ID   PDE11_DROME             Reviewed;        1451 AA.
AC   Q9VJ79; Q8MQW0; Q9VJ78;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 4.
DT   24-JAN-2024, entry version 152.
DE   RecName: Full=Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11;
DE            EC=3.1.4.35 {ECO:0000269|PubMed:15673286};
DE            EC=3.1.4.53 {ECO:0000269|PubMed:15673286};
DE   AltName: Full=cAMP and cGMP phosphodiesterase 11;
DE            Short=PDE11 {ECO:0000303|PubMed:15673286};
GN   Name=Pde11; ORFNames=CG34341;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2]
RP   GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM D).
RC   STRAIN=Berkeley; TISSUE=Embryo;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=15673286; DOI=10.1042/bj20050057;
RA   Day J.P., Dow J.A.T., Houslay M.D., Davies S.A.;
RT   "Cyclic nucleotide phosphodiesterases in Drosophila melanogaster.";
RL   Biochem. J. 388:333-342(2005).
CC   -!- FUNCTION: Plays a role in signal transduction by regulating the
CC       intracellular concentration of cyclic nucleotides cAMP and cGMP. Dual-
CC       specificity phosphodiesterase that catalyzes the hydrolysis of both
CC       cAMP and cGMP to 5'-AMP and 5'-GMP, respectively.
CC       {ECO:0000269|PubMed:15673286}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3',5'-cyclic GMP + H2O = GMP + H(+); Xref=Rhea:RHEA:16957,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57746,
CC         ChEBI:CHEBI:58115; EC=3.1.4.35;
CC         Evidence={ECO:0000269|PubMed:15673286};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16958;
CC         Evidence={ECO:0000269|PubMed:15673286};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3',5'-cyclic AMP + H2O = AMP + H(+); Xref=Rhea:RHEA:25277,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58165,
CC         ChEBI:CHEBI:456215; EC=3.1.4.53;
CC         Evidence={ECO:0000269|PubMed:15673286};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25278;
CC         Evidence={ECO:0000269|PubMed:15673286};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250};
CC       Note=Binds 2 divalent metal cations per subunit. Site 1 may
CC       preferentially bind zinc ions, while site 2 has a preference for
CC       magnesium and/or manganese ions. {ECO:0000250};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=18.5 uM for cAMP {ECO:0000269|PubMed:15673286};
CC         KM=6 uM for cGMP {ECO:0000269|PubMed:15673286};
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=B;
CC         IsoId=Q9VJ79-1; Sequence=Displayed;
CC       Name=C;
CC         IsoId=Q9VJ79-3; Sequence=VSP_030328, VSP_030329;
CC       Name=D;
CC         IsoId=Q9VJ79-2; Sequence=VSP_019906;
CC   -!- TISSUE SPECIFICITY: In adults, it is enriched in Malpighian tubules.
CC       {ECO:0000269|PubMed:15673286}.
CC   -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC       {ECO:0000305}.
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DR   EMBL; AE014134; AAF53675.3; -; Genomic_DNA.
DR   EMBL; AE014134; AAF53676.2; -; Genomic_DNA.
DR   EMBL; AY122262; AAM52774.1; -; mRNA.
DR   RefSeq; NP_001097177.1; NM_001103707.2. [Q9VJ79-3]
DR   RefSeq; NP_001286044.1; NM_001299115.1. [Q9VJ79-1]
DR   RefSeq; NP_001286045.1; NM_001299116.1. [Q9VJ79-3]
DR   RefSeq; NP_609885.2; NM_136041.2. [Q9VJ79-1]
DR   AlphaFoldDB; Q9VJ79; -.
DR   SMR; Q9VJ79; -.
DR   BioGRID; 61102; 6.
DR   STRING; 7227.FBpp0310380; -.
DR   PaxDb; 7227-FBpp0111456; -.
DR   EnsemblMetazoa; FBtr0112544; FBpp0111456; FBgn0085370. [Q9VJ79-1]
DR   EnsemblMetazoa; FBtr0112545; FBpp0111457; FBgn0085370. [Q9VJ79-3]
DR   EnsemblMetazoa; FBtr0343830; FBpp0310380; FBgn0085370. [Q9VJ79-1]
DR   EnsemblMetazoa; FBtr0343831; FBpp0310381; FBgn0085370. [Q9VJ79-3]
DR   GeneID; 35107; -.
DR   KEGG; dme:Dmel_CG34341; -.
DR   AGR; FB:FBgn0085370; -.
DR   CTD; 35107; -.
DR   FlyBase; FBgn0085370; Pde11.
DR   VEuPathDB; VectorBase:FBgn0085370; -.
DR   eggNOG; KOG3689; Eukaryota.
DR   InParanoid; Q9VJ79; -.
DR   OMA; GHQYQYY; -.
DR   OrthoDB; 5479253at2759; -.
DR   PhylomeDB; Q9VJ79; -.
DR   Reactome; R-DME-2485179; Activation of the phototransduction cascade.
DR   Reactome; R-DME-4086398; Ca2+ pathway.
DR   Reactome; R-DME-418457; cGMP effects.
DR   Reactome; R-DME-445355; Smooth Muscle Contraction.
DR   Reactome; R-DME-9013422; RHOBTB1 GTPase cycle.
DR   BioGRID-ORCS; 35107; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 35107; -.
DR   PRO; PR:Q9VJ79; -.
DR   Proteomes; UP000000803; Chromosome 2L.
DR   Bgee; FBgn0085370; Expressed in saliva-secreting gland and 34 other cell types or tissues.
DR   ExpressionAtlas; Q9VJ79; baseline and differential.
DR   GO; GO:0005829; C:cytosol; HDA:FlyBase.
DR   GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IDA:UniProtKB.
DR   GO; GO:0047555; F:3',5'-cyclic-GMP phosphodiesterase activity; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046058; P:cAMP metabolic process; IDA:UniProtKB.
DR   GO; GO:0046068; P:cGMP metabolic process; IDA:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   CDD; cd00077; HDc; 1.
DR   Gene3D; 3.30.450.40; -; 2.
DR   Gene3D; 1.10.1300.10; 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain; 1.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
DR   InterPro; IPR003607; HD/PDEase_dom.
DR   InterPro; IPR023088; PDEase.
DR   InterPro; IPR002073; PDEase_catalytic_dom.
DR   InterPro; IPR036971; PDEase_catalytic_dom_sf.
DR   InterPro; IPR023174; PDEase_CS.
DR   PANTHER; PTHR11347; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1.
DR   PANTHER; PTHR11347:SF221; DUAL 3',5'-CYCLIC-AMP AND -GMP PHOSPHODIESTERASE 11; 1.
DR   Pfam; PF01590; GAF; 2.
DR   Pfam; PF00233; PDEase_I; 1.
DR   PRINTS; PR00387; PDIESTERASE1.
DR   SMART; SM00065; GAF; 2.
DR   SMART; SM00471; HDc; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 2.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR   PROSITE; PS00126; PDEASE_I_1; 1.
DR   PROSITE; PS51845; PDEASE_I_2; 1.
DR   Genevisible; Q9VJ79; DM.
PE   1: Evidence at protein level;
KW   Alternative splicing; cAMP; cGMP; Hydrolase; Metal-binding;
KW   Reference proteome; Repeat.
FT   CHAIN           1..1451
FT                   /note="Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11"
FT                   /id="PRO_0000247044"
FT   DOMAIN          419..572
FT                   /note="GAF 1"
FT   DOMAIN          604..754
FT                   /note="GAF 2"
FT   DOMAIN          783..1107
FT                   /note="PDEase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT   REGION          1..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          75..100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          125..169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          235..262
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          327..374
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1109..1171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1200..1248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1268..1305
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1325..1364
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..54
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        75..98
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        135..169
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        235..261
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        344..359
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1154..1171
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1217..1248
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1289..1303
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1327..1355
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        860
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         864
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT   BINDING         900
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT   BINDING         901
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT   BINDING         901
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT   BINDING         1011
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT   VAR_SEQ         1..44
FT                   /note="Missing (in isoform C)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_030328"
FT   VAR_SEQ         1
FT                   /note="M -> MKVTQSEENTRNTSDRSKSVQTNRKFDNFNWLLSCGLLAAVKSTKLI
FT                   PQLPRQQQPKKYNLRYAAELLKFDKIQFIKTEGLTFALLAGP (in isoform D)"
FT                   /evidence="ECO:0000303|PubMed:12537569"
FT                   /id="VSP_019906"
FT   VAR_SEQ         45..64
FT                   /note="QTPSHSPQIQHHSEIIPATT -> MASSPNNAAPPVLWRARRKI (in
FT                   isoform C)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_030329"
FT   CONFLICT        38
FT                   /note="Q -> QQQ (in Ref. 3; AAM52774)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1192
FT                   /note="V -> A (in Ref. 3; AAM52774)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1196
FT                   /note="A -> V (in Ref. 3; AAM52774)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1232
FT                   /note="C -> R (in Ref. 3; AAM52774)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1342
FT                   /note="H -> HNH (in Ref. 3; AAM52774)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1451 AA;  160930 MW;  DFEC01058FB600A9 CRC64;
     MGQAASMCRF RGCRYKNKNK SSKQQQQQQQ QQQQQQQQHQ QQQQQTPSHS PQIQHHSEII
     PATTGLHLRS IEEPATTPLQ FQPTGRMNTE QGGTGYGGYG SSEHSLLIAT RHAGVPLPLA
     QHQPLPAHYQ PLNHSGAAPP SSSNGSSSSG GGVQTSATPQ QQQQYQVQQP YQYQYQHHYH
     HQANSPQHHR PYDPEHARME AWLDENQEFV QDYFIRKATR QTVDAWLVSH ATSAGNDVVS
     STSPTHANGQ TSSSRGGSGA TTPVRKISAH EFERGGLLKP IVNTIDGTPT FLSIGPPMDN
     GSVGGSCSNL QNVGGVVAGQ YQYNHQQHHH NHAHLHHSQH SHYQAGGAVG SSSLGSTGGA
     SGAGGAPSLG GSGGAGNGHQ YPYYHCHQRP QRLSRNELKQ LDEKELIFEL VKDICNELEV
     RTLCHKILQN VSILLNADRG SLFLVQGRCN GPDGLKKCLV SKLFDVCPRS TVEEMEQQDE
     VRVAWGTGIA GHVAESGEPV NIPDAYQDER FNCEIDSLTG YRTKALLCMP IKDSSGDVIG
     VAQVINKMNG ECFSEIDEKV FSSYLQFCGI GLRNAQLYEK SQLEIKRNQV LLDLARMIFE
     EQSTIEHMVF RILTHMQSLI QCQRVQILLV HEADKGSFSR VFDFEANDLS EEEATSRTSP
     YESRFPINIG ITGHVATTGE TVNVPNAYED DRFDASVDEN SCFKHRSILC MAIKNSLGQI
     IGVIQLINKF NELDFTKNDE NFVEAFAIFC GMGIHNTHMY EKAIVAMAKQ SVTLEVLSYH
     ASATMDEAHR LRRLRVPSAV HFRLHDFKFD DIHFEDDDTL KACLRMFLDL DFVERFHIDY
     EVLCRWLLSV KKNYRNVTYH NWRHAFNVAQ MMFAILTTTQ WWKIFGEIEC LALIIGCLCH
     DLDHRGTNNS FQIKASSPLA QLYSTSTMEH HHFDQCLMIL NSPGNQILAN LSSDDYCRVI
     RVLEDAILST DLAVYFKKRG PFLESVSQPT SYWVAEEPRA LLRAMSMTVC DLSAITKPWE
     IEKRVADLVS SEFFEQGDME KQELNITPID IMNREKEDEL PMMQVNFIDS ICLPIYEAFA
     TLSDKLEPLV EGVRDNRGHW IDLADVVKTK TSQDQEPEEE QQQQNVISNG DCKAMSDDDV
     AASEAEVAVD SPSEKASVNG SNVANNSSNT NKKIAVASHP TSTQPSDDDN DVDADADDVD
     EQAAEENGHD AEVDEASCRS NSTCSSSTAS SCLSTPPPTG EDDSTPVSPL KTLQAKLVAA
     NLNALQRQTS NQAQTQKQRC KSCDHSRSGL QVRKTSSLRG AQELDLDSKT RNGTHAALCK
     STPVINNHSH HHNHSHSHNH NHHHHHHHHS HHNHSQHGIG IGSASIGGSG LISLTTPLLA
     MDSDRIPKIV GKIGNLDGLP FANGIGGPQN GHGLPFGSYQ HHHHHQHHHH LLARRHSETN
     SNGATAMAVE K
//