ID B4PDD3_DROYA Unreviewed; 1528 AA.
AC B4PDD3;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 113.
DE SubName: Full=Uncharacterized protein, isoform A {ECO:0000313|EMBL:EDW93913.1};
DE EC=1.11.1.7 {ECO:0000313|EMBL:EDW93913.1, ECO:0000313|EMBL:KRK01498.1};
DE SubName: Full=Uncharacterized protein, isoform B {ECO:0000313|EMBL:KRK01498.1};
GN Name=Dyak\GE21698 {ECO:0000313|EMBL:EDW93913.1};
GN ORFNames=Dyak_GE21698 {ECO:0000313|EMBL:EDW93913.1};
OS Drosophila yakuba (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7245 {ECO:0000313|EMBL:EDW93913.1, ECO:0000313|Proteomes:UP000002282};
RN [1] {ECO:0000313|EMBL:EDW93913.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tai18E2 {ECO:0000313|EMBL:EDW93913.1};
RG The Drosophila yakuba Sequencing Consortium;
RT "The Genome of Drosophila yakuba.";
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDW93913.1, ECO:0000313|Proteomes:UP000002282}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tai18E2 {ECO:0000313|EMBL:EDW93913.1}, and Tai18E2 / Tucson
RC 14021-0261.01 {ECO:0000313|Proteomes:UP000002282};
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RA Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A.,
RA Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J.,
RA David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J.,
RA Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G.,
RA Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
RN [3] {ECO:0000313|EMBL:EDW93913.1, ECO:0000313|Proteomes:UP000002282}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tai18E2 {ECO:0000313|EMBL:EDW93913.1}, and Tai18E2 / Tucson
RC 14021-0261.01 {ECO:0000313|Proteomes:UP000002282};
RX PubMed=17550304; DOI=10.1371/journal.pbio.0050152;
RA Ranz J.M., Maurin D., Chan Y.S., von Grotthuss M., Hillier L.W., Roote J.,
RA Ashburner M., Bergman C.M.;
RT "Principles of genome evolution in the Drosophila melanogaster species
RT group.";
RL PLoS Biol. 5:E152-E152(2007).
RN [4] {ECO:0000313|EMBL:EDW93913.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tai18E2 {ECO:0000313|EMBL:EDW93913.1};
RG FlyBase;
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hypobromite + L-tyrosyl-[protein] = 3-bromo-L-tyrosyl-
CC [protein] + H2O; Xref=Rhea:RHEA:69356, Rhea:RHEA-COMP:10136,
CC Rhea:RHEA-COMP:17686, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29250, ChEBI:CHEBI:46858, ChEBI:CHEBI:183512;
CC Evidence={ECO:0000256|ARBA:ARBA00033700};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69357;
CC Evidence={ECO:0000256|ARBA:ARBA00033700};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O2 + L-lysyl-[collagen] + L-methionyl-[collagen] =
CC [collagen]-L-lysyl-N-S-L-methionyl-[collagen] + H(+) + 2 H2O;
CC Xref=Rhea:RHEA:66020, Rhea:RHEA-COMP:12751, Rhea:RHEA-COMP:16949,
CC Rhea:RHEA-COMP:16951, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16044, ChEBI:CHEBI:16240, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:166867; Evidence={ECO:0000256|ARBA:ARBA00033691};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66021;
CC Evidence={ECO:0000256|ARBA:ARBA00033691};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=bromide + H(+) + H2O2 + L-tyrosyl-[protein] = 3-bromo-L-
CC tyrosyl-[protein] + 2 H2O; Xref=Rhea:RHEA:69360, Rhea:RHEA-
CC COMP:10136, Rhea:RHEA-COMP:17686, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15858, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:46858, ChEBI:CHEBI:183512;
CC Evidence={ECO:0000256|ARBA:ARBA00033621};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69361;
CC Evidence={ECO:0000256|ARBA:ARBA00033621};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=bromide + H2O2 = H2O + hypobromite; Xref=Rhea:RHEA:66016,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15858, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:29250; Evidence={ECO:0000256|ARBA:ARBA00033705};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66017;
CC Evidence={ECO:0000256|ARBA:ARBA00033705};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hypobromite + L-lysyl-[collagen] + L-methionyl-[collagen] =
CC [collagen]-L-lysyl-N-S-L-methionyl-[collagen] + bromide + H(+) + H2O;
CC Xref=Rhea:RHEA:66024, Rhea:RHEA-COMP:12751, Rhea:RHEA-COMP:16949,
CC Rhea:RHEA-COMP:16951, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15858, ChEBI:CHEBI:16044, ChEBI:CHEBI:29250,
CC ChEBI:CHEBI:29969, ChEBI:CHEBI:166867;
CC Evidence={ECO:0000256|ARBA:ARBA00033612};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66025;
CC Evidence={ECO:0000256|ARBA:ARBA00033612};
CC ---------------------------------------------------------------------------
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DR EMBL; CM000159; EDW93913.1; -; Genomic_DNA.
DR EMBL; CM000159; KRK01498.1; -; Genomic_DNA.
DR RefSeq; XP_002094201.1; XM_002094165.2.
DR RefSeq; XP_015050059.1; XM_015194573.1.
DR PeroxiBase; 7659; DyaPxd01.
DR EnsemblMetazoa; FBtr0268216; FBpp0266708; FBgn0238946.
DR EnsemblMetazoa; FBtr0405679; FBpp0364301; FBgn0238946.
DR GeneID; 6533490; -.
DR KEGG; dya:Dyak_GE21698; -.
DR eggNOG; KOG0619; Eukaryota.
DR eggNOG; KOG2408; Eukaryota.
DR HOGENOM; CLU_006087_0_1_1; -.
DR OMA; QHFKCAK; -.
DR OrthoDB; 4560at2759; -.
DR Proteomes; UP000002282; Chromosome 3L.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0140825; F:lactoperoxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070831; P:basement membrane assembly; IEA:EnsemblMetazoa.
DR GO; GO:0030199; P:collagen fibril organization; IEA:EnsemblMetazoa.
DR GO; GO:0006909; P:phagocytosis; IEA:EnsemblMetazoa.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd09826; peroxidasin_like; 1.
DR Gene3D; 6.20.200.20; -; 1.
DR Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 4.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR InterPro; IPR019791; Haem_peroxidase_animal.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000372; LRRNT.
DR InterPro; IPR034824; Peroxidasin_peroxidase.
DR InterPro; IPR001007; VWF_dom.
DR PANTHER; PTHR11475; OXIDASE/PEROXIDASE; 1.
DR PANTHER; PTHR11475:SF58; PEROXIDASIN; 1.
DR Pfam; PF03098; An_peroxidase; 1.
DR Pfam; PF07679; I-set; 3.
DR Pfam; PF13927; Ig_3; 1.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF00093; VWC; 1.
DR PRINTS; PR00457; ANPEROXIDASE.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 4.
DR SMART; SM00369; LRR_TYP; 5.
DR SMART; SM00013; LRRNT; 1.
DR SMART; SM00214; VWC; 1.
DR SUPFAM; SSF57603; FnI-like domain; 1.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 4.
DR SUPFAM; SSF52058; L domain-like; 1.
DR PROSITE; PS50835; IG_LIKE; 4.
DR PROSITE; PS51450; LRR; 1.
DR PROSITE; PS50292; PEROXIDASE_3; 1.
DR PROSITE; PS01208; VWFC_1; 1.
DR PROSITE; PS50184; VWFC_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR619791-2};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR619791-2};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR619791-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:EDW93913.1};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000313|EMBL:EDW93913.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1528
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014299050"
FT DOMAIN 235..321
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 366..454
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 459..546
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 554..644
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1464..1525
FT /note="VWFC"
FT /evidence="ECO:0000259|PROSITE:PS50184"
FT REGION 344..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1408..1442
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 1110
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR619791-2"
SQ SEQUENCE 1528 AA; 170586 MW; 1EBB5F5A4E6D5735 CRC64;
MRVPLLLLQL LGLLLLSGGV QSIYCPAGCT CLERTVRCIR AKLTAVPKLP QDTQTLDLRF
NHIEELPANA FSGLAQLTTL FLNDNELAYL QDGALNGLTA LRFLYLNNNR LSRLPAAIFQ
RLPRLEAIFL ENNDIWQLPA GLFDNLPRLN RLIMYNNKLS QLPVDGFNRL NNLKRLRLDG
NNIDCNCGVY SLWRRWHLDV QRQLVSISLT CAAPQLLQNQ GFSSLGEHHF KCAKPQFLVA
AQDAQAAAGE QVELSCEVTG LPRPQITWMH NTQEVGLEEQ ARAEILPSGS LLIRSVEPSD
MGIYQCIARN EMGELHSQPV RLVVNGGNHP LDSPLDARSN QVWADAGTPT HGATPSPSST
PLPSPPHFTH QPHDQIVALH GSGHVLLDCA ASGWPQPDIQ WFVNGRQLLQ STPSLQLQAN
GSLILLQPTQ LSAGTYRCEA RNSLGSVQAT ARIEVKELPE ILTAPQSQTI KLGKAFVLEC
DADGNPLPTI DWQFNGVPLP GNTPDLQLEN ENTELLVGAA RHEHAGVYRC TARNENGETS
MEATIKVERS QSPPQLAIEP SNLVAITGTT IELPCQADQP EDGLQITWRH DGRLIDPNVQ
LAEKYQISGA GSLFVKNVTI PDGGRYECQL KNQFGRISAS ALVTIRNNVD LAPGDRYVRI
AFAEAAKEID LAINNTLDML FSNRSDKAPP NYGELLRVFR FPTGEARQLA RAAEIYERTL
VNIRKHVQEG DNLTMKSEEY EFRDLLSREH LHLVAELSGC MEHREMPNCT DMCFHSRYRS
IDGTCNNLQH PTWGASLTAF RRLAPPIYEN GFSMPVGWTK GMLYSGHAKP SARLVSTSLV
ATKEITPDAR ITHMVMQWGQ FLDHDLDHAI PSVSSESWDG IDCKKSCEMA PPCYPIEVPP
NDPRVRNRRC IDVVRSSAIC GSGMTSLFFD SVQHREQINQ LTSYIDASQM YGYSTAFAQE
LRNLTSQDGL LRVGVHFPRQ KDMLPFAAPQ DGMDCRRNLD ENTMSCFVSG DIRVNEQVGL
LAMHTVWMRE HNRIASKLKQ INGHWDGDTL YQEARKIVGA QMQHITFKQW LPLIIGESGM
KMMGEYSGYN PQVNPSIANE FATAALRFGH TIINPILHRL NETFQPIPQG HLLLHKAFFA
PWRLAYEGGV DPLMRGFLAV PAKLKTPDQN LNTELTEKLF QTAHAVALDL AAINIQRGRD
HGMPGYNVYR KLCNLTVAQD FEDLADEISN AEIRQKMKEL YGHPDNVDVW LGGILEDQVE
GGKVGPLFQC LLVEQFRRLR DGDRLYYENP GVFSPEQLTQ IKQANFGRVL CDVGDNFDQV
TENVFILAKH QGGYKKCEDI AGINLYLWQE CGRCNSPPAI FDSYIPQTYT KRSNRQKRDL
GKVDEEVATA ESYDSPLESL YDVNEERVSG LEELIGSFQK ELKKLHKKLR KLEDSCNSAD
VEPVAQVVQL AAAPPQVVTK PKRSHCVDDK GTTRLNNEVW SPDVCTKCNC FHGQVNCLRE
RCGEVSCPPG VDPLTPPEAC CPHCPMVK
//
