DRSC/TRiP Functional Genomics Resources

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Protein Alignment CG1889 and Fcna

DIOPT Version :10

Sequence 1:NP_727376.2 Gene:CG1889 / 31928 FlyBaseID:FBgn0030164 Length:338 Species:Drosophila melanogaster
Sequence 2:NP_112638.2 Gene:Fcna / 83517 RGDID:621221 Length:335 Species:Rattus norvegicus


Alignment Length:362 Identity:106/362 - (29%)
Similarity:149/362 - (41%) Gaps:82/362 - (22%)


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


  Fly    14 MACLSTTQTDLGGGLLVPPSLGNASSSSCPVSALSGLTTRMQSLNNEIASVKEQIGSLQEQLVDL 78
            :.||.::|           :||. .|.:||...:.||                   ..|:::..:
  Rat    12 LLCLCSSQ-----------ALGQ-ESGACPDVKIVGL-------------------GAQDKVAVI 45

  Fly    79 RRAGS--APVVGLASPNALASRFPFSHNSLDIEPQLLANGGAAAVPIT--------------PAN 127
            :...|  .|......|.:.|.|   ....|...|..:...|:...|.|              .|:
  Rat    46 QSCPSFPGPPGPKGEPGSPAGR---GERGLQGSPGKMGPAGSKGEPGTMGPPGVKGEKGERGTAS 107

  Fly   128 CLKQQH---GVVRIRPRS--------------------NVEPFFVFCDQKVRNGGWTMVVNRYDG 169
            .|.|:.   .:.|..|||                    :..|..|.||..|..||||:...|.||
  Rat   108 PLGQKELGDALCRRGPRSCKDLLTRGIFLTGWYTIYLPDCRPLTVLCDMDVDGGGWTVFQRRVDG 172

  Fly   170 SEDFNRKWADYKIGFGPLTTEFFIGLDKLHQITSSDNYELLVQLQNRKQELRYALYDHFSIGSES 234
            |.:|.|.|..||.|||.|.|||::|.|.||.:|::.|.||.|.|:..:.:..:|.|..|.:..|.
  Rat   173 SINFYRDWDSYKRGFGNLGTEFWLGNDYLHLLTANGNQELRVDLREFQGQTSFAKYSSFQVSGEQ 237

  Fly   235 EQYRLNVLGDY-HGDAADALRDHTGKKFSTHDRVNDEN-EQNCAAQQSGAFWYGGSCNLTNPFGL 297
            |:|:| .||.: .|.|.|:|..|....|||||:.||.| .:||||...||:|| ..|:.:|..|.
  Rat   238 EKYKL-TLGQFLEGTAGDSLTKHNNMAFSTHDQDNDTNGGKNCAALFHGAWWY-HDCHQSNLNGR 300

  Fly   298 Y-QRLLERDVDGFKGILWRGFLNGPKGSLKIVRMMVR 333
            | ....|...||...:..||.    :.|.|:..|.:|
  Rat   301 YLPGSHESYADGINWLSGRGH----RYSYKVAEMKIR 333

Known Domains:


Indicated by green bases in alignment.

GeneSequenceDomainRegion External IDIdentity
CG1889NP_727376.2 FReD 123..335 CDD:238040 86/251 (34%)
FcnaNP_112638.2 Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite 47..114 13/69 (19%)
Collagen <67..108 CDD:460189 7/43 (16%)
FReD 123..333 CDD:238040 80/215 (37%)
A domain, contributes to trimerization. /evidence=ECO:0000250 123..162 8/38 (21%)
B domain, contributes to trimerization. /evidence=ECO:0000250 163..251 37/88 (42%)
P domain. /evidence=ECO:0000250|UniProtKB:O00602 326..335 3/8 (38%)

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