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Database: UniProt
Entry: A0A139WL26_TRICA
LinkDB: A0A139WL26_TRICA
Original site: A0A139WL26_TRICA 
ID   A0A139WL26_TRICA        Unreviewed;      4348 AA.
AC   A0A139WL26;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Muscle M-line assembly protein unc-89-like Protein {ECO:0000313|EMBL:KYB28584.1};
GN   Name=AUGUSTUS-3.0.2_32479 {ECO:0000313|EMBL:KYB28584.1};
GN   ORFNames=TcasGA2_TC032479 {ECO:0000313|EMBL:KYB28584.1};
OS   Tribolium castaneum (Red flour beetle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC   Tenebrionidae; Tenebrionidae incertae sedis; Tribolium.
OX   NCBI_TaxID=7070 {ECO:0000313|EMBL:KYB28584.1, ECO:0000313|Proteomes:UP000007266};
RN   [1] {ECO:0000313|EMBL:KYB28584.1, ECO:0000313|Proteomes:UP000007266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:KYB28584.1,
RC   ECO:0000313|Proteomes:UP000007266};
RX   PubMed=18362917; DOI=10.1038/nature06784;
RG   Tribolium Genome Sequencing Consortium;
RA   Richards S., Gibbs R.A., Weinstock G.M., Brown S.J., Denell R.,
RA   Beeman R.W., Gibbs R., Beeman R.W., Brown S.J., Bucher G., Friedrich M.,
RA   Grimmelikhuijzen C.J., Klingler M., Lorenzen M., Richards S., Roth S.,
RA   Schroder R., Tautz D., Zdobnov E.M., Muzny D., Gibbs R.A., Weinstock G.M.,
RA   Attaway T., Bell S., Buhay C.J., Chandrabose M.N., Chavez D.,
RA   Clerk-Blankenburg K.P., Cree A., Dao M., Davis C., Chacko J., Dinh H.,
RA   Dugan-Rocha S., Fowler G., Garner T.T., Garnes J., Gnirke A., Hawes A.,
RA   Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N., Joshi V.,
RA   Khan Z.M., Jackson L., Kovar C., Kowis A., Lee S., Lewis L.R., Margolis J.,
RA   Morgan M., Nazareth L.V., Nguyen N., Okwuonu G., Parker D., Richards S.,
RA   Ruiz S.J., Santibanez J., Savard J., Scherer S.E., Schneider B.,
RA   Sodergren E., Tautz D., Vattahil S., Villasana D., White C.S., Wright R.,
RA   Park Y., Beeman R.W., Lord J., Oppert B., Lorenzen M., Brown S., Wang L.,
RA   Savard J., Tautz D., Richards S., Weinstock G., Gibbs R.A., Liu Y.,
RA   Worley K., Weinstock G., Elsik C.G., Reese J.T., Elhaik E., Landan G.,
RA   Graur D., Arensburger P., Atkinson P., Beeman R.W., Beidler J., Brown S.J.,
RA   Demuth J.P., Drury D.W., Du Y.Z., Fujiwara H., Lorenzen M., Maselli V.,
RA   Osanai M., Park Y., Robertson H.M., Tu Z., Wang J.J., Wang S., Richards S.,
RA   Song H., Zhang L., Sodergren E., Werner D., Stanke M., Morgenstern B.,
RA   Solovyev V., Kosarev P., Brown G., Chen H.C., Ermolaeva O., Hlavina W.,
RA   Kapustin Y., Kiryutin B., Kitts P., Maglott D., Pruitt K., Sapojnikov V.,
RA   Souvorov A., Mackey A.J., Waterhouse R.M., Wyder S., Zdobnov E.M.,
RA   Zdobnov E.M., Wyder S., Kriventseva E.V., Kadowaki T., Bork P., Aranda M.,
RA   Bao R., Beermann A., Berns N., Bolognesi R., Bonneton F., Bopp D.,
RA   Brown S.J., Bucher G., Butts T., Chaumot A., Denell R.E., Ferrier D.E.,
RA   Friedrich M., Gordon C.M., Jindra M., Klingler M., Lan Q., Lattorff H.M.,
RA   Laudet V., von Levetsow C., Liu Z., Lutz R., Lynch J.A., da Fonseca R.N.,
RA   Posnien N., Reuter R., Roth S., Savard J., Schinko J.B., Schmitt C.,
RA   Schoppmeier M., Schroder R., Shippy T.D., Simonnet F., Marques-Souza H.,
RA   Tautz D., Tomoyasu Y., Trauner J., Van der Zee M., Vervoort M.,
RA   Wittkopp N., Wimmer E.A., Yang X., Jones A.K., Sattelle D.B., Ebert P.R.,
RA   Nelson D., Scott J.G., Beeman R.W., Muthukrishnan S., Kramer K.J.,
RA   Arakane Y., Beeman R.W., Zhu Q., Hogenkamp D., Dixit R., Oppert B.,
RA   Jiang H., Zou Z., Marshall J., Elpidina E., Vinokurov K., Oppert C.,
RA   Zou Z., Evans J., Lu Z., Zhao P., Sumathipala N., Altincicek B.,
RA   Vilcinskas A., Williams M., Hultmark D., Hetru C., Jiang H.,
RA   Grimmelikhuijzen C.J., Hauser F., Cazzamali G., Williamson M., Park Y.,
RA   Li B., Tanaka Y., Predel R., Neupert S., Schachtner J., Verleyen P.,
RA   Raible F., Bork P., Friedrich M., Walden K.K., Robertson H.M., Angeli S.,
RA   Foret S., Bucher G., Schuetz S., Maleszka R., Wimmer E.A., Beeman R.W.,
RA   Lorenzen M., Tomoyasu Y., Miller S.C., Grossmann D., Bucher G.;
RT   "The genome of the model beetle and pest Tribolium castaneum.";
RL   Nature 452:949-955(2008).
RN   [2] {ECO:0000313|EMBL:KYB28584.1, ECO:0000313|Proteomes:UP000007266}
RP   GENOME REANNOTATION.
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:KYB28584.1,
RC   ECO:0000313|Proteomes:UP000007266};
RX   PubMed=19820115; DOI=10.1093/nar/gkp807;
RA   Kim H.S., Murphy T., Xia J., Caragea D., Park Y., Beeman R.W.,
RA   Lorenzen M.D., Butcher S., Manak J.R., Brown S.J.;
RT   "BeetleBase in 2010: revisions to provide comprehensive genomic information
RT   for Tribolium castaneum.";
RL   Nucleic Acids Res. 38:D437-D442(2010).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC       protein kinase family. {ECO:0000256|ARBA:ARBA00006692}.
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DR   EMBL; KQ971322; KYB28584.1; -; Genomic_DNA.
DR   EnsemblMetazoa; TC032479_006; TC032479_006; TC032479.
DR   Proteomes; UP000007266; Linkage group 3.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProt.
DR   CDD; cd00063; FN3; 2.
DR   CDD; cd00096; Ig; 1.
DR   CDD; cd13325; PH_unc89; 1.
DR   CDD; cd00160; RhoGEF; 1.
DR   Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 21.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR   InterPro; IPR035899; DBL_dom_sf.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
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; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   PANTHER; PTHR47633:SF7; IG-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR47633; IMMUNOGLOBULIN; 1.
DR   Pfam; PF00041; fn3; 2.
DR   Pfam; PF07679; I-set; 19.
DR   Pfam; PF00069; Pkinase; 2.
DR   Pfam; PF00621; RhoGEF; 1.
DR   SMART; SM00060; FN3; 2.
DR   SMART; SM00409; IG; 19.
DR   SMART; SM00408; IGc2; 15.
DR   SMART; SM00325; RhoGEF; 1.
DR   SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 19.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50853; FN3; 2.
DR   PROSITE; PS50835; IG_LIKE; 15.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
PE   3: Inferred from homology;
KW   Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007266};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          136..314
FT                   /note="DH"
FT                   /evidence="ECO:0000259|PROSITE:PS50010"
FT   DOMAIN          326..430
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          1190..1301
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          1316..1405
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          1503..1592
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          1597..1687
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          1692..1783
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          2019..2110
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          2224..2313
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          2325..2416
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          2422..2513
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          2519..2610
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          2616..2707
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          2721..2811
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          2817..2905
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          2919..3008
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          3036..3136
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          3271..3360
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          3390..3644
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          3890..3984
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          4036..4288
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          432..868
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          962..998
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1012..1097
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1919..1948
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1960..2032
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3702..3722
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        455..469
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        499..687
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        694..743
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        751..834
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        835..853
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        962..986
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1012..1048
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1067..1081
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1082..1097
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1919..1947
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1966..2014
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2017..2031
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3706..3720
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   4348 AA;  492748 MW;  997FA644D3ADBD9E CRC64;
     MIFVLRQPTN GEILVAWQKY VACSSDEITL KEGDVVELLD TDDPVASKKP KLDPELDTVS
     GELLDSSAAR HKLSVKPRRT HLSSRHSPTR LNLSARWLVR EITGSKKQGW VPCKVLQTID
     DPSPGGAGLP GDALFRRQAV VKELVETEQE FVKDLDFVVQ KYLLLSESKN VPKVIRDNFD
     IIFGNLKEIA EFHRTVLMEG VKYYANEPHL LGKAFLRLER DFDKHVDYYM YEPQAQAFLD
     ACDEAHDYFD DLSQRLGDDK TISEHLKLPI QRINDYQLLL KELVRYSACL GEDNSDLQKA
     LELMLSVPHR AQDEKFTSNI EGYRGSIHKL GRLLAHDWFS VTFGQVTKER YLFLFKGKIL
     ICKVRRISED RSVFQLKDII QLNRVAVKEH PEEERVLELI DTSGGQALIL TAHRDHITEY
     WLKEIREFAQ EYEENEDTEA EAEDFQIASS SPPTDRSEEG DKFEETAPAL QEDIVETPPP
     LEDRPVPKVL TPPPLLEEET SSKLKEESKE TKQVESLPQV EESKPRQKEE PEKRKETGPQ
     VVEDTKSRPK EEPEKNKHVV EESKPTPKEK PQKPKVVEEK QKETCPQVVE NTRSKPKEEP
     DKTKQVVEES KPRAKEEPQK PKGVEEKQKE TCPHVVEDTR SKPKEEPERT KQVVERTPKE
     EPKKSKPVEE KQHSRPEPKE ETEIKNRPQI VEPAPPPEEK KDVPKRQPTP DKSRKSQEEK
     KVVPQLKVEE KKIKEEPQVQ VEKKVSKAGE VSSVLTKSSV VNVETADDMS RRYTSSSSRA
     EGYSESSYSR RSQSSYSNDG SRYDSIASKY GSAESSIGGS KYESVGSKYD TGDSSYSRRS
     IRDMGDDNDY NYSRRSIKSV TAEYGDGDSY TRRSIRASAE ATGDLDSYSV RKSLKTSAEI
     LGYGGEEGKR SVSIEEVGDG GRYSRKALTA RDNIEEELLS KYSPSKYLED REHEDVYAKY
     ERKYSRTDSS DSKSKYTAKL GGEEDSYTKS KYLSSSIEQK GAEEDVYAKY ARKYSRTDSS
     KSREEDEDKY RKAYKRTDSA KSDRESSSIR SETTISNGKE TRREVAASSE SVSPSTMVKE
     SSRSGKHVEE SHVSGDEERN RFIKTIRGAD IELTPEERLE RAKTDKPEFV VKLKDTELAE
     NTYLRFMVKV RGDPNPDVIF FKDGVIVEKS DRYEVIREHS DRGFYELLIP EVQMSDAGEY
     KCVASNKWGE DSCEATLKVT TEDLHKDMPE GEILPPGETP EFQWKKDGAP FEPDERFKVL
     MGDDEDSLAL VFQHVRAEDV GLYTCVAQTS RGHISCSAEL TVHGTVNQLV REPEKPVLIV
     EKRNPVVNAG GSAMIELQVK GFPKPQVKWT HEGKPIEAGG KYKFLYEDEE TMSLVIKDVQ
     KEDAGKYLCT AENEIGSDTA EMTLTVKTPP KLRKKIEDVD AHADLLLEIP VEIEGTPRPK
     VVFYKDGKEI KKDERIKVVE ENEKVVLVIE KTMLKDSGSY SIVATNELAQ ISEFFNLHVH
     TKPKILEKLG KDKIVSQEEK FELRVKIESE PEAEVKWYKD DAEIKSSDHY VIKKDGETYI
     LKITGAVTTD AARYKVKAVN IHGSVEDDIR VDVKKAPKIT KGLQDMTVNE HDKQVTLDVK
     VEAFPKPSVK WYLDEMEITE TKTEFTRVDS DDGVKLVIKE VNSELSGKYT CKLSNECGST
     ETSAKLTVNC APRIIKQLKD TTVEEGATLH LEVEVEGCPT PTVKWLRNGR EVSADARIKI
     SRDTQRHETF NLAVNLIKYE EEGEYEVVVT NSMGTVSSKS YVTVHKVTHT DAIEVEEEPP
     MQLKVEVVEE ESQQAELAQK EELEVGKEEA QTPEIEDVEK PAQGTIAEKI DIEEKQIKHS
     TPEPIIEEPL SPNIQRGHSD ILEESEFVEN DETDKVQHMK EEDLPKVKSK RAKSIHIEEI
     EENELSSEPK TPIETEVPKR KASKAQAATV EELEIIETLN ETPQQLKESK FERQESQKGV
     REYEEEQDEE MEALLKRAQK QRSLVEELPQ KGELDEAKPT ITSSNMKDSS RPESLDICYI
     VKGTSNPPPK ATWTINGQEL KPDSRVRMTN KGEEFKLEIV KLKMDDAGKI ECILKNPLGE
     ARQTAMLEVT PEKELRRPKL KEGLKDQTIQ KKNTLTFKAV VIGDPVPDAT WSVDGHELTS
     EAFEKYKIIL ETEDHEIQDG LKECTYTLTI PRCERCNAGK YTFFAKNKWG ECNSSAQLTV
     VLRPEIEGPQ NVSVIPGEAT ELVCKIQANP QAEVHWTKDD QVVKETENLK IVSDVANETY
     RLVFKKALLS DEGYYKVVAK NSLGESSSEA RLKAVKEAEP STEKPTIITG LSDDQVEHTK
     EISVMVRADG LPKPQIRWLL NGKPIVEDEK HKIESHADAQ VTSTLTVSDF NDSDSGIYKA
     IAANVQGEAD TSARITMVQT PPTFGKKLER SEDVIEGEPL ELKAKINGSP KPTVVWYKNG
     EPIDDERVKT SVLPDGTVKL NIEHARPSDS GAYKLVIQNP NGESACLCAV AVQQKPQRPK
     FLKCFKDVKL PIGETLRLEA QVQAHPPPEV KWIKDGVPVR VSSNIHFEVH PDGKVALIVD
     CAKPENAGKY ELQVSNKYGD AMGEASVEIE KKPTKPEFLV RLVPQTVVEG FPVKFEVKAV
     GHPAPKLTWS RNGAEVISDN KHVKISELPD GTSVLLLDAA NQARDGLTYR AIAINEAGEA
     ETSAPLTVIP ATNSESPEEK PMFLHPLKDV TADEGKSLVL SAPFTANPVP MVEWSKDGVP
     LSPSDRILVT CDGKKVGLEI LNAVPSDAGR YSVKISNPLG EESSEANAAV HKVFMPPHFT
     QTFTDLQQLP GRDAKFPCRV SGVPQPEVVW TKDGLPIKES DKYHIKRDGD LCCLYVLNCS
     PDDAAVYRAR AINKEGEEVC TASLEVVDQI QAKKKIEPPT FLKRIGDTEL FKGMTAKFTA
     CASGYPEPEV EWYHNDQKLF PSNRIKMETD PNGLLRLIIS DLDEADLGKY SCKITNEYGG
     DICHANLNMD EGLETRAKRP ITDQYTEFDK YKRTGAPVPL SDPPIISQMT DRHCTLSWKP
     SIPPGPRAPV TYQLEMCELP NGDWFTVRTG IRSCTCGVRN LEPFRDYKFR VRVENKYGIS
     DPSPYALTHR AKLEPDLPKF RPWLPPEIDF RPETSPYFPK DFDIERPPHD NMAQAPRFLR
     QEHDTQYGVK DQNTNLFWFV YGYPKPKVSF YFNDELIESG GRFDMSYTRN GQATLFINKM
     LERDVGWYEA VATNEHGEAR QRVRLEIAEM PQFIRRPEIQ YAMHRGKVRF DARIVGVPYP
     EIKWYKDWKP LAASTRIKIQ FIEPDTAVLV INDIITKDEG LYSVSARNVA GSISSSAMLH
     VEEHDHDYNL HTYRNLAQIK PKKKPLTDLY DLGDELGRGT QGVTYHAVAR LNGRNYAAKV
     MHGRGELRPF MYNELEILNE LRHRKLIGLH DCYEGDDTLA LILELAAGGE LVRDYLLKQE
     YYTERDIAGF IRQLLQGLEY MHDRGYGHMG LNIGDLLISH PGTDDLKITD FGLARRIHRD
     NLAPLKYGVP EFASPEAVNG EGTGFGQDMW SVGIITYILL SGRSPFRGND DRETLKNVQA
     GKWIFDEDWW LNISVEAKDF ISKLLVYQSE GRMDVHAALR HPWLERADKI YSDEYRISSK
     YLESYYRLFR EWYDNASCKK WFRRRTLESA FTHPSRMVYP PGEYDSPRAT PAPIKPPRLP
     TWEDQLPTRS PLNYEIGAIK SESHYQNGPD TYLLQLRDVD FPVRLREYMK VAGSRGPGVG
     YIVSNENGFD WHTPTIRERR RFTDIMDEEI DDERRARIKP KSKLVFTTTN DSIVAESHRV
     KIDTDEFGRS HLKFSPALSF DQGMYKVVAR NKIGQTVARA RIVFGSTPEE PDSPESDQSS
     DTEIFLTWKQ PRFDGNSPVL CYSLEYKLAD DIEWTKKADN IDHEFYLMRG LTPSSSYMFR
     LAARNAIGWS DFGVPSGMIK TKPVGAPRVQ VSPAVVHLQQ ITDSGEPVEV QARTYPDYEA
     ETHPVEWENE NAQENYNFIS EIAKGQFSTV LKAIDKRTDA VVVAKVLDLA NSDDVEGEFA
     ALRSLRHERI AGLIAAYKSS ASPVAVFILE KLQGADVLTY LAAKHEYTEQ TVATIVSQVL
     DGLQYLHWRG LCHLDLQPDN VVMAGVRSVQ VKLVDLGAAH RVTKLGTKVP IVGHLDYMSP
     EVLNEEPAFP QTDIWTVGVL TYIMLSGVTP FKGVDENETK QNITFVRYRF EHLYKEITQE
     STRFLMLLFK RQPNKRPSAE ECHENRWLLP TDYMIKKRER AVFLGNRLKE YSSEYHNEKA
     QKAQDITSKL GGKFSRSHSI QEELLTAP
//
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