ID A0A0L0C7B9_LUCCU Unreviewed; 604 AA.
AC A0A0L0C7B9;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Neither inactivation nor afterpotential protein G {ECO:0000313|EMBL:KNC28170.1};
GN ORFNames=FF38_04345 {ECO:0000313|EMBL:KNC28170.1};
OS Lucilia cuprina (Green bottle fly) (Australian sheep blowfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC Calliphoridae; Luciliinae; Lucilia.
OX NCBI_TaxID=7375 {ECO:0000313|EMBL:KNC28170.1, ECO:0000313|Proteomes:UP000037069};
RN [1] {ECO:0000313|EMBL:KNC28170.1, ECO:0000313|Proteomes:UP000037069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LS {ECO:0000313|EMBL:KNC28170.1,
RC ECO:0000313|Proteomes:UP000037069};
RC TISSUE=Full body {ECO:0000313|EMBL:KNC28170.1};
RX PubMed=26108605; DOI=10.1038/ncomms8344;
RA Anstead C.A., Korhonen P.K., Young N.D., Hall R.S., Jex A.R., Murali S.C.,
RA Hughes D.S., Lee S.F., Perry T., Stroehlein A.J., Ansell B.R.,
RA Breugelmans B., Hofmann A., Qu J., Dugan S., Lee S.L., Chao H., Dinh H.,
RA Han Y., Doddapaneni H.V., Worley K.C., Muzny D.M., Ioannidis P.,
RA Waterhouse R.M., Zdobnov E.M., James P.J., Bagnall N.H., Kotze A.C.,
RA Gibbs R.A., Richards S., Batterham P., Gasser R.B.;
RT "Lucilia cuprina genome unlocks parasitic fly biology to underpin future
RT interventions.";
RL Nat. Commun. 6:7344-7344(2015).
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KNC28170.1}.
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DR EMBL; JRES01000819; KNC28170.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L0C7B9; -.
DR STRING; 7375.A0A0L0C7B9; -.
DR EnsemblMetazoa; KNC28170; KNC28170; FF38_04345.
DR OMA; IEQRQCL; -.
DR Proteomes; UP000037069; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012132; GMC_OxRdtase.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR PANTHER; PTHR11552:SF188; NEITHER INACTIVATION NOR AFTERPOTENTIAL PROTEIN G; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR PIRSF; PIRSF000137; Alcohol_oxidase; 2.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000037069}.
FT DOMAIN 287..301
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
SQ SEQUENCE 604 AA; 67886 MW; 85BF8D25658D934A CRC64;
MNFNKILILA ALIIGLLSML WFVIAALLEQ RVPNALMAKE GYIFDYVVVG AGTAGSVVAS
LLSKHSNATV LLIEAGDRFG LLSKIPLFTT FQQKGLNDWS FLTTSQKHSS KGLEEQRQSL
PRGKGLGGSG ELNYMLHSDG YEGDFERWSQ DYNLSDWNWL SVKPFLEAGN AKPHERLEIP
DSYSKITLAI QKAQNEFMHK PWRFRKARYN IKNGLRYSVY QRFLHDAHKY KNLRIMTNTM
AKKIEFEYNK SNDVQVRALK ISTKDENTRK EYIFEVEVQK ELIVCAGAFQ SPQLLMVSGI
GEKAELRKRH VAVPDFVPEL PAVGQNLHDH INLPLYSSIQ VVGPTLNQRS LLDPFAIFNY
LTVGSGHLGN FGVLSHIYSL EGNINDTFGL TFFGAGAIDE LALMSISNFK RAHFRALFPR
YFNTSQEGFV IISNCLQPKS RGNVKIQNAN IRKNPLIDPN YLAEQQDVEC TIKAIRAAVE
IVTSFSFSEL GPKIHWPRIK ECANFGPFER DFLLNNPSDH YLECILRYVG LGSHHAAGTC
TMGNNPENSV VDSNFKVHGI KNLRVIDASV FPTPISGYPN SIVVGLATRG AAMILRDYKR
NISK
//
