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Database: UniProt
Entry: A0A433TAC1_ELYCH
LinkDB: A0A433TAC1_ELYCH
Original site: A0A433TAC1_ELYCH 
ID   A0A433TAC1_ELYCH        Unreviewed;      2535 AA.
AC   A0A433TAC1;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:RUS78537.1};
DE   Flags: Fragment;
GN   ORFNames=EGW08_013715 {ECO:0000313|EMBL:RUS78537.1};
OS   Elysia chlorotica (Eastern emerald elysia) (Sea slug).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Heterobranchia; Euthyneura; Panpulmonata; Sacoglossa; Placobranchoidea;
OC   Plakobranchidae; Elysia.
OX   NCBI_TaxID=188477 {ECO:0000313|EMBL:RUS78537.1, ECO:0000313|Proteomes:UP000271974};
RN   [1] {ECO:0000313|EMBL:RUS78537.1, ECO:0000313|Proteomes:UP000271974}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EC2010 {ECO:0000313|EMBL:RUS78537.1};
RC   TISSUE=Whole organism of an adult {ECO:0000313|EMBL:RUS78537.1};
RA   Cai H., Li Q., Fang X., Li J., Curtis N.E., Altenburger A., Shibata T.,
RA   Feng M., Maeda T., Schwartz J.A., Shigenobu S., Lundholm N., Nishiyama T.,
RA   Yang H., Hasebe M., Li S., Pierce S.K., Wang J.;
RT   "A draft genome assembly of the solar-powered sea slug Elysia chlorotica.";
RL   Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC       protein kinase family. {ECO:0000256|ARBA:ARBA00006692}.
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:RUS78537.1}.
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DR   EMBL; RQTK01000504; RUS78537.1; -; Genomic_DNA.
DR   STRING; 188477.A0A433TAC1; -.
DR   Proteomes; UP000271974; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   CDD; cd00063; FN3; 12.
DR   CDD; cd00096; Ig; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 15.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
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; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   PANTHER; PTHR14340; MICROFIBRIL-ASSOCIATED GLYCOPROTEIN 3; 1.
DR   PANTHER; PTHR14340:SF9; TITIN; 1.
DR   Pfam; PF00041; fn3; 10.
DR   Pfam; PF07679; I-set; 3.
DR   Pfam; PF00069; Pkinase; 2.
DR   SMART; SM00060; FN3; 12.
DR   SMART; SM00409; IG; 3.
DR   SMART; SM00408; IGc2; 3.
DR   SMART; SM00220; S_TKc; 2.
DR   SUPFAM; SSF49265; Fibronectin type III; 8.
DR   SUPFAM; SSF48726; Immunoglobulin; 3.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR   PROSITE; PS50853; FN3; 12.
DR   PROSITE; PS50835; IG_LIKE; 3.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Reference proteome {ECO:0000313|Proteomes:UP000271974};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          21..119
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          121..222
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          225..324
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          326..424
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          425..517
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          533..629
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          634..731
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          735..835
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          870..967
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          995..1092
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1130..1231
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1301..1395
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          1397..1486
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          1507..1761
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          1967..2056
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          2063..2156
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          2214..2468
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          511..533
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1119..1139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1229..1299
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1877..1902
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1229..1260
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1536
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:RUS78537.1"
SQ   SEQUENCE   2535 AA;  286082 MW;  6360529F4E92A5A4 CRC64;
     GGKSSFLLIN FTLVSVRPRL PSREPIISDL GLDSVRLTWK PAELPYYSRH ATPITYTVDY
     QEIPSREWIV AGRSIPETSY TIRGLNPERD YRFRITPETE FGPGEPSLPV LARRHVAPVF
     PKREPLLSNI TPTSATLSWS PATFPDTSSL SSRNITYRVE AREPPSSLWA PLSGGRGLTG
     TSYDLQFLHP DQDYMFRVVA EFGEFESEPS MTAYLSHRAG PPKMPRDAPQ VSSVQPESLF
     LSWRSVELPS RITDYSPVTY RIEVQEGPHG HWSPLVRQIN QTHYHVTGLK PDVSYNFRVR
     AENAFGVSDP TDPVLVRKRA VAPTLSEHEP LISDVRGDSL RLTWKPAELP SYLTDSVPVT
     YTILMQEPGD HSWSPIARRV SGTSYYVTGL YPDRDYSFRV QAENNYGTSL PSFPSRLHRE
     IKGPIYSPEI EDVEPSSFRL SWRSPSVSRP TTYAVETLEP STWKWRPLVS RLPHPSYKIT
     DVAPGRDYAF RVRAEVDSVV TEPSLPISFS NRRVPSRANS MPPRHYRAPP TAPVERPTLS
     EIYEDSVRVN WHPILHYGST RKSAPESFRL EVRELPDTYW RTLIPSTDAW SYEVTSLRAD
     QDYAFRVRTV TDTGMSEPSL PVYLYRKAAT PKVPLPSPEI SDVGDNYIGI RWNKVDVPAF
     DLDETPLSFM IEAQSVPDYD WKPVARGVTG ASHRITGLEP KRDYQFRLRG ETPLGLTQPS
     SPVPAFRTPL RSGVPIVNVK IERDSNLPYS ARLRWNPVYV PPYSPTRGGT TYAIEMQEPP
     RTDWYTLAQN VSSTSYTVPE LSPKRDYMFR IRARSVEGDL SAPTLPVPYY RAPESSWSNL
     PSMPGPAIDY SPLNRPYIEG LIVKVPPRMS IEKPEMTLLS PDCVQLSWRA ARVPPATASL
     SPTTYRVEAR HEDSFEWIER ATNISGLSTE VKGLNPHVEY AFRVRAVNDF GWSESTLPVF
     LHRSQDLKDA AVEMEFEEIE TMGSIFGDTS PPKMPMDTPR MGIVQSDGSM KLSWTEARIP
     VYARKTPITY SIEKKEPLDQ DWVVVVNDLE DNQYLIPGIQ PQQDYLFRVK AHNEFGASEA
     TLPAALTRSK APKFIRNSAS RERELEVAAS QRRSSSSSYS YIDSISTGVP PRVPQGRPSM
     SDIKDTSLTL SWQPGRMPSY IKGPVKISYI VECREPPNHL WNKLNSDVGS TTYKVTNLRP
     DQDYMFRVRA FNDSGMSEPT LPVTLTREKA PEVEPRTMRR RSSVERFASV ERRTSRERSL
     SMDRGSSVPR AGLLSREGSK REVDEEDMFA GQTPDTTPAA PEFVVSDAGS EIQHGIDARP
     VKITLQLRGV PLPNVEWYFN DKKIIYGDRH EGYVTPTGLA VLEFSPMGWG DVGDYKCVAE
     NDQGETSFTV KLQMSDPPTF LEPIRDLHLK TMATDRFVCQ VDGIPYPTVK FMKDWRPLTE
     TSRQKVVQEG SVWNLEVDQA IPADSGCYIC VAENAAGKVF CTARLTVDDD APAESVVYKK
     TNLEDDYYIL EELGRGRHSI VRRVIEKHTG KEFAAKFTQV REETDKDFFR QELDALVRQG
     GKNVEGLHDA YETQRQLILV LESVKQGNVL DRVISDQQWT EVKAAQVVKA LVESLQAVHA
     THYLHLDVKP SNLRFTSNDL SSLRLTDFGF SRKLPLSKDL EFNFGTPEFC SPEAVNNEAV
     TPASDIWAVG VITHLLLTGV SPFYAPSVQD ILSKTQTCDW NRDDPGFKAL SSEAQDFVSK
     ILVRDPQARL SAKACLEHPW LKDDKKAGTK KLDTSKLKSF QDRIDSEQKT NEVKTVACLR
     TLSRLLEGPT PIQGLQPTTD TQTGDVILPD TEEYGEFLDE ESWYDWQSRH QQGPDTELFP
     LKDASYTLRV RGYKRAAGSV DESGGPPVYV DSDEELDPQD KEKMRTMKER TKLAEIDKEE
     IPPSLEKELE WMEEKRRRRK SKDADEFSLT SKRSSIASVT SESLPGPYFK EKLHNMAFGV
     DDTVILRCVV AGPPTPTCVW YKNEELLTEG NRLKVNLEED GEATLTIRNA KPYDAGVYKC
     VGRNKHGRVS NRMRLSLGDV PGRPGQPVVG RVSSTEAMVI WEAPRSDGHS DILFYKVDYK
     PSGKDRWSSG LYTTLEATVI SGLSPNTDYR FRVSATNRFG TSHYSWSSVE VSTAGEGSKA
     IESDDFFDVS KLRSGQCESQ PSLPTEHDDI IPEEELVQGK PEISLQKVKP DTAYNISSLL
     YRGKFYEDKS VTLPSQNDKA FVMRTVFSQA AGLREFETLK SLHHEHLACL CAAFSDETEK
     DGPVHLVLEY LQGEHVTRHL SQRRKYSEDT VASIIRQVLY GLEYLHGQNI LHLNLQPASV
     VVSALEGCEV KVTDFSLARP AVVPHGEKVP RLGYADFIAP EVITQDLVSF PADVWGVGVL
     TFVLLSGTSP FRDVSYEATL VNIALNRYDA VDLYENITTE ALKFLYKVMK RMPRNRLSVR
     ECLEHKWLQL TDKIVKERED TVFLTNTLAR FVAEYDAARQ AQDFRQDFQS DTLPIQMSKA
     IPFEMTTADI SKAKP
//
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