ID D2W484_NAEGR Unreviewed; 2050 AA.
AC D2W484;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EFC36118.1};
GN ORFNames=NAEGRDRAFT_76212 {ECO:0000313|EMBL:EFC36118.1};
OS Naegleria gruberi (Amoeba).
OC Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC Vahlkampfiidae; Naegleria.
OX NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671};
RN [1] {ECO:0000313|EMBL:EFC36118.1, ECO:0000313|Proteomes:UP000006671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEG-M {ECO:0000313|EMBL:EFC36118.1,
RC ECO:0000313|Proteomes:UP000006671};
RX PubMed=20211133; DOI=10.1016/j.cell.2010.01.032;
RA Fritz-Laylin L.K., Prochnik S.E., Ginger M.L., Dacks J.B., Carpenter M.L.,
RA Field M.C., Kuo A., Paredez A., Chapman J., Pham J., Shu S., Neupane R.,
RA Cipriano M., Mancuso J., Tu H., Salamov A., Lindquist E., Shapiro H.,
RA Lucas S., Grigoriev I.V., Cande W.Z., Fulton C., Rokhsar D.S., Dawson S.C.;
RT "The genome of Naegleria gruberi illuminates early eukaryotic
RT versatility.";
RL Cell 140:631-642(2010).
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; GG738941; EFC36118.1; -; Genomic_DNA.
DR RefSeq; XP_002668862.1; XM_002668816.1.
DR STRING; 5762.D2W484; -.
DR EnsemblProtists; EFC36118; EFC36118; NAEGRDRAFT_76212.
DR GeneID; 8860451; -.
DR VEuPathDB; AmoebaDB:NAEGRDRAFT_76212; -.
DR eggNOG; KOG1217; Eukaryota.
DR InParanoid; D2W484; -.
DR OMA; DICECEG; -.
DR OrthoDB; 2540323at2759; -.
DR Proteomes; UP000006671; Unassembled WGS sequence.
DR Gene3D; 2.10.25.10; Laminin; 5.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR013111; EGF_extracell.
DR PANTHER; PTHR11219; TENEURIN AND N-ACETYLGLUCOSAMINE-1-PHOSPHODIESTER ALPHA-N-ACETYLGLUCOSAMINIDASE; 1.
DR PANTHER; PTHR11219:SF69; TENEURIN-M; 1.
DR Pfam; PF07974; EGF_2; 1.
DR SMART; SM00181; EGF; 13.
DR SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR PROSITE; PS00022; EGF_1; 7.
DR PROSITE; PS01186; EGF_2; 5.
DR PROSITE; PS50026; EGF_3; 6.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Reference proteome {ECO:0000313|Proteomes:UP000006671};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..2050
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003038197"
FT DOMAIN 366..404
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 540..579
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 891..925
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 956..989
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1093..1132
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1201..1238
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 394..403
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 569..578
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 915..924
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 979..988
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1122..1131
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1228..1237
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 2050 AA; 221273 MW; 1005BEF5BFA3F4B3 CRC64;
MAKAEFVLWL SLLLWACFAT TTSQAYVCDS PTMCGSYFNY TVSKVCDYGN SVLPWNQKMV
ISDGTSFKVL DGSNSISSLG SVSNLNFDQF IINKNGDVIV MPELGQTDVF LFSLHNYQRT
ILVETSKWSM SDFVRSITYD PTTDILYFIQ IRDGDGINGK RTGSFCSSVN YPSSCIQIFI
SQTSNAKLQL FNNKFYMLLD NKIKIWGKDE SVSSATDFIT LSSTKYTNFR VSPSGVIFLI
TDDGVFRLVG SKEVRIFGTG TIGVTGNDGP ALSADASPIS LDFDQFGNIY VAEGSATRKL
TPSGCMNQAF INHTTCDIVC NGLSRLDAHV CSGVGQCSEF LPQNGTSQNE TVGCACKPGT
SGINCEVIPC FGKNASSNAC SGRGVCIDVD ICECEGDWDG PECEIAPFNC SNIAHKNPLA
CSEHGFEVKC IAQDTCEHTC NSIGASSASV CSGVGECSSQ NNCSCSFGFI GNNCEFLKPC
VSNMGCGGEC FYLKGVETCV HKCNGVYNFN SSVCSGHGVC VAQDFCYCDK AHYGSDCSKA
YDTCYGLAFS DPKVCSGKGK CISQNNCACD SGYGGSQCEK RTDIDLFPLY GPLGLAELKA
SAFVYSNGVI YASAVADKSV FAFDLATRNV TTFISNLDCY PSISILFNKF GDLVYLCDGD
VYKYSFTSKT STYLGTVGRP PLATSLTYVP ETDTYYVSMS GKIGKFTDSG SQITIQPEST
DYALGFLRYF NGKLYHLNSD LYSWTPGQAS GATLVAESCP GSYFRFNPAG ELYTYGAQQI
SKFSGGSFSQ VVFGGAGSDI LDIFFYGNDL YFFDNKLKYI NIAQLKGCVS ETYIDQATCS
LICEGVPAAS YLSCNGGNCS RYTNVELNLE LTQCSCLPGY SGYDCTEYSC YGNSSLSSAV
CSGHGTCVKP DMCSCQDGYT GNMCQNYTCY GSAGCTMFGN DAKCIGPNTC EPICSKIPAS
NANVCSGEGT CVSMNNCSCH YGRYGVNCEL SIPCVNTTCA SSNYVCFYEH SKEVCLASCS
GIPSTSTLVC SGNGVCTDKC YCNLGWKGSN CNVTEPVCFG ISQSNSSVCS GSGNCTANNV
CSCNEGAYGS ECSDFSCFSI LSNNASVCSG RGACVDNDDC SCNETWTGSN CEIPICDGIP
SNNASVCNGT KMCIAPNTCV DQCNGISALD SKRVCSGRGK CTGYNTCTTC TNGYSGQYCE
IQTPCSTLTC ENNGTCFHYK DGSETCVCPL GFKGKTCERR LCETTSDCPI YGKKYCGTTR
ESEYDTTVTS YKWCREDTCW PNYASPCTDP NFPKCVDIDI YVTYKGRCVA ECMQDSQCSS
PTPKCKMSAD GSYGKCVPEC TSNENCTSIG KHYCSDGGCK MYSCANDTQC QSYGYSQCNN
SICRNECLES KDCPVGSSKY FECGSDKTNI ETYHRCLYKN CKSNADCDSP FTGTPKCDLT
TFNCSSVSCS ATSDCYPYHY SKCTNIGTCE VECTNHTNCK EFGFERCGSN PNNTAEYRNT
TQCDVCGEDR ITCMKCASGY VWDGTECVVK CSSNSYCKTL DPEKPLCSSE GLCGYVACQY
DFECTTNYAL PKCTDGKCSI VCHSDSDCAS QKTSPRCQTD PAVFLYGYCV EECSENGISD
YCTKKNPLLP SCNSGKCGHL RGCWTDDSCQ TLSNNNKYLT SCTSDPTGES YQKVCVPACF
NNTDCEQRGI DKSTANLCSS DSNCTLPGAA VCRGPNVEIA FPSGYVTFQE KTCLPQCFAN
WECSSTPDRP KCSTKMDSTY RTCVPDCLTN DDCVEKGLSI GKSECVNQVC TEKTCSADTD
CTVKGFTFCN SGKKCGRECT ADTDCSEPKP FCSLKEDMTK YRCLPECYNN TDCAPNIKGS
NYNLCSTSKG RCVELPCSSD SDCIYTGYSY CNPTSKVCTK ECLANYMCTI DPKKPTCDMT
TGRCKPECVS DIECGTNGKP VCDITTQHCV AKTCSNSSEC TKTGYTSCTN GICAPECVND
LECVGKGTGI CETKSSESTY HQCTATPYSC SSTNYCYNTI TGYPKCVILI VQENIDTTYT
ILCINNYMSF
//
