:|         :.:.|.:.::|.:|.:...::
Human   320 LLANDSQLQNLPLTYILTCQHDLLRDDGLMYVTRL---------RNVGVQVVHEHIEDGIHGALS 375

  Fly   394 QRIESFYFKSG 404
            .....||.:.|
Human   376 FMTSPFYLRLG 386

Known Domains:


Indicated by green bases in alignment.

GeneSequenceDomainRegion External IDIdentity
CG6414NP_570089.1 COesterase 28..567 CDD:395084 67/336 (20%)
AADACL2NP_997248.2 Abhydrolase_3 107..372 CDD:400284 61/303 (20%)
Involved in the stabilization of the negatively charged intermediate by the formation of the oxyanion hole. /evidence=ECO:0000250|UniProtKB:Q5NUF3 111..113 1/1 (100%)

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